data_4173 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution Structure of the Catalytic Domain of Human Stromelysin-1 Complexed to a Potent, Non-peptidic Inhibitor ; _BMRB_accession_number 4173 _BMRB_flat_file_name bmr4173.str _Entry_type original _Submission_date 1998-08-03 _Accession_date 1998-08-03 _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 Li Y. . . 2 Zhang X. . . 3 Melton R. . . 4 Ganu V. . . 5 Gonnella N. C. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 760 "15N chemical shifts" 151 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2000-04-03 original author . stop_ _Original_release_date 2000-04-03 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Solution Structure of the Catalytic Domain of Human Stromelysin-1 Complexed to a Potent, Non-peptidic Inhibitor ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 98434377 _PubMed_ID 9760240 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Li Y. . . 2 Zhang X. . . 3 Melton R. . . 4 Ganu V. . . 5 Gonnella N. C. . stop_ _Journal_abbreviation Biochemistry _Journal_name_full Biochemistry _Journal_volume 37 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 14048 _Page_last 14056 _Year 1998 _Details . loop_ _Keyword Metzincins stop_ save_ ################################## # Molecular system description # ################################## save_system_SLN _Saveframe_category molecular_system _Mol_system_name 'stromelysin-1 subunit 1' _Abbreviation_common SLN _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label STROMELYSIN-1 $SLN entity_ZN $entity_ZN entity_HAI $entity_HAI stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' _Database_query_date . _Details ; Solution structure of the catalytic domain of human stromelysin-1 complexed to a potent, non-peptidic inhibitor ; save_ ######################## # Monomeric polymers # ######################## save_SLN _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common STROMELYSIN-1 _Abbreviation_common SLN _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 173 _Mol_residue_sequence ; FRTFPGIPKWRKTHLTYRIV NYTPDLPKDAVDSAVEKALK VWEEVTPLTFSRLYEGEADI MISFAVREHGDFYPFDGPGN VLAHAYAPGPGINGDAHFDD DEQWTKDTTGTNLFLVAAHE IGHSLGLFHSANTEALMYPL YHSLTDLTRFRLSQDDINGI QSLYGPPPDSPET ; loop_ _Residue_seq_code _Residue_label 1 PHE 2 ARG 3 THR 4 PHE 5 PRO 6 GLY 7 ILE 8 PRO 9 LYS 10 TRP 11 ARG 12 LYS 13 THR 14 HIS 15 LEU 16 THR 17 TYR 18 ARG 19 ILE 20 VAL 21 ASN 22 TYR 23 THR 24 PRO 25 ASP 26 LEU 27 PRO 28 LYS 29 ASP 30 ALA 31 VAL 32 ASP 33 SER 34 ALA 35 VAL 36 GLU 37 LYS 38 ALA 39 LEU 40 LYS 41 VAL 42 TRP 43 GLU 44 GLU 45 VAL 46 THR 47 PRO 48 LEU 49 THR 50 PHE 51 SER 52 ARG 53 LEU 54 TYR 55 GLU 56 GLY 57 GLU 58 ALA 59 ASP 60 ILE 61 MET 62 ILE 63 SER 64 PHE 65 ALA 66 VAL 67 ARG 68 GLU 69 HIS 70 GLY 71 ASP 72 PHE 73 TYR 74 PRO 75 PHE 76 ASP 77 GLY 78 PRO 79 GLY 80 ASN 81 VAL 82 LEU 83 ALA 84 HIS 85 ALA 86 TYR 87 ALA 88 PRO 89 GLY 90 PRO 91 GLY 92 ILE 93 ASN 94 GLY 95 ASP 96 ALA 97 HIS 98 PHE 99 ASP 100 ASP 101 ASP 102 GLU 103 GLN 104 TRP 105 THR 106 LYS 107 ASP 108 THR 109 THR 110 GLY 111 THR 112 ASN 113 LEU 114 PHE 115 LEU 116 VAL 117 ALA 118 ALA 119 HIS 120 GLU 121 ILE 122 GLY 123 HIS 124 SER 125 LEU 126 GLY 127 LEU 128 PHE 129 HIS 130 SER 131 ALA 132 ASN 133 THR 134 GLU 135 ALA 136 LEU 137 MET 138 TYR 139 PRO 140 LEU 141 TYR 142 HIS 143 SER 144 LEU 145 THR 146 ASP 147 LEU 148 THR 149 ARG 150 PHE 151 ARG 152 LEU 153 SER 154 GLN 155 ASP 156 ASP 157 ILE 158 ASN 159 GLY 160 ILE 161 GLN 162 SER 163 LEU 164 TYR 165 GLY 166 PRO 167 PRO 168 PRO 169 ASP 170 SER 171 PRO 172 GLU 173 THR stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-02-04 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 15120 MMP3 93.06 161 100.00 100.00 8.56e-114 BMRB 15395 MMP3 93.06 161 99.38 99.38 1.91e-112 BMRB 15396 MMP3 93.06 161 99.38 99.38 1.91e-112 BMRB 4364 stromelysin 95.95 166 99.40 99.40 1.47e-116 BMRB 4365 stromelysin 95.95 166 99.40 99.40 1.47e-116 BMRB 4366 stromelysin 95.95 166 99.40 99.40 1.47e-116 PDB 1B3D Stromelysin-1 100.00 173 100.00 100.00 3.08e-123 PDB 1B8Y "X-Ray Structure Of Human Stromelysin Catalytic Domain Complexed With Non-Peptide Inhibitors: Implications For Inhibitor Selecti" 96.53 167 100.00 100.00 8.03e-119 PDB 1BIW "Design And Synthesis Of Conformationally-Constrained Mmp Inhibitors" 100.00 173 100.00 100.00 3.08e-123 PDB 1BM6 "Solution Structure Of The Catalytic Domain Of Human Stromelysin-1 Complexed To A Potent Non-Peptidic Inhibitor, Nmr, 20 Structu" 100.00 173 100.00 100.00 3.08e-123 PDB 1BQO "Discovery Of Potent, Achiral Matrix Metalloproteinase Inhibitors" 100.00 173 100.00 100.00 3.08e-123 PDB 1C3I "Human Stromelysin-1 Catalytic Domain Complexed With Ro-26-2812" 100.00 173 100.00 100.00 3.08e-123 PDB 1C8T "Human Stromelysin-1 (E202q) Catalytic Domain Complexed With Ro-26-2812" 95.95 167 99.40 100.00 2.00e-117 PDB 1CAQ "X-Ray Structure Of Human Stromelysin Catalytic Domain Complexes With Non-Peptide Inhibitors: Implication For Inhibitor Selectiv" 97.11 168 100.00 100.00 1.17e-119 PDB 1CIZ "X-ray Structure Of Human Stromelysin Catalytic Domain Complexes With Non-peptide Inhibitors: Implication For Inhibitor Selectiv" 97.11 168 100.00 100.00 1.17e-119 PDB 1CQR "Crystal Structure Of The Stromelysin Catalytic Domain At 2.0 A Resolution" 100.00 173 100.00 100.00 3.08e-123 PDB 1D5J "Crystal Structure Of Mmp3 Complexed With A Thiazepine Based Inhibitor." 100.00 173 100.00 100.00 3.08e-123 PDB 1D7X "Crystal Structure Of Mmp3 Complexed With A Modified Proline Scaffold Based Inhibitor." 100.00 173 100.00 100.00 3.08e-123 PDB 1D8F "Crystal Structure Of Mmp3 Complexed With A Piperazine Based Inhibitor." 100.00 173 100.00 100.00 3.08e-123 PDB 1D8M "Crystal Structure Of Mmp3 Complexed With A Heterocycle- Based Inhibitor" 100.00 173 100.00 100.00 3.08e-123 PDB 1G05 "Heterocycle-Based Mmp Inhibitor With P2'substituents" 100.00 173 100.00 100.00 3.08e-123 PDB 1G49 "A Carboxylic Acid Based Inhibitor In Complex With Mmp3" 100.00 173 100.00 100.00 3.08e-123 PDB 1G4K "X-ray Structure Of A Novel Matrix Metalloproteinase Inhibitor Complexed To Stromelysin" 97.11 168 100.00 100.00 1.17e-119 PDB 1HFS "Crystal Structure Of The Catalytic Domain Of Human Fibroblast Stromelysin-1 Inhibited With The N-Carboxy-Alkyl Inhibitor L-764," 92.49 160 100.00 100.00 4.86e-113 PDB 1HY7 "A Carboxylic Acid Based Inhibitor In Complex With Mmp3" 100.00 173 100.00 100.00 3.08e-123 PDB 1OO9 "Orientation In Solution Of Mmp-3 Catalytic Domain And N- Timp-1 From Residual Dipolar Couplings" 97.11 168 100.00 100.00 1.17e-119 PDB 1QIA "Crystal Structure Of Stromelysin Catalytic Domain" 93.64 162 100.00 100.00 1.06e-114 PDB 1QIC "Crystal Structure Of Stromelysin Catalytic Domain" 93.06 161 100.00 100.00 6.51e-114 PDB 1SLM "Crystal Structure Of Fibroblast Stromelysin-1: The C-Truncated Human Proenzyme" 100.00 255 100.00 100.00 2.10e-123 PDB 1SLN "Crystal Structure Of The Catalytic Domain Of Human Fibroblast Stromelysin-1 Inhibited With The N-Carboxy-Alkyl Inhibitor L-702," 100.00 173 100.00 100.00 3.08e-123 PDB 1UEA "Mmp-3TIMP-1 Complex" 100.00 173 98.84 98.84 3.91e-121 PDB 1UMS "Stromelysin-1 Catalytic Domain With Hydrophobic Inhibitor Bound, Ph 7.0, 32oc, 20 Mm Cacl2, 15% Acetonitrile; Nmr Ensemble Of 2" 100.00 174 100.00 100.00 4.33e-123 PDB 1UMT "Stromelysin-1 Catalytic Domain With Hydrophobic Inhibitor Bound, Ph 7.0, 32oc, 20 Mm Cacl2, 15% Acetonitrile; Nmr Average Of 20" 100.00 174 100.00 100.00 4.33e-123 PDB 1USN "Crystal Structure Of The Catalytic Domain Of Human Fibroblast Stromelysin-1 Inhibited With Thiadiazole Inhibitor Pnu-142372" 95.38 165 100.00 100.00 3.48e-117 PDB 2D1O "Stromelysin-1 (Mmp-3) Complexed To A Hydroxamic Acid Inhibitor" 98.84 171 100.00 100.00 7.90e-122 PDB 2JNP "Solution Structure Of Matrix Metalloproteinase 3 (Mmp-3) In The Presence Of N-Isobutyl-N-[4- Methoxyphenylsulfonyl]glycyl Hydro" 93.06 161 100.00 100.00 8.56e-114 PDB 2JT5 "Solution Structure Of Matrix Metalloproteinase 3 (mmp-3) In The Presence Of N-hydroxy-2-[n-(2-hydroxyethyl)biphenyl-4- Sulfonam" 93.06 161 100.00 100.00 8.56e-114 PDB 2JT6 "Solution Structure Of Matrix Metalloproteinase 3 (Mmp-3) In The Presence Of 3-4'-Cyanobyphenyl-4-Yloxy)-N- Hdydroxypropionamide" 93.06 161 100.00 100.00 8.56e-114 PDB 2SRT "Catalytic Domain Of Human Stromelysin-1 At Ph 5.5 And 40oc Complexed With Inhibitor" 100.00 173 100.00 100.00 3.08e-123 PDB 2USN "Crystal Structure Of The Catalytic Domain Of Human Fibroblast Stromelysin-1 Inhibited With Thiadiazole Inhibitor Pnu-141803" 95.38 165 100.00 100.00 3.48e-117 PDB 3OHL "Catalytic Domain Of Stromelysin-1 In Complex With N-Hydroxy-2-(4- Methoxy-N-(Pyridine-3-Ylmethyl)phenylsulfonamido)acetamide" 96.53 167 100.00 100.00 8.03e-119 PDB 3OHO "Catalytic Domain Of Stromelysin-1 In Complex With N-Hydroxy-2-(4- Methylphenylsulfonamido)acetamide" 97.69 169 100.00 100.00 2.63e-120 PDB 3USN "Structure Of The Catalytic Domain Of Human Fibroblast Stromelysin-1 Inhibited With The Thiadiazole Inhibitor Ipnu-107859, Nmr, " 97.11 168 100.00 100.00 1.17e-119 PDB 4DPE "Structure Of Mmp3 Complexed With A Platinum-based Inhibitor." 100.00 173 100.00 100.00 3.08e-123 PDB 4G9L "Structure Of Mmp3 Complexed With Nngh Inhibitor" 100.00 173 100.00 100.00 3.08e-123 PDB 4JA1 "Structure Of Mmp3 Complexed With A Platinum-based Inhibitor" 100.00 173 100.00 100.00 3.08e-123 DBJ BAD97003 "matrix metalloproteinase 3 preproprotein variant [Homo sapiens]" 100.00 477 100.00 100.00 4.35e-120 DBJ BAD97011 "matrix metalloproteinase 3 preproprotein variant [Homo sapiens]" 100.00 477 100.00 100.00 4.35e-120 DBJ BAG36115 "unnamed protein product [Homo sapiens]" 100.00 477 100.00 100.00 3.50e-120 EMBL CAA28859 "preprostromelysin [Homo sapiens]" 100.00 477 100.00 100.00 3.50e-120 GB AAA00036 "prostromelysin=matrix metalloproteinase [human, Peptide, 477 aa]" 100.00 477 100.00 100.00 4.35e-120 GB AAA36321 "matrix metalloproteinase-3 [Homo sapiens]" 100.00 477 100.00 100.00 4.35e-120 GB AAB36942 "stromelysin [Homo sapiens]" 100.00 477 100.00 100.00 4.35e-120 GB AAD45887 "stromelysin catalytic domain [synthetic construct]" 100.00 174 100.00 100.00 4.33e-123 GB AAH69676 "Matrix metallopeptidase 3 (stromelysin 1, progelatinase) [Homo sapiens]" 100.00 477 100.00 100.00 4.35e-120 REF NP_002413 "stromelysin-1 preproprotein [Homo sapiens]" 100.00 477 100.00 100.00 3.50e-120 REF XP_002822450 "PREDICTED: stromelysin-1 [Pongo abelii]" 100.00 477 98.84 100.00 1.37e-119 REF XP_003253099 "PREDICTED: stromelysin-1 [Nomascus leucogenys]" 100.00 477 99.42 100.00 2.67e-120 REF XP_003828425 "PREDICTED: stromelysin-1 [Pan paniscus]" 100.00 477 100.00 100.00 2.10e-120 REF XP_004052086 "PREDICTED: stromelysin-1 [Gorilla gorilla gorilla]" 100.00 477 98.84 99.42 1.07e-118 SP P08254 "RecName: Full=Stromelysin-1; Short=SL-1; AltName: Full=Matrix metalloproteinase-3; Short=MMP-3; AltName: Full=Transin-1; Flags:" 100.00 477 100.00 100.00 3.50e-120 stop_ save_ ############# # Ligands # ############# save_HAI _Saveframe_category ligand _Mol_type "non-polymer (NON-POLYMER)" _Name_common 'CYCLOHEXYLAMMONIUM ION' _BMRB_code HAI _PDB_code HAI _Molecular_mass 100.182 _Mol_charge 1 _Mol_paramagnetic . _Mol_aromatic no _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons C1 C1 C . 0 . ? C2 C2 C . 0 . ? C3 C3 C . 0 . ? C4 C4 C . 0 . ? C5 C5 C . 0 . ? C6 C6 C . 0 . ? N N N . 1 . ? H1 H1 H . 0 . ? H21 H21 H . 0 . ? H22 H22 H . 0 . ? H31 H31 H . 0 . ? H32 H32 H . 0 . ? H41 H41 H . 0 . ? H42 H42 H . 0 . ? H51 H51 H . 0 . ? H52 H52 H . 0 . ? H61 H61 H . 0 . ? H62 H62 H . 0 . ? HN1 HN1 H . 0 . ? HN2 HN2 H . 0 . ? HN3 HN3 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 SING C1 C2 ? ? SING C1 C6 ? ? SING C1 N ? ? SING C1 H1 ? ? SING C2 C3 ? ? SING C2 H21 ? ? SING C2 H22 ? ? SING C3 C4 ? ? SING C3 H31 ? ? SING C3 H32 ? ? SING C4 C5 ? ? SING C4 H41 ? ? SING C4 H42 ? ? SING C5 C6 ? ? SING C5 H51 ? ? SING C5 H52 ? ? SING C6 H61 ? ? SING C6 H62 ? ? SING N HN1 ? ? SING N HN2 ? ? SING N HN3 ? ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ save_ZN _Saveframe_category ligand _Mol_type "non-polymer (NON-POLYMER)" _Name_common 'ZINC ION' _BMRB_code ZN _PDB_code ZN _Molecular_mass 65.409 _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 ZN ZN ZN . 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 _Strain $SLN 'E. coli' 562 Eubacteria . Escherichia coli BL21(DE3) 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 $SLN 'recombinant technology' E.coli Escherichia coli BL21(DE3) . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $SLN . mM . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_one _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H,15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H,15N HSQC' _Sample_label $sample_one save_ save_1H,13C,HMQC_2 _Saveframe_category NMR_applied_experiment _Experiment_name 1H,13C,HMQC _Sample_label $sample_one save_ save_3D_CBCA(CO)NH_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_one save_ save_3D_HNCA_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_one save_ save_3D_HNHA_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNHA' _Sample_label $sample_one save_ save_3D_HCCH-TOCSY_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HCCH-TOCSY' _Sample_label $sample_one save_ save_13C-FILTERED_COSY_7 _Saveframe_category NMR_applied_experiment _Experiment_name '13C-FILTERED COSY' _Sample_label $sample_one save_ save_13C,15N_FILTERED_NOESY_8 _Saveframe_category NMR_applied_experiment _Experiment_name '13C,15N FILTERED NOESY' _Sample_label $sample_one save_ save_3D_15N_EDITED_NOESY_9 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N EDITED NOESY' _Sample_label $sample_one save_ save_3D_13C_EDITED_NOESY_10 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 13C EDITED NOESY' _Sample_label $sample_one save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H,15N HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name 1H,13C,HMQC _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNHA' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HCCH-TOCSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name '13C-FILTERED COSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_8 _Saveframe_category NMR_applied_experiment _Experiment_name '13C,15N FILTERED NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_9 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N EDITED NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_10 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 13C EDITED NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_sample_conditions_one _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.8 0.2 n/a temperature 310 1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_one _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio_citation_label _Correction_value_citation_label . H 1 . . . . . . . . $entry_citation $entry_citation . N 15 . . . . . . . . $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_one stop_ _Sample_conditions_label $sample_conditions_one _Chem_shift_reference_set_label $chemical_shift_reference_one _Mol_system_component_name STROMELYSIN-1 _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 . 2 ARG HA H 4.87 . 1 2 . 2 ARG HB2 H 1.98 . 1 3 . 2 ARG HB3 H 1.98 . 1 4 . 2 ARG HG2 H 1.80 . 2 5 . 2 ARG HG3 H 1.68 . 2 6 . 2 ARG HD2 H 3.39 . 1 7 . 2 ARG HD3 H 3.39 . 1 8 . 3 THR H H 8.44 . 1 9 . 3 THR HA H 4.83 . 1 10 . 3 THR HB H 5.09 . 1 11 . 3 THR HG2 H 1.36 . 1 12 . 3 THR N N 112.50 . 1 13 . 4 PHE H H 7.62 . 1 14 . 4 PHE N N 118.50 . 1 15 . 5 PRO HA H 4.22 . 1 16 . 5 PRO HB2 H 2.65 . 1 17 . 5 PRO HB3 H 2.14 . 1 18 . 6 GLY H H 8.42 . 1 19 . 6 GLY HA2 H 3.65 . 2 20 . 6 GLY HA3 H 4.18 . 2 21 . 6 GLY N N 112.90 . 1 22 . 7 ILE H H 8.43 . 1 23 . 7 ILE HA H 3.88 . 1 24 . 7 ILE HB H 2.11 . 1 25 . 7 ILE HG12 H 1.38 . 4 26 . 7 ILE HG13 H 1.08 . 4 27 . 7 ILE HG2 H 0.88 . 4 28 . 7 ILE HD1 H 0.90 . 1 29 . 7 ILE N N 118.70 . 1 30 . 8 PRO HA H 4.42 . 1 31 . 8 PRO HB2 H 1.96 . 1 32 . 9 LYS H H 7.39 . 1 33 . 9 LYS HA H 4.53 . 1 34 . 9 LYS HB2 H 1.72 . 2 35 . 9 LYS HB3 H 1.83 . 2 36 . 9 LYS HG2 H 1.49 . 2 37 . 9 LYS HG3 H 1.15 . 2 38 . 9 LYS HD2 H 1.72 . 1 39 . 9 LYS HD3 H 1.72 . 1 40 . 9 LYS HE2 H 2.94 . 1 41 . 9 LYS HE3 H 2.94 . 1 42 . 9 LYS N N 114.30 . 1 43 . 10 TRP H H 8.26 . 1 44 . 10 TRP HA H 4.46 . 1 45 . 10 TRP HB2 H 3.51 . 2 46 . 10 TRP HB3 H 3.26 . 2 47 . 10 TRP HD1 H 7.45 . 1 48 . 10 TRP HZ2 H 7.46 . 1 49 . 10 TRP N N 123.80 . 1 50 . 11 ARG H H 9.20 . 1 51 . 11 ARG HA H 4.63 . 1 52 . 11 ARG HB2 H 2.22 . 2 53 . 11 ARG HB3 H 1.88 . 2 54 . 11 ARG HG2 H 1.86 . 2 55 . 11 ARG HG3 H 1.74 . 2 56 . 11 ARG HD2 H 3.28 . 1 57 . 11 ARG HD3 H 3.28 . 1 58 . 11 ARG N N 122.70 . 1 59 . 12 LYS H H 7.60 . 1 60 . 12 LYS HA H 4.80 . 1 61 . 12 LYS HB2 H 2.02 . 1 62 . 12 LYS HB3 H 2.02 . 1 63 . 12 LYS HG2 H 1.44 . 2 64 . 12 LYS HG3 H 1.23 . 2 65 . 12 LYS HD2 H 1.83 . 2 66 . 12 LYS HD3 H 1.74 . 2 67 . 12 LYS HE2 H 2.99 . 1 68 . 12 LYS HE3 H 2.99 . 1 69 . 12 LYS N N 117.10 . 1 70 . 13 THR H H 8.08 . 1 71 . 13 THR HA H 4.38 . 1 72 . 13 THR HB H 4.41 . 1 73 . 13 THR HG2 H 1.17 . 1 74 . 13 THR N N 105.20 . 1 75 . 14 HIS H H 7.06 . 1 76 . 14 HIS HA H 5.17 . 1 77 . 14 HIS HB2 H 3.05 . 2 78 . 14 HIS HB3 H 2.78 . 2 79 . 14 HIS N N 120.50 . 1 80 . 15 LEU H H 8.31 . 1 81 . 15 LEU HA H 4.57 . 1 82 . 15 LEU HB2 H 1.32 . 2 83 . 15 LEU HB3 H 0.92 . 2 84 . 15 LEU HG H 0.80 . 1 85 . 15 LEU HD1 H -0.24 . 2 86 . 15 LEU HD2 H 0.01 . 2 87 . 15 LEU N N 128.60 . 1 88 . 16 THR H H 9.26 . 1 89 . 16 THR HA H 5.87 . 1 90 . 16 THR HB H 4.12 . 1 91 . 16 THR HG2 H 1.18 . 1 92 . 16 THR N N 110.58 . 1 93 . 17 TYR H H 8.66 . 1 94 . 17 TYR HA H 5.75 . 1 95 . 17 TYR HB2 H 2.69 . 2 96 . 17 TYR HB3 H 2.90 . 2 97 . 17 TYR N N 118.10 . 1 98 . 18 ARG H H 8.22 . 1 99 . 18 ARG HA H 4.39 . 1 100 . 18 ARG HB2 H 2.16 . 2 101 . 18 ARG HB3 H 2.20 . 2 102 . 18 ARG HG2 H 1.73 . 2 103 . 18 ARG HG3 H 1.66 . 2 104 . 18 ARG HD2 H 3.19 . 1 105 . 18 ARG HD3 H 3.19 . 1 106 . 18 ARG N N 119.90 . 1 107 . 19 ILE H H 8.40 . 1 108 . 19 ILE HA H 4.37 . 1 109 . 19 ILE HB H 1.69 . 1 110 . 19 ILE HD1 H 0.32 . 1 111 . 19 ILE N N 128.80 . 1 112 . 20 VAL H H 9.54 . 1 113 . 20 VAL HA H 3.44 . 1 114 . 20 VAL HB H 2.14 . 1 115 . 20 VAL HG1 H 1.07 . 2 116 . 20 VAL HG2 H 1.02 . 2 117 . 20 VAL N N 130.60 . 1 118 . 21 ASN H H 7.72 . 1 119 . 21 ASN HA H 4.77 . 1 120 . 21 ASN HB2 H 3.16 . 2 121 . 21 ASN HB3 H 3.03 . 2 122 . 21 ASN N N 116.30 . 1 123 . 22 TYR H H 8.16 . 1 124 . 22 TYR HA H 4.29 . 1 125 . 22 TYR HB2 H 2.89 . 2 126 . 22 TYR HB3 H 2.51 . 2 127 . 22 TYR N N 112.50 . 1 128 . 23 THR HA H 5.02 . 1 129 . 23 THR HB H 3.15 . 1 130 . 23 THR HG2 H 0.45 . 1 131 . 24 PRO HA H 4.69 . 1 132 . 24 PRO HB2 H 2.12 . 1 133 . 24 PRO HB3 H 2.12 . 1 134 . 25 ASP H H 8.91 . 1 135 . 25 ASP HA H 4.13 . 1 136 . 25 ASP HB2 H 3.30 . 2 137 . 25 ASP HB3 H 2.76 . 2 138 . 25 ASP N N 122.10 . 1 139 . 26 LEU H H 7.05 . 1 140 . 26 LEU HA H 4.92 . 1 141 . 26 LEU HB2 H 1.50 . 1 142 . 26 LEU HB3 H 1.50 . 1 143 . 26 LEU HG H 1.59 . 1 144 . 26 LEU HD1 H 1.02 . 2 145 . 26 LEU HD2 H 0.60 . 2 146 . 26 LEU N N 117.10 . 1 147 . 27 PRO HA H 4.57 . 1 148 . 27 PRO HB2 H 2.06 . 1 149 . 27 PRO HB3 H 2.48 . 1 150 . 28 LYS H H 8.68 . 1 151 . 28 LYS HA H 3.76 . 1 152 . 28 LYS HB2 H 1.47 . 2 153 . 28 LYS HB3 H 1.38 . 2 154 . 28 LYS HG2 H 1.08 . 2 155 . 28 LYS HG3 H 0.71 . 2 156 . 28 LYS HD2 H 1.29 . 2 157 . 28 LYS HD3 H 1.22 . 2 158 . 28 LYS HE2 H 2.75 . 2 159 . 28 LYS HE3 H 2.71 . 2 160 . 28 LYS N N 124.40 . 1 161 . 29 ASP H H 8.54 . 1 162 . 29 ASP HA H 4.40 . 1 163 . 29 ASP HB2 H 2.69 . 2 164 . 29 ASP HB3 H 2.72 . 2 165 . 29 ASP N N 113.80 . 1 166 . 30 ALA H H 7.39 . 1 167 . 30 ALA HA H 4.38 . 1 168 . 30 ALA HB H 1.63 . 1 169 . 30 ALA N N 123.10 . 1 170 . 31 VAL H H 7.60 . 1 171 . 31 VAL HA H 3.59 . 1 172 . 31 VAL HB H 2.61 . 1 173 . 31 VAL HG1 H 0.96 . 2 174 . 31 VAL HG2 H 0.92 . 2 175 . 31 VAL N N 122.60 . 1 176 . 32 ASP H H 8.62 . 1 177 . 32 ASP HA H 4.23 . 1 178 . 32 ASP HB2 H 2.85 . 2 179 . 32 ASP HB3 H 2.71 . 2 180 . 32 ASP N N 120.00 . 1 181 . 33 SER H H 8.08 . 1 182 . 33 SER HA H 4.29 . 1 183 . 33 SER HB2 H 4.06 . 2 184 . 33 SER HB3 H 3.97 . 2 185 . 33 SER N N 112.60 . 1 186 . 34 ALA H H 7.73 . 1 187 . 34 ALA HA H 4.26 . 1 188 . 34 ALA HB H 1.52 . 1 189 . 34 ALA N N 124.60 . 1 190 . 35 VAL H H 8.09 . 1 191 . 35 VAL HA H 3.32 . 1 192 . 35 VAL HB H 2.10 . 1 193 . 35 VAL HG1 H 0.79 . 2 194 . 35 VAL HG2 H 0.59 . 2 195 . 35 VAL N N 116.10 . 1 196 . 36 GLU H H 8.51 . 1 197 . 36 GLU HA H 3.76 . 1 198 . 36 GLU HB2 H 2.22 . 2 199 . 36 GLU HB3 H 2.08 . 2 200 . 36 GLU HG2 H 2.53 . 2 201 . 36 GLU HG3 H 2.24 . 2 202 . 36 GLU N N 118.40 . 1 203 . 37 LYS H H 8.34 . 1 204 . 37 LYS HA H 3.99 . 1 205 . 37 LYS HB2 H 1.87 . 2 206 . 37 LYS HB3 H 1.73 . 2 207 . 37 LYS HG2 H 1.56 . 2 208 . 37 LYS HG3 H 1.25 . 2 209 . 37 LYS HD2 H 1.36 . 2 210 . 37 LYS HD3 H 1.06 . 2 211 . 37 LYS HE2 H 2.57 . 2 212 . 37 LYS HE3 H 2.53 . 2 213 . 37 LYS N N 119.70 . 1 214 . 38 ALA H H 8.11 . 1 215 . 38 ALA HA H 4.10 . 1 216 . 38 ALA HB H 1.45 . 1 217 . 38 ALA N N 123.60 . 1 218 . 39 LEU H H 7.74 . 1 219 . 39 LEU HA H 3.75 . 1 220 . 39 LEU HB2 H 0.62 . 2 221 . 39 LEU HB3 H 1.45 . 2 222 . 39 LEU HG H 1.22 . 1 223 . 39 LEU HD1 H -0.47 . 2 224 . 39 LEU HD2 H -0.41 . 2 225 . 39 LEU N N 115.60 . 1 226 . 40 LYS H H 7.96 . 1 227 . 40 LYS HA H 4.18 . 1 228 . 40 LYS HB2 H 2.03 . 1 229 . 40 LYS HB3 H 2.03 . 1 230 . 40 LYS HG2 H 1.64 . 1 231 . 40 LYS HG3 H 1.64 . 1 232 . 40 LYS HD2 H 1.76 . 1 233 . 40 LYS HD3 H 1.76 . 1 234 . 40 LYS HE2 H 3.04 . 1 235 . 40 LYS HE3 H 3.04 . 1 236 . 40 LYS N N 119.50 . 1 237 . 41 VAL H H 7.57 . 1 238 . 41 VAL HA H 3.89 . 1 239 . 41 VAL HB H 2.10 . 1 240 . 41 VAL HG1 H 0.92 . 2 241 . 41 VAL HG2 H 0.74 . 2 242 . 41 VAL N N 114.30 . 1 243 . 42 TRP H H 6.76 . 1 244 . 42 TRP HA H 4.73 . 1 245 . 42 TRP HB2 H 3.16 . 1 246 . 42 TRP HB3 H 3.16 . 1 247 . 42 TRP HD1 H 7.51 . 1 248 . 42 TRP HZ2 H 7.37 . 1 249 . 42 TRP N N 118.10 . 1 250 . 43 GLU H H 8.62 . 1 251 . 43 GLU HA H 4.01 . 1 252 . 43 GLU HB2 H 2.38 . 1 253 . 43 GLU HB3 H 2.38 . 1 254 . 43 GLU HG2 H 2.88 . 2 255 . 43 GLU HG3 H 2.46 . 2 256 . 43 GLU N N 123.30 . 1 257 . 44 GLU H H 7.89 . 1 258 . 44 GLU HA H 4.22 . 1 259 . 44 GLU HB2 H 2.22 . 2 260 . 44 GLU HB3 H 2.10 . 2 261 . 44 GLU HG2 H 2.66 . 2 262 . 44 GLU HG3 H 2.45 . 2 263 . 44 GLU N N 111.70 . 1 264 . 45 VAL H H 7.13 . 1 265 . 45 VAL HA H 4.76 . 1 266 . 45 VAL HB H 2.70 . 1 267 . 45 VAL HG1 H 1.21 . 2 268 . 45 VAL HG2 H 0.98 . 2 269 . 45 VAL N N 104.90 . 1 270 . 46 THR H H 7.69 . 1 271 . 46 THR HA H 5.58 . 1 272 . 46 THR HB H 4.28 . 1 273 . 46 THR HG2 H 1.58 . 1 274 . 46 THR N N 111.40 . 1 275 . 47 PRO HA H 5.04 . 1 276 . 47 PRO HB2 H 2.15 . 1 277 . 47 PRO HB3 H 2.15 . 1 278 . 48 LEU H H 7.37 . 1 279 . 48 LEU HA H 4.57 . 1 280 . 48 LEU HB2 H 1.42 . 2 281 . 48 LEU HB3 H 0.58 . 2 282 . 48 LEU HG H 1.18 . 1 283 . 48 LEU HD1 H 0.32 . 2 284 . 48 LEU HD2 H 0.39 . 2 285 . 48 LEU N N 118.10 . 1 286 . 49 THR H H 8.19 . 1 287 . 49 THR HA H 4.62 . 1 288 . 49 THR HB H 4.14 . 1 289 . 49 THR HG2 H 1.11 . 1 290 . 49 THR N N 110.70 . 1 291 . 50 PHE H H 8.30 . 1 292 . 50 PHE HA H 5.80 . 1 293 . 50 PHE HB2 H 2.86 . 1 294 . 50 PHE HB3 H 2.86 . 1 295 . 50 PHE HD1 H 7.11 . 1 296 . 50 PHE HD2 H 7.11 . 1 297 . 50 PHE HE1 H 6.92 . 1 298 . 50 PHE HE2 H 6.92 . 1 299 . 50 PHE N N 117.90 . 1 300 . 51 SER H H 8.77 . 1 301 . 51 SER HA H 4.95 . 1 302 . 51 SER HB2 H 3.92 . 2 303 . 51 SER HB3 H 3.76 . 2 304 . 51 SER N N 117.00 . 1 305 . 52 ARG H H 8.52 . 1 306 . 52 ARG HA H 3.60 . 1 307 . 52 ARG HB2 H 1.20 . 1 308 . 52 ARG HB3 H 1.20 . 1 309 . 52 ARG HD2 H 2.87 . 2 310 . 52 ARG HD3 H 2.77 . 2 311 . 52 ARG N N 125.80 . 1 312 . 53 LEU H H 8.63 . 1 313 . 53 LEU HA H 4.71 . 1 314 . 53 LEU HB2 H 1.71 . 2 315 . 53 LEU HB3 H 1.25 . 2 316 . 53 LEU HG H 1.55 . 1 317 . 53 LEU HD1 H 0.93 . 2 318 . 53 LEU HD2 H 0.84 . 2 319 . 53 LEU N N 124.90 . 1 320 . 54 TYR H H 9.24 . 1 321 . 54 TYR HA H 4.46 . 1 322 . 54 TYR HB2 H 3.32 . 2 323 . 54 TYR HB3 H 2.72 . 2 324 . 54 TYR HD1 H 7.23 . 1 325 . 54 TYR HD2 H 7.23 . 1 326 . 54 TYR HE1 H 6.84 . 1 327 . 54 TYR HE2 H 6.84 . 1 328 . 54 TYR N N 119.00 . 1 329 . 55 GLU H H 7.53 . 1 330 . 55 GLU HA H 4.44 . 1 331 . 55 GLU HB2 H 2.11 . 2 332 . 55 GLU HB3 H 1.97 . 2 333 . 55 GLU HG2 H 2.23 . 2 334 . 55 GLU HG3 H 2.14 . 2 335 . 55 GLU N N 117.10 . 1 336 . 56 GLY H H 8.52 . 1 337 . 56 GLY HA2 H 4.14 . 2 338 . 56 GLY HA3 H 3.83 . 2 339 . 56 GLY N N 108.30 . 1 340 . 57 GLU H H 8.22 . 1 341 . 57 GLU HA H 4.38 . 1 342 . 57 GLU HB2 H 1.90 . 2 343 . 57 GLU HB3 H 1.91 . 2 344 . 57 GLU HG2 H 2.19 . 1 345 . 57 GLU HG3 H 2.19 . 1 346 . 57 GLU N N 119.50 . 1 347 . 58 ALA H H 8.06 . 1 348 . 58 ALA HA H 4.49 . 1 349 . 58 ALA HB H 0.95 . 1 350 . 58 ALA N N 132.10 . 1 351 . 59 ASP H H 8.35 . 1 352 . 59 ASP HA H 4.57 . 1 353 . 59 ASP HB2 H 2.46 . 2 354 . 59 ASP HB3 H 2.34 . 2 355 . 59 ASP N N 122.60 . 1 356 . 60 ILE H H 8.67 . 1 357 . 60 ILE HA H 4.30 . 1 358 . 60 ILE HB H 1.91 . 1 359 . 60 ILE HD1 H 0.83 . 1 360 . 60 ILE N N 124.40 . 1 361 . 61 MET H H 7.31 . 1 362 . 61 MET HA H 5.01 . 1 363 . 61 MET HB2 H 2.22 . 1 364 . 61 MET HB3 H 2.22 . 1 365 . 61 MET HE H 2.27 . 1 366 . 61 MET N N 127.10 . 1 367 . 62 ILE H H 9.24 . 1 368 . 62 ILE HA H 5.42 . 1 369 . 62 ILE HB H 1.95 . 1 370 . 62 ILE HG12 H 1.76 . 2 371 . 62 ILE HG13 H 0.98 . 2 372 . 62 ILE HG2 H 0.75 . 1 373 . 62 ILE HD1 H 0.82 . 1 374 . 62 ILE N N 129.00 . 1 375 . 63 SER H H 8.67 . 1 376 . 63 SER HA H 5.08 . 1 377 . 63 SER HB2 H 3.78 . 2 378 . 63 SER HB3 H 3.07 . 2 379 . 63 SER N N 118.90 . 1 380 . 64 PHE H H 9.50 . 1 381 . 64 PHE HA H 5.32 . 1 382 . 64 PHE HB2 H 2.85 . 2 383 . 64 PHE HB3 H 2.66 . 2 384 . 64 PHE N N 121.00 . 1 385 . 65 ALA H H 9.38 . 1 386 . 65 ALA HA H 4.97 . 1 387 . 65 ALA HB H 1.09 . 1 388 . 65 ALA N N 126.30 . 1 389 . 66 VAL H H 8.24 . 1 390 . 66 VAL HA H 5.01 . 1 391 . 66 VAL HB H 2.24 . 1 392 . 66 VAL HG1 H 0.93 . 2 393 . 66 VAL HG2 H 0.90 . 2 394 . 66 VAL N N 111.90 . 1 395 . 67 ARG H H 9.65 . 1 396 . 67 ARG HA H 3.85 . 1 397 . 67 ARG HB2 H 2.23 . 1 398 . 67 ARG HB3 H 2.23 . 1 399 . 67 ARG HG2 H 1.85 . 2 400 . 67 ARG HG3 H 1.72 . 2 401 . 67 ARG HD2 H 3.28 . 1 402 . 67 ARG HD3 H 3.28 . 1 403 . 67 ARG N N 117.90 . 1 404 . 68 GLU HA H 4.32 . 1 405 . 68 GLU HG2 H 2.43 . 2 406 . 68 GLU HG3 H 2.30 . 2 407 . 69 HIS H H 9.21 . 1 408 . 69 HIS HA H 5.17 . 1 409 . 69 HIS N N 121.50 . 1 410 . 70 GLY H H 8.49 . 1 411 . 70 GLY HA2 H 4.20 . 2 412 . 70 GLY HA3 H 3.58 . 2 413 . 70 GLY N N 110.30 . 1 414 . 71 ASP H H 6.99 . 1 415 . 71 ASP HA H 4.53 . 1 416 . 71 ASP N N 117.40 . 1 417 . 72 PHE H H 8.31 . 1 418 . 72 PHE HA H 4.24 . 1 419 . 72 PHE N N 117.20 . 1 420 . 73 TYR H H 6.91 . 1 421 . 73 TYR HA H 4.91 . 1 422 . 73 TYR N N 117.20 . 1 423 . 75 PHE H H 8.27 . 1 424 . 75 PHE HA H 5.00 . 1 425 . 75 PHE HB2 H 3.89 . 2 426 . 75 PHE HB3 H 3.05 . 2 427 . 75 PHE N N 121.10 . 1 428 . 76 ASP H H 8.18 . 1 429 . 76 ASP HA H 4.77 . 1 430 . 76 ASP HB2 H 3.23 . 2 431 . 76 ASP HB3 H 2.63 . 2 432 . 76 ASP N N 117.60 . 1 433 . 77 GLY H H 8.99 . 1 434 . 77 GLY HA2 H 4.41 . 1 435 . 77 GLY HA3 H 4.41 . 1 436 . 77 GLY N N 110.40 . 1 437 . 78 PRO HA H 3.92 . 1 438 . 79 GLY H H 11.03 . 1 439 . 79 GLY HA2 H 4.10 . 2 440 . 79 GLY HA3 H 3.49 . 2 441 . 79 GLY N N 119.50 . 1 442 . 80 ASN HA H 4.10 . 1 443 . 80 ASN HB2 H 3.45 . 2 444 . 80 ASN HB3 H 3.26 . 2 445 . 81 VAL H H 10.23 . 1 446 . 81 VAL HA H 4.06 . 1 447 . 81 VAL HB H 2.48 . 1 448 . 81 VAL HG1 H 1.29 . 2 449 . 81 VAL HG2 H 1.08 . 2 450 . 81 VAL N N 126.90 . 1 451 . 82 LEU H H 8.30 . 1 452 . 82 LEU HA H 4.57 . 1 453 . 82 LEU HB2 H 1.41 . 1 454 . 82 LEU HB3 H 1.41 . 1 455 . 82 LEU HG H 1.88 . 1 456 . 82 LEU HD1 H 0.33 . 2 457 . 82 LEU HD2 H 0.03 . 2 458 . 82 LEU N N 127.60 . 1 459 . 83 ALA H H 7.48 . 1 460 . 83 ALA HA H 4.73 . 1 461 . 83 ALA HB H 1.15 . 1 462 . 83 ALA N N 114.20 . 1 463 . 84 HIS H H 9.27 . 1 464 . 84 HIS HA H 4.09 . 1 465 . 84 HIS HB2 H 3.01 . 2 466 . 84 HIS HB3 H 3.43 . 2 467 . 84 HIS N N 117.10 . 1 468 . 85 ALA H H 8.59 . 1 469 . 85 ALA HA H 5.10 . 1 470 . 85 ALA HB H 1.54 . 1 471 . 85 ALA N N 121.60 . 1 472 . 86 TYR H H 8.05 . 1 473 . 86 TYR HA H 4.25 . 1 474 . 86 TYR HB2 H 2.91 . 1 475 . 86 TYR HB3 H 2.91 . 1 476 . 86 TYR HD1 H 6.92 . 1 477 . 86 TYR HD2 H 6.92 . 1 478 . 86 TYR HE1 H 6.26 . 1 479 . 86 TYR HE2 H 6.26 . 1 480 . 86 TYR N N 119.20 . 1 481 . 87 ALA HA H 4.00 . 1 482 . 87 ALA HB H 0.04 . 1 483 . 88 PRO HA H 3.08 . 1 484 . 89 GLY H H 5.55 . 1 485 . 89 GLY HA2 H 3.48 . 1 486 . 89 GLY HA3 H 3.48 . 1 487 . 89 GLY N N 108.00 . 1 488 . 90 PRO HA H 4.79 . 1 489 . 91 GLY H H 8.81 . 1 490 . 91 GLY HA2 H 4.06 . 2 491 . 91 GLY HA3 H 3.91 . 2 492 . 91 GLY N N 109.90 . 1 493 . 92 ILE H H 8.93 . 1 494 . 92 ILE HA H 4.26 . 1 495 . 92 ILE HB H 1.59 . 1 496 . 92 ILE N N 132.90 . 1 497 . 93 ASN H H 7.22 . 1 498 . 93 ASN HA H 4.20 . 1 499 . 93 ASN HB2 H 2.64 . 2 500 . 93 ASN HB3 H 2.43 . 2 501 . 93 ASN N N 118.70 . 1 502 . 94 GLY H H 7.75 . 1 503 . 94 GLY HA2 H 4.61 . 2 504 . 94 GLY HA3 H 4.11 . 2 505 . 94 GLY N N 119.50 . 1 506 . 95 ASP H H 7.98 . 1 507 . 95 ASP HA H 4.81 . 1 508 . 95 ASP HB2 H 3.16 . 2 509 . 95 ASP HB3 H 2.93 . 2 510 . 95 ASP N N 122.00 . 1 511 . 96 ALA H H 8.21 . 1 512 . 96 ALA HA H 4.98 . 1 513 . 96 ALA HB H 1.14 . 1 514 . 96 ALA N N 118.50 . 1 515 . 97 HIS H H 9.34 . 1 516 . 97 HIS HA H 5.78 . 1 517 . 97 HIS HB2 H 3.22 . 2 518 . 97 HIS HB3 H 2.67 . 2 519 . 97 HIS N N 121.00 . 1 520 . 98 PHE H H 8.90 . 1 521 . 98 PHE HA H 4.34 . 1 522 . 98 PHE HB2 H 1.91 . 1 523 . 98 PHE HB3 H 1.91 . 1 524 . 98 PHE HD1 H 6.66 . 1 525 . 98 PHE HD2 H 6.66 . 1 526 . 98 PHE HE1 H 6.37 . 1 527 . 98 PHE HE2 H 6.37 . 1 528 . 98 PHE N N 123.00 . 1 529 . 99 ASP H H 8.15 . 1 530 . 99 ASP HA H 4.42 . 1 531 . 99 ASP HB2 H 3.08 . 2 532 . 99 ASP HB3 H 0.65 . 2 533 . 99 ASP N N 123.60 . 1 534 . 100 ASP H H 9.95 . 1 535 . 100 ASP HA H 5.59 . 1 536 . 100 ASP HB2 H 2.93 . 2 537 . 100 ASP HB3 H 2.50 . 2 538 . 100 ASP N N 129.10 . 1 539 . 101 ASP H H 9.37 . 1 540 . 101 ASP HA H 5.05 . 1 541 . 101 ASP HB2 H 2.67 . 1 542 . 101 ASP HB3 H 2.67 . 1 543 . 101 ASP N N 124.70 . 1 544 . 102 GLU H H 7.30 . 1 545 . 102 GLU HA H 4.54 . 1 546 . 102 GLU N N 116.10 . 1 547 . 103 GLN H H 8.41 . 1 548 . 103 GLN HA H 4.42 . 1 549 . 103 GLN HB2 H 1.96 . 2 550 . 103 GLN HB3 H 1.73 . 2 551 . 103 GLN HG2 H 2.22 . 2 552 . 103 GLN HG3 H 2.13 . 2 553 . 103 GLN N N 127.20 . 1 554 . 104 TRP H H 9.63 . 1 555 . 104 TRP HA H 5.16 . 1 556 . 104 TRP HB2 H 3.10 . 1 557 . 104 TRP HB3 H 3.10 . 1 558 . 104 TRP HD1 H 7.56 . 1 559 . 104 TRP HZ2 H 7.98 . 1 560 . 104 TRP N N 132.00 . 1 561 . 105 THR H H 8.81 . 1 562 . 105 THR HA H 4.97 . 1 563 . 105 THR HB H 4.54 . 1 564 . 105 THR HG2 H 1.07 . 1 565 . 105 THR N N 111.20 . 1 566 . 106 LYS H H 9.08 . 1 567 . 106 LYS HA H 4.61 . 1 568 . 106 LYS HB2 H 1.99 . 2 569 . 106 LYS HB3 H 1.83 . 2 570 . 106 LYS HG2 H 1.54 . 1 571 . 106 LYS HG3 H 1.54 . 1 572 . 106 LYS HD2 H 1.76 . 2 573 . 106 LYS HD3 H 1.65 . 2 574 . 106 LYS HE2 H 3.02 . 1 575 . 106 LYS HE3 H 3.02 . 1 576 . 106 LYS N N 120.20 . 1 577 . 107 ASP H H 7.57 . 1 578 . 107 ASP HA H 4.96 . 1 579 . 107 ASP HB2 H 3.49 . 2 580 . 107 ASP HB3 H 2.76 . 2 581 . 107 ASP N N 121.10 . 1 582 . 108 THR HA H 4.69 . 1 583 . 108 THR HB H 4.97 . 1 584 . 108 THR HG2 H 1.32 . 1 585 . 109 THR H H 8.30 . 1 586 . 109 THR HA H 4.26 . 1 587 . 109 THR HB H 4.23 . 1 588 . 109 THR HG2 H 1.32 . 1 589 . 109 THR N N 115.60 . 1 590 . 110 GLY H H 7.38 . 1 591 . 110 GLY HA2 H 4.30 . 2 592 . 110 GLY HA3 H 3.55 . 2 593 . 110 GLY N N 112.20 . 1 594 . 111 THR H H 8.55 . 1 595 . 111 THR HA H 3.76 . 1 596 . 111 THR HB H 2.81 . 1 597 . 111 THR HG2 H 0.28 . 1 598 . 111 THR N N 124.10 . 1 599 . 112 ASN H H 8.49 . 1 600 . 112 ASN HA H 4.85 . 1 601 . 112 ASN HB2 H 2.92 . 2 602 . 112 ASN HB3 H 2.64 . 2 603 . 112 ASN N N 127.50 . 1 604 . 113 LEU H H 8.14 . 1 605 . 113 LEU HA H 4.63 . 1 606 . 113 LEU HB2 H 1.87 . 2 607 . 113 LEU HB3 H 1.52 . 2 608 . 113 LEU HG H 1.18 . 1 609 . 113 LEU HD1 H 0.74 . 2 610 . 113 LEU HD2 H -0.06 . 2 611 . 113 LEU N N 128.80 . 1 612 . 114 PHE H H 8.44 . 1 613 . 114 PHE HA H 4.08 . 1 614 . 114 PHE HB2 H 3.44 . 2 615 . 114 PHE HB3 H 3.28 . 2 616 . 114 PHE N N 119.50 . 1 617 . 115 LEU H H 8.76 . 1 618 . 115 LEU HA H 3.18 . 1 619 . 115 LEU HB2 H 1.73 . 2 620 . 115 LEU HB3 H 1.60 . 2 621 . 115 LEU HG H 1.76 . 1 622 . 115 LEU HD1 H 0.88 . 2 623 . 115 LEU HD2 H 0.66 . 2 624 . 115 LEU N N 120.20 . 1 625 . 116 VAL H H 7.36 . 1 626 . 116 VAL HA H 4.11 . 1 627 . 116 VAL HB H 2.38 . 1 628 . 116 VAL HG1 H 1.23 . 2 629 . 116 VAL HG2 H 0.95 . 2 630 . 116 VAL N N 115.10 . 1 631 . 117 ALA H H 9.59 . 1 632 . 117 ALA HA H 4.18 . 1 633 . 117 ALA HB H 1.25 . 1 634 . 117 ALA N N 122.70 . 1 635 . 118 ALA H H 8.96 . 1 636 . 118 ALA HA H 4.07 . 1 637 . 118 ALA HB H 1.12 . 1 638 . 118 ALA N N 121.00 . 1 639 . 119 HIS H H 7.74 . 1 640 . 119 HIS HA H 4.57 . 1 641 . 119 HIS N N 119.90 . 1 642 . 120 GLU H H 9.30 . 1 643 . 120 GLU HA H 4.10 . 1 644 . 120 GLU HB2 H 2.08 . 1 645 . 120 GLU HB3 H 2.08 . 1 646 . 120 GLU N N 117.30 . 1 647 . 121 ILE H H 9.08 . 1 648 . 121 ILE HA H 3.88 . 1 649 . 121 ILE HB H 2.03 . 1 650 . 121 ILE HG12 H 1.61 . 2 651 . 121 ILE HG13 H 1.28 . 2 652 . 121 ILE HG2 H 0.65 . 1 653 . 121 ILE HD1 H 0.56 . 1 654 . 121 ILE N N 118.10 . 1 655 . 122 GLY H H 7.60 . 1 656 . 122 GLY HA2 H 4.08 . 2 657 . 122 GLY HA3 H 2.45 . 2 658 . 122 GLY N N 108.60 . 1 659 . 123 HIS H H 7.27 . 1 660 . 123 HIS HA H 5.71 . 1 661 . 123 HIS HB2 H 4.15 . 2 662 . 123 HIS HB3 H 2.75 . 2 663 . 123 HIS N N 120.00 . 1 664 . 124 SER H H 8.61 . 1 665 . 124 SER HA H 4.75 . 1 666 . 124 SER HB2 H 3.95 . 2 667 . 124 SER HB3 H 3.91 . 2 668 . 124 SER N N 118.70 . 1 669 . 125 LEU H H 7.81 . 1 670 . 125 LEU HA H 4.65 . 1 671 . 125 LEU HB2 H 1.68 . 1 672 . 125 LEU HB3 H 1.68 . 1 673 . 125 LEU HG H 1.95 . 1 674 . 125 LEU HD1 H 0.82 . 2 675 . 125 LEU HD2 H 0.39 . 2 676 . 125 LEU N N 114.00 . 1 677 . 126 GLY H H 8.61 . 1 678 . 126 GLY HA2 H 5.01 . 2 679 . 126 GLY HA3 H 3.55 . 2 680 . 126 GLY N N 108.30 . 1 681 . 127 LEU H H 8.95 . 1 682 . 127 LEU HA H 4.89 . 1 683 . 127 LEU HB2 H 1.53 . 1 684 . 127 LEU HB3 H 1.53 . 1 685 . 127 LEU HG H 1.46 . 1 686 . 127 LEU HD1 H 1.03 . 2 687 . 127 LEU HD2 H 0.69 . 2 688 . 127 LEU N N 121.60 . 1 689 . 128 PHE H H 8.90 . 1 690 . 128 PHE N N 124.90 . 1 691 . 129 HIS H H 5.30 . 1 692 . 129 HIS HA H 5.00 . 1 693 . 130 SER H H 6.65 . 1 694 . 130 SER HA H 4.52 . 1 695 . 130 SER HB2 H 4.23 . 2 696 . 130 SER HB3 H 4.17 . 2 697 . 130 SER N N 115.80 . 1 698 . 131 ALA H H 8.58 . 1 699 . 131 ALA HA H 4.67 . 1 700 . 131 ALA HB H 1.50 . 1 701 . 131 ALA N N 127.00 . 1 702 . 132 ASN H H 8.85 . 1 703 . 132 ASN HA H 4.69 . 1 704 . 132 ASN HB2 H 2.93 . 2 705 . 132 ASN HB3 H 2.57 . 2 706 . 132 ASN N N 121.20 . 1 707 . 133 THR H H 8.05 . 1 708 . 133 THR HA H 2.49 . 1 709 . 133 THR HB H 3.84 . 1 710 . 133 THR HG2 H 0.90 . 1 711 . 133 THR N N 117.10 . 1 712 . 134 GLU H H 8.95 . 1 713 . 134 GLU HA H 4.38 . 1 714 . 134 GLU HB2 H 2.14 . 2 715 . 134 GLU HB3 H 2.07 . 2 716 . 134 GLU N N 120.50 . 1 717 . 135 ALA H H 7.83 . 1 718 . 135 ALA HA H 4.63 . 1 719 . 135 ALA HB H 1.83 . 1 720 . 135 ALA N N 124.60 . 1 721 . 136 LEU H H 11.58 . 1 722 . 136 LEU HA H 4.59 . 1 723 . 136 LEU HB2 H 1.84 . 2 724 . 136 LEU HB3 H 2.00 . 2 725 . 136 LEU HG H 1.39 . 1 726 . 136 LEU HD1 H 0.97 . 1 727 . 136 LEU HD2 H 0.97 . 1 728 . 136 LEU N N 132.70 . 1 729 . 137 MET H H 8.05 . 1 730 . 137 MET HA H 4.61 . 1 731 . 137 MET HB2 H 2.69 . 1 732 . 137 MET HB3 H 2.69 . 1 733 . 137 MET HE H 0.62 . 1 734 . 137 MET N N 111.20 . 1 735 . 138 TYR H H 8.17 . 1 736 . 138 TYR HA H 4.80 . 1 737 . 138 TYR N N 128.80 . 1 738 . 139 PRO HA H 3.63 . 1 739 . 139 PRO HB2 H 1.60 . 2 740 . 139 PRO HB3 H 0.87 . 2 741 . 140 LEU H H 7.60 . 1 742 . 140 LEU HA H 4.65 . 1 743 . 140 LEU HB2 H 1.59 . 2 744 . 140 LEU HB3 H 1.40 . 2 745 . 140 LEU N N 122.30 . 1 746 . 141 TYR H H 9.07 . 1 747 . 141 TYR HA H 4.61 . 1 748 . 141 TYR HB2 H 2.92 . 2 749 . 141 TYR HB3 H 2.46 . 2 750 . 141 TYR N N 127.20 . 1 751 . 142 HIS H H 8.28 . 1 752 . 142 HIS HA H 4.83 . 1 753 . 142 HIS N N 128.50 . 1 754 . 143 SER H H 7.62 . 1 755 . 143 SER HA H 4.14 . 1 756 . 143 SER HB2 H 3.96 . 1 757 . 143 SER HB3 H 3.96 . 1 758 . 143 SER N N 118.40 . 1 759 . 144 LEU H H 7.76 . 1 760 . 144 LEU HA H 4.69 . 1 761 . 144 LEU HB2 H 1.51 . 1 762 . 144 LEU HB3 H 1.51 . 1 763 . 144 LEU N N 123.30 . 1 764 . 145 THR H H 8.01 . 1 765 . 145 THR HA H 4.23 . 1 766 . 145 THR HB H 4.08 . 1 767 . 145 THR HG2 H 1.25 . 1 768 . 145 THR N N 120.20 . 1 769 . 146 ASP H H 7.63 . 1 770 . 146 ASP HA H 4.85 . 1 771 . 146 ASP HB2 H 2.85 . 2 772 . 146 ASP HB3 H 2.65 . 2 773 . 146 ASP N N 122.40 . 1 774 . 147 LEU H H 8.87 . 1 775 . 147 LEU HA H 4.19 . 1 776 . 147 LEU HB2 H 1.79 . 2 777 . 147 LEU HB3 H 1.64 . 2 778 . 147 LEU HG H 1.81 . 1 779 . 147 LEU HD1 H 1.05 . 2 780 . 147 LEU HD2 H 0.97 . 2 781 . 147 LEU N N 126.80 . 1 782 . 148 THR H H 8.48 . 1 783 . 148 THR HA H 4.20 . 1 784 . 148 THR HB H 4.30 . 1 785 . 148 THR HG2 H 1.33 . 1 786 . 148 THR N N 111.90 . 1 787 . 149 ARG H H 7.48 . 1 788 . 149 ARG HA H 4.50 . 1 789 . 149 ARG HB2 H 2.06 . 2 790 . 149 ARG HB3 H 1.64 . 2 791 . 149 ARG HG2 H 1.66 . 2 792 . 149 ARG HG3 H 1.54 . 2 793 . 149 ARG HD2 H 3.19 . 1 794 . 149 ARG HD3 H 3.19 . 1 795 . 149 ARG N N 120.00 . 1 796 . 150 PHE H H 7.39 . 1 797 . 150 PHE HA H 4.27 . 1 798 . 150 PHE HB2 H 3.20 . 2 799 . 150 PHE HB3 H 2.96 . 2 800 . 150 PHE N N 121.40 . 1 801 . 151 ARG H H 7.08 . 1 802 . 151 ARG HA H 4.02 . 1 803 . 151 ARG HB2 H 1.74 . 2 804 . 151 ARG HB3 H 1.52 . 2 805 . 151 ARG HG2 H 1.52 . 2 806 . 151 ARG HG3 H 1.44 . 2 807 . 151 ARG HD2 H 3.15 . 1 808 . 151 ARG HD3 H 3.15 . 1 809 . 151 ARG N N 126.90 . 1 810 . 152 LEU H H 8.46 . 1 811 . 152 LEU HA H 3.91 . 1 812 . 152 LEU HB2 H 1.44 . 1 813 . 152 LEU HB3 H 1.44 . 1 814 . 152 LEU HG H 1.43 . 1 815 . 152 LEU HD1 H 0.21 . 2 816 . 152 LEU HD2 H 0.31 . 2 817 . 152 LEU N N 122.60 . 1 818 . 153 SER H H 8.34 . 1 819 . 153 SER HA H 4.57 . 1 820 . 153 SER HB2 H 4.14 . 2 821 . 153 SER HB3 H 4.30 . 2 822 . 153 SER N N 118.40 . 1 823 . 154 GLN H H 9.06 . 1 824 . 154 GLN HA H 3.95 . 1 825 . 154 GLN HB2 H 2.11 . 2 826 . 154 GLN HB3 H 2.18 . 2 827 . 154 GLN HG2 H 2.50 . 2 828 . 154 GLN HG3 H 2.23 . 2 829 . 154 GLN N N 122.50 . 1 830 . 155 ASP H H 8.25 . 1 831 . 155 ASP HA H 4.58 . 1 832 . 155 ASP HB2 H 2.86 . 2 833 . 155 ASP HB3 H 2.58 . 2 834 . 155 ASP N N 118.40 . 1 835 . 156 ASP H H 7.46 . 1 836 . 156 ASP HA H 4.73 . 1 837 . 156 ASP HB2 H 3.07 . 2 838 . 156 ASP HB3 H 2.93 . 2 839 . 156 ASP N N 116.80 . 1 840 . 157 ILE H H 7.97 . 1 841 . 157 ILE HA H 3.64 . 1 842 . 157 ILE HB H 1.75 . 1 843 . 157 ILE HD1 H 0.77 . 1 844 . 157 ILE N N 120.70 . 1 845 . 158 ASN H H 9.24 . 1 846 . 158 ASN HA H 4.38 . 1 847 . 158 ASN HB2 H 3.12 . 2 848 . 158 ASN HB3 H 2.89 . 2 849 . 158 ASN N N 119.00 . 1 850 . 159 GLY H H 8.20 . 1 851 . 159 GLY HA2 H 2.73 . 2 852 . 159 GLY HA3 H 1.41 . 2 853 . 159 GLY N N 109.10 . 1 854 . 160 ILE H H 8.76 . 1 855 . 160 ILE HA H 4.38 . 1 856 . 160 ILE HB H 2.22 . 1 857 . 160 ILE HD1 H 0.94 . 1 858 . 160 ILE N N 125.90 . 1 859 . 161 GLN H H 8.64 . 1 860 . 161 GLN HA H 4.26 . 1 861 . 161 GLN HG2 H 2.95 . 2 862 . 161 GLN HG3 H 2.85 . 2 863 . 161 GLN N N 122.60 . 1 864 . 162 SER H H 7.89 . 1 865 . 162 SER HA H 4.03 . 1 866 . 162 SER N N 119.70 . 1 867 . 163 LEU H H 6.76 . 1 868 . 163 LEU HA H 4.14 . 1 869 . 163 LEU HB2 H 1.76 . 2 870 . 163 LEU HB3 H 0.32 . 2 871 . 163 LEU HG H 1.60 . 1 872 . 163 LEU HD1 H 0.93 . 2 873 . 163 LEU HD2 H 0.74 . 2 874 . 163 LEU N N 120.80 . 1 875 . 164 TYR H H 7.50 . 1 876 . 164 TYR HA H 4.88 . 1 877 . 164 TYR HB2 H 3.48 . 2 878 . 164 TYR HB3 H 2.65 . 2 879 . 164 TYR N N 113.00 . 1 880 . 165 GLY H H 8.40 . 1 881 . 165 GLY HA2 H 4.45 . 2 882 . 165 GLY HA3 H 4.09 . 2 883 . 165 GLY N N 109.10 . 1 884 . 168 PRO HA H 4.46 . 1 885 . 168 PRO HB2 H 2.30 . 2 886 . 168 PRO HB3 H 1.91 . 2 887 . 169 ASP H H 8.33 . 1 888 . 169 ASP HA H 4.65 . 1 889 . 169 ASP HB2 H 2.69 . 2 890 . 169 ASP HB3 H 2.90 . 2 891 . 169 ASP N N 120.50 . 1 892 . 170 SER H H 8.16 . 1 893 . 170 SER HA H 4.85 . 1 894 . 170 SER N N 117.00 . 1 895 . 171 PRO HA H 4.54 . 1 896 . 171 PRO HB2 H 2.34 . 2 897 . 171 PRO HB3 H 1.99 . 2 898 . 171 PRO HG2 H 2.05 . 1 899 . 171 PRO HG3 H 2.05 . 1 900 . 171 PRO HD2 H 3.81 . 1 901 . 171 PRO HD3 H 3.81 . 1 902 . 172 GLU H H 8.48 . 1 903 . 172 GLU HA H 4.41 . 1 904 . 172 GLU HB2 H 2.14 . 2 905 . 172 GLU HB3 H 1.98 . 2 906 . 172 GLU N N 121.80 . 1 907 . 173 THR H H 7.76 . 1 908 . 173 THR HA H 4.23 . 1 909 . 173 THR HB H 4.30 . 1 910 . 173 THR HG2 H 1.20 . 1 911 . 173 THR N N 120.50 . 1 stop_ save_