data_7195 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; NMR solution structure of the antitumor compound PT523 and NADPH in the ternary complex with human dihydrofolate reductase ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Johnson J. M. . 2 Meiering E. M. . 3 Wright J. E. . 4 Pardo J. . . 5 Rosowsky A. . . 6 Wagner G. . . stop_ _BMRB_accession_number 7195 _BMRB_flat_file_name bmr7195.str _Entry_type new _Submission_date 2006-06-27 _Accession_date 2006-06-28 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 604 "15N chemical shifts" 170 stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_title ; NMR solution structure of the antitumor compound PT523 and NADPH in the ternary complex with human DHFR ; _Citation_status published _Citation_type journal _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Johnson J. M. . 2 Meiering E. M. . 3 Wright J. E. . 4 Pardo J. . . 5 Rosowsky A. . . 6 Wagner G. . . stop_ _Journal_abbreviation Biochemistry _Journal_volume 36 _Journal_issue 15 _Page_first 4399 _Page_last 4411 _Year 1997 save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name "DHFR ternary complex" _Abbreviation_common "DHFR ternary complex" loop_ _Mol_system_component_name _Mol_label "dihydrofolate reductase" $DHFR PT523 $PT523 NADPH $NADPH stop_ _System_physical_state native _System_oligomer_state complex _System_paramagnetic no _System_thiol_state "not reported" save_ ######################## # Monomeric polymers # ######################## save_DHFR _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common "dihydrofolate reductase" _Mol_thiol_state "not reported" ############################## # Polymer residue sequence # ############################## _Residue_count 186 _Mol_residue_sequence ; VGSLNCIVAVSQNMGIGKNG DLPWPPLRNEFRYFQRMTTT SSVEGKQNLVIMGKKTWFSI PEKNRPLKGRINLVLSRELK EPPQGAHFLSRSLDDALKLT EQPELANKVDMVWIVGGSSV YKEAMNHPGHLKLFVTRIMQ DFESDTFFPEIDLEKYKLLP EYPGVLSDVQEEKGIKYKFE VYEKND ; loop_ _Residue_seq_code _Residue_label 1 VAL 2 GLY 3 SER 4 LEU 5 ASN 6 CYS 7 ILE 8 VAL 9 ALA 10 VAL 11 SER 12 GLN 13 ASN 14 MET 15 GLY 16 ILE 17 GLY 18 LYS 19 ASN 20 GLY 21 ASP 22 LEU 23 PRO 24 TRP 25 PRO 26 PRO 27 LEU 28 ARG 29 ASN 30 GLU 31 PHE 32 ARG 33 TYR 34 PHE 35 GLN 36 ARG 37 MET 38 THR 39 THR 40 THR 41 SER 42 SER 43 VAL 44 GLU 45 GLY 46 LYS 47 GLN 48 ASN 49 LEU 50 VAL 51 ILE 52 MET 53 GLY 54 LYS 55 LYS 56 THR 57 TRP 58 PHE 59 SER 60 ILE 61 PRO 62 GLU 63 LYS 64 ASN 65 ARG 66 PRO 67 LEU 68 LYS 69 GLY 70 ARG 71 ILE 72 ASN 73 LEU 74 VAL 75 LEU 76 SER 77 ARG 78 GLU 79 LEU 80 LYS 81 GLU 82 PRO 83 PRO 84 GLN 85 GLY 86 ALA 87 HIS 88 PHE 89 LEU 90 SER 91 ARG 92 SER 93 LEU 94 ASP 95 ASP 96 ALA 97 LEU 98 LYS 99 LEU 100 THR 101 GLU 102 GLN 103 PRO 104 GLU 105 LEU 106 ALA 107 ASN 108 LYS 109 VAL 110 ASP 111 MET 112 VAL 113 TRP 114 ILE 115 VAL 116 GLY 117 GLY 118 SER 119 SER 120 VAL 121 TYR 122 LYS 123 GLU 124 ALA 125 MET 126 ASN 127 HIS 128 PRO 129 GLY 130 HIS 131 LEU 132 LYS 133 LEU 134 PHE 135 VAL 136 THR 137 ARG 138 ILE 139 MET 140 GLN 141 ASP 142 PHE 143 GLU 144 SER 145 ASP 146 THR 147 PHE 148 PHE 149 PRO 150 GLU 151 ILE 152 ASP 153 LEU 154 GLU 155 LYS 156 TYR 157 LYS 158 LEU 159 LEU 160 PRO 161 GLU 162 TYR 163 PRO 164 GLY 165 VAL 166 LEU 167 SER 168 ASP 169 VAL 170 GLN 171 GLU 172 GLU 173 LYS 174 GLY 175 ILE 176 LYS 177 TYR 178 LYS 179 PHE 180 GLU 181 VAL 182 TYR 183 GLU 184 LYS 185 ASN 186 ASP stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 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 17096 DHFR 100.00 187 100.00 100.00 1.19e-133 BMRB 19563 DHFR 100.00 187 100.00 100.00 1.19e-133 BMRB 19564 DHFR 100.00 187 100.00 100.00 1.19e-133 BMRB 19565 DHFR 100.00 187 100.00 100.00 1.19e-133 BMRB 19566 DHFR 100.00 187 100.00 100.00 1.19e-133 BMRB 19567 DHFR 100.00 187 100.00 100.00 1.19e-133 BMRB 5981 DHFR 100.00 186 100.00 100.00 1.10e-133 PDB 1BOZ "Structure-Based Design And Synthesis Of Lipophilic 2,4- Diamino-6-Substituted Quinazolines And Their Evaluation As Inhibitors O" 100.00 186 99.46 99.46 4.23e-132 PDB 1DHF "Crystal Structures Of Recombinant Human Dihydrofolate Reductase Complexed With Folate And 5-Deazofolate" 100.00 186 100.00 100.00 1.10e-133 PDB 1DLR "Methotrexate-Resistant Variants Of Human Dihydrofolate Reductase With Substitution Of Leucine 22: Kinetics, Crystallography And" 100.00 186 99.46 99.46 6.96e-133 PDB 1DLS "Methotrexate-Resistant Variants Of Human Dihydrofolate Reductase With Substitution Of Leucine 22: Kinetics, Crystallography And" 100.00 186 99.46 99.46 8.47e-133 PDB 1DRF "Crystal Structure Of Human Dihydrofolate Reductase Complexed With Folate" 100.00 186 100.00 100.00 1.10e-133 PDB 1HFP "Comparison Of Ternary Crystal Complexes Of Human Dihydrofolate Reductase With Nadph And A Classical Antitumor Furopyrimdine" 100.00 186 99.46 99.46 4.23e-132 PDB 1HFQ "Comparison Of Ternary Crystal Complexes Of Human Dihydrofolate Reductase With Nadph And A Classical Antitumor Furopyrimdine" 100.00 186 99.46 99.46 1.62e-132 PDB 1HFR "Comparison Of Ternary Crystal Complexes Of Human Dihydrofolate Reductase With Nadph And A Classical Antitumor Furopyrimdine" 100.00 186 100.00 100.00 1.10e-133 PDB 1KMS "Human Dihydrofolate Reductase Complexed With Nadph And 6- ([5-Quinolylamino]methyl)-2,4-Diamino-5-Methylpyrido[2,3- D]pyrimidin" 100.00 186 100.00 100.00 1.10e-133 PDB 1KMV "Human Dihydrofolate Reductase Complexed With Nadph And (Z)- 6-(2-[2,5-Dimethoxyphenyl]ethen-1-Yl)-2,4-Diamino-5- Methylpyrido[2" 100.00 186 100.00 100.00 1.10e-133 PDB 1MVS "Analysis Of Two Polymorphic Forms Of A Pyrido[2,3- D]pyrimidine N9-C10 Reverse-Bridge Antifolate Binary Complex With Human Dihy" 100.00 187 100.00 100.00 1.19e-133 PDB 1MVT "Analysis Of Two Polymorphic Forms Of A Pyrido[2,3- D]pyrimidine N9-C10 Reverse-Bridge Antifolate Binary Complex With Human Dihy" 100.00 187 100.00 100.00 1.19e-133 PDB 1OHJ "Human Dihydrofolate Reductase, Monoclinic (P21) Crystal Form" 100.00 186 100.00 100.00 1.10e-133 PDB 1OHK "Human Dihydrofolate Reductase, Orthorhombic (P21 21 21) Crystal Form" 100.00 186 100.00 100.00 1.10e-133 PDB 1PD8 "Analysis Of Three Crystal Structure Determinations Of A 5- Methyl-6-n-methylanilino Pyridopyrimidine Antifolate Complex With Hu" 100.00 186 100.00 100.00 1.10e-133 PDB 1PD9 "Analysis Of Three Crystal Structure Determinations Of A 5- Methyl-6-N-Methylanilino Pyridopyrimidine Antifolate Complex With Hu" 100.00 186 100.00 100.00 1.10e-133 PDB 1PDB "Analysis Of Three Crystal Structure Determinations Of A 5- Methyl-6-N-Methylanilino Pyridopyrimidine Antifolate Complex With Hu" 100.00 186 100.00 100.00 1.10e-133 PDB 1S3U "Structure Determination Of Tetrahydroquinazoline Antifolates In Complex With Human And Pneumocystis Carinii Dihydrofolate Reduc" 100.00 186 100.00 100.00 1.10e-133 PDB 1S3V "Structure Determination Of Tetrahydroquinazoline Antifolates In Complex With Human And Pneumocystis Carinii Dihydrofolate Reduc" 100.00 186 100.00 100.00 1.10e-133 PDB 1S3W "Structure Determination Of Tetrahydroquinazoline Antifoaltes In Complex With Human And Pneumocystis Carinii Dihydrofolate Reduc" 100.00 186 100.00 100.00 1.10e-133 PDB 1U71 "Understanding The Role Of Leu22 Variants In Methotrexate Resistance: Comparison Of Wild-type And Leu22arg Variant Mouse And Hum" 100.00 186 99.46 99.46 9.66e-133 PDB 1U72 "Understanding The Role Of Leu22 Variants In Methotrexate Resistance: Comparison Of Wild-Type And Leu22arg Variant Mouse And Hum" 100.00 186 100.00 100.00 1.10e-133 PDB 1YHO "Solution Structure Of Human Dihydrofolate Reductase Complexed With Trimethoprim And Nadph, 25 Structures" 100.00 186 100.00 100.00 1.10e-133 PDB 2C2S "Human Dihydrofolate Reductase Complexed With Nadph And 2,4- Diamino-5-(1-O-Carboranylmethyl)-6-Methylpyrimidine, A Novel Boron " 100.00 186 100.00 100.00 1.10e-133 PDB 2C2T "Human Dihydrofolate Reductase Complexed With Nadph And 2,4- Diamino-5-((7,8-Dicarbaundecaboran-7-Yl)methyl)-6- Methylpyrimidine" 100.00 186 100.00 100.00 1.10e-133 PDB 2DHF "Crystal Structures Of Recombinant Human Dihydrofolate Reductase Complexed With Folate And 5-Deazofolate" 100.00 186 100.00 100.00 1.10e-133 PDB 2W3A "Human Dihydrofolate Reductase Complexed With Nadph And Trimethoprim" 100.00 187 100.00 100.00 1.19e-133 PDB 2W3B "Human Dihydrofolate Reductase Complexed With Nadph And A Lipophilic Antifolate Selective For Mycobacterium Avium Dhfr, 6-((2,5-" 100.00 187 100.00 100.00 1.19e-133 PDB 2W3M "Human Dihydrofolate Reductase Complexed With Nadph And Folate" 100.00 187 100.00 100.00 1.19e-133 PDB 3EIG "Crystal Structure Of A Methotrexate-Resistant Mutant Of Human Dihydrofolate Reductase" 100.00 186 98.92 99.46 8.90e-132 PDB 3F8Y "Correlations Of Human Dihydrofolate Reductase With Structural Data For Human Active Site Mutant Enzyme Complexes" 100.00 187 99.46 100.00 4.60e-133 PDB 3F8Z "Human Dihydrofolate Reductase Structural Data With Active Site Mutant Enzyme Complexes" 100.00 187 98.92 99.46 3.33e-132 PDB 3F91 "Structural Data For Human Active Site Mutant Enzyme Complexes" 100.00 187 98.92 98.92 1.54e-131 PDB 3FS6 "Correlations Of Inhibitor Kinetics For Pneumocystis Jirovecii And Human Dihydrofolate Reductase With Structural Data For Human " 100.00 187 100.00 100.00 1.19e-133 PDB 3GHC "Design, Synthesis, And X-Ray Crystal Structure Of Classical And Nonclassical 2-Amino-4-Oxo-5-Substituted-6-Thieno[2,3- D]pyrimi" 100.00 186 98.92 99.46 3.40e-132 PDB 3GHV "Human Dihydrofolate Reductase Q35kN64F DOUBLE MUTANT INHIBITOR Complex" 100.00 186 98.92 99.46 1.50e-131 PDB 3GHW "Human Dihydrofolate Reductase Inhibitor Complex" 100.00 186 100.00 100.00 1.10e-133 PDB 3GI2 "Human Dihydrofolate Reductase Q35k Mutant Inhibitor Complex" 100.00 187 99.46 100.00 4.60e-133 PDB 3GYF "Human Dhfr With Z-Isomer In Orthorhombic Lattice" 100.00 187 100.00 100.00 1.19e-133 PDB 3L3R "Structural, Computational And Kinetic Data For Antifolate Interactions Against Pneumocystis Jirovecii, Pneumocystis Carinii And" 100.00 186 99.46 100.00 5.12e-133 PDB 3N0H "Hdhfr Double Mutant Q35sN64F TRIMETHOPRIM BINARY COMPLEX" 100.00 186 98.92 98.92 2.02e-131 PDB 3NTZ "Design, Synthesis, Biological Evaluation And X-Ray Crystal Structures Of Novel Classical 6,5,6-Tricyclicbenzo[4,5]thieno[2,3-D]" 100.00 186 100.00 100.00 1.10e-133 PDB 3NU0 "Design, Synthesis, Biological Evaluation And X-ray Crystal Structure Of Novel Classical 6,5,6-tricyclicbenzo[4,5]thieno[2,3-d]p" 100.00 186 100.00 100.00 1.10e-133 PDB 3NXO "Perferential Selection Of Isomer Binding From Chiral Mixtures: Alternate Binding Modes Observed For The E- And Z-Isomers Of A S" 100.00 186 99.46 100.00 2.90e-133 PDB 3NXR "Perferential Selection Of Isomer Binding From Chiral Mixtures: Alternate Binding Modes Observed For The E- And Z-Isomers Of A S" 100.00 186 100.00 100.00 1.10e-133 PDB 3NXT "Preferential Selection Of Isomer Binding From Chiral Mixtures: Alternate Binding Modes Observed For The E-And Z-Isomers Of A Se" 100.00 186 100.00 100.00 1.10e-133 PDB 3NXV "Preferential Selection Of Isomer Binding From Chiral Mixtures: Alternate Binding Modes Observed For The E- And Z-Isomers Of A S" 100.00 186 100.00 100.00 1.10e-133 PDB 3NXX "Preferential Selection Of Isomer Binding From Chiral Mixtures: Alternate Binding Modes Observed For The E- And Z-Isomers Of A S" 100.00 186 100.00 100.00 1.10e-133 PDB 3NXY "Preferential Selection Of Isomer Binding From Chiral Mixtures: Alernate Binding Modes Observed Fro The E- And Z-Isomers Of A Se" 100.00 186 100.00 100.00 1.10e-133 PDB 3NZD "Structural Analysis Of Pneumocystis Carinii And Human Dhfr Complexes With Nadph And A Series Of Five 5-(Omega-Carboxy(Alkyloxy(" 100.00 186 100.00 100.00 1.10e-133 PDB 3OAF "Structural And Kinetic Data For Antifolate Interactions Against Pneumocystis Jirovecii, Pneumocystis Carinii And Human Dihydrof" 100.00 186 98.92 98.92 2.02e-131 PDB 3S3V "Human Dihydrofolate Reductase Q35kN64F DOUBLE MUTANT BINARY COMPLEX With Trimethoprim" 100.00 186 98.92 99.46 1.50e-131 PDB 3S7A "Human Dihydrofolate Reductase Binary Complex With Pt684" 100.00 186 100.00 100.00 1.10e-133 PDB 4DDR "Human Dihydrofolate Reductase Complexed With Nadph And P218" 100.00 186 100.00 100.00 1.10e-133 PDB 4G95 "Hdhfr-oag Binary Complex" 100.00 186 100.00 100.00 1.10e-133 PDB 4KAK "Crystal Structure Of Human Dihydrofolate Reductase Complexed With Nadph And 6-ethyl-5-[(3s)-3-[3-methoxy-5-(pyridine-4-yl)pheny" 100.00 186 100.00 100.00 1.10e-133 PDB 4KBN "Human Dihydrofolate Reductase Complexed With Nadph And 5-{3-[3-(3,5- Pyrimidine)]-phenyl-prop-1-yn-1-yl}-6-ethyl-pyrimidine-2,4" 100.00 186 100.00 100.00 1.10e-133 PDB 4KD7 "Human Dihydrofolate Reductase Complexed With Nadph And 5-{3-[3- Methoxy-5(pyridine-4-yl)phenyl]prop-1-yn-1-yl}-6-ethyl-pyrimidi" 100.00 186 100.00 100.00 1.10e-133 PDB 4KEB "Human Dihydrofolate Reductase Complexed With Nadph And 5-{3-[3- Methoxy-5-(isoquin-5-yl)phenyl]but-1-yn-1-yl}6-ethylpyrimidine-" 100.00 186 100.00 100.00 1.10e-133 PDB 4KFJ "Human Dihydrofolate Reductase Complexed With Nadph And 5-{3-[3- Methoxy-5-(isoquin-5-yl)phenyl]prop-1-yn-1-yl}6-ethylprimidine-" 100.00 186 100.00 100.00 1.10e-133 PDB 4M6J "Crystal Structure Of Human Dihydrofolate Reductase (dhfr) Bound To Nadph" 100.00 187 100.00 100.00 1.19e-133 PDB 4M6K "Crystal Structure Of Human Dihydrofolate Reductase (dhfr) Bound To Nadp+ And Folate" 100.00 187 100.00 100.00 1.19e-133 PDB 4M6L "Crystal Structure Of Human Dihydrofolate Reductase (dhfr) Bound To Nadp+ And 5,10-dideazatetrahydrofolic Acid" 100.00 187 100.00 100.00 1.19e-133 DBJ BAG35526 "unnamed protein product [Homo sapiens]" 100.00 187 100.00 100.00 1.19e-133 DBJ BAG56693 "unnamed protein product [Homo sapiens]" 72.58 135 100.00 100.00 3.13e-92 DBJ BAG59770 "unnamed protein product [Homo sapiens]" 65.59 129 100.00 100.00 1.14e-82 DBJ BAJ20267 "dihydrofolate reductase [synthetic construct]" 100.00 187 100.00 100.00 1.19e-133 EMBL CAA23765 "unnamed protein product [Homo sapiens]" 100.00 187 100.00 100.00 1.19e-133 EMBL CAA25409 "dihydrofolate reductase [Homo sapiens]" 100.00 187 100.00 100.00 1.19e-133 GB AAA58484 "dihydrofolate reductase (EC 1.5.1.3) [Homo sapiens]" 100.00 187 100.00 100.00 1.19e-133 GB AAA58485 "dihydrofolate reductase [Homo sapiens]" 100.00 187 100.00 100.00 1.19e-133 GB AAH00192 "Dihydrofolate reductase [Homo sapiens]" 100.00 187 100.00 100.00 1.19e-133 GB AAH03584 "DHFR protein [Homo sapiens]" 100.00 187 100.00 100.00 1.19e-133 GB AAH70280 "Dihydrofolate reductase [Homo sapiens]" 100.00 187 99.46 100.00 3.78e-133 PRF 0905195A reductase,dihydrofolate 100.00 186 100.00 100.00 1.10e-133 PRF 0906214A reductase,dihydrofolate 100.00 186 98.39 99.46 9.09e-132 REF NP_000782 "dihydrofolate reductase isoform 1 [Homo sapiens]" 100.00 187 100.00 100.00 1.19e-133 REF NP_001277283 "dihydrofolate reductase isoform 2 [Homo sapiens]" 72.58 135 100.00 100.00 3.13e-92 REF NP_001277286 "dihydrofolate reductase isoform 3 [Homo sapiens]" 65.59 129 100.00 100.00 1.14e-82 REF XP_001099963 "PREDICTED: dihydrofolate reductase, partial [Macaca mulatta]" 100.00 207 97.31 98.39 2.64e-130 REF XP_001110551 "PREDICTED: dihydrofolate reductase [Macaca mulatta]" 100.00 262 97.85 98.92 2.77e-131 SP P00374 "RecName: Full=Dihydrofolate reductase [Homo sapiens]" 100.00 187 100.00 100.00 1.19e-133 stop_ save_ ############# # Ligands # ############# save_PT523 _Saveframe_category ligand _Mol_type complete _Name_common PT523 _Mol_charge 2- _Mol_paramagnetic no _Mol_aromatic no save_ save_NADPH _Saveframe_category ligand _Mol_type complete _Name_common NADPH _Mol_charge 3- _Mol_paramagnetic no _Mol_aromatic no save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $DHFR Human 9606 Eukaryota Metazoa Homo sapiens stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name $DHFR "recombinant technology" ? ? ? ? ? $PT523 "chemical synthesis" ? ? ? ? ? $NADPH "obtained from a vendor" ? ? ? ? ? stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $DHFR ? mM [U-15N] KCl 25 mM ? "sodium azide" 1 mM ? "potassium phosphate" 50 mM ? stop_ save_ ####################### # Sample conditions # ####################### save_conditions_1 _Saveframe_category sample_conditions loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units temperature 298 0 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_referencing _Saveframe_category chemical_shift_reference 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 water H 1 protons ppm 4.76 direct internal ? ? ? NH4Cl N 15 nitrogen ppm 24.93 direct external ? ? ? 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_list_1 _Saveframe_category assigned_chemical_shifts loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $conditions_1 _Chem_shift_reference_set_label $chemical_shift_referencing _Mol_system_component_name "dihydrofolate reductase" 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 1 VAL HA H 4.21 . . 2 2 2 GLY H H 8.60 . . 3 2 2 GLY HA2 H 4.02 . . 4 2 2 GLY HA3 H 4.78 . . 5 2 2 GLY N N 114.60 . . 6 3 3 SER H H 7.70 . . 7 3 3 SER HA H 4.53 . . 8 3 3 SER HB2 H 3.71 . . 9 3 3 SER HB3 H 3.71 . . 10 3 3 SER N N 115.40 . . 11 4 4 LEU H H 8.34 . . 12 4 4 LEU HA H 4.57 . . 13 4 4 LEU N N 126.10 . . 14 5 5 ASN H H 7.76 . . 15 5 5 ASN HA H 5.68 . . 16 5 5 ASN HB2 H 1.25 . . 17 5 5 ASN HB3 H 1.45 . . 18 5 5 ASN N N 123.10 . . 19 6 6 CYS H H 9.51 . . 20 6 6 CYS HA H 5.80 . . 21 6 6 CYS HB2 H 2.97 . . 22 6 6 CYS HB3 H 3.16 . . 23 6 6 CYS N N 121.00 . . 24 7 7 ILE H H 9.32 . . 25 7 7 ILE HA H 6.33 . . 26 7 7 ILE HB H 1.34 . . 27 7 7 ILE N N 125.40 . . 28 8 8 VAL H H 9.57 . . 29 8 8 VAL HA H 4.76 . . 30 8 8 VAL HG1 H 0.58 . . 31 8 8 VAL HG2 H 0.58 . . 32 8 8 VAL N N 136.80 . . 33 9 9 ALA H H 9.43 . . 34 9 9 ALA HA H 5.14 . . 35 9 9 ALA HB H 1.19 . . 36 9 9 ALA N N 133.90 . . 37 10 10 VAL H H 8.91 . . 38 10 10 VAL HA H 5.36 . . 39 10 10 VAL HB H 1.85 . . 40 10 10 VAL HG1 H 0.57 . . 41 10 10 VAL HG2 H 0.79 . . 42 10 10 VAL N N 117.10 . . 43 11 11 SER H H 9.21 . . 44 11 11 SER HA H 5.13 . . 45 11 11 SER HB2 H 4.44 . . 46 11 11 SER HB3 H 5.44 . . 47 11 11 SER N N 118.70 . . 48 12 12 GLN H H 8.17 . . 49 12 12 GLN HA H 4.19 . . 50 12 12 GLN N N 125.10 . . 51 13 13 ASN H H 9.11 . . 52 13 13 ASN HA H 4.84 . . 53 13 13 ASN HB2 H 2.84 . . 54 13 13 ASN HB3 H 3.31 . . 55 13 13 ASN N N 114.20 . . 56 14 14 MET H H 8.13 . . 57 14 14 MET HA H 4.42 . . 58 14 14 MET N N 113.10 . . 59 15 15 GLY H H 8.17 . . 60 15 15 GLY HA2 H 3.93 . . 61 15 15 GLY HA3 H 4.18 . . 62 15 15 GLY N N 109.80 . . 63 16 16 ILE H H 8.57 . . 64 16 16 ILE HA H 4.97 . . 65 16 16 ILE N N 111.70 . . 66 17 17 GLY H H 6.99 . . 67 17 17 GLY HA2 H 3.57 . . 68 17 17 GLY HA3 H 4.77 . . 69 17 17 GLY N N 106.90 . . 70 18 18 LYS H H 8.88 . . 71 18 18 LYS HA H 4.28 . . 72 18 18 LYS N N 124.10 . . 73 19 19 ASN H H 10.71 . . 74 19 19 ASN HA H 4.36 . . 75 19 19 ASN HB2 H 2.56 . . 76 19 19 ASN HB3 H 3.07 . . 77 19 19 ASN N N 132.70 . . 78 20 20 GLY H H 9.49 . . 79 20 20 GLY HA2 H 3.44 . . 80 20 20 GLY HA3 H 4.07 . . 81 20 20 GLY N N 107.60 . . 82 21 21 ASP H H 7.70 . . 83 21 21 ASP HA H 4.92 . . 84 21 21 ASP HB2 H 2.86 . . 85 21 21 ASP HB3 H 2.86 . . 86 21 21 ASP N N 123.30 . . 87 22 22 LEU H H 9.69 . . 88 22 22 LEU HA H 4.27 . . 89 22 22 LEU HB2 H -0.22 . . 90 22 22 LEU HB3 H 1.34 . . 91 22 22 LEU HG H 1.64 . . 92 22 22 LEU HD1 H 0.67 . . 93 22 22 LEU HD2 H 0.91 . . 94 22 22 LEU N N 125.90 . . 95 24 24 TRP H H 5.13 . . 96 24 24 TRP HA H 4.26 . . 97 24 24 TRP HB2 H 2.54 . . 98 24 24 TRP HB3 H 2.54 . . 99 24 24 TRP HD1 H 7.30 . . 100 24 24 TRP HE1 H 9.29 . . 101 24 24 TRP HE3 H 6.54 . . 102 24 24 TRP HZ2 H 6.85 . . 103 24 24 TRP HZ3 H 7.07 . . 104 24 24 TRP HH2 H 7.13 . . 105 24 24 TRP N N 112.60 . . 106 27 27 LEU H H 8.67 . . 107 27 27 LEU HA H 4.40 . . 108 27 27 LEU HG H 2.01 . . 109 27 27 LEU HD1 H -0.01 . . 110 27 27 LEU HD2 H 0.60 . . 111 27 27 LEU N N 130.10 . . 112 28 28 ARG H H 8.93 . . 113 28 28 ARG HA H 3.61 . . 114 28 28 ARG N N 128.90 . . 115 29 29 ASN H H 10.95 . . 116 29 29 ASN HA H 4.56 . . 117 29 29 ASN HB2 H 2.80 . . 118 29 29 ASN HB3 H 3.11 . . 119 29 29 ASN N N 121.20 . . 120 30 30 GLU H H 7.52 . . 121 30 30 GLU HA H 4.07 . . 122 30 30 GLU N N 131.50 . . 123 31 31 PHE H H 8.13 . . 124 31 31 PHE HA H 4.06 . . 125 31 31 PHE HB2 H 2.77 . . 126 31 31 PHE HB3 H 3.16 . . 127 31 31 PHE HD1 H 6.66 . . 128 31 31 PHE HD2 H 6.66 . . 129 31 31 PHE HE1 H 6.35 . . 130 31 31 PHE HE2 H 6.35 . . 131 31 31 PHE HZ H 7.05 . . 132 31 31 PHE N N 118.30 . . 133 32 32 ARG H H 8.70 . . 134 32 32 ARG HA H 4.00 . . 135 32 32 ARG N N 120.70 . . 136 33 33 TYR H H 7.82 . . 137 33 33 TYR HA H 4.14 . . 138 33 33 TYR HB2 H 3.05 . . 139 33 33 TYR HB3 H 3.34 . . 140 33 33 TYR HD1 H 6.68 . . 141 33 33 TYR HD2 H 6.68 . . 142 33 33 TYR N N 126.70 . . 143 34 34 PHE H H 8.52 . . 144 34 34 PHE HA H 4.07 . . 145 34 34 PHE HB2 H 2.74 . . 146 34 34 PHE HB3 H 3.36 . . 147 34 34 PHE HD1 H 6.92 . . 148 34 34 PHE HD2 H 6.92 . . 149 34 34 PHE N N 122.70 . . 150 35 35 GLN H H 8.98 . . 151 35 35 GLN N N 124.90 . . 152 36 36 ARG H H 8.45 . . 153 36 36 ARG HA H 3.76 . . 154 36 36 ARG N N 125.00 . . 155 37 37 MET H H 8.32 . . 156 37 37 MET HA H 3.84 . . 157 37 37 MET N N 119.70 . . 158 38 38 THR H H 6.68 . . 159 38 38 THR HA H 2.01 . . 160 38 38 THR HB H 3.06 . . 161 38 38 THR HG2 H -0.16 . . 162 38 38 THR N N 104.00 . . 163 39 39 THR H H 7.43 . . 164 39 39 THR HA H 3.88 . . 165 39 39 THR N N 117.50 . . 166 40 40 THR H H 7.12 . . 167 40 40 THR HA H 3.92 . . 168 40 40 THR HB H 4.18 . . 169 40 40 THR HG2 H 1.13 . . 170 40 40 THR N N 119.50 . . 171 41 41 SER H H 8.69 . . 172 41 41 SER HA H 4.95 . . 173 41 41 SER N N 128.70 . . 174 42 42 SER H H 9.65 . . 175 42 42 SER HA H 4.48 . . 176 42 42 SER N N 123.20 . . 177 43 43 VAL H H 7.64 . . 178 43 43 VAL HA H 4.23 . . 179 43 43 VAL N N 123.70 . . 180 44 44 GLU H H 8.70 . . 181 44 44 GLU HA H 4.05 . . 182 44 44 GLU N N 130.60 . . 183 45 45 GLY H H 8.87 . . 184 45 45 GLY HA2 H 3.69 . . 185 45 45 GLY HA3 H 4.23 . . 186 45 45 GLY N N 114.70 . . 187 46 46 LYS H H 7.50 . . 188 46 46 LYS HA H 4.74 . . 189 46 46 LYS N N 120.20 . . 190 47 47 GLN H H 8.41 . . 191 47 47 GLN HA H 4.86 . . 192 47 47 GLN N N 120.00 . . 193 48 48 ASN H H 9.99 . . 194 48 48 ASN HA H 5.52 . . 195 48 48 ASN N N 122.40 . . 196 49 49 LEU H H 8.91 . . 197 49 49 LEU HA H 5.19 . . 198 49 49 LEU N N 125.60 . . 199 50 50 VAL H H 9.49 . . 200 50 50 VAL HA H 5.54 . . 201 50 50 VAL N N 123.90 . . 202 51 51 ILE H H 9.02 . . 203 51 51 ILE HA H 4.85 . . 204 51 51 ILE N N 126.60 . . 205 52 52 MET H H 8.73 . . 206 52 52 MET HA H 5.65 . . 207 52 52 MET N N 126.30 . . 208 53 53 GLY H H 9.29 . . 209 53 53 GLY HA2 H 4.11 . . 210 53 53 GLY N N 108.30 . . 211 55 55 LYS H H 7.83 . . 212 55 55 LYS HA H 4.34 . . 213 55 55 LYS HB2 H 1.98 . . 214 55 55 LYS HB3 H 2.26 . . 215 55 55 LYS N N 116.90 . . 216 56 56 THR H H 9.00 . . 217 56 56 THR HA H 3.62 . . 218 56 56 THR HG2 H 1.10 . . 219 56 56 THR N N 123.30 . . 220 57 57 TRP H H 7.78 . . 221 57 57 TRP HA H 3.36 . . 222 57 57 TRP HB2 H 2.96 . . 223 57 57 TRP HB3 H 3.20 . . 224 57 57 TRP HD1 H 4.69 . . 225 57 57 TRP HE1 H 9.71 . . 226 57 57 TRP HE3 H 7.86 . . 227 57 57 TRP HZ2 H 7.38 . . 228 57 57 TRP HZ3 H 7.29 . . 229 57 57 TRP HH2 H 6.24 . . 230 57 57 TRP N N 124.60 . . 231 58 58 PHE H H 7.46 . . 232 58 58 PHE HA H 4.08 . . 233 58 58 PHE HB2 H 2.83 . . 234 58 58 PHE HB3 H 3.32 . . 235 58 58 PHE N N 112.80 . . 236 59 59 SER H H 7.95 . . 237 59 59 SER HA H 4.49 . . 238 59 59 SER N N 118.90 . . 239 60 60 ILE H H 7.17 . . 240 60 60 ILE HA H 3.68 . . 241 60 60 ILE HB H 1.07 . . 242 60 60 ILE HG12 H 0.23 . . 243 60 60 ILE HG13 H 0.23 . . 244 60 60 ILE HG2 H 0.19 . . 245 60 60 ILE HD1 H -0.78 . . 246 60 60 ILE N N 132.00 . . 247 62 62 GLU H H 8.60 . . 248 62 62 GLU HA H 3.35 . . 249 62 62 GLU N N 127.20 . . 250 63 63 LYS H H 8.27 . . 251 63 63 LYS HA H 4.09 . . 252 63 63 LYS N N 117.30 . . 253 64 64 ASN H H 8.08 . . 254 64 64 ASN HA H 4.72 . . 255 64 64 ASN HB2 H 2.29 . . 256 64 64 ASN HB3 H 2.90 . . 257 64 64 ASN N N 119.50 . . 258 65 65 ARG H H 7.08 . . 259 65 65 ARG HA H 4.04 . . 260 65 65 ARG HB2 H 1.24 . . 261 65 65 ARG HB3 H 1.24 . . 262 65 65 ARG N N 118.80 . . 263 67 67 LEU H H 9.27 . . 264 67 67 LEU HA H 4.19 . . 265 67 67 LEU HD1 H 0.74 . . 266 67 67 LEU HD2 H 0.74 . . 267 67 67 LEU N N 121.80 . . 268 68 68 LYS H H 8.78 . . 269 68 68 LYS HA H 4.12 . . 270 68 68 LYS N N 129.50 . . 271 70 70 ARG H H 7.45 . . 272 70 70 ARG HA H 4.73 . . 273 70 70 ARG HE H 5.72 . . 274 70 70 ARG N N 120.10 . . 275 71 71 ILE H H 9.07 . . 276 71 71 ILE HA H 4.19 . . 277 71 71 ILE HD1 H 6.98 . . 278 71 71 ILE N N 126.60 . . 279 72 72 ASN H H 12.84 . . 280 72 72 ASN HA H 5.17 . . 281 72 72 ASN N N 133.40 . . 282 73 73 LEU H H 9.26 . . 283 73 73 LEU HA H 5.05 . . 284 73 73 LEU N N 131.60 . . 285 74 74 VAL H H 8.12 . . 286 74 74 VAL HA H 4.73 . . 287 74 74 VAL HG1 H 0.06 . . 288 74 74 VAL HG2 H 0.43 . . 289 74 74 VAL N N 128.30 . . 290 75 75 LEU H H 8.40 . . 291 75 75 LEU HA H 4.94 . . 292 75 75 LEU N N 128.40 . . 293 76 76 SER H H 7.94 . . 294 76 76 SER HA H 5.08 . . 295 76 76 SER HB2 H 3.25 . . 296 76 76 SER HB3 H 3.25 . . 297 76 76 SER N N 115.40 . . 298 77 77 ARG H H 11.04 . . 299 77 77 ARG HA H 4.50 . . 300 77 77 ARG HB2 H 1.93 . . 301 77 77 ARG HB3 H 1.93 . . 302 77 77 ARG N N 130.60 . . 303 78 78 GLU H H 8.28 . . 304 78 78 GLU HA H 4.30 . . 305 78 78 GLU N N 121.20 . . 306 79 79 LEU H H 8.33 . . 307 79 79 LEU HA H 4.12 . . 308 79 79 LEU N N 121.60 . . 309 80 80 LYS H H 8.72 . . 310 80 80 LYS HA H 4.18 . . 311 80 80 LYS N N 120.30 . . 312 81 81 GLU H H 7.46 . . 313 81 81 GLU HA H 4.63 . . 314 81 81 GLU N N 118.50 . . 315 84 84 GLN H H 8.46 . . 316 84 84 GLN HA H 3.89 . . 317 84 84 GLN N N 123.50 . . 318 85 85 GLY H H 8.80 . . 319 85 85 GLY HA2 H 3.46 . . 320 85 85 GLY HA3 H 4.44 . . 321 85 85 GLY N N 118.80 . . 322 86 86 ALA H H 7.94 . . 323 86 86 ALA HA H 3.53 . . 324 86 86 ALA HB H 0.15 . . 325 86 86 ALA N N 125.10 . . 326 87 87 HIS H H 7.60 . . 327 87 87 HIS HA H 4.06 . . 328 87 87 HIS HD1 H 7.03 . . 329 87 87 HIS HD2 H 7.03 . . 330 87 87 HIS HE1 H 8.05 . . 331 87 87 HIS N N 120.50 . . 332 88 88 PHE H H 7.66 . . 333 88 88 PHE HA H 4.70 . . 334 88 88 PHE HB2 H 2.20 . . 335 88 88 PHE HB3 H 2.20 . . 336 88 88 PHE HD1 H 7.03 . . 337 88 88 PHE HD2 H 7.03 . . 338 88 88 PHE HE1 H 7.23 . . 339 88 88 PHE HE2 H 7.23 . . 340 88 88 PHE N N 113.90 . . 341 89 89 LEU H H 8.77 . . 342 89 89 LEU HA H 5.50 . . 343 89 89 LEU HB2 H 1.56 . . 344 89 89 LEU HB3 H 1.56 . . 345 89 89 LEU N N 126.00 . . 346 90 90 SER H H 8.53 . . 347 90 90 SER HA H 4.92 . . 348 90 90 SER HB2 H 3.34 . . 349 90 90 SER HB3 H 3.84 . . 350 90 90 SER N N 121.70 . . 351 91 91 ARG H H 8.86 . . 352 91 91 ARG HA H 4.61 . . 353 91 91 ARG N N 121.50 . . 354 92 92 SER H H 7.47 . . 355 92 92 SER HA H 5.25 . . 356 92 92 SER N N 110.90 . . 357 93 93 LEU H H 9.49 . . 358 93 93 LEU HA H 3.95 . . 359 93 93 LEU N N 125.90 . . 360 94 94 ASP H H 8.64 . . 361 94 94 ASP HA H 4.31 . . 362 94 94 ASP HB2 H 2.61 . . 363 94 94 ASP HB3 H 2.61 . . 364 94 94 ASP N N 119.90 . . 365 95 95 ASP H H 8.08 . . 366 95 95 ASP HA H 4.26 . . 367 95 95 ASP HB2 H 2.67 . . 368 95 95 ASP HB3 H 2.67 . . 369 95 95 ASP N N 121.5 . . 370 96 96 ALA H H 7.82 . . 371 96 96 ALA HA H 4.05 . . 372 96 96 ALA HB H 1.40 . . 373 96 96 ALA N N 126.70 . . 374 97 97 LEU H H 8.11 . . 375 97 97 LEU HA H 3.98 . . 376 97 97 LEU N N 115.80 . . 377 98 98 LYS H H 8.11 . . 378 98 98 LYS HA H 4.01 . . 379 98 98 LYS N N 124.20 . . 380 99 99 LEU H H 7.68 . . 381 99 99 LEU HA H 3.94 . . 382 99 99 LEU N N 124.10 . . 383 100 100 THR H H 7.09 . . 384 100 100 THR HA H 3.74 . . 385 100 100 THR N N 106.40 . . 386 101 101 GLU H H 7.28 . . 387 101 101 GLU HA H 4.34 . . 388 101 101 GLU N N 118.90 . . 389 102 102 GLN H H 7.62 . . 390 102 102 GLN HA H 4.52 . . 391 102 102 GLN N N 123.30 . . 392 104 104 GLU H H 9.22 . . 393 104 104 GLU HA H 4.09 . . 394 104 104 GLU N N 117.90 . . 395 105 105 LEU H H 7.46 . . 396 105 105 LEU HA H 4.53 . . 397 105 105 LEU N N 118.50 . . 398 106 106 ALA H H 8.43 . . 399 106 106 ALA HA H 4.18 . . 400 106 106 ALA N N 125.90 . . 401 107 107 ASN H H 8.42 . . 402 107 107 ASN HA H 4.67 . . 403 107 107 ASN N N 114.70 . . 404 108 108 LYS H H 7.93 . . 405 108 108 LYS HA H 4.55 . . 406 108 108 LYS N N 119.70 . . 407 109 109 VAL H H 7.53 . . 408 109 109 VAL HA H 5.05 . . 409 109 109 VAL N N 120.10 . . 410 110 110 ASP H H 8.54 . . 411 110 110 ASP HA H 5.00 . . 412 110 110 ASP N N 128.10 . . 413 111 111 MET H H 8.00 . . 414 111 111 MET HA H 4.35 . . 415 111 111 MET N N 117.60 . . 416 112 112 VAL H H 8.39 . . 417 112 112 VAL HA H 4.73 . . 418 112 112 VAL N N 122.30 . . 419 113 113 TRP H H 9.55 . . 420 113 113 TRP HA H 5.19 . . 421 113 113 TRP HB2 H 2.80 . . 422 113 113 TRP HB3 H 3.00 . . 423 113 113 TRP HD1 H 6.72 . . 424 113 113 TRP HE1 H 8.52 . . 425 113 113 TRP HE3 H 6.88 . . 426 113 113 TRP HZ2 H 6.94 . . 427 113 113 TRP HZ3 H 6.34 . . 428 113 113 TRP HH2 H 5.22 . . 429 113 113 TRP N N 129.60 . . 430 114 114 ILE H H 9.74 . . 431 114 114 ILE HA H 4.74 . . 432 114 114 ILE HB H 2.61 . . 433 114 114 ILE HG2 H 0.88 . . 434 114 114 ILE N N 127.10 . . 435 115 115 VAL H H 8.78 . . 436 115 115 VAL HA H 5.35 . . 437 115 115 VAL HB H 2.97 . . 438 115 115 VAL HG1 H 1.16 . . 439 115 115 VAL HG2 H 1.16 . . 440 115 115 VAL N N 121.60 . . 441 116 116 GLY H H 6.10 . . 442 116 116 GLY HA2 H 2.61 . . 443 116 116 GLY HA3 H 4.75 . . 444 116 116 GLY N N 103.10 . . 445 117 117 GLY H H 7.34 . . 446 117 117 GLY HA2 H 3.59 . . 447 117 117 GLY HA3 H 4.38 . . 448 117 117 GLY N N 111.70 . . 449 118 118 SER H H 8.91 . . 450 118 118 SER N N 120.00 . . 451 119 119 SER H H 10.04 . . 452 119 119 SER HA H 4.32 . . 453 119 119 SER HB2 H 4.04 . . 454 119 119 SER HB3 H 4.04 . . 455 119 119 SER N N 118.70 . . 456 120 120 VAL H H 7.56 . . 457 120 120 VAL HA H 3.81 . . 458 120 120 VAL HB H 1.83 . . 459 120 120 VAL HG1 H 0.76 . . 460 120 120 VAL HG2 H 0.89 . . 461 120 120 VAL N N 126.50 . . 462 121 121 TYR H H 8.06 . . 463 121 121 TYR HA H 4.36 . . 464 121 121 TYR HB2 H 2.95 . . 465 121 121 TYR HB3 H 2.95 . . 466 121 121 TYR N N 119.90 . . 467 122 122 LYS H H 8.20 . . 468 122 122 LYS HA H 3.75 . . 469 122 122 LYS N N 119.10 . . 470 123 123 GLU H H 7.32 . . 471 123 123 GLU HA H 4.17 . . 472 123 123 GLU HB2 H 2.18 . . 473 123 123 GLU HB3 H 2.18 . . 474 123 123 GLU N N 118.60 . . 475 124 124 ALA H H 8.46 . . 476 124 124 ALA HA H 3.80 . . 477 124 124 ALA HB H 1.43 . . 478 124 124 ALA N N 123.50 . . 479 125 125 MET H H 8.53 . . 480 125 125 MET HA H 4.07 . . 481 125 125 MET N N 114.40 . . 482 126 126 ASN H H 7.29 . . 483 126 126 ASN HA H 4.87 . . 484 126 126 ASN N N 117.60 . . 485 127 127 HIS H H 7.73 . . 486 127 127 HIS HA H 4.66 . . 487 127 127 HIS N N 126.10 . . 488 129 129 GLY H H 8.53 . . 489 129 129 GLY HA2 H 3.82 . . 490 129 129 GLY HA3 H 4.37 . . 491 129 129 GLY N N 112.40 . . 492 130 130 HIS H H 8.57 . . 493 130 130 HIS HA H 5.00 . . 494 130 130 HIS N N 121.70 . . 495 131 131 LEU H H 8.19 . . 496 131 131 LEU HA H 5.02 . . 497 131 131 LEU N N 132.20 . . 498 132 132 LYS H H 7.76 . . 499 132 132 LYS HA H 5.43 . . 500 132 132 LYS N N 123.10 . . 501 133 133 LEU H H 9.24 . . 502 133 133 LEU HA H 5.08 . . 503 133 133 LEU N N 123.20 . . 504 134 134 PHE H H 9.75 . . 505 134 134 PHE HA H 5.04 . . 506 134 134 PHE HB2 H 3.41 . . 507 134 134 PHE HB3 H 3.41 . . 508 134 134 PHE N N 129.10 . . 509 135 135 VAL H H 9.12 . . 510 135 135 VAL HA H 4.60 . . 511 135 135 VAL HB H 2.07 . . 512 135 135 VAL HG1 H 0.55 . . 513 135 135 VAL HG2 H 0.55 . . 514 135 135 VAL N N 129.90 . . 515 136 136 THR H H 9.32 . . 516 136 136 THR HA H 5.17 . . 517 136 136 THR HB H 4.09 . . 518 136 136 THR HG2 H 0.77 . . 519 136 136 THR N N 128.80 . . 520 137 137 ARG H H 9.30 . . 521 137 137 ARG HA H 4.29 . . 522 137 137 ARG N N 130.10 . . 523 138 138 ILE H H 8.99 . . 524 138 138 ILE HA H 3.98 . . 525 138 138 ILE HD1 H -0.99 . . 526 138 138 ILE N N 128.40 . . 527 139 139 MET H H 8.86 . . 528 139 139 MET HA H 4.21 . . 529 139 139 MET HB2 H 2.21 . . 530 139 139 MET HB3 H 2.21 . . 531 139 139 MET N N 134.80 . . 532 140 140 GLN H H 8.42 . . 533 140 140 GLN HA H 4.29 . . 534 140 140 GLN N N 121.40 . . 535 141 141 ASP H H 8.72 . . 536 141 141 ASP HA H 4.85 . . 537 141 141 ASP N N 127.50 . . 538 142 142 PHE H H 8.08 . . 539 142 142 PHE HA H 4.76 . . 540 142 142 PHE N N 119.50 . . 541 143 143 GLU H H 8.21 . . 542 143 143 GLU HA H 4.30 . . 543 143 143 GLU HB2 H 2.05 . . 544 143 143 GLU HB3 H 2.05 . . 545 143 143 GLU N N 129.40 . . 546 144 144 SER H H 8.83 . . 547 144 144 SER HA H 4.86 . . 548 144 144 SER N N 122.90 . . 549 145 145 ASP H H 9.19 . . 550 145 145 ASP HA H 4.96 . . 551 145 145 ASP HB2 H 3.18 . . 552 145 145 ASP HB3 H 3.18 . . 553 145 145 ASP N N 120.30 . . 554 146 146 THR H H 7.14 . . 555 146 146 THR HA H 4.65 . . 556 146 146 THR HB H 3.57 . . 557 146 146 THR HG2 H 1.45 . . 558 146 146 THR N N 120.50 . . 559 147 147 PHE H H 9.43 . . 560 147 147 PHE HA H 5.38 . . 561 147 147 PHE HB2 H 2.67 . . 562 147 147 PHE HB3 H 3.15 . . 563 147 147 PHE N N 129.20 . . 564 148 148 PHE H H 9.26 . . 565 148 148 PHE HA H 4.82 . . 566 148 148 PHE HB2 H 2.78 . . 567 148 148 PHE HB3 H 2.88 . . 568 148 148 PHE HD1 H 6.94 . . 569 148 148 PHE HD2 H 6.94 . . 570 148 148 PHE HE1 H 6.23 . . 571 148 148 PHE HE2 H 6.23 . . 572 148 148 PHE HZ H 6.74 . . 573 148 148 PHE N N 128.00 . . 574 150 150 GLU H H 7.56 . . 575 150 150 GLU HA H 3.89 . . 576 150 150 GLU HB2 H 1.81 . . 577 150 150 GLU HB3 H 1.81 . . 578 150 150 GLU N N 117.60 . . 579 151 151 ILE H H 8.12 . . 580 151 151 ILE HA H 3.44 . . 581 151 151 ILE HG2 H -0.02 . . 582 151 151 ILE N N 126.50 . . 583 152 152 ASP H H 8.47 . . 584 152 152 ASP HA H 4.61 . . 585 152 152 ASP HB2 H 2.68 . . 586 152 152 ASP HB3 H 2.97 . . 587 152 152 ASP N N 129.40 . . 588 153 153 LEU H H 8.71 . . 589 153 153 LEU HA H 4.73 . . 590 153 153 LEU N N 131.30 . . 591 154 154 GLU H H 8.62 . . 592 154 154 GLU HA H 4.30 . . 593 154 154 GLU N N 119.50 . . 594 155 155 LYS H H 7.45 . . 595 155 155 LYS HA H 4.28 . . 596 155 155 LYS N N 120.10 . . 597 156 156 TYR H H 8.29 . . 598 156 156 TYR HA H 4.52 . . 599 156 156 TYR HD1 H 6.99 . . 600 156 156 TYR HD2 H 6.99 . . 601 156 156 TYR HE1 H 6.68 . . 602 156 156 TYR HE2 H 6.68 . . 603 156 156 TYR N N 119.60 . . 604 157 157 LYS H H 8.53 . . 605 157 157 LYS HA H 4.66 . . 606 157 157 LYS HB2 H 1.52 . . 607 157 157 LYS HB3 H 1.86 . . 608 157 157 LYS N N 121.70 . . 609 158 158 LEU H H 8.61 . . 610 158 158 LEU HA H 3.87 . . 611 158 158 LEU N N 128.30 . . 612 159 159 LEU H H 9.11 . . 613 159 159 LEU HA H 4.73 . . 614 159 159 LEU N N 133.10 . . 615 161 161 GLU H H 7.56 . . 616 161 161 GLU HA H 4.40 . . 617 161 161 GLU N N 115.00 . . 618 162 162 TYR H H 8.77 . . 619 162 162 TYR HA H 4.66 . . 620 162 162 TYR HD1 H 7.21 . . 621 162 162 TYR HD2 H 7.21 . . 622 162 162 TYR HE1 H 6.90 . . 623 162 162 TYR HE2 H 6.90 . . 624 164 164 GLY H H 8.63 . . 625 164 164 GLY HA2 H 3.66 . . 626 164 164 GLY HA3 H 4.17 . . 627 164 164 GLY N N 112.60 . . 628 165 165 VAL H H 7.95 . . 629 165 165 VAL HA H 4.39 . . 630 165 165 VAL N N 124.10 . . 631 166 166 LEU H H 8.79 . . 632 166 166 LEU HA H 4.44 . . 633 166 166 LEU N N 132.00 . . 634 167 167 SER H H 8.74 . . 635 167 167 SER HA H 4.74 . . 636 167 167 SER N N 118.70 . . 637 168 168 ASP H H 7.93 . . 638 168 168 ASP HA H 4.64 . . 639 168 168 ASP N N 122.10 . . 640 169 169 VAL H H 8.67 . . 641 169 169 VAL HA H 3.59 . . 642 169 169 VAL N N 126.60 . . 643 170 170 GLN H H 8.93 . . 644 170 170 GLN HA H 4.08 . . 645 170 170 GLN N N 130.00 . . 646 171 171 GLU H H 7.93 . . 647 171 171 GLU HA H 5.10 . . 648 171 171 GLU N N 119.70 . . 649 172 172 GLU H H 8.77 . . 650 172 172 GLU HA H 4.47 . . 651 172 172 GLU HB2 H 2.13 . . 652 172 172 GLU HB3 H 2.13 . . 653 172 172 GLU N N 128.10 . . 654 173 173 LYS H H 9.25 . . 655 173 173 LYS HA H 3.87 . . 656 173 173 LYS N N 122.30 . . 657 174 174 GLY H H 8.71 . . 658 174 174 GLY HA2 H 3.63 . . 659 174 174 GLY HA3 H 4.06 . . 660 174 174 GLY N N 105.90 . . 661 175 175 ILE H H 8.31 . . 662 175 175 ILE HA H 4.07 . . 663 175 175 ILE N N 127.10 . . 664 176 176 LYS H H 8.30 . . 665 176 176 LYS HA H 5.29 . . 666 176 176 LYS N N 128.30 . . 667 177 177 TYR H H 8.49 . . 668 177 177 TYR HA H 5.35 . . 669 177 177 TYR HB2 H 2.11 . . 670 177 177 TYR HB3 H 2.66 . . 671 177 177 TYR HD1 H 6.09 . . 672 177 177 TYR HD2 H 6.09 . . 673 177 177 TYR HE1 H 6.43 . . 674 177 177 TYR HE2 H 6.43 . . 675 177 177 TYR N N 117.90 . . 676 178 178 LYS H H 8.17 . . 677 178 178 LYS HA H 4.30 . . 678 178 178 LYS N N 118.40 . . 679 179 179 PHE H H 9.26 . . 680 179 179 PHE HA H 5.12 . . 681 179 179 PHE N N 125.40 . . 682 180 180 GLU H H 9.31 . . 683 180 180 GLU HA H 4.67 . . 684 180 180 GLU N N 124.50 . . 685 181 181 VAL H H 8.61 . . 686 181 181 VAL HA H 4.72 . . 687 181 181 VAL HG1 H 0.47 . . 688 181 181 VAL HG2 H -0.36 . . 689 181 181 VAL N N 125.40 . . 690 182 182 TYR H H 9.20 . . 691 182 182 TYR HA H 5.53 . . 692 182 182 TYR N N 125.20 . . 693 183 183 GLU H H 9.28 . . 694 183 183 GLU HA H 5.40 . . 695 183 183 GLU N N 122.10 . . 696 184 184 LYS H H 8.86 . . 697 184 184 LYS HA H 4.64 . . 698 184 184 LYS N N 128.30 . . 699 185 185 ASN H H 8.77 . . 700 185 185 ASN HA H 4.74 . . 701 185 185 ASN N N 124.70 . . 702 186 186 ASP H H 7.72 . . 703 186 186 ASP HA H 4.35 . . 704 186 186 ASP N N 128.30 . . stop_ save_