data_4300 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H , 13C, 15N Assigned Chemical Shifts for HPPK-AMPPCP Complex ; _BMRB_accession_number 4300 _BMRB_flat_file_name bmr4300.str _Entry_type original _Submission_date 1999-01-22 _Accession_date 1999-01-25 _Entry_origination author _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 Shi Genbin . . 2 Gao Jinhai . . 3 Yan Honggao . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 718 "13C chemical shifts" 240 "15N chemical shifts" 139 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 1999-08-12 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 4299 apo-HPPK stop_ _Original_release_date 1999-08-12 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Shi, G., Gao, J., and Yan, H., "1H, 13C and 15N Resonance Assignments of Escherichia coli 6-hydroxymethyl-7,8-dihydropterin Pyrophosphokinase and its Complex with MgAMPPCP," J. Biomol. NMR 14, 189-190 (1999). ; _Citation_title ; 1H, 13C and 15N Resonance Assignments of Escherichia coli 6-hydroxymethyl-7,8-dihydropterin Pyrophosphokinase and its Complex with MgAMPPCP ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 99356754 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Shi Genbin . . 2 Gao Jinhai . . 3 Yan Honggao . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of Biomolecular NMR' _Journal_volume 14 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 189 _Page_last 190 _Year 1999 _Details . save_ ################################## # Molecular system description # ################################## save_HPPK_AMPPCP _Saveframe_category molecular_system _Mol_system_name 'HPPK-AMPPCP complex' _Abbreviation_common 'HPPK AMPPCP' _Enzyme_commission_number 2.7.6.3 loop_ _Mol_system_component_name _Mol_label 'HPPK monomer' $HPPK AMPPCP $AMPPCP Mg $MG stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state . loop_ _Biological_function pyrophosphokinase stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_HPPK _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common '6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase' _Molecular_mass . _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 158 _Mol_residue_sequence ; TVAYIAIGSNLASPLEQVNA ALKALGDIPESHILTVSSFY RTPPLGPQDQPDYLNAAVAL ETSLAPEELLNHTQRIELQQ GRVRKAERWGPRTLDLDIML FGNEVINTERLTVPHYDMKN RGFMLWPLFEIAPELVFPDG EMLRQILHTRAFDKLNKW ; loop_ _Residue_seq_code _Residue_label 1 THR 2 VAL 3 ALA 4 TYR 5 ILE 6 ALA 7 ILE 8 GLY 9 SER 10 ASN 11 LEU 12 ALA 13 SER 14 PRO 15 LEU 16 GLU 17 GLN 18 VAL 19 ASN 20 ALA 21 ALA 22 LEU 23 LYS 24 ALA 25 LEU 26 GLY 27 ASP 28 ILE 29 PRO 30 GLU 31 SER 32 HIS 33 ILE 34 LEU 35 THR 36 VAL 37 SER 38 SER 39 PHE 40 TYR 41 ARG 42 THR 43 PRO 44 PRO 45 LEU 46 GLY 47 PRO 48 GLN 49 ASP 50 GLN 51 PRO 52 ASP 53 TYR 54 LEU 55 ASN 56 ALA 57 ALA 58 VAL 59 ALA 60 LEU 61 GLU 62 THR 63 SER 64 LEU 65 ALA 66 PRO 67 GLU 68 GLU 69 LEU 70 LEU 71 ASN 72 HIS 73 THR 74 GLN 75 ARG 76 ILE 77 GLU 78 LEU 79 GLN 80 GLN 81 GLY 82 ARG 83 VAL 84 ARG 85 LYS 86 ALA 87 GLU 88 ARG 89 TRP 90 GLY 91 PRO 92 ARG 93 THR 94 LEU 95 ASP 96 LEU 97 ASP 98 ILE 99 MET 100 LEU 101 PHE 102 GLY 103 ASN 104 GLU 105 VAL 106 ILE 107 ASN 108 THR 109 GLU 110 ARG 111 LEU 112 THR 113 VAL 114 PRO 115 HIS 116 TYR 117 ASP 118 MET 119 LYS 120 ASN 121 ARG 122 GLY 123 PHE 124 MET 125 LEU 126 TRP 127 PRO 128 LEU 129 PHE 130 GLU 131 ILE 132 ALA 133 PRO 134 GLU 135 LEU 136 VAL 137 PHE 138 PRO 139 ASP 140 GLY 141 GLU 142 MET 143 LEU 144 ARG 145 GLN 146 ILE 147 LEU 148 HIS 149 THR 150 ARG 151 ALA 152 PHE 153 ASP 154 LYS 155 LEU 156 ASN 157 LYS 158 TRP stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-07-14 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 4299 "6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase" 100.00 158 100.00 100.00 4.12e-111 PDB 1DY3 "Ternary Complex Of 7,8-Dihydro-6- Hydroxymethylpterinpyrophosphokinase From Escherichia Coli With Atp And A Substrate Analogue." 100.00 158 100.00 100.00 4.12e-111 PDB 1EQ0 "Solution Structure Of 6-Hydroxymethyl-7,8-Dihydropterin Pyrophosphokinase Complexed With Mgamppcp" 100.00 158 100.00 100.00 4.12e-111 PDB 1EQM "Crystal Structure Of Binary Complex Of 6-Hydroxymethyl-7,8- Dihydropterin Pyrophosphokinase With Adenosine-5'- Diphosphate" 100.00 158 100.00 100.00 4.12e-111 PDB 1EX8 "Crystal Structure Of 6-Hydroxymethyl-7,8-Dihydropterin Pyrophosphokinase Complexed With Hp4a, The Two-Substrate- Mimicking Inhi" 100.00 158 100.00 100.00 4.12e-111 PDB 1F9H "Crystal Structure Of The Ternary Complex Of E. Coli Hppk(R92a) With Mgampcpp And 6-Hydroxymethyl-7,8- Dihydropterin At 1.50 Ang" 100.00 158 99.37 99.37 3.40e-110 PDB 1G4C "Crystal Structure Of A Complex Of Hppk(R92a) From E.Coli With Mg2+ At 1.65 Angstrom Resolution" 100.00 158 99.37 99.37 3.40e-110 PDB 1HKA "6-Hydroxymethyl-7,8-Dihydropterin Pyrophosphokinase" 100.00 158 100.00 100.00 4.12e-111 PDB 1HQ2 "Crystal Structure Of A Ternary Complex Of E.Coli Hppk(R82a) With Mgampcpp And 6-Hydroxymethyl-7,8-Dihydropterin At 1.25 Angstro" 100.00 158 99.37 99.37 3.40e-110 PDB 1IM6 "Crystal Structure Of Unligated Hppk(R82a) From E.Coli At 1.74 Angstrom Resolution" 100.00 158 99.37 99.37 3.40e-110 PDB 1KBR "Crystal Structure Of Unligated Hppk(R92a) From E.Coli At 1.55 Angstrom Resolution" 100.00 158 99.37 99.37 3.40e-110 PDB 1Q0N "Crystal Structure Of A Ternary Complex Of 6-Hydroxymethyl-7, 8-Dihydropterin Pyrophosphokinase From E. Coli With Mgampcpp And 6" 100.00 158 100.00 100.00 4.12e-111 PDB 1RAO "Crystal Structure Of A Ternary Complex Of E. Coli Hppk With Amp And 6-Hydroxymethylpterin-Diphosphate At 1.56 Angstrom Resoluti" 100.00 158 100.00 100.00 4.12e-111 PDB 1RB0 "Crystal Structure Of A Binary Complex Of E. Coli Hppk With 6-Hydroxymethylpterin-Diphosphate At 1.35 Angstrom Resolution" 100.00 158 100.00 100.00 4.12e-111 PDB 1TMJ "Crystal Structure Of E.Coli Apo-Hppk(W89a) At 1.45 Angstrom Resolution" 100.00 158 99.37 99.37 1.09e-109 PDB 1TMM "Crystal Structure Of Ternary Complex Of E.Coli Hppk(W89a) With Mgampcpp And 6-Hydroxymethylpterin" 100.00 158 99.37 99.37 1.09e-109 PDB 2F63 "Solution Structure Of Hppk In Complex With Inhibitor Analogs Ampcpp And Hp-1" 100.00 158 100.00 100.00 4.12e-111 PDB 2F65 "Solution Structure Of Hppk In Complex With Inhibitor Analog Ampcpp" 100.00 158 100.00 100.00 4.12e-111 PDB 3HCX "Crystal Structure Of E. Coli Hppk(N10a)" 100.00 158 99.37 99.37 4.56e-110 PDB 3HD1 "Crystal Structure Of E. Coli Hppk(N10a) In Complex With Mgam" 100.00 158 99.37 99.37 4.56e-110 PDB 3HD2 "Crystal Structure Of E. Coli Hppk(Q50a) In Complex With Mgam Pterin" 100.00 158 99.37 99.37 2.73e-110 PDB 3HSD "Crystal Structure Of E. Coli Hppk(Y53a)" 100.00 158 99.37 99.37 6.06e-110 PDB 3HSG "Crystal Structure Of E. Coli Hppk(Y53a) In Complex With Mgampcpp" 100.00 158 99.37 99.37 6.06e-110 PDB 3HSJ "Crystal Structure Of E. Coli Hppk(N55a)" 100.00 158 99.37 99.37 4.56e-110 PDB 3HSZ "Crystal Structure Of E. Coli Hppk(F123a)" 100.00 158 99.37 99.37 5.49e-110 PDB 3HT0 "Crystal Structure Of E. Coli Hppk(F123a) In Complex With Mgampcpp" 100.00 158 99.37 99.37 5.49e-110 PDB 3ILI "Crystal Structure Of E. Coli Hppk(D95a)" 100.00 158 99.37 99.37 3.83e-110 PDB 3ILJ "Crystal Structure Of E. Coli Hppk(D95a) In Complex With Mgampcpp" 100.00 158 99.37 99.37 3.83e-110 PDB 3ILL "Crystal Structure Of E. Coli Hppk(D97a)" 100.00 158 99.37 99.37 3.83e-110 PDB 3ILO "Crystal Structure Of E. Coli Hppk(D97a) In Complex With Mgampcpp And 6-Hydroxymethyl-7,8-Dihydropterin" 100.00 158 99.37 99.37 3.83e-110 PDB 3IP0 "Crystal Structure Of E. Coli Hppk In Complx With Mgampcpp And 6-Hydroxymethylpterin6-Carboxypterin" 100.00 158 100.00 100.00 4.12e-111 PDB 3KUE "Crystal Structure Of E. Coli Hppk(E77a)" 100.00 158 99.37 99.37 2.27e-110 PDB 3KUG "Crystal Structure Of E. Coli Hppk(H115a)" 100.00 158 99.37 99.37 6.76e-110 PDB 3KUH "Crystal Structure Of E. Coli Hppk(H115a) In Complex With Ampcpp And Hp" 100.00 158 99.37 99.37 6.76e-110 PDB 3UD5 "Crystal Structure Of E. Coli Hppk In Complex With Bisubstrate Analogue Inhibitor J1a" 100.00 158 100.00 100.00 4.12e-111 PDB 3UDE "Crystal Structure Of E. Coli Hppk In Complex With Bisubstrate Analogue Inhibitor J1b" 100.00 158 100.00 100.00 4.12e-111 PDB 3UDV "Crystal Structure Of E. Coli Hppk In Complex With Bisubstrate Analogue Inhibitor J1c" 100.00 158 100.00 100.00 4.12e-111 PDB 4F7V "Crystal Structure Of E. Coli Hppk In Complex With Bisubstrate Analogue Inhibitor J1d (Hp26)" 100.00 158 100.00 100.00 4.12e-111 PDB 4M5G "The Identification, Analysis And Structure-based Development Of Novel Inhibitors Of 6-hydroxymethyl-7,8-dihydropterin Pyrophosp" 100.00 162 100.00 100.00 3.55e-111 PDB 4M5H "The Identification, Analysis And Structure-based Development Of Novel Inhibitors Of 6-hydroxymethyl-7,8-dihydropterin Pyrophosp" 100.00 162 100.00 100.00 3.55e-111 PDB 4M5I "The Identification, Analysis And Structure-based Development Of Novel Inhibitors Of 6-hydroxymethyl-7,8-dihydropterin Pyrophosp" 100.00 162 100.00 100.00 3.55e-111 PDB 4M5J "The Identification, Analysis And Structure-based Development Of Novel Inhibitors Of 6-hydroxymethyl-7,8-dihydropterin Pyrophosp" 100.00 162 100.00 100.00 3.55e-111 PDB 4M5K "The Identification, Analysis And Structure-based Development Of Novel Inhibitors Of 6-hydroxymethyl-7,8-dihydropterin Pyrophosp" 100.00 162 100.00 100.00 3.55e-111 PDB 4M5L "The Identification, Analysis And Structure-based Development Of Novel Inhibitors Of 6-hydroxymethyl-7,8-dihydropterin Pyrophosp" 100.00 162 100.00 100.00 3.55e-111 PDB 4M5M "The Identification, Analysis And Structure-based Development Of Novel Inhibitors Of 6-hydroxymethyl-7,8-dihydropterin Pyrophosp" 100.00 162 100.00 100.00 3.55e-111 PDB 4M5N "The Identification, Analysis And Structure-based Development Of Novel Inhibitors Of 6-hydroxymethyl-7,8-dihydropterin Pyrophosp" 100.00 162 100.00 100.00 3.55e-111 DBJ BAB96719 "2-amino-4-hydroxy-6- hydroxymethyldihyropteridine pyrophosphokinase [Escherichia coli str. K12 substr. W3110]" 100.00 159 100.00 100.00 4.45e-111 DBJ BAJ41992 "2-amino-4-hydroxy-6-hydroxymethyldihyropteridinepyrophosphokinase [Escherichia coli DH1]" 100.00 159 99.37 100.00 1.75e-110 DBJ BAL37452 "2-amino-4-hydroxy-6-hydroxymethyldihyropteridine pyrophosphokinase [Escherichia coli str. K-12 substr. MDS42]" 100.00 159 100.00 100.00 4.45e-111 EMBL CBI99639 "2-amino-4-hydroxy-6-hydroxymethyldihyropteridin e pyrophosphokinase [Escherichia coli ETEC H10407]" 100.00 159 100.00 100.00 4.45e-111 EMBL CCP97244 "2-amino-4-hydroxy-6-hydroxymethyldihydropteridinepyrophosphokinase [Escherichia coli O10:K5(L):H4 str. ATCC 23506]" 100.00 159 100.00 100.00 4.45e-111 EMBL CDJ70723 "2-amino-4-hydroxy-6-hydroxymethyldihydropteridinepyrophosphokinase [Escherichia coli str. K-12 substr. MC4100]" 100.00 159 100.00 100.00 4.45e-111 EMBL CDK83585 "2-amino-4-hydroxy-6-hydroxymethyldihydropteridinepyrophosphokinase [Escherichia coli IS25]" 100.00 159 100.00 100.00 4.45e-111 EMBL CDY54783 "6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase [Escherichia coli]" 100.00 159 100.00 100.00 4.45e-111 GB AAB53446 "hydroxymethyldihydropterin pyrophosphokinase [Escherichia coli]" 100.00 159 100.00 100.00 4.45e-111 GB AAC73253 "2-amino-4-hydroxy-6-hydroxymethyldihyropteridine pyrophosphokinase [Escherichia coli str. K-12 substr. MG1655]" 100.00 159 100.00 100.00 4.45e-111 GB ACA79131 "2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase [Escherichia coli ATCC 8739]" 93.04 159 97.96 98.64 1.26e-98 GB ACB01321 "2-amino-4-hydroxy-6-hydroxymethyldihyropteridine pyrophosphokinase [Escherichia coli str. K-12 substr. DH10B]" 100.00 159 100.00 100.00 4.45e-111 GB ACR61761 "2-amino-4-hydroxy-6-hydroxymethyldihyropteridine pyrophosphokinase [Escherichia coli BW2952]" 100.00 159 100.00 100.00 4.45e-111 REF NP_414684 "2-amino-4-hydroxy-6-hydroxymethyldihyropteridine pyrophosphokinase [Escherichia coli str. K-12 substr. MG1655]" 100.00 159 100.00 100.00 4.45e-111 REF WP_000215127 "2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase [Escherichia coli]" 100.00 159 98.10 99.37 1.13e-109 REF WP_000215131 "2-amino-4-hydroxy-6-hydroxymethyldihyropteridine pyrophosphokinase [Escherichia coli]" 100.00 159 98.10 98.10 1.66e-108 REF WP_000215137 "MULTISPECIES: 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase [Enterobacteriaceae]" 93.04 159 97.96 98.64 1.26e-98 REF WP_000215138 "2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase [Escherichia coli]" 100.00 159 98.73 100.00 1.97e-110 SP P26281 "RecName: Full=2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase; AltName: Full=6-hydroxymethyl-7,8-dihydropte" 100.00 159 100.00 100.00 4.45e-111 stop_ save_ ############# # Ligands # ############# save_AMPPCP _Saveframe_category ligand _Mol_type non-polymer _Name_common 'beta gamma-methyleneadenosine 5'triphosphate' _Abbreviation_common AMPPCP _BMRB_code . _PDB_code . _Molecular_mass . _Mol_charge . _Mol_paramagnetic no _Mol_aromatic yes _Details . _Mol_thiol_state . _Sequence_homology_query_date . save_ save_MG _Saveframe_category ligand _Mol_type "non-polymer (NON-POLYMER)" _Name_common 'MAGNESIUM ION' _BMRB_code MG _PDB_code MG _Molecular_mass 24.305 _Mol_charge 2 _Mol_paramagnetic . _Mol_aromatic no _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons MG MG MG . 2 . ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $HPPK E.coli 562 Eubacteria . Escherichia coli stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_type _Vector_name $HPPK 'recombinant technology' 'E. coli' Escherichia coli BL21(DE3)plysS plasmid pET-17B stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $HPPK 1.5 mM [U-15N] 'sodium phosphate' 20 mM . 'B,r-Methyleneadenosine 5`-triphosphate' 8 mM . 'Magnesium chloride' 40 mM . H2O 90 % . D2O 10 % . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $HPPK 1.5 mM '[U-15N; U-13C]' 'sodium phosphate' 20 mM . 'B,r-Methyleneadenosine 5`-triphosphate' 8 mM . 'Magnesium chloride' 40 mM . H2O 90 % . D2O 10 % . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_list _Saveframe_category NMR_spectrometer _Manufacturer . _Model . _Field_strength . _Details . save_ ############################# # NMR applied experiments # ############################# save__1 _Saveframe_category NMR_applied_experiment _Sample_label . save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH* 7.4 0.2 na temperature 298 0.2 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio_citation_label _Correction_value_citation_label H20 H 1 protons ppm 4.7 . . . . . $entry_citation $entry_citation 'sodium acetate' C 13 'methyl carbon' ppm 25.85 . . . . . $entry_citation $entry_citation 'ammonium chloride' N 15 nitrogen ppm 78.98 . . . . . $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_assigned_chemical_shifts_one _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 $sample_2 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'HPPK monomer' _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 THR HA H 3.51 . 9 2 . 1 THR HB H 3.43 . 9 3 . 1 THR HG1 H 0.43 . 9 4 . 1 THR CA C 62.97 . 9 5 . 1 THR CB C 70.4 . 9 6 . 2 VAL H H 8.65 . 1 7 . 2 VAL HA H 4.11 . 1 8 . 2 VAL HB H 1.66 . 1 9 . 2 VAL HG1 H 0.67 . 1 10 . 2 VAL HG2 H 0.04 . 1 11 . 2 VAL CA C 63.9 . 1 12 . 2 VAL N N 130.84 . 1 13 . 3 ALA H H 9.16 . 1 14 . 3 ALA HA H 4.88 . 1 15 . 3 ALA HB H 1.12 . 1 16 . 3 ALA CA C 49.91 . 1 17 . 3 ALA CB C 21.78 . 1 18 . 3 ALA N N 134.98 . 1 19 . 4 TYR H H 8.47 . 1 20 . 4 TYR HA H 5.52 . 1 21 . 4 TYR HB2 H 2.63 . 1 22 . 4 TYR HB3 H 2.63 . 1 23 . 4 TYR CA C 57.7 . 1 24 . 4 TYR CB C 41.1 . 1 25 . 4 TYR N N 121.17 . 1 26 . 5 ILE H H 9.41 . 1 27 . 5 ILE HA H 4.83 . 1 28 . 5 ILE HB H 1.87 . 1 29 . 5 ILE HG12 H 1.64 . 1 30 . 5 ILE HG13 H 1.44 . 1 31 . 5 ILE HG2 H 0.87 . 1 32 . 5 ILE HD1 H 0.73 . 1 33 . 5 ILE CA C 60.5 . 1 34 . 5 ILE CB C 42.74 . 1 35 . 5 ILE CG2 C 17.84 . 1 36 . 5 ILE CD1 C 15.22 . 1 37 . 5 ILE N N 128.2 . 1 38 . 6 ALA H H 9.9 . 1 39 . 6 ALA HA H 4.97 . 1 40 . 6 ALA HB H 1.68 . 1 41 . 6 ALA CA C 52.08 . 1 42 . 6 ALA CB C 21.77 . 1 43 . 6 ALA N N 134.31 . 1 44 . 7 ILE H H 8.72 . 1 45 . 7 ILE HA H 4.76 . 1 46 . 7 ILE HB H 1.34 . 1 47 . 7 ILE HG12 H 1.44 . 1 48 . 7 ILE HG13 H 1.44 . 1 49 . 7 ILE HG2 H 0.57 . 1 50 . 7 ILE HD1 H 0.69 . 1 51 . 7 ILE CA C 60.7 . 1 52 . 7 ILE CB C 41.6 . 1 53 . 7 ILE N N 123.85 . 1 54 . 8 GLY H H 8.74 . 1 55 . 8 GLY HA2 H 5.68 . 1 56 . 8 GLY HA3 H 3.63 . 1 57 . 8 GLY CA C 45.45 . 1 58 . 8 GLY N N 116.09 . 1 59 . 9 SER H H 8.5 . 1 60 . 9 SER N N 118.45 . 1 61 . 10 ASN H H 8.09 . 1 62 . 10 ASN N N 126.88 . 1 63 . 11 LEU H H 7.26 . 1 64 . 11 LEU N N 122.16 . 1 65 . 12 ALA H H 8.16 . 1 66 . 12 ALA N N 126.53 . 1 67 . 13 SER H H 7.56 . 1 68 . 13 SER N N 110.78 . 1 69 . 15 LEU H H 8.08 . 1 70 . 15 LEU HA H 3.37 . 1 71 . 15 LEU HB2 H 1.55 . 2 72 . 15 LEU HB3 H 1.35 . 2 73 . 15 LEU HG H 0.85 . 1 74 . 15 LEU HD1 H 0.56 . 1 75 . 15 LEU HD2 H 0.56 . 1 76 . 15 LEU CA C 60.25 . 1 77 . 15 LEU CD1 C 24.36 . 1 78 . 15 LEU CD2 C 24.36 . 1 79 . 15 LEU N N 122.99 . 1 80 . 16 GLU H H 8.12 . 1 81 . 16 GLU N N 119.43 . 1 82 . 17 GLN H H 8.1 . 1 83 . 17 GLN N N 124.05 . 1 84 . 18 VAL H H 8.36 . 1 85 . 18 VAL HA H 3.23 . 1 86 . 18 VAL HB H 1.51 . 1 87 . 18 VAL HG1 H 0.55 . 1 88 . 18 VAL HG2 H 0.23 . 1 89 . 18 VAL CA C 68.09 . 1 90 . 18 VAL CG1 C 24.5 . 1 91 . 18 VAL CG2 C 21.45 . 1 92 . 18 VAL N N 122.03 . 1 93 . 19 ASN H H 8.38 . 1 94 . 19 ASN N N 120.34 . 1 95 . 20 ALA H H 8.22 . 1 96 . 20 ALA N N 126.88 . 1 97 . 21 ALA H H 8.53 . 1 98 . 21 ALA N N 125.62 . 1 99 . 22 LEU H H 8.45 . 1 100 . 22 LEU HA H 3.85 . 1 101 . 22 LEU HB2 H 1.98 . 2 102 . 22 LEU HB3 H 1.34 . 2 103 . 22 LEU HG H 1.75 . 1 104 . 22 LEU HD1 H 0.99 . 1 105 . 22 LEU HD2 H 0.75 . 1 106 . 22 LEU CA C 59.16 . 1 107 . 22 LEU CB C 42.5 . 1 108 . 22 LEU N N 120.21 . 1 109 . 23 LYS H H 7.69 . 1 110 . 23 LYS HA H 3.88 . 1 111 . 23 LYS HB2 H 1.85 . 1 112 . 23 LYS HB3 H 1.85 . 1 113 . 23 LYS HG2 H 1.43 . 2 114 . 23 LYS HG3 H 1.33 . 2 115 . 23 LYS HD2 H 1.59 . 1 116 . 23 LYS HD3 H 1.59 . 1 117 . 23 LYS HE2 H 2.89 . 1 118 . 23 LYS HE3 H 2.89 . 1 119 . 23 LYS CA C 60.13 . 1 120 . 23 LYS CG C 25.6 . 1 121 . 23 LYS N N 122.7 . 1 122 . 24 ALA H H 7.78 . 1 123 . 24 ALA HA H 4.08 . 1 124 . 24 ALA HB H 1.42 . 1 125 . 24 ALA CA C 55.86 . 1 126 . 24 ALA N N 122.96 . 1 127 . 25 LEU H H 8.84 . 1 128 . 25 LEU HA H 3.77 . 1 129 . 25 LEU HB2 H 1.99 . 2 130 . 25 LEU HB3 H 1.15 . 2 131 . 25 LEU HG H 1.82 . 1 132 . 25 LEU HD1 H 0.72 . 1 133 . 25 LEU HD2 H 0.72 . 1 134 . 25 LEU CA C 58.26 . 1 135 . 25 LEU CB C 43.01 . 1 136 . 25 LEU CD1 C 24.5 . 1 137 . 25 LEU CD2 C 24.5 . 1 138 . 25 LEU N N 123.71 . 1 139 . 26 GLY H H 7.49 . 1 140 . 26 GLY HA2 H 3.79 . 1 141 . 26 GLY HA3 H 3.79 . 1 142 . 26 GLY CA C 46.78 . 1 143 . 26 GLY N N 102.56 . 1 144 . 27 ASP H H 7.21 . 1 145 . 27 ASP HA H 4.82 . 1 146 . 27 ASP HB2 H 2.81 . 2 147 . 27 ASP HB3 H 2.48 . 2 148 . 27 ASP CA C 54.31 . 1 149 . 27 ASP CB C 42.6 . 1 150 . 27 ASP N N 120.31 . 1 151 . 28 ILE H H 7.01 . 1 152 . 28 ILE HA H 3.69 . 1 153 . 28 ILE HB H 1.44 . 1 154 . 28 ILE HG12 H 0.68 . 4 155 . 28 ILE HG13 H 0.68 . 4 156 . 28 ILE HG2 H 0.9 . 4 157 . 28 ILE HD1 H 0.51 . 4 158 . 28 ILE CA C 62 . 1 159 . 28 ILE CB C 38.74 . 1 160 . 28 ILE N N 126.93 . 1 161 . 29 PRO HA H 4.2 . 1 162 . 29 PRO HB2 H 2.28 . 2 163 . 29 PRO HB3 H 1.77 . 2 164 . 29 PRO HG2 H 1.93 . 1 165 . 29 PRO HG3 H 1.93 . 1 166 . 29 PRO HD2 H 3.56 . 2 167 . 29 PRO HD3 H 2.66 . 2 168 . 29 PRO CA C 64.08 . 1 169 . 29 PRO CB C 33.45 . 1 170 . 29 PRO CD C 51.54 . 1 171 . 30 GLU H H 8.78 . 1 172 . 30 GLU HA H 3.82 . 1 173 . 30 GLU HB2 H 2.31 . 2 174 . 30 GLU HB3 H 1.83 . 2 175 . 30 GLU HG2 H 2.06 . 2 176 . 30 GLU HG3 H 2.01 . 2 177 . 30 GLU CA C 57.54 . 1 178 . 30 GLU CB C 27.67 . 1 179 . 30 GLU N N 116.15 . 1 180 . 31 SER H H 7.17 . 1 181 . 31 SER HA H 5.84 . 1 182 . 31 SER HB2 H 3.49 . 1 183 . 31 SER CA C 58.2 . 1 184 . 31 SER CB C 68.37 . 1 185 . 31 SER N N 111.76 . 1 186 . 32 HIS H H 8.87 . 1 187 . 32 HIS HA H 4.81 . 1 188 . 32 HIS HB2 H 3.05 . 2 189 . 32 HIS HB3 H 3.25 . 2 190 . 32 HIS CA C 56.17 . 1 191 . 32 HIS CB C 31.8 . 1 192 . 32 HIS N N 117.04 . 1 193 . 33 ILE H H 9.08 . 1 194 . 33 ILE HA H 3.76 . 1 195 . 33 ILE HB H 1.67 . 1 196 . 33 ILE HG12 H 1.47 . 4 197 . 33 ILE HG13 H 0.67 . 4 198 . 33 ILE HG2 H 0.77 . 4 199 . 33 ILE CA C 64.15 . 1 200 . 33 ILE CB C 39.99 . 1 201 . 33 ILE CG1 C 29.9 . 1 202 . 33 ILE CG2 C 13.89 . 1 203 . 33 ILE N N 126.8 . 1 204 . 34 LEU H H 9.04 . 1 205 . 34 LEU HA H 4.4 . 1 206 . 34 LEU HB2 H 1.41 . 2 207 . 34 LEU HB3 H 1.61 . 2 208 . 34 LEU HG H 1.53 . 1 209 . 34 LEU HD1 H 0.73 . 1 210 . 34 LEU HD2 H 0.7 . 1 211 . 34 LEU CA C 56.84 . 1 212 . 34 LEU N N 130.77 . 1 213 . 35 THR H H 7.26 . 1 214 . 35 THR HA H 4.5 . 1 215 . 35 THR HB H 4.01 . 1 216 . 35 THR HG1 H 1.13 . 1 217 . 35 THR CA C 62.08 . 1 218 . 35 THR CB C 63.69 . 1 219 . 35 THR N N 112.33 . 1 220 . 36 VAL H H 8.16 . 1 221 . 36 VAL HA H 4.7 . 1 222 . 36 VAL HB H 1.85 . 1 223 . 36 VAL HG1 H 1.23 . 1 224 . 36 VAL HG2 H 0.99 . 1 225 . 36 VAL CA C 61.87 . 1 226 . 36 VAL CB C 35.93 . 1 227 . 36 VAL N N 127.24 . 1 228 . 37 SER H H 9.13 . 1 229 . 37 SER HA H 4.16 . 1 230 . 37 SER HB2 H 3.96 . 2 231 . 37 SER HB3 H 4.95 . 2 232 . 37 SER CA C 60.22 . 1 233 . 37 SER CB C 66.68 . 1 234 . 37 SER N N 125.15 . 1 235 . 38 SER H H 9.37 . 1 236 . 38 SER HA H 4.19 . 1 237 . 38 SER HB2 H 3.65 . 2 238 . 38 SER HB3 H 3.75 . 2 239 . 38 SER CA C 60.79 . 1 240 . 38 SER N N 113.99 . 1 241 . 39 PHE H H 8.62 . 1 242 . 39 PHE HA H 5.3 . 1 243 . 39 PHE HB2 H 3.2 . 2 244 . 39 PHE HB3 H 2.72 . 2 245 . 39 PHE CA C 54.31 . 1 246 . 39 PHE CB C 38.43 . 1 247 . 39 PHE N N 123.72 . 1 248 . 40 TYR H H 9.38 . 1 249 . 40 TYR HA H 5.06 . 1 250 . 40 TYR HB2 H 2.77 . 2 251 . 40 TYR HB3 H 3 . 2 252 . 40 TYR CA C 59.4 . 1 253 . 40 TYR CB C 41.99 . 1 254 . 40 TYR N N 124.96 . 1 255 . 41 ARG H H 8.82 . 1 256 . 41 ARG HA H 5.63 . 1 257 . 41 ARG HB2 H 1.57 . 2 258 . 41 ARG HB3 H 1.61 . 2 259 . 41 ARG HG2 H 1.41 . 1 260 . 41 ARG HG3 H 1.41 . 1 261 . 41 ARG HD2 H 2.66 . 2 262 . 41 ARG HD3 H 3.14 . 2 263 . 41 ARG CA C 55.43 . 1 264 . 41 ARG CB C 35.31 . 1 265 . 41 ARG CG C 25.67 . 1 266 . 41 ARG CD C 43.64 . 1 267 . 41 ARG N N 125.55 . 1 268 . 42 THR H H 8.35 . 1 269 . 42 THR HA H 4.4 . 1 270 . 42 THR HB H 4.32 . 1 271 . 42 THR HG1 H 1.03 . 1 272 . 42 THR CA C 60.91 . 1 273 . 42 THR CB C 70.54 . 1 274 . 42 THR N N 128.71 . 1 275 . 44 PRO HA H 4.37 . 1 276 . 44 PRO HB2 H 2.08 . 2 277 . 44 PRO HB3 H 1.85 . 2 278 . 44 PRO HG2 H 1.93 . 2 279 . 44 PRO HG3 H 1.78 . 2 280 . 44 PRO HD2 H 3.85 . 2 281 . 44 PRO HD3 H 3.65 . 2 282 . 44 PRO CA C 63.27 . 1 283 . 44 PRO CB C 33.15 . 1 284 . 45 LEU H H 8.23 . 1 285 . 45 LEU HA H 4.35 . 1 286 . 45 LEU HB2 H 1.49 . 2 287 . 45 LEU HB3 H 1.57 . 2 288 . 45 LEU HD1 H 0.81 . 1 289 . 45 LEU HD2 H 0.81 . 1 290 . 45 LEU CA C 55.8 . 1 291 . 45 LEU N N 123.91 . 1 292 . 46 GLY H H 8.19 . 1 293 . 46 GLY HA2 H 4.16 . 2 294 . 46 GLY HA3 H 3.81 . 2 295 . 46 GLY CA C 44.92 . 1 296 . 46 GLY N N 111.69 . 1 297 . 47 PRO HA H 4.34 . 1 298 . 47 PRO HB2 H 1.93 . 2 299 . 47 PRO HB3 H 2.21 . 2 300 . 47 PRO HG2 H 1.76 . 2 301 . 47 PRO HG3 H 1.85 . 2 302 . 47 PRO HD2 H 3.6 . 2 303 . 47 PRO HD3 H 3.55 . 2 304 . 47 PRO CA C 64.37 . 1 305 . 48 GLN HA H 4.15 . 1 306 . 48 GLN HB2 H 1.92 . 1 307 . 48 GLN HB3 H 1.92 . 1 308 . 48 GLN HG2 H 2.32 . 1 309 . 48 GLN HG3 H 2.32 . 1 310 . 48 GLN CA C 56.93 . 1 311 . 48 GLN CB C 28.04 . 1 312 . 48 GLN CG C 34.69 . 1 313 . 49 ASP H H 7.49 . 1 314 . 49 ASP HA H 4.5 . 1 315 . 49 ASP HB2 H 2.55 . 2 316 . 49 ASP HB3 H 2.63 . 2 317 . 49 ASP CA C 54.6 . 1 318 . 49 ASP CB C 40.56 . 1 319 . 49 ASP N N 121.96 . 1 320 . 50 GLN H H 8.36 . 1 321 . 50 GLN HA H 4.4 . 1 322 . 50 GLN HB2 H 1.65 . 2 323 . 50 GLN HB3 H 2.19 . 2 324 . 50 GLN HG2 H 2.21 . 2 325 . 50 GLN HG3 H 2.01 . 2 326 . 50 GLN CA C 54.6 . 1 327 . 50 GLN CB C 28.86 . 1 328 . 50 GLN CG C 36.46 . 1 329 . 50 GLN N N 121.22 . 1 330 . 51 PRO HA H 4.3 . 1 331 . 51 PRO HB2 H 1.8 . 2 332 . 51 PRO HB3 H 2.2 . 2 333 . 51 PRO HG2 H 1.77 . 2 334 . 51 PRO HG3 H 1.93 . 2 335 . 51 PRO HD2 H 3.62 . 2 336 . 51 PRO HD3 H 3.43 . 2 337 . 51 PRO CA C 63.37 . 1 338 . 51 PRO CB C 33.2 . 1 339 . 51 PRO CD C 51.5 . 1 340 . 52 ASP H H 7.85 . 1 341 . 52 ASP HA H 4.45 . 1 342 . 52 ASP HB2 H 2.33 . 1 343 . 52 ASP HB3 H 2.33 . 1 344 . 52 ASP CA C 55.77 . 1 345 . 52 ASP N N 120.62 . 1 346 . 53 TYR H H 8.42 . 1 347 . 53 TYR HA H 4.75 . 1 348 . 53 TYR HB2 H 3.05 . 2 349 . 53 TYR HB3 H 3.21 . 2 350 . 53 TYR CA C 57.4 . 1 351 . 53 TYR N N 123.76 . 1 352 . 54 LEU H H 8.53 . 1 353 . 54 LEU HA H 5.29 . 1 354 . 54 LEU HB2 H 0.83 . 1 355 . 54 LEU HB3 H 0.83 . 1 356 . 54 LEU HG H 1.05 . 1 357 . 54 LEU HD1 H 0.05 . 1 358 . 54 LEU HD2 H -0.61 . 1 359 . 54 LEU CA C 55.35 . 1 360 . 54 LEU CB C 44.72 . 1 361 . 54 LEU CG C 29.27 . 1 362 . 54 LEU N N 124.37 . 1 363 . 55 ASN H H 9.05 . 1 364 . 55 ASN HA H 6.04 . 1 365 . 55 ASN HB2 H 3.08 . 2 366 . 55 ASN HB3 H 2.3 . 2 367 . 55 ASN CA C 53.84 . 1 368 . 55 ASN CB C 45.81 . 1 369 . 55 ASN N N 124.61 . 1 370 . 56 ALA H H 9.1 . 1 371 . 56 ALA HA H 4.85 . 1 372 . 56 ALA HB H 1.37 . 1 373 . 56 ALA CA C 52.37 . 1 374 . 56 ALA CB C 24.14 . 1 375 . 56 ALA N N 124 . 1 376 . 57 ALA H H 9.38 . 1 377 . 57 ALA HA H 5.56 . 1 378 . 57 ALA HB H 1.24 . 1 379 . 57 ALA CA C 51.86 . 1 380 . 57 ALA N N 124.96 . 1 381 . 58 VAL H H 9.07 . 1 382 . 58 VAL HA H 4.82 . 1 383 . 58 VAL HB H 1.86 . 1 384 . 58 VAL HG1 H 0.87 . 1 385 . 58 VAL HG2 H 0.87 . 1 386 . 58 VAL CA C 60.65 . 1 387 . 58 VAL N N 119.15 . 1 388 . 59 ALA H H 8.5 . 1 389 . 59 ALA HA H 4.73 . 1 390 . 59 ALA HB H 1.13 . 1 391 . 59 ALA CA C 50.88 . 1 392 . 59 ALA N N 130.97 . 1 393 . 60 LEU H H 9.23 . 1 394 . 60 LEU HA H 4.62 . 1 395 . 60 LEU HB2 H 1.72 . 1 396 . 60 LEU HB3 H 1.72 . 1 397 . 60 LEU HG H 1.17 . 1 398 . 60 LEU HD1 H 0.62 . 1 399 . 60 LEU HD2 H 0.54 . 1 400 . 60 LEU CA C 53.99 . 1 401 . 60 LEU CB C 48.09 . 1 402 . 60 LEU CG C 27.52 . 1 403 . 60 LEU N N 129.74 . 1 404 . 61 GLU H H 8.67 . 1 405 . 61 GLU HA H 4.64 . 1 406 . 61 GLU HB2 H 1.64 . 2 407 . 61 GLU HB3 H 1.21 . 2 408 . 61 GLU HG2 H 1.83 . 2 409 . 61 GLU HG3 H 2.1 . 2 410 . 61 GLU CA C 55.73 . 1 411 . 61 GLU CB C 30.58 . 1 412 . 61 GLU CG C 36.84 . 1 413 . 61 GLU N N 131.15 . 1 414 . 62 THR H H 9.1 . 1 415 . 62 THR HA H 5.41 . 1 416 . 62 THR HB H 3.71 . 1 417 . 62 THR HG1 H 0.98 . 1 418 . 62 THR CA C 61.43 . 1 419 . 62 THR CB C 71.68 . 1 420 . 62 THR CG2 C 19.04 . 1 421 . 62 THR N N 123.06 . 1 422 . 63 SER H H 8.1 . 1 423 . 63 SER HA H 4.89 . 1 424 . 63 SER HB2 H 3.99 . 1 425 . 63 SER HB3 H 3.94 . 1 426 . 63 SER CA C 58.57 . 1 427 . 63 SER CB C 64.7 . 1 428 . 63 SER N N 124.08 . 1 429 . 64 LEU H H 8.42 . 1 430 . 64 LEU HA H 4.12 . 1 431 . 64 LEU HB2 H 1.65 . 2 432 . 64 LEU HB3 H 1.3 . 2 433 . 64 LEU HG H 1.41 . 1 434 . 64 LEU HD1 H 0.59 . 1 435 . 64 LEU HD2 H 0.65 . 1 436 . 64 LEU CA C 55.57 . 1 437 . 64 LEU CB C 43.6 . 1 438 . 64 LEU N N 125.75 . 1 439 . 65 ALA H H 8.27 . 1 440 . 65 ALA HA H 4.5 . 1 441 . 65 ALA HB H 1.34 . 1 442 . 65 ALA CA C 51.2 . 1 443 . 65 ALA N N 124.43 . 1 444 . 66 PRO HA H 4.32 . 1 445 . 66 PRO HB2 H 2.5 . 2 446 . 66 PRO HB3 H 1.81 . 2 447 . 66 PRO HG2 H 1.31 . 2 448 . 66 PRO HG3 H 1.9 . 2 449 . 66 PRO HD2 H 3.11 . 2 450 . 66 PRO HD3 H 3.23 . 2 451 . 66 PRO CA C 66.9 . 1 452 . 66 PRO CB C 31.4 . 1 453 . 67 GLU H H 8.63 . 1 454 . 67 GLU HA H 3.54 . 1 455 . 67 GLU HB2 H 1.75 . 1 456 . 67 GLU HB3 H 1.75 . 1 457 . 67 GLU HG2 H 2.04 . 2 458 . 67 GLU HG3 H 1.89 . 2 459 . 67 GLU CA C 60.52 . 1 460 . 67 GLU N N 115.31 . 1 461 . 68 GLU H H 6.74 . 1 462 . 68 GLU HA H 4.18 . 1 463 . 68 GLU HB2 H 2.07 . 2 464 . 68 GLU HB3 H 2.2 . 2 465 . 68 GLU HG2 H 2.29 . 1 466 . 68 GLU HG3 H 2.29 . 1 467 . 68 GLU CA C 58.69 . 1 468 . 68 GLU N N 119.86 . 1 469 . 69 LEU H H 8.05 . 1 470 . 69 LEU N N 122.81 . 1 471 . 70 LEU H H 7.64 . 1 472 . 70 LEU N N 121.5 . 1 473 . 71 ASN H H 7.58 . 1 474 . 71 ASN HA H 4.18 . 1 475 . 71 ASN HB2 H 2.96 . 2 476 . 71 ASN HB3 H 2.5 . 2 477 . 71 ASN CA C 56.74 . 1 478 . 71 ASN CB C 37.73 . 1 479 . 71 ASN N N 118.7 . 1 480 . 72 HIS H H 7.64 . 1 481 . 72 HIS HA H 4.28 . 1 482 . 72 HIS HB2 H 3.32 . 2 483 . 72 HIS HB3 H 2.85 . 2 484 . 72 HIS CA C 62.04 . 1 485 . 72 HIS N N 120.82 . 1 486 . 73 THR H H 9.23 . 1 487 . 73 THR HA H 3.82 . 1 488 . 73 THR HB H 4.15 . 1 489 . 73 THR HG1 H 0.96 . 1 490 . 73 THR CA C 67.88 . 1 491 . 73 THR N N 116 . 1 492 . 74 GLN H H 8.72 . 1 493 . 74 GLN HA H 4.15 . 1 494 . 74 GLN HB2 H 2.12 . 2 495 . 74 GLN HB3 H 2.16 . 2 496 . 74 GLN HG2 H 2.36 . 2 497 . 74 GLN HG3 H 2.32 . 2 498 . 74 GLN N N 123.85 . 1 499 . 75 ARG H H 7.51 . 1 500 . 75 ARG HA H 4.04 . 1 501 . 75 ARG HB2 H 2.15 . 2 502 . 75 ARG HB3 H 1.78 . 2 503 . 75 ARG HG2 H 1.43 . 2 504 . 75 ARG HG3 H 1.57 . 2 505 . 75 ARG HD2 H 3.07 . 2 506 . 75 ARG HD3 H 3.22 . 2 507 . 75 ARG CA C 60.23 . 1 508 . 75 ARG N N 123.38 . 1 509 . 76 ILE H H 8 . 1 510 . 76 ILE HA H 3.68 . 1 511 . 76 ILE HB H 1.78 . 1 512 . 76 ILE HG12 H 0.77 . 4 513 . 76 ILE HG13 H 0.77 . 4 514 . 76 ILE HG2 H 0.64 . 4 515 . 76 ILE HD1 H 0.87 . 4 516 . 76 ILE CA C 66.52 . 1 517 . 76 ILE N N 123.59 . 1 518 . 77 GLU H H 8.22 . 1 519 . 77 GLU HA H 3.55 . 1 520 . 77 GLU HB2 H 1.76 . 1 521 . 77 GLU HB3 H 1.76 . 1 522 . 77 GLU HG2 H 2.74 . 2 523 . 77 GLU HG3 H 1.97 . 2 524 . 77 GLU CA C 61.4 . 1 525 . 77 GLU CG C 38 . 1 526 . 77 GLU N N 120.83 . 1 527 . 78 LEU H H 7.34 . 1 528 . 78 LEU HA H 3.94 . 1 529 . 78 LEU HB2 H 1.77 . 2 530 . 78 LEU HB3 H 1.38 . 2 531 . 78 LEU HG H 1.63 . 1 532 . 78 LEU HD1 H 0.72 . 1 533 . 78 LEU HD2 H 0.66 . 1 534 . 78 LEU CB C 42.77 . 1 535 . 78 LEU CG C 27.6 . 1 536 . 78 LEU CD1 C 23.68 . 1 537 . 78 LEU CD2 C 25.48 . 1 538 . 78 LEU N N 117.53 . 1 539 . 79 GLN H H 8.47 . 1 540 . 79 GLN N N 119.36 . 1 541 . 81 GLY H H 7.9 . 1 542 . 81 GLY HA2 H 4.09 . 1 543 . 81 GLY HA3 H 4.09 . 1 544 . 81 GLY CA C 47.98 . 1 545 . 81 GLY N N 107.97 . 1 546 . 83 VAL H H 8.49 . 1 547 . 83 VAL N N 123.4 . 1 548 . 84 ARG H H 8.59 . 1 549 . 84 ARG N N 129.79 . 1 550 . 85 LYS H H 8.21 . 1 551 . 85 LYS N N 128.16 . 1 552 . 86 ALA H H 8.67 . 1 553 . 86 ALA N N 130.03 . 1 554 . 87 GLU H H 8.41 . 1 555 . 87 GLU HA H 3.96 . 1 556 . 87 GLU HB2 H 1.9 . 2 557 . 87 GLU HB3 H 1.98 . 2 558 . 87 GLU HG2 H 2.08 . 2 559 . 87 GLU HG3 H 2.14 . 2 560 . 87 GLU CA C 57.62 . 1 561 . 87 GLU N N 118.02 . 1 562 . 88 ARG H H 7.76 . 1 563 . 88 ARG N N 121.8 . 1 564 . 89 TRP HA H 4.77 . 1 565 . 89 TRP HB2 H 3.06 . 2 566 . 89 TRP HB3 H 3.22 . 2 567 . 89 TRP CA C 58.01 . 1 568 . 89 TRP CB C 30.58 . 1 569 . 90 GLY H H 7.36 . 1 570 . 90 GLY HA2 H 3.68 . 2 571 . 90 GLY HA3 H 4.07 . 2 572 . 90 GLY CA C 45.36 . 1 573 . 90 GLY N N 106.89 . 1 574 . 91 PRO HA H 4.41 . 1 575 . 91 PRO HB2 H 2.17 . 2 576 . 91 PRO HB3 H 1.76 . 2 577 . 91 PRO HG2 H 1.86 . 1 578 . 91 PRO HG3 H 1.86 . 1 579 . 91 PRO HD2 H 3.53 . 1 580 . 91 PRO HD3 H 3.53 . 1 581 . 91 PRO CA C 63.28 . 1 582 . 91 PRO CB C 33.45 . 1 583 . 91 PRO CD C 50.23 . 1 584 . 92 ARG H H 8.56 . 1 585 . 92 ARG HA H 4.46 . 1 586 . 92 ARG HB2 H 1.55 . 2 587 . 92 ARG HB3 H 1.45 . 2 588 . 92 ARG HD2 H 3.06 . 2 589 . 92 ARG CA C 57.1 . 1 590 . 92 ARG N N 122.43 . 1 591 . 93 THR H H 8.82 . 1 592 . 93 THR HA H 4.75 . 1 593 . 93 THR HB H 4.42 . 1 594 . 93 THR HG1 H 1.05 . 1 595 . 93 THR CA C 62.4 . 1 596 . 93 THR N N 118.32 . 1 597 . 94 LEU H H 6.87 . 1 598 . 94 LEU HA H 4.98 . 1 599 . 94 LEU HB2 H 1.32 . 2 600 . 94 LEU HB3 H 1.29 . 2 601 . 94 LEU HG H 0.68 . 1 602 . 94 LEU HD1 H 0.63 . 1 603 . 94 LEU CA C 54.6 . 1 604 . 94 LEU N N 123.83 . 1 605 . 95 ASP H H 9.13 . 1 606 . 95 ASP HA H 5.06 . 1 607 . 95 ASP HB2 H 2.49 . 1 608 . 95 ASP HB3 H 2.49 . 1 609 . 95 ASP CA C 53.47 . 1 610 . 95 ASP N N 128.82 . 1 611 . 96 LEU H H 10.41 . 1 612 . 96 LEU HA H 5.37 . 1 613 . 96 LEU HB2 H 1.51 . 1 614 . 96 LEU HB3 H 1.51 . 1 615 . 96 LEU HG H 0.87 . 1 616 . 96 LEU HD1 H 0.83 . 1 617 . 96 LEU HD2 H 0.94 . 1 618 . 96 LEU N N 132.87 . 1 619 . 97 ASP H H 8.79 . 1 620 . 97 ASP HA H 5.38 . 1 621 . 97 ASP HB2 H 2.4 . 2 622 . 97 ASP HB3 H 2.15 . 2 623 . 97 ASP CA C 53.25 . 1 624 . 97 ASP N N 129.02 . 1 625 . 98 ILE H H 10.7 . 1 626 . 98 ILE HA H 4.08 . 1 627 . 98 ILE HB H 2 . 1 628 . 98 ILE HG12 H 1.76 . 4 629 . 98 ILE HG2 H 0.85 . 4 630 . 98 ILE HD1 H 0.71 . 4 631 . 98 ILE CA C 64 . 1 632 . 98 ILE N N 130.51 . 1 633 . 99 MET H H 9.43 . 1 634 . 99 MET HA H 4.42 . 1 635 . 99 MET HB2 H 2.56 . 2 636 . 99 MET HB3 H 2.59 . 2 637 . 99 MET HG2 H 2.15 . 2 638 . 99 MET HG3 H 2.22 . 2 639 . 99 MET CA C 61 . 1 640 . 99 MET N N 130.62 . 1 641 . 100 LEU H H 7.39 . 1 642 . 100 LEU HA H 4.72 . 1 643 . 100 LEU HB2 H 1.9 . 2 644 . 100 LEU HB3 H 1.7 . 2 645 . 100 LEU HG H 1.51 . 1 646 . 100 LEU HD1 H 0.94 . 1 647 . 100 LEU HD2 H 0.58 . 1 648 . 100 LEU CA C 54.91 . 1 649 . 100 LEU N N 113.86 . 1 650 . 101 PHE H H 9.62 . 1 651 . 101 PHE HA H 4.44 . 1 652 . 101 PHE HB2 H 3.22 . 2 653 . 101 PHE HB3 H 2.21 . 2 654 . 101 PHE CA C 58.48 . 1 655 . 101 PHE CB C 42.17 . 1 656 . 101 PHE N N 128.91 . 1 657 . 102 GLY H H 8.29 . 1 658 . 102 GLY HA2 H 3.77 . 1 659 . 102 GLY HA3 H 3.77 . 1 660 . 102 GLY CA C 48.31 . 1 661 . 102 GLY N N 115.98 . 1 662 . 103 ASN H H 9.13 . 1 663 . 103 ASN HA H 5.06 . 1 664 . 103 ASN HB2 H 2.89 . 2 665 . 103 ASN HB3 H 2.57 . 2 666 . 103 ASN CA C 52.65 . 1 667 . 103 ASN CB C 39.96 . 1 668 . 103 ASN N N 130.18 . 1 669 . 104 GLU H H 8.22 . 1 670 . 104 GLU HA H 4.14 . 1 671 . 104 GLU HB2 H 2.05 . 1 672 . 104 GLU HB3 H 2.05 . 1 673 . 104 GLU HG2 H 2.5 . 2 674 . 104 GLU HG3 H 2.41 . 2 675 . 104 GLU CA C 58.4 . 1 676 . 104 GLU CB C 31.48 . 1 677 . 104 GLU N N 119.78 . 1 678 . 105 VAL H H 8.05 . 1 679 . 105 VAL HA H 4.59 . 1 680 . 105 VAL HB H 1.9 . 1 681 . 105 VAL HG1 H 0.92 . 1 682 . 105 VAL HG2 H 0.92 . 1 683 . 105 VAL CA C 62.62 . 1 684 . 105 VAL CB C 33.79 . 1 685 . 105 VAL N N 122.13 . 1 686 . 106 ILE H H 9.28 . 1 687 . 106 ILE HA H 4.21 . 1 688 . 106 ILE HB H 1.3 . 1 689 . 106 ILE HG12 H 0.97 . 1 690 . 106 ILE HG13 H 0.97 . 1 691 . 106 ILE HG2 H 0.82 . 1 692 . 106 ILE HD1 H 0.54 . 1 693 . 106 ILE CA C 61.47 . 1 694 . 106 ILE CG1 C 18.51 . 1 695 . 106 ILE CG2 C 14.72 . 1 696 . 106 ILE N N 131.8 . 1 697 . 107 ASN H H 9.09 . 1 698 . 107 ASN HA H 5.38 . 1 699 . 107 ASN HB2 H 2.63 . 2 700 . 107 ASN HB3 H 2.57 . 2 701 . 107 ASN CA C 53.93 . 1 702 . 107 ASN CB C 42.79 . 1 703 . 107 ASN N N 129.8 . 1 704 . 108 THR H H 8.73 . 1 705 . 108 THR HA H 4.75 . 1 706 . 108 THR HB H 4.53 . 1 707 . 108 THR HG1 H 1.11 . 1 708 . 108 THR CA C 60.23 . 1 709 . 108 THR CB C 73.49 . 1 710 . 108 THR N N 116.64 . 1 711 . 109 GLU H H 8.73 . 1 712 . 109 GLU HA H 3.91 . 1 713 . 109 GLU HB2 H 1.91 . 1 714 . 109 GLU HB3 H 1.91 . 1 715 . 109 GLU HG2 H 2.18 . 2 716 . 109 GLU HG3 H 1.85 . 2 717 . 109 GLU CA C 60 . 1 718 . 109 GLU CB C 30 . 1 719 . 109 GLU CG C 37.81 . 1 720 . 109 GLU N N 121.37 . 1 721 . 110 ARG H H 7.88 . 1 722 . 110 ARG HA H 4.13 . 1 723 . 110 ARG HB2 H 1.29 . 2 724 . 110 ARG HB3 H 1.5 . 2 725 . 110 ARG HG2 H 1.65 . 2 726 . 110 ARG HD2 H 3.13 . 2 727 . 110 ARG CA C 57.66 . 1 728 . 110 ARG N N 114.54 . 1 729 . 111 LEU H H 7.46 . 1 730 . 111 LEU HA H 3.88 . 1 731 . 111 LEU HB2 H 1.31 . 2 732 . 111 LEU HB3 H 0.7 . 2 733 . 111 LEU HG H 0.96 . 1 734 . 111 LEU HD1 H 0.3 . 1 735 . 111 LEU HD2 H 0.26 . 1 736 . 111 LEU CA C 54.27 . 1 737 . 111 LEU N N 122.38 . 1 738 . 112 THR HA H 5.16 . 1 739 . 112 THR HB H 4.27 . 1 740 . 112 THR HG1 H 1.34 . 1 741 . 113 VAL H H 9.23 . 1 742 . 113 VAL HA H 4.21 . 1 743 . 113 VAL HG2 H 0.76 . 1 744 . 113 VAL CA C 60.15 . 1 745 . 113 VAL CB C 38.16 . 1 746 . 113 VAL N N 130 . 1 747 . 114 PRO HA H 5.3 . 1 748 . 114 PRO HB3 H 1.98 . 2 749 . 114 PRO HG2 H 2.37 . 2 750 . 114 PRO HD3 H 4.06 . 2 751 . 114 PRO CA C 63.28 . 1 752 . 114 PRO CB C 35.3 . 1 753 . 114 PRO CG C 27.01 . 1 754 . 115 HIS H H 8.61 . 1 755 . 115 HIS HA H 4.47 . 1 756 . 115 HIS HB2 H 3.69 . 2 757 . 115 HIS HB3 H 2.82 . 2 758 . 115 HIS CA C 60 . 1 759 . 115 HIS CB C 32.13 . 1 760 . 115 HIS N N 127.71 . 1 761 . 116 TYR HA H 4.39 . 9 762 . 116 TYR HB2 H 3.19 . 9 763 . 116 TYR HB3 H 3.11 . 9 764 . 116 TYR CA C 61 . 9 765 . 117 ASP H H 8.38 . 1 766 . 117 ASP N N 125.83 . 1 767 . 118 MET H H 7.44 . 1 768 . 118 MET HA H 3.73 . 1 769 . 118 MET HB2 H 2.81 . 2 770 . 118 MET HB3 H 1.87 . 2 771 . 118 MET HG2 H 3.15 . 2 772 . 118 MET HG3 H 2.04 . 2 773 . 118 MET CA C 60.74 . 1 774 . 118 MET N N 121.74 . 1 775 . 119 LYS H H 7.97 . 1 776 . 119 LYS HA H 3.67 . 1 777 . 119 LYS HB2 H 1.46 . 2 778 . 119 LYS HB3 H 1.55 . 2 779 . 119 LYS HG2 H 1.18 . 2 780 . 119 LYS HG3 H 1.14 . 2 781 . 119 LYS HD2 H 1.39 . 2 782 . 119 LYS HD3 H 1.58 . 2 783 . 119 LYS HE2 H 3.15 . 1 784 . 119 LYS CA C 59.86 . 1 785 . 119 LYS CB C 32.51 . 1 786 . 119 LYS N N 116.93 . 1 787 . 120 ASN H H 7.36 . 1 788 . 120 ASN HA H 4.91 . 1 789 . 120 ASN HB2 H 2.44 . 2 790 . 120 ASN HB3 H 2.89 . 2 791 . 120 ASN CA C 53.11 . 1 792 . 120 ASN N N 111.7 . 1 793 . 121 ARG H H 6.91 . 1 794 . 121 ARG HA H 4.16 . 1 795 . 121 ARG HB2 H 1.31 . 2 796 . 121 ARG HB3 H 1.29 . 2 797 . 121 ARG HG2 H 0.93 . 2 798 . 121 ARG HD2 H 2.73 . 2 799 . 121 ARG CA C 54.3 . 1 800 . 121 ARG N N 121.09 . 1 801 . 122 GLY H H 9.16 . 1 802 . 122 GLY HA2 H 3.94 . 2 803 . 122 GLY HA3 H 2.72 . 2 804 . 122 GLY CA C 48.42 . 1 805 . 122 GLY N N 120.4 . 1 806 . 123 PHE H H 6.87 . 1 807 . 123 PHE HA H 4.24 . 1 808 . 123 PHE HB2 H 2.79 . 2 809 . 123 PHE HB3 H 3.08 . 2 810 . 123 PHE CA C 58.5 . 1 811 . 123 PHE CB C 38.13 . 1 812 . 123 PHE N N 112 . 1 813 . 124 MET H H 6.37 . 1 814 . 124 MET HA H 4.26 . 1 815 . 124 MET HB2 H 1.46 . 1 816 . 124 MET HB3 H 1.46 . 1 817 . 124 MET N N 119.22 . 1 818 . 125 LEU H H 7.32 . 1 819 . 125 LEU HA H 3.7 . 1 820 . 125 LEU HB2 H 0.82 . 2 821 . 125 LEU HB3 H 0.98 . 2 822 . 125 LEU HG H 1.7 . 1 823 . 125 LEU HD1 H 0.36 . 1 824 . 125 LEU HD2 H 0.23 . 1 825 . 125 LEU CA C 58.27 . 1 826 . 125 LEU CB C 43.79 . 1 827 . 125 LEU CG C 22.58 . 1 828 . 125 LEU CD1 C 27.33 . 1 829 . 125 LEU N N 117.06 . 1 830 . 126 TRP H H 8.58 . 1 831 . 126 TRP HA H 4.66 . 1 832 . 126 TRP HB2 H 2.85 . 2 833 . 126 TRP HB3 H 2.92 . 2 834 . 126 TRP CA C 62.9 . 1 835 . 126 TRP N N 118.59 . 1 836 . 127 PRO HA H 4.31 . 1 837 . 127 PRO HB2 H 2.51 . 2 838 . 127 PRO HB3 H 1.81 . 2 839 . 127 PRO HG2 H 1.91 . 2 840 . 127 PRO HG3 H 1.31 . 2 841 . 127 PRO HD2 H 3.14 . 2 842 . 127 PRO HD3 H 3.08 . 2 843 . 127 PRO CA C 66.77 . 1 844 . 127 PRO CB C 31.48 . 1 845 . 128 LEU H H 6.43 . 1 846 . 128 LEU HA H 3.78 . 1 847 . 128 LEU HB2 H 1.11 . 1 848 . 128 LEU HB3 H 1.11 . 1 849 . 128 LEU HG H 1.11 . 1 850 . 128 LEU HD1 H 0.48 . 1 851 . 128 LEU HD2 H 0.24 . 1 852 . 128 LEU CA C 57.89 . 1 853 . 128 LEU N N 116.33 . 1 854 . 129 PHE H H 8.47 . 1 855 . 129 PHE HA H 3.78 . 1 856 . 129 PHE HB2 H 3.06 . 2 857 . 129 PHE HB3 H 2.8 . 2 858 . 129 PHE CA C 60.85 . 1 859 . 129 PHE N N 121.17 . 1 860 . 130 GLU H H 7.45 . 1 861 . 130 GLU HA H 3.78 . 1 862 . 130 GLU HB2 H 2.2 . 2 863 . 130 GLU HB3 H 2.4 . 2 864 . 130 GLU HG2 H 2.18 . 2 865 . 130 GLU HG3 H 2.45 . 2 866 . 130 GLU CA C 59.73 . 1 867 . 130 GLU N N 118.08 . 1 868 . 131 ILE H H 6.8 . 1 869 . 131 ILE HA H 4.39 . 1 870 . 131 ILE HB H 2.03 . 1 871 . 131 ILE HG12 H 1.75 . 4 872 . 131 ILE HG2 H 0.75 . 4 873 . 131 ILE HD1 H 0.92 . 4 874 . 131 ILE CA C 62.15 . 1 875 . 131 ILE CB C 39.74 . 1 876 . 131 ILE N N 106.94 . 1 877 . 132 ALA H H 8.21 . 1 878 . 132 ALA HA H 4.66 . 1 879 . 132 ALA HB H 0.9 . 1 880 . 132 ALA CA C 51.5 . 1 881 . 132 ALA CB C 19.69 . 1 882 . 132 ALA N N 131.37 . 1 883 . 133 PRO HA H 4.02 . 1 884 . 133 PRO HB2 H 1.51 . 2 885 . 133 PRO HB3 H 1.43 . 2 886 . 133 PRO HG2 H 1.7 . 1 887 . 133 PRO HG3 H 1.7 . 1 888 . 133 PRO HD2 H 3.3 . 2 889 . 133 PRO HD3 H 3 . 2 890 . 133 PRO CA C 65.45 . 1 891 . 133 PRO CB C 32.19 . 1 892 . 133 PRO CG C 28 . 1 893 . 134 GLU H H 8.17 . 1 894 . 134 GLU HA H 4.43 . 1 895 . 134 GLU HB2 H 2.2 . 2 896 . 134 GLU HB3 H 1.66 . 2 897 . 134 GLU HG2 H 2.2 . 2 898 . 134 GLU HG3 H 2.01 . 2 899 . 134 GLU CB C 36.55 . 1 900 . 134 GLU CG C 28.5 . 1 901 . 134 GLU N N 116.51 . 1 902 . 135 LEU HA H 3.74 . 1 903 . 135 LEU HB2 H 1.63 . 2 904 . 135 LEU HB3 H 1.21 . 2 905 . 135 LEU HG H 1.11 . 1 906 . 135 LEU HD1 H 0.01 . 1 907 . 135 LEU HD2 H 0.3 . 1 908 . 135 LEU CA C 58.69 . 1 909 . 135 LEU CB C 43.1 . 1 910 . 135 LEU CG C 27.44 . 1 911 . 135 LEU N N 124.46 . 1 912 . 136 VAL H H 8.29 . 1 913 . 136 VAL HA H 4.41 . 1 914 . 136 VAL HB H 1.84 . 1 915 . 136 VAL HG1 H 0.93 . 1 916 . 136 VAL HG2 H 0.93 . 1 917 . 136 VAL CA C 61.88 . 1 918 . 136 VAL CB C 34.94 . 1 919 . 136 VAL N N 130.53 . 1 920 . 137 PHE H H 9.11 . 1 921 . 137 PHE HA H 4.2 . 1 922 . 137 PHE HB2 H 3.25 . 2 923 . 137 PHE HB3 H 3.15 . 2 924 . 137 PHE CA C 59.507 . 1 925 . 137 PHE CB C 39.08 . 1 926 . 137 PHE N N 128.06 . 1 927 . 138 PRO HA H 4.38 . 1 928 . 138 PRO HB2 H 1.92 . 2 929 . 138 PRO HB3 H 1.77 . 2 930 . 138 PRO HG2 H 1.86 . 2 931 . 138 PRO HG3 H 1.9 . 2 932 . 138 PRO HD2 H 3.56 . 1 933 . 138 PRO HD3 H 3.56 . 1 934 . 138 PRO CA C 66.52 . 1 935 . 139 ASP H H 7.42 . 1 936 . 139 ASP HA H 4.4 . 1 937 . 139 ASP HB2 H 2.52 . 2 938 . 139 ASP HB3 H 2.93 . 2 939 . 139 ASP CA C 54.31 . 1 940 . 139 ASP CB C 41.09 . 1 941 . 139 ASP N N 112.78 . 1 942 . 140 GLY H H 8.27 . 1 943 . 140 GLY HA2 H 4.3 . 2 944 . 140 GLY HA3 H 3.42 . 2 945 . 140 GLY CA C 45.59 . 1 946 . 140 GLY N N 109.6 . 1 947 . 141 GLU H H 7.88 . 1 948 . 141 GLU HA H 4.19 . 1 949 . 141 GLU HB2 H 1.66 . 2 950 . 141 GLU HB3 H 1.78 . 2 951 . 141 GLU HG2 H 2.18 . 2 952 . 141 GLU HG3 H 1.96 . 2 953 . 141 GLU CA C 58.02 . 1 954 . 141 GLU CB C 31.26 . 1 955 . 141 GLU N N 123.23 . 1 956 . 142 MET H H 9.13 . 1 957 . 142 MET HA H 4.7 . 1 958 . 142 MET HB2 H 2.16 . 2 959 . 142 MET HB3 H 1.97 . 2 960 . 142 MET HG2 H 2.71 . 2 961 . 142 MET HG3 H 2.55 . 2 962 . 142 MET CA C 56.66 . 1 963 . 142 MET N N 125.15 . 1 964 . 143 LEU H H 8.31 . 1 965 . 143 LEU HA H 4.08 . 1 966 . 143 LEU HB2 H 1.2 . 1 967 . 143 LEU HB3 H 1.2 . 1 968 . 143 LEU HG H 0.9 . 1 969 . 143 LEU HD1 H 0.83 . 1 970 . 143 LEU HD2 H 0.83 . 1 971 . 143 LEU CA C 59.53 . 1 972 . 143 LEU CB C 41.27 . 1 973 . 143 LEU N N 129.95 . 1 974 . 144 ARG H H 9.47 . 1 975 . 144 ARG HA H 3.42 . 1 976 . 144 ARG HB2 H 2.01 . 2 977 . 144 ARG HB3 H 1.7 . 2 978 . 144 ARG HG2 H 1.52 . 1 979 . 144 ARG HG3 H 1.52 . 1 980 . 144 ARG HD2 H 3.29 . 2 981 . 144 ARG HD3 H 3.17 . 2 982 . 144 ARG CA C 60.58 . 1 983 . 144 ARG N N 117.59 . 1 984 . 145 GLN H H 6.64 . 1 985 . 145 GLN HA H 4.15 . 1 986 . 145 GLN HB2 H 1.92 . 2 987 . 145 GLN HB3 H 2.15 . 2 988 . 145 GLN HG2 H 2.36 . 1 989 . 145 GLN CA C 58.89 . 1 990 . 145 GLN N N 117.81 . 1 991 . 146 ILE H H 7.77 . 1 992 . 146 ILE HA H 3.54 . 1 993 . 146 ILE HB H 1.7 . 1 994 . 146 ILE HG12 H 0.87 . 4 995 . 146 ILE HG13 H 0.65 . 4 996 . 146 ILE HD1 H 0.37 . 4 997 . 146 ILE CA C 65.9 . 1 998 . 146 ILE N N 124.56 . 1 999 . 147 LEU H H 7.35 . 1 1000 . 147 LEU HA H 3.59 . 1 1001 . 147 LEU HB2 H 0.6 . 2 1002 . 147 LEU HB3 H 0.99 . 2 1003 . 147 LEU HG H 0.78 . 1 1004 . 147 LEU HD1 H -0.58 . 1 1005 . 147 LEU HD2 H -0.64 . 1 1006 . 147 LEU CA C 58.39 . 1 1007 . 147 LEU CB C 42.53 . 1 1008 . 147 LEU N N 118.17 . 1 1009 . 148 HIS H H 7.45 . 1 1010 . 148 HIS HA H 4.38 . 1 1011 . 148 HIS HB2 H 3.77 . 2 1012 . 148 HIS HB3 H 3.21 . 2 1013 . 148 HIS CA C 59.1 . 1 1014 . 148 HIS N N 117.28 . 1 1015 . 149 THR H H 8.22 . 1 1016 . 149 THR HA H 3.94 . 1 1017 . 149 THR HB H 4.09 . 1 1018 . 149 THR HG1 H 1.16 . 1 1019 . 149 THR CA C 65.6 . 1 1020 . 149 THR N N 113.97 . 1 1021 . 150 ARG H H 7.74 . 1 1022 . 150 ARG HA H 3.93 . 1 1023 . 150 ARG HB2 H 2.85 . 2 1024 . 150 ARG HB3 H 2.99 . 2 1025 . 150 ARG HG2 H 1.13 . 2 1026 . 150 ARG HG3 H 0.83 . 2 1027 . 150 ARG CA C 56.48 . 1 1028 . 150 ARG N N 121.17 . 1 1029 . 151 ALA H H 7.46 . 1 1030 . 151 ALA HA H 4.01 . 1 1031 . 151 ALA HB H 1.08 . 1 1032 . 151 ALA CA C 54.1 . 1 1033 . 151 ALA N N 122.38 . 1 1034 . 152 PHE H H 7.13 . 1 1035 . 152 PHE HA H 4.55 . 1 1036 . 152 PHE HB2 H 3.3 . 2 1037 . 152 PHE HB3 H 2.6 . 2 1038 . 152 PHE CA C 58.16 . 1 1039 . 152 PHE N N 118.84 . 1 1040 . 153 ASP H H 8.71 . 1 1041 . 153 ASP HA H 4.48 . 1 1042 . 153 ASP HB2 H 2.5 . 2 1043 . 153 ASP HB3 H 2.63 . 2 1044 . 153 ASP CA C 55.52 . 1 1045 . 153 ASP CB C 43.62 . 1 1046 . 153 ASP N N 127.12 . 1 1047 . 154 LYS H H 8.26 . 1 1048 . 154 LYS HA H 2.8 . 1 1049 . 154 LYS HB2 H 1.24 . 1 1050 . 154 LYS HB3 H 1.24 . 1 1051 . 154 LYS HG2 H 0.88 . 2 1052 . 154 LYS HG3 H 0.62 . 2 1053 . 154 LYS HD2 H 1.27 . 1 1054 . 154 LYS HD3 H 1.27 . 1 1055 . 154 LYS HE2 H 2.74 . 1 1056 . 154 LYS HE3 H 2.74 . 1 1057 . 154 LYS CA C 57.5 . 1 1058 . 154 LYS CB C 33.06 . 1 1059 . 154 LYS CG C 25.6 . 1 1060 . 154 LYS CD C 29.72 . 1 1061 . 154 LYS CE C 42.8 . 1 1062 . 154 LYS N N 124.08 . 1 1063 . 155 LEU H H 7.21 . 1 1064 . 155 LEU HA H 4.42 . 1 1065 . 155 LEU HB2 H 1.37 . 2 1066 . 155 LEU HB3 H 1.52 . 2 1067 . 155 LEU HG H 0.82 . 1 1068 . 155 LEU HD1 H 0.74 . 1 1069 . 155 LEU HD2 H 0.74 . 1 1070 . 155 LEU CA C 54.26 . 1 1071 . 155 LEU CG C 23.8 . 1 1072 . 155 LEU CD1 C 26.4 . 1 1073 . 155 LEU CD2 C 26.4 . 1 1074 . 155 LEU N N 124.76 . 1 1075 . 156 ASN H H 8.94 . 1 1076 . 156 ASN HA H 4.75 . 1 1077 . 156 ASN HB2 H 2.77 . 2 1078 . 156 ASN HB3 H 2.66 . 2 1079 . 156 ASN CA C 53.48 . 1 1080 . 156 ASN CB C 40.76 . 1 1081 . 156 ASN N N 122.74 . 1 1082 . 157 LYS H H 8.45 . 1 1083 . 157 LYS HA H 4.35 . 1 1084 . 157 LYS HB2 H 1.46 . 2 1085 . 157 LYS HB3 H 1.09 . 2 1086 . 157 LYS HG2 H 1.88 . 2 1087 . 157 LYS HG3 H 2.31 . 2 1088 . 157 LYS CA C 57.35 . 1 1089 . 157 LYS CB C 29.64 . 1 1090 . 157 LYS CG C 26.6 . 1 1091 . 157 LYS N N 122.75 . 1 1092 . 158 TRP H H 8.54 . 1 1093 . 158 TRP HA H 3.77 . 1 1094 . 158 TRP HB2 H 3.03 . 2 1095 . 158 TRP HB3 H 2.71 . 2 1096 . 158 TRP CA C 62.85 . 1 1097 . 158 TRP N N 130.56 . 1 stop_ save_