data_5231 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Resonance assignments for stromelysin complexed with a beta-sulfonyl hydroxamate inhibitor ; _BMRB_accession_number 5231 _BMRB_flat_file_name bmr5231.str _Entry_type new _Submission_date 2001-12-12 _Accession_date 2001-12-12 _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 Sahasrabudhe Parag V. . 2 Stockman Brian J. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 420 "13C chemical shifts" 477 "15N chemical shifts" 134 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-01-12 update BMRB 'complete entry citation' 2003-06-09 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Resonance assignments for stromelysin complexed with a beta-sulfonyl hydroxamate inhibitor' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 19888686 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Sahasrabudhe Parag V. . 2 Stockman Brian J. . stop_ _Journal_abbreviation 'Biomol. NMR Assignments' _Journal_volume 3 _Journal_issue 2 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 183 _Page_last 186 _Year 2009 _Details . save_ ####################################### # Cited references within the entry # ####################################### save_ref_1 _Saveframe_category citation _Citation_full ; Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, Bax A. NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR. 1995 Nov;6(3):277-93. ; _Citation_title 'NMRPipe: a multidimensional spectral processing system based on UNIX pipes.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 8520220 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Delaglio F . . 2 Grzesiek S . . 3 Vuister 'G W' W. . 4 Zhu G . . 5 Pfeifer J . . 6 Bax A . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of biomolecular NMR' _Journal_volume 6 _Journal_issue 3 _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 277 _Page_last 293 _Year 1995 _Details ; The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks. ; save_ save_ref_2 _Saveframe_category citation _Citation_full ; Moseley HN, Monleon D, Montelione GT. Automatic determination of protein backbone resonance assignments from triple resonance nuclear magnetic resonance data. Methods Enzymol. 2001;339:91-108. ; _Citation_title 'Automatic determination of protein backbone resonance assignments from triple resonance nuclear magnetic resonance data.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 11462827 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Moseley 'H N' N. . 2 Monleon D . . 3 Montelione 'G T' T. . stop_ _Journal_abbreviation 'Meth. Enzymol.' _Journal_name_full 'Methods in enzymology' _Journal_volume 339 _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 91 _Page_last 108 _Year 2001 _Details . save_ ################################## # Molecular system description # ################################## save_system_stromelysin _Saveframe_category molecular_system _Mol_system_name 'Stromelysin complex with a ligand' _Abbreviation_common stromelysin _Enzyme_commission_number 3.4.24.17 loop_ _Mol_system_component_name _Mol_label stromelysin $stromelysin 'beta-hydroxamate inhibitor' $HYIN stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' loop_ _Biological_function 'matrix metalloproteinase' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_stromelysin _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common stromelysin _Abbreviation_common stromelysin _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 173 _Mol_residue_sequence ; FRTFPGIPKWRKTHLTYRIV NYTPDLPKDAVDSAVEKALK VWEEVTPLTFSRLYEGEADI MISFAVREHGDFYPFDGPGN VLAHAYAPGPGINGDAHFDD DEQWTKDTTGTNLFLVAAHE IGHSLGLFHSANTEALMYPL YHSLTDLTRFRLSQDDINGI QSLYGPPPDSPET ; loop_ _Residue_seq_code _Residue_label 1 PHE 2 ARG 3 THR 4 PHE 5 PRO 6 GLY 7 ILE 8 PRO 9 LYS 10 TRP 11 ARG 12 LYS 13 THR 14 HIS 15 LEU 16 THR 17 TYR 18 ARG 19 ILE 20 VAL 21 ASN 22 TYR 23 THR 24 PRO 25 ASP 26 LEU 27 PRO 28 LYS 29 ASP 30 ALA 31 VAL 32 ASP 33 SER 34 ALA 35 VAL 36 GLU 37 LYS 38 ALA 39 LEU 40 LYS 41 VAL 42 TRP 43 GLU 44 GLU 45 VAL 46 THR 47 PRO 48 LEU 49 THR 50 PHE 51 SER 52 ARG 53 LEU 54 TYR 55 GLU 56 GLY 57 GLU 58 ALA 59 ASP 60 ILE 61 MET 62 ILE 63 SER 64 PHE 65 ALA 66 VAL 67 ARG 68 GLU 69 HIS 70 GLY 71 ASP 72 PHE 73 TYR 74 PRO 75 PHE 76 ASP 77 GLY 78 PRO 79 GLY 80 ASN 81 VAL 82 LEU 83 ALA 84 HIS 85 ALA 86 TYR 87 ALA 88 PRO 89 GLY 90 PRO 91 GLY 92 ILE 93 ASN 94 GLY 95 ASP 96 ALA 97 HIS 98 PHE 99 ASP 100 ASP 101 ASP 102 GLU 103 GLN 104 TRP 105 THR 106 LYS 107 ASP 108 THR 109 THR 110 GLY 111 THR 112 ASN 113 LEU 114 PHE 115 LEU 116 VAL 117 ALA 118 ALA 119 HIS 120 GLU 121 ILE 122 GLY 123 HIS 124 SER 125 LEU 126 GLY 127 LEU 128 PHE 129 HIS 130 SER 131 ALA 132 ASN 133 THR 134 GLU 135 ALA 136 LEU 137 MET 138 TYR 139 PRO 140 LEU 141 TYR 142 HIS 143 SER 144 LEU 145 THR 146 ASP 147 LEU 148 THR 149 ARG 150 PHE 151 ARG 152 LEU 153 SER 154 GLN 155 ASP 156 ASP 157 ILE 158 ASN 159 GLY 160 ILE 161 GLN 162 SER 163 LEU 164 TYR 165 GLY 166 PRO 167 PRO 168 PRO 169 ASP 170 SER 171 PRO 172 GLU 173 THR stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2014-11-09 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value BMRB 15120 MMP3 93.06 161 100.00 100.00 7.84e-114 BMRB 15395 MMP3 93.06 161 99.38 99.38 1.75e-112 BMRB 15396 MMP3 93.06 161 99.38 99.38 1.75e-112 BMRB 4173 SLN 100.00 173 100.00 100.00 2.82e-123 BMRB 4364 stromelysin 95.95 166 99.40 99.40 1.35e-116 BMRB 4365 stromelysin 95.95 166 99.40 99.40 1.35e-116 BMRB 4366 stromelysin 95.95 166 99.40 99.40 1.35e-116 BMRB 5099 MMP-3 100.00 173 99.42 100.00 6.99e-123 BMRB 5153 MMP-3 100.00 173 99.42 100.00 6.99e-123 PDB 1B3D Stromelysin-1 100.00 173 100.00 100.00 2.82e-123 PDB 1B8Y "X-Ray Structure Of Human Stromelysin Catalytic Domain Complexed With Non-Peptide Inhibitors: Implications For Inhibitor Selecti" 96.53 167 100.00 100.00 7.35e-119 PDB 1BIW "Design And Synthesis Of Conformationally-Constrained Mmp Inhibitors" 100.00 173 100.00 100.00 2.82e-123 PDB 1BM6 "Solution Structure Of The Catalytic Domain Of Human Stromelysin-1 Complexed To A Potent Non-Peptidic Inhibitor, Nmr, 20 Structu" 100.00 173 100.00 100.00 2.82e-123 PDB 1BQO "Discovery Of Potent, Achiral Matrix Metalloproteinase Inhibitors" 100.00 173 100.00 100.00 2.82e-123 PDB 1C3I "Human Stromelysin-1 Catalytic Domain Complexed With Ro-26-2812" 100.00 173 100.00 100.00 2.82e-123 PDB 1C8T "Human Stromelysin-1 (E202q) Catalytic Domain Complexed With Ro-26-2812" 95.95 167 99.40 100.00 1.83e-117 PDB 1CAQ "X-Ray Structure Of Human Stromelysin Catalytic Domain Complexes With Non-Peptide Inhibitors: Implication For Inhibitor Selectiv" 97.11 168 100.00 100.00 1.08e-119 PDB 1CIZ "X-ray Structure Of Human Stromelysin Catalytic Domain Complexes With Non-peptide Inhibitors: Implication For Inhibitor Selectiv" 97.11 168 100.00 100.00 1.08e-119 PDB 1CQR "Crystal Structure Of The Stromelysin Catalytic Domain At 2.0 A Resolution" 100.00 173 100.00 100.00 2.82e-123 PDB 1D5J "Crystal Structure Of Mmp3 Complexed With A Thiazepine Based Inhibitor." 100.00 173 100.00 100.00 2.82e-123 PDB 1D7X "Crystal Structure Of Mmp3 Complexed With A Modified Proline Scaffold Based Inhibitor." 100.00 173 100.00 100.00 2.82e-123 PDB 1D8F "Crystal Structure Of Mmp3 Complexed With A Piperazine Based Inhibitor." 100.00 173 100.00 100.00 2.82e-123 PDB 1D8M "Crystal Structure Of Mmp3 Complexed With A Heterocycle- Based Inhibitor" 100.00 173 100.00 100.00 2.82e-123 PDB 1G05 "Heterocycle-Based Mmp Inhibitor With P2'substituents" 100.00 173 100.00 100.00 2.82e-123 PDB 1G49 "A Carboxylic Acid Based Inhibitor In Complex With Mmp3" 100.00 173 100.00 100.00 2.82e-123 PDB 1G4K "X-ray Structure Of A Novel Matrix Metalloproteinase Inhibitor Complexed To Stromelysin" 97.11 168 100.00 100.00 1.08e-119 PDB 1HFS "Crystal Structure Of The Catalytic Domain Of Human Fibroblast Stromelysin-1 Inhibited With The N-Carboxy-Alkyl Inhibitor L-764," 92.49 160 100.00 100.00 4.45e-113 PDB 1HY7 "A Carboxylic Acid Based Inhibitor In Complex With Mmp3" 100.00 173 100.00 100.00 2.82e-123 PDB 1OO9 "Orientation In Solution Of Mmp-3 Catalytic Domain And N- Timp-1 From Residual Dipolar Couplings" 97.11 168 100.00 100.00 1.08e-119 PDB 1QIA "Crystal Structure Of Stromelysin Catalytic Domain" 93.64 162 100.00 100.00 9.73e-115 PDB 1QIC "Crystal Structure Of Stromelysin Catalytic Domain" 93.06 161 100.00 100.00 5.96e-114 PDB 1SLM "Crystal Structure Of Fibroblast Stromelysin-1: The C-Truncated Human Proenzyme" 100.00 255 100.00 100.00 1.92e-123 PDB 1SLN "Crystal Structure Of The Catalytic Domain Of Human Fibroblast Stromelysin-1 Inhibited With The N-Carboxy-Alkyl Inhibitor L-702," 100.00 173 100.00 100.00 2.82e-123 PDB 1UEA "Mmp-3TIMP-1 Complex" 100.00 173 98.84 98.84 3.58e-121 PDB 1UMS "Stromelysin-1 Catalytic Domain With Hydrophobic Inhibitor Bound, Ph 7.0, 32oc, 20 Mm Cacl2, 15% Acetonitrile; Nmr Ensemble Of 2" 100.00 174 100.00 100.00 3.97e-123 PDB 1UMT "Stromelysin-1 Catalytic Domain With Hydrophobic Inhibitor Bound, Ph 7.0, 32oc, 20 Mm Cacl2, 15% Acetonitrile; Nmr Average Of 20" 100.00 174 100.00 100.00 3.97e-123 PDB 1USN "Crystal Structure Of The Catalytic Domain Of Human Fibroblast Stromelysin-1 Inhibited With Thiadiazole Inhibitor Pnu-142372" 95.38 165 100.00 100.00 3.18e-117 PDB 2D1O "Stromelysin-1 (Mmp-3) Complexed To A Hydroxamic Acid Inhibitor" 98.84 171 100.00 100.00 7.23e-122 PDB 2JNP "Solution Structure Of Matrix Metalloproteinase 3 (Mmp-3) In The Presence Of N-Isobutyl-N-[4- Methoxyphenylsulfonyl]glycyl Hydro" 93.06 161 100.00 100.00 7.84e-114 PDB 2JT5 "Solution Structure Of Matrix Metalloproteinase 3 (mmp-3) In The Presence Of N-hydroxy-2-[n-(2-hydroxyethyl)biphenyl-4- Sulfonam" 93.06 161 100.00 100.00 7.84e-114 PDB 2JT6 "Solution Structure Of Matrix Metalloproteinase 3 (Mmp-3) In The Presence Of 3-4'-Cyanobyphenyl-4-Yloxy)-N- Hdydroxypropionamide" 93.06 161 100.00 100.00 7.84e-114 PDB 2SRT "Catalytic Domain Of Human Stromelysin-1 At Ph 5.5 And 40oc Complexed With Inhibitor" 100.00 173 100.00 100.00 2.82e-123 PDB 2USN "Crystal Structure Of The Catalytic Domain Of Human Fibroblast Stromelysin-1 Inhibited With Thiadiazole Inhibitor Pnu-141803" 95.38 165 100.00 100.00 3.18e-117 PDB 3OHL "Catalytic Domain Of Stromelysin-1 In Complex With N-Hydroxy-2-(4- Methoxy-N-(Pyridine-3-Ylmethyl)phenylsulfonamido)acetamide" 96.53 167 100.00 100.00 7.35e-119 PDB 3OHO "Catalytic Domain Of Stromelysin-1 In Complex With N-Hydroxy-2-(4- Methylphenylsulfonamido)acetamide" 97.69 169 100.00 100.00 2.41e-120 PDB 3USN "Structure Of The Catalytic Domain Of Human Fibroblast Stromelysin-1 Inhibited With The Thiadiazole Inhibitor Ipnu-107859, Nmr, " 97.11 168 100.00 100.00 1.08e-119 PDB 4DPE "Structure Of Mmp3 Complexed With A Platinum-based Inhibitor." 100.00 173 100.00 100.00 2.82e-123 PDB 4G9L "Structure Of Mmp3 Complexed With Nngh Inhibitor" 100.00 173 100.00 100.00 2.82e-123 PDB 4JA1 "Structure Of Mmp3 Complexed With A Platinum-based Inhibitor" 100.00 173 100.00 100.00 2.82e-123 DBJ BAD97003 "matrix metalloproteinase 3 preproprotein variant [Homo sapiens]" 100.00 477 100.00 100.00 3.99e-120 DBJ BAD97011 "matrix metalloproteinase 3 preproprotein variant [Homo sapiens]" 100.00 477 100.00 100.00 3.99e-120 DBJ BAG36115 "unnamed protein product [Homo sapiens]" 100.00 477 100.00 100.00 3.21e-120 EMBL CAA28859 "preprostromelysin [Homo sapiens]" 100.00 477 100.00 100.00 3.21e-120 GB AAA00036 "prostromelysin=matrix metalloproteinase [human, Peptide, 477 aa]" 100.00 477 100.00 100.00 3.99e-120 GB AAA36321 "matrix metalloproteinase-3 [Homo sapiens]" 100.00 477 100.00 100.00 3.99e-120 GB AAB36942 "stromelysin [Homo sapiens]" 100.00 477 100.00 100.00 3.99e-120 GB AAD45887 "stromelysin catalytic domain [synthetic construct]" 100.00 174 100.00 100.00 3.97e-123 GB AAH69676 "Matrix metallopeptidase 3 (stromelysin 1, progelatinase) [Homo sapiens]" 100.00 477 100.00 100.00 3.99e-120 REF NP_002413 "stromelysin-1 preproprotein [Homo sapiens]" 100.00 477 100.00 100.00 3.21e-120 REF XP_002822450 "PREDICTED: stromelysin-1 [Pongo abelii]" 100.00 477 98.84 100.00 1.26e-119 REF XP_003253099 "PREDICTED: stromelysin-1 [Nomascus leucogenys]" 100.00 477 99.42 100.00 2.45e-120 REF XP_003828425 "PREDICTED: stromelysin-1 [Pan paniscus]" 100.00 477 100.00 100.00 1.93e-120 REF XP_004052086 "PREDICTED: stromelysin-1 [Gorilla gorilla gorilla]" 100.00 477 98.84 99.42 9.78e-119 SP P08254 "RecName: Full=Stromelysin-1; Short=SL-1; AltName: Full=Matrix metalloproteinase-3; Short=MMP-3; AltName: Full=Transin-1; Flags:" 100.00 477 100.00 100.00 3.21e-120 stop_ save_ ############# # Ligands # ############# save_HYIN _Saveframe_category ligand _Mol_type non-polymer _Name_common 'beta-hydroxamate inhibitor' _Name_IUPAC N-hydroxy-3-[(4-methoxyphenyl)sulfonyl]-2-{[(4-methoxyphenyl)sulfonyl]methyl}propanamide _BMRB_code HYIN _PDB_code . _Molecular_mass . _Mol_charge 0 _Mol_paramagnetic no _Mol_aromatic yes _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons N1 . N . 0 . ? S1 . S . 0 . ? S2 . S . 0 . ? O1 . O . 0 . ? O2 . O . 0 . ? O3 . O . 0 . ? O4 . O . 0 . ? O5 . O . 0 . ? O6 . O . 0 . ? O7 . O . 0 . ? O8 . O . 0 . ? C1 . C . 0 . ? C2 . C . 0 . ? C3 . C . 0 . ? C4 . C . 0 . ? C5 . C . 0 . ? C6 . C . 0 . ? C7 . C . 0 . ? C8 . C . 0 . ? C9 . C . 0 . ? C10 . C . 0 . ? C11 . C . 0 . ? C12 . C . 0 . ? C13 . C . 0 . ? C14 . C . 0 . ? C15 . C . 0 . ? C16 . C . 0 . ? C17 . C . 0 . ? C18 . C . 0 . ? HO . H . 0 . ? HN . H . 0 . ? H2 . H . 0 . ? H3A . H . 0 . ? H3B . H . 0 . ? H4A . H . 0 . ? H4B . H . 0 . ? H6 . H . 0 . ? H7 . H . 0 . ? H9 . H . 0 . ? H10 . H . 0 . ? H13 . H . 0 . ? H14 . H . 0 . ? H16 . H . 0 . ? H17 . H . 0 . ? H11A . H . 0 . ? H11B . H . 0 . ? H11C . H . 0 . ? H18A . H . 0 . ? H18B . H . 0 . ? H18C . H . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name SING HO O1 . . SING O1 N1 . . SING N1 HN . . SING N1 C1 . . SING C1 C2 . . SING C2 C3 . . SING C2 C4 . . SING C2 H2 . . SING C3 H3A . . SING C3 H3B . . SING C3 S1 . . SING S1 C5 . . SING C5 C6 . . SING C6 H6 . . SING C7 H7 . . SING C7 C8 . . SING C8 O5 . . SING C9 H9 . . SING C9 C10 . . SING C10 H10 . . SING O5 C11 . . SING C11 H11A . . SING C11 H11B . . SING C11 H11C . . SING C4 H4A . . SING C4 H4B . . SING C4 S2 . . SING S2 C12 . . SING C12 C13 . . SING C13 H13 . . SING C14 H14 . . SING C14 C15 . . SING C15 O8 . . SING C16 H16 . . SING C16 C17 . . SING C17 H17 . . SING O8 C18 . . SING C18 H18A . . SING C18 H18B . . SING C18 H18C . . DOUB C1 O2 . . DOUB S1 O3 . . DOUB S1 O4 . . DOUB C5 C6 . . DOUB C7 C8 . . DOUB C9 C10 . . DOUB S2 O6 . . DOUB S2 O7 . . DOUB C12 C13 . . DOUB C14 C15 . . DOUB C16 C17 . . 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 $stromelysin Human 9606 Eukaryota Metazoa Homo sapiens stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name _Details $stromelysin 'recombinant technology' 'E. coli' . . BL21(DE3)(pLyseE) pstro255 ; Stromelysin was prepared by overexpression in E.coli strain BL21(DE3)(pLyseE) transformed with pstro255 expression vector. ; $HYIN 'chemical synthesis' . . . . . . 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 $stromelysin 0.9 mM '[U-100% 13C; U-100% 15N]' $HYIN 1 mM . d-imidazole 10 mM . CaCl2 2.5 mM . ZnCl2 5 uM . NaN3 0.02 % . stop_ save_ ############################ # Computer software used # ############################ save_XWINNMR _Saveframe_category software _Name XWINNMR _Version 2.6 loop_ _Task 'data acquisition' stop_ _Details . save_ save_NMRPIPE _Saveframe_category software _Name NMRPIPE _Version . loop_ _Task 'data processing' stop_ _Details . _Citation_label $ref_1 save_ save_SPARKY _Saveframe_category software _Name SPARKY _Version . loop_ _Task 'peak picking' 'peak management' stop_ _Details 'Goddard and Kneller, University of California, San Francisco.' save_ save_AUTOASSIGN _Saveframe_category software _Name AUTOASSIGN _Version . loop_ _Task 'Automated resonance assignment' stop_ _Details 'Licensed from Geneformatics (http://www.geneformatics.com).' _Citation_label $ref_2 save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _Sample_label . save_ save_HNCO_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label . save_ save_HNCA_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label . save_ save_HN(CO)CA_4 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _Sample_label . save_ save_CBCA(CO)NH_5 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _Sample_label . save_ save_CBCANH_6 _Saveframe_category NMR_applied_experiment _Experiment_name CBCANH _Sample_label . save_ save_HBHA(CO)NH_7 _Saveframe_category NMR_applied_experiment _Experiment_name HBHA(CO)NH _Sample_label . save_ save_(H)CC(CO)NH-TOCSY_8 _Saveframe_category NMR_applied_experiment _Experiment_name (H)CC(CO)NH-TOCSY _Sample_label . save_ save_H(CC)(CO)NH-TOCSY_9 _Saveframe_category NMR_applied_experiment _Experiment_name H(CC)(CO)NH-TOCSY _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name CBCANH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name HBHA(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_8 _Saveframe_category NMR_applied_experiment _Experiment_name (H)CC(CO)NH-TOCSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_9 _Saveframe_category NMR_applied_experiment _Experiment_name H(CC)(CO)NH-TOCSY _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_stromelysin_condition_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.6 0.1 pH temperature 300 0.1 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 H2O H 1 protons ppm 4.70 internal direct cylindrical internal parallel . H2O C 13 protons ppm 4.70 internal indirect cylindrical internal parallel 0.251449530 H2O N 15 protons ppm 4.70 internal indirect cylindrical internal parallel 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_stromelysin_CS _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $stromelysin_condition_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name stromelysin _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 2 ARG HA H 4.879 0.02 1 2 . 2 ARG C C 175.4 0.1 1 3 . 2 ARG CA C 55.74 0.1 1 4 . 2 ARG CB C 35.74 0.1 1 5 . 2 ARG CG C 31.56 0.1 1 6 . 3 THR H H 8.36 0.02 1 7 . 3 THR CA C 60.38 0.1 1 8 . 3 THR N N 112.5 0.1 1 9 . 11 ARG HA H 4.648 0.02 1 10 . 11 ARG HB2 H 2.268 0.02 2 11 . 11 ARG HG2 H 1.889 0.02 2 12 . 11 ARG HD2 H 3.295 0.02 2 13 . 11 ARG C C 174.8 0.1 1 14 . 11 ARG CA C 55.39 0.1 1 15 . 11 ARG CB C 29.06 0.1 1 16 . 11 ARG CG C 27.98 0.1 1 17 . 11 ARG CD C 43.51 0.1 1 18 . 12 LYS H H 7.50 0.02 1 19 . 12 LYS HA H 4.822 0.02 1 20 . 12 LYS HB2 H 2.077 0.02 2 21 . 12 LYS C C 174.3 0.1 1 22 . 12 LYS CA C 54.36 0.1 1 23 . 12 LYS CB C 34.58 0.1 1 24 . 12 LYS N N 116.7 0.1 1 25 . 13 THR H H 7.99 0.02 1 26 . 13 THR HA H 4.396 0.02 1 27 . 13 THR HG2 H 1.175 0.02 1 28 . 13 THR C C 172.6 0.1 1 29 . 13 THR CA C 61.29 0.1 1 30 . 13 THR CB C 69.49 0.1 1 31 . 13 THR CG2 C 21.84 0.1 1 32 . 13 THR N N 105.4 0.1 1 33 . 14 HIS H H 7.01 0.02 1 34 . 14 HIS HA H 5.181 0.02 1 35 . 14 HIS HB2 H 3.471 0.02 1 36 . 14 HIS HB3 H 3.124 0.02 1 37 . 14 HIS C C 173.8 0.1 1 38 . 14 HIS CA C 54.17 0.1 1 39 . 14 HIS CB C 29.76 0.1 1 40 . 14 HIS N N 119.7 0.1 1 41 . 15 LEU H H 8.21 0.02 1 42 . 15 LEU HA H 4.551 0.02 1 43 . 15 LEU HB2 H 1.381 0.02 2 44 . 15 LEU HG H 1.255 0.02 1 45 . 15 LEU HD1 H 0.781 0.02 2 46 . 15 LEU C C 176.3 0.1 1 47 . 15 LEU CA C 53.12 0.1 1 48 . 15 LEU CB C 45.28 0.1 1 49 . 15 LEU N N 128.0 0.1 1 50 . 16 THR H H 9.16 0.02 1 51 . 16 THR HA H 5.809 0.02 1 52 . 16 THR HG2 H 1.192 0.02 1 53 . 16 THR C C 174.5 0.1 1 54 . 16 THR CA C 58.31 0.1 1 55 . 16 THR CB C 73.3 0.1 1 56 . 16 THR CG2 C 22.29 0.1 1 57 . 16 THR N N 110.5 0.1 1 58 . 17 TYR H H 8.58 0.02 1 59 . 17 TYR CA C 54.97 0.1 1 60 . 17 TYR CB C 42.34 0.1 1 61 . 17 TYR N N 117.8 0.1 1 62 . 18 ARG HA H 4.412 0.02 1 63 . 18 ARG C C 174.0 0.1 1 64 . 18 ARG CA C 55.15 0.1 1 65 . 18 ARG CB C 34.91 0.1 1 66 . 18 ARG CG C 27.44 0.1 1 67 . 19 ILE H H 8.37 0.02 1 68 . 19 ILE HA H 4.369 0.02 1 69 . 19 ILE HG2 H 1.241 0.02 1 70 . 19 ILE C C 175.5 0.1 1 71 . 19 ILE CA C 61.76 0.1 1 72 . 19 ILE CB C 37.39 0.1 1 73 . 19 ILE N N 128.2 0.1 1 74 . 20 VAL H H 9.50 0.02 1 75 . 20 VAL HA H 3.465 0.02 1 76 . 20 VAL HB H 2.143 0.02 1 77 . 20 VAL HG1 H 1.051 0.02 2 78 . 20 VAL C C 175.4 0.1 1 79 . 20 VAL CA C 66.29 0.1 1 80 . 20 VAL CB C 32.86 0.1 1 81 . 20 VAL CG1 C 24.01 0.1 1 82 . 20 VAL CG2 C 21.42 0.1 1 83 . 20 VAL N N 129.9 0.1 1 84 . 21 ASN H H 7.63 0.02 1 85 . 21 ASN HA H 4.757 0.02 1 86 . 21 ASN C C 169.9 0.1 1 87 . 21 ASN CA C 51.49 0.1 1 88 . 21 ASN CB C 39.81 0.1 1 89 . 21 ASN N N 116.2 0.1 1 90 . 22 TYR H H 8.05 0.02 1 91 . 22 TYR HA H 4.504 0.02 1 92 . 22 TYR HB2 H 3.121 0.02 1 93 . 22 TYR HB3 H 2.864 0.02 1 94 . 22 TYR C C 177.5 0.1 1 95 . 22 TYR CA C 58.76 0.1 1 96 . 22 TYR CB C 41.61 0.1 1 97 . 22 TYR N N 112.0 0.1 1 98 . 23 THR H H 8.56 0.02 1 99 . 23 THR CA C 60.87 0.1 1 100 . 23 THR N N 123.8 0.1 1 101 . 24 PRO HA H 4.668 0.02 1 102 . 24 PRO C C 177.4 0.1 1 103 . 24 PRO CA C 63.34 0.1 1 104 . 24 PRO CB C 32.03 0.1 1 105 . 25 ASP H H 8.83 0.02 1 106 . 25 ASP HA H 4.157 0.02 1 107 . 25 ASP HB2 H 3.32 0.02 2 108 . 25 ASP C C 175.4 0.1 1 109 . 25 ASP CA C 56.06 0.1 1 110 . 25 ASP CB C 41.63 0.1 1 111 . 25 ASP N N 121.8 0.1 1 112 . 26 LEU H H 6.94 0.02 1 113 . 26 LEU CA C 51.36 0.1 1 114 . 26 LEU CB C 47.6 0.1 1 115 . 26 LEU N N 116.4 0.1 1 116 . 27 PRO HA H 4.563 0.02 1 117 . 27 PRO C C 177.7 0.1 1 118 . 27 PRO CA C 62.32 0.1 1 119 . 27 PRO CB C 32.65 0.1 1 120 . 28 LYS H H 8.60 0.02 1 121 . 28 LYS HA H 3.793 0.02 1 122 . 28 LYS HG2 H 1.302 0.02 2 123 . 28 LYS C C 178.2 0.1 1 124 . 28 LYS CA C 60.61 0.1 1 125 . 28 LYS CB C 32.74 0.1 1 126 . 28 LYS CG C 24.94 0.1 1 127 . 28 LYS N N 123.8 0.1 1 128 . 29 ASP H H 8.45 0.02 1 129 . 29 ASP HA H 4.411 0.02 1 130 . 29 ASP HB2 H 2.732 0.02 2 131 . 29 ASP C C 178.4 0.1 1 132 . 29 ASP CA C 56.8 0.1 1 133 . 29 ASP CB C 40.15 0.1 1 134 . 29 ASP N N 113.7 0.1 1 135 . 30 ALA H H 7.28 0.02 1 136 . 30 ALA HA H 4.368 0.02 1 137 . 30 ALA HB H 1.643 0.02 1 138 . 30 ALA C C 180.6 0.1 1 139 . 30 ALA CA C 54.34 0.1 1 140 . 30 ALA CB C 19.4 0.1 1 141 . 30 ALA N N 122.7 0.1 1 142 . 31 VAL H H 7.48 0.02 1 143 . 31 VAL HA H 3.606 0.02 1 144 . 31 VAL HB H 2.794 0.02 1 145 . 31 VAL HG1 H 0.982 0.02 2 146 . 31 VAL C C 176.9 0.1 1 147 . 31 VAL CA C 66.46 0.1 1 148 . 31 VAL CB C 31.6 0.1 1 149 . 31 VAL CG1 C 24.56 0.1 2 150 . 31 VAL N N 121.8 0.1 1 151 . 32 ASP H H 8.52 0.02 1 152 . 32 ASP HA H 4.681 0.02 1 153 . 32 ASP HB2 H 3.086 0.02 2 154 . 32 ASP C C 178.6 0.1 1 155 . 32 ASP CA C 58.18 0.1 1 156 . 32 ASP CB C 40.16 0.1 1 157 . 32 ASP N N 119.6 0.1 1 158 . 33 SER H H 8.00 0.02 1 159 . 33 SER HA H 4.299 0.02 1 160 . 33 SER HB2 H 4.04 0.02 2 161 . 33 SER C C 176.5 0.1 1 162 . 33 SER CA C 61.7 0.1 1 163 . 33 SER CB C 63.52 0.1 1 164 . 33 SER N N 112.4 0.1 1 165 . 34 ALA H H 7.63 0.02 1 166 . 34 ALA HA H 4.252 0.02 1 167 . 34 ALA HB H 1.531 0.02 1 168 . 34 ALA C C 179.3 0.1 1 169 . 34 ALA CA C 55.92 0.1 1 170 . 34 ALA CB C 18.49 0.1 1 171 . 34 ALA N N 124.0 0.1 1 172 . 35 VAL H H 7.97 0.02 1 173 . 35 VAL HA H 3.314 0.02 1 174 . 35 VAL HB H 2.149 0.02 1 175 . 35 VAL HG1 H 0.784 0.02 2 176 . 35 VAL C C 176.9 0.1 1 177 . 35 VAL CA C 67.24 0.1 1 178 . 35 VAL CB C 31.51 0.1 1 179 . 35 VAL CG1 C 22.37 0.1 2 180 . 35 VAL N N 116.0 0.1 1 181 . 36 GLU H H 8.39 0.02 1 182 . 36 GLU HA H 3.764 0.02 1 183 . 36 GLU HB2 H 2.274 0.02 2 184 . 36 GLU HG2 H 2.556 0.02 2 185 . 36 GLU C C 179.6 0.1 1 186 . 36 GLU CA C 60.5 0.1 1 187 . 36 GLU CB C 29.8 0.1 1 188 . 36 GLU CG C 37.46 0.1 1 189 . 36 GLU N N 118.2 0.1 1 190 . 37 LYS H H 8.25 0.02 1 191 . 37 LYS HA H 4.018 0.02 1 192 . 37 LYS HB2 H 1.953 0.02 1 193 . 37 LYS HB3 H 1.762 0.02 1 194 . 37 LYS HG2 H 1.399 0.02 2 195 . 37 LYS C C 178.7 0.1 1 196 . 37 LYS CA C 59.87 0.1 1 197 . 37 LYS CB C 32.67 0.1 1 198 . 37 LYS CG C 26.26 0.1 1 199 . 37 LYS N N 119.2 0.1 1 200 . 38 ALA H H 8.05 0.02 1 201 . 38 ALA HA H 4.09 0.02 1 202 . 38 ALA HB H 1.501 0.02 1 203 . 38 ALA C C 177.8 0.1 1 204 . 38 ALA CA C 55.88 0.1 1 205 . 38 ALA CB C 18.47 0.1 1 206 . 38 ALA N N 123.5 0.1 1 207 . 39 LEU H H 7.66 0.02 1 208 . 39 LEU HA H 3.77 0.02 1 209 . 39 LEU HB2 H 1.699 0.02 1 210 . 39 LEU HB3 H 1.566 0.02 1 211 . 39 LEU C C 179.7 0.1 1 212 . 39 LEU CA C 57.86 0.1 1 213 . 39 LEU CB C 41.1 0.1 1 214 . 39 LEU N N 115.3 0.1 1 215 . 40 LYS H H 7.77 0.02 1 216 . 40 LYS HA H 4.196 0.02 1 217 . 40 LYS HB2 H 2.078 0.02 2 218 . 40 LYS HG2 H 1.38 0.02 2 219 . 40 LYS HD2 H 1.685 0.02 2 220 . 40 LYS HE2 H 2.751 0.02 2 221 . 40 LYS C C 178.6 0.1 1 222 . 40 LYS CA C 58.77 0.1 1 223 . 40 LYS CB C 32.39 0.1 1 224 . 40 LYS CG C 25.49 0.1 1 225 . 40 LYS CD C 28.98 0.1 1 226 . 40 LYS N N 119.0 0.1 1 227 . 41 VAL H H 7.41 0.02 1 228 . 41 VAL HA H 3.89 0.02 1 229 . 41 VAL HB H 2.14 0.02 1 230 . 41 VAL HG1 H 0.969 0.02 1 231 . 41 VAL HG2 H 0.716 0.02 1 232 . 41 VAL C C 177.2 0.1 1 233 . 41 VAL CA C 65.4 0.1 1 234 . 41 VAL CB C 31.64 0.1 1 235 . 41 VAL CG1 C 22.03 0.1 2 236 . 41 VAL N N 114.3 0.1 1 237 . 42 TRP H H 6.65 0.02 1 238 . 42 TRP HA H 4.795 0.02 1 239 . 42 TRP HB2 H 3.924 0.02 2 240 . 42 TRP C C 180.1 0.1 1 241 . 42 TRP CA C 57.97 0.1 1 242 . 42 TRP CB C 30.72 0.1 1 243 . 42 TRP N N 117.6 0.1 1 244 . 43 GLU H H 8.47 0.02 1 245 . 43 GLU HA H 4.064 0.02 1 246 . 43 GLU HB2 H 2.408 0.02 2 247 . 43 GLU HG2 H 2.529 0.02 2 248 . 43 GLU C C 178.2 0.1 1 249 . 43 GLU CA C 59.85 0.1 1 250 . 43 GLU CB C 31.37 0.1 1 251 . 43 GLU CG C 36.81 0.1 1 252 . 43 GLU N N 122.9 0.1 1 253 . 44 GLU H H 7.74 0.02 1 254 . 44 GLU HA H 4.209 0.02 1 255 . 44 GLU HB2 H 1.824 0.02 2 256 . 44 GLU HG2 H 2.676 0.02 1 257 . 44 GLU HG3 H 2.435 0.02 1 258 . 44 GLU C C 177.9 0.1 1 259 . 44 GLU CA C 58.88 0.1 1 260 . 44 GLU CB C 31.14 0.1 1 261 . 44 GLU CG C 37.32 0.1 1 262 . 44 GLU N N 111.4 0.1 1 263 . 45 VAL H H 7.02 0.02 1 264 . 45 VAL HA H 4.766 0.02 1 265 . 45 VAL HB H 2.747 0.02 1 266 . 45 VAL HG1 H 1.235 0.02 1 267 . 45 VAL HG2 H 0.986 0.02 1 268 . 45 VAL C C 174.5 0.1 1 269 . 45 VAL CA C 60.4 0.1 1 270 . 45 VAL CB C 32.78 0.1 1 271 . 45 VAL CG1 C 21.8 0.1 1 272 . 45 VAL CG2 C 19.45 0.1 1 273 . 45 VAL N N 104.8 0.1 1 274 . 46 THR H H 7.59 0.02 1 275 . 46 THR CA C 60.43 0.1 1 276 . 46 THR CB C 72.42 0.1 1 277 . 46 THR N N 111.6 0.1 1 278 . 47 PRO HA H 5.01 0.02 1 279 . 47 PRO HB2 H 2.654 0.02 1 280 . 47 PRO HB3 H 1.75 0.02 1 281 . 47 PRO HG2 H 2.167 0.02 2 282 . 47 PRO C C 176.7 0.1 1 283 . 47 PRO CA C 62.27 0.1 1 284 . 47 PRO CB C 31.95 0.1 1 285 . 48 LEU H H 7.35 0.02 1 286 . 48 LEU HA H 4.575 0.02 1 287 . 48 LEU HG H 1.427 0.02 1 288 . 48 LEU C C 176.8 0.1 1 289 . 48 LEU CA C 55.17 0.1 1 290 . 48 LEU CB C 43.11 0.1 1 291 . 48 LEU CG C 26.98 0.1 1 292 . 48 LEU N N 117.8 0.1 1 293 . 49 THR H H 8.11 0.02 1 294 . 49 THR HA H 4.633 0.02 1 295 . 49 THR HB H 4.234 0.02 1 296 . 49 THR HG2 H 1.144 0.02 1 297 . 49 THR C C 172.5 0.1 1 298 . 49 THR CA C 59.9 0.1 1 299 . 49 THR CB C 72.84 0.1 1 300 . 49 THR CG2 C 22.43 0.1 1 301 . 49 THR N N 110.2 0.1 1 302 . 50 PHE H H 8.24 0.02 1 303 . 50 PHE HA H 5.795 0.02 1 304 . 50 PHE HB2 H 2.882 0.02 2 305 . 50 PHE C C 176.9 0.1 1 306 . 50 PHE CA C 56.4 0.1 1 307 . 50 PHE CB C 43.66 0.1 1 308 . 50 PHE N N 117.1 0.1 1 309 . 51 SER H H 8.67 0.02 1 310 . 51 SER HA H 4.994 0.02 1 311 . 51 SER HB2 H 3.97 0.02 1 312 . 51 SER HB3 H 3.76 0.02 1 313 . 51 SER C C 171.4 0.1 1 314 . 51 SER CA C 57.78 0.1 1 315 . 51 SER CB C 65.85 0.1 1 316 . 51 SER N N 116.5 0.1 1 317 . 52 ARG H H 8.54 0.02 1 318 . 52 ARG HA H 3.592 0.02 1 319 . 52 ARG HB2 H 1.962 0.02 2 320 . 52 ARG C C 175.7 0.1 1 321 . 52 ARG CA C 55.75 0.1 1 322 . 52 ARG CB C 32.15 0.1 1 323 . 52 ARG N N 125.1 0.1 1 324 . 53 LEU H H 8.54 0.02 1 325 . 53 LEU HA H 4.746 0.02 1 326 . 53 LEU HB2 H 1.734 0.02 2 327 . 53 LEU C C 176.9 0.1 1 328 . 53 LEU CA C 53.16 0.1 1 329 . 53 LEU CB C 45.75 0.1 1 330 . 53 LEU N N 125.3 0.1 1 331 . 54 TYR H H 9.20 0.02 1 332 . 54 TYR HA H 4.439 0.02 1 333 . 54 TYR HB2 H 2.759 0.02 2 334 . 54 TYR C C 174.1 0.1 1 335 . 54 TYR CA C 58.91 0.1 1 336 . 54 TYR CB C 39.72 0.1 1 337 . 54 TYR N N 119.0 0.1 1 338 . 55 GLU H H 7.45 0.02 1 339 . 55 GLU HA H 4.466 0.02 1 340 . 55 GLU HB2 H 2.149 0.02 1 341 . 55 GLU HB3 H 1.985 0.02 1 342 . 55 GLU HG2 H 2.213 0.02 2 343 . 55 GLU C C 174.7 0.1 1 344 . 55 GLU CA C 54.79 0.1 1 345 . 55 GLU CB C 33.2 0.1 1 346 . 55 GLU CG C 35.63 0.1 1 347 . 55 GLU N N 116.7 0.1 1 348 . 56 GLY H H 8.49 0.02 1 349 . 56 GLY HA2 H 4.104 0.02 1 350 . 56 GLY HA3 H 3.831 0.02 1 351 . 56 GLY C C 172.3 0.1 1 352 . 56 GLY CA C 44.69 0.1 1 353 . 56 GLY N N 108.5 0.1 1 354 . 57 GLU H H 8.18 0.02 1 355 . 57 GLU HA H 4.421 0.02 1 356 . 57 GLU HB2 H 1.978 0.02 2 357 . 57 GLU HG2 H 2.225 0.02 2 358 . 57 GLU C C 175.5 0.1 1 359 . 57 GLU CA C 56.1 0.1 1 360 . 57 GLU CB C 30.14 0.1 1 361 . 57 GLU CG C 36.35 0.1 1 362 . 57 GLU N N 119.2 0.1 1 363 . 58 ALA H H 7.99 0.02 1 364 . 58 ALA HA H 4.457 0.02 1 365 . 58 ALA HB H 2.014 0.02 1 366 . 58 ALA C C 176.7 0.1 1 367 . 58 ALA CA C 49.77 0.1 1 368 . 58 ALA CB C 22.22 0.1 1 369 . 58 ALA N N 131.6 0.1 1 370 . 59 ASP H H 8.30 0.02 1 371 . 59 ASP CA C 59.7 0.1 1 372 . 59 ASP CB C 41.36 0.1 1 373 . 59 ASP N N 122.2 0.1 1 374 . 60 ILE HA H 4.309 0.02 1 375 . 60 ILE HB H 1.56 0.02 1 376 . 60 ILE HG12 H 1.791 0.02 2 377 . 60 ILE HG2 H 1.048 0.02 1 378 . 60 ILE C C 174.5 0.1 1 379 . 60 ILE CA C 60.96 0.1 1 380 . 60 ILE CB C 39.56 0.1 1 381 . 61 MET H H 7.19 0.02 1 382 . 61 MET C C 177.0 0.1 1 383 . 61 MET CA C 54.05 0.1 1 384 . 61 MET CG C 32.61 0.1 1 385 . 61 MET N N 126.5 0.1 1 386 . 62 ILE H H 9.20 0.02 1 387 . 62 ILE HA H 5.464 0.02 1 388 . 62 ILE C C 174.1 0.1 1 389 . 62 ILE CA C 61.19 0.1 1 390 . 62 ILE CB C 40.21 0.1 1 391 . 62 ILE CG1 C 17.1 0.1 2 392 . 62 ILE N N 128.7 0.1 1 393 . 63 SER H H 8.58 0.02 1 394 . 63 SER HA H 5.124 0.02 1 395 . 63 SER HB2 H 3.837 0.02 2 396 . 63 SER C C 172.0 0.1 1 397 . 63 SER CA C 57.0 0.1 1 398 . 63 SER CB C 66.79 0.1 1 399 . 63 SER N N 118.5 0.1 1 400 . 64 PHE H H 9.47 0.02 1 401 . 64 PHE HA H 5.405 0.02 1 402 . 64 PHE HB2 H 1.164 0.02 2 403 . 64 PHE C C 176.0 0.1 1 404 . 64 PHE CA C 56.78 0.1 1 405 . 64 PHE CB C 42.13 0.1 1 406 . 64 PHE N N 120.2 0.1 1 407 . 65 ALA H H 9.29 0.02 1 408 . 65 ALA HA H 4.954 0.02 1 409 . 65 ALA HB H 1.164 0.02 1 410 . 65 ALA C C 175.1 0.1 1 411 . 65 ALA CA C 51.31 0.1 1 412 . 65 ALA CB C 23.77 0.1 1 413 . 65 ALA N N 125.6 0.1 1 414 . 66 VAL H H 8.16 0.02 1 415 . 66 VAL HA H 4.544 0.02 1 416 . 66 VAL C C 176.3 0.1 1 417 . 66 VAL CA C 59.33 0.1 1 418 . 66 VAL CB C 29.52 0.1 1 419 . 66 VAL N N 111.8 0.1 1 420 . 67 ARG H H 9.18 0.02 1 421 . 67 ARG HA H 3.87 0.02 1 422 . 67 ARG HB2 H 1.134 0.02 2 423 . 67 ARG C C 177.4 0.1 1 424 . 67 ARG CA C 56.77 0.1 1 425 . 67 ARG CB C 28.86 0.1 1 426 . 67 ARG N N 117.3 0.1 1 427 . 68 GLU H H 8.29 0.02 1 428 . 68 GLU C C 175.2 0.1 1 429 . 68 GLU CA C 58.34 0.1 1 430 . 68 GLU CB C 29.14 0.1 1 431 . 68 GLU CG C 36.82 0.1 1 432 . 68 GLU N N 128.4 0.1 1 433 . 69 HIS H H 9.10 0.02 1 434 . 69 HIS CA C 54.86 0.1 1 435 . 69 HIS CB C 29.13 0.1 1 436 . 69 HIS N N 121.3 0.1 1 437 . 70 GLY HA2 H 4.181 0.02 1 438 . 70 GLY HA3 H 3.62 0.02 1 439 . 70 GLY C C 173.7 0.1 1 440 . 70 GLY CA C 46.17 0.1 1 441 . 71 ASP H H 6.92 0.02 1 442 . 71 ASP CA C 51.27 0.1 1 443 . 71 ASP CB C 41.38 0.1 1 444 . 71 ASP N N 117.3 0.1 1 445 . 72 PHE CA C 58.62 0.1 1 446 . 72 PHE CB C 38.15 0.1 1 447 . 73 TYR H H 6.77 0.02 1 448 . 73 TYR CA C 54.65 0.1 1 449 . 73 TYR CB C 39.91 0.1 1 450 . 73 TYR N N 116.9 0.1 1 451 . 75 PHE C C 175.6 0.1 1 452 . 75 PHE CB C 39.02 0.1 1 453 . 76 ASP H H 7.96 0.02 1 454 . 76 ASP HA H 4.758 0.02 1 455 . 76 ASP HB2 H 2.738 0.02 2 456 . 76 ASP C C 178.0 0.1 1 457 . 76 ASP CA C 53.67 0.1 1 458 . 76 ASP CB C 41.97 0.1 1 459 . 76 ASP N N 116.0 0.1 1 460 . 77 GLY H H 8.91 0.02 1 461 . 77 GLY CA C 44.51 0.1 1 462 . 77 GLY N N 110.5 0.1 1 463 . 78 PRO HA H 3.948 0.02 1 464 . 78 PRO HB2 H 2.277 0.02 2 465 . 78 PRO C C 178.0 0.1 1 466 . 78 PRO CA C 64.21 0.1 1 467 . 78 PRO CB C 31.77 0.1 1 468 . 78 PRO CG C 25.86 0.1 1 469 . 79 GLY H H 11.33 0.02 1 470 . 79 GLY HA2 H 4.094 0.02 1 471 . 79 GLY HA3 H 3.446 0.02 1 472 . 79 GLY C C 173.8 0.1 1 473 . 79 GLY CA C 43.71 0.1 1 474 . 79 GLY N N 119.7 0.1 1 475 . 80 ASN H H 8.80 0.02 1 476 . 80 ASN HA H 4.032 0.02 1 477 . 80 ASN HB2 H 3.188 0.02 1 478 . 80 ASN HB3 H 2.911 0.02 1 479 . 80 ASN C C 175.0 0.1 1 480 . 80 ASN CA C 56.15 0.1 1 481 . 80 ASN CB C 38.42 0.1 1 482 . 80 ASN N N 117.9 0.1 1 483 . 81 VAL H H 10.24 0.02 1 484 . 81 VAL CA C 67.03 0.1 1 485 . 81 VAL CG1 C 24.09 0.1 2 486 . 81 VAL N N 127.5 0.1 1 487 . 82 LEU H H 8.54 0.02 1 488 . 82 LEU HA H 4.568 0.02 1 489 . 82 LEU HB2 H 1.493 0.02 2 490 . 82 LEU C C 176.0 0.1 1 491 . 82 LEU CA C 55.45 0.1 1 492 . 82 LEU CB C 43.49 0.1 1 493 . 82 LEU N N 128.9 0.1 1 494 . 83 ALA H H 7.57 0.02 1 495 . 83 ALA HA H 4.695 0.02 1 496 . 83 ALA HB H 1.244 0.02 1 497 . 83 ALA C C 175.3 0.1 1 498 . 83 ALA CA C 51.87 0.1 1 499 . 83 ALA CB C 22.8 0.1 1 500 . 83 ALA N N 114.5 0.1 1 501 . 84 HIS H H 9.17 0.02 1 502 . 84 HIS CA C 54.33 0.1 1 503 . 84 HIS CB C 31.6 0.1 1 504 . 84 HIS N N 115.1 0.1 1 505 . 88 PRO C C 174.5 0.1 1 506 . 88 PRO CA C 64.37 0.1 1 507 . 88 PRO CB C 32.46 0.1 1 508 . 89 GLY H H 5.47 0.02 1 509 . 89 GLY CA C 44.23 0.1 1 510 . 89 GLY N N 108.3 0.1 1 511 . 90 PRO HA H 4.754 0.02 1 512 . 90 PRO HB2 H 2.079 0.02 2 513 . 90 PRO HG2 H 1.832 0.02 2 514 . 90 PRO C C 177.7 0.1 1 515 . 90 PRO CA C 62.94 0.1 1 516 . 90 PRO CB C 33.51 0.1 1 517 . 90 PRO CG C 26.97 0.1 1 518 . 91 GLY H H 8.74 0.02 1 519 . 91 GLY HA2 H 4.055 0.02 2 520 . 91 GLY C C 175.2 0.1 1 521 . 91 GLY CA C 46.97 0.1 1 522 . 91 GLY N N 109.9 0.1 1 523 . 92 ILE H H 8.89 0.02 1 524 . 92 ILE HA H 4.248 0.02 1 525 . 92 ILE HB H 1.621 0.02 1 526 . 92 ILE C C 174.3 0.1 1 527 . 92 ILE CA C 62.07 0.1 1 528 . 92 ILE CB C 37.78 0.1 1 529 . 92 ILE CG1 C 16.65 0.1 2 530 . 92 ILE N N 131.8 0.1 1 531 . 93 ASN H H 7.13 0.02 1 532 . 93 ASN HA H 4.239 0.02 1 533 . 93 ASN C C 175.4 0.1 1 534 . 93 ASN CA C 56.18 0.1 1 535 . 93 ASN CB C 36.0 0.1 1 536 . 93 ASN N N 118.4 0.1 1 537 . 94 GLY H H 7.60 0.02 1 538 . 94 GLY HA2 H 3.905 0.02 2 539 . 94 GLY C C 171.6 0.1 1 540 . 94 GLY CA C 46.02 0.1 1 541 . 94 GLY N N 119.0 0.1 1 542 . 95 ASP H H 7.88 0.02 1 543 . 95 ASP HA H 4.767 0.02 1 544 . 95 ASP HB2 H 2.153 0.02 2 545 . 95 ASP C C 173.8 0.1 1 546 . 95 ASP CA C 55.55 0.1 1 547 . 95 ASP CB C 40.81 0.1 1 548 . 95 ASP N N 121.8 0.1 1 549 . 96 ALA H H 8.07 0.02 1 550 . 96 ALA HA H 5.029 0.02 1 551 . 96 ALA HB H 1.185 0.02 1 552 . 96 ALA CA C 51.44 0.1 1 553 . 96 ALA CB C 22.46 0.1 1 554 . 96 ALA N N 118.2 0.1 1 555 . 97 HIS H H 9.20 0.02 1 556 . 97 HIS HB2 H 3.265 0.02 2 557 . 97 HIS C C 173.4 0.1 1 558 . 97 HIS CA C 51.12 0.1 1 559 . 97 HIS CB C 34.72 0.1 1 560 . 97 HIS N N 120.5 0.1 1 561 . 98 PHE H H 8.85 0.02 1 562 . 98 PHE HA H 4.352 0.02 1 563 . 98 PHE HB2 H 2.231 0.02 2 564 . 98 PHE C C 173.9 0.1 1 565 . 98 PHE CA C 56.99 0.1 1 566 . 98 PHE CB C 41.81 0.1 1 567 . 98 PHE N N 122.6 0.1 1 568 . 99 ASP H H 8.15 0.02 1 569 . 99 ASP HA H 4.442 0.02 1 570 . 99 ASP HB2 H 3.187 0.02 2 571 . 99 ASP C C 179.4 0.1 1 572 . 99 ASP CA C 54.03 0.1 1 573 . 99 ASP CB C 40.73 0.1 1 574 . 99 ASP N N 123.5 0.1 1 575 . 100 ASP H H 9.83 0.02 1 576 . 100 ASP HA H 5.583 0.02 1 577 . 100 ASP HB2 H 2.959 0.02 2 578 . 100 ASP C C 179.0 0.1 1 579 . 100 ASP CA C 53.38 0.1 1 580 . 100 ASP CB C 40.95 0.1 1 581 . 100 ASP N N 128.4 0.1 1 582 . 101 ASP H H 9.26 0.02 1 583 . 101 ASP HA H 5.021 0.02 1 584 . 101 ASP HB2 H 2.705 0.02 2 585 . 101 ASP C C 177.1 0.1 1 586 . 101 ASP CA C 56.72 0.1 1 587 . 101 ASP CB C 39.08 0.1 1 588 . 101 ASP N N 124.1 0.1 1 589 . 102 GLU H H 7.19 0.02 1 590 . 102 GLU HA H 4.559 0.02 1 591 . 102 GLU C C 175.5 0.1 1 592 . 102 GLU CA C 53.53 0.1 1 593 . 102 GLU CB C 26.2 0.1 1 594 . 102 GLU CG C 35.61 0.1 1 595 . 102 GLU N N 115.8 0.1 1 596 . 103 GLN H H 8.34 0.02 1 597 . 103 GLN HA H 4.431 0.02 1 598 . 103 GLN HB2 H 1.97 0.02 2 599 . 103 GLN HG2 H 2.271 0.02 2 600 . 103 GLN C C 173.3 0.1 1 601 . 103 GLN CA C 53.67 0.1 1 602 . 103 GLN CB C 27.63 0.1 1 603 . 103 GLN CG C 33.56 0.1 1 604 . 103 GLN N N 126.5 0.1 1 605 . 104 TRP H H 9.57 0.02 1 606 . 104 TRP HA H 5.118 0.02 1 607 . 104 TRP HB2 H 3.097 0.02 2 608 . 104 TRP C C 177.6 0.1 1 609 . 104 TRP CA C 57.31 0.1 1 610 . 104 TRP CB C 30.49 0.1 1 611 . 104 TRP N N 131.1 0.1 1 612 . 105 THR H H 8.79 0.02 1 613 . 105 THR HA H 4.951 0.02 1 614 . 105 THR HB H 4.548 0.02 1 615 . 105 THR C C 175.7 0.1 1 616 . 105 THR CA C 60.3 0.1 1 617 . 105 THR CB C 73.25 0.1 1 618 . 105 THR CG2 C 21.25 0.1 1 619 . 105 THR N N 111.1 0.1 1 620 . 106 LYS H H 9.04 0.02 1 621 . 106 LYS HA H 4.587 0.02 1 622 . 106 LYS HB2 H 2.028 0.02 2 623 . 106 LYS HG2 H 1.566 0.02 2 624 . 106 LYS C C 176.1 0.1 1 625 . 106 LYS CA C 56.83 0.1 1 626 . 106 LYS CB C 33.61 0.1 1 627 . 106 LYS CG C 24.71 0.1 1 628 . 106 LYS CD C 29.95 0.1 1 629 . 106 LYS CE C 42.09 0.1 1 630 . 106 LYS N N 119.8 0.1 1 631 . 107 ASP H H 7.46 0.02 1 632 . 107 ASP HA H 4.767 0.02 1 633 . 107 ASP HB2 H 2.738 0.02 1 634 . 107 ASP HB3 H 2.593 0.02 1 635 . 107 ASP C C 175.5 0.1 1 636 . 107 ASP CA C 52.66 0.1 1 637 . 107 ASP CB C 42.1 0.1 1 638 . 107 ASP N N 120.8 0.1 1 639 . 108 THR H H 7.74 0.02 1 640 . 108 THR HA H 4.949 0.02 1 641 . 108 THR HB H 4.646 0.02 1 642 . 108 THR HG2 H 1.343 0.02 1 643 . 108 THR C C 174.9 0.1 1 644 . 108 THR CA C 61.96 0.1 1 645 . 108 THR CB C 68.03 0.1 1 646 . 108 THR CG2 C 22.21 0.1 1 647 . 108 THR N N 109.3 0.1 1 648 . 109 THR H H 8.20 0.02 1 649 . 109 THR HA H 4.277 0.02 1 650 . 109 THR HB H 4.272 0.02 1 651 . 109 THR HG2 H 1.328 0.02 1 652 . 109 THR C C 175.4 0.1 1 653 . 109 THR CA C 64.35 0.1 1 654 . 109 THR CB C 70.08 0.1 1 655 . 109 THR CG2 C 22.51 0.1 1 656 . 109 THR N N 115.2 0.1 1 657 . 110 GLY H H 7.33 0.02 1 658 . 110 GLY HA2 H 4.305 0.02 1 659 . 110 GLY HA3 H 3.56 0.02 1 660 . 110 GLY C C 173.5 0.1 1 661 . 110 GLY CA C 45.52 0.1 1 662 . 110 GLY N N 112.1 0.1 1 663 . 111 THR H H 8.50 0.02 1 664 . 111 THR HA H 3.903 0.02 1 665 . 111 THR HB H 3.714 0.02 1 666 . 111 THR HG2 H 1.282 0.02 1 667 . 111 THR C C 172.8 0.1 1 668 . 111 THR CA C 62.79 0.1 1 669 . 111 THR CB C 67.93 0.1 1 670 . 111 THR CG2 C 24.98 0.1 1 671 . 111 THR N N 123.7 0.1 1 672 . 112 ASN H H 8.33 0.02 1 673 . 112 ASN HA H 4.431 0.02 1 674 . 112 ASN HB2 H 2.766 0.02 2 675 . 112 ASN C C 174.8 0.1 1 676 . 112 ASN CA C 55.94 0.1 1 677 . 112 ASN CB C 41.4 0.1 1 678 . 112 ASN N N 126.8 0.1 1 679 . 113 LEU H H 8.00 0.02 1 680 . 113 LEU HA H 4.578 0.02 1 681 . 113 LEU HB2 H 1.759 0.02 2 682 . 113 LEU C C 176.4 0.1 1 683 . 113 LEU CA C 58.22 0.1 1 684 . 113 LEU CB C 41.72 0.1 1 685 . 113 LEU CG C 29.21 0.1 1 686 . 113 LEU N N 128.3 0.1 1 687 . 114 PHE H H 8.36 0.02 1 688 . 114 PHE HA H 4.114 0.02 1 689 . 114 PHE HB2 H 3.284 0.02 2 690 . 114 PHE C C 175.2 0.1 1 691 . 114 PHE CA C 61.41 0.1 1 692 . 114 PHE CB C 37.77 0.1 1 693 . 114 PHE N N 119.3 0.1 1 694 . 115 LEU H H 8.67 0.02 1 695 . 115 LEU HA H 4.731 0.02 1 696 . 115 LEU HB2 H 2.10 0.02 2 697 . 115 LEU C C 178.0 0.1 1 698 . 115 LEU CA C 57.86 0.1 1 699 . 115 LEU CB C 44.1 0.1 1 700 . 115 LEU N N 120.0 0.1 1 701 . 116 VAL H H 7.85 0.02 1 702 . 116 VAL HA H 4.113 0.02 1 703 . 116 VAL HB H 2.464 0.02 1 704 . 116 VAL HG1 H 1.265 0.02 2 705 . 116 VAL C C 179.0 0.1 1 706 . 116 VAL CA C 66.02 0.1 1 707 . 116 VAL CB C 32.62 0.1 1 708 . 116 VAL CG1 C 26.12 0.1 1 709 . 116 VAL CG2 C 23.82 0.1 1 710 . 116 VAL N N 119.8 0.1 1 711 . 117 ALA H H 9.51 0.02 1 712 . 117 ALA HA H 4.17 0.02 1 713 . 117 ALA HB H 1.284 0.02 1 714 . 117 ALA C C 178.4 0.1 1 715 . 117 ALA CA C 56.16 0.1 1 716 . 117 ALA CB C 16.81 0.1 1 717 . 117 ALA N N 122.3 0.1 1 718 . 118 ALA H H 8.85 0.02 1 719 . 118 ALA HA H 4.054 0.02 1 720 . 118 ALA HB H 1.126 0.02 1 721 . 118 ALA C C 179.9 0.1 1 722 . 118 ALA CA C 56.82 0.1 1 723 . 118 ALA CB C 17.14 0.1 1 724 . 118 ALA N N 120.8 0.1 1 725 . 119 HIS H H 7.60 0.02 1 726 . 119 HIS C C 174.4 0.1 1 727 . 119 HIS CA C 59.34 0.1 1 728 . 119 HIS CB C 29.34 0.1 1 729 . 119 HIS N N 119.5 0.1 1 730 . 120 GLU H H 9.56 0.02 1 731 . 120 GLU HA H 4.085 0.02 1 732 . 120 GLU HB2 H 1.615 0.02 2 733 . 120 GLU C C 178.1 0.1 1 734 . 120 GLU CA C 58.8 0.1 1 735 . 120 GLU CB C 28.48 0.1 1 736 . 120 GLU CG C 33.46 0.1 1 737 . 120 GLU N N 117.5 0.1 1 738 . 121 ILE H H 9.01 0.02 1 739 . 121 ILE HA H 3.917 0.02 1 740 . 121 ILE HB H 2.057 0.02 1 741 . 121 ILE C C 177.3 0.1 1 742 . 121 ILE CA C 61.99 0.1 1 743 . 121 ILE CB C 36.08 0.1 1 744 . 121 ILE CG1 C 18.99 0.1 2 745 . 121 ILE N N 117.9 0.1 1 746 . 122 GLY H H 7.48 0.02 1 747 . 122 GLY HA2 H 4.095 0.02 1 748 . 122 GLY HA3 H 2.471 0.02 1 749 . 122 GLY C C 177.0 0.1 1 750 . 122 GLY CA C 48.71 0.1 1 751 . 122 GLY N N 108.9 0.1 1 752 . 123 HIS H H 7.20 0.02 1 753 . 123 HIS HA H 5.664 0.02 1 754 . 123 HIS C C 178.6 0.1 1 755 . 123 HIS CA C 57.6 0.1 1 756 . 123 HIS CB C 28.98 0.1 1 757 . 123 HIS N N 119.9 0.1 1 758 . 124 SER H H 8.50 0.02 1 759 . 124 SER C C 175.8 0.1 1 760 . 124 SER CA C 62.75 0.1 1 761 . 124 SER CB C 63.68 0.1 1 762 . 124 SER N N 118.3 0.1 1 763 . 125 LEU H H 7.73 0.02 1 764 . 125 LEU HA H 4.635 0.02 1 765 . 125 LEU C C 178.4 0.1 1 766 . 125 LEU CA C 55.45 0.1 1 767 . 125 LEU CB C 43.63 0.1 1 768 . 125 LEU N N 108.5 0.1 1 769 . 126 GLY H H 8.53 0.02 1 770 . 126 GLY C C 173.3 0.1 1 771 . 126 GLY CA C 45.2 0.1 1 772 . 126 GLY N N 108.5 0.1 1 773 . 127 LEU H H 8.86 0.02 1 774 . 127 LEU CA C 54.29 0.1 1 775 . 127 LEU CB C 42.53 0.1 1 776 . 127 LEU N N 120.1 0.1 1 777 . 129 HIS HA H 4.966 0.02 1 778 . 129 HIS HB2 H 3.511 0.02 2 779 . 129 HIS C C 173.7 0.1 1 780 . 129 HIS CA C 55.62 0.1 1 781 . 129 HIS CB C 29.57 0.1 1 782 . 130 SER H H 6.54 0.02 1 783 . 130 SER CA C 56.8 0.1 1 784 . 130 SER N N 115.7 0.1 1 785 . 131 ALA HA H 4.681 0.02 1 786 . 131 ALA HB H 1.517 0.02 1 787 . 131 ALA C C 176.8 0.1 1 788 . 131 ALA CA C 52.46 0.1 1 789 . 131 ALA CB C 19.52 0.1 1 790 . 132 ASN H H 8.75 0.02 1 791 . 132 ASN HA H 4.615 0.02 1 792 . 132 ASN HB2 H 2.687 0.02 2 793 . 132 ASN C C 175.6 0.1 1 794 . 132 ASN CA C 53.64 0.1 1 795 . 132 ASN CB C 37.44 0.1 1 796 . 132 ASN N N 120.7 0.1 1 797 . 133 THR H H 8.00 0.02 1 798 . 133 THR HA H 3.85 0.02 1 799 . 133 THR HB H 2.453 0.02 1 800 . 133 THR HG2 H 0.977 0.02 1 801 . 133 THR C C 175.4 0.1 1 802 . 133 THR CA C 63.91 0.1 1 803 . 133 THR CB C 68.55 0.1 1 804 . 133 THR CG2 C 22.18 0.1 1 805 . 133 THR N N 116.9 0.1 1 806 . 134 GLU H H 8.94 0.02 1 807 . 134 GLU HA H 4.417 0.02 1 808 . 134 GLU HB2 H 2.123 0.02 2 809 . 134 GLU HG2 H 2.416 0.02 2 810 . 134 GLU C C 176.2 0.1 1 811 . 134 GLU CA C 56.19 0.1 1 812 . 134 GLU CB C 29.23 0.1 1 813 . 134 GLU CG C 36.22 0.1 1 814 . 134 GLU N N 120.4 0.1 1 815 . 135 ALA H H 7.68 0.02 1 816 . 135 ALA HA H 4.636 0.02 1 817 . 135 ALA HB H 1.848 0.02 1 818 . 135 ALA C C 179.0 0.1 1 819 . 135 ALA CA C 52.0 0.1 1 820 . 135 ALA CB C 19.59 0.1 1 821 . 135 ALA N N 124.4 0.1 1 822 . 136 LEU H H 11.47 0.02 1 823 . 136 LEU HA H 4.596 0.02 1 824 . 136 LEU C C 180.5 0.1 1 825 . 136 LEU CA C 58.06 0.1 1 826 . 136 LEU CB C 42.0 0.1 1 827 . 136 LEU N N 131.7 0.1 1 828 . 137 MET H H 7.93 0.02 1 829 . 137 MET HA H 4.55 0.02 1 830 . 137 MET C C 177.2 0.1 1 831 . 137 MET CA C 53.36 0.1 1 832 . 137 MET CB C 27.31 0.1 1 833 . 137 MET N N 110.9 0.1 1 834 . 138 TYR H H 8.03 0.02 1 835 . 138 TYR CA C 57.45 0.1 1 836 . 138 TYR CB C 39.38 0.1 1 837 . 138 TYR N N 128.5 0.1 1 838 . 142 HIS H H 8.20 0.02 1 839 . 142 HIS HA H 4.16 0.02 1 840 . 142 HIS HB2 H 2.442 0.02 2 841 . 142 HIS C C 177.8 0.1 1 842 . 142 HIS CA C 56.97 0.1 1 843 . 142 HIS CB C 37.3 0.1 1 844 . 142 HIS N N 127.6 0.1 1 845 . 143 SER H H 7.44 0.02 1 846 . 143 SER HA H 4.65 0.02 1 847 . 143 SER HB2 H 3.338 0.02 2 848 . 143 SER C C 174.9 0.1 1 849 . 143 SER CA C 59.23 0.1 1 850 . 143 SER CB C 61.86 0.1 1 851 . 143 SER N N 112.9 0.1 1 852 . 144 LEU H H 6.63 0.02 1 853 . 144 LEU CA C 56.88 0.1 1 854 . 144 LEU CB C 44.13 0.1 1 855 . 144 LEU N N 120.5 0.1 1 856 . 146 ASP HA H 4.827 0.02 1 857 . 146 ASP HB2 H 2.874 0.02 1 858 . 146 ASP HB3 H 2.667 0.02 1 859 . 146 ASP C C 177.0 0.1 1 860 . 146 ASP CA C 53.1 0.1 1 861 . 146 ASP CB C 41.33 0.1 1 862 . 147 LEU H H 8.85 0.02 1 863 . 147 LEU HA H 4.223 0.02 1 864 . 147 LEU HB2 H 1.691 0.02 2 865 . 147 LEU C C 179.1 0.1 1 866 . 147 LEU CA C 57.24 0.1 1 867 . 147 LEU CB C 42.26 0.1 1 868 . 147 LEU N N 126.3 0.1 1 869 . 148 THR H H 8.37 0.02 1 870 . 148 THR HA H 4.233 0.02 1 871 . 148 THR HB H 4.341 0.02 1 872 . 148 THR HG2 H 1.35 0.02 1 873 . 148 THR C C 175.7 0.1 1 874 . 148 THR CA C 64.7 0.1 1 875 . 148 THR CB C 69.18 0.1 1 876 . 148 THR CG2 C 22.21 0.1 1 877 . 148 THR N N 111.9 0.1 1 878 . 149 ARG H H 7.37 0.02 1 879 . 149 ARG HA H 4.493 0.02 1 880 . 149 ARG HB2 H 2.098 0.02 1 881 . 149 ARG HB3 H 1.688 0.02 1 882 . 149 ARG HG2 H 1.694 0.02 2 883 . 149 ARG HD2 H 3.20 0.02 2 884 . 149 ARG C C 175.6 0.1 1 885 . 149 ARG CA C 55.06 0.1 1 886 . 149 ARG CB C 30.7 0.1 1 887 . 149 ARG CG C 27.8 0.1 1 888 . 149 ARG CD C 43.67 0.1 1 889 . 149 ARG N N 119.5 0.1 1 890 . 150 PHE H H 7.32 0.02 1 891 . 150 PHE HA H 4.277 0.02 1 892 . 150 PHE HB2 H 2.971 0.02 2 893 . 150 PHE C C 174.7 0.1 1 894 . 150 PHE CA C 60.49 0.1 1 895 . 150 PHE CB C 39.88 0.1 1 896 . 150 PHE N N 121.1 0.1 1 897 . 151 ARG H H 6.97 0.02 1 898 . 151 ARG HA H 4.037 0.02 1 899 . 151 ARG HB2 H 1.766 0.02 2 900 . 151 ARG HG2 H 1.502 0.02 2 901 . 151 ARG HD2 H 3.172 0.02 2 902 . 151 ARG C C 174.7 0.1 1 903 . 151 ARG CA C 54.32 0.1 1 904 . 151 ARG CB C 33.46 0.1 1 905 . 151 ARG CG C 26.68 0.1 1 906 . 151 ARG CD C 43.81 0.1 1 907 . 151 ARG N N 126.4 0.1 1 908 . 152 LEU H H 8.43 0.02 1 909 . 152 LEU HA H 3.906 0.02 1 910 . 152 LEU HB2 H 1.494 0.02 2 911 . 152 LEU HG H 1.404 0.02 1 912 . 152 LEU C C 177.1 0.1 1 913 . 152 LEU CA C 55.31 0.1 1 914 . 152 LEU CB C 43.39 0.1 1 915 . 152 LEU CG C 27.3 0.1 1 916 . 152 LEU N N 122.2 0.1 1 917 . 153 SER H H 8.24 0.02 1 918 . 153 SER HA H 4.559 0.02 1 919 . 153 SER HB2 H 4.175 0.02 2 920 . 153 SER C C 175.2 0.1 1 921 . 153 SER CA C 58.63 0.1 1 922 . 153 SER CB C 66.07 0.1 1 923 . 153 SER N N 117.9 0.1 1 924 . 154 GLN H H 9.01 0.02 1 925 . 154 GLN HA H 3.939 0.02 1 926 . 154 GLN HB2 H 2.104 0.02 2 927 . 154 GLN HG2 H 2.537 0.02 2 928 . 154 GLN C C 177.4 0.1 1 929 . 154 GLN CA C 58.6 0.1 1 930 . 154 GLN CB C 28.33 0.1 1 931 . 154 GLN CG C 34.3 0.1 1 932 . 154 GLN N N 122.2 0.1 1 933 . 155 ASP H H 8.19 0.02 1 934 . 155 ASP HA H 4.588 0.02 1 935 . 155 ASP HB2 H 3.548 0.02 2 936 . 155 ASP C C 177.9 0.1 1 937 . 155 ASP CA C 58.97 0.1 1 938 . 155 ASP CB C 43.54 0.1 1 939 . 155 ASP N N 118.0 0.1 1 940 . 156 ASP H H 7.35 0.02 1 941 . 156 ASP HA H 4.844 0.02 1 942 . 156 ASP HB2 H 2.742 0.02 2 943 . 156 ASP C C 176.2 0.1 1 944 . 156 ASP CA C 57.69 0.1 1 945 . 156 ASP CB C 39.05 0.1 1 946 . 156 ASP N N 116.3 0.1 1 947 . 157 ILE H H 7.92 0.02 1 948 . 157 ILE HA H 3.645 0.02 1 949 . 157 ILE HB H 3.651 0.02 1 950 . 157 ILE HG2 H 0.934 0.02 1 951 . 157 ILE C C 177.6 0.1 1 952 . 157 ILE CA C 66.0 0.1 1 953 . 157 ILE CB C 38.73 0.1 1 954 . 157 ILE CG1 C 17.48 0.1 2 955 . 157 ILE N N 116.1 0.1 1 956 . 158 ASN H H 9.15 0.02 1 957 . 158 ASN HA H 4.357 0.02 1 958 . 158 ASN HB2 H 3.134 0.02 2 959 . 158 ASN C C 178.9 0.1 1 960 . 158 ASN CA C 55.32 0.1 1 961 . 158 ASN CB C 37.46 0.1 1 962 . 158 ASN N N 118.7 0.1 1 963 . 159 GLY H H 8.09 0.02 1 964 . 159 GLY C C 176.1 0.1 1 965 . 159 GLY CA C 46.36 0.1 1 966 . 159 GLY N N 109.3 0.1 1 967 . 160 ILE H H 8.66 0.02 1 968 . 160 ILE HA H 4.345 0.02 1 969 . 160 ILE C C 178.3 0.1 1 970 . 160 ILE CA C 61.15 0.1 1 971 . 160 ILE CB C 39.06 0.1 1 972 . 160 ILE N N 125.5 0.1 1 973 . 161 GLN H H 8.55 0.02 1 974 . 161 GLN HA H 4.297 0.02 1 975 . 161 GLN C C 179.8 0.1 1 976 . 161 GLN CA C 58.54 0.1 1 977 . 161 GLN CB C 26.84 0.1 1 978 . 161 GLN N N 122.1 0.1 1 979 . 162 SER H H 7.78 0.02 1 980 . 162 SER CA C 61.82 0.1 1 981 . 162 SER N N 119.5 0.1 1 982 . 164 TYR HA H 4.864 0.02 1 983 . 164 TYR HB2 H 3.495 0.02 2 984 . 164 TYR C C 175.7 0.1 1 985 . 164 TYR CA C 58.97 0.1 1 986 . 164 TYR CB C 41.73 0.1 1 987 . 165 GLY H H 8.29 0.02 1 988 . 165 GLY CA C 44.44 0.1 1 989 . 165 GLY N N 109.0 0.1 1 990 . 168 PRO HA H 4.477 0.02 1 991 . 168 PRO HB2 H 2.351 0.02 1 992 . 168 PRO HB3 H 2.012 0.02 1 993 . 168 PRO C C 176.5 0.1 1 994 . 168 PRO CA C 63.13 0.1 1 995 . 168 PRO CB C 32.3 0.1 1 996 . 168 PRO CG C 27.82 0.1 1 997 . 168 PRO CD C 50.69 0.1 1 998 . 169 ASP H H 8.28 0.02 1 999 . 169 ASP HA H 4.619 0.02 1 1000 . 169 ASP HB2 H 2.675 0.02 2 1001 . 169 ASP C C 176.0 0.1 1 1002 . 169 ASP CA C 54.53 0.1 1 1003 . 169 ASP CB C 41.31 0.1 1 1004 . 169 ASP N N 120.2 0.1 1 1005 . 170 SER H H 8.10 0.02 1 1006 . 170 SER CA C 56.38 0.1 1 1007 . 170 SER CB C 63.89 0.1 1 1008 . 170 SER N N 116.7 0.1 1 1009 . 171 PRO HA H 4.496 0.02 1 1010 . 171 PRO HB2 H 2.359 0.02 1 1011 . 171 PRO HB3 H 2.024 0.02 1 1012 . 171 PRO HG2 H 2.804 0.02 2 1013 . 171 PRO HD2 H 3.826 0.02 2 1014 . 171 PRO C C 176.8 0.1 1 1015 . 171 PRO CA C 63.45 0.1 1 1016 . 171 PRO CB C 32.47 0.1 1 1017 . 171 PRO CG C 27.81 0.1 1 1018 . 171 PRO CD C 51.06 0.1 1 1019 . 172 GLU H H 8.43 0.02 1 1020 . 172 GLU HA H 4.376 0.02 1 1021 . 172 GLU HB2 H 2.159 0.02 1 1022 . 172 GLU HB3 H 2.017 0.02 1 1023 . 172 GLU C C 176.0 0.1 1 1024 . 172 GLU CA C 57.03 0.1 1 1025 . 172 GLU CB C 30.59 0.1 1 1026 . 172 GLU CG C 36.74 0.1 1 1027 . 172 GLU N N 121.5 0.1 1 1028 . 173 THR H H 7.69 0.02 1 1029 . 173 THR CA C 63.27 0.1 1 1030 . 173 THR CB C 71.11 0.1 1 1031 . 173 THR N N 120.2 0.1 1 stop_ save_