data_4364 #Corrected using PDB structure: 1SLM_ # #N.B. (Observed* = Observed shift + Offset correction) # #After reference correction, the following residues still #have a HA chemical shift difference (obs*-pred) greater than 0.7ppm: #NUM AA CS Observed* Predicted #115 G HA 4.01 2.99 #116 H HA 5.64 4.40 # #After reference correction, the following residues still #have a N chemical shift difference (obs*-pred) greater than 10.0ppm: #NUM AA CS Observed* Predicted # 72 G N 119.53 109.19 # #After reference correction, the following residues still #have a HN chemical shift difference (obs*-pred) greater than 2.0ppm: #NUM AA CS Observed* Predicted # 72 G H 11.59 8.82 #122 H H 5.25 8.70 #129 L H 11.68 9.02 # #The average CS difference between predicted and observed: #HA CA CB CO N HN #0.07 2.21 2.29 N/A -0.17 0.02 # #bmr4364.str.corr chemical shifts have been re-referenced with the following #offsets (these values have been added to the original bmr4364.str file): #HA CA CB CO N HN #N/A +2.25 +2.25 N/A -0.17 N/A # #The 95% confidence intervals for the above recommended offsets are: # HA CA CB CO N HN #+/-0.03 +/-0.16 +/-0.21 N/A +/-0.32 +/-0.06 # #The Correlation Coefficients between predicted and observed #chemical shifts are: #HA CA CB CO N HN #0.853 0.974 0.996 N/A 0.854 0.638 # #The RMSD between predicted and observed* (reference #corrected) chemical shifts are: #HA CA CB CO N HN #0.158 1.007 0.976 N/A 1.894 0.344 # ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Dynamics of Stromelysin/Inhibitor Interactions Studied by 15N NMR Relaxation Measurements: Comparison of Ligand Binding to the S1-S3 and S1-S3PSubsites ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Yuan Peng . . 2 Marshall Vincent P . 3 Petzold Gary L . 4 Poorman Roger A . 5 Stockman Brian J . stop_ _BMRB_accession_number 4364 _BMRB_flat_file_name bmr4364.str _Entry_type new _Submission_date 1999-06-28 _Accession_date 1999-06-29 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 T1_relaxation 1 T2_relaxation 1 heteronuclear_NOE 1 S2_parameters 1 stop_ loop_ _Data_type _Data_type_count '1H chemical shifts' 254 '13C chemical shifts' 252 '15N chemical shifts' 142 'T1 relaxation values' 138 'T2 relaxation values' 138 'heteronuclear NOE values' 138 'S2 parameters' 138 stop_ loop_ _Related_BMRB_accession_number _Relationship 4365 'complex with PNU-107859' 4366 'complex with PNU-142372' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_title ; Dynamics of Stromelysin/Inhibitor Interactions Studied by 15N NMR Relaxation Measurements: Comparison of Ligand Binding to the S1-S3 and S1-S3 Subsites ; _Citation_status published _Citation_type journal _MEDLINE_UI_code 10549133 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Yuan Peng . . 2 Marshall Vincent P . 3 Petzold Gary L . 4 Poorman Roger A . 5 Stockman Brian J . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 15 _Page_first 55 _Page_last 64 _Year 1999 loop_ _Keyword 'Hydroxamic acid' 'Ligand' 'Matrix metalloproteinase' 'Protein dynamics' 'Stromelysin' 'Thiadiazole' stop_ save_ ################################## # Molecular system description # ################################## save_stromelysin_PNU-99533 _Saveframe_category molecular_system _Mol_system_name 'stromelysin-ligand complexes' _Abbreviation_common 'stromelysin-ligand complexes' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label stromelysin $stromelysin PNU-99533 $PNU-99533 stop_ _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Database_entry_details PDB 1HFS "Crystal Structure Of The Catalytic Domain Of Human Fibroblast Stromelysin-1 Inhibited With The N-Carboxy-Alkyl Inhibitor L-764,004" . PDB 2USN "Crystal Structure Of The Catalytic Domain Of Human Fibroblast Stromelysin-1 Inhibited With Thiadiazole Inhibitor Pnu-141803" . PDB 1USN "Crystal Structure Of The Catalytic Domain Of Human Fibroblast Stromelysin-1 Inhibited With Thiadiazole Inhibitor Pnu-142372" . PDB 1B8Y "A Chain A, X-Ray Structure Of Human Stromelysin Catalytic Domain Complexed With Non-Peptide Inhibitors: Implications For Inhibitor Selectivity" . PDB 3USN "Structure Of The Catalytic Domain Of Human Fibroblast Stromelysin-1 Inhibited With The Thiadiazole Inhibitor Ipnu-107859, Nmr, 1 Structure" . PDB 1CAQ "A Chain A, X-Ray Structure Of Human Stromelysin Catalytic Domain Complexes With Non-Peptide Inhibitors: Implication For Inhibitor Selectivity" . PDB 1CIZ "A Chain A, X-Ray Structure Of Human Stromelysin Catalytic Domain Complexes With Non-Peptide Inhibitors: Implication For Inhibitor Selectivity" . PDB 1SLN "Crystal Structure Of The Catalytic Domain Of Human Fibroblast Stromelysin-1 Inhibited With The N-Carboxy-Alkyl Inhibitor L-702,842" . PDB 2SRT "Catalytic Domain Of Human Stromelysin-1 At Ph 5.5 And 40oc Complexed With Inhibitor" . PDB 1BM6 "Solution Structure Of The Catalytic Domain Of Human Stromelysin-1 Complexed To A Potent Non-Peptidic Inhibitor, Nmr, 20 Structures" . PDB 1BIW "B Chain B, Design And Synthesis Of Conformationally-Constrained Mmp Inhibitors" . PDB 1SLM "Crystal Structure Of Fibroblast Stromelysin-1: The C-Truncated Human Proenzyme" . PDB 1UMS "A Chain A, Stromelysin-1 Catalytic Domain With Hydrophobic Inhibitor Bound, Ph 7.0, 32oc, 20 Mm Cacl2, 15% Acetonitrile; Nmr Ensemble Of 20 Structures" . PDB 1UMT "A Chain A, Stromelysin-1 Catalytic Domain With Hydrophobic Inhibitor Bound, Ph 7.0, 32oc, 20 Mm Cacl2, 15% Acetonitrile; Nmr Average Of 20 Structures Minimized With Restraints" . PDB 1C3I "A Chain A, Human Stromelysin-1 Catalytic Domain Complexed With Ro-26- 2812" . PDB 1D8M "A Chain A, Crystal Structure Of Mmp3 Complexed With A Heterocycle- Based Inhibitor" . PDB 1D7X "A Chain A, Crystal Structure Of Mmp3 Complexed With A Modified Proline Scaffold Based Inhibitor." . PDB 1D8F "A Chain A, Crystal Structure Of Mmp3 Complexed With A Piperazine Based Inhibitor." . PDB 1D5J "A Chain A, Crystal Structure Of Mmp3 Complexed With A Thiazepine Based Inhibitor." . PDB 1CQR "B Chain B, Crystal Structure Of The Stromelysin Catalytic Domain At 2.0 A Resolution" . PDB 1B3D "B Chain B, Stromelysin-1" . PDB 1BQO "B Chain B, Discovery Of Potent, Achiral Matrix Metalloproteinase Inhibitors" . PDB 1UEA "A Chain A, Mmp-3TIMP-1 Complex" . PDB 1C8T "A Chain A, Human Stromelysin-1 (E202q) Catalytic Domain Complexed With Ro-26-2812" . stop_ save_ ######################## # Monomeric polymers # ######################## save_stromelysin _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common stromelysin _Name_variant . _Abbreviation_common . _Mol_thiol_state 'not present' ############################## # Polymer residue sequence # ############################## _Residue_count 166 _Mol_residue_sequence ; PKWRKTHLTYRIVNYPPDLP KDAVDSAVEKALKVWEEVTP LTFSRLYEGEADIMISFAVR EHGDFYPFDGPGNVLAHAYA PGPGINGDAHFDDDEQWTKD TTGTNLFLVAAHEIGHSLGL FHSANTEALMYPLYHSLTDL TRFRLSQDDINGIQSLYGPP PDSPET ; loop_ _Residue_seq_code _Residue_label 1 PRO 2 LYS 3 TRP 4 ARG 5 LYS 6 THR 7 HIS 8 LEU 9 THR 10 TYR 11 ARG 12 ILE 13 VAL 14 ASN 15 TYR 16 PRO 17 PRO 18 ASP 19 LEU 20 PRO 21 LYS 22 ASP 23 ALA 24 VAL 25 ASP 26 SER 27 ALA 28 VAL 29 GLU 30 LYS 31 ALA 32 LEU 33 LYS 34 VAL 35 TRP 36 GLU 37 GLU 38 VAL 39 THR 40 PRO 41 LEU 42 THR 43 PHE 44 SER 45 ARG 46 LEU 47 TYR 48 GLU 49 GLY 50 GLU 51 ALA 52 ASP 53 ILE 54 MET 55 ILE 56 SER 57 PHE 58 ALA 59 VAL 60 ARG 61 GLU 62 HIS 63 GLY 64 ASP 65 PHE 66 TYR 67 PRO 68 PHE 69 ASP 70 GLY 71 PRO 72 GLY 73 ASN 74 VAL 75 LEU 76 ALA 77 HIS 78 ALA 79 TYR 80 ALA 81 PRO 82 GLY 83 PRO 84 GLY 85 ILE 86 ASN 87 GLY 88 ASP 89 ALA 90 HIS 91 PHE 92 ASP 93 ASP 94 ASP 95 GLU 96 GLN 97 TRP 98 THR 99 LYS 100 ASP 101 THR 102 THR 103 GLY 104 THR 105 ASN 106 LEU 107 PHE 108 LEU 109 VAL 110 ALA 111 ALA 112 HIS 113 GLU 114 ILE 115 GLY 116 HIS 117 SER 118 LEU 119 GLY 120 LEU 121 PHE 122 HIS 123 SER 124 ALA 125 ASN 126 THR 127 GLU 128 ALA 129 LEU 130 MET 131 TYR 132 PRO 133 LEU 134 TYR 135 HIS 136 SER 137 LEU 138 THR 139 ASP 140 LEU 141 THR 142 ARG 143 PHE 144 ARG 145 LEU 146 SER 147 GLN 148 ASP 149 ASP 150 ILE 151 ASN 152 GLY 153 ILE 154 GLN 155 SER 156 LEU 157 TYR 158 GLY 159 PRO 160 PRO 161 PRO 162 ASP 163 SER 164 PRO 165 GLU 166 THR stop_ _Sequence_homology_query_date 2004-07-29 _Sequence_homology_query_revised_last_date 2004-07-16 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value PDB 1HFS "Crystal Structure Of The Catalytic Domain OfHuman Fibroblast Stromelysin-1 Inhibited With TheN-Carboxy-Alkyl Inhibitor L-764,004" 103.75 160 99 99 4e-90 PDB 1QIC "A Chain A, Crystal Structure Of StromelysinCatalytic Domain" 103.11 161 99 99 10e-92 PDB 1QIA "A Chain A, Crystal Structure Of StromelysinCatalytic Domain" 102.47 162 99 99 1e-92 PDB 1USN "Crystal Structure Of The Catalytic Domain OfHuman Fibroblast Stromelysin-1 Inhibited WithThiadiazole Inhibitor Pnu-142372" 100.61 165 99 99 4e-90 PDB 2USN "Crystal Structure Of The Catalytic Domain OfHuman Fibroblast Stromelysin-1 Inhibited WithThiadiazole Inhibitor Pnu-141803" 100.61 165 99 99 4e-90 PDB 1B8Y "A Chain A, X-Ray Structure Of Human StromelysinCatalytic Domain Complexed With Non-Peptide Inhibitors:Implications For Inhibitor Selectivity" 99.40 167 99 99 10e-92 PDB 1C8T "A Chain A, Human Stromelysin-1 (E202q)Catalytic Domain Complexed With Ro-26-2812" 99.40 167 99 99 7e-93 PDB 1CAQ "A Chain A, X-Ray Structure Of Human StromelysinCatalytic Domain Complexes With Non-Peptide Inhibitors:Implication For Inhibitor Selectivity" 98.81 168 99 99 1e-92 PDB 1CIZ "A Chain A, X-Ray Structure Of Human StromelysinCatalytic Domain Complexes With Non-Peptide Inhibitors:Implication For Inhibitor Selectivity" 98.81 168 99 99 1e-92 PDB 1G4K "A Chain A, X-Ray Structure Of A Novel MatrixMetalloproteinase Inhibitor Complexed To Stromelysin" 98.81 168 99 99 1e-92 PDB 1OO9 "A Chain A, Orientation In Solution Of Mmp-3Catalytic Domain And N- Timp-1 From Residual DipolarCouplings" 98.81 168 99 99 1e-92 PDB 3USN "Structure Of The Catalytic Domain Of HumanFibroblast Stromelysin-1 Inhibited With The ThiadiazoleInhibitor Ipnu-107859, Nmr, 1 Structure" 98.81 168 99 99 1e-92 PDB 1B3D "A Chain A, Stromelysin-1" 95.95 173 99 99 1e-95 PDB 1BIW "A Chain A, Design And Synthesis OfConformationally-Constrained Mmp Inhibitors" 95.95 173 99 99 1e-95 PDB 1BM6 "Solution Structure Of The Catalytic Domain OfHuman Stromelysin-1 Complexed To A Potent Non-PeptidicInhibitor, Nmr, 20 Structures" 95.95 173 99 99 1e-95 PDB 1BQO "A Chain A, Discovery Of Potent, Achiral MatrixMetalloproteinase Inhibitors" 95.95 173 99 99 1e-95 PDB 1C3I "A Chain A, Human Stromelysin-1 Catalytic DomainComplexed With Ro-26- 2812" 95.95 173 99 99 1e-95 PDB 1CQR "A Chain A, Crystal Structure Of The StromelysinCatalytic Domain At 2.0 A Resolution" 95.95 173 99 99 1e-95 PDB 1D5J "A Chain A, Crystal Structure Of Mmp3 ComplexedWith A Thiazepine Based Inhibitor." 95.95 173 99 99 1e-95 PDB 1D7X "A Chain A, Crystal Structure Of Mmp3 ComplexedWith A Modified Proline Scaffold Based Inhibitor." 95.95 173 99 99 1e-95 PDB 1D8F "A Chain A, Crystal Structure Of Mmp3 ComplexedWith A Piperazine Based Inhibitor." 95.95 173 99 99 1e-95 PDB 1D8M "A Chain A, Crystal Structure Of Mmp3 ComplexedWith A Heterocycle- Based Inhibitor" 95.95 173 99 99 1e-95 PDB 1G05 "A Chain A, Heterocycle-Based Mmp InhibitorWith P2'substituents" 95.95 173 99 99 1e-95 PDB 1G49 "A Chain A, A Carboxylic Acid Based InhibitorIn Complex With Mmp3" 95.95 173 99 99 1e-95 PDB 1HY7 "A Chain A, A Carboxylic Acid Based InhibitorIn Complex With Mmp3" 95.95 173 99 99 1e-95 PDB 1SLN "Crystal Structure Of The Catalytic Domain OfHuman Fibroblast Stromelysin-1 Inhibited With TheN-Carboxy-Alkyl Inhibitor L-702,842" 95.95 173 99 99 1e-95 PDB 2SRT "Catalytic Domain Of Human Stromelysin-1 At Ph5.5 And 40oc Complexed With Inhibitor" 95.95 173 99 99 1e-95 PDB 1UEA "A Chain A, Mmp-3TIMP-1 Complex" 95.95 173 98 98 3e-94 PDB 1UMS "A Chain A, Stromelysin-1 Catalytic Domain WithHydrophobic Inhibitor Bound, Ph 7.0, 32oc, 20 Mm Cacl2,15% Acetonitrile; Nmr Ensemble Of 20 Structures" 95.40 174 99 99 1e-95 PDB 1UMT "A Chain A, Stromelysin-1 Catalytic Domain WithHydrophobic Inhibitor Bound, Ph 7.0, 32oc, 20 Mm Cacl2,15% Acetonitrile; Nmr Average Of 20 Structures MinimizedWith Restraints" 95.40 174 99 99 1e-95 PDB 1SLM "Crystal Structure Of FibroblastStromelysin-1: The C-Truncated Human Proenzyme" 65.10 255 99 99 1e-95 EMBL CAA28859.1 "preprostromelysin [Homo sapiens]" 34.80 477 99 99 1e-95 GenBank AAD45887.1 "stromelysin catalytic domain [syntheticconstruct]" 95.40 174 99 99 1e-95 GenBank AAA00036.1 "prostromelysin=matrix metalloproteinase[human, Peptide, 477 aa]" 34.80 477 99 99 1e-95 GenBank AAA36321.1 "matrix metalloproteinase-3" 34.80 477 99 99 1e-95 GenBank AAB36942.1 "stromelysin [Homo sapiens]" 34.80 477 99 99 1e-95 GenBank AAH69676.1 "Matrix metalloproteinase 3,preproprotein [Homo sapiens]" 34.80 477 99 99 1e-95 PIR KCHUS1 "stromelysin 1 (EC 3.4.24.17) precursor[validated] - human" 34.80 477 99 99 1e-95 REF NP_002413.1 "matrix metalloproteinase 3preproprotein; stromelysin 1; progelatinase; transin-1;proteoglycanase [Homo sapiens]" 34.80 477 99 99 1e-95 SWISS-PROT P08254 "MM03_HUMAN Stromelysin-1 precursor (Matrixmetalloproteinase-3) (MMP-3) (Transin-1) (SL-1)" 34.80 477 99 99 1e-95 stop_ save_ ############# # Ligands # ############# save_PNU-99533 _Saveframe_category ligand _Mol_type non-polymer _Name_common ; (2S)-N-methyl-3-(2,3,4,5,6-pentafluorophenyl)-2-({[(5-thioxo-4,5-dihydro- 1,3,4-thiadiazol-2-yl)amino]carbonyl}amino)propanamide ; _Abbreviation_common PNU-99533 _Name_CAS . _CAS_registry_number . _Name_IUPAC . _PDB_code . _Mol_empirical_formula . _Molecular_mass . _Mol_charge . _Mol_paramagnetic no _Mol_aromatic yes save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $stromelysin 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 $stromelysin 'recombinat technology' . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample _Saveframe_category sample _Sample_type solution loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $stromelysin 0.9 mM '[U-15N]' $PNU-99533 0.9 mM . imidazole 10 mM '[U-2H]' CaCl2 2.5 mM . ZnCl2 5 uM . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AMX _Field_strength 600 save_ ############################# # NMR applied experiments # ############################# save_experiment_label _Saveframe_category NMR_applied_experiment _Experiment_name ; 3D 1H-15N NOESY-HMQC 3D 1H-13C-15N HNCA HN(CO)CA CBCACONH HNCACB HBHACONH 2D 1H-15N HSQC 15N R1 15N R2 15N-1H NOE ; save_ ####################### # Sample conditions # ####################### save_conditions _Saveframe_category sample_conditions loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.5 . n/a temperature 300 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_one _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 _Indirect_shift_ratio H2O H 1 protons ppm 4.70 direct . . . . . TMS C 13 'methyl protons' ppm 0.00 indirect . . . . 0.25145002 TMS N 15 'methyl protons' ppm 0.00 indirect . . . . 0.10132914 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # Index Value Definition # # # # 1 Unique # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups # # 3 Aromatic atoms on opposite sides of the ring # # (e.g. Tyr HE1 and HE2 protons) # # 4 Intraresidue ambiguities (e.g. Lys HG and # # HD protons) # # 5 Interresidue ambiguities (Lys 12 vs. Lys 27) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_chemical_shifts _Saveframe_category assigned_chemical_shifts loop_ _Sample_label $sample stop_ _Sample_conditions_label $conditions _Chem_shift_reference_set_label $chemical_shift_reference_one _Mol_system_component_name stromelysin loop_ _Atom_shift_assign_ID _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 1 PRO HA H 4.32 0.02 1 2 1 PRO CA C 63.35 0.1 1 3 2 LYS H H 7.34 0.02 1 4 2 LYS HA H 4.38 0.02 1 5 2 LYS CA C 54.55 0.1 1 6 2 LYS CB C 35.35 0.1 1 7 2 LYS N N 113.53 0.1 1 8 3 TRP H H 8.16 0.02 1 9 3 TRP HA H 4.09 0.02 1 10 3 TRP CA C 57.65 0.1 1 11 3 TRP N N 122.73 0.1 1 12 4 ARG CA C 55.35 0.1 1 13 4 ARG CB C 28.95 0.1 1 14 5 LYS H H 7.53 0.02 1 15 5 LYS CA C 54.15 0.1 1 16 5 LYS CB C 34.35 0.1 1 17 5 LYS N N 116.13 0.1 1 18 6 THR H H 8.03 0.02 1 19 6 THR HA H 4.27 0.02 1 20 6 THR CA C 61.15 0.1 1 21 6 THR CB C 69.05 0.1 1 22 6 THR N N 104.93 0.1 1 23 7 HIS H H 7.01 0.02 1 24 7 HIS HA H 5.03 0.02 1 25 7 HIS CA C 53.95 0.1 1 26 7 HIS CB C 29.65 0.1 1 27 7 HIS N N 119.33 0.1 1 28 8 LEU H H 8.25 0.02 1 29 8 LEU HA H 4.43 0.02 1 30 8 LEU CA C 52.75 0.1 1 31 8 LEU N N 127.53 0.1 1 32 9 THR H H 9.19 0.02 1 33 9 THR HA H 5.71 0.02 1 34 9 THR CA C 58.05 0.1 1 35 9 THR CB C 72.95 0.1 1 36 9 THR N N 109.93 0.1 1 37 10 TYR H H 8.61 0.02 1 38 10 TYR HA H 5.60 0.02 1 39 10 TYR CA C 54.75 0.1 1 40 10 TYR CB C 42.15 0.1 1 41 10 TYR N N 117.23 0.1 1 42 11 ARG H H 8.16 0.02 1 43 11 ARG HA H 4.30 0.02 1 44 11 ARG CA C 54.95 0.1 1 45 11 ARG CB C 34.35 0.1 1 46 11 ARG N N 119.13 0.1 1 47 12 ILE H H 8.38 0.02 1 48 12 ILE HA H 4.30 0.02 1 49 12 ILE CA C 61.45 0.1 1 50 12 ILE N N 127.73 0.1 1 51 13 VAL H H 9.51 0.02 1 52 13 VAL HA H 3.35 0.02 1 53 13 VAL CA C 65.95 0.1 1 54 13 VAL CB C 32.55 0.1 1 55 13 VAL N N 129.33 0.1 1 56 14 ASN H H 7.66 0.02 1 57 14 ASN CA C 51.05 0.1 1 58 14 ASN CB C 39.25 0.1 1 59 14 ASN N N 115.73 0.1 1 60 15 TYR H H 8.03 0.02 1 61 15 TYR HA H 4.29 0.02 1 62 15 TYR CA C 58.75 0.1 1 63 15 TYR N N 111.23 0.1 1 64 17 PRO CA C 63.25 0.1 1 65 17 PRO CB C 31.55 0.1 1 66 18 ASP H H 8.84 0.02 1 67 18 ASP HA H 4.05 0.02 1 68 18 ASP CA C 55.85 0.1 1 69 18 ASP N N 121.03 0.1 1 70 19 LEU H H 6.84 0.02 1 71 19 LEU HA H 4.85 0.02 1 72 19 LEU CA C 56.45 0.1 1 73 19 LEU N N 115.63 0.1 1 74 20 PRO CA C 62.05 0.1 1 75 20 PRO CB C 32.25 0.1 1 76 21 LYS H H 8.61 0.02 1 77 21 LYS HA H 3.67 0.02 1 78 21 LYS CA C 60.55 0.1 1 79 21 LYS CB C 32.25 0.1 1 80 21 LYS N N 123.23 0.1 1 81 22 ASP H H 8.47 0.02 1 82 22 ASP HA H 4.28 0.02 1 83 22 ASP CA C 56.65 0.1 1 84 22 ASP CB C 39.75 0.1 1 85 22 ASP N N 113.23 0.1 1 86 23 ALA H H 7.29 0.02 1 87 23 ALA HA H 4.25 0.02 1 88 23 ALA HB H 1.53 0.02 1 89 23 ALA CA C 54.15 0.1 1 90 23 ALA CB C 19.05 0.1 1 91 23 ALA N N 122.13 0.1 1 92 24 VAL H H 7.50 0.02 1 93 24 VAL HA H 3.52 0.02 1 94 24 VAL CA C 66.15 0.1 1 95 24 VAL N N 121.33 0.1 1 96 25 ASP H H 8.53 0.02 1 97 25 ASP CA C 58.05 0.1 1 98 25 ASP CB C 40.05 0.1 1 99 25 ASP N N 119.03 0.1 1 100 26 SER H H 8.02 0.02 1 101 26 SER HA H 4.20 0.02 1 102 26 SER CA C 61.45 0.1 1 103 26 SER CB C 63.35 0.1 1 104 26 SER N N 111.93 0.1 1 105 27 ALA H H 7.65 0.02 1 106 27 ALA HA H 4.13 0.02 1 107 27 ALA CA C 55.65 0.1 1 108 27 ALA CB C 18.35 0.1 1 109 27 ALA N N 123.53 0.1 1 110 28 VAL H H 7.96 0.02 1 111 28 VAL HA H 3.18 0.02 1 112 28 VAL CA C 67.25 0.1 1 113 28 VAL CB C 31.55 0.1 1 114 28 VAL N N 115.33 0.1 1 115 29 GLU H H 8.37 0.02 1 116 29 GLU HA H 3.62 0.02 1 117 29 GLU CA C 60.15 0.1 1 118 29 GLU CB C 29.45 0.1 1 119 29 GLU N N 117.63 0.1 1 120 30 LYS H H 8.28 0.02 1 121 30 LYS HA H 3.87 0.02 1 122 30 LYS CA C 59.75 0.1 1 123 30 LYS CB C 32.25 0.1 1 124 30 LYS N N 118.63 0.1 1 125 31 ALA H H 8.03 0.02 1 126 31 ALA HA H 3.96 0.02 1 127 31 ALA CA C 55.65 0.1 1 128 31 ALA CB C 18.55 0.1 1 129 31 ALA N N 122.83 0.1 1 130 32 LEU H H 7.68 0.02 1 131 32 LEU HA H 3.60 0.02 1 132 32 LEU CA C 57.65 0.1 1 133 32 LEU CB C 40.85 0.1 1 134 32 LEU N N 114.93 0.1 1 135 33 LYS H H 7.80 0.02 1 136 33 LYS CA C 58.55 0.1 1 137 33 LYS CB C 32.05 0.1 1 138 33 LYS N N 118.43 0.1 1 139 34 VAL H H 7.44 0.02 1 140 34 VAL HA H 3.74 0.02 1 141 34 VAL CA C 65.35 0.1 1 142 34 VAL CB C 31.25 0.1 1 143 34 VAL N N 114.33 0.1 1 144 35 TRP H H 6.66 0.02 1 145 35 TRP CA C 57.85 0.1 1 146 35 TRP CB C 30.25 0.1 1 147 35 TRP N N 117.13 0.1 1 148 36 GLU H H 8.58 0.02 1 149 36 GLU HA H 3.91 0.02 1 150 36 GLU CA C 59.55 0.1 1 151 36 GLU CB C 31.25 0.1 1 152 36 GLU N N 122.33 0.1 1 153 37 GLU H H 7.80 0.02 1 154 37 GLU HA H 4.10 0.02 1 155 37 GLU CA C 58.55 0.1 1 156 37 GLU CB C 30.75 0.1 1 157 37 GLU N N 110.93 0.1 1 158 38 VAL H H 7.04 0.02 1 159 38 VAL CA C 60.15 0.1 1 160 38 VAL CB C 32.25 0.1 1 161 38 VAL N N 104.43 0.1 1 162 39 THR H H 7.63 0.02 1 163 39 THR HA H 5.42 0.02 1 164 39 THR CA C 60.15 0.1 1 165 39 THR N N 111.03 0.1 1 166 40 PRO CA C 62.35 0.1 1 167 40 PRO CB C 31.55 0.1 1 168 41 LEU H H 7.32 0.02 1 169 41 LEU CA C 54.75 0.1 1 170 41 LEU CB C 42.65 0.1 1 171 41 LEU N N 117.43 0.1 1 172 42 THR H H 8.12 0.02 1 173 42 THR HA H 4.48 0.02 1 174 42 THR CA C 59.75 0.1 1 175 42 THR CB C 72.35 0.1 1 176 42 THR N N 109.63 0.1 1 177 43 PHE H H 8.27 0.02 1 178 43 PHE HA H 5.70 0.02 1 179 43 PHE CA C 56.25 0.1 1 180 43 PHE CB C 43.15 0.1 1 181 43 PHE N N 116.63 0.1 1 182 44 SER H H 8.80 0.02 1 183 44 SER HA H 4.86 0.02 1 184 44 SER CA C 57.25 0.1 1 185 44 SER CB C 65.65 0.1 1 186 44 SER N N 115.93 0.1 1 187 45 ARG H H 8.50 0.02 1 188 45 ARG HA H 3.47 0.02 1 189 45 ARG CA C 55.65 0.1 1 190 45 ARG N N 124.53 0.1 1 191 46 LEU H H 8.58 0.02 1 192 46 LEU CA C 52.95 0.1 1 193 46 LEU CB C 45.45 0.1 1 194 46 LEU N N 124.73 0.1 1 195 47 TYR H H 9.21 0.02 1 196 47 TYR HA H 4.33 0.02 1 197 47 TYR CA C 58.75 0.1 1 198 47 TYR CB C 39.55 0.1 1 199 47 TYR N N 118.43 0.1 1 200 48 GLU H H 7.47 0.02 1 201 48 GLU HA H 4.33 0.02 1 202 48 GLU CA C 54.55 0.1 1 203 48 GLU CB C 32.75 0.1 1 204 48 GLU N N 116.23 0.1 1 205 49 GLY H H 8.52 0.02 1 206 49 GLY HA2 H 3.70 0.02 2 207 49 GLY HA3 H 4.00 0.02 2 208 49 GLY CA C 44.45 0.1 1 209 49 GLY N N 107.93 0.1 1 210 50 GLU H H 8.21 0.02 1 211 50 GLU HA H 4.30 0.02 1 212 50 GLU HB2 H 1.83 0.02 2 213 50 GLU CA C 55.85 0.1 1 214 50 GLU CB C 29.65 0.1 1 215 50 GLU N N 118.73 0.1 1 216 51 ALA H H 8.02 0.02 1 217 51 ALA HA H 4.40 0.02 1 218 51 ALA HB H 0.85 0.02 1 219 51 ALA CA C 49.35 0.1 1 220 51 ALA CB C 21.95 0.1 1 221 51 ALA N N 131.13 0.1 1 222 52 ASP H H 8.30 0.02 1 223 52 ASP HA H 4.30 0.02 1 224 52 ASP CA C 58.75 0.1 1 225 52 ASP CB C 41.05 0.1 1 226 52 ASP N N 121.53 0.1 1 227 53 ILE H H 8.61 0.02 1 228 53 ILE CA C 60.55 0.1 1 229 53 ILE CB C 39.25 0.1 1 230 53 ILE N N 123.33 0.1 1 231 54 MET H H 7.26 0.02 1 232 54 MET HA H 4.90 0.02 1 233 54 MET CA C 53.75 0.1 1 234 54 MET N N 126.13 0.1 1 235 55 ILE H H 9.18 0.02 1 236 55 ILE HA H 5.34 0.02 1 237 55 ILE CA C 60.75 0.1 1 238 55 ILE CB C 40.05 0.1 1 239 55 ILE N N 127.83 0.1 1 240 56 SER H H 8.52 0.02 1 241 56 SER HA H 4.99 0.02 1 242 56 SER CA C 56.85 0.1 1 243 56 SER CB C 66.45 0.1 1 244 56 SER N N 117.83 0.1 1 245 57 PHE H H 9.56 0.02 1 246 57 PHE HA H 5.20 0.02 1 247 57 PHE CA C 56.65 0.1 1 248 57 PHE N N 119.73 0.1 1 249 58 ALA H H 9.25 0.02 1 250 58 ALA HA H 4.77 0.02 1 251 58 ALA HB H 0.96 0.02 1 252 58 ALA CA C 51.05 0.1 1 253 58 ALA CB C 23.45 0.1 1 254 58 ALA N N 124.93 0.1 1 255 59 VAL H H 8.19 0.02 1 256 59 VAL HA H 4.89 0.02 1 257 59 VAL CA C 59.55 0.1 1 258 59 VAL N N 111.53 0.1 1 259 60 ARG H H 9.55 0.02 1 260 60 ARG HA H 3.77 0.02 1 261 60 ARG CA C 56.45 0.1 1 262 60 ARG N N 117.03 0.1 1 263 61 GLU H H 8.31 0.02 1 264 61 GLU HA H 4.25 0.02 1 265 61 GLU CA C 58.05 0.1 1 266 61 GLU N N 127.83 0.1 1 267 62 HIS H H 9.15 0.02 1 268 62 HIS HA H 5.05 0.02 1 269 62 HIS CA C 54.55 0.1 1 270 62 HIS CB C 28.65 0.1 1 271 62 HIS N N 120.83 0.1 1 272 63 GLY H H 8.46 0.02 1 273 63 GLY CA C 45.85 0.1 1 274 63 GLY N N 108.73 0.1 1 275 64 ASP H H 6.93 0.02 1 276 64 ASP HA H 4.50 0.02 1 277 64 ASP CA C 51.05 0.1 1 278 64 ASP N N 116.73 0.1 1 279 65 PHE CA C 58.45 0.1 1 280 65 PHE CB C 37.75 0.1 1 281 66 TYR H H 6.81 0.02 1 282 66 TYR HA H 4.87 0.02 1 283 66 TYR CA C 54.15 0.1 1 284 66 TYR N N 116.23 0.1 1 285 68 PHE CA C 57.65 0.1 1 286 68 PHE CB C 38.25 0.1 1 287 69 ASP H H 7.82 0.02 1 288 69 ASP CA C 53.55 0.1 1 289 69 ASP N N 115.53 0.1 1 290 70 GLY H H 8.89 0.02 1 291 70 GLY CA C 44.25 0.1 1 292 70 GLY N N 109.93 0.1 1 293 71 PRO CA C 63.85 0.1 1 294 71 PRO CB C 31.55 0.1 1 295 72 GLY H H 11.57 0.02 1 296 72 GLY HA2 H 3.93 0.02 2 297 72 GLY CA C 43.35 0.1 1 298 72 GLY N N 119.53 0.1 1 299 73 ASN H H 9.05 0.02 1 300 73 ASN HA H 3.75 0.02 1 301 73 ASN CA C 56.05 0.1 1 302 73 ASN CB C 38.25 0.1 1 303 73 ASN N N 118.83 0.1 1 304 74 VAL H H 10.12 0.02 1 305 74 VAL HA H 3.58 0.02 1 306 74 VAL CA C 65.75 0.1 1 307 74 VAL N N 126.63 0.1 1 308 75 LEU H H 9.20 0.02 1 309 75 LEU CA C 55.85 0.1 1 310 75 LEU CB C 43.95 0.1 1 311 75 LEU N N 127.33 0.1 1 312 76 ALA H H 7.25 0.02 1 313 76 ALA HA H 4.43 0.02 1 314 76 ALA CA C 51.65 0.1 1 315 76 ALA CB C 21.65 0.1 1 316 76 ALA N N 113.33 0.1 1 317 77 HIS H H 9.24 0.02 1 318 77 HIS CA C 54.35 0.1 1 319 77 HIS N N 113.83 0.1 1 320 78 ALA H H 8.46 0.02 1 321 78 ALA CA C 51.25 0.1 1 322 78 ALA N N 120.33 0.1 1 323 79 TYR H H 7.80 0.02 1 324 79 TYR HA H 4.29 0.02 1 325 79 TYR CA C 56.85 0.1 1 326 79 TYR N N 117.53 0.1 1 327 80 ALA H H 7.50 0.02 1 328 80 ALA CA C 50.25 0.1 1 329 80 ALA N N 120.13 0.1 1 330 82 GLY H H 5.51 0.02 1 331 82 GLY CA C 43.65 0.1 1 332 82 GLY N N 107.73 0.1 1 333 83 PRO CA C 62.85 0.1 1 334 83 PRO CB C 33.35 0.1 1 335 84 GLY H H 8.77 0.02 1 336 84 GLY HA2 H 3.75 0.02 2 337 84 GLY HA3 H 3.89 0.02 2 338 84 GLY CA C 46.75 0.1 1 339 84 GLY N N 109.43 0.1 1 340 85 ILE H H 8.93 0.02 1 341 85 ILE HA H 4.14 0.02 1 342 85 ILE CA C 61.85 0.1 1 343 85 ILE N N 131.43 0.1 1 344 86 ASN H H 7.15 0.02 1 345 86 ASN HA H 4.15 0.02 1 346 86 ASN CA C 55.85 0.1 1 347 86 ASN CB C 35.65 0.1 1 348 86 ASN N N 117.93 0.1 1 349 87 GLY H H 7.68 0.02 1 350 87 GLY CA C 45.85 0.1 1 351 87 GLY N N 118.53 0.1 1 352 88 ASP H H 7.93 0.02 1 353 88 ASP CA C 55.35 0.1 1 354 88 ASP N N 121.13 0.1 1 355 89 ALA H H 8.08 0.02 1 356 89 ALA HB H 1.00 0.02 1 357 89 ALA CA C 51.25 0.1 1 358 89 ALA CB C 21.95 0.1 1 359 89 ALA N N 117.33 0.1 1 360 90 HIS H H 9.09 0.02 1 361 90 HIS HA H 5.75 0.02 1 362 90 HIS CA C 50.65 0.1 1 363 90 HIS CB C 34.35 0.1 1 364 90 HIS N N 119.53 0.1 1 365 91 PHE H H 8.84 0.02 1 366 91 PHE HA H 4.07 0.02 1 367 91 PHE CA C 56.65 0.1 1 368 91 PHE CB C 41.35 0.1 1 369 91 PHE N N 122.23 0.1 1 370 92 ASP H H 7.96 0.02 1 371 92 ASP HA H 4.39 0.02 1 372 92 ASP CA C 53.75 0.1 1 373 92 ASP CB C 40.55 0.1 1 374 92 ASP N N 123.03 0.1 1 375 93 ASP H H 9.84 0.02 1 376 93 ASP HA H 5.50 0.02 1 377 93 ASP HB2 H 2.60 0.02 2 378 93 ASP HB3 H 2.71 0.02 2 379 93 ASP CA C 53.15 0.1 1 380 93 ASP CB C 40.55 0.1 1 381 93 ASP N N 127.83 0.1 1 382 94 ASP H H 9.28 0.02 1 383 94 ASP CA C 56.45 0.1 1 384 94 ASP CB C 38.75 0.1 1 385 94 ASP N N 123.63 0.1 1 386 95 GLU H H 7.22 0.02 1 387 95 GLU HA H 4.48 0.02 1 388 95 GLU CA C 53.35 0.1 1 389 95 GLU CB C 26.05 0.1 1 390 95 GLU N N 115.43 0.1 1 391 96 GLN H H 8.36 0.02 1 392 96 GLN HA H 4.33 0.02 1 393 96 GLN CA C 53.35 0.1 1 394 96 GLN CB C 27.35 0.1 1 395 96 GLN N N 126.03 0.1 1 396 97 TRP H H 9.60 0.02 1 397 97 TRP HA H 4.97 0.02 1 398 97 TRP CA C 57.65 0.1 1 399 97 TRP N N 130.43 0.1 1 400 98 THR H H 8.89 0.02 1 401 98 THR HA H 4.86 0.02 1 402 98 THR CA C 60.15 0.1 1 403 98 THR N N 110.63 0.1 1 404 99 LYS H H 9.06 0.02 1 405 99 LYS HA H 4.47 0.02 1 406 99 LYS CA C 56.65 0.1 1 407 99 LYS CB C 33.35 0.1 1 408 99 LYS N N 119.23 0.1 1 409 100 ASP H H 7.50 0.02 1 410 100 ASP HA H 4.88 0.02 1 411 100 ASP CA C 52.55 0.1 1 412 100 ASP N N 120.43 0.1 1 413 101 THR CA C 61.85 0.1 1 414 101 THR CB C 67.75 0.1 1 415 102 THR H H 8.19 0.02 1 416 102 THR HA H 4.17 0.02 1 417 102 THR CA C 64.05 0.1 1 418 102 THR CB C 69.85 0.1 1 419 102 THR N N 114.43 0.1 1 420 103 GLY H H 7.34 0.02 1 421 103 GLY HA2 H 3.48 0.02 2 422 103 GLY CA C 45.05 0.1 1 423 103 GLY N N 111.53 0.1 1 424 104 THR H H 8.44 0.02 1 425 104 THR HA H 3.67 0.02 1 426 104 THR CA C 62.85 0.1 1 427 104 THR CB C 67.45 0.1 1 428 104 THR N N 122.13 0.1 1 429 105 ASN H H 8.31 0.02 1 430 105 ASN CA C 55.35 0.1 1 431 105 ASN N N 126.93 0.1 1 432 106 LEU H H 7.99 0.02 1 433 106 LEU HA H 4.07 0.02 1 434 106 LEU CA C 58.05 0.1 1 435 106 LEU CB C 41.35 0.1 1 436 106 LEU N N 127.73 0.1 1 437 107 PHE H H 8.30 0.02 1 438 107 PHE CA C 60.95 0.1 1 439 107 PHE N N 119.33 0.1 1 440 108 LEU H H 8.71 0.02 1 441 108 LEU CA C 57.95 0.1 1 442 108 LEU CB C 42.85 0.1 1 443 108 LEU N N 119.33 0.1 1 444 109 VAL H H 7.56 0.02 1 445 109 VAL HA H 3.63 0.02 1 446 109 VAL CA C 66.55 0.1 1 447 109 VAL N N 115.83 0.1 1 448 110 ALA H H 9.48 0.02 1 449 110 ALA HA H 3.98 0.02 1 450 110 ALA CA C 55.85 0.1 1 451 110 ALA CB C 16.45 0.1 1 452 110 ALA N N 121.93 0.1 1 453 111 ALA H H 8.74 0.02 1 454 111 ALA HA H 3.90 0.02 1 455 111 ALA CA C 56.85 0.1 1 456 111 ALA CB C 16.75 0.1 1 457 111 ALA N N 119.43 0.1 1 458 112 HIS H H 7.47 0.02 1 459 112 HIS HA H 4.27 0.02 1 460 112 HIS CA C 59.75 0.1 1 461 112 HIS CB C 27.85 0.1 1 462 112 HIS N N 117.33 0.1 1 463 113 GLU H H 8.87 0.02 1 464 113 GLU CA C 58.25 0.1 1 465 113 GLU N N 114.83 0.1 1 466 114 ILE H H 8.92 0.02 1 467 114 ILE CA C 61.65 0.1 1 468 114 ILE N N 117.13 0.1 1 469 115 GLY H H 7.38 0.02 1 470 115 GLY HA2 H 3.94 0.02 2 471 115 GLY CA C 48.35 0.1 1 472 115 GLY N N 107.53 0.1 1 473 116 HIS H H 7.01 0.02 1 474 116 HIS HA H 5.57 0.02 1 475 116 HIS CA C 57.25 0.1 1 476 116 HIS N N 118.43 0.1 1 477 117 SER CA C 63.05 0.1 1 478 118 LEU H H 7.63 0.02 1 479 118 LEU CA C 55.15 0.1 1 480 118 LEU N N 112.73 0.1 1 481 119 GLY CA C 44.95 0.1 1 482 120 LEU H H 8.86 0.02 1 483 120 LEU CA C 54.15 0.1 1 484 120 LEU CB C 42.35 0.1 1 485 120 LEU N N 119.73 0.1 1 486 121 PHE H H 8.90 0.02 1 487 121 PHE CA C 53.75 0.1 1 488 121 PHE N N 123.73 0.1 1 489 122 HIS H H 5.23 0.02 1 490 122 HIS N N 121.13 0.1 1 491 124 ALA H H 8.55 0.02 1 492 124 ALA HA H 4.58 0.02 1 493 124 ALA HB H 1.41 0.02 1 494 124 ALA CA C 52.05 0.1 1 495 124 ALA CB C 19.35 0.1 1 496 124 ALA N N 126.23 0.1 1 497 125 ASN H H 8.77 0.02 1 498 125 ASN CA C 53.55 0.1 1 499 125 ASN CB C 37.45 0.1 1 500 125 ASN N N 120.13 0.1 1 501 126 THR H H 8.05 0.02 1 502 126 THR HA H 2.33 0.02 1 503 126 THR CA C 63.85 0.1 1 504 126 THR CB C 68.25 0.1 1 505 126 THR N N 116.73 0.1 1 506 127 GLU H H 8.84 0.02 1 507 127 GLU HA H 4.22 0.02 1 508 127 GLU CA C 55.85 0.1 1 509 127 GLU CB C 28.95 0.1 1 510 127 GLU N N 118.93 0.1 1 511 128 ALA H H 7.77 0.02 1 512 128 ALA CA C 51.85 0.1 1 513 128 ALA CB C 19.35 0.1 1 514 128 ALA N N 123.53 0.1 1 515 129 LEU H H 11.66 0.02 1 516 129 LEU CA C 57.65 0.1 1 517 129 LEU N N 131.73 0.1 1 518 131 TYR H H 7.94 0.02 1 519 131 TYR CA C 57.85 0.1 1 520 131 TYR N N 127.83 0.1 1 521 132 PRO CA C 65.15 0.1 1 522 132 PRO CB C 30.45 0.1 1 523 133 LEU H H 6.48 0.02 1 524 133 LEU HA H 4.96 0.02 1 525 133 LEU HB2 H 1.61 0.02 2 526 133 LEU CA C 53.55 0.1 1 527 133 LEU CB C 43.45 0.1 1 528 133 LEU N N 118.93 0.1 1 529 134 TYR H H 8.55 0.02 1 530 134 TYR HA H 4.18 0.02 1 531 134 TYR CA C 58.05 0.1 1 532 134 TYR CB C 40.05 0.1 1 533 134 TYR N N 123.63 0.1 1 534 135 HIS H H 8.33 0.02 1 535 135 HIS CA C 54.15 0.1 1 536 135 HIS CB C 29.65 0.1 1 537 135 HIS N N 127.23 0.1 1 538 136 SER H H 8.10 0.02 1 539 136 SER CA C 58.05 0.1 1 540 136 SER CB C 63.35 0.1 1 541 136 SER N N 117.33 0.1 1 542 137 LEU H H 7.47 0.02 1 543 137 LEU CA C 54.15 0.1 1 544 137 LEU N N 122.43 0.1 1 545 138 THR HA H 4.27 0.02 1 546 138 THR CA C 63.85 0.1 1 547 138 THR CB C 69.25 0.1 1 548 139 ASP H H 7.72 0.02 1 549 139 ASP HA H 4.74 0.02 1 550 139 ASP CA C 52.75 0.1 1 551 139 ASP CB C 41.35 0.1 1 552 139 ASP N N 119.83 0.1 1 553 140 LEU H H 8.92 0.02 1 554 140 LEU HA H 4.07 0.02 1 555 140 LEU CA C 57.25 0.1 1 556 140 LEU CB C 41.85 0.1 1 557 140 LEU N N 125.23 0.1 1 558 141 THR H H 8.43 0.02 1 559 141 THR HA H 4.14 0.02 1 560 141 THR CA C 64.55 0.1 1 561 141 THR CB C 69.05 0.1 1 562 141 THR N N 111.13 0.1 1 563 142 ARG H H 7.44 0.02 1 564 142 ARG HA H 4.35 0.02 1 565 142 ARG CA C 54.75 0.1 1 566 142 ARG CB C 30.25 0.1 1 567 142 ARG N N 118.63 0.1 1 568 143 PHE H H 7.38 0.02 1 569 143 PHE HA H 4.08 0.02 1 570 143 PHE CA C 60.35 0.1 1 571 143 PHE CB C 39.25 0.1 1 572 143 PHE N N 120.43 0.1 1 573 144 ARG H H 7.01 0.02 1 574 144 ARG HA H 3.89 0.02 1 575 144 ARG HB2 H 1.40 0.02 2 576 144 ARG CA C 54.15 0.1 1 577 144 ARG CB C 33.05 0.1 1 578 144 ARG N N 126.03 0.1 1 579 145 LEU H H 8.43 0.02 1 580 145 LEU HA H 3.78 0.02 1 581 145 LEU CA C 55.15 0.1 1 582 145 LEU N N 122.13 0.1 1 583 146 SER H H 8.24 0.02 1 584 146 SER CA C 58.55 0.1 1 585 146 SER N N 117.63 0.1 1 586 147 GLN H H 9.02 0.02 1 587 147 GLN CA C 58.25 0.1 1 588 147 GLN N N 121.63 0.1 1 589 148 ASP H H 8.19 0.02 1 590 148 ASP CA C 58.75 0.1 1 591 148 ASP N N 117.43 0.1 1 592 149 ASP CA C 57.65 0.1 1 593 150 ILE H H 7.90 0.02 1 594 150 ILE HA H 3.52 0.02 1 595 150 ILE CA C 65.75 0.1 1 596 150 ILE N N 119.33 0.1 1 597 151 ASN H H 9.18 0.02 1 598 151 ASN HA H 4.23 0.02 1 599 151 ASN CA C 55.15 0.1 1 600 151 ASN CB C 37.15 0.1 1 601 151 ASN N N 118.13 0.1 1 602 152 GLY H H 8.09 0.02 1 603 152 GLY HA2 H 4.00 0.02 2 604 152 GLY CA C 46.05 0.1 1 605 152 GLY N N 108.63 0.1 1 606 153 ILE H H 8.72 0.02 1 607 153 ILE CA C 60.95 0.1 1 608 153 ILE N N 125.03 0.1 1 609 154 GLN H H 8.58 0.02 1 610 154 GLN CA C 58.25 0.1 1 611 154 GLN N N 121.63 0.1 1 612 155 SER H H 7.80 0.02 1 613 155 SER HA H 4.20 0.02 1 614 155 SER CA C 61.65 0.1 1 615 155 SER N N 118.93 0.1 1 616 156 LEU H H 6.68 0.02 1 617 156 LEU HA H 4.07 0.02 1 618 156 LEU HB2 H 1.71 0.02 2 619 156 LEU CA C 56.25 0.1 1 620 156 LEU N N 120.03 0.1 1 621 157 TYR H H 7.42 0.02 1 622 157 TYR CA C 58.95 0.1 1 623 157 TYR CB C 41.55 0.1 1 624 157 TYR N N 112.23 0.1 1 625 158 GLY H H 8.31 0.02 1 626 158 GLY CA C 44.25 0.1 1 627 158 GLY N N 108.53 0.1 1 628 161 PRO CA C 62.85 0.1 1 629 161 PRO CB C 31.75 0.1 1 630 162 ASP H H 8.31 0.02 1 631 162 ASP HA H 4.52 0.02 1 632 162 ASP CA C 54.15 0.1 1 633 162 ASP CB C 41.05 0.1 1 634 162 ASP N N 119.73 0.1 1 635 163 SER H H 8.13 0.02 1 636 163 SER CA C 56.25 0.1 1 637 163 SER N N 116.23 0.1 1 638 164 PRO CA C 63.25 0.1 1 639 164 PRO CB C 32.05 0.1 1 640 165 GLU H H 8.44 0.02 1 641 165 GLU HA H 4.26 0.02 1 642 165 GLU CA C 56.65 0.1 1 643 165 GLU CB C 30.25 0.1 1 644 165 GLU N N 120.93 0.1 1 645 166 THR H H 7.72 0.02 1 646 166 THR HA H 4.11 0.02 1 647 166 THR CA C 63.05 0.1 1 648 166 THR N N 119.73 0.1 1 stop_ save_ save_T1_relaxation_label _Saveframe_category T1_relaxation loop_ _Sample_label $sample stop_ _Sample_conditions_label $conditions _Spectrometer_frequency_1H 600 _T1_coherence_type Nz _T1_value_units s-1 _Mol_system_component_name stromelysin loop_ _Residue_seq_code _Residue_label _Atom_name _T1_value _T1_value_error 2 LYS N 1.0616 0.0531 3 TRP N 0.9181 0.0427 5 LYS N 0.927 0.0463 6 THR N 0.8868 0.0443 7 HIS N 1.0426 0.0521 8 LEU N 0.9846 0.0569 9 THR N 0.9196 0.0551 10 TYR N 0.9886 0.0494 11 ARG N 1.1068 0.0651 12 ILE N 1.0231 0.0742 13 VAL N 0.8646 0.0375 14 ASN N 1.0416 0.0521 15 TYR N 0.9137 0.0457 18 ASP N 1.1082 0.0554 19 LEU N 1.115 0.0751 21 LYS N 1.1336 0.0306 22 ASP N 1.0266 0.0513 23 ALA N 1.0099 0.0505 24 VAL N 1.009 0.0504 25 ASP N 1.0277 0.0514 26 SER N 1.0156 0.0508 27 ALA N 1.0451 0.0523 28 VAL N 1.0569 0.0528 29 GLU N 1.0974 0.0549 30 LYS N 1.0528 0.0526 31 ALA N 1.0569 0.0528 32 LEU N 0.9519 0.0476 33 LYS N 1.0315 0.0516 34 VAL N 0.9713 0.0486 35 TRP N 1.0283 0.0514 36 GLU N 1.0086 0.0504 37 GLU N 1.0146 0.0507 38 VAL N 1.022 0.0511 39 THR N 1.0965 0.0548 41 LEU N 1.0107 0.0393 42 THR N 0.8758 0.0438 43 PHE N 0.9311 0.0466 44 SER N 1.0071 0.0479 45 ARG N 0.9481 0.0559 46 LEU N 0.8618 0.0776 47 TYR N 0.8466 0.0642 48 GLU N 0.9189 0.0459 49 GLY N 0.9978 0.0499 50 GLU N 0.992 0.0496 51 ALA N 0.8739 0.0539 52 ASP N 1.0807 0.0543 54 MET N 0.9697 0.063 55 ILE N 0.9172 0.063 56 SER N 1.04 0.0526 57 PHE N 0.9514 0.0711 58 ALA N 1.0323 0.0516 59 VAL N 1.0021 0.0501 60 ARG N 0.9056 0.225 61 GLU N 0.9698 0.0763 62 HIS N 0.7995 0.1053 63 GLY N 0.8602 0.1145 64 ASP N 0.9308 0.0465 66 TYR N 1.0107 0.0505 69 ASP N 0.8928 0.0628 70 GLY N 1.0857 0.0723 72 GLY N 0.8323 0.0667 73 ASN N 0.9425 0.0478 74 VAL N 0.9442 0.0522 75 LEU N 0.8655 0.0976 76 ALA N 0.9774 0.0534 77 HIS N 1.0681 0.0547 78 ALA N 1.0242 0.0815 79 TYR N 1.0283 0.0531 80 ALA N 1.0075 0.0572 82 GLY N 1.1583 0.0719 84 GLY N 0.9736 0.0547 85 ILE N 0.7915 0.1142 86 ASN N 1.0811 0.0574 87 GLY N 0.8584 0.0892 88 ASP N 1.0547 0.0578 89 ALA N 1.0635 0.0532 90 HIS N 1.0535 0.0704 91 PHE N 0.9936 0.058 92 ASP N 1.102 0.0596 93 ASP N 1.1159 0.0638 94 ASP N 1.0944 0.0567 95 GLU N 1.072 0.0558 96 GLN N 1.0422 0.0341 97 TRP N 0.9323 0.0356 98 THR N 1.0502 0.0525 99 LYS N 0.949 0.068 100 ASP N 1.1041 0.0559 102 THR N 1.1546 0.1252 103 GLY N 1.0817 0.0571 104 THR N 1.0534 0.0432 105 ASN N 1.0649 0.0788 106 LEU N 1.0588 0.0557 107 PHE N 1.0923 0.0546 108 LEU N 1.097 0.0549 109 VAL N 1.052 0.0422 110 ALA N 1.0552 0.0553 111 ALA N 1.0834 0.0542 112 HIS N 1.0614 0.0531 113 GLU N 1.1172 0.1436 114 ILE N 1.059 0.053 115 GLY N 1.0449 0.0538 116 HIS N 0.9681 0.0484 118 LEU N 0.9634 0.0599 120 LEU N 1.1078 0.0624 121 PHE N 0.9482 0.0546 124 ALA N 0.8172 0.0992 125 ASN N 1.0454 0.0569 126 THR N 1.082 0.0541 127 GLU N 1.0688 0.0534 128 ALA N 1.1018 0.0301 129 LEU N 1.0216 0.0503 131 TYR N 1.089 0.0568 133 LEU N 0.9269 0.0463 134 TYR N 1.1063 0.0575 135 HIS N 1.0377 0.0519 137 LEU N 0.9989 0.0499 140 LEU N 0.9004 0.1007 141 THR N 1.1107 0.0555 142 ARG N 1.1345 0.0567 143 PHE N 1.0495 0.0525 144 ARG N 1.0425 0.0372 145 LEU N 1.0644 0.0432 146 SER N 1.0213 0.0597 147 GLN N 1.0239 0.0766 148 ASP N 1.0074 0.0547 150 ILE N 1.0494 0.0721 151 ASN N 1.0719 0.0536 152 GLY N 1.0422 0.0572 153 ILE N 1.0994 0.0575 154 GLN N 1.1499 0.0575 155 SER N 1.0439 0.0522 156 LEU N 0.9564 0.0609 157 TYR N 0.8074 0.0615 158 GLY N 0.8671 0.0368 162 ASP N 1.0266 0.0513 163 SER N 1.052 0.0526 165 GLU N 1.1012 0.0551 166 THR N 0.8652 0.0433 stop_ save_ save_T2_relaxation_label _Saveframe_category T2_relaxation loop_ _Sample_label $sample stop_ _Sample_conditions_label $conditions _Spectrometer_frequency_1H 600 _T2_coherence_type Nz _T2_value_units s-1 _Mol_system_component_name stromelysin loop_ _Residue_seq_code _Residue_label _Atom_name _T2_value _T2_value_error _Rex_value _Rex_error 2 LYS N 16.3 0.793 1.08 0.95 3 TRP N 19.4609 0.4828 6.51 0.88 5 LYS N 13.476 0.6738 . . 6 THR N 15.5289 0.8836 2.81 1.14 7 HIS N 15.0688 0.7534 . . 8 LEU N 14.3508 0.8687 . . 9 THR N 15.7419 0.9628 2.56 1.24 10 TYR N 18.839 1.2369 4.67 1.44 11 ARG N 17.6406 1.0146 1.77 1.13 12 ILE N 15.2226 1.3286 . . 13 VAL N 14.6811 0.483 2.54 0.72 14 ASN N 16.4712 0.8236 1.54 1.04 15 TYR N 12.738 0.9464 . . 18 ASP N 17.7664 0.8883 1.88 0.97 19 LEU N 16.1474 0.9552 . . 21 LYS N 15.36 0.5046 . . 22 ASP N 15.8114 0.7906 . . 23 ALA N 17.6142 0.8807 3.14 1.17 24 VAL N 16.1352 0.8068 1.67 1.04 25 ASP N 17.5473 0.8774 2.81 1.14 26 SER N 16.3062 0.8153 1.75 1.15 27 ALA N 17.2584 0.8629 2.27 1.1 28 VAL N 16.2291 0.8115 . . 29 GLU N 17.1287 0.8564 1.4 1.06 30 LYS N 17.8074 0.8904 2.71 1.19 31 ALA N 18.0625 0.9031 2.91 1.14 32 LEU N 17.2115 0.8606 3.56 1.1 33 LYS N 16.9985 0.8499 2.21 1.16 34 VAL N 17.172 0.8586 3.25 1.13 35 TRP N 15.9959 0.7998 . . 36 GLU N 17.9796 0.899 3.52 1.16 37 GLU N 16.2368 0.8118 1.69 1.08 38 VAL N 17.1764 0.8588 2.52 1.09 39 THR N 15.9302 0.7965 1.78 1 41 LEU N 16.3986 0.4743 2.3 0.8 42 THR N 14.3796 0.719 . . 43 PHE N 14.2042 0.7373 . . 44 SER N 15.4 0.77 . . 45 ARG N 13.7743 0.7468 . . 46 LEU N 15.4375 1.0252 3.08 1.54 47 TYR N 16.1874 1.1577 4.05 1.51 48 GLU N 16.0665 0.8033 2.89 1.09 49 GLY N 15.5148 0.7757 . . 50 GLU N 15.1748 0.7587 . . 51 ALA N 15.1006 0.8256 2.57 1.15 52 ASP N 18.0135 0.9417 2.52 1.16 54 MET N 16.7184 1.0905 2.82 1.33 55 ILE N 17.5148 1.1662 4.36 1.53 56 SER N 18.458 0.931 3.55 1.25 57 PHE N 14.3663 1.0086 . . 58 ALA N 15.3314 0.7666 . . 59 VAL N 14.8817 0.7441 . . 60 ARG N 7.7283 1.4365 . . 61 GLU N 16.601 0.8822 2.7 1.36 62 HIS N 15.513 1.7044 4.05 2.2 63 GLY N 10.1184 1.5117 . . 64 ASP N 19.0319 1.1783 5.69 1.29 66 TYR N 16.4177 0.8788 1.93 1.11 69 ASP N 14.581 0.8241 . . 70 GLY N 17.4061 0.8867 1.84 1.24 72 GLY N 19.1712 1.6064 7.24 1.88 73 ASN N 14.9681 0.7484 . . 74 VAL N 15.5797 0.8872 2.04 1.12 75 LEU N 13.2574 1.4161 . . 76 ALA N 16.054 0.7912 2.04 1.08 77 HIS N 16.684 0.8279 1.37 1.06 78 ALA N 15.8966 0.112 1.21 0.98 79 TYR N 16.5846 0.0937 1.84 0.77 80 ALA N 17.9065 1.0429 3.46 1.35 82 GLY N 14.7689 0.7866 . . 84 GLY N 13.7372 0.9789 . . 85 ILE N 17.7056 1.6957 3.7 2.33 86 ASN N 18.0965 0.8129 2.6 1.16 87 GLY N 15.916 0.9646 3.61 1.56 88 ASP N 17.3104 0.8655 2.19 1.23 89 ALA N 15.3467 0.7673 . . 90 HIS N 14.9974 0.8966 . . 91 PHE N 16.4696 0.8047 2.22 1.16 92 ASP N 14.0426 0.8682 . . 93 ASP N 14.6162 1.046 . . 94 ASP N 14.619 0.9375 . . 95 GLU N 17.2818 0.8641 1.91 1.2 96 GLN N 14.523 0.3325 . . 97 TRP N 15.3831 0.5154 2.27 0.73 98 THR N 15.463 0.7831 . . 99 LYS N 19.1228 1.1133 5.52 1.54 100 ASP N 15.302 0.7857 . . 102 THR N 15.2341 0.6832 . . 103 GLY N 13.292 1.0949 . . 104 THR N 14.0963 0.4024 . . 105 ASN N 14.8689 1.0925 . . 106 LEU N 14.7484 0.9298 . . 107 PHE N 14.4888 0.9627 . . 108 LEU N 18.1032 0.9052 2.38 1.19 109 VAL N 16.9283 0.0717 1.85 0.61 110 ALA N 15.954 0.7937 . . 111 ALA N 17.3491 0.8675 1.82 1.1 112 HIS N 17.8265 0.8913 2.61 1.16 113 GLU N 15.3889 0.8817 . . 114 ILE N 16.2507 0.8785 . . 115 GLY N 16.0624 0.8169 . . 116 HIS N 17.5726 0.8786 3.69 1.14 118 LEU N 14.7385 0.8589 . . 120 LEU N 16.2944 0.9996 0.86 0.41 121 PHE N 18.086 0.9286 4.49 1.28 124 ALA N 15.8098 1.9397 . . 125 ASN N 15.5086 0.9674 . . 126 THR N 15.9968 0.7998 0.82 0.48 127 GLU N 15.4269 0.7713 . . 128 ALA N 10.599 0.4012 . . 129 LEU N 16.889 1.4216 2.24 1.49 131 TYR N 15.131 0.7682 . . 133 LEU N 15.781 0.8374 3.02 1.11 134 TYR N 14.957 0.8171 . . 135 HIS N 16.3398 0.8807 . . 137 LEU N 11.5784 0.5638 . . 140 LEU N 13.4953 1.0967 . . 141 THR N 15.017 0.7509 . . 142 ARG N 14.461 0.7148 . . 143 PHE N 13.906 0.7334 . . 144 ARG N 16.1747 0.5042 1.73 0.75 145 LEU N 14.0473 0.4024 . . 146 SER N 16.3263 0.097 1.68 0.84 147 GLN N 17.4016 1.2957 2.72 1.63 148 ASP N 16.3162 0.8183 1.87 1.09 150 ILE N 15.6162 1.13 . . 151 ASN N 16.1085 0.8054 . . 152 GLY N 15.196 0.6172 . . 153 ILE N 15.4441 0.8952 . . 154 GLN N 14.1547 0.8836 . . 155 SER N 17.054 0.8527 2.09 1.11 156 LEU N 15.193 0.9714 . . 157 TYR N 18.933 0.8594 7.88 1.31 158 GLY N 15.3127 0.58 2.76 0.78 162 ASP N 9.6111 0.4806 . . 163 SER N 17.0026 0.8501 1.92 1.05 165 GLU N 2.7786 0.1389 . . 166 THR N 1.6672 0.2128 . . stop_ save_ save_heteronuclear_NOE _Saveframe_category heteronuclear_NOE loop_ _Sample_label $sample stop_ _Sample_conditions_label $conditions _Spectrometer_frequency_1H 600 _Mol_system_component_name stromelysin _Atom_one_atom_name N _Atom_two_atom_name H _Heteronuclear_NOE_value_type 'relative intensities' _NOE_reference_value . _NOE_reference_description ; Simple relative intensities with and without NOE effect ; loop_ _Residue_seq_code _Residue_label _Heteronuclear_NOE_value _Heteronuclear_NOE_value_error 2 LYS 0.8227 0.134 3 TRP 0.7512 0.0636 5 LYS 0.6295 0.0315 6 THR 0.7961 0.1066 7 HIS 0.838 0.0419 8 LEU 0.8364 0.0418 9 THR 0.8512 0.1387 10 TYR 0.89 0.0445 11 ARG 0.7697 0.1011 12 ILE 0.8162 0.0686 13 VAL 0.7315 0.0519 14 ASN 0.8219 0.0411 15 TYR 0.8536 0.0427 18 ASP 0.8662 0.0481 19 LEU 0.8631 0.0432 21 LYS 0.797 0.0737 22 ASP 0.8305 0.0632 23 ALA 0.8241 0.1236 24 VAL 0.7785 0.0389 25 ASP 0.7539 0.0989 26 SER 0.868 0.0566 27 ALA 0.8132 0.0828 28 VAL 0.8258 0.0413 29 GLU 0.7165 0.07 30 LYS 0.8027 0.1096 31 ALA 0.8418 0.0714 32 LEU 0.8098 0.0405 33 LYS 0.7881 0.0581 34 VAL 0.8382 0.0419 35 TRP 0.8717 0.0684 36 GLU 0.8221 0.0411 37 GLU 0.8416 0.0582 38 VAL 0.7969 0.0398 39 THR 0.8662 0.0672 41 LEU 0.7021 0.0351 42 THR 0.855 0.0428 43 PHE 0.8397 0.0647 44 SER 0.8376 0.0598 45 ARG 0.8158 0.0849 46 LEU 0.8333 0.0524 47 TYR 0.8094 0.0731 48 GLU 0.796 0.0505 49 GLY 0.8039 0.0738 50 GLU 0.828 0.0878 51 ALA 0.7992 0.0546 52 ASP 0.7503 0.0653 54 MET 0.7623 0.0437 55 ILE 0.7682 0.0557 56 SER 0.7734 0.0614 57 PHE 0.7709 0.0699 58 ALA 0.8413 0.0775 59 VAL 0.7988 0.0694 60 ARG 0.863 0.0918 61 GLU 0.8182 0.0409 62 HIS 0.8474 0.066 63 GLY 0.8231 0.0412 64 ASP 0.8852 0.0459 66 TYR 0.7816 0.0391 69 ASP 0.6822 0.0702 70 GLY 0.8197 0.0479 72 GLY 0.8538 0.0921 73 ASN 0.8522 0.1067 74 VAL 0.8315 0.1416 75 LEU 0.8816 0.1025 76 ALA 0.8412 0.0452 77 HIS 0.9026 0.0851 78 ALA 0.717 0.029 79 TYR 0.796 0.068 80 ALA 0.7975 0.0439 82 GLY 0.8456 0.0591 84 GLY 0.8197 0.1133 85 ILE 0.8037 0.0506 86 ASN 0.8053 0.0652 87 GLY 0.8177 0.1287 88 ASP 0.8652 0.1042 89 ALA 0.7687 0.0384 90 HIS 0.7334 0.0715 91 PHE 0.8184 0.1098 92 ASP 0.8192 0.0512 93 ASP 0.8213 0.0657 94 ASP 0.8502 0.0774 95 GLU 0.7915 0.0822 96 GLN 0.7309 0.0365 97 TRP 0.7375 0.0502 98 THR 0.8428 0.0773 99 LYS 0.7955 0.0721 100 ASP 0.74 0.0867 102 THR 0.7301 0.0777 103 GLY 0.7808 0.0594 104 THR 0.6364 0.0856 105 ASN 0.7658 0.0717 106 LEU 0.7736 0.0429 107 PHE 0.8246 0.0413 108 LEU 0.925 0.0863 109 VAL 0.902 0.071 110 ALA 0.7514 0.0616 111 ALA 0.8556 0.0598 112 HIS 0.7646 0.1612 113 GLU 0.7993 0.0828 114 ILE 0.8005 0.0573 115 GLY 0.8311 0.0798 116 HIS 0.8785 0.0727 118 LEU 0.891 0.0759 120 LEU 0.8687 0.0643 121 PHE 0.723 0.0609 124 ALA 0.8173 0.1576 125 ASN 0.7721 0.0555 126 THR 0.8185 0.0659 127 GLU 0.8366 0.0457 128 ALA 0.6997 0.0425 129 LEU 0.8179 0.0539 131 TYR 0.891 0.0745 133 LEU 0.6404 0.0335 134 TYR 0.8444 0.1175 135 HIS 0.7305 0.1102 137 LEU 0.4032 0.0474 140 LEU 0.7533 0.0542 141 THR 0.79 0.0395 142 ARG 0.5428 0.073 143 PHE 0.6103 0.0443 144 ARG 0.6718 0.0473 145 LEU 0.6525 0.0298 146 SER 0.833 0.049 147 GLN 0.7586 0.0652 148 ASP 0.7656 0.0451 150 ILE 0.8198 0.0753 151 ASN 0.8661 0.1043 152 GLY 0.7903 0.0474 153 ILE 0.8075 0.0607 154 GLN 0.842 0.0749 155 SER 0.7915 0.0568 156 LEU 0.7572 0.0846 157 TYR 0.6151 0.0532 158 GLY 0.7724 0.0386 162 ASP 0.4402 0.022 163 SER 0.853 0.1516 165 GLU -0.7563 -0.0504 166 THR -1.6927 -0.07 stop_ save_ save_S2_parameters_label _Saveframe_category S2_parameters loop_ _Sample_label $sample stop_ _Sample_conditions_label $conditions _Mol_system_component_name stromelysin _Tau_e_value_units ps _Tau_s_value_units . loop_ _Residue_seq_code _Residue_label _Atom_name _Model_fit _S2_value _S2_value_fit_error _Tau_e_value _Tau_e_value_fit_error 2 LYS N . 0.911 0.043 . . 3 TRP N . 0.774 0.044 12.5 13.7 5 LYS N . 0.78 0.029 34.7 10.6 6 THR N . 0.761 0.04 . . 7 HIS N . 0.898 0.032 . . 8 LEU N . 0.851 0.037 . . 9 THR N . 0.789 0.044 . . 10 TYR N . 0.848 0.043 . . 11 ARG N . 0.949 0.047 . . 12 ILE N . 0.89 0.048 . . 13 VAL N . 0.725 0.032 12.2 6.7 14 ASN N . 0.893 0.043 . . 15 TYR N . 0.777 0.031 . . 18 ASP N . 0.95 0.033 . . 19 LEU N . 0.962 0.038 . . 21 LYS N . 0.949 0.019 . . 22 ASP N . 0.911 0.031 . . 23 ALA N . 0.866 0.044 . . 24 VAL N . 0.865 0.044 . . 25 ASP N . 0.881 0.045 . . 26 SER N . 0.871 0.045 . . 27 ALA N . 0.896 0.045 . . 28 VAL N . 0.936 0.032 . . 29 GLU N . 0.941 0.044 . . 30 LYS N . 0.903 0.044 . . 31 ALA N . 0.906 0.043 . . 32 LEU N . 0.816 0.039 . . 33 LYS N . 0.885 0.045 . . 34 VAL N . 0.833 0.043 . . 35 TRP N . 0.916 0.034 . . 36 GLU N . 0.865 0.043 . . 37 GLU N . 0.87 0.044 . . 38 VAL N . 0.877 0.042 . . 39 THR N . 0.94 0.044 . . 41 LEU N . 0.842 0.039 32.8 24 42 THR N . 0.798 0.028 . . 43 PHE N . 0.822 0.029 . . 44 SER N . 0.889 0.029 . . 45 ARG N . 0.819 0.031 . . 46 LEU N . 0.739 0.066 . . 47 TYR N . 0.726 0.056 . . 48 GLU N . 0.788 0.04 . . 49 GLY N . 0.889 0.031 . . 50 GLU N . 0.877 0.032 . . 51 ALA N . 0.75 0.048 . . 52 ASP N . 0.927 0.043 . . 54 MET N . 0.832 0.052 . . 55 ILE N . 0.787 0.054 . . 56 SER N . 0.892 0.044 . . 57 PHE N . 0.838 0.043 . . 58 ALA N . 0.901 0.034 . . 59 VAL N . 0.874 0.031 . . 60 ARG N . 0.514 0.079 . . 61 GLU N . 0.832 0.065 . . 62 HIS N . 0.686 0.09 . . 63 GLY N . 0.666 0.065 . . 64 ASP N . 0.798 0.038 . . 66 TYR N . 0.867 0.043 . . 69 ASP N . 0.811 0.037 25.9 18.3 70 GLY N . 0.931 0.055 . . 72 GLY N . 0.714 0.059 . . 73 ASN N . 0.848 0.031 . . 74 VAL N . 0.81 0.044 . . 75 LEU N . 0.767 0.061 . . 76 ALA N . 0.838 0.046 . . 77 HIS N . 0.916 0.047 . . 78 ALA N . 0.8784 0.0647 . . 79 TYR N . 0.8819 0.0459 . . 80 ALA N . 0.864 0.053 . . 82 GLY N . 0.924 0.037 . . 84 GLY N . 0.83 0.037 . . 85 ILE N . 0.838 0.092 . . 86 ASN N . 0.927 0.046 . . 87 GLY N . 0.736 0.076 . . 88 ASP N . 0.905 0.05 . . 89 ALA N . 0.915 0.032 . . 90 HIS N . 0.9 0.041 . . 91 PHE N . 0.852 0.05 . . 92 ASP N . 0.893 0.038 . . 93 ASP N . 0.921 0.042 . . 94 ASP N . 0.911 0.037 . . 95 GLU N . 0.919 0.049 . . 96 GLN N . 0.869 0.017 31.7 13.6 97 TRP N . 0.783 0.033 15.6 10.7 98 THR N . 0.912 0.033 . . 99 LYS N . 0.814 0.057 . . 100 ASP N . 0.931 0.032 . . 102 THR N . 0.921 0.039 . . 103 GLY N . 0.88 0.04 . . 104 THR N . 0.847 0.019 58.8 35.5 105 ASN N . 0.901 0.046 . . 106 LEU N . 0.897 0.037 . . 107 PHE N . 0.909 0.036 . . 108 LEU N . 0.941 0.044 . . 109 VAL N . 0.9022 0.0365 . . 110 ALA N . 0.93 0.032 . . 111 ALA N . 0.929 0.044 . . 112 HIS N . 0.91 0.045 . . 113 GLU N . 0.926 0.045 . . 114 ILE N . 0.936 0.035 . . 115 GLY N . 0.927 0.032 . . 116 HIS N . 0.83 0.041 . . 118 LEU N . 0.854 0.035 . . 120 LEU N . 0.95 0.046 . . 121 PHE N . 0.813 0.048 . . 124 ALA N . 0.787 0.069 . . 125 ASN N . 0.91 0.037 . . 126 THR N . 0.928 0.043 . . 127 GLU N . 0.92 0.033 . . 128 ALA N . 0.6 0.025 1968 584.2 129 LEU N . 0.876 0.043 . . 131 TYR N . 0.919 0.034 . . 133 LEU N . 0.761 0.042 29.6 12.5 134 TYR N . 0.922 0.034 . . 135 HIS N . 0.926 0.033 . . 137 LEU N . 0.679 0.042 573.4 200.6 140 LEU N . 0.795 0.053 . . 141 THR N . 0.924 0.034 . . 142 ARG N . 0.856 0.042 494.4 312.1 143 PHE N . 0.842 0.033 60.6 58.2 144 ARG N . 0.862 0.033 48.8 22.7 145 LEU N . 0.85 0.02 51.1 32.8 146 SER N . 0.8759 0.0515 . . 147 GLN N . 0.878 0.064 . . 148 ASP N . 0.864 0.047 . . 150 ILE N . 0.916 0.043 . . 151 ASN N . 0.94 0.031 . . 152 GLY N . 0.904 0.03 . . 153 ILE N . 0.934 0.035 . . 154 GLN N . 0.921 0.034 . . 155 SER N . 0.895 0.046 . . 156 LEU N . 0.86 0.039 . . 157 TYR N . 0.659 0.058 20.4 13.3 158 GLY N . 0.734 0.03 7.2 4.9 162 ASP N . 0.547 0.031 987.7 97.5 163 SER N . 0.902 0.045 . . 165 GLU N . 0.1 0.012 651.1 20.4 166 THR N . 0.044 0.015 424.7 19.1 stop_ save_