data_4262 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; NMR SOLUTION STRUCTURE AND DYNAMICS OF THE COMPLEX OF LACTOBACILLUS CASEI DIHYDROFOLATE REDUCTASE WITH THE NEW LIPOPHILIC ANTIFOLATE DRUG TRIMETREXATE ; _BMRB_accession_number 4262 _BMRB_flat_file_name bmr4262.str _Entry_type original _Submission_date 1998-10-30 _Accession_date 1998-10-30 _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 POLSHAKOV V. I. . 2 BIRDSALL B. . . 3 FRENKIEL T. A. . 4 GARGARO A. R. . 5 FEENEY J. . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 2 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 884 "15N chemical shifts" 168 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2000-05-22 update BMRB 'update ligand save frame' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Structure and dynamics in solution of the complex of Lactobillus casei dihydrofolate reductase with the new lipophilic antifolate drug trimetrexate" ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 10091649 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 POLSHAKOV V. I. . 2 BIRDSALL B. . . 3 FRENKIEL T. A. . 4 GARGARO A. R. . 5 FEENEY J. . . stop_ _Journal_abbreviation 'Protein Sci.' _Journal_name_full 'Protein Science' _Journal_volume 8 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 467 _Page_last 481 _Year 1999 _Details . loop_ _Keyword OXIDOREDUCTASE 'INHIBITOR/ENZYME COMPLEX' DHFR trimetrexate 'antifolate drug' stop_ save_ ################################## # Molecular system description # ################################## save_system_DHFR _Saveframe_category molecular_system _Mol_system_name 'DIHYDROFOLATE REDUCTASE' _Abbreviation_common DHFR _Enzyme_commission_number 1.5.1.3 loop_ _Mol_system_component_name _Mol_label 'DIHYDROFOLATE REDUCTASE' $DHFR TRIMETREXATE $TMQ stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' loop_ _Biological_function ; Reduces 7,8-dihydrofolate to 5,6,7,8-tetrahydrofolate using NADPH as the coenzyme" ; stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_DHFR _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'DIHYDROFOLATE REDUCTASE' _Name_variant none _Abbreviation_common DHFR _Molecular_mass 18300 _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 162 _Mol_residue_sequence ; TAFLWAQDRDGLIGKDGHLP WHLPDDLHYFRAQTVGKIMV VGRRTYESFPKRPLPERTNV VLTHQEDYQAQGAVVVHDVA AVFAYAKQHPDQELVIAGGA QIFTAFKDDVDTLLVTRLAG SFEGDTKMIPLNWDDFTKVS SRTVEDTNPALTHTYEVWQK KA ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 THR 2 2 ALA 3 3 PHE 4 4 LEU 5 5 TRP 6 6 ALA 7 7 GLN 8 8 ASP 9 9 ARG 10 10 ASP 11 11 GLY 12 12 LEU 13 13 ILE 14 14 GLY 15 15 LYS 16 16 ASP 17 17 GLY 18 18 HIS 19 19 LEU 20 20 PRO 21 21 TRP 22 22 HIS 23 23 LEU 24 24 PRO 25 25 ASP 26 26 ASP 27 27 LEU 28 28 HIS 29 29 TYR 30 30 PHE 31 31 ARG 32 32 ALA 33 33 GLN 34 34 THR 35 35 VAL 36 36 GLY 37 37 LYS 38 38 ILE 39 39 MET 40 40 VAL 41 41 VAL 42 42 GLY 43 43 ARG 44 44 ARG 45 45 THR 46 46 TYR 47 47 GLU 48 48 SER 49 49 PHE 50 50 PRO 51 51 LYS 52 52 ARG 53 53 PRO 54 54 LEU 55 55 PRO 56 56 GLU 57 57 ARG 58 58 THR 59 59 ASN 60 60 VAL 61 61 VAL 62 62 LEU 63 63 THR 64 64 HIS 65 65 GLN 66 66 GLU 67 67 ASP 68 68 TYR 69 69 GLN 70 70 ALA 71 71 GLN 72 72 GLY 73 73 ALA 74 74 VAL 75 75 VAL 76 76 VAL 77 77 HIS 78 78 ASP 79 79 VAL 80 80 ALA 81 81 ALA 82 82 VAL 83 83 PHE 84 84 ALA 85 85 TYR 86 86 ALA 87 87 LYS 88 88 GLN 89 89 HIS 90 90 PRO 91 91 ASP 92 92 GLN 93 93 GLU 94 94 LEU 95 95 VAL 96 96 ILE 97 97 ALA 98 98 GLY 99 99 GLY 100 100 ALA 101 101 GLN 102 102 ILE 103 103 PHE 104 104 THR 105 105 ALA 106 106 PHE 107 107 LYS 108 108 ASP 109 109 ASP 110 110 VAL 111 111 ASP 112 112 THR 113 113 LEU 114 114 LEU 115 115 VAL 116 116 THR 117 117 ARG 118 118 LEU 119 119 ALA 120 120 GLY 121 121 SER 122 122 PHE 123 123 GLU 124 124 GLY 125 125 ASP 126 126 THR 127 127 LYS 128 128 MET 129 129 ILE 130 130 PRO 131 131 LEU 132 132 ASN 133 133 TRP 134 134 ASP 135 135 ASP 136 136 PHE 137 137 THR 138 138 LYS 139 139 VAL 140 140 SER 141 141 SER 142 142 ARG 143 143 THR 144 144 VAL 145 145 GLU 146 146 ASP 147 147 THR 148 148 ASN 149 149 PRO 150 150 ALA 151 151 LEU 152 152 THR 153 153 HIS 154 154 THR 155 155 TYR 156 156 GLU 157 157 VAL 158 158 TRP 159 159 GLN 160 160 LYS 161 161 LYS 162 162 ALA stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-10-13 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 17125 DHFR 100.00 162 100.00 100.00 2.01e-114 BMRB 17310 DHFR 100.00 162 100.00 100.00 2.01e-114 BMRB 17311 DHFR 100.00 162 100.00 100.00 2.01e-114 BMRB 3524 "dihydrofolate reductase" 100.00 162 100.00 100.00 2.01e-114 BMRB 3525 "dihydrofolate reductase" 100.00 162 100.00 100.00 2.01e-114 PDB 1AO8 "Dihydrofolate Reductase Complexed With Methotrexate, Nmr, 21 Structures" 100.00 162 100.00 100.00 2.01e-114 PDB 1BZF "Nmr Solution Structure And Dynamics Of The Complex Of Lactobacillus Casei Dihydrofolate Reductase With The New Lipophilic Antif" 100.00 162 100.00 100.00 2.01e-114 PDB 1DIS "Dihydrofolate Reductase (E.C.1.5.1.3) Complex With Brodimoprim-4,6-Dicarboxylate" 100.00 162 100.00 100.00 2.01e-114 PDB 1DIU "Dihydrofolate Reductase (E.C.1.5.1.3) Complex With Brodimoprim-4,6-Dicarboxylate" 100.00 162 100.00 100.00 2.01e-114 PDB 1LUD "Solution Structure Of Dihydrofolate Reductase Complexed With Trimethoprim And Nadph, 24 Structures" 100.00 162 100.00 100.00 2.01e-114 PDB 2HM9 "Solution Structure Of Dihydrofolate Reductase Complexed With Trimethoprim, 33 Structures" 100.00 162 100.00 100.00 2.01e-114 PDB 2HQP "Solution Structure Of L.Casei Dihydrofolate Reductase Complexed With Nadph, 32 Structures" 100.00 162 100.00 100.00 2.01e-114 PDB 2L28 "Solution Structure Of Lactobacillus Casei Dihydrofolate Reductase Apo- Form, 25 Conformers" 100.00 162 100.00 100.00 2.01e-114 PDB 2LF1 "Solution Structure Of L. Casei Dihydrofolate Reductase Complexed With Nadph, 30 Structures" 100.00 162 100.00 100.00 2.01e-114 PDB 3DFR "Crystal Structures Of Escherichia Coli And Lactobacillus Casei Dihydrofolate Reductase Refined At 1.7 Angstroms Resolution. I. " 100.00 162 98.15 99.38 2.16e-112 DBJ BAI41869 "dihydrofolate reductase [Lactobacillus rhamnosus GG]" 100.00 163 98.15 99.38 9.34e-113 EMBL CAR87293 "Dihydrofolate reductase [Lactobacillus rhamnosus GG]" 100.00 163 98.15 99.38 9.34e-113 EMBL CAR90253 "Dihydrofolate reductase [Lactobacillus rhamnosus Lc 705]" 100.00 163 100.00 100.00 1.29e-114 EMBL CDN23977 "dihydrofolate reductase [Lactobacillus rhamnosus]" 100.00 163 100.00 100.00 1.29e-114 GB AAA25237 "dihydrofolate reductase [Lactobacillus casei]" 100.00 163 100.00 100.00 1.29e-114 GB AER64174 "dihydrofolate reductase [Lactobacillus rhamnosus ATCC 8530]" 100.00 163 100.00 100.00 1.29e-114 GB AGP71178 "Dihydrofolate reductase [Lactobacillus rhamnosus LOCK900]" 100.00 163 98.77 99.38 3.53e-113 GB AGP74091 "Dihydrofolate reductase [Lactobacillus rhamnosus LOCK908]" 100.00 163 100.00 100.00 1.29e-114 GB EDY98474 "Dihydrofolate reductase [Lactobacillus rhamnosus HN001]" 100.00 163 98.77 99.38 3.53e-113 PRF 0309272A reductase,dihydrofolate 100.00 162 98.77 99.38 1.10e-112 PRF 1107232A reductase,dihydrofolate 100.00 163 100.00 100.00 1.29e-114 REF WP_005686414 "dihydrofolate reductase [Lactobacillus rhamnosus]" 100.00 163 98.77 99.38 3.53e-113 REF WP_005689288 "dihydrofolate reductase [Lactobacillus rhamnosus]" 100.00 163 100.00 100.00 1.29e-114 REF WP_014569635 "dihydrofolate reductase [Lactobacillus rhamnosus]" 100.00 163 98.15 99.38 9.34e-113 REF WP_033573062 "dihydrofolate reductase [Lactobacillus rhamnosus]" 100.00 163 98.15 99.38 9.76e-113 REF WP_047676754 "dihydrofolate reductase [Lactobacillus rhamnosus]" 100.00 163 98.15 99.38 4.54e-113 SP P00381 "RecName: Full=Dihydrofolate reductase" 100.00 163 100.00 100.00 1.29e-114 stop_ save_ ############# # Ligands # ############# save_TMQ _Saveframe_category ligand _Mol_type non-polymer _Name_common "TMQ (TRIMETREXATE)" _BMRB_code . _PDB_code TMQ _Molecular_mass 370.426 _Mol_charge 1 _Mol_paramagnetic . _Mol_aromatic yes _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Thu Jun 9 10:35:50 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons N1 N1 N . 1 . ? C2 C2 C . 0 . ? N3 N3 N . 0 . ? C4 C4 C . 0 . ? C3A C3A C . 0 . ? C4A C4A C . 0 . ? C5 C5 C . 0 . ? C6 C6 C . 0 . ? C7 C7 C . 0 . ? C8 C8 C . 0 . ? C9 C9 C . 0 . ? N10 N10 N . 0 . ? C11 C11 C . 0 . ? C12 C12 C . 0 . ? C13 C13 C . 0 . ? C14 C14 C . 0 . ? C15 C15 C . 0 . ? C16 C16 C . 0 . ? C17 C17 C . 0 . ? O18 O18 O . 0 . ? O19 O19 O . 0 . ? O20 O20 O . 0 . ? C21 C21 C . 0 . ? C22 C22 C . 0 . ? C23 C23 C . 0 . ? N24 N24 N . 0 . ? N25 N25 N . 0 . ? HN HN H . 0 . ? H7 H7 H . 0 . ? H8 H8 H . 0 . ? H91 H91 H . 0 . ? H92 H92 H . 0 . ? HN1 HN1 H . 0 . ? H12 H12 H . 0 . ? H16 H16 H . 0 . ? H171 H171 H . 0 . ? H172 H172 H . 0 . ? H173 H173 H . 0 . ? H211 H211 H . 0 . ? H212 H212 H . 0 . ? H213 H213 H . 0 . ? H221 H221 H . 0 . ? H222 H222 H . 0 . ? H223 H223 H . 0 . ? H231 H231 H . 0 . ? H232 H232 H . 0 . ? H233 H233 H . 0 . ? HN21 HN21 H . 0 . ? HN22 HN22 H . 0 . ? HN51 HN51 H . 0 . ? HN52 HN52 H . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name DOUB N1 C2 ? ? SING N1 C3A ? ? SING N1 HN ? ? SING C2 N3 ? ? SING C2 N24 ? ? DOUB N3 C4 ? ? SING C4 C4A ? ? SING C4 N25 ? ? DOUB C3A C4A ? ? SING C3A C8 ? ? SING C4A C5 ? ? DOUB C5 C6 ? ? SING C5 C17 ? ? SING C6 C7 ? ? SING C6 C9 ? ? DOUB C7 C8 ? ? SING C7 H7 ? ? SING C8 H8 ? ? SING C9 N10 ? ? SING C9 H91 ? ? SING C9 H92 ? ? SING N10 C11 ? ? SING N10 HN1 ? ? DOUB C11 C12 ? ? SING C11 C16 ? ? SING C12 C13 ? ? SING C12 H12 ? ? DOUB C13 C14 ? ? SING C13 O18 ? ? SING C14 C15 ? ? SING C14 O19 ? ? DOUB C15 C16 ? ? SING C15 O20 ? ? SING C16 H16 ? ? SING C17 H171 ? ? SING C17 H172 ? ? SING C17 H173 ? ? SING O18 C21 ? ? SING O19 C22 ? ? SING O20 C23 ? ? SING C21 H211 ? ? SING C21 H212 ? ? SING C21 H213 ? ? SING C22 H221 ? ? SING C22 H222 ? ? SING C22 H223 ? ? SING C23 H231 ? ? SING C23 H232 ? ? SING C23 H233 ? ? SING N24 HN21 ? ? SING N24 HN22 ? ? SING N25 HN51 ? ? SING N25 HN52 ? ? 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 _Strain _Plasmid $DHFR 'Lactobacillus casei' 1582 Bacteria . Lactobacillus casei NF1 PMT702 stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Variant _Vector_type _Vector_name $DHFR 'recombinant technology' 'E. coli' Escherichia coli NF1 NF1 PLASMID PLASMID 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 _Concentration_min_value _Concentration_max_value _Isotopic_labeling $DHFR . mM 1.0 4.0 [U-15N] 'potassium phosphate' 50 mM . . . $TMQ . mM 1.0 4.0 . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $DHFR . mM 1.0 4.0 . 'potassium phosphate' 50 mM . . . $TMQ . mM 1.0 4.0 . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer VARIAN _Model UNITY _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_DQF-COSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name DQF-COSY _Sample_label . save_ save_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name NOESY _Sample_label . save_ save_ROESY_3 _Saveframe_category NMR_applied_experiment _Experiment_name ROESY _Sample_label . save_ save_HNHA_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNHA _Sample_label . save_ save_HNHB_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNHB _Sample_label . save_ save_HSQC_6 _Saveframe_category NMR_applied_experiment _Experiment_name HSQC _Sample_label . save_ save_3D-1H/15N-TOCSY-HMQC_7 _Saveframe_category NMR_applied_experiment _Experiment_name 3D-1H/15N-TOCSY-HMQC _Sample_label . save_ save_3D-1H/_15N-ROESY-HMQC_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D-1H/ 15N-ROESY-HMQC' _Sample_label . save_ save_3D-1H/15N-NOESY-HMQC_9 _Saveframe_category NMR_applied_experiment _Experiment_name 3D-1H/15N-NOESY-HMQC _Sample_label . save_ save_1D-NOE_DIFFERENCE_10 _Saveframe_category NMR_applied_experiment _Experiment_name '1D-NOE DIFFERENCE' _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name DQF-COSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name NOESY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name ROESY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNHA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNHB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name HSQC _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name 3D-1H/15N-TOCSY-HMQC _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D-1H/ 15N-ROESY-HMQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_9 _Saveframe_category NMR_applied_experiment _Experiment_name 3D-1H/15N-NOESY-HMQC _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_10 _Saveframe_category NMR_applied_experiment _Experiment_name '1D-NOE DIFFERENCE' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.5 . pH temperature 308 . K 'ionic strength' 550 . mM pressure 1 . atm stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_ref _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 . H 1 . . . . . . . . $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_chem_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 $sample_2 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chem_shift_ref _Mol_system_component_name 'DIHYDROFOLATE REDUCTASE' _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 4.19 . 1 2 . 1 THR HB H 4.45 . 1 3 . 1 THR HG2 H 1.23 . 1 4 . 2 ALA N N 132.30 . 1 5 . 2 ALA H H 8.90 . 1 6 . 2 ALA HA H 6.04 . 1 7 . 2 ALA HB H 1.54 . 1 8 . 3 PHE N N 120.30 . 1 9 . 3 PHE H H 8.84 . 1 10 . 3 PHE HA H 6.01 . 1 11 . 3 PHE HB2 H 3.27 . 1 12 . 3 PHE HB3 H 3.52 . 1 13 . 3 PHE HD1 H 6.79 . 3 14 . 3 PHE HE1 H 7.07 . 3 15 . 3 PHE HZ H 7.49 . 1 16 . 4 LEU N N 125.25 . 1 17 . 4 LEU H H 8.90 . 1 18 . 4 LEU HA H 6.21 . 1 19 . 4 LEU HB2 H 1.37 . 1 20 . 4 LEU HB3 H 2.09 . 1 21 . 4 LEU HG H 2.44 . 1 22 . 4 LEU HD1 H 1.23 . 1 23 . 4 LEU HD2 H 0.67 . 1 24 . 5 TRP N N 127.20 . 1 25 . 5 TRP H H 9.28 . 1 26 . 5 TRP HA H 5.60 . 1 27 . 5 TRP HB2 H 3.58 . 2 28 . 5 TRP HB3 H 3.55 . 2 29 . 5 TRP HE1 H 11.08 . 1 30 . 5 TRP HD1 H 6.97 . 1 31 . 5 TRP HE3 H 7.23 . 1 32 . 5 TRP HZ3 H 6.73 . 1 33 . 5 TRP HH2 H 6.64 . 1 34 . 5 TRP HZ2 H 7.38 . 1 35 . 6 ALA N N 122.20 . 1 36 . 6 ALA H H 8.59 . 1 37 . 6 ALA HA H 5.41 . 1 38 . 6 ALA HB H 1.43 . 1 39 . 7 GLN N N 114.80 . 1 40 . 7 GLN H H 9.06 . 1 41 . 7 GLN HA H 6.25 . 1 42 . 7 GLN HB2 H 2.33 . 1 43 . 7 GLN HB3 H 1.90 . 1 44 . 7 GLN HG2 H 2.09 . 2 45 . 7 GLN HG3 H 2.39 . 2 46 . 7 GLN HE21 H 6.90 . 1 47 . 7 GLN HE22 H 7.39 . 1 48 . 7 GLN NE2 N 111.00 . 1 49 . 8 ASP N N 120.20 . 1 50 . 8 ASP H H 8.40 . 1 51 . 8 ASP HA H 4.63 . 1 52 . 8 ASP HB2 H 4.16 . 1 53 . 8 ASP HB3 H 2.80 . 1 54 . 9 ARG N N 115.50 . 1 55 . 9 ARG H H 7.71 . 1 56 . 9 ARG HA H 4.14 . 1 57 . 9 ARG HB2 H 1.60 . 1 58 . 9 ARG HB3 H 1.85 . 1 59 . 9 ARG HG2 H 1.45 . 1 60 . 9 ARG HG3 H 1.45 . 1 61 . 9 ARG HD2 H 3.13 . 1 62 . 9 ARG HD3 H 3.13 . 1 63 . 9 ARG HE H 7.26 . 1 64 . 9 ARG NE N 85.70 . 1 65 . 10 ASP N N 118.80 . 1 66 . 10 ASP H H 8.42 . 1 67 . 10 ASP HA H 5.02 . 1 68 . 10 ASP HB2 H 2.70 . 1 69 . 10 ASP HB3 H 2.99 . 1 70 . 11 GLY N N 107.30 . 1 71 . 11 GLY H H 7.95 . 1 72 . 11 GLY HA2 H 3.52 . 2 73 . 11 GLY HA3 H 4.61 . 2 74 . 12 LEU N N 124.80 . 1 75 . 12 LEU H H 9.08 . 1 76 . 12 LEU HA H 4.33 . 1 77 . 12 LEU HB2 H 1.90 . 1 78 . 12 LEU HB3 H 1.72 . 1 79 . 12 LEU HG H 1.70 . 1 80 . 12 LEU HD1 H 0.93 . 1 81 . 12 LEU HD2 H 0.81 . 1 82 . 13 ILE N N 112.40 . 1 83 . 13 ILE H H 8.93 . 1 84 . 13 ILE HA H 5.21 . 1 85 . 13 ILE HB H 2.34 . 1 86 . 13 ILE HG13 H 1.12 . 2 87 . 13 ILE HG12 H 0.68 . 2 88 . 13 ILE HG2 H 1.32 . 1 89 . 13 ILE HD1 H 0.89 . 1 90 . 14 GLY N N 107.10 . 1 91 . 14 GLY H H 7.52 . 1 92 . 14 GLY HA2 H 3.81 . 2 93 . 14 GLY HA3 H 4.35 . 2 94 . 15 LYS N N 122.20 . 1 95 . 15 LYS H H 8.61 . 1 96 . 15 LYS HA H 4.38 . 1 97 . 15 LYS HB2 H 1.73 . 1 98 . 15 LYS HB3 H 1.45 . 1 99 . 15 LYS HG2 H 1.16 . 2 100 . 15 LYS HG3 H 1.03 . 2 101 . 16 ASP N N 129.20 . 1 102 . 16 ASP H H 10.09 . 1 103 . 16 ASP HA H 4.25 . 1 104 . 16 ASP HB2 H 2.45 . 1 105 . 16 ASP HB3 H 2.93 . 1 106 . 17 GLY N N 104.20 . 1 107 . 17 GLY H H 9.02 . 1 108 . 17 GLY HA2 H 3.45 . 2 109 . 17 GLY HA3 H 3.97 . 2 110 . 18 HIS N N 117.50 . 1 111 . 18 HIS H H 7.83 . 1 112 . 18 HIS HA H 5.02 . 1 113 . 18 HIS HB2 H 3.25 . 1 114 . 18 HIS HB3 H 3.25 . 1 115 . 18 HIS HE1 H 8.45 . 1 116 . 18 HIS HD2 H 7.21 . 1 117 . 19 LEU HA H 4.15 . 1 118 . 19 LEU HB2 H 0.40 . 2 119 . 19 LEU HB3 H 1.54 . 2 120 . 19 LEU HG H 1.35 . 1 121 . 19 LEU HD1 H 0.55 . 1 122 . 19 LEU HD2 H 0.38 . 1 123 . 20 PRO HA H 4.34 . 1 124 . 20 PRO HB2 H 1.83 . 1 125 . 20 PRO HB3 H 2.42 . 1 126 . 20 PRO HG2 H 1.35 . 2 127 . 20 PRO HD2 H 0.46 . 2 128 . 20 PRO HD3 H 3.14 . 2 129 . 21 TRP N N 111.60 . 1 130 . 21 TRP H H 5.84 . 1 131 . 21 TRP HA H 4.67 . 1 132 . 21 TRP HB2 H 2.48 . 1 133 . 21 TRP HB3 H 2.28 . 1 134 . 21 TRP HE1 H 10.01 . 1 135 . 21 TRP HD1 H 6.49 . 1 136 . 21 TRP HE3 H 6.09 . 1 137 . 21 TRP HZ3 H 6.57 . 1 138 . 21 TRP HH2 H 7.38 . 1 139 . 21 TRP HZ2 H 6.92 . 1 140 . 22 HIS N N 119.70 . 1 141 . 22 HIS H H 8.65 . 1 142 . 22 HIS HA H 4.93 . 1 143 . 22 HIS HB2 H 2.89 . 1 144 . 22 HIS HB3 H 3.21 . 1 145 . 22 HIS HE1 H 8.11 . 1 146 . 22 HIS HD2 H 7.18 . 1 147 . 23 LEU N N 126.40 . 1 148 . 23 LEU H H 8.59 . 1 149 . 23 LEU HA H 4.92 . 1 150 . 23 LEU HB2 H 1.20 . 1 151 . 23 LEU HB3 H 1.99 . 1 152 . 23 LEU HG H 1.13 . 1 153 . 23 LEU HD1 H 0.66 . 1 154 . 23 LEU HD2 H 0.16 . 1 155 . 24 PRO HA H 3.95 . 1 156 . 24 PRO HB2 H 2.05 . 2 157 . 24 PRO HB3 H 2.42 . 2 158 . 24 PRO HG2 H 1.85 . 2 159 . 24 PRO HD2 H 3.07 . 2 160 . 24 PRO HD3 H 3.87 . 2 161 . 25 ASP N N 114.40 . 1 162 . 25 ASP H H 8.85 . 1 163 . 25 ASP HA H 4.53 . 1 164 . 25 ASP HB2 H 3.10 . 1 165 . 25 ASP HB3 H 2.40 . 1 166 . 26 ASP N N 118.00 . 1 167 . 26 ASP H H 6.99 . 1 168 . 26 ASP HA H 5.40 . 1 169 . 26 ASP HB2 H 2.43 . 1 170 . 26 ASP HB3 H 2.63 . 1 171 . 27 LEU N N 121.00 . 1 172 . 27 LEU H H 7.68 . 1 173 . 27 LEU HA H 4.05 . 1 174 . 27 LEU HB2 H 2.04 . 1 175 . 27 LEU HB3 H 1.33 . 1 176 . 27 LEU HG H 1.66 . 1 177 . 27 LEU HD1 H 0.74 . 1 178 . 27 LEU HD2 H 0.49 . 1 179 . 28 HIS N N 119.20 . 1 180 . 28 HIS H H 8.04 . 1 181 . 28 HIS HA H 4.45 . 1 182 . 28 HIS HB2 H 3.35 . 1 183 . 28 HIS HB3 H 3.35 . 1 184 . 28 HIS HE1 H 7.86 . 1 185 . 28 HIS HD2 H 7.03 . 1 186 . 29 TYR N N 124.35 . 1 187 . 29 TYR H H 8.17 . 1 188 . 29 TYR HA H 4.18 . 1 189 . 29 TYR HB2 H 3.17 . 1 190 . 29 TYR HB3 H 3.41 . 1 191 . 29 TYR HD1 H 6.83 . 3 192 . 29 TYR HE1 H 6.72 . 3 193 . 30 PHE N N 119.60 . 1 194 . 30 PHE H H 9.25 . 1 195 . 30 PHE HA H 3.63 . 1 196 . 30 PHE HB2 H 2.78 . 1 197 . 30 PHE HB3 H 3.07 . 1 198 . 30 PHE HD1 H 6.52 . 3 199 . 30 PHE HE1 H 6.95 . 3 200 . 30 PHE HZ H 7.25 . 1 201 . 31 ARG N N 119.60 . 1 202 . 31 ARG H H 7.72 . 1 203 . 31 ARG HA H 3.34 . 1 204 . 31 ARG HB2 H 2.03 . 1 205 . 31 ARG HB3 H 2.07 . 1 206 . 31 ARG HD2 H 2.85 . 1 207 . 31 ARG HD3 H 2.85 . 1 208 . 32 ALA N N 121.50 . 1 209 . 32 ALA H H 7.95 . 1 210 . 32 ALA HA H 3.97 . 1 211 . 32 ALA HB H 1.33 . 1 212 . 33 GLN N N 112.40 . 1 213 . 33 GLN H H 8.00 . 1 214 . 33 GLN HA H 4.05 . 1 215 . 33 GLN HB2 H 1.32 . 1 216 . 33 GLN HB3 H 1.95 . 1 217 . 33 GLN HG2 H 1.51 . 2 218 . 33 GLN HG3 H 1.54 . 2 219 . 33 GLN HE21 H 6.59 . 1 220 . 33 GLN HE22 H 5.96 . 1 221 . 33 GLN NE2 N 111.20 . 1 222 . 34 THR N N 103.80 . 1 223 . 34 THR H H 7.08 . 1 224 . 34 THR HA H 4.16 . 1 225 . 34 THR HB H 3.83 . 1 226 . 34 THR HG2 H 0.41 . 1 227 . 34 THR HG1 H 3.58 . 1 228 . 35 VAL N N 121.80 . 1 229 . 35 VAL H H 7.46 . 1 230 . 35 VAL HA H 3.62 . 1 231 . 35 VAL HB H 2.02 . 1 232 . 35 VAL HG2 H 0.96 . 2 233 . 35 VAL HG1 H 1.02 . 2 234 . 36 GLY N N 112.70 . 1 235 . 36 GLY H H 9.23 . 1 236 . 36 GLY HA2 H 4.20 . 2 237 . 36 GLY HA3 H 3.91 . 2 238 . 37 LYS N N 119.80 . 1 239 . 37 LYS H H 7.68 . 1 240 . 37 LYS HA H 4.73 . 1 241 . 37 LYS HB2 H 2.05 . 1 242 . 37 LYS HB3 H 1.65 . 1 243 . 37 LYS HG2 H 1.27 . 2 244 . 38 ILE N N 119.30 . 1 245 . 38 ILE H H 8.43 . 1 246 . 38 ILE HA H 4.15 . 1 247 . 38 ILE HB H 1.84 . 1 248 . 38 ILE HG13 H 1.75 . 2 249 . 38 ILE HG12 H 0.75 . 2 250 . 38 ILE HG2 H 0.69 . 1 251 . 38 ILE HD1 H 1.04 . 1 252 . 39 MET N N 129.25 . 1 253 . 39 MET H H 8.82 . 1 254 . 39 MET HA H 5.18 . 1 255 . 39 MET HB2 H 2.19 . 1 256 . 39 MET HB3 H 2.46 . 1 257 . 39 MET HE H 2.16 . 1 258 . 40 VAL N N 128.60 . 1 259 . 40 VAL H H 9.16 . 1 260 . 40 VAL HA H 5.09 . 1 261 . 40 VAL HB H 1.83 . 1 262 . 40 VAL HG2 H 0.70 . 1 263 . 40 VAL HG1 H 0.57 . 1 264 . 41 VAL N N 119.70 . 1 265 . 41 VAL H H 9.11 . 1 266 . 41 VAL HA H 5.53 . 1 267 . 41 VAL HB H 2.35 . 1 268 . 41 VAL HG2 H 1.20 . 1 269 . 41 VAL HG1 H 1.00 . 1 270 . 42 GLY N N 106.00 . 1 271 . 42 GLY H H 8.28 . 1 272 . 42 GLY HA2 H 4.70 . 2 273 . 42 GLY HA3 H 4.23 . 2 274 . 43 ARG N N 119.20 . 1 275 . 43 ARG H H 8.63 . 1 276 . 43 ARG HA H 3.59 . 1 277 . 43 ARG HB2 H 1.55 . 1 278 . 43 ARG HB3 H 1.27 . 1 279 . 43 ARG HG2 H 1.05 . 2 280 . 43 ARG HD2 H 2.87 . 2 281 . 43 ARG HD3 H 2.52 . 2 282 . 43 ARG HE H 8.02 . 1 283 . 43 ARG NE N 85.30 . 1 284 . 44 ARG N N 117.10 . 1 285 . 44 ARG H H 8.30 . 1 286 . 44 ARG HA H 3.88 . 1 287 . 44 ARG HB2 H 1.82 . 1 288 . 44 ARG HB3 H 1.92 . 1 289 . 44 ARG HG2 H 1.70 . 2 290 . 44 ARG HG3 H 1.58 . 2 291 . 44 ARG HD2 H 3.16 . 2 292 . 45 THR N N 118.70 . 1 293 . 45 THR H H 7.91 . 1 294 . 45 THR HA H 3.69 . 1 295 . 45 THR HB H 4.02 . 1 296 . 45 THR HG2 H 1.00 . 1 297 . 46 TYR N N 123.70 . 1 298 . 46 TYR H H 8.49 . 1 299 . 46 TYR HA H 3.46 . 1 300 . 46 TYR HB2 H 2.96 . 2 301 . 46 TYR HB3 H 2.95 . 2 302 . 46 TYR HD1 H 7.03 . 3 303 . 47 GLU N N 112.10 . 1 304 . 47 GLU H H 8.06 . 1 305 . 47 GLU HA H 3.58 . 1 306 . 47 GLU HB2 H 2.08 . 1 307 . 47 GLU HB3 H 1.85 . 1 308 . 47 GLU HG2 H 2.82 . 2 309 . 47 GLU HG3 H 2.33 . 2 310 . 48 SER N N 115.00 . 1 311 . 48 SER H H 7.43 . 1 312 . 48 SER HA H 4.23 . 1 313 . 48 SER HB2 H 4.01 . 1 314 . 48 SER HB3 H 3.85 . 1 315 . 49 PHE N N 123.10 . 1 316 . 49 PHE H H 7.07 . 1 317 . 49 PHE HA H 4.37 . 1 318 . 49 PHE HB2 H 2.98 . 2 319 . 49 PHE HB3 H 2.89 . 2 320 . 49 PHE HD1 H 6.90 . 3 321 . 49 PHE HE1 H 7.22 . 3 322 . 49 PHE HZ H 7.22 . 1 323 . 50 PRO HB2 H 1.95 . 2 324 . 50 PRO HB3 H 2.35 . 2 325 . 50 PRO HG2 H 1.94 . 2 326 . 50 PRO HD2 H 3.85 . 2 327 . 50 PRO HD3 H 4.23 . 2 328 . 51 LYS N N 116.10 . 1 329 . 51 LYS H H 7.18 . 1 330 . 51 LYS HA H 4.40 . 1 331 . 51 LYS HB2 H 1.57 . 1 332 . 51 LYS HB3 H 1.67 . 1 333 . 51 LYS HG2 H 1.39 . 1 334 . 51 LYS HG3 H 1.39 . 1 335 . 52 ARG N N 120.50 . 1 336 . 52 ARG H H 8.20 . 1 337 . 52 ARG HA H 4.40 . 1 338 . 52 ARG HB2 H 1.30 . 1 339 . 52 ARG HB3 H 1.30 . 1 340 . 52 ARG HG2 H 1.05 . 2 341 . 52 ARG HG3 H 1.15 . 2 342 . 52 ARG HD2 H 2.50 . 1 343 . 52 ARG HD3 H 2.50 . 1 344 . 52 ARG HE H 6.70 . 1 345 . 52 ARG NE N 83.10 . 1 346 . 53 PRO HA H 4.60 . 1 347 . 53 PRO HB2 H 2.02 . 2 348 . 53 PRO HB3 H 2.40 . 2 349 . 54 LEU N N 121.90 . 1 350 . 54 LEU H H 9.45 . 1 351 . 54 LEU HA H 4.48 . 1 352 . 54 LEU HB2 H 1.39 . 1 353 . 54 LEU HB3 H 1.09 . 1 354 . 54 LEU HG H 1.41 . 1 355 . 54 LEU HD1 H 0.25 . 1 356 . 54 LEU HD2 H 0.53 . 1 357 . 55 PRO HA H 4.56 . 1 358 . 55 PRO HB2 H 2.01 . 1 359 . 55 PRO HB3 H 2.37 . 1 360 . 55 PRO HD2 H 3.58 . 2 361 . 55 PRO HD3 H 3.91 . 2 362 . 56 GLU N N 114.00 . 1 363 . 56 GLU H H 9.17 . 1 364 . 56 GLU HA H 3.90 . 1 365 . 56 GLU HB2 H 2.20 . 1 366 . 56 GLU HB3 H 2.36 . 1 367 . 57 ARG N N 112.00 . 1 368 . 57 ARG H H 7.71 . 1 369 . 57 ARG HA H 4.63 . 1 370 . 57 ARG HB2 H 2.60 . 1 371 . 57 ARG HB3 H 1.40 . 1 372 . 57 ARG HD2 H 2.55 . 2 373 . 57 ARG HD3 H 2.92 . 2 374 . 57 ARG HE H 6.01 . 1 375 . 57 ARG NE N 82.30 . 1 376 . 58 THR N N 118.80 . 1 377 . 58 THR H H 8.47 . 1 378 . 58 THR HA H 4.40 . 1 379 . 58 THR HB H 4.11 . 1 380 . 58 THR HG2 H 1.12 . 1 381 . 59 ASN N N 127.20 . 1 382 . 59 ASN H H 9.65 . 1 383 . 59 ASN HA H 5.01 . 1 384 . 59 ASN HB2 H 2.26 . 1 385 . 59 ASN HB3 H 3.13 . 1 386 . 59 ASN HD21 H 6.85 . 1 387 . 59 ASN HD22 H 8.00 . 1 388 . 59 ASN ND2 N 111.70 . 1 389 . 60 VAL N N 125.90 . 1 390 . 60 VAL H H 9.22 . 1 391 . 60 VAL HA H 4.83 . 1 392 . 60 VAL HB H 1.87 . 1 393 . 60 VAL HG2 H 0.60 . 1 394 . 60 VAL HG1 H 0.36 . 1 395 . 61 VAL N N 126.70 . 1 396 . 61 VAL H H 8.70 . 1 397 . 61 VAL HA H 4.70 . 1 398 . 61 VAL HB H 1.58 . 1 399 . 61 VAL HG2 H 0.40 . 1 400 . 61 VAL HG1 H -0.12 . 1 401 . 62 LEU N N 128.60 . 1 402 . 62 LEU H H 8.12 . 1 403 . 62 LEU HA H 4.77 . 1 404 . 62 LEU HB2 H 0.73 . 1 405 . 62 LEU HB3 H 1.55 . 1 406 . 62 LEU HG H 1.20 . 1 407 . 62 LEU HD1 H 0.44 . 1 408 . 62 LEU HD2 H 0.67 . 1 409 . 63 THR N N 119.70 . 1 410 . 63 THR H H 8.51 . 1 411 . 63 THR HA H 4.77 . 1 412 . 63 THR HB H 3.74 . 1 413 . 63 THR HG2 H 0.93 . 1 414 . 64 HIS H H 8.04 . 1 415 . 64 HIS HA H 4.77 . 1 416 . 64 HIS HB2 H 3.40 . 2 417 . 64 HIS HB3 H 3.28 . 2 418 . 64 HIS HE1 H 8.37 . 1 419 . 64 HIS HD2 H 7.30 . 1 420 . 65 GLN N N 122.10 . 1 421 . 65 GLN H H 8.35 . 1 422 . 65 GLN HA H 4.15 . 1 423 . 65 GLN HB2 H 2.00 . 2 424 . 65 GLN HB3 H 2.10 . 2 425 . 65 GLN HG2 H 2.35 . 1 426 . 65 GLN HG3 H 2.35 . 1 427 . 65 GLN HE21 H 6.82 . 1 428 . 65 GLN HE22 H 7.47 . 1 429 . 65 GLN NE2 N 110.80 . 1 430 . 66 GLU N N 127.80 . 1 431 . 66 GLU H H 8.73 . 1 432 . 66 GLU HA H 3.32 . 1 433 . 66 GLU HB2 H 1.87 . 2 434 . 66 GLU HB3 H 1.85 . 2 435 . 66 GLU HG2 H 2.20 . 2 436 . 67 ASP N N 116.00 . 1 437 . 67 ASP H H 8.40 . 1 438 . 67 ASP HA H 4.64 . 1 439 . 67 ASP HB2 H 2.65 . 1 440 . 67 ASP HB3 H 2.83 . 1 441 . 68 TYR N N 121.20 . 1 442 . 68 TYR H H 7.23 . 1 443 . 68 TYR HA H 4.17 . 1 444 . 68 TYR HB2 H 2.93 . 1 445 . 68 TYR HB3 H 2.63 . 1 446 . 68 TYR HD1 H 6.91 . 3 447 . 68 TYR HE1 H 6.66 . 3 448 . 69 GLN N N 126.20 . 1 449 . 69 GLN H H 7.59 . 1 450 . 69 GLN HA H 4.31 . 1 451 . 69 GLN HB2 H 1.75 . 1 452 . 69 GLN HB3 H 1.88 . 1 453 . 69 GLN HG2 H 2.27 . 1 454 . 69 GLN HG3 H 2.27 . 1 455 . 69 GLN HE21 H 6.76 . 1 456 . 69 GLN HE22 H 7.38 . 1 457 . 69 GLN NE2 N 112.20 . 1 458 . 70 ALA N N 126.50 . 1 459 . 70 ALA H H 8.31 . 1 460 . 70 ALA HA H 4.38 . 1 461 . 70 ALA HB H 1.09 . 1 462 . 71 GLN N N 123.50 . 1 463 . 71 GLN H H 8.54 . 1 464 . 71 GLN HA H 4.14 . 1 465 . 71 GLN HB2 H 2.06 . 1 466 . 71 GLN HB3 H 2.06 . 1 467 . 71 GLN HG2 H 2.35 . 1 468 . 71 GLN HG3 H 2.35 . 1 469 . 71 GLN HE21 H 6.77 . 1 470 . 71 GLN HE22 H 7.84 . 1 471 . 71 GLN NE2 N 111.70 . 1 472 . 72 GLY N N 113.10 . 1 473 . 72 GLY H H 8.93 . 1 474 . 72 GLY HA2 H 4.26 . 2 475 . 72 GLY HA3 H 3.74 . 2 476 . 73 ALA N N 122.90 . 1 477 . 73 ALA H H 7.94 . 1 478 . 73 ALA HA H 4.82 . 1 479 . 73 ALA HB H 1.14 . 1 480 . 74 VAL N N 123.10 . 1 481 . 74 VAL H H 8.74 . 1 482 . 74 VAL HA H 3.98 . 1 483 . 74 VAL HB H 1.71 . 1 484 . 74 VAL HG2 H 0.51 . 1 485 . 74 VAL HG1 H 0.61 . 1 486 . 75 VAL N N 127.70 . 1 487 . 75 VAL H H 8.42 . 1 488 . 75 VAL HA H 4.65 . 1 489 . 75 VAL HB H 1.99 . 1 490 . 75 VAL HG2 H 0.80 . 1 491 . 75 VAL HG1 H 0.86 . 1 492 . 76 VAL N N 120.00 . 1 493 . 76 VAL H H 8.76 . 1 494 . 76 VAL HA H 4.43 . 1 495 . 76 VAL HB H 2.19 . 1 496 . 76 VAL HG2 H 0.67 . 1 497 . 76 VAL HG1 H 0.52 . 1 498 . 77 HIS N N 113.80 . 1 499 . 77 HIS H H 8.79 . 1 500 . 77 HIS HA H 5.48 . 1 501 . 77 HIS HB2 H 3.07 . 1 502 . 77 HIS HB3 H 3.52 . 1 503 . 77 HIS HE1 H 8.36 . 1 504 . 77 HIS HD2 H 7.35 . 1 505 . 78 ASP N N 114.70 . 1 506 . 78 ASP H H 7.34 . 1 507 . 78 ASP HA H 4.64 . 1 508 . 78 ASP HB2 H 2.94 . 1 509 . 78 ASP HB3 H 2.94 . 1 510 . 79 VAL N N 119.20 . 1 511 . 79 VAL H H 8.32 . 1 512 . 79 VAL HA H 3.42 . 1 513 . 79 VAL HB H 1.82 . 1 514 . 79 VAL HG2 H 0.66 . 2 515 . 79 VAL HG1 H 0.59 . 2 516 . 80 ALA N N 123.20 . 1 517 . 80 ALA H H 8.38 . 1 518 . 80 ALA HA H 4.33 . 1 519 . 80 ALA HB H 1.54 . 1 520 . 81 ALA N N 120.30 . 1 521 . 81 ALA H H 8.23 . 1 522 . 81 ALA HA H 4.34 . 1 523 . 81 ALA HB H 1.67 . 1 524 . 82 VAL N N 119.40 . 1 525 . 82 VAL H H 7.70 . 1 526 . 82 VAL HA H 3.54 . 1 527 . 82 VAL HB H 2.49 . 1 528 . 82 VAL HG2 H 0.80 . 1 529 . 82 VAL HG1 H 1.11 . 1 530 . 83 PHE N N 117.80 . 1 531 . 83 PHE H H 7.90 . 1 532 . 83 PHE HA H 4.55 . 1 533 . 83 PHE HB2 H 3.03 . 1 534 . 83 PHE HB3 H 3.36 . 1 535 . 83 PHE HD1 H 7.39 . 3 536 . 83 PHE HE1 H 7.39 . 3 537 . 84 ALA N N 122.50 . 1 538 . 84 ALA H H 8.66 . 1 539 . 84 ALA HA H 4.25 . 1 540 . 84 ALA HB H 1.60 . 1 541 . 85 TYR N N 120.00 . 1 542 . 85 TYR H H 7.83 . 1 543 . 85 TYR HA H 4.13 . 1 544 . 85 TYR HB2 H 3.19 . 1 545 . 85 TYR HB3 H 3.27 . 1 546 . 85 TYR HD1 H 7.00 . 3 547 . 85 TYR HE1 H 6.56 . 3 548 . 86 ALA N N 122.70 . 1 549 . 86 ALA H H 8.87 . 1 550 . 86 ALA HA H 3.99 . 1 551 . 86 ALA HB H 1.75 . 1 552 . 87 LYS N N 117.80 . 1 553 . 87 LYS H H 8.23 . 1 554 . 87 LYS HA H 4.08 . 1 555 . 87 LYS HB2 H 2.00 . 1 556 . 87 LYS HB3 H 2.00 . 1 557 . 87 LYS HG2 H 1.73 . 2 558 . 87 LYS HG3 H 1.61 . 2 559 . 88 GLN N N 114.50 . 1 560 . 88 GLN H H 7.27 . 1 561 . 88 GLN HA H 4.11 . 1 562 . 88 GLN HB2 H 1.86 . 1 563 . 88 GLN HB3 H 1.86 . 1 564 . 88 GLN HG2 H 2.30 . 2 565 . 88 GLN HG3 H 2.44 . 2 566 . 88 GLN HE21 H 6.82 . 1 567 . 88 GLN HE22 H 7.31 . 1 568 . 88 GLN NE2 N 111.00 . 1 569 . 89 HIS N N 117.50 . 1 570 . 89 HIS H H 7.54 . 1 571 . 89 HIS HA H 4.82 . 1 572 . 89 HIS HB2 H 2.72 . 1 573 . 89 HIS HB3 H 3.47 . 1 574 . 89 HIS HE1 H 8.28 . 1 575 . 89 HIS HD2 H 6.59 . 1 576 . 90 PRO HD2 H 3.50 . 2 577 . 90 PRO HD3 H 3.31 . 2 578 . 91 ASP N N 116.60 . 1 579 . 91 ASP H H 8.86 . 1 580 . 91 ASP HA H 4.55 . 1 581 . 91 ASP HB2 H 2.75 . 1 582 . 91 ASP HB3 H 2.75 . 1 583 . 92 GLN N N 119.20 . 1 584 . 92 GLN H H 7.83 . 1 585 . 92 GLN HA H 4.86 . 1 586 . 92 GLN HB2 H 2.24 . 1 587 . 92 GLN HB3 H 2.00 . 1 588 . 92 GLN HG2 H 2.37 . 2 589 . 92 GLN HG3 H 2.24 . 2 590 . 92 GLN HE21 H 6.25 . 1 591 . 92 GLN HE22 H 6.93 . 1 592 . 92 GLN NE2 N 107.90 . 1 593 . 93 GLU N N 122.20 . 1 594 . 93 GLU H H 8.33 . 1 595 . 93 GLU HA H 4.39 . 1 596 . 93 GLU HB2 H 1.85 . 2 597 . 93 GLU HB3 H 2.03 . 2 598 . 94 LEU N N 123.30 . 1 599 . 94 LEU H H 8.51 . 1 600 . 94 LEU HA H 4.97 . 1 601 . 94 LEU HB2 H 1.70 . 2 602 . 94 LEU HB3 H 1.64 . 2 603 . 94 LEU HG H 1.49 . 1 604 . 94 LEU HD1 H 0.78 . 1 605 . 94 LEU HD2 H 0.78 . 1 606 . 95 VAL N N 126.70 . 1 607 . 95 VAL H H 9.47 . 1 608 . 95 VAL HA H 4.86 . 1 609 . 95 VAL HB H 1.90 . 1 610 . 95 VAL HG2 H 0.94 . 2 611 . 95 VAL HG1 H 0.89 . 2 612 . 96 ILE N N 128.00 . 1 613 . 96 ILE H H 9.77 . 1 614 . 96 ILE HA H 4.53 . 1 615 . 96 ILE HB H 2.58 . 1 616 . 96 ILE HG13 H 1.42 . 2 617 . 96 ILE HG12 H 0.90 . 2 618 . 96 ILE HG2 H 0.53 . 1 619 . 96 ILE HD1 H -0.07 . 1 620 . 97 ALA N N 128.40 . 1 621 . 97 ALA H H 9.15 . 1 622 . 97 ALA HA H 6.01 . 1 623 . 97 ALA HB H 1.77 . 1 624 . 98 GLY N N 102.70 . 1 625 . 98 GLY H H 5.97 . 1 626 . 98 GLY HA2 H 2.23 . 2 627 . 98 GLY HA3 H 4.18 . 2 628 . 99 GLY N N 108.20 . 1 629 . 99 GLY H H 7.81 . 1 630 . 99 GLY HA2 H 3.74 . 2 631 . 99 GLY HA3 H 4.05 . 2 632 . 100 ALA N N 124.10 . 1 633 . 100 ALA H H 9.04 . 1 634 . 100 ALA HA H 4.01 . 1 635 . 100 ALA HB H 1.50 . 1 636 . 101 GLN N N 115.20 . 1 637 . 101 GLN H H 8.89 . 1 638 . 101 GLN HA H 4.18 . 1 639 . 101 GLN HB2 H 2.10 . 1 640 . 101 GLN HB3 H 1.47 . 1 641 . 101 GLN HG2 H 2.55 . 2 642 . 101 GLN HG3 H 2.38 . 2 643 . 101 GLN HE21 H 7.08 . 1 644 . 101 GLN HE22 H 7.57 . 1 645 . 101 GLN NE2 N 112.70 . 1 646 . 102 ILE N N 121.50 . 1 647 . 102 ILE H H 7.22 . 1 648 . 102 ILE HA H 3.83 . 1 649 . 102 ILE HB H 1.79 . 1 650 . 102 ILE HG13 H 1.46 . 2 651 . 102 ILE HG12 H 1.17 . 2 652 . 102 ILE HG2 H 0.69 . 1 653 . 102 ILE HD1 H 0.65 . 1 654 . 103 PHE N N 117.90 . 1 655 . 103 PHE H H 7.74 . 1 656 . 103 PHE HA H 4.02 . 1 657 . 103 PHE HB2 H 2.74 . 1 658 . 103 PHE HB3 H 2.52 . 1 659 . 103 PHE HD1 H 5.83 . 3 660 . 103 PHE HE1 H 7.03 . 3 661 . 103 PHE HZ H 7.44 . 1 662 . 104 THR N N 114.30 . 1 663 . 104 THR H H 8.32 . 1 664 . 104 THR HA H 3.73 . 1 665 . 104 THR HB H 4.25 . 1 666 . 104 THR HG2 H 1.26 . 1 667 . 105 ALA N N 122.30 . 1 668 . 105 ALA H H 7.26 . 1 669 . 105 ALA HA H 4.09 . 1 670 . 105 ALA HB H 1.33 . 1 671 . 106 PHE N N 112.40 . 1 672 . 106 PHE H H 7.45 . 1 673 . 106 PHE HA H 4.98 . 1 674 . 106 PHE HB2 H 2.97 . 1 675 . 106 PHE HB3 H 3.91 . 1 676 . 106 PHE HD1 H 7.64 . 3 677 . 106 PHE HE1 H 6.81 . 3 678 . 106 PHE HZ H 6.89 . 1 679 . 107 LYS N N 120.60 . 1 680 . 107 LYS H H 7.58 . 1 681 . 107 LYS HA H 4.08 . 1 682 . 107 LYS HB2 H 2.03 . 1 683 . 107 LYS HB3 H 2.03 . 1 684 . 107 LYS HG2 H 1.66 . 2 685 . 107 LYS HG3 H 1.77 . 2 686 . 107 LYS HD2 H 1.40 . 1 687 . 108 ASP N N 118.10 . 1 688 . 108 ASP H H 8.64 . 1 689 . 108 ASP HA H 4.81 . 1 690 . 108 ASP HB2 H 2.56 . 1 691 . 108 ASP HB3 H 2.83 . 1 692 . 109 ASP N N 118.20 . 1 693 . 109 ASP H H 7.99 . 1 694 . 109 ASP HA H 4.94 . 1 695 . 109 ASP HB2 H 2.67 . 1 696 . 109 ASP HB3 H 3.12 . 1 697 . 110 VAL N N 117.20 . 1 698 . 110 VAL H H 7.03 . 1 699 . 110 VAL HA H 3.87 . 1 700 . 110 VAL HB H 1.28 . 1 701 . 110 VAL HG2 H 0.44 . 1 702 . 110 VAL HG1 H 0.38 . 1 703 . 111 ASP N N 121.60 . 1 704 . 111 ASP H H 8.50 . 1 705 . 111 ASP HA H 5.01 . 1 706 . 111 ASP HB2 H 2.75 . 2 707 . 111 ASP HB3 H 3.01 . 2 708 . 112 THR N N 117.40 . 1 709 . 112 THR H H 7.74 . 1 710 . 112 THR HA H 5.59 . 1 711 . 112 THR HB H 3.93 . 1 712 . 112 THR HG2 H 1.42 . 1 713 . 113 LEU N N 125.30 . 1 714 . 113 LEU H H 9.61 . 1 715 . 113 LEU HA H 5.02 . 1 716 . 113 LEU HB2 H 1.92 . 1 717 . 113 LEU HB3 H 1.43 . 1 718 . 113 LEU HG H 0.92 . 1 719 . 113 LEU HD1 H -0.96 . 1 720 . 113 LEU HD2 H 0.30 . 1 721 . 114 LEU N N 126.00 . 1 722 . 114 LEU H H 9.40 . 1 723 . 114 LEU HA H 5.38 . 1 724 . 114 LEU HB2 H 2.60 . 1 725 . 114 LEU HB3 H 1.69 . 1 726 . 114 LEU HG H 1.81 . 1 727 . 114 LEU HD1 H 1.00 . 1 728 . 114 LEU HD2 H 1.08 . 1 729 . 115 VAL N N 121.50 . 1 730 . 115 VAL H H 7.93 . 1 731 . 115 VAL HA H 4.33 . 1 732 . 115 VAL HB H 0.58 . 1 733 . 115 VAL HG2 H 0.63 . 1 734 . 115 VAL HG1 H -0.02 . 1 735 . 116 THR N N 125.50 . 1 736 . 116 THR H H 8.50 . 1 737 . 116 THR HA H 4.83 . 1 738 . 116 THR HB H 4.08 . 1 739 . 116 THR HG2 H 0.55 . 1 740 . 116 THR HG1 H 5.27 . 1 741 . 117 ARG N N 127.30 . 1 742 . 117 ARG H H 9.16 . 1 743 . 117 ARG HA H 4.72 . 1 744 . 117 ARG HB2 H 1.37 . 1 745 . 117 ARG HB3 H 1.75 . 1 746 . 117 ARG HG2 H 1.27 . 2 747 . 117 ARG HG3 H 1.17 . 2 748 . 117 ARG HD2 H 2.90 . 2 749 . 117 ARG HD3 H 3.24 . 2 750 . 117 ARG HE H 8.31 . 1 751 . 117 ARG NE N 84.80 . 1 752 . 118 LEU N N 130.20 . 1 753 . 118 LEU H H 9.10 . 1 754 . 118 LEU HA H 4.54 . 1 755 . 118 LEU HB2 H 1.07 . 1 756 . 118 LEU HB3 H 1.88 . 1 757 . 118 LEU HG H 0.95 . 1 758 . 118 LEU HD1 H -0.24 . 1 759 . 118 LEU HD2 H -0.57 . 1 760 . 119 ALA N N 120.30 . 1 761 . 119 ALA H H 8.36 . 1 762 . 119 ALA HA H 4.05 . 1 763 . 119 ALA HB H 1.37 . 1 764 . 120 GLY N N 103.40 . 1 765 . 120 GLY H H 8.09 . 1 766 . 120 GLY HA2 H 4.21 . 2 767 . 120 GLY HA3 H 3.55 . 2 768 . 121 SER N N 111.70 . 1 769 . 121 SER H H 7.64 . 1 770 . 121 SER HA H 5.05 . 1 771 . 121 SER HB2 H 3.61 . 2 772 . 121 SER HB3 H 3.50 . 2 773 . 122 PHE N N 126.40 . 1 774 . 122 PHE H H 9.69 . 1 775 . 122 PHE HA H 4.76 . 1 776 . 122 PHE HB2 H 2.91 . 1 777 . 122 PHE HB3 H 3.38 . 1 778 . 122 PHE HD1 H 7.52 . 3 779 . 122 PHE HE1 H 7.17 . 3 780 . 122 PHE HZ H 6.99 . 1 781 . 123 GLU N N 119.30 . 1 782 . 123 GLU H H 8.31 . 1 783 . 123 GLU HA H 4.62 . 1 784 . 123 GLU HB2 H 2.02 . 1 785 . 123 GLU HB3 H 2.02 . 1 786 . 123 GLU HG2 H 2.34 . 2 787 . 123 GLU HG3 H 2.23 . 2 788 . 124 GLY N N 108.00 . 1 789 . 124 GLY H H 8.20 . 1 790 . 124 GLY HA2 H 4.16 . 2 791 . 124 GLY HA3 H 4.05 . 2 792 . 125 ASP N N 115.70 . 1 793 . 125 ASP H H 8.49 . 1 794 . 125 ASP HA H 4.96 . 1 795 . 125 ASP HB2 H 3.01 . 1 796 . 125 ASP HB3 H 2.64 . 1 797 . 126 THR N N 116.90 . 1 798 . 126 THR H H 7.71 . 1 799 . 126 THR HA H 4.63 . 1 800 . 126 THR HB H 3.76 . 1 801 . 126 THR HG2 H 1.23 . 1 802 . 127 LYS N N 127.90 . 1 803 . 127 LYS H H 8.76 . 1 804 . 127 LYS HA H 5.07 . 1 805 . 127 LYS HB2 H 1.69 . 1 806 . 127 LYS HB3 H 1.89 . 1 807 . 127 LYS HG2 H 1.50 . 2 808 . 128 MET N N 119.30 . 1 809 . 128 MET H H 8.90 . 1 810 . 128 MET HA H 4.07 . 1 811 . 128 MET HB2 H 1.84 . 1 812 . 128 MET HB3 H 2.02 . 1 813 . 128 MET HE H -0.34 . 1 814 . 129 ILE N N 117.40 . 1 815 . 129 ILE H H 7.47 . 1 816 . 129 ILE HA H 4.34 . 1 817 . 129 ILE HB H 1.97 . 1 818 . 129 ILE HG13 H 1.31 . 2 819 . 129 ILE HG12 H 0.64 . 2 820 . 129 ILE HG2 H 1.12 . 1 821 . 129 ILE HD1 H 0.76 . 1 822 . 130 PRO HA H 4.50 . 1 823 . 130 PRO HB2 H 1.85 . 1 824 . 130 PRO HB3 H 2.29 . 1 825 . 131 LEU N N 122.20 . 1 826 . 131 LEU H H 7.49 . 1 827 . 131 LEU HA H 4.36 . 1 828 . 131 LEU HB2 H 0.50 . 1 829 . 131 LEU HB3 H 0.21 . 1 830 . 131 LEU HG H 1.27 . 1 831 . 131 LEU HD1 H -0.01 . 1 832 . 131 LEU HD2 H 0.44 . 1 833 . 132 ASN N N 119.10 . 1 834 . 132 ASN H H 8.84 . 1 835 . 132 ASN HA H 5.01 . 1 836 . 132 ASN HB2 H 3.05 . 1 837 . 132 ASN HB3 H 2.74 . 1 838 . 132 ASN HD21 H 6.88 . 1 839 . 132 ASN HD22 H 7.64 . 1 840 . 132 ASN ND2 N 112.20 . 1 841 . 133 TRP N N 123.70 . 1 842 . 133 TRP H H 7.79 . 1 843 . 133 TRP HA H 3.78 . 1 844 . 133 TRP HB2 H 2.98 . 1 845 . 133 TRP HB3 H 3.20 . 1 846 . 133 TRP HE1 H 10.05 . 1 847 . 133 TRP HD1 H 7.41 . 1 848 . 133 TRP HE3 H 5.68 . 1 849 . 133 TRP HZ3 H 4.58 . 1 850 . 133 TRP HH2 H 6.65 . 1 851 . 133 TRP HZ2 H 7.61 . 1 852 . 134 ASP N N 115.20 . 1 853 . 134 ASP H H 8.27 . 1 854 . 134 ASP HA H 4.77 . 1 855 . 134 ASP HB2 H 2.85 . 2 856 . 134 ASP HB3 H 2.77 . 2 857 . 135 ASP N N 117.60 . 1 858 . 135 ASP H H 8.03 . 1 859 . 135 ASP HA H 4.78 . 1 860 . 135 ASP HB2 H 2.76 . 2 861 . 135 ASP HB3 H 2.54 . 2 862 . 136 PHE N N 118.60 . 1 863 . 136 PHE H H 8.34 . 1 864 . 136 PHE HA H 5.21 . 1 865 . 136 PHE HB2 H 3.38 . 1 866 . 136 PHE HB3 H 3.25 . 1 867 . 136 PHE HD1 H 7.00 . 3 868 . 136 PHE HE1 H 6.88 . 3 869 . 136 PHE HZ H 7.00 . 1 870 . 137 THR N N 115.10 . 1 871 . 137 THR H H 9.39 . 1 872 . 137 THR HA H 4.90 . 1 873 . 137 THR HB H 3.99 . 1 874 . 137 THR HG2 H 1.22 . 1 875 . 138 LYS N N 131.25 . 1 876 . 138 LYS H H 8.58 . 1 877 . 138 LYS HA H 3.61 . 1 878 . 138 LYS HB2 H -0.74 . 1 879 . 138 LYS HB3 H 1.13 . 1 880 . 138 LYS HG2 H 0.09 . 2 881 . 138 LYS HG3 H 0.58 . 2 882 . 138 LYS HD2 H 1.29 . 2 883 . 138 LYS HD3 H 1.19 . 2 884 . 138 LYS HE2 H 2.63 . 2 885 . 138 LYS HE3 H 2.52 . 2 886 . 139 VAL N N 126.00 . 1 887 . 139 VAL H H 9.11 . 1 888 . 139 VAL HA H 4.22 . 1 889 . 139 VAL HB H 2.14 . 1 890 . 139 VAL HG2 H 0.95 . 2 891 . 139 VAL HG1 H 0.91 . 2 892 . 140 SER N N 112.70 . 1 893 . 140 SER H H 7.51 . 1 894 . 140 SER HA H 4.61 . 1 895 . 140 SER HB2 H 3.70 . 2 896 . 140 SER HB3 H 3.84 . 2 897 . 141 SER N N 115.00 . 1 898 . 141 SER H H 8.08 . 1 899 . 141 SER HA H 5.29 . 1 900 . 141 SER HB2 H 3.46 . 1 901 . 141 SER HB3 H 3.63 . 1 902 . 142 ARG N N 125.50 . 1 903 . 142 ARG H H 8.50 . 1 904 . 142 ARG HA H 4.87 . 1 905 . 142 ARG HB2 H 1.89 . 2 906 . 142 ARG HB3 H 1.85 . 2 907 . 142 ARG HG2 H 1.53 . 2 908 . 142 ARG HG3 H 1.65 . 2 909 . 143 THR N N 124.30 . 1 910 . 143 THR H H 9.07 . 1 911 . 143 THR HA H 4.76 . 1 912 . 143 THR HB H 3.82 . 1 913 . 143 THR HG2 H 0.90 . 1 914 . 144 VAL N N 130.20 . 1 915 . 144 VAL H H 9.10 . 1 916 . 144 VAL HA H 4.00 . 1 917 . 144 VAL HB H 0.66 . 1 918 . 144 VAL HG2 H 0.94 . 2 919 . 144 VAL HG1 H 0.85 . 2 920 . 145 GLU N N 126.60 . 1 921 . 145 GLU H H 8.52 . 1 922 . 145 GLU HA H 4.48 . 1 923 . 145 GLU HB2 H 1.85 . 2 924 . 145 GLU HB3 H 1.82 . 2 925 . 145 GLU HG2 H 2.24 . 2 926 . 145 GLU HG3 H 2.07 . 2 927 . 146 ASP N N 126.30 . 1 928 . 146 ASP H H 8.21 . 1 929 . 146 ASP HA H 4.86 . 1 930 . 146 ASP HB2 H 2.01 . 1 931 . 146 ASP HB3 H 3.12 . 1 932 . 147 THR N N 117.80 . 1 933 . 147 THR H H 7.92 . 1 934 . 147 THR HA H 3.91 . 1 935 . 147 THR HB H 4.14 . 1 936 . 147 THR HG2 H 1.29 . 1 937 . 148 ASN N N 122.20 . 1 938 . 148 ASN H H 9.83 . 1 939 . 148 ASN HA H 5.14 . 1 940 . 148 ASN HB2 H 2.86 . 1 941 . 148 ASN HB3 H 3.36 . 1 942 . 148 ASN HD21 H 7.19 . 1 943 . 148 ASN HD22 H 7.84 . 1 944 . 148 ASN ND2 N 110.20 . 1 945 . 149 PRO HA H 4.58 . 1 946 . 149 PRO HB2 H 2.12 . 1 947 . 149 PRO HB3 H 2.27 . 1 948 . 149 PRO HG2 H 1.96 . 2 949 . 149 PRO HD2 H 3.97 . 2 950 . 149 PRO HD3 H 4.16 . 2 951 . 150 ALA N N 119.00 . 1 952 . 150 ALA H H 7.70 . 1 953 . 150 ALA HA H 3.95 . 1 954 . 150 ALA HB H 1.38 . 1 955 . 151 LEU N N 112.20 . 1 956 . 151 LEU H H 8.15 . 1 957 . 151 LEU HA H 4.35 . 1 958 . 151 LEU HB2 H 2.01 . 1 959 . 151 LEU HB3 H 1.75 . 1 960 . 151 LEU HG H 1.60 . 1 961 . 151 LEU HD1 H 1.15 . 1 962 . 151 LEU HD2 H 0.83 . 1 963 . 152 THR N N 124.80 . 1 964 . 152 THR H H 7.43 . 1 965 . 152 THR HA H 4.32 . 1 966 . 152 THR HB H 4.21 . 1 967 . 152 THR HG2 H 1.12 . 1 968 . 153 HIS N N 120.00 . 1 969 . 153 HIS H H 8.56 . 1 970 . 153 HIS HA H 5.73 . 1 971 . 153 HIS HB2 H 2.15 . 1 972 . 153 HIS HB3 H 2.73 . 1 973 . 153 HIS HE1 H 9.48 . 1 974 . 153 HIS HD2 H 5.99 . 1 975 . 154 THR N N 116.30 . 1 976 . 154 THR H H 8.60 . 1 977 . 154 THR HA H 5.05 . 1 978 . 154 THR HB H 3.73 . 1 979 . 154 THR HG2 H 1.05 . 1 980 . 155 TYR N N 125.00 . 1 981 . 155 TYR H H 9.07 . 1 982 . 155 TYR HA H 4.96 . 1 983 . 155 TYR HB2 H 2.63 . 1 984 . 155 TYR HB3 H 2.83 . 1 985 . 155 TYR HD1 H 6.53 . 3 986 . 155 TYR HE1 H 6.64 . 3 987 . 156 GLU N N 123.80 . 1 988 . 156 GLU H H 9.60 . 1 989 . 156 GLU HA H 5.33 . 1 990 . 156 GLU HB2 H 2.38 . 1 991 . 156 GLU HB3 H 2.05 . 1 992 . 156 GLU HG2 H 2.14 . 2 993 . 156 GLU HG3 H 2.27 . 2 994 . 157 VAL N N 122.80 . 1 995 . 157 VAL H H 8.07 . 1 996 . 157 VAL HA H 5.28 . 1 997 . 157 VAL HB H 2.01 . 1 998 . 157 VAL HG2 H 0.95 . 1 999 . 157 VAL HG1 H 0.95 . 1 1000 . 158 TRP N N 127.50 . 1 1001 . 158 TRP H H 9.90 . 1 1002 . 158 TRP HA H 5.90 . 1 1003 . 158 TRP HB2 H 3.14 . 1 1004 . 158 TRP HB3 H 3.45 . 1 1005 . 158 TRP HE1 H 11.19 . 1 1006 . 158 TRP HD1 H 7.09 . 1 1007 . 158 TRP HE3 H 7.49 . 1 1008 . 158 TRP HZ3 H 7.44 . 1 1009 . 158 TRP HH2 H 7.18 . 1 1010 . 158 TRP HZ2 H 7.26 . 1 1011 . 159 GLN N N 120.30 . 1 1012 . 159 GLN H H 9.53 . 1 1013 . 159 GLN HA H 5.65 . 1 1014 . 159 GLN HB2 H 2.04 . 1 1015 . 159 GLN HB3 H 2.23 . 1 1016 . 159 GLN HG2 H 2.48 . 2 1017 . 159 GLN HG3 H 2.58 . 2 1018 . 159 GLN HE21 H 6.79 . 1 1019 . 159 GLN HE22 H 7.40 . 1 1020 . 159 GLN NE2 N 110.80 . 1 1021 . 160 LYS N N 127.20 . 1 1022 . 160 LYS H H 8.84 . 1 1023 . 160 LYS HA H 3.76 . 1 1024 . 160 LYS HB2 H 1.53 . 1 1025 . 160 LYS HB3 H 1.80 . 1 1026 . 161 LYS N N 126.80 . 1 1027 . 161 LYS H H 8.55 . 1 1028 . 161 LYS HA H 4.15 . 1 1029 . 161 LYS HB2 H 1.60 . 1 1030 . 161 LYS HB3 H 1.84 . 1 1031 . 161 LYS HG2 H 1.22 . 2 1032 . 161 LYS HG3 H 1.43 . 2 1033 . 162 ALA N N 130.90 . 1 1034 . 162 ALA H H 7.90 . 1 1035 . 162 ALA HA H 4.14 . 1 1036 . 162 ALA HB H 1.33 . 1 stop_ save_ save_chem_shift_set_2 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 $sample_2 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chem_shift_ref _Mol_system_component_name TRIMETREXATE _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 TMQ H H 15.47 . 1 2 . 1 TMQ HN21 H 9.53 . 1 3 . 1 TMQ HN22 H 5.76 . 1 4 . 1 TMQ HN41 H 9.52 . 1 5 . 1 TMQ HN42 H 7.88 . 1 6 . 1 TMQ H5 H 2.65 . 1 7 . 1 TMQ H7 H 7.38 . 1 8 . 1 TMQ H8 H 7.06 . 1 9 . 1 TMQ H91 H 4.11 . 1 10 . 1 TMQ H92 H 4.48 . 1 11 . 1 TMQ HN10 H 5.99 . 1 12 . 1 TMQ H2' H 5.19 . 1 13 . 1 TMQ H3' H 3.37 . 1 14 . 1 TMQ H4' H 3.78 . 1 15 . 1 TMQ H5' H 3.96 . 1 16 . 1 TMQ H6' H 6.37 . 1 stop_ save_