data_5099 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone and side chain 1H, 13C, and 15N Chemical Shift Assignments for N-TIMP-1 in N-TIMP-1/MMP-3(E202Q) Complex ; _BMRB_accession_number 5099 _BMRB_flat_file_name bmr5099.str _Entry_type original _Submission_date 2001-08-03 _Accession_date 2001-08-03 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Arumugam S. . . 2 'Van Doren' Steven R. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 392 "13C chemical shifts" 327 "15N chemical shifts" 113 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2003-05-20 update author 'correction of chemical shifts' 2003-05-20 update author 'addition of side chain assignmnets' 2002-08-22 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Increased backbone mobility in Beta-barrel enhances entropy gain driving binding of N-TIMP-1 to MMP-3 ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 12634064 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Arumugam S. . . 2 Gao G. . . 3 Patton B. . . 4 Semenchenko V. . . 5 Brew K. . . 6 'Van Doren' Steven R. . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_volume 327 _Journal_issue 3 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 719 _Page_last 734 _Year 2003 _Details . loop_ _Keyword 'TIMP-1/MMP-3(E202Q) complex' 'tissue inhibitor of matrix metalloproteinases' 'NMR assignments' 'matrix metalloproteinase-3' stop_ save_ ####################################### # Cited references within the entry # ####################################### save_entry_reference_1 _Saveframe_category citation _Citation_full . _Citation_title ; Global Orientation of Bound MMP-3 and N-TIMP-1 in Solution via Residual Dipolar Couplings ; _Citation_status . _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 Arumugam S. . . 2 'Van Doren' Steven R. . stop_ _Journal_abbreviation Biochemistry _Journal_name_full . _Journal_volume . _Journal_issue . _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first . _Page_last . _Year . _Details . loop_ _Keyword 'protein-protein interactions' docking 'residual dipolar couplings' NMR stop_ save_ ################################## # Molecular system description # ################################## save_system_N-TIMP-1_MMP-3(deltaC)_complex _Saveframe_category molecular_system _Mol_system_name 'N-terminus of Tissue Inhibitor of Metalloproteinases-1/Matrix MetalloProteinase-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' $CA 'ZINC (II) ION' $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 contains only the N-terminal 2/3 of the Tissue Inhibitor of Metalloproteinase, whereas the related system is full-length. In addition, the present system has been studied in solution as a complex with a mutant matrix metalloproteinase-3(E202Q). The system of PDB 1D2B 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-terminus of Tissue Inhibitor of Metalloproteinases-1/Matrix MetalloProteinases-3(catalytic domain) complex' _Abbreviation_common 'N-TIMP-1/MMP-3(deltaC) complex' _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 2014-03-02 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 1.25e-113 BMRB 15395 MMP3 93.06 161 98.76 99.38 3.00e-112 BMRB 15396 MMP3 93.06 161 98.76 99.38 3.00e-112 BMRB 4173 SLN 100.00 173 99.42 100.00 5.06e-123 BMRB 4364 stromelysin 95.95 166 98.80 99.40 2.29e-116 BMRB 4365 stromelysin 95.95 166 98.80 99.40 2.29e-116 BMRB 4366 stromelysin 95.95 166 98.80 99.40 2.29e-116 BMRB 5153 MMP-3 100.00 173 100.00 100.00 1.11e-123 BMRB 5231 stromelysin 100.00 173 99.42 100.00 5.06e-123 PDB 1B3D Stromelysin-1 100.00 173 99.42 100.00 5.06e-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 1.39e-118 PDB 1BIW "Design And Synthesis Of Conformationally-Constrained Mmp Inhibitors" 100.00 173 99.42 100.00 5.06e-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 5.06e-123 PDB 1BQO "Discovery Of Potent, Achiral Matrix Metalloproteinase Inhibitors" 100.00 173 99.42 100.00 5.06e-123 PDB 1C3I "Human Stromelysin-1 Catalytic Domain Complexed With Ro-26-2812" 100.00 173 99.42 100.00 5.06e-123 PDB 1C8T "Human Stromelysin-1 (E202q) Catalytic Domain Complexed With Ro-26-2812" 95.95 167 100.00 100.00 3.81e-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 2.08e-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 2.08e-119 PDB 1CQR "Crystal Structure Of The Stromelysin Catalytic Domain At 2.0 A Resolution" 100.00 173 99.42 100.00 5.06e-123 PDB 1D5J "Crystal Structure Of Mmp3 Complexed With A Thiazepine Based Inhibitor." 100.00 173 99.42 100.00 5.06e-123 PDB 1D7X "Crystal Structure Of Mmp3 Complexed With A Modified Proline Scaffold Based Inhibitor." 100.00 173 99.42 100.00 5.06e-123 PDB 1D8F "Crystal Structure Of Mmp3 Complexed With A Piperazine Based Inhibitor." 100.00 173 99.42 100.00 5.06e-123 PDB 1D8M "Crystal Structure Of Mmp3 Complexed With A Heterocycle- Based Inhibitor" 100.00 173 99.42 100.00 5.06e-123 PDB 1G05 "Heterocycle-Based Mmp Inhibitor With P2'substituents" 100.00 173 99.42 100.00 5.06e-123 PDB 1G49 "A Carboxylic Acid Based Inhibitor In Complex With Mmp3" 100.00 173 99.42 100.00 5.06e-123 PDB 1G4K "X-ray Structure Of A Novel Matrix Metalloproteinase Inhibitor Complexed To Stromelysin" 97.11 168 99.40 100.00 2.08e-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 8.52e-113 PDB 1HY7 "A Carboxylic Acid Based Inhibitor In Complex With Mmp3" 100.00 173 99.42 100.00 5.06e-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 2.08e-119 PDB 1QIA "Crystal Structure Of Stromelysin Catalytic Domain" 93.64 162 99.38 100.00 1.67e-114 PDB 1QIC "Crystal Structure Of Stromelysin Catalytic Domain" 93.06 161 99.38 100.00 1.06e-113 PDB 1SLM "Crystal Structure Of Fibroblast Stromelysin-1: The C-Truncated Human Proenzyme" 100.00 255 99.42 100.00 3.98e-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 5.06e-123 PDB 1UEA "Mmp-3TIMP-1 Complex" 100.00 173 98.27 98.84 6.57e-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 5.54e-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 5.54e-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 6.10e-117 PDB 2D1O "Stromelysin-1 (Mmp-3) Complexed To A Hydroxamic Acid Inhibitor" 98.84 171 99.42 100.00 1.37e-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 1.25e-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 1.25e-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 1.25e-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 5.06e-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 6.10e-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 1.39e-118 PDB 3OHO "Catalytic Domain Of Stromelysin-1 In Complex With N-Hydroxy-2-(4- Methylphenylsulfonamido)acetamide" 97.69 169 99.41 100.00 4.56e-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 2.08e-119 PDB 4DPE "Structure Of Mmp3 Complexed With A Platinum-based Inhibitor." 100.00 173 99.42 100.00 5.06e-123 PDB 4G9L "Structure Of Mmp3 Complexed With Nngh Inhibitor" 100.00 173 99.42 100.00 5.06e-123 PDB 4JA1 "Structure Of Mmp3 Complexed With A Platinum-based Inhibitor" 100.00 173 99.42 100.00 5.06e-123 DBJ BAD97003 "matrix metalloproteinase 3 preproprotein variant [Homo sapiens]" 100.00 477 99.42 100.00 5.42e-120 DBJ BAD97011 "matrix metalloproteinase 3 preproprotein variant [Homo sapiens]" 100.00 477 99.42 100.00 5.42e-120 DBJ BAG36115 "unnamed protein product [Homo sapiens]" 100.00 477 99.42 100.00 5.42e-120 EMBL CAA28859 "preprostromelysin [Homo sapiens]" 100.00 477 99.42 100.00 5.42e-120 GB AAA00036 "prostromelysin=matrix metalloproteinase [human, Peptide, 477 aa]" 100.00 477 99.42 100.00 5.42e-120 GB AAA36321 "matrix metalloproteinase-3 [Homo sapiens]" 100.00 477 99.42 100.00 5.42e-120 GB AAB36942 "stromelysin [Homo sapiens]" 100.00 477 99.42 100.00 5.42e-120 GB AAD45887 "stromelysin catalytic domain [synthetic construct]" 100.00 174 99.42 100.00 5.54e-123 GB AAH69676 "Matrix metallopeptidase 3 (stromelysin 1, progelatinase) [Homo sapiens]" 100.00 477 99.42 100.00 5.42e-120 REF NP_002413 "stromelysin-1 preproprotein [Homo sapiens]" 100.00 477 99.42 100.00 5.42e-120 REF XP_002822450 "PREDICTED: stromelysin-1 [Pongo abelii]" 100.00 477 98.27 100.00 2.17e-119 REF XP_003253099 "PREDICTED: stromelysin-1 [Nomascus leucogenys]" 100.00 477 98.84 100.00 4.13e-120 REF XP_003828425 "PREDICTED: stromelysin-1 [Pan paniscus]" 100.00 477 99.42 100.00 3.36e-120 REF XP_004052086 "PREDICTED: stromelysin-1 [Gorilla gorilla gorilla]" 100.00 477 98.27 99.42 1.78e-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 5.42e-120 stop_ save_ save_MMP-3 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Metalloproteinases-1/Matrix MetalloProteinase-3(catalytic domain, residue 83-255)' _Abbreviation_common 'N-TIMP-1/MMP-3(deltaC) complex' _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) In The Presence Of 3-4'-Cyanobyphenyl-4-Yloxy)-N- Hdydroxypropionamide (Mmp-3 Inhibitor Vii)' 93.06 161 99.38 100.00 1.07e-89 PDB 2JT5 'Solution Structure Of Matrix Metalloproteinase 3 (Mmp-3) In The Presence Of N-Hydroxy-2-[n-(2-Hydroxyethyl)biphenyl-4- Sulfonamide] Hydroxamic Acid (Mlc88)' 93.06 161 99.38 100.00 1.07e-89 PDB 2JNP 'Solution Structure Of Matrix Metalloproteinase 3 (Mmp-3) In The Presence Of N-Isobutyl-N-[4- Methoxyphenylsulfonyl]glycyl Hydroxamic Acid (Nngh)' 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 Inhibited With Thiadiazole Inhibitor Pnu-142372' 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; Nmr Average Of 20 Structures Minimized With Restraints' 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; Nmr Ensemble Of 20 Structures' 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 Inhibited With The N-Carboxy- Alkyl Inhibitor L-702,842' 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 Inhibited With The N-Carboxy- Alkyl Inhibitor L-764,004' 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: Implication For Inhibitor Selectivity' 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: Implication For Inhibitor Selectivity' 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 Complexed To A Potent Non-Peptidic Inhibitor, Nmr, 20 Structures' 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: Implications For Inhibitor Selectivity' 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 5153 'MatrixMetalloProteinases-3(catalytic domain)' 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_type _Vector_name $N-TIMP-1 'recombinant technology' 'E. coli' Escherichia coli 'BL21 (DE3)' 'T7 expression' pET3a $MMP-3 'recombinant technology' 'E. coli' Escherichia coli 'BL21 (DE3)' 'T7 expression' pET3a 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 0.66 mM '[U-13C; U-15N]' $MMP-3 0.66 mM . Tris 20 mM [U-2H] NaCl 125 mM . CaCl2 10 mM . NaN3 1 mM . ZnCl2 50 uM . D2O 7 % . H2O 93 % . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $N-TIMP-1 0.52 mM '[U-50% 2H; U-13C; U-15N]' $MMP-3 0.52 mM . Tris 20 mM [U-2H] NaCl 125 mM . CaCl2 10 mM . NaN3 1 mM . ZnCl2 50 uM . D2O 7 % . H2O 93 % . stop_ save_ save_sample_3 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $N-TIMP-1 0.30 mM '[U-2H; U-13C; U-15N]' $MMP-3 0.30 mM . Tris 20 mM [U-2H] NaCl 125 mM . CaCl2 10 mM . NaN3 1 mM . ZnCl2 50 uM . D2O 7 % . H2O 93 % . stop_ save_ ############################ # Computer software used # ############################ save_SYBYL_TRIAD _Saveframe_category software _Name 'SYBYL TRIAD' _Version '6.2, 6.3, 6.6' loop_ _Task 'process NMR spectra' 'interpret NMR spectra' stop_ _Details ; At times, use of NMRPIPE software for an intermediate data conversion was necessary before processing with Sybyl. ; save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 750 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 500 _Details . save_ save_NMR_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model Inova _Field_strength 600 _Details . save_ save_NMR_spectrometer_4 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model UnityPlus _Field_strength 720 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 15N HSQC' _Sample_label . save_ save_3D_HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label . save_ save_3D_HN(CO)CA_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label . save_ save_3D_HNCO_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label . save_ save_3D_TROSY-HNCA_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY-HNCA' _Sample_label . save_ save_NOESY-HSQC_6 _Saveframe_category NMR_applied_experiment _Experiment_name NOESY-HSQC _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 15N HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY-HNCA' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name NOESY-HSQC _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_EX-COND-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 'ionic strength' 0.186 0.02 M 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 DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 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_timpcpxshifts08022001 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $EX-COND-1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'N-TIMP-1, inhibitor' _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 . 1 CYS C C 177.1 0.12 1 2 . 1 CYS HB2 H 2.94 0.01 2 3 . 2 THR H H 7.83 0.01 1 4 . 2 THR HG2 H 1.16 0.01 1 5 . 2 THR C C 176.18 0.12 1 6 . 2 THR CA C 62.68 0.12 1 7 . 2 THR N N 128.39 0.12 1 8 . 3 CYS H H 8.85 0.01 1 9 . 3 CYS HA H 4.95 0.01 1 10 . 3 CYS HB2 H 3.46 0.01 2 11 . 3 CYS C C 176.17 0.12 1 12 . 3 CYS CA C 52.71 0.12 1 13 . 3 CYS N N 124.99 0.12 1 14 . 4 VAL H H 8.29 0.01 1 15 . 4 VAL HB H 1.94 0.01 1 16 . 4 VAL HG1 H 1.10 0.01 1 17 . 4 VAL CA C 62.46 0.12 1 18 . 4 VAL N N 124.61 0.12 1 19 . 6 PRO HA H 4.32 0.01 1 20 . 6 PRO CA C 59.03 0.12 1 21 . 7 HIS H H 8.31 0.01 1 22 . 7 HIS CA C 55.43 0.12 1 23 . 7 HIS N N 120.48 0.12 1 24 . 8 PRO C C 176.58 0.12 1 25 . 8 PRO CA C 66.39 0.12 1 26 . 9 GLN H H 8.38 0.01 1 27 . 9 GLN HB2 H 2.55 0.01 9 28 . 9 GLN HB3 H 2.15 0.01 9 29 . 9 GLN HG2 H 1.90 0.01 2 30 . 9 GLN HG3 H 1.65 0.01 2 31 . 9 GLN C C 178.29 0.12 1 32 . 9 GLN CA C 59.19 0.12 1 33 . 9 GLN CG C 33.87 0.12 1 34 . 9 GLN N N 117.68 0.12 1 35 . 10 THR H H 7.17 0.12 1 36 . 10 THR HA H 3.66 0.01 1 37 . 10 THR HB H 4.07 0.01 1 38 . 10 THR HG2 H 1.02 0.01 1 39 . 10 THR C C 176.92 0.12 1 40 . 10 THR CA C 65.78 0.12 1 41 . 10 THR CB C 63.98 0.12 9 42 . 10 THR CG2 C 22.48 0.12 1 43 . 10 THR N N 115.01 0.12 1 44 . 11 ALA H H 8.72 0.01 1 45 . 11 ALA HA H 3.89 0.01 1 46 . 11 ALA HB H 1.32 0.01 1 47 . 11 ALA C C 180.89 0.12 1 48 . 11 ALA CA C 55.21 0.12 1 49 . 11 ALA CB C 19.27 0.12 1 50 . 11 ALA N N 124.11 0.12 1 51 . 12 PHE H H 8.23 0.01 1 52 . 12 PHE C C 177.04 0.12 1 53 . 12 PHE CA C 62.62 0.12 1 54 . 12 PHE N N 119.9 0.12 1 55 . 13 CYS H H 7.92 0.01 1 56 . 13 CYS HA H 4.26 0.01 1 57 . 13 CYS HB2 H 3.17 0.01 2 58 . 13 CYS HB3 H 2.66 0.01 2 59 . 13 CYS C C 176.43 0.12 1 60 . 13 CYS CA C 56.93 0.12 1 61 . 13 CYS CB C 37.04 0.12 1 62 . 13 CYS N N 114.57 0.12 1 63 . 14 ASN H H 8.27 0.12 1 64 . 14 ASN HA H 4.54 0.12 1 65 . 14 ASN HB2 H 2.67 0.01 2 66 . 14 ASN HB3 H 2.62 0.01 2 67 . 14 ASN C C 175.82 0.12 1 68 . 14 ASN CA C 54.24 0.12 1 69 . 14 ASN N N 116.21 0.12 1 70 . 15 SER H H 7.21 0.01 1 71 . 15 SER C C 172.4 0.01 1 72 . 15 SER CA C 60.04 0.12 1 73 . 15 SER N N 116.23 0.12 1 74 . 16 ASP H H 8.06 0.01 1 75 . 16 ASP HA H 4.5 0.01 1 76 . 16 ASP HB2 H 2.27 0.01 2 77 . 16 ASP HB3 H 2.51 0.01 2 78 . 16 ASP C C 175.47 0.12 1 79 . 16 ASP CA C 56.61 0.12 1 80 . 16 ASP CB C 43.4 0.12 1 81 . 16 ASP N N 120.1 0.12 1 82 . 17 LEU H H 7.41 0.01 1 83 . 17 LEU HA H 4.57 0.01 1 84 . 17 LEU HB2 H 1.15 0.01 2 85 . 17 LEU HG H 1.44 0.01 1 86 . 17 LEU HD1 H 0.7 0.01 2 87 . 17 LEU C C 175.47 0.12 1 88 . 17 LEU CA C 53.77 0.12 1 89 . 17 LEU CB C 46.32 0.12 1 90 . 17 LEU CG C 28.28 0.12 1 91 . 17 LEU CD1 C 25.9 0.12 2 92 . 17 LEU N N 116.47 0.12 1 93 . 18 VAL H H 8.21 0.01 1 94 . 18 VAL HA H 5.01 0.01 1 95 . 18 VAL HB H 1.85 0.01 1 96 . 18 VAL HG1 H 0.97 0.01 1 97 . 18 VAL HG2 H 0.65 0.01 1 98 . 18 VAL C C 175.98 0.12 1 99 . 18 VAL CA C 61.94 0.12 1 100 . 18 VAL CB C 33.06 0.12 1 101 . 18 VAL CG1 C 22.71 0.12 1 102 . 18 VAL CG2 C 20.86 0.12 1 103 . 18 VAL N N 121.97 0.12 1 104 . 19 ILE H H 9.27 0.01 1 105 . 19 ILE HA H 5.02 0.01 1 106 . 19 ILE HB H 1.85 0.01 1 107 . 19 ILE HG2 H 0.73 0.01 1 108 . 19 ILE HD1 H 0.23 0.01 1 109 . 19 ILE C C 173.50 0.12 1 110 . 19 ILE CA C 59.21 0.12 1 111 . 19 ILE CB C 42.34 0.12 1 112 . 19 ILE CG2 C 18.74 0.12 1 113 . 19 ILE CD1 C 14.01 0.12 1 114 . 19 ILE N N 121.85 0.12 1 115 . 20 ARG H H 8.87 0.01 1 116 . 20 ARG HA H 5.42 0.01 1 117 . 20 ARG HB2 H 0.99 0.01 2 118 . 20 ARG HB3 H 1.55 0.01 2 119 . 20 ARG HG2 H 1.02 0.01 2 120 . 20 ARG HD2 H 1.40 0.01 2 121 . 20 ARG HD3 H 1.66 0.01 2 122 . 20 ARG C C 176.4 0.12 1 123 . 20 ARG CA C 54.53 0.12 1 124 . 20 ARG CB C 33.85 0.12 1 125 . 20 ARG CG C 26.43 0.12 1 126 . 20 ARG CD C 43.93 0.12 1 127 . 20 ARG N N 121.59 0.12 1 128 . 21 ALA H H 9.49 0.01 1 129 . 21 ALA HA H 4.96 0.01 1 130 . 21 ALA HB H 0.73 0.01 1 131 . 21 ALA C C 175.74 0.12 1 132 . 21 ALA CA C 51.56 0.12 1 133 . 21 ALA CB C 24.3 0.12 1 134 . 21 ALA N N 124.83 0.12 1 135 . 22 LYS H H 8.32 0.01 1 136 . 22 LYS HA H 4.79 0.01 1 137 . 22 LYS HB2 H 1.19 0.01 2 138 . 22 LYS HG2 H 1.09 0.01 2 139 . 22 LYS HD2 H 1.71 0.01 9 140 . 22 LYS HE2 H 2.62 0.01 2 141 . 22 LYS HE3 H 2.67 0.01 2 142 . 22 LYS C C 176.41 0.12 1 143 . 22 LYS CA C 55.24 0.12 1 144 . 22 LYS CB C 34.91 0.12 1 145 . 22 LYS CG C 25.9 0.12 1 146 . 22 LYS N N 119.18 0.12 1 147 . 23 PHE H H 9.56 0.01 1 148 . 23 PHE HA H 4.18 0.01 1 149 . 23 PHE HB2 H 2.40 0.01 2 150 . 23 PHE C C 176.68 0.01 1 151 . 23 PHE CA C 58.78 0.12 1 152 . 23 PHE N N 124.86 0.12 1 153 . 24 VAL H H 7.98 0.01 1 154 . 24 VAL HA H 4.11 0.01 1 155 . 24 VAL HB H 1.83 0.01 1 156 . 24 VAL HG1 H 0.58 0.01 1 157 . 24 VAL HG2 H 0.35 0.01 1 158 . 24 VAL C C 176.10 0.12 1 159 . 24 VAL CA C 62.28 0.12 1 160 . 24 VAL CB C 32.79 0.12 1 161 . 24 VAL CG1 C 21.12 0.12 1 162 . 24 VAL CG2 C 19.00 0.12 1 163 . 24 VAL N N 118.7 0.12 1 164 . 25 GLY H H 8.20 0.01 1 165 . 25 GLY HA2 H 4.19 0.01 2 166 . 25 GLY HA3 H 3.96 0.01 2 167 . 25 GLY C C 173.59 0.12 1 168 . 25 GLY CA C 45.57 0.12 1 169 . 25 GLY N N 109.84 0.12 1 170 . 26 THR H H 8.31 0.01 1 171 . 26 THR HA H 4.47 0.01 1 172 . 26 THR HB H 4.10 0.01 1 173 . 26 THR HG2 H 1.1 0.01 1 174 . 26 THR CA C 60.04 0.12 1 175 . 26 THR CB C 69.13 0.12 1 176 . 26 THR CG2 C 21.12 0.12 1 177 . 26 THR N N 116.56 0.12 1 178 . 27 PRO HA H 4.13 0.01 1 179 . 27 PRO C C 176.86 0.12 1 180 . 27 PRO CA C 63.19 0.12 1 181 . 28 GLU H H 8.41 0.01 1 182 . 28 GLU HA H 4.38 0.01 1 183 . 28 GLU HB2 H 1.73 0.01 2 184 . 28 GLU HB3 H 1.67 0.01 2 185 . 28 GLU HG2 H 2.06 0.01 2 186 . 28 GLU HG3 H 1.85 0.01 2 187 . 28 GLU CA C 54.93 0.12 1 188 . 28 GLU CB C 31.75 0.12 1 189 . 28 GLU CG C 35.82 0.12 1 190 . 28 GLU N N 121.59 0.12 1 191 . 29 VAL H H 8.85 0.01 1 192 . 29 VAL C C 172.99 0.12 1 193 . 29 VAL N N 127.76 0.12 1 194 . 30 ASN H H 8.69 0.01 1 195 . 30 ASN HA H 4.73 0.01 1 196 . 30 ASN HB2 H 2.58 0.01 9 197 . 30 ASN CA C 52.26 0.12 1 198 . 30 ASN N N 128.89 0.12 1 199 . 31 GLN H H 9.64 0.01 1 200 . 31 GLN HB2 H 2.04 0.01 9 201 . 31 GLN HB3 H 1.81 0.01 2 202 . 31 GLN CB C 28.28 0.12 9 203 . 31 GLN N N 120.63 0.12 1 204 . 32 THR H H 8.89 0.01 1 205 . 32 THR CA C 64.95 0.12 1 206 . 32 THR N N 115.8 0.12 1 207 . 33 THR H H 7.60 0.01 1 208 . 33 THR N N 112.07 0.12 1 209 . 34 LEU H H 8.19 0.01 1 210 . 34 LEU N N 116.56 0.12 1 211 . 35 TYR H H 7.91 0.01 1 212 . 35 TYR C C 175.16 0.12 1 213 . 35 TYR CA C 58.51 0.12 1 214 . 35 TYR N N 118.83 0.12 1 215 . 36 GLN H H 9.85 0.01 1 216 . 36 GLN HA H 5.16 0.01 1 217 . 36 GLN C C 172.91 0.12 1 218 . 36 GLN CA C 52.87 0.12 1 219 . 36 GLN N N 119.96 0.12 1 220 . 37 ARG H H 8.34 0.01 1 221 . 37 ARG HA H 5.19 0.01 1 222 . 37 ARG HB2 H 0.73 0.01 2 223 . 37 ARG HB3 H 1.01 0.01 2 224 . 37 ARG HG2 H 0.63 0.01 2 225 . 37 ARG HG3 H 1.20 0.01 9 226 . 37 ARG HD2 H 1.5 0.01 2 227 . 37 ARG HD3 H 2.34 0.01 2 228 . 37 ARG C C 174.52 0.12 1 229 . 37 ARG CA C 53.26 0.12 1 230 . 37 ARG CD C 43.47 0.12 1 231 . 37 ARG N N 118.58 0.12 1 232 . 38 TYR H H 9.07 0.01 1 233 . 38 TYR C C 175.24 0.12 1 234 . 38 TYR CA C 56.9 0.12 1 235 . 38 TYR N N 122.09 0.12 1 236 . 39 GLU H H 8.93 0.01 1 237 . 39 GLU HA H 4.35 0.01 1 238 . 39 GLU HB2 H 1.68 0.01 2 239 . 39 GLU HB3 H 1.60 0.01 2 240 . 39 GLU HG2 H 1.74 0.01 2 241 . 39 GLU C C 175.91 0.12 1 242 . 39 GLU CA C 56.24 0.12 1 243 . 39 GLU N N 125.99 0.12 1 244 . 40 ILE H H 8.32 0.01 1 245 . 40 ILE HA H 4.88 0.01 1 246 . 40 ILE HB H 0.90 0.01 1 247 . 40 ILE HG12 H 0.77 0.01 2 248 . 40 ILE HG2 H -0.36 0.01 1 249 . 40 ILE HD1 H -0.02 0.01 1 250 . 40 ILE C C 175.04 0.12 1 251 . 40 ILE CA C 58.73 0.12 1 252 . 40 ILE CB C 43.15 0.12 1 253 . 40 ILE CG1 C 24.84 0.12 9 254 . 40 ILE CG2 C 16.88 0.12 1 255 . 40 ILE CD1 C 14.76 0.12 1 256 . 40 ILE N N 121.21 0.12 1 257 . 41 LYS H H 8.56 0.01 1 258 . 41 LYS C C 175.79 0.12 1 259 . 41 LYS CA C 54.20 0.12 1 260 . 41 LYS N N 121.21 0.12 1 261 . 42 MET H H 9.30 0.12 1 262 . 42 MET C C 176.28 0.12 1 263 . 42 MET CA C 56.92 0.12 1 264 . 42 MET N N 128.64 0.12 1 265 . 43 THR H H 9.19 0.01 1 266 . 43 THR HA H 4.14 0.01 1 267 . 43 THR HB H 3.82 0.01 1 268 . 43 THR HG2 H 0.78 0.01 1 269 . 43 THR C C 175.64 0.12 1 270 . 43 THR CA C 62.24 0.12 1 271 . 43 THR CB C 68.54 0.12 1 272 . 43 THR CG2 C 22.64 0.12 1 273 . 43 THR N N 119.96 0.12 1 274 . 44 LYS H H 7.30 0.01 1 275 . 44 LYS HA H 4.03 0.01 1 276 . 44 LYS HB2 H 1.19 0.01 2 277 . 44 LYS HB3 H 0.76 0.01 2 278 . 44 LYS HG2 H 0.55 0.01 2 279 . 44 LYS HG3 H 0.67 0.01 2 280 . 44 LYS HD2 H 1.34 0.01 2 281 . 44 LYS HE2 H 2.68 0.01 2 282 . 44 LYS HE3 H 2.60 0.01 2 283 . 44 LYS C C 173.35 0.12 1 284 . 44 LYS CA C 55.85 0.12 1 285 . 44 LYS CB C 36.15 0.12 1 286 . 44 LYS CG C 24.27 0.12 1 287 . 44 LYS CD C 28.01 0.12 1 288 . 44 LYS CE C 42.17 0.12 1 289 . 44 LYS N N 121.59 0.12 1 290 . 45 MET H H 8.60 0.01 1 291 . 45 MET CA C 55.61 0.12 1 292 . 45 MET N N 125.11 0.12 1 293 . 46 TYR H H 8.63 0.01 1 294 . 46 TYR HA H 4.88 0.01 1 295 . 46 TYR HB2 H 3.75 0.01 9 296 . 46 TYR C C 175.63 0.12 1 297 . 46 TYR CA C 58.60 0.12 1 298 . 46 TYR N N 123.58 0.12 1 299 . 47 LYS H H 7.94 0.01 1 300 . 47 LYS CA C 57.2 0.12 1 301 . 47 LYS N N 121.34 0.12 1 302 . 48 GLY H H 8.69 0.01 1 303 . 48 GLY C C 173.43 0.12 1 304 . 48 GLY CA C 45.76 0.12 1 305 . 48 GLY N N 114.29 0.12 1 306 . 49 PHE H H 7.49 0.01 1 307 . 49 PHE HA H 4.01 0.01 1 308 . 49 PHE HB2 H 2.79 0.01 2 309 . 49 PHE HB3 H 3.06 0.01 2 310 . 49 PHE C C 177.11 0.12 1 311 . 49 PHE CA C 60.07 0.12 1 312 . 49 PHE CB C 39.24 0.12 1 313 . 49 PHE N N 119.51 0.12 1 314 . 50 GLN H H 8.72 0.01 1 315 . 50 GLN CA C 57.92 0.12 1 316 . 50 GLN N N 118.14 0.12 1 317 . 51 ALA H H 7.68 0.01 1 318 . 51 ALA HA H 4.08 0.01 1 319 . 51 ALA HB H 1.18 0.01 1 320 . 51 ALA CA C 53.68 0.12 1 321 . 51 ALA CB C 19.27 0.12 1 322 . 51 ALA N N 122.47 0.12 1 323 . 52 LEU H H 7.64 0.01 1 324 . 52 LEU HA H 4.16 0.01 1 325 . 52 LEU HB2 H 1.45 0.01 2 326 . 52 LEU HG H 1.40 0.01 1 327 . 52 LEU HD1 H 0.63 0.01 1 328 . 52 LEU HD2 H 0.69 0.01 1 329 . 52 LEU C C 178.01 0.12 1 330 . 52 LEU CA C 55.35 0.12 1 331 . 52 LEU CB C 42.34 0.12 1 332 . 52 LEU CG C 26.96 0.12 1 333 . 52 LEU CD1 C 23.24 0.12 1 334 . 52 LEU CD2 C 25.37 0.12 1 335 . 52 LEU N N 116.69 0.12 1 336 . 53 GLY H H 7.90 0.01 1 337 . 53 GLY HA2 H 3.99 0.01 2 338 . 53 GLY HA3 H 3.65 0.01 2 339 . 53 GLY C C 174.22 0.12 1 340 . 53 GLY CA C 45.88 0.12 1 341 . 53 GLY N N 108.88 0.12 1 342 . 54 ASP H H 8.24 0.01 1 343 . 54 ASP C C 176.48 0.12 1 344 . 54 ASP CA C 55.29 0.12 1 345 . 54 ASP N N 120.95 0.12 1 346 . 55 ALA H H 8.09 0.01 1 347 . 55 ALA HA H 4.09 0.01 1 348 . 55 ALA HB H 1.18 0.01 1 349 . 55 ALA C C 176.98 0.12 1 350 . 55 ALA CA C 52.41 0.12 1 351 . 55 ALA CB C 19.27 0.12 1 352 . 55 ALA N N 123.86 0.12 1 353 . 56 ALA H H 7.70 0.01 1 354 . 56 ALA HA H 4.07 0.01 1 355 . 56 ALA HB H 1.12 0.01 1 356 . 56 ALA C C 176.69 0.12 1 357 . 56 ALA CA C 52.71 0.12 1 358 . 56 ALA CB C 19.27 0.12 1 359 . 56 ALA N N 121.91 0.12 1 360 . 57 ASP H H 8.01 0.01 1 361 . 57 ASP HA H 4.44 0.01 1 362 . 57 ASP HB2 H 2.51 0.01 2 363 . 57 ASP HB3 H 2.37 0.01 2 364 . 57 ASP C C 175.37 0.12 1 365 . 57 ASP CA C 54.24 0.12 1 366 . 57 ASP CB C 41.54 0.12 1 367 . 57 ASP N N 119.07 0.12 1 368 . 58 ILE H H 7.58 0.01 1 369 . 58 ILE HA H 3.97 0.01 1 370 . 58 ILE HB H 1.64 0.01 1 371 . 58 ILE HG12 H 1.19 0.01 2 372 . 58 ILE HG13 H 1.03 0.01 2 373 . 58 ILE HG2 H 0.64 0.01 1 374 . 58 ILE HD1 H 0.55 0.01 1 375 . 58 ILE C C 175.04 0.12 1 376 . 58 ILE CA C 61.21 0.12 1 377 . 58 ILE CB C 37.57 0.12 1 378 . 58 ILE CG1 C 26.96 0.12 1 379 . 58 ILE CG2 C 18.03 0.12 1 380 . 58 ILE N N 123.65 0.12 1 381 . 59 ARG H H 8.47 0.01 1 382 . 59 ARG HA H 4.13 0.01 1 383 . 59 ARG HB2 H 1.26 0.01 2 384 . 59 ARG HG2 H 1.00 0.01 2 385 . 59 ARG HG3 H 1.18 0.01 2 386 . 59 ARG HD2 H 2.86 0.01 2 387 . 59 ARG C C 174.36 0.12 1 388 . 59 ARG CA C 56.02 0.12 1 389 . 59 ARG CB C 32.57 0.12 1 390 . 59 ARG CG C 27.36 0.12 1 391 . 59 ARG CD C 43.31 0.12 1 392 . 59 ARG N N 124.87 0.12 1 393 . 60 PHE H H 7.14 0.01 1 394 . 60 PHE HA H 5.45 0.01 1 395 . 60 PHE HB2 H 2.48 0.01 2 396 . 60 PHE HB3 H 2.26 0.01 2 397 . 60 PHE C C 174.98 0.12 1 398 . 60 PHE CA C 56.21 0.12 1 399 . 60 PHE CB C 45.26 0.12 1 400 . 60 PHE N N 114.16 0.12 1 401 . 61 VAL H H 8.58 0.01 1 402 . 61 VAL HA H 4.67 0.01 1 403 . 61 VAL HB H 1.53 0.01 1 404 . 61 VAL HG1 H 0.56 0.01 1 405 . 61 VAL C C 173.61 0.12 1 406 . 61 VAL CA C 60.06 0.12 1 407 . 61 VAL CB C 34.65 0.12 1 408 . 61 VAL CG1 C 21.92 0.12 1 409 . 61 VAL N N 116.72 0.12 1 410 . 62 TYR H H 9.25 0.01 1 411 . 62 TYR HA H 5.06 0.01 1 412 . 62 TYR C C 175.32 0.12 1 413 . 62 TYR CA C 57.89 0.12 1 414 . 62 TYR N N 125.83 0.12 1 415 . 63 THR H H 9.04 0.01 1 416 . 63 THR HA H 5.30 0.01 9 417 . 63 THR HG2 H 1.42 0.01 1 418 . 63 THR CA C 60.06 0.12 1 419 . 63 THR CG2 C 20.06 0.12 1 420 . 63 THR N N 114.78 0.12 1 421 . 65 ALA HA H 3.74 0.01 1 422 . 65 ALA HB H 0.91 0.01 1 423 . 65 ALA CA C 53.21 0.12 9 424 . 65 ALA CB C 19.00 0.12 1 425 . 66 MET HB2 H 2.10 0.01 2 426 . 68 SER HA H 5.02 0.01 1 427 . 68 SER HB2 H 3.72 0.01 2 428 . 69 VAL HA H 4.40 0.01 1 429 . 69 VAL HB H 2.57 0.01 1 430 . 69 VAL HG1 H 0.04 0.01 1 431 . 69 VAL HG2 H -0.39 0.01 1 432 . 69 VAL C C 174.05 0.12 1 433 . 70 CYS H H 7.83 0.01 1 434 . 70 CYS C C 176.43 0.12 1 435 . 70 CYS N N 109.91 0.12 1 436 . 71 GLY H H 8.15 0.01 1 437 . 71 GLY C C 172.45 0.12 1 438 . 71 GLY N N 110.41 0.12 1 439 . 72 TYR H H 8.85 0.01 1 440 . 72 TYR C C 174.19 0.12 1 441 . 72 TYR CA C 58.76 0.12 1 442 . 72 TYR N N 124.99 0.12 1 443 . 73 PHE H H 8.00 0.01 1 444 . 73 PHE C C 173.27 0.12 1 445 . 73 PHE CA C 56.86 0.12 1 446 . 73 PHE N N 130.72 0.12 1 447 . 74 HIS H H 7.28 0.01 1 448 . 74 HIS HA H 3.30 0.01 1 449 . 74 HIS HB2 H 1.67 0.01 2 450 . 74 HIS HB3 H 2.53 0.01 2 451 . 74 HIS C C 176.02 0.12 1 452 . 74 HIS CA C 56.90 0.12 1 453 . 74 HIS CB C 32.57 0.12 1 454 . 74 HIS N N 125.52 0.12 1 455 . 75 ARG H H 7.81 0.01 1 456 . 75 ARG HA H 3.98 0.01 1 457 . 75 ARG HB2 H 1.56 0.01 2 458 . 75 ARG HB3 H 1.52 0.01 2 459 . 75 ARG HG2 H 1.29 0.01 2 460 . 75 ARG HG3 H 1.23 0.01 2 461 . 75 ARG HD2 H 2.89 0.01 2 462 . 75 ARG C C 175.37 0.12 1 463 . 75 ARG CA C 55.96 0.12 1 464 . 75 ARG CB C 30.45 0.12 1 465 . 75 ARG CG C 27.03 0.12 1 466 . 75 ARG CD C 43.14 0.12 1 467 . 75 ARG N N 126.88 0.12 1 468 . 76 SER H H 6.61 0.01 1 469 . 76 SER HA H 4.13 0.01 1 470 . 76 SER HB2 H 3.62 0.01 2 471 . 76 SER HB3 H 3.17 0.01 2 472 . 76 SER CB C 63.82 0.12 1 473 . 76 SER N N 113.48 0.12 1 474 . 77 HIS CA C 55.69 0.12 1 475 . 78 ASN H H 8.18 0.01 1 476 . 78 ASN HA H 4.71 0.01 1 477 . 78 ASN HB2 H 2.85 0.01 2 478 . 78 ASN HB3 H 2.59 0.01 2 479 . 78 ASN CA C 52.67 0.12 1 480 . 78 ASN CB C 38.63 0.12 1 481 . 78 ASN N N 119.22 0.12 1 482 . 79 ARG H H 8.83 0.01 1 483 . 79 ARG HA H 4.18 0.01 1 484 . 79 ARG HB2 H 1.84 0.01 2 485 . 79 ARG HB3 H 1.74 0.01 2 486 . 79 ARG HG2 H 1.62 0.01 2 487 . 79 ARG HD2 H 3.06 0.01 2 488 . 79 ARG C C 177.97 0.12 1 489 . 79 ARG CA C 58.78 0.12 1 490 . 79 ARG CB C 29.87 0.12 1 491 . 79 ARG CD C 43.40 0.12 1 492 . 79 ARG N N 124.97 0.12 1 493 . 80 SER H H 8.28 0.01 1 494 . 80 SER HA H 4.26 0.01 1 495 . 80 SER HB2 H 3.78 0.01 2 496 . 80 SER C C 174.15 0.12 1 497 . 80 SER CA C 59.39 0.12 1 498 . 80 SER CB C 64.09 0.12 1 499 . 80 SER N N 114.42 0.12 1 500 . 81 GLU H H 7.49 0.01 1 501 . 81 GLU HA H 4.01 0.01 1 502 . 81 GLU HB2 H 2.11 0.01 2 503 . 81 GLU HB3 H 2.03 0.01 2 504 . 81 GLU HG2 H 1.92 0.01 2 505 . 81 GLU C C 176.25 0.12 1 506 . 81 GLU CA C 57.05 0.12 1 507 . 81 GLU CG C 35.98 0.12 1 508 . 81 GLU N N 123.35 0.12 1 509 . 82 GLU H H 8.88 0.01 1 510 . 82 GLU HG2 H 2.10 0.01 2 511 . 82 GLU HG3 H 1.65 0.01 2 512 . 82 GLU C C 177.27 0.12 1 513 . 82 GLU CA C 56.96 0.12 1 514 . 82 GLU CG C 37.94 0.12 1 515 . 82 GLU N N 124.36 0.12 1 516 . 83 PHE H H 9.90 0.01 1 517 . 83 PHE C C 173.85 0.12 1 518 . 83 PHE CA C 58.04 0.12 1 519 . 83 PHE N N 125.24 0.12 1 520 . 84 LEU H H 9.60 0.01 1 521 . 84 LEU HA H 4.91 0.01 1 522 . 84 LEU HB2 H 1.50 0.01 2 523 . 84 LEU HD2 H 0.41 0.01 1 524 . 84 LEU C C 175.67 0.12 1 525 . 84 LEU CA C 52.80 0.12 1 526 . 84 LEU CD2 C 23.61 0.12 1 527 . 84 LEU N N 126.37 0.12 1 528 . 85 ILE H H 9.31 0.01 1 529 . 85 ILE C C 173.27 0.12 1 530 . 85 ILE CA C 61.64 0.12 1 531 . 85 ILE N N 124.99 0.12 1 532 . 86 ALA H H 7.98 0.01 1 533 . 86 ALA HA H 5.33 0.01 1 534 . 86 ALA HB H 1.42 0.01 1 535 . 86 ALA C C 176.41 0.12 1 536 . 86 ALA CA C 50.8 0.12 1 537 . 86 ALA CB C 20.06 0.12 1 538 . 86 ALA N N 132.66 0.12 1 539 . 87 GLY H H 8.55 0.01 1 540 . 87 GLY HA2 H 4.97 0.01 1 541 . 87 GLY HA3 H 3.43 0.01 1 542 . 87 GLY C C 172.97 0.12 1 543 . 87 GLY CA C 44.99 0.12 1 544 . 87 GLY N N 106.74 0.12 1 545 . 88 LYS H H 8.50 0.01 1 546 . 88 LYS HA H 4.70 0.01 1 547 . 88 LYS HB2 H 1.60 0.01 2 548 . 88 LYS HG2 H 1.37 0.01 2 549 . 88 LYS HG3 H 1.39 0.01 2 550 . 88 LYS HD2 H 1.58 0.01 2 551 . 88 LYS HE2 H 2.87 0.01 2 552 . 88 LYS C C 175.36 0.12 1 553 . 88 LYS CA C 54.48 0.12 1 554 . 88 LYS CB C 35.66 0.12 1 555 . 88 LYS CG C 24.84 0.12 1 556 . 88 LYS CD C 28.55 0.12 1 557 . 88 LYS CE C 42.01 0.12 1 558 . 88 LYS N N 120.84 0.12 1 559 . 89 LEU H H 9.83 0.01 1 560 . 89 LEU HA H 4.92 0.01 1 561 . 89 LEU HB2 H 1.30 0.01 2 562 . 89 LEU HG H 1.21 0.01 1 563 . 89 LEU HD1 H 0.49 0.01 1 564 . 89 LEU HD2 H 0.55 0.01 1 565 . 89 LEU C C 177.27 0.12 1 566 . 89 LEU CA C 54.17 0.12 1 567 . 89 LEU CB C 43.40 0.12 1 568 . 89 LEU CD1 C 23.77 0.12 1 569 . 89 LEU CD2 C 24.83 0.12 1 570 . 89 LEU N N 125.37 0.12 1 571 . 90 GLN H H 9.21 0.01 1 572 . 90 GLN HA H 4.31 0.01 1 573 . 90 GLN HB2 H 1.34 0.01 2 574 . 90 GLN HG2 H 1.74 0.01 1 575 . 90 GLN C C 175.55 0.12 1 576 . 90 GLN CA C 55.30 0.12 1 577 . 90 GLN CB C 30.4 0.12 1 578 . 90 GLN CG C 33.22 0.12 1 579 . 90 GLN N N 125.24 0.12 1 580 . 91 ASP H H 9.30 0.01 1 581 . 91 ASP HA H 4.18 0.01 1 582 . 91 ASP HB2 H 2.62 0.01 2 583 . 91 ASP HB3 H 2.36 0.01 2 584 . 91 ASP C C 175.70 0.12 1 585 . 91 ASP CA C 55.85 0.12 1 586 . 91 ASP CB C 39.89 0.12 1 587 . 91 ASP N N 128.64 0.12 1 588 . 92 GLY H H 8.35 0.01 1 589 . 92 GLY HA2 H 3.89 0.01 2 590 . 92 GLY HA3 H 3.28 0.01 2 591 . 92 GLY C C 173.03 0.12 1 592 . 92 GLY CA C 45.63 0.12 1 593 . 92 GLY N N 102.72 0.12 1 594 . 93 LEU H H 7.66 0.01 1 595 . 93 LEU HA H 4.47 0.01 1 596 . 93 LEU HB2 H 1.37 0.01 2 597 . 93 LEU HB3 H 0.87 0.01 2 598 . 93 LEU HG H 1.26 0.01 1 599 . 93 LEU HD1 H 0.49 0.01 1 600 . 93 LEU HD2 H -0.01 0.01 1 601 . 93 LEU CA C 53.40 0.12 1 602 . 93 LEU CG C 25.90 0.12 1 603 . 93 LEU CD1 C 21.92 0.12 1 604 . 93 LEU CD2 C 23.51 0.12 1 605 . 93 LEU N N 121.34 0.12 1 606 . 94 LEU H H 9.46 0.01 1 607 . 94 LEU HA H 4.53 0.01 9 608 . 94 LEU HB2 H 1.06 0.01 9 609 . 94 LEU HB3 H 1.00 0.01 9 610 . 94 LEU HG H 1.30 0.01 1 611 . 94 LEU HD1 H 0.66 0.01 1 612 . 94 LEU HD2 H 0.53 0.01 1 613 . 94 LEU C C 174.54 0.12 1 614 . 94 LEU CA C 55.81 0.12 1 615 . 94 LEU CG C 27.55 0.12 1 616 . 94 LEU CD1 C 23.51 0.12 1 617 . 94 LEU CD2 C 25.90 0.12 1 618 . 94 LEU N N 126.75 0.12 1 619 . 95 HIS H H 9.78 0.01 1 620 . 95 HIS HA H 5.49 0.01 1 621 . 95 HIS HB2 H 3.00 0.01 2 622 . 95 HIS C C 176.80 0.12 1 623 . 95 HIS CA C 56.35 0.12 1 624 . 95 HIS N N 129.14 0.12 1 625 . 96 ILE H H 9.02 0.01 1 626 . 96 ILE HA H 4.99 0.01 1 627 . 96 ILE HB H 1.75 0.01 1 628 . 96 ILE C C 177.07 0.12 1 629 . 96 ILE CA C 60.04 0.12 1 630 . 96 ILE N N 113.66 0.12 1 631 . 97 THR H H 9.62 0.01 1 632 . 97 THR C C 176.66 0.12 1 633 . 97 THR CA C 61.71 0.12 1 634 . 97 THR N N 114.67 0.12 1 635 . 98 THR H H 8.91 0.01 1 636 . 98 THR C C 172.88 0.12 1 637 . 98 THR CA C 66.36 0.12 1 638 . 98 THR N N 116.56 0.12 1 639 . 99 CYS H H 8.48 0.01 1 640 . 99 CYS C C 176.08 0.12 1 641 . 99 CYS N N 114.32 0.12 1 642 . 100 SER H H 7.84 0.01 1 643 . 100 SER C C 172.93 0.12 1 644 . 100 SER CA C 59.71 0.12 1 645 . 100 SER N N 119.09 0.12 1 646 . 101 PHE H H 9.72 0.01 1 647 . 101 PHE C C 172.37 0.12 1 648 . 101 PHE CA C 59.88 0.12 1 649 . 101 PHE N N 127.63 0.12 1 650 . 102 VAL H H 7.01 0.01 1 651 . 102 VAL HA H 4.93 0.01 1 652 . 102 VAL HB H 1.61 0.01 1 653 . 102 VAL HG1 H 0.52 0.01 1 654 . 102 VAL HG2 H 0.40 0.01 1 655 . 102 VAL C C 176.12 0.12 1 656 . 102 VAL CA C 61.05 0.12 1 657 . 102 VAL CB C 34.91 0.12 1 658 . 102 VAL CG1 C 20.59 0.12 1 659 . 102 VAL CG2 C 21.39 0.12 1 660 . 102 VAL N N 129.27 0.12 1 661 . 103 ALA H H 8.75 0.01 1 662 . 103 ALA HA H 4.83 0.01 1 663 . 103 ALA HB H 0.85 0.01 1 664 . 103 ALA CA C 50.27 0.12 1 665 . 103 ALA CB C 21.65 0.12 1 666 . 103 ALA N N 128.26 0.12 1 667 . 104 PRO C C 178.93 0.12 1 668 . 104 PRO CA C 62.84 0.12 1 669 . 105 TRP H H 8.99 0.01 1 670 . 105 TRP C C 177.12 0.12 1 671 . 105 TRP CA C 60.47 0.12 1 672 . 105 TRP N N 131.15 0.12 1 673 . 106 ASN H H 9.06 0.01 1 674 . 106 ASN HA H 4.16 0.01 1 675 . 106 ASN HB2 H 2.55 0.01 2 676 . 106 ASN HB3 H 2.68 0.01 2 677 . 106 ASN C C 176.00 0.12 1 678 . 106 ASN CA C 54.78 0.12 1 679 . 106 ASN CB C 37.61 0.12 1 680 . 106 ASN N N 112.66 0.12 1 681 . 107 SER H H 7.58 0.01 1 682 . 107 SER HA H 4.22 0.01 1 683 . 107 SER HB2 H 3.67 0.01 2 684 . 107 SER HB3 H 3.79 0.01 2 685 . 107 SER C C 174.47 0.12 1 686 . 107 SER CA C 59.41 0.12 1 687 . 107 SER CB C 64.09 0.12 1 688 . 107 SER N N 113.92 0.12 1 689 . 108 LEU H H 7.12 0.01 1 690 . 108 LEU HA H 4.26 0.01 1 691 . 108 LEU HG H 1.72 0.01 1 692 . 108 LEU HD1 H 0.76 0.01 1 693 . 108 LEU HD2 H 0.61 0.01 1 694 . 108 LEU C C 177.93 0.12 1 695 . 108 LEU CA C 54.57 0.12 1 696 . 108 LEU CG C 26.43 0.12 1 697 . 108 LEU CD1 C 22.71 0.12 1 698 . 108 LEU CD2 C 27.22 0.12 1 699 . 108 LEU N N 123.48 0.12 1 700 . 109 SER H H 8.61 0.01 1 701 . 109 SER C C 175.14 0.12 1 702 . 109 SER CA C 57.33 0.12 1 703 . 109 SER N N 119.96 0.12 1 704 . 110 LEU H H 8.75 0.01 1 705 . 110 LEU HA H 3.62 0.01 1 706 . 110 LEU HB2 H 1.44 0.01 2 707 . 110 LEU HG H 1.38 0.01 1 708 . 110 LEU HD1 H 0.71 0.01 1 709 . 110 LEU HD2 H 0.63 0.01 1 710 . 110 LEU C C 179.34 0.12 1 711 . 110 LEU CA C 59.12 0.12 1 712 . 110 LEU CB C 41.03 0.12 1 713 . 110 LEU CG C 27.03 0.12 1 714 . 110 LEU CD1 C 24.27 0.12 1 715 . 110 LEU CD2 C 23.90 0.12 1 716 . 110 LEU N N 123.23 0.12 1 717 . 111 ALA H H 8.29 0.01 1 718 . 111 ALA HA H 3.71 0.01 1 719 . 111 ALA HB H 1.13 0.01 1 720 . 111 ALA C C 181.26 0.12 1 721 . 111 ALA CA C 55.42 0.12 1 722 . 111 ALA CB C 18.24 0.12 1 723 . 111 ALA N N 120.47 0.12 1 724 . 112 GLN H H 7.58 0.01 1 725 . 112 GLN C C 178.31 0.12 1 726 . 112 GLN CA C 58.21 0.12 1 727 . 112 GLN N N 119.33 0.12 1 728 . 113 ARG H H 8.34 0.01 1 729 . 113 ARG C C 179.85 0.12 1 730 . 113 ARG CA C 60.95 0.12 1 731 . 113 ARG N N 119.58 0.12 1 732 . 114 ARG H H 8.30 0.01 1 733 . 114 ARG HA H 3.74 0.01 1 734 . 114 ARG HB2 H 1.50 0.01 2 735 . 114 ARG HG2 H 1.49 0.01 2 736 . 114 ARG HG3 H 1.38 0.01 2 737 . 114 ARG HD2 H 2.86 0.01 9 738 . 114 ARG C C 178.63 0.12 1 739 . 114 ARG CA C 59.02 0.12 1 740 . 114 ARG CB C 29.64 0.12 1 741 . 114 ARG CG C 27.52 0.12 1 742 . 114 ARG CD C 43.31 0.01 1 743 . 114 ARG N N 120.71 0.12 1 744 . 115 GLY H H 7.49 0.01 1 745 . 115 GLY C C 176.21 0.12 1 746 . 115 GLY CA C 44.96 0.12 1 747 . 115 GLY N N 111.65 0.12 1 748 . 116 PHE H H 7.71 0.01 1 749 . 116 PHE C C 175.47 0.12 1 750 . 116 PHE CA C 63.19 0.12 1 751 . 116 PHE N N 120.08 0.12 1 752 . 117 THR H H 7.56 0.01 1 753 . 117 THR HA H 3.77 0.01 1 754 . 117 THR HB H 4.04 0.01 1 755 . 117 THR HG2 H 1.17 0.01 1 756 . 117 THR C C 175.60 0.12 1 757 . 117 THR CA C 64.74 0.12 1 758 . 117 THR CB C 69.51 0.12 1 759 . 117 THR CG2 C 21.99 0.12 1 760 . 117 THR N N 107.12 0.12 1 761 . 118 LYS H H 7.90 0.01 1 762 . 118 LYS HA H 4.38 0.01 1 763 . 118 LYS HB2 H 1.62 0.01 2 764 . 118 LYS HB3 H 1.57 0.01 2 765 . 118 LYS HG2 H 1.16 0.01 2 766 . 118 LYS HG3 H 1.11 0.01 2 767 . 118 LYS HD2 H 1.45 0.01 2 768 . 118 LYS C C 177.10 0.12 1 769 . 118 LYS CA C 59.41 0.12 1 770 . 118 LYS N N 120.21 0.12 1 771 . 119 THR H H 8.09 0.01 1 772 . 119 THR HA H 3.98 0.01 1 773 . 119 THR HG2 H 0.84 0.01 1 774 . 119 THR C C 177.72 0.12 1 775 . 119 THR CA C 65.44 0.12 1 776 . 119 THR N N 111.40 0.12 1 777 . 120 TYR H H 9.29 0.01 1 778 . 120 TYR C C 178.81 0.12 1 779 . 120 TYR CA C 56.94 0.12 1 780 . 120 TYR N N 124.23 0.12 1 781 . 121 THR H H 7.95 0.01 1 782 . 121 THR HA H 3.97 0.01 1 783 . 121 THR HB H 4.07 0.01 1 784 . 121 THR HG2 H 1.14 0.01 1 785 . 121 THR C C 176.04 0.12 1 786 . 121 THR CA C 65.24 0.12 1 787 . 121 THR CB C 68.70 0.12 1 788 . 121 THR CG2 C 21.39 0.12 1 789 . 121 THR N N 112.91 0.12 1 790 . 122 VAL H H 7.01 0.01 1 791 . 122 VAL HA H 3.92 0.01 1 792 . 122 VAL HB H 2.04 0.01 1 793 . 122 VAL HG1 H 0.78 0.01 1 794 . 122 VAL C C 177.53 0.12 1 795 . 122 VAL CA C 63.81 0.12 1 796 . 122 VAL CB C 31.47 0.12 1 797 . 122 VAL CG1 C 20.86 0.12 1 798 . 122 VAL N N 118.32 0.12 1 799 . 123 GLY H H 7.86 0.01 1 800 . 123 GLY HA2 H 3.61 0.01 2 801 . 123 GLY HA3 H 4.01 0.01 2 802 . 123 GLY C C 175.12 0.01 1 803 . 123 GLY CA C 45.61 0.12 1 804 . 123 GLY N N 108.63 0.12 1 805 . 124 CYS H H 7.74 0.01 1 806 . 124 CYS HA H 4.64 0.01 1 807 . 124 CYS HB2 H 3.28 0.01 2 808 . 124 CYS HB3 H 2.82 0.01 2 809 . 124 CYS C C 175.25 0.12 1 810 . 124 CYS CA C 54.38 0.12 1 811 . 124 CYS CB C 37.83 0.12 1 812 . 124 CYS N N 118.07 0.12 1 813 . 125 GLU H H 8.31 0.01 1 814 . 125 GLU HA H 4.16 0.01 1 815 . 125 GLU HB2 H 1.79 0.01 2 816 . 125 GLU HB3 H 1.93 0.01 2 817 . 125 GLU HG2 H 2.13 0.01 2 818 . 125 GLU HG3 H 2.08 0.01 2 819 . 125 GLU C C 175.70 0.12 1 820 . 125 GLU CA C 57.02 0.12 1 821 . 125 GLU CB C 30.14 0.12 1 822 . 125 GLU CG C 35.97 0.12 1 823 . 125 GLU N N 122.47 0.12 1 824 . 126 GLU H H 7.94 0.01 1 825 . 126 GLU HA H 3.95 0.01 1 826 . 126 GLU HB2 H 1.71 0.01 2 827 . 126 GLU HB3 H 1.85 0.01 2 828 . 126 GLU HG2 H 2.03 0.01 2 829 . 126 GLU CA C 58.40 0.12 1 830 . 126 GLU CB C 30.94 0.12 1 831 . 126 GLU CG C 36.51 0.12 1 832 . 126 GLU N N 127.50 0.12 1 stop_ save_