data_15396 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; SOLUTION STRUCTURE OF MATRIX METALLOPROTEINASE 3 (MMP-3) IN THE PRESENCE OF 3-4'-CYANOBYPHENYL-4-YLOXY)-N-HDYDROXYPROPIONAMIDE (MMP-3 INHIBITOR VII) ; _BMRB_accession_number 15396 _BMRB_flat_file_name bmr15396.str _Entry_type original _Submission_date 2007-07-20 _Accession_date 2007-07-20 _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 Alcaraz 'Luis A.' A. . 2 Banci Lucia . . 3 Bertini Ivano . . 4 Cantini Francesca . . 5 Donaire Antonio . . 6 Gonnelli Leonardo . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 150 "15N chemical shifts" 150 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2009-02-05 update BMRB 'Update residue code in entity' 2008-03-13 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 15395 'MMP-3 with MLC88' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Matrix metalloproteinase-inhibitor interaction: the solution structure of the catalytic domain of human matrix metalloproteinase-3 with different inhibitors. ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 17710450 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Alcaraz Luis A. . 2 Banci Lucia . . 3 Bertini Ivano . . 4 Cantini Francesca . . 5 Donaire Antonio . . 6 Gonnelli Leonardo . . stop_ _Journal_abbreviation 'J. Biol. Inorg. Chem.' _Journal_volume 12 _Journal_issue 8 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1197 _Page_last 1206 _Year 2007 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'MMP3 complex' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label MMP3 $MMP3 'ZINC ION 1' $ZN 'ZINC ION 2' $ZN 'CALCIUM ION 1' $CA 'CALCIUM ION 2' $CA stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_MMP3 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common MMP3 _Molecular_mass 18053.283 _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 161 _Mol_residue_sequence ; GIPKWRKTHLTYRIVNYTPD LPKDAVDSAVEKALKVWEEV TPLTFSRLYEGEADIMISFA VREHGDDYPFDGPGNVLAHA YAPGPGINGDAHFDDDEQWT KDTTGTNLFLVAAHEIGHSL GLFHSANTEALMYPLYHSLT DLTRFRLSQDDINGIQSLYG P ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 88 GLY 2 89 ILE 3 90 PRO 4 91 LYS 5 92 TRP 6 93 ARG 7 94 LYS 8 95 THR 9 96 HIS 10 97 LEU 11 98 THR 12 99 TYR 13 100 ARG 14 101 ILE 15 102 VAL 16 103 ASN 17 104 TYR 18 105 THR 19 106 PRO 20 107 ASP 21 108 LEU 22 109 PRO 23 110 LYS 24 111 ASP 25 112 ALA 26 113 VAL 27 114 ASP 28 115 SER 29 116 ALA 30 117 VAL 31 118 GLU 32 119 LYS 33 120 ALA 34 121 LEU 35 122 LYS 36 123 VAL 37 124 TRP 38 125 GLU 39 126 GLU 40 127 VAL 41 128 THR 42 129 PRO 43 130 LEU 44 131 THR 45 132 PHE 46 133 SER 47 134 ARG 48 135 LEU 49 136 TYR 50 137 GLU 51 138 GLY 52 139 GLU 53 140 ALA 54 141 ASP 55 142 ILE 56 143 MET 57 144 ILE 58 145 SER 59 146 PHE 60 147 ALA 61 148 VAL 62 149 ARG 63 150 GLU 64 151 HIS 65 152 GLY 66 153 ASP 67 154 ASP 68 155 TYR 69 156 PRO 70 157 PHE 71 158 ASP 72 159 GLY 73 160 PRO 74 161 GLY 75 162 ASN 76 163 VAL 77 164 LEU 78 165 ALA 79 166 HIS 80 167 ALA 81 168 TYR 82 169 ALA 83 170 PRO 84 171 GLY 85 172 PRO 86 173 GLY 87 174 ILE 88 175 ASN 89 176 GLY 90 177 ASP 91 178 ALA 92 179 HIS 93 180 PHE 94 181 ASP 95 182 ASP 96 183 ASP 97 184 GLU 98 185 GLN 99 186 TRP 100 187 THR 101 188 LYS 102 189 ASP 103 190 THR 104 191 THR 105 192 GLY 106 193 THR 107 194 ASN 108 195 LEU 109 196 PHE 110 197 LEU 111 198 VAL 112 199 ALA 113 200 ALA 114 201 HIS 115 202 GLU 116 203 ILE 117 204 GLY 118 205 HIS 119 206 SER 120 207 LEU 121 208 GLY 122 209 LEU 123 210 PHE 124 211 HIS 125 212 SER 126 213 ALA 127 214 ASN 128 215 THR 129 216 GLU 130 217 ALA 131 218 LEU 132 219 MET 133 220 TYR 134 221 PRO 135 222 LEU 136 223 TYR 137 224 HIS 138 225 SER 139 226 LEU 140 227 THR 141 228 ASP 142 229 LEU 143 230 THR 144 231 ARG 145 232 PHE 146 233 ARG 147 234 LEU 148 235 SER 149 236 GLN 150 237 ASP 151 238 ASP 152 239 ILE 153 240 ASN 154 241 GLY 155 242 ILE 156 243 GLN 157 244 SER 158 245 LEU 159 246 TYR 160 247 GLY 161 248 PRO stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-02-06 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 100.00 161 99.38 99.38 7.52e-113 BMRB 15395 MMP3 100.00 161 100.00 100.00 3.80e-114 BMRB 4173 STROMELYSIN-1 100.00 173 99.38 99.38 1.77e-112 BMRB 4364 stromelysin 98.76 166 98.74 98.74 3.76e-110 BMRB 4365 stromelysin 98.76 166 98.74 98.74 3.76e-110 BMRB 4366 stromelysin 98.76 166 98.74 98.74 3.76e-110 PDB 1B3D Stromelysin-1 100.00 173 99.38 99.38 1.77e-112 PDB 1B8Y "X-Ray Structure Of Human Stromelysin Catalytic Domain Complexed With Non-Peptide Inhibitors: Implications For Inhibitor Selecti" 100.00 167 99.38 99.38 1.51e-112 PDB 1BIW "Design And Synthesis Of Conformationally-Constrained Mmp Inhibitors" 100.00 173 99.38 99.38 1.77e-112 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 99.38 99.38 1.77e-112 PDB 1BQO "Discovery Of Potent, Achiral Matrix Metalloproteinase Inhibitors" 100.00 173 99.38 99.38 1.77e-112 PDB 1C3I "Human Stromelysin-1 Catalytic Domain Complexed With Ro-26-2812" 100.00 173 99.38 99.38 1.77e-112 PDB 1C8T "Human Stromelysin-1 (E202q) Catalytic Domain Complexed With Ro-26-2812" 100.00 167 98.76 99.38 6.46e-112 PDB 1CAQ "X-Ray Structure Of Human Stromelysin Catalytic Domain Complexes With Non-Peptide Inhibitors: Implication For Inhibitor Selectiv" 100.00 168 99.38 99.38 1.82e-112 PDB 1CIZ "X-ray Structure Of Human Stromelysin Catalytic Domain Complexes With Non-peptide Inhibitors: Implication For Inhibitor Selectiv" 100.00 168 99.38 99.38 1.82e-112 PDB 1CQR "Crystal Structure Of The Stromelysin Catalytic Domain At 2.0 A Resolution" 100.00 173 99.38 99.38 1.77e-112 PDB 1D5J "Crystal Structure Of Mmp3 Complexed With A Thiazepine Based Inhibitor." 100.00 173 99.38 99.38 1.77e-112 PDB 1D7X "Crystal Structure Of Mmp3 Complexed With A Modified Proline Scaffold Based Inhibitor." 100.00 173 99.38 99.38 1.77e-112 PDB 1D8F "Crystal Structure Of Mmp3 Complexed With A Piperazine Based Inhibitor." 100.00 173 99.38 99.38 1.77e-112 PDB 1D8M "Crystal Structure Of Mmp3 Complexed With A Heterocycle- Based Inhibitor" 100.00 173 99.38 99.38 1.77e-112 PDB 1G05 "Heterocycle-Based Mmp Inhibitor With P2'substituents" 100.00 173 99.38 99.38 1.77e-112 PDB 1G49 "A Carboxylic Acid Based Inhibitor In Complex With Mmp3" 100.00 173 99.38 99.38 1.77e-112 PDB 1G4K "X-ray Structure Of A Novel Matrix Metalloproteinase Inhibitor Complexed To Stromelysin" 100.00 168 99.38 99.38 1.82e-112 PDB 1HFS "Crystal Structure Of The Catalytic Domain Of Human Fibroblast Stromelysin-1 Inhibited With The N-Carboxy-Alkyl Inhibitor L-764," 99.38 160 99.38 99.38 6.54e-112 PDB 1HY7 "A Carboxylic Acid Based Inhibitor In Complex With Mmp3" 100.00 173 99.38 99.38 1.77e-112 PDB 1OO9 "Orientation In Solution Of Mmp-3 Catalytic Domain And N- Timp-1 From Residual Dipolar Couplings" 100.00 168 99.38 99.38 1.82e-112 PDB 1QIA "Crystal Structure Of Stromelysin Catalytic Domain" 99.38 162 99.38 99.38 8.34e-112 PDB 1QIC "Crystal Structure Of Stromelysin Catalytic Domain" 99.38 161 99.38 99.38 7.22e-112 PDB 1SLM "Crystal Structure Of Fibroblast Stromelysin-1: The C-Truncated Human Proenzyme" 100.00 255 99.38 99.38 3.29e-112 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 99.38 99.38 1.77e-112 PDB 1UEA "Mmp-3TIMP-1 Complex" 100.00 173 98.14 98.14 3.08e-110 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 99.38 99.38 2.31e-112 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 99.38 99.38 2.31e-112 PDB 1USN "Crystal Structure Of The Catalytic Domain Of Human Fibroblast Stromelysin-1 Inhibited With Thiadiazole Inhibitor Pnu-142372" 99.38 165 99.38 99.38 8.46e-112 PDB 2D1O "Stromelysin-1 (Mmp-3) Complexed To A Hydroxamic Acid Inhibitor" 100.00 171 99.38 99.38 2.02e-112 PDB 2JNP "Solution Structure Of Matrix Metalloproteinase 3 (Mmp-3) In The Presence Of N-Isobutyl-N-[4- Methoxyphenylsulfonyl]glycyl Hydro" 100.00 161 99.38 99.38 7.52e-113 PDB 2JT5 "Solution Structure Of Matrix Metalloproteinase 3 (mmp-3) In The Presence Of N-hydroxy-2-[n-(2-hydroxyethyl)biphenyl-4- Sulfonam" 100.00 161 99.38 99.38 7.52e-113 PDB 2JT6 "Solution Structure Of Matrix Metalloproteinase 3 (Mmp-3) In The Presence Of 3-4'-Cyanobyphenyl-4-Yloxy)-N- Hdydroxypropionamide" 100.00 161 99.38 99.38 7.52e-113 PDB 2SRT "Catalytic Domain Of Human Stromelysin-1 At Ph 5.5 And 40oc Complexed With Inhibitor" 100.00 173 99.38 99.38 1.77e-112 PDB 2USN "Crystal Structure Of The Catalytic Domain Of Human Fibroblast Stromelysin-1 Inhibited With Thiadiazole Inhibitor Pnu-141803" 99.38 165 99.38 99.38 8.46e-112 PDB 3OHL "Catalytic Domain Of Stromelysin-1 In Complex With N-Hydroxy-2-(4- Methoxy-N-(Pyridine-3-Ylmethyl)phenylsulfonamido)acetamide" 100.00 167 99.38 99.38 1.51e-112 PDB 3OHO "Catalytic Domain Of Stromelysin-1 In Complex With N-Hydroxy-2-(4- Methylphenylsulfonamido)acetamide" 100.00 169 99.38 99.38 2.29e-112 PDB 3USN "Structure Of The Catalytic Domain Of Human Fibroblast Stromelysin-1 Inhibited With The Thiadiazole Inhibitor Ipnu-107859, Nmr, " 100.00 168 99.38 99.38 1.82e-112 PDB 4DPE "Structure Of Mmp3 Complexed With A Platinum-based Inhibitor." 100.00 173 99.38 99.38 1.77e-112 PDB 4G9L "Structure Of Mmp3 Complexed With Nngh Inhibitor" 100.00 173 99.38 99.38 1.77e-112 PDB 4JA1 "Structure Of Mmp3 Complexed With A Platinum-based Inhibitor" 100.00 173 99.38 99.38 1.77e-112 DBJ BAD97003 "matrix metalloproteinase 3 preproprotein variant [Homo sapiens]" 100.00 477 99.38 99.38 1.76e-109 DBJ BAD97011 "matrix metalloproteinase 3 preproprotein variant [Homo sapiens]" 100.00 477 99.38 99.38 1.76e-109 DBJ BAG36115 "unnamed protein product [Homo sapiens]" 100.00 477 99.38 99.38 1.56e-109 EMBL CAA28859 "preprostromelysin [Homo sapiens]" 100.00 477 99.38 99.38 1.56e-109 GB AAA00036 "prostromelysin=matrix metalloproteinase [human, Peptide, 477 aa]" 100.00 477 99.38 99.38 1.76e-109 GB AAA36321 "matrix metalloproteinase-3 [Homo sapiens]" 100.00 477 99.38 99.38 1.76e-109 GB AAB36942 "stromelysin [Homo sapiens]" 100.00 477 99.38 99.38 1.76e-109 GB AAD45887 "stromelysin catalytic domain [synthetic construct]" 100.00 174 99.38 99.38 2.31e-112 GB AAH69676 "Matrix metallopeptidase 3 (stromelysin 1, progelatinase) [Homo sapiens]" 100.00 477 99.38 99.38 1.76e-109 REF NP_002413 "stromelysin-1 preproprotein [Homo sapiens]" 100.00 477 99.38 99.38 1.56e-109 REF XP_002822450 "PREDICTED: stromelysin-1 [Pongo abelii]" 100.00 477 98.76 99.38 2.07e-109 REF XP_003253099 "PREDICTED: stromelysin-1 [Nomascus leucogenys]" 100.00 477 98.76 99.38 1.55e-109 REF XP_003828425 "PREDICTED: stromelysin-1 [Pan paniscus]" 100.00 477 99.38 99.38 1.36e-109 REF XP_004052086 "PREDICTED: stromelysin-1 [Gorilla gorilla gorilla]" 100.00 477 98.14 98.76 4.16e-108 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 99.38 99.38 1.56e-109 stop_ save_ ############# # Ligands # ############# save_ZN _Saveframe_category ligand _Mol_type non-polymer _Name_common "ZN (ZINC ION)" _BMRB_code . _PDB_code ZN _Molecular_mass 65.409 _Mol_charge 2 _Mol_paramagnetic . _Mol_aromatic . _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Fri Jun 22 03:38:33 2007 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons ZN ZN ZN N 2 . ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ save_CA _Saveframe_category ligand _Mol_type non-polymer _Name_common "CA (CALCIUM ION)" _BMRB_code . _PDB_code CA _Molecular_mass 40.078 _Mol_charge 2 _Mol_paramagnetic . _Mol_aromatic . _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Thu Jun 21 18:50:00 2007 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons CA CA CA N 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 $MMP3 Human 9606 Eukaryota Metazoa Homo sapiens stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name $MMP3 'recombinant technology' . Escherichia coli BL21(DE3) pET21A stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $MMP3 1 mM '[U-98% 15N]' H2O 90 % . D2O 10 % . stop_ save_ ############################ # Computer software used # ############################ save_X-PLOR_NIH _Saveframe_category software _Name 'X-PLOR NIH' _Version . loop_ _Vendor _Address _Electronic_address 'Schwieters, Kuszewski, Tjandra and Clore' . . stop_ loop_ _Task refinement stop_ _Details . save_ save_AUTODOCK _Saveframe_category software _Name AUTODOCK _Version 3.0 loop_ _Vendor _Address _Electronic_address 'Morris, Goodsell, Huey, Lindstorm, Hart, Kurowski, Halliday, Belew, Olson' . . stop_ loop_ _Task refinement stop_ _Details . save_ save_SPARKY _Saveframe_category software _Name SPARKY _Version . loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'data analysis' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 900 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_3D_1H-15N_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 300 . mM pH 8 . pH pressure 1 . atm temperature 298 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio dioxane C 13 'methyl carbon' ppm 69.3 external direct . . . 1.0 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 . indirect . . . 0.101329118 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_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Software_label $SPARKY $X-PLOR_NIH stop_ loop_ _Experiment_label '2D 1H-15N HSQC' '3D 1H-15N NOESY' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name MMP3 _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 89 2 ILE H H 8.49 . . 2 89 2 ILE N N 115.85 . . 3 91 4 LYS H H 7.01 . . 4 91 4 LYS N N 111.92 . . 5 92 5 TRP H H 8.09 . . 6 92 5 TRP N N 124.80 . . 7 93 6 ARG H H 7.96 . . 8 93 6 ARG N N 119.51 . . 9 94 7 LYS H H 7.43 . . 10 94 7 LYS N N 116.88 . . 11 95 8 THR H H 7.96 . . 12 95 8 THR N N 105.59 . . 13 96 9 HIS H H 6.99 . . 14 96 9 HIS N N 120.20 . . 15 97 10 LEU H H 8.12 . . 16 97 10 LEU N N 127.83 . . 17 98 11 THR H H 9.21 . . 18 98 11 THR N N 110.68 . . 19 99 12 TYR H H 8.55 . . 20 99 12 TYR N N 117.49 . . 21 100 13 ARG H H 8.16 . . 22 100 13 ARG N N 119.42 . . 23 101 14 ILE H H 8.32 . . 24 101 14 ILE N N 128.17 . . 25 102 15 VAL H H 9.48 . . 26 102 15 VAL N N 129.72 . . 27 103 16 ASN H H 7.58 . . 28 103 16 ASN N N 116.08 . . 29 104 17 TYR H H 7.93 . . 30 104 17 TYR N N 111.36 . . 31 105 18 THR H H 8.47 . . 32 105 18 THR N N 109.23 . . 33 107 20 ASP H H 8.75 . . 34 107 20 ASP N N 121.64 . . 35 108 21 LEU H H 6.88 . . 36 108 21 LEU N N 116.17 . . 37 110 23 LYS H H 8.56 . . 38 110 23 LYS N N 123.63 . . 39 111 24 ASP H H 8.44 . . 40 111 24 ASP N N 113.75 . . 41 112 25 ALA H H 7.21 . . 42 112 25 ALA N N 122.31 . . 43 113 26 VAL H H 7.46 . . 44 113 26 VAL N N 121.82 . . 45 114 27 ASP H H 8.46 . . 46 114 27 ASP N N 119.39 . . 47 115 28 SER H H 7.97 . . 48 115 28 SER N N 112.58 . . 49 116 29 ALA H H 7.61 . . 50 116 29 ALA N N 124.02 . . 51 117 30 VAL H H 7.93 . . 52 117 30 VAL N N 115.96 . . 53 118 31 GLU H H 8.28 . . 54 118 31 GLU N N 118.05 . . 55 119 32 LYS H H 8.22 . . 56 119 32 LYS N N 118.94 . . 57 120 33 ALA H H 7.97 . . 58 120 33 ALA N N 123.08 . . 59 121 34 LEU H H 7.57 . . 60 121 34 LEU N N 115.23 . . 61 122 35 LYS H H 7.73 . . 62 122 35 LYS N N 118.78 . . 63 123 36 VAL H H 7.34 . . 64 123 36 VAL N N 115.29 . . 65 124 37 TRP H H 6.53 . . 66 124 37 TRP N N 117.00 . . 67 125 38 GLU H H 8.69 . . 68 125 38 GLU N N 122.09 . . 69 126 39 GLU H H 7.63 . . 70 126 39 GLU N N 112.77 . . 71 127 40 VAL H H 6.97 . . 72 127 40 VAL N N 106.14 . . 73 128 41 THR H H 7.25 . . 74 128 41 THR N N 108.91 . . 75 130 43 LEU H H 7.19 . . 76 130 43 LEU N N 118.32 . . 77 131 44 THR H H 7.98 . . 78 131 44 THR N N 110.45 . . 79 132 45 PHE H H 8.11 . . 80 132 45 PHE N N 117.17 . . 81 133 46 SER H H 8.60 . . 82 133 46 SER N N 116.46 . . 83 134 47 ARG H H 8.51 . . 84 134 47 ARG N N 125.15 . . 85 135 48 LEU H H 8.21 . . 86 135 48 LEU N N 126.05 . . 87 136 49 TYR H H 9.17 . . 88 136 49 TYR N N 118.87 . . 89 137 50 GLU H H 7.41 . . 90 137 50 GLU N N 116.52 . . 91 138 51 GLY H H 8.46 . . 92 138 51 GLY N N 108.37 . . 93 139 52 GLU H H 8.13 . . 94 139 52 GLU N N 118.96 . . 95 140 53 ALA H H 7.98 . . 96 140 53 ALA N N 131.38 . . 97 141 54 ASP H H 8.26 . . 98 141 54 ASP N N 121.90 . . 99 142 55 ILE H H 8.45 . . 100 142 55 ILE N N 123.39 . . 101 143 56 MET H H 7.13 . . 102 143 56 MET N N 126.40 . . 103 144 57 ILE H H 9.15 . . 104 144 57 ILE N N 128.35 . . 105 145 58 SER H H 8.49 . . 106 145 58 SER N N 118.25 . . 107 146 59 PHE H H 9.57 . . 108 146 59 PHE N N 119.91 . . 109 147 60 ALA H H 9.21 . . 110 147 60 ALA N N 125.00 . . 111 148 61 VAL H H 8.15 . . 112 148 61 VAL N N 111.65 . . 113 149 62 ARG H H 9.53 . . 114 149 62 ARG N N 117.49 . . 115 150 63 GLU H H 7.47 . . 116 150 63 GLU N N 124.38 . . 117 151 64 HIS H H 9.29 . . 118 151 64 HIS N N 123.75 . . 119 152 65 GLY H H 8.06 . . 120 152 65 GLY N N 108.79 . . 121 153 66 ASP H H 6.81 . . 122 153 66 ASP N N 115.56 . . 123 154 67 ASP H H 7.78 . . 124 154 67 ASP N N 115.56 . . 125 155 68 TYR H H 6.98 . . 126 155 68 TYR N N 117.78 . . 127 157 70 PHE H H 8.48 . . 128 157 70 PHE N N 122.58 . . 129 158 71 ASP H H 7.89 . . 130 158 71 ASP N N 115.70 . . 131 159 72 GLY H H 8.79 . . 132 159 72 GLY N N 110.26 . . 133 161 74 GLY H H 11.33 . . 134 161 74 GLY N N 119.67 . . 135 162 75 ASN H H 8.76 . . 136 162 75 ASN N N 117.32 . . 137 163 76 VAL H H 10.15 . . 138 163 76 VAL N N 128.54 . . 139 164 77 LEU H H 8.62 . . 140 164 77 LEU N N 123.41 . . 141 165 78 ALA H H 7.50 . . 142 165 78 ALA N N 114.35 . . 143 166 79 HIS H H 9.35 . . 144 166 79 HIS N N 116.67 . . 145 167 80 ALA H H 8.00 . . 146 167 80 ALA N N 121.68 . . 147 168 81 TYR H H 8.02 . . 148 168 81 TYR N N 123.83 . . 149 169 82 ALA H H 7.45 . . 150 169 82 ALA N N 119.58 . . 151 171 84 GLY H H 6.27 . . 152 171 84 GLY N N 110.43 . . 153 173 86 GLY H H 8.69 . . 154 173 86 GLY N N 109.51 . . 155 174 87 ILE H H 8.90 . . 156 174 87 ILE N N 131.86 . . 157 175 88 ASN H H 7.11 . . 158 175 88 ASN N N 118.08 . . 159 176 89 GLY H H 8.04 . . 160 176 89 GLY N N 120.34 . . 161 177 90 ASP H H 7.77 . . 162 177 90 ASP N N 123.88 . . 163 178 91 ALA H H 8.18 . . 164 178 91 ALA N N 122.46 . . 165 179 92 HIS H H 9.13 . . 166 179 92 HIS N N 120.67 . . 167 180 93 PHE H H 8.77 . . 168 180 93 PHE N N 123.29 . . 169 181 94 ASP H H 8.13 . . 170 181 94 ASP N N 121.81 . . 171 182 95 ASP H H 9.79 . . 172 182 95 ASP N N 128.11 . . 173 183 96 ASP H H 9.15 . . 174 183 96 ASP N N 123.41 . . 175 184 97 GLU H H 7.14 . . 176 184 97 GLU N N 115.81 . . 177 185 98 GLN H H 8.40 . . 178 185 98 GLN N N 126.07 . . 179 186 99 TRP H H 9.45 . . 180 186 99 TRP N N 130.70 . . 181 187 100 THR H H 8.76 . . 182 187 100 THR N N 111.08 . . 183 188 101 LYS H H 9.02 . . 184 188 101 LYS N N 119.74 . . 185 189 102 ASP H H 7.42 . . 186 189 102 ASP N N 120.55 . . 187 190 103 THR H H 7.71 . . 188 190 103 THR N N 127.23 . . 189 191 104 THR H H 8.14 . . 190 191 104 THR N N 114.74 . . 191 192 105 GLY H H 7.31 . . 192 192 105 GLY N N 111.65 . . 193 193 106 THR H H 8.56 . . 194 193 106 THR N N 123.91 . . 195 194 107 ASN H H 8.14 . . 196 194 107 ASN N N 127.01 . . 197 195 108 LEU H H 7.95 . . 198 195 108 LEU N N 127.43 . . 199 196 109 PHE H H 8.47 . . 200 196 109 PHE N N 120.11 . . 201 197 110 LEU H H 8.67 . . 202 197 110 LEU N N 120.25 . . 203 198 111 VAL H H 7.12 . . 204 198 111 VAL N N 111.37 . . 205 199 112 ALA H H 9.66 . . 206 199 112 ALA N N 122.91 . . 207 200 113 ALA H H 8.84 . . 208 200 113 ALA N N 119.61 . . 209 201 114 HIS H H 7.79 . . 210 201 114 HIS N N 119.36 . . 211 202 115 GLU H H 9.14 . . 212 202 115 GLU N N 116.77 . . 213 203 116 ILE H H 8.91 . . 214 203 116 ILE N N 117.75 . . 215 204 117 GLY H H 7.47 . . 216 204 117 GLY N N 107.97 . . 217 205 118 HIS H H 7.06 . . 218 205 118 HIS N N 119.70 . . 219 206 119 SER H H 8.17 . . 220 206 119 SER N N 119.05 . . 221 207 120 LEU H H 7.79 . . 222 207 120 LEU N N 115.10 . . 223 208 121 GLY H H 8.35 . . 224 208 121 GLY N N 109.43 . . 225 209 122 LEU H H 8.79 . . 226 209 122 LEU N N 122.23 . . 227 210 123 PHE H H 8.44 . . 228 210 123 PHE N N 124.87 . . 229 211 124 HIS H H 5.24 . . 230 211 124 HIS N N 106.93 . . 231 212 125 SER H H 6.75 . . 232 212 125 SER N N 110.94 . . 233 213 126 ALA H H 8.68 . . 234 213 126 ALA N N 126.77 . . 235 214 127 ASN H H 8.78 . . 236 214 127 ASN N N 120.62 . . 237 215 128 THR H H 8.04 . . 238 215 128 THR N N 117.24 . . 239 216 129 GLU H H 8.60 . . 240 216 129 GLU N N 120.86 . . 241 217 130 ALA H H 7.83 . . 242 217 130 ALA N N 123.02 . . 243 218 131 LEU H H 11.51 . . 244 218 131 LEU N N 131.85 . . 245 219 132 MET H H 8.18 . . 246 219 132 MET N N 114.54 . . 247 220 133 TYR H H 8.07 . . 248 220 133 TYR N N 128.41 . . 249 222 135 LEU H H 7.52 . . 250 222 135 LEU N N 120.19 . . 251 223 136 TYR H H 9.02 . . 252 223 136 TYR N N 127.85 . . 253 224 137 HIS H H 8.13 . . 254 224 137 HIS N N 127.46 . . 255 225 138 SER H H 7.67 . . 256 225 138 SER N N 118.76 . . 257 226 139 LEU H H 7.75 . . 258 226 139 LEU N N 121.72 . . 259 227 140 THR H H 7.91 . . 260 227 140 THR N N 121.63 . . 261 228 141 ASP H H 7.92 . . 262 228 141 ASP N N 123.70 . . 263 229 142 LEU H H 8.85 . . 264 229 142 LEU N N 125.81 . . 265 230 143 THR H H 8.34 . . 266 230 143 THR N N 111.37 . . 267 231 144 ARG H H 7.39 . . 268 231 144 ARG N N 119.29 . . 269 232 145 PHE H H 7.30 . . 270 232 145 PHE N N 120.80 . . 271 233 146 ARG H H 7.08 . . 272 233 146 ARG N N 126.48 . . 273 234 147 LEU H H 8.43 . . 274 234 147 LEU N N 122.47 . . 275 235 148 SER H H 8.71 . . 276 235 148 SER N N 118.63 . . 277 236 149 GLN H H 9.03 . . 278 236 149 GLN N N 122.13 . . 279 237 150 ASP H H 8.10 . . 280 237 150 ASP N N 118.12 . . 281 238 151 ASP H H 8.00 . . 282 238 151 ASP N N 117.93 . . 283 239 152 ILE H H 8.03 . . 284 239 152 ILE N N 119.45 . . 285 240 153 ASN H H 9.06 . . 286 240 153 ASN N N 118.31 . . 287 241 154 GLY H H 8.18 . . 288 241 154 GLY N N 108.17 . . 289 242 155 ILE H H 8.49 . . 290 242 155 ILE N N 123.58 . . 291 243 156 GLN H H 8.18 . . 292 243 156 GLN N N 120.83 . . 293 244 157 SER H H 7.97 . . 294 244 157 SER N N 117.21 . . 295 245 158 LEU H H 6.69 . . 296 245 158 LEU N N 118.23 . . 297 246 159 TYR H H 7.57 . . 298 246 159 TYR N N 113.08 . . 299 247 160 GLY H H 8.25 . . 300 247 160 GLY N N 109.99 . . stop_ save_