data_5153 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone dynamics of the N-TIMP-1 bound to MMP-3 catalytic domain ; _BMRB_accession_number 5153 _BMRB_flat_file_name bmr5153.str _Entry_type original _Submission_date 2001-09-16 _Accession_date 2001-09-17 _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 Gao Guanghua . . 2 Arumugam Sengodagounder . . 3 'Van Doren' Steven R. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count S2_parameters 1 T1_relaxation 1 T2_relaxation 1 heteronucl_NOE 1 stop_ loop_ _Data_type _Data_type_count "T1 relaxation values" 85 "T2 relaxation values" 85 "order parameters" 86 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2003-01-29 update author 'update of the S2 and rex values' 2002-02-04 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 5154 'N-terminal domain of Tissue Inhibitor of Metalloproteinases-1' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Binding of the MMP-3 catalytic domain to N-TIMP-1 is driven by a large gain in entropy that includes modest contributions from the hydrophobic effect and the TIMP-1 backbone ; _Citation_status 'in press' _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Gao Guanghua . . 2 Arumugam Sengodagounder . . 3 Patton Brian . . 4 Semenchenko Valentyna . . 5 Brew Keith . . 6 'Van Doren' Steven R. . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_volume . _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first . _Page_last . _Year . _Details . save_ ################################## # Molecular system description # ################################## save_system_N-TIMP-1_MMP-3(deltaC)_complex _Saveframe_category molecular_system _Mol_system_name 'N-terminal domain of Tissue Inhibitor of Metalloproteinases-1/MatrixMetalloProteinase-3(E202Q)(deltaC) complex' _Abbreviation_common 'N-TIMP-1/MMP-3(deltaC) complex' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'N-TIMP-1, inhibitor' $N-TIMP-1 'MMP-3, metalloproteinase' $MMP-3 'CALCIUM (II) ION, I' $CA 'CALCIUM (II) ION, II' $CA 'CALCIUM (II) ION, III' $CA 'ZINC (II) ION, I' $ZN 'ZINC (II) ION, II' $ZN stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all disulfide bound' loop_ _Biological_function 'N-TIMP-1 inhibits the enzymatic activity of matrix metalloproteinases-1,-2, &-3 with Ki values less than 2.0 nM' stop_ _Database_query_date . _Details ; Present system is contains only the N-terminal domain of the Tissue Inhibitor of Metalloproteinase where as the related system in the X-ray structure (PDB entry 1UEA) has a full length. In addtion, the present system has been studied in solution as a complex with a mutant matrix metalloproteinase-3(E202Q). ; save_ ######################## # Monomeric polymers # ######################## save_N-TIMP-1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'N-terminal domain of Tissue Inhibitor of Metalloproteinases-1' _Abbreviation_common N-TIMP-1 _Molecular_mass . _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 126 _Mol_residue_sequence ; CTCVPPHPQTAFCNSDLVIR AKFVGTPEVNQTTLYQRYEI KMTKMYKGFQALGDAADIRF VYTPAMESVCGYFHRSHNRS EEFLIAGKLQDGLLHITTCS FVAPWNSLSLAQRRGFTKTY TVGCEE ; loop_ _Residue_seq_code _Residue_label 1 CYS 2 THR 3 CYS 4 VAL 5 PRO 6 PRO 7 HIS 8 PRO 9 GLN 10 THR 11 ALA 12 PHE 13 CYS 14 ASN 15 SER 16 ASP 17 LEU 18 VAL 19 ILE 20 ARG 21 ALA 22 LYS 23 PHE 24 VAL 25 GLY 26 THR 27 PRO 28 GLU 29 VAL 30 ASN 31 GLN 32 THR 33 THR 34 LEU 35 TYR 36 GLN 37 ARG 38 TYR 39 GLU 40 ILE 41 LYS 42 MET 43 THR 44 LYS 45 MET 46 TYR 47 LYS 48 GLY 49 PHE 50 GLN 51 ALA 52 LEU 53 GLY 54 ASP 55 ALA 56 ALA 57 ASP 58 ILE 59 ARG 60 PHE 61 VAL 62 TYR 63 THR 64 PRO 65 ALA 66 MET 67 GLU 68 SER 69 VAL 70 CYS 71 GLY 72 TYR 73 PHE 74 HIS 75 ARG 76 SER 77 HIS 78 ASN 79 ARG 80 SER 81 GLU 82 GLU 83 PHE 84 LEU 85 ILE 86 ALA 87 GLY 88 LYS 89 LEU 90 GLN 91 ASP 92 GLY 93 LEU 94 LEU 95 HIS 96 ILE 97 THR 98 THR 99 CYS 100 SER 101 PHE 102 VAL 103 ALA 104 PRO 105 TRP 106 ASN 107 SER 108 LEU 109 SER 110 LEU 111 ALA 112 GLN 113 ARG 114 ARG 115 GLY 116 PHE 117 THR 118 LYS 119 THR 120 TYR 121 THR 122 VAL 123 GLY 124 CYS 125 GLU 126 GLU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2014-10-26 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 99.38 100.00 1.71e-113 BMRB 15395 MMP3 93.06 161 98.76 99.38 4.11e-112 BMRB 15396 MMP3 93.06 161 98.76 99.38 4.11e-112 BMRB 4173 SLN 100.00 173 99.42 100.00 6.94e-123 BMRB 4364 stromelysin 95.95 166 98.80 99.40 3.14e-116 BMRB 4365 stromelysin 95.95 166 98.80 99.40 3.14e-116 BMRB 4366 stromelysin 95.95 166 98.80 99.40 3.14e-116 BMRB 5099 MMP-3 100.00 173 100.00 100.00 1.52e-123 BMRB 5231 stromelysin 100.00 173 99.42 100.00 6.94e-123 PDB 1B3D Stromelysin-1 100.00 173 99.42 100.00 6.94e-123 PDB 1B8Y "X-Ray Structure Of Human Stromelysin Catalytic Domain Complexed With Non-Peptide Inhibitors: Implications For Inhibitor Selecti" 96.53 167 99.40 100.00 1.91e-118 PDB 1BIW "Design And Synthesis Of Conformationally-Constrained Mmp Inhibitors" 100.00 173 99.42 100.00 6.94e-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 99.42 100.00 6.94e-123 PDB 1BQO "Discovery Of Potent, Achiral Matrix Metalloproteinase Inhibitors" 100.00 173 99.42 100.00 6.94e-123 PDB 1C3I "Human Stromelysin-1 Catalytic Domain Complexed With Ro-26-2812" 100.00 173 99.42 100.00 6.94e-123 PDB 1C8T "Human Stromelysin-1 (E202q) Catalytic Domain Complexed With Ro-26-2812" 95.95 167 100.00 100.00 5.22e-118 PDB 1CAQ "X-Ray Structure Of Human Stromelysin Catalytic Domain Complexes With Non-Peptide Inhibitors: Implication For Inhibitor Selectiv" 97.11 168 99.40 100.00 2.86e-119 PDB 1CIZ "X-ray Structure Of Human Stromelysin Catalytic Domain Complexes With Non-peptide Inhibitors: Implication For Inhibitor Selectiv" 97.11 168 99.40 100.00 2.86e-119 PDB 1CQR "Crystal Structure Of The Stromelysin Catalytic Domain At 2.0 A Resolution" 100.00 173 99.42 100.00 6.94e-123 PDB 1D5J "Crystal Structure Of Mmp3 Complexed With A Thiazepine Based Inhibitor." 100.00 173 99.42 100.00 6.94e-123 PDB 1D7X "Crystal Structure Of Mmp3 Complexed With A Modified Proline Scaffold Based Inhibitor." 100.00 173 99.42 100.00 6.94e-123 PDB 1D8F "Crystal Structure Of Mmp3 Complexed With A Piperazine Based Inhibitor." 100.00 173 99.42 100.00 6.94e-123 PDB 1D8M "Crystal Structure Of Mmp3 Complexed With A Heterocycle- Based Inhibitor" 100.00 173 99.42 100.00 6.94e-123 PDB 1G05 "Heterocycle-Based Mmp Inhibitor With P2'substituents" 100.00 173 99.42 100.00 6.94e-123 PDB 1G49 "A Carboxylic Acid Based Inhibitor In Complex With Mmp3" 100.00 173 99.42 100.00 6.94e-123 PDB 1G4K "X-ray Structure Of A Novel Matrix Metalloproteinase Inhibitor Complexed To Stromelysin" 97.11 168 99.40 100.00 2.86e-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 99.38 100.00 1.17e-112 PDB 1HY7 "A Carboxylic Acid Based Inhibitor In Complex With Mmp3" 100.00 173 99.42 100.00 6.94e-123 PDB 1OO9 "Orientation In Solution Of Mmp-3 Catalytic Domain And N- Timp-1 From Residual Dipolar Couplings" 97.11 168 99.40 100.00 2.86e-119 PDB 1QIA "Crystal Structure Of Stromelysin Catalytic Domain" 93.64 162 99.38 100.00 2.29e-114 PDB 1QIC "Crystal Structure Of Stromelysin Catalytic Domain" 93.06 161 99.38 100.00 1.45e-113 PDB 1SLM "Crystal Structure Of Fibroblast Stromelysin-1: The C-Truncated Human Proenzyme" 100.00 255 99.42 100.00 5.45e-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 99.42 100.00 6.94e-123 PDB 1UEA "Mmp-3TIMP-1 Complex" 100.00 173 98.27 98.84 9.00e-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 99.42 100.00 7.59e-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 99.42 100.00 7.59e-123 PDB 1USN "Crystal Structure Of The Catalytic Domain Of Human Fibroblast Stromelysin-1 Inhibited With Thiadiazole Inhibitor Pnu-142372" 95.38 165 99.39 100.00 8.36e-117 PDB 2D1O "Stromelysin-1 (Mmp-3) Complexed To A Hydroxamic Acid Inhibitor" 98.84 171 99.42 100.00 1.88e-121 PDB 2JNP "Solution Structure Of Matrix Metalloproteinase 3 (Mmp-3) In The Presence Of N-Isobutyl-N-[4- Methoxyphenylsulfonyl]glycyl Hydro" 93.06 161 99.38 100.00 1.71e-113 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 99.38 100.00 1.71e-113 PDB 2JT6 "Solution Structure Of Matrix Metalloproteinase 3 (Mmp-3) In The Presence Of 3-4'-Cyanobyphenyl-4-Yloxy)-N- Hdydroxypropionamide" 93.06 161 99.38 100.00 1.71e-113 PDB 2SRT "Catalytic Domain Of Human Stromelysin-1 At Ph 5.5 And 40oc Complexed With Inhibitor" 100.00 173 99.42 100.00 6.94e-123 PDB 2USN "Crystal Structure Of The Catalytic Domain Of Human Fibroblast Stromelysin-1 Inhibited With Thiadiazole Inhibitor Pnu-141803" 95.38 165 99.39 100.00 8.36e-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 99.40 100.00 1.91e-118 PDB 3OHO "Catalytic Domain Of Stromelysin-1 In Complex With N-Hydroxy-2-(4- Methylphenylsulfonamido)acetamide" 97.69 169 99.41 100.00 6.26e-120 PDB 3USN "Structure Of The Catalytic Domain Of Human Fibroblast Stromelysin-1 Inhibited With The Thiadiazole Inhibitor Ipnu-107859, Nmr, " 97.11 168 99.40 100.00 2.86e-119 PDB 4DPE "Structure Of Mmp3 Complexed With A Platinum-based Inhibitor." 100.00 173 99.42 100.00 6.94e-123 PDB 4G9L "Structure Of Mmp3 Complexed With Nngh Inhibitor" 100.00 173 99.42 100.00 6.94e-123 PDB 4JA1 "Structure Of Mmp3 Complexed With A Platinum-based Inhibitor" 100.00 173 99.42 100.00 6.94e-123 DBJ BAD97003 "matrix metalloproteinase 3 preproprotein variant [Homo sapiens]" 100.00 477 99.42 100.00 7.43e-120 DBJ BAD97011 "matrix metalloproteinase 3 preproprotein variant [Homo sapiens]" 100.00 477 99.42 100.00 7.43e-120 DBJ BAG36115 "unnamed protein product [Homo sapiens]" 100.00 477 99.42 100.00 7.43e-120 EMBL CAA28859 "preprostromelysin [Homo sapiens]" 100.00 477 99.42 100.00 7.43e-120 GB AAA00036 "prostromelysin=matrix metalloproteinase [human, Peptide, 477 aa]" 100.00 477 99.42 100.00 7.43e-120 GB AAA36321 "matrix metalloproteinase-3 [Homo sapiens]" 100.00 477 99.42 100.00 7.43e-120 GB AAB36942 "stromelysin [Homo sapiens]" 100.00 477 99.42 100.00 7.43e-120 GB AAD45887 "stromelysin catalytic domain [synthetic construct]" 100.00 174 99.42 100.00 7.59e-123 GB AAH69676 "Matrix metallopeptidase 3 (stromelysin 1, progelatinase) [Homo sapiens]" 100.00 477 99.42 100.00 7.43e-120 REF NP_002413 "stromelysin-1 preproprotein [Homo sapiens]" 100.00 477 99.42 100.00 7.43e-120 REF XP_002822450 "PREDICTED: stromelysin-1 [Pongo abelii]" 100.00 477 98.27 100.00 2.98e-119 REF XP_003253099 "PREDICTED: stromelysin-1 [Nomascus leucogenys]" 100.00 477 98.84 100.00 5.66e-120 REF XP_003828425 "PREDICTED: stromelysin-1 [Pan paniscus]" 100.00 477 99.42 100.00 4.61e-120 REF XP_004052086 "PREDICTED: stromelysin-1 [Gorilla gorilla gorilla]" 100.00 477 98.27 99.42 2.44e-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 99.42 100.00 7.43e-120 stop_ save_ save_MMP-3 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'MatrixMetalloProteinases-3(catalytic domain)' _Abbreviation_common MMP-3(deltaC) _Molecular_mass . _Mol_thiol_state 'not present' _Details . _Residue_count 173 _Mol_residue_sequence ; FRTFPGIPKWRKTHLTYRIV NYTPDLPKDAVDSAVEKALK VWEEVTPLTFSRLYEGEADI MISFAVREHGDFYPFDGPGN VLAHAYAPGPGINGDAHFDD DEQWTKDTTGTNLFLVAAHQ 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 GLN 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 2008-08-19 _Sequence_homology_query_revised_last_date 2008-08-19 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 SWISS-PROT P08254 'Stromelysin-1 precursor (SL-1) (Matrix metalloproteinase-3) (MMP-3) (Transin-1)' 100.00 477 99.42 100.00 4.94e-98 REF XP_508723 'PREDICTED: matrix metalloproteinase 3 isoform 4 [Pan troglodytes]' 100.00 477 99.42 100.00 3.42e-98 REF XP_001154004 'PREDICTED: matrix metalloproteinase 3 isoform 2 [Pan troglodytes]' 100.00 410 99.42 100.00 4.15e-98 REF XP_001153941 'PREDICTED: matrix metalloproteinase 3 isoform 1 [Pan troglodytes]' 100.00 447 99.42 100.00 7.82e-98 REF NP_002413 'matrix metalloproteinase 3 preproprotein [Homo sapiens]' 100.00 477 99.42 100.00 4.94e-98 GenBank AAH69676 'Matrix metallopeptidase 3 (stromelysin 1, progelatinase) [Homo sapiens]' 100.00 477 99.42 100.00 4.94e-98 GenBank AAD45887 'stromelysin catalytic domain [synthetic construct]' 100.00 174 99.42 100.00 5.51e-97 GenBank AAB36942 'stromelysin [Homo sapiens]' 100.00 477 99.42 100.00 4.94e-98 GenBank AAA36321 'matrix metalloproteinase-3' 100.00 477 99.42 100.00 4.94e-98 GenBank AAA00036 'prostromelysin=matrix metalloproteinase [human, Peptide, 477 aa]' 100.00 477 99.42 100.00 4.94e-98 EMBL CAA28859 'preprostromelysin [Homo sapiens]' 100.00 477 99.42 100.00 4.94e-98 DBJ BAG36115 'unnamed protein product [Homo sapiens]' 100.00 477 99.42 100.00 4.94e-98 DBJ BAD97011 'matrix metalloproteinase 3 preproprotein variant [Homo sapiens]' 100.00 477 99.42 100.00 4.94e-98 DBJ BAD97003 'matrix metalloproteinase 3 preproprotein variant [Homo sapiens]' 100.00 477 99.42 100.00 4.94e-98 PDB 3USN 'Structure Of The Catalytic Domain Of Human Fibroblast Stromelysin-1' 97.11 168 99.40 100.00 3.46e-94 PDB 2USN 'Crystal Structure Of The Catalytic Domain Of Human Fibroblast Stromelysin-1 Inhibited With Thiadiazole Inhibitor Pnu-141803' 95.38 165 99.39 100.00 2.85e-92 PDB 2SRT 'Catalytic Domain Of Human Stromelysin-1 At Ph 5.5 And 40oc Complexed With Inhibitor' 100.00 173 99.42 100.00 5.28e-97 PDB 2JT6 'Solution Structure Of Matrix Metalloproteinase 3 (Mmp-3)' 93.06 161 99.38 100.00 1.07e-89 PDB 2JT5 'Solution Structure Of Matrix Metalloproteinase 3 (Mmp-3)' 93.06 161 99.38 100.00 1.07e-89 PDB 2JNP 'Solution Structure Of Matrix Metalloproteinase 3 (Mmp-3)' 93.06 161 99.38 100.00 1.07e-89 PDB 2D1O 'Stromelysin-1 (Mmp-3) Complexed To A Hydroxamic Acid Inhibitor' 98.84 171 99.42 100.00 6.90e-96 PDB 1USN 'Crystal Structure Of The Catalytic Domain Of Human Fibroblast Stromelysin-1' 95.38 165 99.39 100.00 2.85e-92 PDB 1UMT 'Stromelysin-1 Catalytic Domain With Hydrophobic Inhibitor Bound, Ph 7.0, 32oc, 20 Mm Cacl2, 15% Acetonitrile' 100.00 174 99.42 100.00 5.51e-97 PDB 1UMS 'Stromelysin-1 Catalytic Domain With Hydrophobic Inhibitor Bound, Ph 7.0, 32oc, 20 Mm Cacl2, 15% Acetonitrile' 100.00 174 99.42 100.00 5.51e-97 PDB 1UEA 'Mmp-3TIMP-1 Complex' 100.00 173 98.27 98.84 2.16e-95 PDB 1SLN 'Crystal Structure Of The Catalytic Domain Of Human Fibroblast Stromelysin-1' 99.42 173 99.42 100.00 2.16e-96 PDB 1SLM 'Crystal Structure Of Fibroblast Stromelysin-1: The C- Truncated Human Proenzyme' 100.00 255 99.42 100.00 5.02e-98 PDB 1QIC 'Crystal Structure Of Stromelysin Catalytic Domain' 93.06 161 99.38 100.00 9.41e-90 PDB 1QIA 'Crystal Structure Of Stromelysin Catalytic Domain' 93.64 162 99.38 100.00 2.24e-90 PDB 1OO9 'Orientation In Solution Of Mmp-3 Catalytic Domain And N- Timp-1 From Residual Dipolar Couplings' 97.11 168 99.40 100.00 3.46e-94 PDB 1HY7 'A Carboxylic Acid Based Inhibitor In Complex With Mmp3' 100.00 173 99.42 100.00 5.28e-97 PDB 1HFS 'Crystal Structure Of The Catalytic Domain Of Human Fibroblast Stromelysin-1' 92.49 160 99.38 100.00 4.75e-89 PDB 1G4K 'X-Ray Structure Of A Novel Matrix Metalloproteinase Inhibitor Complexed To Stromelysin' 97.11 168 99.40 100.00 3.46e-94 PDB 1G49 'A Carboxylic Acid Based Inhibitor In Complex With Mmp3' 100.00 173 99.42 100.00 5.28e-97 PDB 1G05 'Heterocycle-Based Mmp Inhibitor With P2'substituents' 100.00 173 99.42 100.00 5.28e-97 PDB 1D8M 'Crystal Structure Of Mmp3 Complexed With A Heterocycle- Based Inhibitor' 100.00 173 99.42 100.00 5.28e-97 PDB 1D8F 'Crystal Structure Of Mmp3 Complexed With A Piperazine Based Inhibitor.' 100.00 173 99.42 100.00 5.28e-97 PDB 1D7X 'Crystal Structure Of Mmp3 Complexed With A Modified Proline Scaffold Based Inhibitor.' 100.00 173 99.42 100.00 5.28e-97 PDB 1D5J 'Crystal Structure Of Mmp3 Complexed With A Thiazepine Based Inhibitor.' 100.00 173 99.42 100.00 5.28e-97 PDB 1CQR 'Crystal Structure Of The Stromelysin Catalytic Domain At 2.0 A Resolution' 100.00 173 99.42 100.00 5.28e-97 PDB 1CIZ 'X-Ray Structure Of Human Stromelysin Catalytic Domain Complexes With Non-Peptide Inhibitors' 97.11 168 99.40 100.00 3.46e-94 PDB 1CAQ 'X-Ray Structure Of Human Stromelysin Catalytic Domain Complexes With Non-Peptide Inhibitors' 97.11 168 99.40 100.00 3.46e-94 PDB 1C8T 'Human Stromelysin-1 (E202q) Catalytic Domain Complexed With Ro-26-2812' 95.95 167 100.00 100.00 3.26e-93 PDB 1C3I 'Human Stromelysin-1 Catalytic Domain Complexed With Ro-26- 2812' 100.00 173 99.42 100.00 5.28e-97 PDB 1BQO 'Discovery Of Potent, Achiral Matrix Metalloproteinase Inhibitors' 100.00 173 99.42 100.00 5.28e-97 PDB 1BM6 'Solution Structure Of The Catalytic Domain Of Human Stromelysin-1' 100.00 173 99.42 100.00 5.28e-97 PDB 1BIW 'Design And Synthesis Of Conformationally-Constrained Mmp Inhibitors' 100.00 173 99.42 100.00 5.28e-97 PDB 1B8Y 'X-Ray Structure Of Human Stromelysin Catalytic Domain Complexed With Non-Peptide Inhibitors' 96.53 167 99.40 100.00 1.51e-93 PDB 1B3D Stromelysin-1 100.00 173 99.42 100.00 5.28e-97 BMRB 5785 'Matrix MetalloProteinases-3 or stromelysin 1' 100.00 173 100.00 100.00 1.66e-97 BMRB 5231 stromelysin 100.00 173 99.42 100.00 5.28e-97 BMRB 5099 'Metalloproteinases-1/Matrix MetalloProteinase-3(catalytic domain, residue 83-255)' 100.00 173 100.00 100.00 1.66e-97 BMRB 4366 stromelysin 95.95 166 98.80 99.40 7.64e-92 BMRB 4365 stromelysin 95.95 166 98.80 99.40 7.64e-92 BMRB 4364 stromelysin 95.95 166 98.80 99.40 7.64e-92 BMRB 4173 STROMELYSIN-1 100.00 173 99.42 100.00 5.28e-97 BMRB 15396 MMP3 93.06 161 99.38 100.00 1.07e-89 BMRB 15395 MMP3 93.06 161 99.38 100.00 1.07e-89 BMRB 15120 entity_1 93.06 161 99.38 100.00 1.07e-89 stop_ save_ ############# # Ligands # ############# 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 no _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Mon Jun 13 13:55:41 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons CA CA CA . 2 . ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ 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 no _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Mon Jun 13 14:00:03 2011 ; 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 $N-TIMP-1 Human 9606 Eukaryota Metazoa Homo sapiens $MMP-3 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 $N-TIMP-1 'recombinant technology' . . . . . $MMP-3 'recombinant technology' . . . . . 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 $N-TIMP-1 0.3 mM '[U-98% 15N; U-98% 2H]' $MMP-3 0.3 mM '[U-98% 15N; U-98% 2H]' Tris 20 mM [U-2H] NaCl 125 mM . CaCl2 10 mM . NaN3 1 mM . ZnCl2 50 mM . H2O 93 % . D2O 7 % . stop_ save_ ############################ # Computer software used # ############################ save_Sybyl_TRIAD _Saveframe_category software _Name 'Sybyl TRIAD' _Version 6.3 _Details . save_ save_ModelFree _Saveframe_category software _Name ModelFree _Version 4.1 _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model Inova _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_15N_T1_relaxation_1 _Saveframe_category NMR_applied_experiment _Experiment_name '15N T1 relaxation' _Sample_label $sample_1 save_ save_15N_T2_relaxation_2 _Saveframe_category NMR_applied_experiment _Experiment_name '15N T2 relaxation' _Sample_label $sample_1 save_ save_heteronuclear_1H-15N_NOE_3 _Saveframe_category NMR_applied_experiment _Experiment_name 'heteronuclear 1H-15N NOE' _Sample_label $sample_1 save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '15N T1 relaxation' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '15N T2 relaxation' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name 'heteronuclear 1H-15N NOE' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_condition_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.22 0.05 n/a temperature 307 0.5 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _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 _Indirect_shift_ratio_citation_label _Correction_value_citation_label DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 $entry_citation $entry_citation stop_ save_ save_T1_relaxation_label _Saveframe_category T1_relaxation _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $condition_1 _Spectrometer_frequency_1H 600 _T1_coherence_type Nz _T1_value_units s _Mol_system_component_name 'N-TIMP-1, inhibitor' _Text_data_format . _Text_data . loop_ _T1_ID _Residue_seq_code _Residue_label _Atom_name _T1_value _T1_value_error 1 2 THR N 1.0190 0.036 2 3 CYS N 0.9191 0.027 3 4 VAL N 0.9345 0.037 4 9 GLN N 0.8176 0.039 5 10 THR N 0.8097 0.042 6 11 ALA N 0.7158 0.037 7 12 PHE N 0.8077 0.040 8 13 CYS N 0.7627 0.027 9 15 SER N 0.8038 0.033 10 16 ASP N 0.7262 0.067 11 17 LEU N 1.1918 0.121 12 19 ILE N 0.9661 0.077 13 20 ARG N 0.7593 0.027 14 21 ALA N 0.8554 0.044 15 22 LYS N 0.8802 0.036 16 23 PHE N 0.8143 0.030 17 24 VAL N 0.7861 0.021 18 25 GLY N 0.5770 0.016 19 28 GLU N 0.8912 0.043 20 29 VAL N 0.7230 0.073 21 30 ASN N 0.7843 0.039 22 35 TYR N 0.7246 0.045 23 36 GLN N 0.8445 0.039 24 37 ARG N 0.8841 0.068 25 38 TYR N 0.8169 0.040 26 39 GLU N 0.9208 0.026 27 40 ILE N 0.8665 0.026 28 41 LYS N 0.9276 0.019 29 42 MET N 0.8291 0.033 30 43 THR N 0.7547 0.046 31 44 LYS N 1.0030 0.055 32 45 MET N 0.8196 0.025 33 48 GLY N 0.6968 0.051 34 49 PHE N 0.6027 0.029 35 54 ASP N 0.6199 0.034 36 56 ALA N 0.7645 0.043 37 58 ILE N 0.6317 0.029 38 59 ARG N 0.7936 0.025 39 61 VAL N 0.9541 0.041 40 62 TYR N 0.8726 0.045 41 63 THR N 0.8250 0.040 42 70 CYS N 0.8936 0.033 43 71 GLY N 0.8382 0.054 44 73 PHE N 0.7662 0.030 45 74 HIS N 0.8658 0.028 46 80 SER N 0.6680 0.051 47 81 GLU N 0.7733 0.026 48 82 GLU N 0.8403 0.036 49 83 PHE N 0.7980 0.046 50 84 LEU N 0.7782 0.052 51 85 ILE N 0.9689 0.048 52 86 ALA N 0.9276 0.074 53 87 GLY N 1.0224 0.052 54 88 LYS N 0.8857 0.040 55 90 GLN N 0.9891 0.076 56 91 ASP N 0.7961 0.063 57 92 GLY N 0.8032 0.031 58 95 HIS N 0.8718 0.046 59 96 ILE N 0.8620 0.025 60 97 THR N 0.8090 0.037 61 98 THR N 0.8488 0.032 62 99 CYS N 0.7581 0.041 63 100 SER N 0.7980 0.029 64 101 PHE N 0.8488 0.016 65 102 VAL N 0.9699 0.032 66 103 ALA N 0.9699 0.032 67 105 TRP N 0.7473 0.041 68 106 ASN N 0.7479 0.025 69 107 SER N 0.7892 0.023 70 108 LEU N 0.6973 0.056 71 109 SER N 0.8058 0.033 72 110 LEU N 0.8130 0.050 73 112 GLN N 0.7710 0.030 74 113 ARG N 0.8110 0.024 75 115 GLY N 0.8077 0.033 76 116 PHE N 0.7215 0.020 77 117 THR N 0.7446 0.045 78 118 LYS N 0.7158 0.036 79 119 THR N 0.7002 0.021 80 120 TYR N 0.7501 0.034 81 121 THR N 0.6930 0.027 82 122 VAL N 0.8857 0.046 83 124 CYS N 0.7788 0.029 84 125 GLU N 0.5364 0.017 85 126 GLU N 0.7698 0.044 stop_ save_ save_T2_relaxation_label _Saveframe_category T2_relaxation _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $condition_1 _Spectrometer_frequency_1H 600 _T2_coherence_type Nx _T2_value_units s _Mol_system_component_name 'N-TIMP-1, inhibitor' _Text_data_format . _Text_data . loop_ _T2_ID _Residue_seq_code _Residue_label _Atom_name _T2_value _T2_value_error _Rex_value _Rex_error 1 2 THR N 0.048239 0.0025 5.6 1.2 2 3 CYS N 0.048828 0.0034 4.3 1.4 3 4 VAL N 0.050454 0.0026 . . 4 9 GLN N 0.050838 0.0028 . . 5 10 THR N 0.046040 0.0021 2.7 1.3 6 11 ALA N 0.047755 0.0020 3.4 1.1 7 12 PHE N 0.048123 0.0015 3.4 0.8 8 13 CYS N 0.049019 0.0011 2.2 0.6 9 15 SER N 0.053879 0.0030 . . 10 17 LEU N 0.046490 0.0079 6.9 3.7 11 18 VAL N 0.042808 0.0047 8.5 3.5 12 19 ILE N 0.041017 0.0013 8.3 1.4 13 20 ARG N 0.047258 0.0023 . . 14 21 ALA N 0.046040 0.0014 2.8 1.0 15 22 LYS N 0.049358 0.0017 2.4 0.9 16 23 PHE N 0.047483 0.0016 3.1 0.9 17 24 VAL N 0.047393 0.0022 4.1 1.0 18 25 GLY N 0.081833 0.0064 . . 19 28 GLU N 0.053879 0.0014 1.6 0.8 20 29 VAL N 0.036818 0.0013 11.2 1.7 21 30 ASN N 0.043478 0.0009 5.6 0.8 22 35 TYR N 0.042808 0.0025 5.8 1.7 23 36 GLN N 0.049188 0.0028 2.5 1.2 24 37 ARG N 0.036630 0.0023 11.2 2.0 25 38 TYR N 0.044682 0.0011 5.0 0.8 26 39 GLU N 0.048053 0.0018 4.7 1.0 27 40 ILE N 0.046040 0.0015 3.6 0.8 28 41 LYS N 0.046382 0.0012 2.3 0.6 29 42 MET N 0.046816 0.0008 4.4 0.7 30 43 THR N 0.048169 0.0017 1.7 1.1 31 44 LYS N 0.050761 0.0028 2.2 1.4 32 45 MET N 0.042301 0.0032 5.9 1.8 33 48 GLY N 0.044247 0.0021 5.5 1.5 34 49 PHE N 0.096246 0.0032 . . 35 54 ASP N 0.107492 0.0035 . . 36 56 ALA N 0.058309 0.0027 . . 37 58 ILE N 0.078247 0.0094 . . 38 59 ARG N 0.048449 0.0026 4.2 1.1 39 61 VAL N 0.043327 0.0020 6.6 1.3 40 62 TYR N 0.044822 0.0021 4.6 1.1 41 63 THR N 0.044444 0.0016 5.2 1.0 42 70 CYS N 0.038372 0.0028 7.5 2.1 43 71 GLY N 0.037893 0.0024 8.8 2.0 44 73 PHE N 0.045850 0.0012 4.9 0.8 45 74 HIS N 0.048923 0.0032 3.2 1.3 46 80 SER N 0.048780 0.0022 3.8 1.4 47 81 GLU N 0.046794 0.0027 . . 48 82 GLU N 0.046232 0.0025 5.4 1.3 49 83 PHE N 0.045766 0.0031 . . 50 84 LEU N 0.046168 0.0029 . . 51 85 ILE N 0.044563 0.0025 4.7 1.5 52 86 ALA N 0.042069 0.0018 5.8 1.4 53 87 GLY N 0.044883 0.0017 5.5 0.8 54 88 LYS N 0.044091 0.0016 4.4 1.0 55 90 GLN N 0.047641 0.0012 5.2 1.3 56 91 ASP N 0.046554 0.0042 4.8 2.2 57 92 GLY N 0.052029 0.0020 2.6 0.8 58 95 HIS N 0.043649 0.0018 5.8 1.2 59 96 ILE N 0.045475 0.0015 4.8 0.9 60 97 THR N 0.042087 0.0017 6.4 1.1 61 98 THR N 0.042607 0.0027 6.5 1.6 62 99 CYS N 0.044722 0.0021 4.6 1.2 63 100 SER N 0.043440 0.0020 5.7 1.1 64 101 PHE N 0.048285 0.0012 2.5 0.6 65 102 VAL N 0.044483 0.0011 4.3 0.7 66 103 ALA N 0.044424 0.0028 3.8 1.5 67 105 TRP N 0.043687 0.0010 5.6 0.9 68 106 ASN N 0.048590 0.0023 3.8 1.0 69 107 SER N 0.050530 0.0012 2.8 0.7 70 108 LEU N 0.046882 0.0019 3.9 1.4 71 109 SER N 0.047281 0.0014 4.4 0.8 72 110 LEU N 0.045787 0.0027 3.5 1.6 73 112 GLN N 0.047664 0.0029 . . 74 113 ARG N 0.048100 0.0019 . . 75 115 GLY N 0.042337 0.0034 . . 76 116 PHE N 0.048614 0.0016 . . 77 117 THR N 0.047778 0.0021 3.2 1.3 78 118 LYS N 0.050709 0.0016 . . 79 119 THR N 0.048285 0.0042 . . 80 120 TYR N 0.045065 0.0024 5.6 1.3 81 121 THR N 0.048520 0.0025 . . 82 122 VAL N 0.050942 0.0022 3.9 1.1 83 124 CYS N 0.057803 0.0039 . . 84 125 GLU N 0.125992 0.0069 . . 85 126 GLU N 0.190114 0.0243 . . stop_ save_ save_heteronuclear_NOE _Saveframe_category heteronuclear_NOE _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $condition_1 _Spectrometer_frequency_1H 600 _Mol_system_component_name ? _Atom_one_atom_name . _Atom_two_atom_name . _Heteronuclear_NOE_value_type 'relative intensities' _NOE_reference_value . _NOE_reference_description . _Text_data_format . _Text_data . loop_ _Residue_seq_code _Residue_label _Heteronuclear_NOE_value _Heteronuclear_NOE_value_error 2 THR 0.78988 0.0461 3 CYS 0.72767 0.00117 4 VAL 0.7034 0.00316 9 GLN 0.62824 0.07397 10 THR 0.82976 0.05307 11 ALA 0.71282 0.05718 12 PHE 0.63577 0.03363 13 CYS 0.71925 0.03559 15 SER 0.6635 0.05561 16 ASP 0.76289 0.04428 17 LEU 0.83455 0.03023 18 VAL 0.45049 0.04109 19 ILE 0.76894 0.03385 20 ARG 0.76886 0.09079 21 ALA 0.77777 0.05225 22 LYS 0.71659 0.01431 23 PHE 0.74083 0.05912 24 VAL 0.65351 0.03895 25 GLY 0.51599 0.02791 28 GLU 0.71808 0.03552 29 VAL 0.58445 0.0537 30 ASN 0.82765 0.06686 35 TYR 0.73737 0.02509 36 GLN 0.79827 0.13211 37 ARG 0.72997 0.06675 38 TYR 0.8264 0.03071 39 GLU 0.52371 0.07463 40 ILE 0.71854 0.05589 41 LYS 0.74496 0.06298 42 MET 0.61142 0.11438 43 THR 0.76142 0.06857 44 LYS 0.67879 0.03523 45 MET 0.62283 0.0463 48 GLY 0.81073 0.11882 49 PHE 0.52792 0.07276 54 ASP -0.2344 0.04075 56 ALA 0.69326 0.02575 59 ARG 0.57419 0.02857 61 VAL 0.71894 0.08581 62 TYR 0.73965 0.05917 63 THR 0.83377 0.04118 70 CYS 0.784 0.00375 71 GLY 0.83031 0.10691 73 PHE 0.6538 0.08179 74 HIS 0.64035 0.0356 80 SER 0.61472 0.03469 81 GLU 0.72049 0.07103 82 GLU 0.58992 0.04211 83 PHE 0.74753 0.01209 84 LEU 0.79494 0.04217 85 ILE 0.76752 0.03809 86 ALA 0.76983 0.03978 87 GLY 0.77216 0.00312 88 LYS 0.75851 0.04555 90 GLN 0.72569 0.02192 91 ASP 0.69118 0.03561 92 GLY 0.67448 0.04432 95 HIS 0.83652 0.04606 96 ILE 0.79271 0.08429 97 THR 0.74918 0.04205 98 THR 0.76717 0.02232 99 CYS 0.79926 0.09606 100 SER 0.79217 0.04508 101 PHE 0.8199 0.0869 102 VAL 0.70846 0.01488 103 ALA 0.80891 0.04619 105 TRP 0.74565 0.01926 106 ASN 0.71372 0.02755 107 SER 0.67158 0.08608 108 LEU 0.8136 0.01977 109 SER 0.65062 0.02722 110 LEU 0.8268 0.0422 112 GLN 0.68597 0.00814 113 ARG 0.75768 0.01853 115 GLY 0.76224 0.06427 116 PHE 0.77639 0.05065 117 THR 0.7223 0.11009 118 LYS 0.64717 0.04579 119 THR 0.71255 0.04128 120 TYR 0.70066 0.05841 121 THR 0.59259 0.01309 122 VAL 0.57919 0.03625 124 CYS 0.5416 0.02923 125 GLU 0.23194 0.01252 126 GLU -1.0948 0.1182 stop_ save_ save_S2_parameters_label _Saveframe_category S2_parameters _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $condition_1 _Mol_system_component_name 'N-TIMP-1, inhibitor' _Tau_e_value_units ps _Text_data_format . _Text_data . loop_ _Residue_seq_code _Residue_label _Atom_name _Model_fit _S2_value _S2_value_fit_error _Tau_e_value _Tau_e_value_fit_error _S2f_value _S2f_value_fit_error _S2s_value _S2s_value_fit_error _Tau_s_value _Tau_s_value_fit_error _S2H_value _S2H_value_fit_error _S2N_value _S2N_value_fit_error 2 THR N . 0.847 0.031 . . . . . . . . . . . . 3 CYS N . 0.893 0.009 41.6 3.7 . . . . . . . . . . 4 VAL N . 0.951 0.003 149.5 15.9 . . . . . . . . . . 9 GLN N . 0.939 0.027 260.9 142.5 . . . . . . . . . . 10 THR N . 0.969 0.040 19.3 44.5 . . . . . . . . . . 11 ALA N . 0.939 0.037 211.1 156.1 . . . . . . . . . . 12 PHE N . 0.934 0.026 252.2 129.8 . . . . . . . . . . 13 CYS N . 0.952 0.020 251.7 147.6 . . . . . . . . . . 15 SER N . 0.932 0.026 859.9 1071.4 . . . . . . . . . . 16 ASP N . 0.838 0.110 3018.4 2419.2 . . . . . . . . . . 17 LEU N . 0.767 0.077 . . . . . . . . . . . . 18 VAL N . 0.765 0.131 123.6 107.0 . . . . . . . . . . 19 ILE N . 0.886 0.061 34.7 36.2 . . . . . . . . . . 20 ARG N . 0.864 0.042 5485.3 3372.0 . . . . . . . . . . 21 ALA N . 0.978 0.033 . . . . . . . . . . . . 22 LYS N . 0.937 0.025 97.7 32.8 . . . . . . . . . . 23 PHE N . 0.956 0.028 218.8 162.1 . . . . . . . . . . 24 VAL N . 0.937 0.016 308.5 110.2 . . . . . . . . . . 25 GLY N . 0.581 0.030 1516.8 84.0 . . . . . . . . . . 28 GLU N . 0.935 0.030 139.9 114.5 . . . . . . . . . . 29 VAL N . 0.858 0.073 152.3 120.2 . . . . . . . . . . 30 ASN N . 0.980 0.031 . . . . . . . . . . . . 35 TYR N . 0.924 0.041 97.3 64.3 . . . . . . . . . . 36 GLN N . 0.982 0.028 . . . . . . . . . . . . 37 ARG N . 0.919 0.053 113.2 127.8 . . . . . . . . . . 38 TYR N . 0.980 0.029 . . . . . . . . . . . . 39 GLU N . 0.878 0.028 149.7 61.8 . . . . . . . . . . 40 ILE N . 0.957 0.023 253.3 152.7 . . . . . . . . . . 41 LYS N . 0.991 0.012 . . . . . . . . . . . . 42 MET N . 0.919 0.036 288.1 137.6 . . . . . . . . . . 43 THR N . 0.964 0.043 28.5 74.8 . . . . . . . . . . 44 LYS N . 0.898 0.044 95.5 79.3 . . . . . . . . . . 45 MET N . 0.929 0.018 324.2 103.4 . . . . . . . . . . 48 GLY N . 0.961 0.054 . . . . . . . . . . . . 49 PHE N . 0.502 0.023 1641.6 296.1 . . . . . . . . . . 54 ASP N . 0.453 0.020 673.7 32.4 . . . . . . . . . . 56 ALA N . 0.882 0.033 1330.9 328.4 . . . . . . . . . . 58 ILE N . 0.640 0.076 2614.6 2683.1 . . . . . . . . . . 59 ARG N . 0.911 0.013 307.0 109.3 . . . . . . . . . . 61 VAL N . 0.911 0.038 . . . . . . . . . . . . 62 TYR N . 0.980 0.028 . . . . . . . . . . . . 63 THR N . 0.981 0.027 . . . . . . . . . . . . 70 CYS N . 0.938 0.022 39.2 10.6 . . . . . . . . . . 71 GLY N . 0.974 0.037 . . . . . . . . . . . . 73 PHE N . 0.929 0.032 282.3 138.0 . . . . . . . . . . 74 HIS N . 0.936 0.016 315.6 109.9 . . . . . . . . . . 80 SER N . 0.913 0.050 189.0 131.5 . . . . . . . . . . 81 GLU N . 0.912 0.033 5164.7 3677.1 . . . . . . . . . . 82 GLU N . 0.885 0.032 156.3 97.4 . . . . . . . . . . 83 PHE N . 0.925 0.028 1400.5 439.8 . . . . . . . . . . 84 LEU N . 0.906 0.054 4685.1 3729.2 . . . . . . . . . . 85 ILE N . 0.927 0.041 48.9 48.4 . . . . . . . . . . 86 ALA N . 0.922 0.053 57.3 54.3 . . . . . . . . . . 87 GLY N . 0.884 0.017 21.5 5.6 . . . . . . . . . . 88 LYS N . 0.982 0.026 . . . . . . . . . . . . 90 GLN N . 0.866 0.065 50.2 40.7 . . . . . . . . . . 91 ASP N . 0.920 0.044 197.9 132.3 . . . . . . . . . . 92 GLY N . 0.940 0.021 274.8 133.5 . . . . . . . . . . 95 HIS N . 0.966 0.038 . . . . . . . . . . . . 96 ILE N . 0.978 0.023 . . . . . . . . . . . . 97 THR N . 0.983 0.025 . . . . . . . . . . . . 98 THR N . 0.942 0.024 62.6 32.4 . . . . . . . . . . 99 CYS N . 0.978 0.032 . . . . . . . . . . . . 100 SER N . 0.985 0.022 . . . . . . . . . . . . 101 PHE N . 0.992 0.012 . . . . . . . . . . . . 102 VAL N . 0.933 0.023 98.1 36.3 . . . . . . . . . . 103 ALA N . 0.964 0.029 . . . . . . . . . . . . 105 TRP N . 0.929 0.036 74.5 33.7 . . . . . . . . . . 106 ASN N . 0.950 0.016 235.0 138.6 . . . . . . . . . . 107 SER N . 0.935 0.030 278.1 139.0 . . . . . . . . . . 108 LEU N . 0.958 0.054 6.0 11.9 . . . . . . . . . . 109 SER N . 0.938 0.021 253.5 124.8 . . . . . . . . . . 110 LEU N . 0.972 0.041 . . . . . . . . . . . . 112 GLN N . 0.868 0.026 1371.5 207.4 . . . . . . . . . . 113 ARG N . 0.941 0.018 1503.0 654.4 . . . . . . . . . . 115 GLY N . 0.904 0.067 4936.3 3714.9 . . . . . . . . . . 116 PHE N . 0.865 0.037 5853.8 3166.0 . . . . . . . . . . 117 THR N . 0.936 0.045 190.9 170.2 . . . . . . . . . . 118 LYS N . 0.886 0.030 1841.7 1508.5 . . . . . . . . . . 119 THR N . 0.825 0.032 2556.3 1755.6 . . . . . . . . . . 120 TYR N . 0.944 0.029 244.0 153.4 . . . . . . . . . . 121 THR N . 0.834 0.031 1048.7 170.8 . . . . . . . . . . 122 VAL N . 0.884 0.032 151.2 88.1 . . . . . . . . . . 124 CYS N . 0.838 0.029 872.3 146.4 . . . . . . . . . . 125 GLU N . 0.336 0.025 1181.9 24.3 . . . . . . . . . . 126 GLU N . 0.245 0.039 453.3 40.6 . . . . . . . . . . stop_ _Tau_s_value_units . save_