data_4679 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 15N, 13C, and 13CO Assignments and Secondary Structure Determination of Collagenase-3 (MMP-13) Complexed with a Hydroxamic acid Inhibitor ; _BMRB_accession_number 4679 _BMRB_flat_file_name bmr4679.str _Entry_type original _Submission_date 2000-03-06 _Accession_date 2000-03-06 _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 Moy Franklin J. . 2 Chanda Pranab K. . 3 Cosmi Scott . . 4 Edris Wade . . 5 Levin Jeremy I. . 6 Powers Robert . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 776 "13C chemical shifts" 635 "15N chemical shifts" 140 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2002-04-01 original author . stop_ _Original_release_date 2002-04-01 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: 1H, 15N, 13C, and 13CO Assignments and Secondary Structure Determination of Collagenase-3 (MMP-13) Complexed with a Hydroxamic acid Inhibitor ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 20414192 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Moy Franklin J. . 2 Chanda Pranab K. . 3 Cosmi Scott . . 4 Edris Wade . . 5 Levin Jeremy I. . 6 Powers Robert . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of Biomolecular NMR' _Journal_volume 17 _Journal_issue 3 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 269 _Page_last 270 _Year 2000 _Details . loop_ _Keyword 'Matrix Metalloproteinase' Collagenase-3 MMP-13 'Resonance assignments' 'Secondary Structure' 'Hydroxamic acid' stop_ save_ ################################## # Molecular system description # ################################## save_system_MMP-13 _Saveframe_category molecular_system _Mol_system_name 'Human Collagenase-3' _Abbreviation_common MMP-13 _Enzyme_commission_number 3.4.24.- loop_ _Mol_system_component_name _Mol_label 'Human Collagenase-3' $MMP-13 WAY-151693 $WAY 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_MMP-13 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Human Collagenase-3' _Abbreviation_common MMP-13 _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 165 _Mol_residue_sequence ; YNVFPRTLKWSKMNLTYRIV NYTPDMTHSEVEKAFKKAFK VWSDVTPLNFTRLHDGIADI MISFGIKEHGDFYPFDGPSG LLAHAFPPGPNYGGDAHFDD DETWTSSSKGYNLFLVAAHE FGHSLGLDHSKDPGALMFPI YTYTGKSHFMLPDDDVQGIQ SLYGP ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 TYR 2 2 ASN 3 3 VAL 4 4 PHE 5 5 PRO 6 6 ARG 7 7 THR 8 8 LEU 9 9 LYS 10 10 TRP 11 11 SER 12 12 LYS 13 13 MET 14 14 ASN 15 15 LEU 16 16 THR 17 17 TYR 18 18 ARG 19 19 ILE 20 20 VAL 21 21 ASN 22 22 TYR 23 23 THR 24 24 PRO 25 25 ASP 26 26 MET 27 27 THR 28 28 HIS 29 29 SER 30 30 GLU 31 31 VAL 32 32 GLU 33 33 LYS 34 34 ALA 35 35 PHE 36 36 LYS 37 37 LYS 38 38 ALA 39 39 PHE 40 40 LYS 41 41 VAL 42 42 TRP 43 43 SER 44 44 ASP 45 45 VAL 46 46 THR 47 47 PRO 48 48 LEU 49 49 ASN 50 50 PHE 51 51 THR 52 52 ARG 53 53 LEU 54 54 HIS 55 55 ASP 56 56 GLY 57 57 ILE 58 58 ALA 59 59 ASP 60 60 ILE 61 61 MET 62 62 ILE 63 63 SER 64 64 PHE 65 65 GLY 66 66 ILE 67 67 LYS 68 68 GLU 69 69 HIS 70 70 GLY 71 71 ASP 72 72 PHE 73 73 TYR 74 74 PRO 75 75 PHE 76 76 ASP 77 77 GLY 78 78 PRO 79 79 SER 80 80 GLY 81 81 LEU 82 82 LEU 83 83 ALA 84 84 HIS 85 85 ALA 86 86 PHE 87 87 PRO 88 88 PRO 89 89 GLY 90 90 PRO 91 91 ASN 92 92 TYR 93 93 GLY 94 94 GLY 95 95 ASP 96 96 ALA 97 97 HIS 98 98 PHE 99 99 ASP 100 100 ASP 101 101 ASP 102 102 GLU 103 103 THR 104 104 TRP 105 105 THR 106 106 SER 107 107 SER 108 108 SER 109 109 LYS 110 110 GLY 111 111 TYR 112 112 ASN 113 113 LEU 114 114 PHE 115 115 LEU 116 116 VAL 117 117 ALA 118 118 ALA 119 119 HIS 120 120 GLU 121 121 PHE 122 122 GLY 123 123 HIS 124 124 SER 125 125 LEU 126 126 GLY 127 127 LEU 128 128 ASP 129 129 HIS 130 130 SER 131 131 LYS 132 132 ASP 133 133 PRO 134 134 GLY 135 135 ALA 136 136 LEU 137 137 MET 138 138 PHE 139 139 PRO 140 140 ILE 141 141 TYR 142 142 THR 143 143 TYR 144 144 THR 145 145 GLY 146 146 LYS 147 147 SER 148 148 HIS 149 149 PHE 150 150 MET 151 151 LEU 152 152 PRO 153 153 ASP 154 154 ASP 155 155 ASP 156 156 VAL 157 157 GLN 158 158 GLY 159 159 ILE 160 160 GLN 161 161 SER 162 162 LEU 163 163 TYR 164 164 GLY 165 165 PRO stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-07-14 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value PDB 1EUB "Solution Structure Of The Catalytic Domain Of Human Collagenase-3 (Mmp-13) Complexed To A Potent Non-Peptidic Sulfonamide Inhib" 100.00 171 100.00 100.00 1.75e-116 PDB 1FLS "Solution Structure Of The Catalytic Fragment Of Human Collagenase-3 (Mmp-13) Complexed With A Hydroxamic Acid Inhibitor" 100.00 165 100.00 100.00 1.01e-116 PDB 1FM1 "Solution Structure Of The Catalytic Fragment Of Human Collagenase-3 (Mmp-13) Complexed With A Hydroxamic Acid Inhibitor" 100.00 165 100.00 100.00 1.01e-116 PDB 1XUC "Matrix Metalloproteinase-13 Complexed With Non-Zinc Binding Inhibitor" 100.00 171 100.00 100.00 1.75e-116 PDB 1XUD "Matrix Metalloproteinase-13 Complexed With Non-Zinc Binding Inhibitor" 100.00 171 100.00 100.00 1.75e-116 PDB 1XUR "Matrix Metalloproteinase-13 Complexed With Non-Zinc Binding Inhibitor" 100.00 171 100.00 100.00 1.75e-116 PDB 1YOU "Crystal Structure Of The Catalytic Domain Of Mmp-13 Complexed With A Potent Pyrimidinetrione Inhibitor" 100.00 168 100.00 100.00 1.48e-116 PDB 1ZTQ "Crystal Structure Of The Catalytic Domain Of Mmp-13 Complexed With Way-033" 100.00 165 100.00 100.00 1.01e-116 PDB 2D1N "Collagenase-3 (Mmp-13) Complexed To A Hydroxamic Acid Inhibitor" 100.00 166 100.00 100.00 1.19e-116 PDB 2E2D "Flexibility And Variability Of Timp Binding: X-Ray Structure Of The Complex Between Collagenase-3MMP-13 And Timp-2" 100.00 165 100.00 100.00 1.01e-116 PDB 2OW9 "Crystal Structure Analysis Of The Mmp13 Catalytic Domain In Complex With Specific Inhibitor" 100.00 170 100.00 100.00 1.03e-116 PDB 2OZR "Mmp13 Catalytic Domain Complexed With 4-{[1-Methyl-2,4-Dioxo-6-(3- Phenylprop-1-Yn-1-Yl)-1,4-Dihydroquinazolin-3(2h)-Yl]methyl}" 100.00 170 100.00 100.00 1.03e-116 PDB 2PJT "Crystal Structure Of The Catalytic Domain Of Mmp-13 Complexed With Way-344" 100.00 165 100.00 100.00 1.01e-116 PDB 2YIG "Mmp13 In Complex With A Novel Selective Non Zinc Binding Inhibitor" 100.00 171 100.00 100.00 1.75e-116 PDB 3ELM "Crystal Structure Of Mmp-13 Complexed With Inhibitor 24f" 100.00 171 100.00 100.00 1.75e-116 PDB 3I7G "Mmp-13 In Complex With A Non Zinc-Chelating Inhibitor" 100.00 171 100.00 100.00 1.75e-116 PDB 3I7I "Mmp-13 In Complex With A Non Zinc-Chelating Inhibitor" 100.00 171 100.00 100.00 1.75e-116 PDB 3KEC "Crystal Structure Of Human Mmp-13 Complexed With A Phenyl-2h-Tetrazole Compound" 100.00 167 100.00 100.00 1.80e-116 PDB 3KEJ "Crystal Structure Of Human Mmp-13 Complexed With A (Pyridin-4-Yl)-2h- Tetrazole Compound" 100.00 167 100.00 100.00 1.80e-116 PDB 3KEK "Crystal Structure Of Human Mmp-13 Complexed With A (Pyridin-4-Yl)-2h- Tetrazole Compound" 100.00 167 100.00 100.00 1.80e-116 PDB 3KRY "Crystal Structure Of Mmp-13 In Complex With Sc-78080" 99.39 164 100.00 100.00 7.42e-116 PDB 3LJZ "Crystal Structure Of Human Mmp-13 Complexed With An Amino-2-Indanol Compound" 98.79 164 100.00 100.00 3.54e-115 PDB 3O2X "Mmp-13 In Complex With Selective Tetrazole Core Inhibitor" 98.79 164 100.00 100.00 3.54e-115 PDB 3TVC "Human Mmp13 In Complex With L-Glutamate Motif Inhibitor" 100.00 169 100.00 100.00 1.81e-116 PDB 3WV1 "Crystal Structure Of The Catalytic Domain Of Mmp-13 Complexed With 4- (2-((6-fluoro-2-((3-methoxybenzyl)carbamoyl)-4-oxo-3,4- D" 100.00 171 100.00 100.00 1.75e-116 PDB 3WV2 "Crystal Structure Of The Catalytic Domain Of Mmp-13 Complexed With N- (3-methoxybenzyl)-4-oxo-3,4-dihydroquinazoline-2-carboxam" 100.00 171 100.00 100.00 1.75e-116 PDB 3WV3 "Crystal Structure Of The Catalytic Domain Of Mmp-13 Complexed With N- (3-methoxybenzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidin" 100.00 171 100.00 100.00 1.75e-116 PDB 3ZXH "Mmp-13 Complexed With 2-Napthylsulfonamide Hydroxamic Acid Inhibitor" 100.00 171 100.00 100.00 1.75e-116 PDB 456C "Crystal Structure Of Collagenase-3 (Mmp-13) Complexed To A Diphenyl-Ether Sulphone Based Hydroxamic Acid" 100.00 168 100.00 100.00 1.48e-116 PDB 4A7B "Mmp13 In Complex With A Novel Selective Non Zinc Binding Inhibitor Cmpd22" 100.00 169 100.00 100.00 1.81e-116 PDB 4FU4 "Human Collagenase 3 (mmp-13) With Peptide From Pro-domain" 100.00 368 99.39 99.39 3.34e-113 PDB 4FVL "Human Collagenase 3 (mmp-13) Full Form With Peptides From Pro-domain" 100.00 368 99.39 99.39 3.34e-113 PDB 4G0D "Human Collagenase 3 (mmp-13) Full Form With Peptides From Pro-domain" 100.00 368 99.39 99.39 3.34e-113 PDB 4JP4 "Mmp13 In Complex With A Reverse Hydroxamate Zn-binder" 100.00 173 100.00 100.00 1.48e-116 PDB 4JPA "Mmp13 In Complex With A Piperazine Hydantoin Ligand" 100.00 173 100.00 100.00 1.48e-116 PDB 4L19 "Matrix Metalloproteinase-13 Complexed With Selective Inhibitor Compound Q1" 100.00 171 100.00 100.00 1.75e-116 PDB 5BOT "X-ray Co-structure Of Mmp-13 With Ethyl 5-carbamoyl-1h-indole-2- Carboxylate" 100.00 171 100.00 100.00 1.75e-116 PDB 5BOY "X-ray Co-structure Of Mmp-13 With Ethyl 5-(1-methyl-1h-imidazol-5-yl)- 1h-indole-2-carboxylate" 100.00 171 100.00 100.00 1.75e-116 PDB 5BPA "X-ray Co-structure Of Mmp-13 With 4-[({5-[2-(ethoxycarbonyl)-1h-indol- 5-yl]-1-methyl-1h-pyrazol-3-yl}formamido)methyl]benzoate" 100.00 171 100.00 100.00 1.75e-116 PDB 830C "Collagenase-3 (Mmp-13) Complexed To A Sulphone-Based Hydroxamic Acid" 100.00 168 100.00 100.00 1.48e-116 DBJ BAD96468 "matrix metalloproteinase 13 preproprotein variant [Homo sapiens]" 100.00 471 99.39 99.39 3.27e-112 DBJ BAF84900 "unnamed protein product [Homo sapiens]" 100.00 471 100.00 100.00 2.61e-113 DBJ BAG37740 "unnamed protein product [Homo sapiens]" 100.00 471 99.39 99.39 3.23e-112 DBJ BAQ35474 "MMP13, partial [Canis lupus familiaris]" 100.00 478 97.58 98.18 2.21e-110 EMBL CAA53056 "collagenase 3 [Homo sapiens]" 100.00 471 100.00 100.00 2.37e-113 EMBL CAA57108 "collagenase-3 [Homo sapiens]" 100.00 471 100.00 100.00 2.37e-113 GB AAD38037 "matrix metalloproteinase-13 [Canis lupus familiaris]" 80.00 196 98.48 98.48 2.82e-87 GB AAF17559 "matrix metalloproteinase-13 [Canis lupus familiaris]" 100.00 452 97.58 98.18 1.95e-110 GB AAH67522 "Matrix metalloproteinase 13, preproprotein [Homo sapiens]" 100.00 471 100.00 100.00 2.37e-113 GB AAH67523 "Matrix metallopeptidase 13 (collagenase 3) [Homo sapiens]" 100.00 471 100.00 100.00 2.40e-113 GB AAH74807 "Matrix metalloproteinase 13, preproprotein [Homo sapiens]" 100.00 471 100.00 100.00 2.37e-113 REF NP_002418 "collagenase 3 preproprotein [Homo sapiens]" 100.00 471 100.00 100.00 2.37e-113 REF XP_001098794 "PREDICTED: collagenase 3 isoform 2 [Macaca mulatta]" 100.00 489 99.39 99.39 1.42e-112 REF XP_001098996 "PREDICTED: collagenase 3 isoform 4 [Macaca mulatta]" 100.00 471 99.39 99.39 1.69e-112 REF XP_001154361 "PREDICTED: collagenase 3 [Pan troglodytes]" 100.00 471 100.00 100.00 2.20e-113 REF XP_003253103 "PREDICTED: collagenase 3 [Nomascus leucogenys]" 100.00 471 99.39 99.39 1.88e-112 SP P45452 "RecName: Full=Collagenase 3; AltName: Full=Matrix metalloproteinase-13; Short=MMP-13; Flags: Precursor" 100.00 471 100.00 100.00 2.37e-113 stop_ save_ ############# # Ligands # ############# save_WAY _Saveframe_category ligand _Mol_type "non-polymer (NON-POLYMER)" _Name_common "WAY-151693 (N-HYDROXY-2-[(4-METHOXY-BENZENESULFONYL)-PYRIDIN-3-YLMETHYL-AMINO]-3-METHYL-BENZAMIDE)" _Abbreviation_common WAY _BMRB_code WAY _PDB_code WAY _Molecular_mass 427.474 _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 C1 C1 C . 0 . ? C10 C10 C . 0 . ? C2 C2 C . 0 . ? C27 C27 C . 0 . ? C35 C35 C . 0 . ? C38 C38 C . 0 . ? C6 C6 C . 0 . ? CA CA C . 0 . ? CB1 CB1 C . 0 . ? CB2 CB2 C . 0 . ? CC1 CC1 C . 0 . ? CC2 CC2 C . 0 . ? CD CD C . 0 . ? CE CE C . 0 . ? CF1 CF1 C . 0 . ? CF2 CF2 C . 0 . ? CH CH C . 0 . ? CI CI C . 0 . ? CJ CJ C . 0 . ? CK CK C . 0 . ? CM CM C . 0 . ? H14 H14 H . 0 . ? H15 H15 H . 0 . ? HA1 HA1 H . 0 . ? HA2 HA2 H . 0 . ? HA3 HA3 H . 0 . ? HB1 HB1 H . 0 . ? HB2 HB2 H . 0 . ? HC1 HC1 H . 0 . ? HC2 HC2 H . 0 . ? HD1 HD1 H . 0 . ? HD2 HD2 H . 0 . ? HE1 HE1 H . 0 . ? HE2 HE2 H . 0 . ? HE3 HE3 H . 0 . ? HF1 HF1 H . 0 . ? HF2 HF2 H . 0 . ? HH HH H . 0 . ? HI HI H . 0 . ? HJ HJ H . 0 . ? HK HK H . 0 . ? HL HL H . 0 . ? N12 N12 N . 0 . ? N20 N20 N . 0 . ? N25 N25 N . 0 . ? O11 O11 O . 0 . ? O13 O13 O . 0 . ? O45 O45 O . 0 . ? O50 O50 O . 0 . ? O51 O51 O . 0 . ? S21 S21 S . 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 DOUB C1 C2 ? ? SING C1 C6 ? ? SING C1 N20 ? ? SING C2 CF2 ? ? SING C2 C10 ? ? DOUB CF2 CH ? ? SING CF2 HF2 ? ? SING CH CF1 ? ? SING CH HH ? ? DOUB CF1 C6 ? ? SING CF1 HF1 ? ? SING C6 CE ? ? DOUB C10 O11 ? ? SING C10 N12 ? ? SING N12 O13 ? ? SING N12 H14 ? ? SING O13 H15 ? ? SING CE HE1 ? ? SING CE HE2 ? ? SING CE HE3 ? ? SING N20 S21 ? ? SING N20 CD ? ? SING S21 C35 ? ? DOUB S21 O50 ? ? DOUB S21 O51 ? ? SING CD C27 ? ? SING CD HD1 ? ? SING CD HD2 ? ? DOUB CK CM ? ? SING CK CI ? ? SING CK HK ? ? SING CM N25 ? ? SING CM HL ? ? DOUB N25 CJ ? ? SING CJ C27 ? ? SING CJ HJ ? ? DOUB C27 CI ? ? SING CI HI ? ? DOUB C35 CC1 ? ? SING C35 CC2 ? ? SING CC1 CB1 ? ? SING CC1 HC1 ? ? DOUB CB1 C38 ? ? SING CB1 HB1 ? ? SING C38 CB2 ? ? SING C38 O45 ? ? DOUB CB2 CC2 ? ? SING CB2 HB2 ? ? SING CC2 HC2 ? ? SING O45 CA ? ? SING CA HA1 ? ? SING CA HA2 ? ? SING CA HA3 ? ? stop_ _Mol_thiol_state 'not present' _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 $MMP-13 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 $MMP-13 'recombinant technology' 'E. coli' Escherichia coli BL21(DE3) plasmid pProMMP-13 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 $MMP-13 1.0 mM [U-15N] $WAY 1.0 mM . Tris-Base 10 mM [U-2H] NaCl 100 mM . CaCl2 5 mM . ZnCl2 0.1 mM . NaN3 2 mM . DTT 10 mM [U-2H] H2O 90 % . D2O 10 % . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $MMP-13 1.0 mM '[U-13C; U-15N]' $WAY 1.0 mM . Tris-Base 10 mM [U-2H] NaCl 100 mM . CaCl2 5 mM . ZnCl2 0.1 mM . NaN3 2 mM . DTT 10 mM [U-2H] H2O 90 % . D2O 10 % . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AMX-2 _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save__1 _Saveframe_category NMR_applied_experiment _Sample_label . save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.5 0.05 pH temperature 308 0.2 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio _Indirect_shift_ratio_citation_label _Correction_value_citation_label DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 $entry_citation $entry_citation DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 $entry_citation $entry_citation DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449537 $entry_citation $entry_citation 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_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 $sample_2 stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'Human Collagenase-3' _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 TYR CA C 55.5800 0.25 . 2 . 1 TYR HA H 4.3200 0.2 . 3 . 1 TYR CB C 38.0900 0.25 . 4 . 1 TYR HB3 H 3.3200 0.2 . 5 . 1 TYR HB2 H 3.0900 0.2 . 6 . 1 TYR CD1 C 129.7000 0.25 . 7 . 1 TYR HD1 H 6.8400 0.2 . 8 . 1 TYR C C 171.7100 0.25 . 9 . 2 ASN N N 118.9500 0.25 . 10 . 2 ASN H H 9.8000 0.2 . 11 . 2 ASN CA C 53.4000 0.25 . 12 . 2 ASN HA H 5.0700 0.2 . 13 . 2 ASN CB C 43.3000 0.25 . 14 . 2 ASN HB3 H 2.5000 0.2 . 15 . 2 ASN C C 173.3200 0.25 . 16 . 3 VAL N N 115.4800 0.25 . 17 . 3 VAL H H 8.4000 0.2 . 18 . 3 VAL CA C 59.8200 0.25 . 19 . 3 VAL HA H 4.7450 0.2 . 20 . 3 VAL CB C 32.5300 0.25 . 21 . 3 VAL HB H 2.7600 0.2 . 22 . 3 VAL CG1 C 19.0000 0.25 . 23 . 3 VAL HG1 H 1.2700 0.2 . 24 . 3 VAL CG2 C 18.6000 0.25 . 25 . 3 VAL HG2 H 1.0400 0.2 . 26 . 3 VAL C C 176.3700 0.25 . 27 . 4 PHE N N 121.4300 0.25 . 28 . 4 PHE H H 8.0400 0.2 . 29 . 4 PHE CA C 58.6600 0.25 . 30 . 4 PHE HA H 4.3200 0.2 . 31 . 4 PHE CB C 43.3000 0.25 . 32 . 4 PHE HB3 H 3.8700 0.2 . 33 . 4 PHE HD1 H 7.2700 0.2 . 34 . 5 PRO CA C 64.3300 0.25 . 35 . 5 PRO HA H 4.4100 0.2 . 36 . 5 PRO CB C 31.7000 0.25 . 37 . 5 PRO HB3 H 1.9300 0.2 . 38 . 5 PRO HB2 H 2.3800 0.2 . 39 . 5 PRO CG C 28.1000 0.25 . 40 . 5 PRO HG3 H 2.1900 0.2 . 41 . 5 PRO CD C 49.3000 0.25 . 42 . 5 PRO HD3 H 3.7000 0.2 . 43 . 5 PRO HD2 H 3.4800 0.2 . 44 . 5 PRO C C 177.2100 0.25 . 45 . 6 ARG N N 116.0900 0.25 . 46 . 6 ARG H H 8.4800 0.2 . 47 . 6 ARG CA C 57.7000 0.25 . 48 . 6 ARG HA H 3.9950 0.2 . 49 . 6 ARG CB C 28.0700 0.25 . 50 . 6 ARG HB3 H 1.6300 0.2 . 51 . 6 ARG CG C 32.9000 0.25 . 52 . 6 ARG HG3 H 1.6400 0.2 . 53 . 6 ARG CD C 43.4000 0.25 . 54 . 6 ARG HD3 H 3.2500 0.2 . 55 . 6 ARG C C 175.8300 0.25 . 56 . 7 THR N N 114.3500 0.25 . 57 . 7 THR H H 8.4100 0.2 . 58 . 7 THR CA C 62.6200 0.25 . 59 . 7 THR HA H 3.8650 0.2 . 60 . 7 THR CB C 67.4600 0.25 . 61 . 7 THR HB H 4.3200 0.2 . 62 . 7 THR CG2 C 22.7000 0.25 . 63 . 7 THR HG2 H 1.2400 0.2 . 64 . 7 THR C C 173.8300 0.25 . 65 . 8 LEU N N 122.6900 0.25 . 66 . 8 LEU H H 6.8900 0.2 . 67 . 8 LEU CA C 54.7000 0.25 . 68 . 8 LEU HA H 4.2900 0.2 . 69 . 8 LEU CB C 42.2200 0.25 . 70 . 8 LEU HB3 H 1.6200 0.2 . 71 . 8 LEU HB2 H 1.3600 0.2 . 72 . 8 LEU CG C 26.5000 0.25 . 73 . 8 LEU HG H 1.7100 0.2 . 74 . 8 LEU CD1 C 25.7000 0.25 . 75 . 8 LEU HD1 H 0.8200 0.2 . 76 . 8 LEU CD2 C 22.7000 0.25 . 77 . 8 LEU HD2 H 0.8200 0.2 . 78 . 8 LEU C C 175.8000 0.25 . 79 . 9 LYS N N 116.6200 0.25 . 80 . 9 LYS H H 7.8500 0.2 . 81 . 9 LYS CA C 55.0200 0.25 . 82 . 9 LYS HA H 4.5050 0.2 . 83 . 9 LYS CB C 34.6000 0.25 . 84 . 9 LYS HB3 H 1.8400 0.2 . 85 . 9 LYS CG C 22.9000 0.25 . 86 . 9 LYS HG3 H 1.4700 0.2 . 87 . 9 LYS HG2 H 1.1900 0.2 . 88 . 9 LYS CD C 29.7000 0.25 . 89 . 9 LYS HD3 H 1.5600 0.2 . 90 . 9 LYS HD2 H 1.4700 0.2 . 91 . 9 LYS CE C 42.0000 0.25 . 92 . 9 LYS HE3 H 2.9600 0.2 . 93 . 9 LYS C C 175.5800 0.25 . 94 . 10 TRP N N 122.8000 0.25 . 95 . 10 TRP H H 8.2000 0.2 . 96 . 10 TRP CA C 57.9200 0.25 . 97 . 10 TRP HA H 4.6000 0.2 . 98 . 10 TRP CB C 30.4100 0.25 . 99 . 10 TRP HB3 H 3.6100 0.2 . 100 . 10 TRP HB2 H 3.2900 0.2 . 101 . 10 TRP HD1 H 7.3700 0.2 . 102 . 10 TRP NE1 N 128.7700 0.25 . 103 . 10 TRP HE1 H 10.7300 0.2 . 104 . 10 TRP CE3 C 121.6000 0.25 . 105 . 10 TRP HE3 H 7.8800 0.2 . 106 . 10 TRP CZ3 C 121.7000 0.25 . 107 . 10 TRP HZ3 H 7.0900 0.2 . 108 . 10 TRP CH2 C 124.9000 0.25 . 109 . 10 TRP HH2 H 7.5300 0.2 . 110 . 10 TRP CZ2 C 112.6000 0.25 . 111 . 10 TRP HZ2 H 7.4000 0.2 . 112 . 11 SER CA C 58.4400 0.25 . 113 . 11 SER HA H 4.6500 0.2 . 114 . 11 SER CB C 63.5200 0.25 . 115 . 11 SER HB3 H 4.2100 0.2 . 116 . 11 SER HB2 H 4.0800 0.2 . 117 . 11 SER C C 172.8300 0.25 . 118 . 12 LYS N N 119.0500 0.25 . 119 . 12 LYS H H 7.5200 0.2 . 120 . 12 LYS CA C 54.0850 0.25 . 121 . 12 LYS HA H 4.7450 0.2 . 122 . 12 LYS CB C 34.5300 0.25 . 123 . 12 LYS HB3 H 1.9300 0.2 . 124 . 12 LYS HB2 H 2.8900 0.2 . 125 . 12 LYS CG C 23.6000 0.25 . 126 . 12 LYS HG3 H 1.4400 0.2 . 127 . 12 LYS HG2 H 1.2800 0.2 . 128 . 12 LYS CD C 29.7000 0.25 . 129 . 12 LYS HD3 H 1.9600 0.2 . 130 . 12 LYS HD2 H 1.7500 0.2 . 131 . 12 LYS CE C 42.4000 0.25 . 132 . 12 LYS HE3 H 2.9900 0.2 . 133 . 12 LYS C C 173.5000 0.25 . 134 . 13 MET N N 113.9700 0.25 . 135 . 13 MET H H 8.1900 0.2 . 136 . 13 MET CA C 54.3150 0.25 . 137 . 13 MET HA H 4.5050 0.2 . 138 . 13 MET CB C 33.9400 0.25 . 139 . 13 MET HB3 H 2.1100 0.2 . 140 . 13 MET HB2 H 1.9000 0.2 . 141 . 13 MET CG C 33.3000 0.25 . 142 . 13 MET HG3 H 2.7700 0.2 . 143 . 13 MET HG2 H 2.5400 0.2 . 144 . 13 MET CE C 19.0000 0.25 . 145 . 13 MET HE H 2.2000 0.2 . 146 . 13 MET C C 174.4200 0.25 . 147 . 14 ASN N N 115.8100 0.25 . 148 . 14 ASN H H 7.3600 0.2 . 149 . 14 ASN CA C 51.8000 0.25 . 150 . 14 ASN HA H 4.8700 0.2 . 151 . 14 ASN CB C 37.9300 0.25 . 152 . 14 ASN HB3 H 2.6300 0.2 . 153 . 14 ASN HB2 H 2.5700 0.2 . 154 . 14 ASN C C 173.4000 0.25 . 155 . 15 LEU N N 124.6300 0.25 . 156 . 15 LEU H H 8.0500 0.2 . 157 . 15 LEU CA C 53.2150 0.25 . 158 . 15 LEU HA H 4.5300 0.2 . 159 . 15 LEU CB C 44.8500 0.25 . 160 . 15 LEU HB3 H 0.8400 0.2 . 161 . 15 LEU HB2 H 1.2600 0.2 . 162 . 15 LEU CG C 27.7000 0.25 . 163 . 15 LEU HG H 0.8900 0.2 . 164 . 15 LEU CD1 C 25.0000 0.25 . 165 . 15 LEU HD1 H 0.0100 0.2 . 166 . 15 LEU CD2 C 23.2000 0.25 . 167 . 15 LEU HD2 H -0.1800 0.2 . 168 . 15 LEU C C 177.2700 0.25 . 169 . 16 THR N N 112.4700 0.25 . 170 . 16 THR H H 9.3900 0.2 . 171 . 16 THR CA C 58.1200 0.25 . 172 . 16 THR HA H 5.5650 0.2 . 173 . 16 THR CB C 72.9400 0.25 . 174 . 16 THR HB H 4.1100 0.2 . 175 . 16 THR CG2 C 21.9000 0.25 . 176 . 16 THR HG2 H 1.1400 0.2 . 177 . 16 THR C C 174.2200 0.25 . 178 . 17 TYR N N 117.5000 0.25 . 179 . 17 TYR H H 8.6500 0.2 . 180 . 17 TYR CA C 54.8100 0.25 . 181 . 17 TYR HA H 5.6400 0.2 . 182 . 17 TYR CB C 42.5700 0.25 . 183 . 17 TYR HB3 H 2.9300 0.2 . 184 . 17 TYR HB2 H 2.3300 0.2 . 185 . 17 TYR HD1 H 6.3200 0.2 . 186 . 17 TYR C C 172.0400 0.25 . 187 . 18 ARG N N 119.3700 0.25 . 188 . 18 ARG H H 8.2400 0.2 . 189 . 18 ARG CA C 55.0950 0.25 . 190 . 18 ARG HA H 4.5450 0.2 . 191 . 18 ARG CB C 34.3300 0.25 . 192 . 18 ARG HB3 H 1.8600 0.2 . 193 . 18 ARG CG C 28.4000 0.25 . 194 . 18 ARG HG3 H 1.7300 0.2 . 195 . 18 ARG CD C 44.5000 0.25 . 196 . 18 ARG HD3 H 2.9700 0.2 . 197 . 18 ARG HD2 H 2.7000 0.2 . 198 . 18 ARG C C 173.5300 0.25 . 199 . 19 ILE N N 128.6200 0.25 . 200 . 19 ILE H H 8.8300 0.2 . 201 . 19 ILE CA C 61.3150 0.25 . 202 . 19 ILE HA H 4.1650 0.2 . 203 . 19 ILE CB C 37.4300 0.25 . 204 . 19 ILE HB H 1.7600 0.2 . 205 . 19 ILE CG1 C 36.8000 0.25 . 206 . 19 ILE HG13 H 1.3600 0.2 . 207 . 19 ILE CG2 C 17.6000 0.25 . 208 . 19 ILE HG2 H 0.3900 0.2 . 209 . 19 ILE HD1 H 1.0100 0.2 . 210 . 19 ILE C C 174.9400 0.25 . 211 . 20 VAL N N 130.2000 0.25 . 212 . 20 VAL H H 9.6600 0.2 . 213 . 20 VAL CA C 66.4950 0.25 . 214 . 20 VAL HA H 3.4850 0.2 . 215 . 20 VAL CB C 32.2500 0.25 . 216 . 20 VAL HB H 2.2500 0.2 . 217 . 20 VAL CG1 C 23.5000 0.25 . 218 . 20 VAL HG1 H 1.1100 0.2 . 219 . 20 VAL CG2 C 21.0000 0.25 . 220 . 20 VAL HG2 H 1.0500 0.2 . 221 . 20 VAL C C 175.5100 0.25 . 222 . 21 ASN N N 115.5500 0.25 . 223 . 21 ASN H H 7.7800 0.2 . 224 . 21 ASN CA C 51.3350 0.25 . 225 . 21 ASN HA H 4.7100 0.2 . 226 . 21 ASN CB C 39.1800 0.25 . 227 . 21 ASN HB3 H 3.2400 0.2 . 228 . 21 ASN HB2 H 3.1600 0.2 . 229 . 21 ASN C C 181.9900 0.25 . 230 . 22 TYR N N 111.7300 0.25 . 231 . 22 TYR H H 8.1600 0.2 . 232 . 22 TYR CA C 57.6200 0.25 . 233 . 22 TYR HA H 4.4500 0.2 . 234 . 22 TYR CB C 41.2200 0.25 . 235 . 22 TYR HB3 H 2.8500 0.2 . 236 . 22 TYR HB2 H 2.5200 0.2 . 237 . 22 TYR CD1 C 132.5000 0.25 . 238 . 22 TYR HD1 H 6.9200 0.2 . 239 . 22 TYR HE1 H 6.8400 0.2 . 240 . 22 TYR C C 175.3900 0.25 . 241 . 23 THR N N 110.7700 0.25 . 242 . 23 THR H H 7.6100 0.2 . 243 . 23 THR CA C 55.2000 0.25 . 244 . 23 THR HA H 4.9800 0.2 . 245 . 23 THR CB C 67.5000 0.25 . 246 . 23 THR HB H 2.9700 0.2 . 247 . 23 THR CG2 C 19.7000 0.25 . 248 . 23 THR HG2 H 0.6100 0.2 . 249 . 24 PRO CA C 63.1900 0.25 . 250 . 24 PRO HA H 4.7500 0.2 . 251 . 24 PRO CB C 31.7100 0.25 . 252 . 24 PRO HB3 H 2.2800 0.2 . 253 . 24 PRO HB2 H 2.1400 0.2 . 254 . 24 PRO CG C 26.8000 0.25 . 255 . 24 PRO HG3 H 2.0400 0.2 . 256 . 24 PRO CD C 51.4000 0.25 . 257 . 24 PRO HD3 H 4.5100 0.2 . 258 . 24 PRO HD2 H 3.6500 0.2 . 259 . 24 PRO C C 177.4100 0.25 . 260 . 25 ASP N N 121.8500 0.25 . 261 . 25 ASP H H 8.9400 0.2 . 262 . 25 ASP CA C 55.9800 0.25 . 263 . 25 ASP HA H 4.1750 0.2 . 264 . 25 ASP CB C 41.7400 0.25 . 265 . 25 ASP HB3 H 3.4000 0.2 . 266 . 25 ASP HB2 H 2.7800 0.2 . 267 . 25 ASP C C 175.5600 0.25 . 268 . 26 MET N N 114.3100 0.25 . 269 . 26 MET H H 7.2400 0.2 . 270 . 26 MET CA C 53.4800 0.25 . 271 . 26 MET HA H 4.7650 0.2 . 272 . 26 MET CB C 40.6100 0.25 . 273 . 26 MET HB3 H 2.4100 0.2 . 274 . 26 MET HB2 H 1.4600 0.2 . 275 . 26 MET CG C 32.1000 0.25 . 276 . 26 MET HG3 H 2.5600 0.2 . 277 . 26 MET HG2 H 2.2400 0.2 . 278 . 26 MET CE C 16.7000 0.25 . 279 . 26 MET HE H 1.8200 0.2 . 280 . 26 MET C C 174.7900 0.25 . 281 . 27 THR N N 110.3200 0.25 . 282 . 27 THR H H 8.5800 0.2 . 283 . 27 THR CA C 61.5800 0.25 . 284 . 27 THR HA H 4.4400 0.2 . 285 . 27 THR CB C 70.4200 0.25 . 286 . 27 THR HB H 4.7100 0.2 . 287 . 27 THR CG2 C 22.0000 0.25 . 288 . 27 THR HG2 H 1.4000 0.2 . 289 . 28 HIS CA C 58.7600 0.25 . 290 . 28 HIS HA H 4.2600 0.2 . 291 . 28 HIS CB C 28.3700 0.25 . 292 . 28 HIS HB3 H 3.0400 0.2 . 293 . 28 HIS HB2 H 2.8500 0.2 . 294 . 28 HIS CD2 C 118.0000 0.25 . 295 . 28 HIS HD2 H 7.0500 0.2 . 296 . 28 HIS C C 177.7900 0.25 . 297 . 29 SER N N 112.5100 0.25 . 298 . 29 SER H H 8.5900 0.2 . 299 . 29 SER CA C 61.3000 0.25 . 300 . 29 SER HA H 4.3800 0.2 . 301 . 29 SER CB C 62.5500 0.25 . 302 . 29 SER HB3 H 3.9700 0.2 . 303 . 29 SER C C 177.3100 0.25 . 304 . 30 GLU N N 121.8200 0.25 . 305 . 30 GLU H H 7.7200 0.2 . 306 . 30 GLU CA C 59.5300 0.25 . 307 . 30 GLU HA H 4.0200 0.2 . 308 . 30 GLU CB C 30.3400 0.25 . 309 . 30 GLU HB3 H 2.0700 0.2 . 310 . 30 GLU HB2 H 2.3400 0.2 . 311 . 30 GLU CG C 37.7000 0.25 . 312 . 30 GLU HG3 H 2.5000 0.2 . 313 . 30 GLU HG2 H 2.2800 0.2 . 314 . 30 GLU C C 179.8800 0.25 . 315 . 31 VAL N N 122.5300 0.25 . 316 . 31 VAL H H 8.0900 0.2 . 317 . 31 VAL CA C 66.8850 0.25 . 318 . 31 VAL HA H 3.2250 0.2 . 319 . 31 VAL CB C 32.0200 0.25 . 320 . 31 VAL HB H 2.5000 0.2 . 321 . 31 VAL CG1 C 25.0000 0.25 . 322 . 31 VAL HG1 H 1.0600 0.2 . 323 . 31 VAL CG2 C 23.3000 0.25 . 324 . 31 VAL HG2 H 0.9000 0.2 . 325 . 31 VAL C C 176.7200 0.25 . 326 . 32 GLU N N 117.5200 0.25 . 327 . 32 GLU H H 8.5100 0.2 . 328 . 32 GLU CA C 59.9050 0.25 . 329 . 32 GLU HA H 4.0100 0.2 . 330 . 32 GLU CB C 29.1400 0.25 . 331 . 32 GLU HB3 H 2.4400 0.2 . 332 . 32 GLU HB2 H 2.1700 0.2 . 333 . 32 GLU CG C 37.3000 0.25 . 334 . 32 GLU HG3 H 2.8900 0.2 . 335 . 32 GLU HG2 H 2.5200 0.2 . 336 . 32 GLU C C 180.0200 0.25 . 337 . 33 LYS N N 119.8100 0.25 . 338 . 33 LYS H H 8.4400 0.2 . 339 . 33 LYS CA C 59.3450 0.25 . 340 . 33 LYS HA H 4.0950 0.2 . 341 . 33 LYS CB C 32.8500 0.25 . 342 . 33 LYS HB3 H 1.9600 0.2 . 343 . 33 LYS CG C 25.3000 0.25 . 344 . 33 LYS HG3 H 1.6400 0.2 . 345 . 33 LYS CD C 29.4000 0.25 . 346 . 33 LYS HD3 H 1.8800 0.2 . 347 . 33 LYS HD2 H 1.7700 0.2 . 348 . 33 LYS CE C 42.1000 0.25 . 349 . 33 LYS HE3 H 3.1700 0.2 . 350 . 33 LYS C C 178.3000 0.25 . 351 . 34 ALA N N 122.5800 0.25 . 352 . 34 ALA H H 7.8400 0.2 . 353 . 34 ALA CA C 55.6250 0.25 . 354 . 34 ALA HA H 4.1950 0.2 . 355 . 34 ALA CB C 17.6530 0.25 . 356 . 34 ALA HB H 1.2548 0.2 . 357 . 34 ALA C C 180.0500 0.25 . 358 . 35 PHE N N 113.8200 0.25 . 359 . 35 PHE H H 7.9300 0.2 . 360 . 35 PHE CA C 58.7700 0.25 . 361 . 35 PHE HA H 4.6800 0.2 . 362 . 35 PHE CB C 37.1800 0.25 . 363 . 35 PHE HB3 H 3.1200 0.2 . 364 . 35 PHE CD1 C 129.6000 0.25 . 365 . 35 PHE HD1 H 7.0200 0.2 . 366 . 35 PHE CE1 C 131.2000 0.25 . 367 . 35 PHE HE1 H 6.6700 0.2 . 368 . 35 PHE CZ C 129.8000 0.25 . 369 . 35 PHE HZ H 6.1600 0.2 . 370 . 35 PHE C C 177.2700 0.25 . 371 . 36 LYS N N 120.0300 0.25 . 372 . 36 LYS H H 8.4900 0.2 . 373 . 36 LYS CA C 60.8150 0.25 . 374 . 36 LYS HA H 4.1850 0.2 . 375 . 36 LYS CB C 33.0200 0.25 . 376 . 36 LYS HB3 H 2.1700 0.2 . 377 . 36 LYS CG C 25.2000 0.25 . 378 . 36 LYS HG3 H 1.8000 0.2 . 379 . 36 LYS HG2 H 1.6400 0.2 . 380 . 36 LYS CD C 32.8000 0.25 . 381 . 36 LYS HD3 H 1.9200 0.2 . 382 . 36 LYS CE C 42.1000 0.25 . 383 . 36 LYS HE3 H 3.1900 0.2 . 384 . 36 LYS C C 180.0200 0.25 . 385 . 37 LYS N N 119.8100 0.25 . 386 . 37 LYS H H 8.4400 0.2 . 387 . 37 LYS CA C 59.7800 0.25 . 388 . 37 LYS HA H 4.0800 0.2 . 389 . 37 LYS CB C 32.7900 0.25 . 390 . 37 LYS HB3 H 1.9100 0.2 . 391 . 37 LYS HB2 H 1.8000 0.2 . 392 . 37 LYS CG C 25.4000 0.25 . 393 . 37 LYS HG3 H 1.6300 0.2 . 394 . 37 LYS HG2 H 1.3000 0.2 . 395 . 37 LYS CD C 29.3000 0.25 . 396 . 37 LYS HD3 H 1.4700 0.2 . 397 . 37 LYS HD2 H 1.1500 0.2 . 398 . 37 LYS CE C 41.5000 0.25 . 399 . 37 LYS HE3 H 2.4300 0.2 . 400 . 37 LYS C C 178.6800 0.25 . 401 . 38 ALA N N 123.3700 0.25 . 402 . 38 ALA H H 8.3800 0.2 . 403 . 38 ALA CA C 55.7200 0.25 . 404 . 38 ALA HA H 4.2550 0.2 . 405 . 38 ALA CB C 19.3430 0.25 . 406 . 38 ALA HB H 1.5100 0.2 . 407 . 38 ALA C C 178.2900 0.25 . 408 . 39 PHE N N 114.3300 0.25 . 409 . 39 PHE H H 8.1200 0.2 . 410 . 39 PHE CA C 63.0500 0.25 . 411 . 39 PHE HA H 4.2250 0.2 . 412 . 39 PHE CB C 38.8300 0.25 . 413 . 39 PHE HB3 H 2.5500 0.2 . 414 . 39 PHE HB2 H 2.6700 0.2 . 415 . 39 PHE CD1 C 129.7000 0.25 . 416 . 39 PHE HD1 H 5.6700 0.2 . 417 . 39 PHE CE1 C 128.7000 0.25 . 418 . 39 PHE HE1 H 5.3200 0.2 . 419 . 39 PHE CZ C 126.6000 0.25 . 420 . 39 PHE HZ H 5.4800 0.2 . 421 . 39 PHE C C 178.4100 0.25 . 422 . 40 LYS N N 120.8500 0.25 . 423 . 40 LYS H H 7.8500 0.2 . 424 . 40 LYS CA C 58.3400 0.25 . 425 . 40 LYS HA H 4.6250 0.2 . 426 . 40 LYS CB C 32.8200 0.25 . 427 . 40 LYS HB3 H 2.1800 0.2 . 428 . 40 LYS HB2 H 2.0100 0.2 . 429 . 40 LYS CG C 25.4000 0.25 . 430 . 40 LYS HG3 H 1.7300 0.2 . 431 . 40 LYS HG2 H 1.5000 0.2 . 432 . 40 LYS CD C 29.8000 0.25 . 433 . 40 LYS HD3 H 1.8800 0.2 . 434 . 40 LYS HD2 H 1.7600 0.2 . 435 . 40 LYS CE C 42.4000 0.25 . 436 . 40 LYS HE3 H 3.2200 0.2 . 437 . 40 LYS C C 177.4900 0.25 . 438 . 41 VAL N N 112.9300 0.25 . 439 . 41 VAL H H 7.3500 0.2 . 440 . 41 VAL CA C 65.0700 0.25 . 441 . 41 VAL HA H 3.9550 0.2 . 442 . 41 VAL CB C 31.2300 0.25 . 443 . 41 VAL HB H 2.0800 0.2 . 444 . 41 VAL CG1 C 22.7000 0.25 . 445 . 41 VAL HG1 H 0.7300 0.2 . 446 . 41 VAL CG2 C 21.4000 0.25 . 447 . 41 VAL HG2 H 0.8300 0.2 . 448 . 41 VAL C C 176.8400 0.25 . 449 . 42 TRP N N 116.2400 0.25 . 450 . 42 TRP H H 6.8600 0.2 . 451 . 42 TRP CA C 57.7400 0.25 . 452 . 42 TRP HA H 4.9200 0.2 . 453 . 42 TRP CB C 30.9100 0.25 . 454 . 42 TRP HB3 H 3.3500 0.2 . 455 . 42 TRP NE1 N 127.8100 0.25 . 456 . 42 TRP HE1 H 10.1800 0.2 . 457 . 42 TRP CD1 C 127.8000 0.25 . 458 . 42 TRP HD1 H 7.4800 0.2 . 459 . 42 TRP CE3 C 119.3000 0.25 . 460 . 42 TRP HE3 H 7.5200 0.2 . 461 . 42 TRP CZ3 C 121.9000 0.25 . 462 . 42 TRP HZ3 H 6.9900 0.2 . 463 . 42 TRP CZ2 C 115.7000 0.25 . 464 . 42 TRP HZ2 H 7.5000 0.2 . 465 . 42 TRP CH2 C 123.8000 0.25 . 466 . 42 TRP HH2 H 7.0100 0.2 . 467 . 42 TRP C C 180.6200 0.25 . 468 . 43 SER N N 117.4600 0.25 . 469 . 43 SER H H 9.1700 0.2 . 470 . 43 SER CA C 61.5150 0.25 . 471 . 43 SER HA H 4.3950 0.2 . 472 . 43 SER CB C 63.3300 0.25 . 473 . 43 SER HB3 H 4.5100 0.2 . 474 . 43 SER HB2 H 4.0500 0.2 . 475 . 43 SER C C 176.7000 0.25 . 476 . 44 ASP N N 120.6000 0.25 . 477 . 44 ASP H H 8.6800 0.2 . 478 . 44 ASP CA C 56.8200 0.25 . 479 . 44 ASP HA H 4.7600 0.2 . 480 . 44 ASP CB C 41.1300 0.25 . 481 . 44 ASP HB3 H 3.0100 0.2 . 482 . 44 ASP HB2 H 2.8100 0.2 . 483 . 44 ASP C C 178.0100 0.25 . 484 . 45 VAL N N 107.7600 0.25 . 485 . 45 VAL H H 7.1500 0.2 . 486 . 45 VAL CA C 60.3950 0.25 . 487 . 45 VAL HA H 5.0150 0.2 . 488 . 45 VAL CB C 32.5700 0.25 . 489 . 45 VAL HB H 2.7600 0.2 . 490 . 45 VAL CG1 C 21.5000 0.25 . 491 . 45 VAL HG1 H 1.0500 0.2 . 492 . 45 VAL CG2 C 19.0000 0.25 . 493 . 45 VAL HG2 H 1.2700 0.2 . 494 . 45 VAL C C 173.8000 0.25 . 495 . 46 THR N N 109.2300 0.25 . 496 . 46 THR H H 7.4000 0.2 . 497 . 46 THR CA C 60.4600 0.25 . 498 . 46 THR HA H 5.6700 0.2 . 499 . 46 THR CB C 72.4000 0.25 . 500 . 46 THR HB H 4.2800 0.2 . 501 . 46 THR CG2 C 24.8000 0.25 . 502 . 46 THR HG2 H 1.6700 0.2 . 503 . 46 THR C C 173.8400 0.25 . 504 . 47 PRO CA C 62.3100 0.25 . 505 . 47 PRO HA H 4.9300 0.2 . 506 . 47 PRO CB C 31.0400 0.25 . 507 . 47 PRO HB3 H 2.4300 0.2 . 508 . 47 PRO HB2 H 2.0700 0.2 . 509 . 47 PRO CG C 27.7000 0.25 . 510 . 47 PRO HG3 H 2.1200 0.2 . 511 . 47 PRO HG2 H 1.9900 0.2 . 512 . 47 PRO CD C 52.1000 0.25 . 513 . 47 PRO HD3 H 4.0100 0.2 . 514 . 47 PRO HD2 H 3.2800 0.2 . 515 . 47 PRO C C 176.6700 0.25 . 516 . 48 LEU N N 117.2600 0.25 . 517 . 48 LEU H H 7.2400 0.2 . 518 . 48 LEU CA C 55.2700 0.25 . 519 . 48 LEU HA H 4.3150 0.2 . 520 . 48 LEU CB C 43.7300 0.25 . 521 . 48 LEU HB3 H 1.3800 0.2 . 522 . 48 LEU HB2 H 0.5900 0.2 . 523 . 48 LEU CG C 27.4000 0.25 . 524 . 48 LEU HG H 1.1900 0.2 . 525 . 48 LEU CD1 C 26.8000 0.25 . 526 . 48 LEU HD1 H 0.5700 0.2 . 527 . 48 LEU CD2 C 22.6000 0.25 . 528 . 48 LEU HD2 H 0.4200 0.2 . 529 . 48 LEU C C 176.5700 0.25 . 530 . 49 ASN N N 117.8500 0.25 . 531 . 49 ASN H H 8.1800 0.2 . 532 . 49 ASN CA C 52.1750 0.25 . 533 . 49 ASN HA H 4.7400 0.2 . 534 . 49 ASN CB C 42.8100 0.25 . 535 . 49 ASN HB3 H 2.5600 0.2 . 536 . 49 ASN C C 172.1100 0.25 . 537 . 50 PHE N N 118.9300 0.25 . 538 . 50 PHE H H 8.3700 0.2 . 539 . 50 PHE CA C 56.6250 0.25 . 540 . 50 PHE HA H 5.1950 0.2 . 541 . 50 PHE CB C 41.5900 0.25 . 542 . 50 PHE HB3 H 2.4900 0.2 . 543 . 50 PHE HB2 H 2.0600 0.2 . 544 . 50 PHE CD1 C 132.6000 0.25 . 545 . 50 PHE HD1 H 6.7200 0.2 . 546 . 50 PHE CE1 C 130.3000 0.25 . 547 . 50 PHE HE1 H 6.9800 0.2 . 548 . 50 PHE CZ C 128.9000 0.25 . 549 . 50 PHE HZ H 7.1700 0.2 . 550 . 50 PHE C C 175.6100 0.25 . 551 . 51 THR N N 120.1500 0.25 . 552 . 51 THR H H 8.5200 0.2 . 553 . 51 THR CA C 61.5500 0.25 . 554 . 51 THR HA H 4.4400 0.2 . 555 . 51 THR CB C 71.4700 0.25 . 556 . 51 THR HB H 3.7100 0.2 . 557 . 51 THR CG2 C 21.0000 0.25 . 558 . 51 THR HG2 H 1.1200 0.2 . 559 . 51 THR C C 171.7800 0.25 . 560 . 52 ARG N N 128.5100 0.25 . 561 . 52 ARG H H 8.5200 0.2 . 562 . 52 ARG CA C 55.2900 0.25 . 563 . 52 ARG HA H 3.3400 0.2 . 564 . 52 ARG CB C 30.9400 0.25 . 565 . 52 ARG HB3 H 1.1148 0.2 . 566 . 52 ARG HB2 H 1.5800 0.2 . 567 . 52 ARG CG C 27.7000 0.25 . 568 . 52 ARG HG3 H 0.9200 0.2 . 569 . 52 ARG HG2 H 0.8700 0.2 . 570 . 52 ARG CD C 44.2000 0.25 . 571 . 52 ARG HD3 H 3.1600 0.2 . 572 . 52 ARG HD2 H 3.0700 0.2 . 573 . 52 ARG C C 175.2700 0.25 . 574 . 53 LEU N N 127.0500 0.25 . 575 . 53 LEU H H 8.9800 0.2 . 576 . 53 LEU CA C 52.9800 0.25 . 577 . 53 LEU HA H 4.6800 0.2 . 578 . 53 LEU CB C 44.2200 0.25 . 579 . 53 LEU HB3 H 1.7500 0.2 . 580 . 53 LEU HB2 H 1.3500 0.2 . 581 . 53 LEU CG C 27.1000 0.25 . 582 . 53 LEU HG H 1.5800 0.2 . 583 . 53 LEU CD1 C 24.9000 0.25 . 584 . 53 LEU HD1 H 0.8700 0.2 . 585 . 54 HIS CA C 57.3800 0.25 . 586 . 54 HIS HA H 4.4600 0.2 . 587 . 54 HIS CB C 31.5400 0.25 . 588 . 54 HIS HB3 H 3.2800 0.2 . 589 . 54 HIS HB2 H 3.0000 0.2 . 590 . 54 HIS CD2 C 119.3000 0.25 . 591 . 54 HIS HD2 H 7.0500 0.2 . 592 . 54 HIS C C 174.0100 0.25 . 593 . 55 ASP N N 117.0000 0.25 . 594 . 55 ASP H H 7.6800 0.2 . 595 . 55 ASP CA C 52.5200 0.25 . 596 . 55 ASP HA H 4.6250 0.2 . 597 . 55 ASP CB C 43.8900 0.25 . 598 . 55 ASP HB3 H 2.6200 0.2 . 599 . 55 ASP C C 174.6700 0.25 . 600 . 56 GLY N N 106.8500 0.25 . 601 . 56 GLY H H 8.3200 0.2 . 602 . 56 GLY CA C 44.4850 0.25 . 603 . 56 GLY HA3 H 4.1200 0.2 . 604 . 56 GLY HA2 H 3.8000 0.2 . 605 . 56 GLY C C 172.8400 0.25 . 606 . 57 ILE N N 118.9200 0.25 . 607 . 57 ILE H H 8.2200 0.2 . 608 . 57 ILE CA C 60.4600 0.25 . 609 . 57 ILE HA H 4.1550 0.2 . 610 . 57 ILE CB C 37.3800 0.25 . 611 . 57 ILE HB H 1.8100 0.2 . 612 . 57 ILE CG1 C 27.3000 0.25 . 613 . 57 ILE HG13 H 1.5200 0.2 . 614 . 57 ILE HG12 H 1.2400 0.2 . 615 . 57 ILE CG2 C 17.8000 0.25 . 616 . 57 ILE HG2 H 0.9100 0.2 . 617 . 57 ILE CD1 C 11.6000 0.25 . 618 . 57 ILE HD1 H 0.8700 0.2 . 619 . 57 ILE C C 175.0000 0.25 . 620 . 58 ALA N N 131.4800 0.25 . 621 . 58 ALA H H 7.9400 0.2 . 622 . 58 ALA CA C 49.0700 0.25 . 623 . 58 ALA HA H 4.5450 0.2 . 624 . 58 ALA CB C 22.6700 0.25 . 625 . 58 ALA HB H 0.9548 0.2 . 626 . 58 ALA C C 176.9700 0.25 . 627 . 59 ASP N N 121.1500 0.25 . 628 . 59 ASP H H 8.3200 0.2 . 629 . 59 ASP CA C 58.6000 0.25 . 630 . 59 ASP HA H 4.4100 0.2 . 631 . 59 ASP CB C 41.1800 0.25 . 632 . 59 ASP HB3 H 2.3000 0.2 . 633 . 59 ASP HB2 H 2.8200 0.2 . 634 . 59 ASP C C 177.4200 0.25 . 635 . 60 ILE N N 123.8900 0.25 . 636 . 60 ILE H H 8.8500 0.2 . 637 . 60 ILE CA C 61.2350 0.25 . 638 . 60 ILE HA H 4.1650 0.2 . 639 . 60 ILE CB C 39.1000 0.25 . 640 . 60 ILE HB H 1.8400 0.2 . 641 . 60 ILE HG13 H 1.4300 0.2 . 642 . 60 ILE HG12 H 1.3300 0.2 . 643 . 60 ILE CG2 C 15.2000 0.25 . 644 . 60 ILE HG2 H 1.0600 0.2 . 645 . 60 ILE CD1 C 13.8000 0.25 . 646 . 60 ILE HD1 H 0.8200 0.2 . 647 . 60 ILE C C 174.1700 0.25 . 648 . 61 MET N N 126.9600 0.25 . 649 . 61 MET H H 7.4800 0.2 . 650 . 61 MET CA C 53.8450 0.25 . 651 . 61 MET HA H 4.9500 0.2 . 652 . 61 MET CB C 32.8500 0.25 . 653 . 61 MET HB3 H 2.2200 0.2 . 654 . 61 MET HB2 H 1.8600 0.2 . 655 . 61 MET HG3 H 2.7400 0.2 . 656 . 61 MET CE C 18.9000 0.25 . 657 . 61 MET HE H 2.2900 0.2 . 658 . 61 MET C C 176.7400 0.25 . 659 . 62 ILE N N 128.0800 0.25 . 660 . 62 ILE H H 9.0900 0.2 . 661 . 62 ILE CA C 60.8200 0.25 . 662 . 62 ILE HA H 5.4150 0.2 . 663 . 62 ILE CB C 40.6900 0.25 . 664 . 62 ILE HB H 1.7600 0.2 . 665 . 62 ILE CG2 C 19.0000 0.25 . 666 . 62 ILE HG2 H 0.5200 0.2 . 667 . 62 ILE CG1 C 28.3000 0.25 . 668 . 62 ILE HG13 H 0.7900 0.2 . 669 . 62 ILE CD1 C 16.1000 0.25 . 670 . 62 ILE HD1 H 0.4900 0.2 . 671 . 62 ILE C C 174.4000 0.25 . 672 . 63 SER N N 117.7600 0.25 . 673 . 63 SER H H 8.8200 0.2 . 674 . 63 SER CA C 56.8350 0.25 . 675 . 63 SER HA H 5.1750 0.2 . 676 . 63 SER CB C 66.5900 0.25 . 677 . 63 SER HB3 H 3.8400 0.2 . 678 . 63 SER C C 172.3600 0.25 . 679 . 64 PHE N N 120.7200 0.25 . 680 . 64 PHE H H 9.9300 0.2 . 681 . 64 PHE CA C 56.3300 0.25 . 682 . 64 PHE HA H 5.5350 0.2 . 683 . 64 PHE CB C 41.8600 0.25 . 684 . 64 PHE HB3 H 2.9400 0.2 . 685 . 64 PHE HB2 H 2.7800 0.2 . 686 . 64 PHE HD1 H 7.0700 0.2 . 687 . 64 PHE C C 177.1900 0.25 . 688 . 65 GLY N N 109.5400 0.25 . 689 . 65 GLY H H 9.0300 0.2 . 690 . 65 GLY CA C 44.5150 0.25 . 691 . 65 GLY HA3 H 4.8400 0.2 . 692 . 65 GLY HA2 H 3.6000 0.2 . 693 . 65 GLY C C 182.4600 0.25 . 694 . 66 ILE N N 116.4800 0.25 . 695 . 66 ILE H H 8.4300 0.2 . 696 . 66 ILE CA C 59.7050 0.25 . 697 . 66 ILE HA H 4.8100 0.2 . 698 . 66 ILE CB C 42.2000 0.25 . 699 . 66 ILE HB H 1.9000 0.2 . 700 . 66 ILE CG1 C 26.7000 0.25 . 701 . 66 ILE HG13 H 1.5200 0.2 . 702 . 66 ILE HG12 H 1.1200 0.2 . 703 . 66 ILE CG2 C 18.7000 0.25 . 704 . 66 ILE HG2 H 1.0000 0.2 . 705 . 66 ILE CD1 C 13.5000 0.25 . 706 . 66 ILE HD1 H 0.9400 0.2 . 707 . 66 ILE C C 174.4200 0.25 . 708 . 67 LYS N N 121.5500 0.25 . 709 . 67 LYS H H 9.8500 0.2 . 710 . 67 LYS CA C 57.3650 0.25 . 711 . 67 LYS HA H 3.8450 0.2 . 712 . 67 LYS CB C 30.2900 0.25 . 713 . 67 LYS HB3 H 2.1200 0.2 . 714 . 67 LYS HB2 H 2.0100 0.2 . 715 . 67 LYS CG C 25.4000 0.25 . 716 . 67 LYS HG3 H 1.7100 0.2 . 717 . 67 LYS HG2 H 1.4000 0.2 . 718 . 67 LYS CD C 28.4000 0.25 . 719 . 67 LYS HD3 H 1.8300 0.2 . 720 . 67 LYS HD2 H 1.7200 0.2 . 721 . 67 LYS CE C 41.9000 0.25 . 722 . 67 LYS HE3 H 2.9400 0.2 . 723 . 67 LYS C C 177.6600 0.25 . 724 . 68 GLU N N 127.7600 0.25 . 725 . 68 GLU H H 8.1800 0.2 . 726 . 68 GLU CA C 57.7500 0.25 . 727 . 68 GLU HA H 4.3100 0.2 . 728 . 68 GLU CB C 28.5000 0.25 . 729 . 68 GLU HB3 H 2.2000 0.2 . 730 . 68 GLU HG3 H 2.4500 0.2 . 731 . 68 GLU C C 174.7600 0.25 . 732 . 74 PRO CA C 63.0400 0.25 . 733 . 74 PRO HA H 4.3700 0.2 . 734 . 74 PRO CB C 31.5600 0.25 . 735 . 74 PRO HB3 H 2.0400 0.2 . 736 . 74 PRO HB2 H 1.9400 0.2 . 737 . 74 PRO CD C 53.9400 0.25 . 738 . 74 PRO HD3 H 2.5400 0.2 . 739 . 74 PRO HD2 H 2.4100 0.2 . 740 . 74 PRO C C 178.3600 0.25 . 741 . 75 PHE N N 118.2800 0.25 . 742 . 75 PHE H H 7.9700 0.2 . 743 . 75 PHE CA C 56.8750 0.25 . 744 . 75 PHE HA H 4.7950 0.2 . 745 . 75 PHE CB C 38.1400 0.25 . 746 . 75 PHE HB3 H 3.9100 0.2 . 747 . 75 PHE HB2 H 3.0900 0.2 . 748 . 75 PHE HD1 H 7.2700 0.2 . 749 . 75 PHE C C 175.8800 0.25 . 750 . 76 ASP N N 116.1100 0.25 . 751 . 76 ASP H H 8.3500 0.2 . 752 . 76 ASP CA C 53.4050 0.25 . 753 . 76 ASP HA H 4.7350 0.2 . 754 . 76 ASP CB C 41.9300 0.25 . 755 . 76 ASP HB3 H 3.1500 0.2 . 756 . 76 ASP HB2 H 2.6700 0.2 . 757 . 76 ASP C C 177.3700 0.25 . 758 . 77 GLY N N 110.0400 0.25 . 759 . 77 GLY H H 8.6800 0.2 . 760 . 77 GLY CA C 43.9600 0.25 . 761 . 77 GLY HA3 H 4.4700 0.2 . 762 . 78 PRO CA C 63.9000 0.25 . 763 . 78 PRO HA H 4.0500 0.2 . 764 . 78 PRO CB C 31.7000 0.25 . 765 . 78 PRO HB3 H 2.2900 0.2 . 766 . 78 PRO HB2 H 1.8500 0.2 . 767 . 78 PRO CG C 27.7000 0.25 . 768 . 78 PRO HG3 H 2.1400 0.2 . 769 . 78 PRO HG2 H 2.0400 0.2 . 770 . 79 SER N N 124.7500 0.25 . 771 . 79 SER H H 13.0200 0.2 . 772 . 79 SER CA C 58.4300 0.25 . 773 . 79 SER HA H 3.5600 0.2 . 774 . 79 SER CB C 63.0800 0.25 . 775 . 79 SER HB3 H 4.0200 0.2 . 776 . 79 SER HB2 H 4.2400 0.2 . 777 . 79 SER C C 174.3900 0.25 . 778 . 80 GLY N N 111.4900 0.25 . 779 . 80 GLY H H 8.3600 0.2 . 780 . 80 GLY CA C 46.3450 0.25 . 781 . 80 GLY HA3 H 4.0200 0.2 . 782 . 80 GLY HA2 H 3.4100 0.2 . 783 . 80 GLY C C 173.6000 0.25 . 784 . 81 LEU N N 130.1400 0.25 . 785 . 81 LEU H H 10.0600 0.2 . 786 . 81 LEU CA C 56.4300 0.25 . 787 . 81 LEU HA H 3.7150 0.2 . 788 . 81 LEU CB C 41.2600 0.25 . 789 . 81 LEU HB3 H 1.7700 0.2 . 790 . 81 LEU HB2 H 1.5100 0.2 . 791 . 81 LEU CG C 27.3000 0.25 . 792 . 81 LEU HG H 1.3800 0.2 . 793 . 81 LEU CD1 C 27.3000 0.25 . 794 . 81 LEU HD1 H 0.7800 0.2 . 795 . 81 LEU CD2 C 24.7000 0.25 . 796 . 81 LEU HD2 H 0.4300 0.2 . 797 . 81 LEU C C 177.3100 0.25 . 798 . 82 LEU N N 127.5800 0.25 . 799 . 82 LEU H H 7.9800 0.2 . 800 . 82 LEU CA C 55.8550 0.25 . 801 . 82 LEU HA H 4.3000 0.2 . 802 . 82 LEU CB C 43.6600 0.25 . 803 . 82 LEU HB3 H 1.1400 0.2 . 804 . 82 LEU HB2 H 1.0700 0.2 . 805 . 82 LEU CG C 25.5000 0.25 . 806 . 82 LEU HG H 1.5300 0.2 . 807 . 82 LEU CD1 C 25.0000 0.25 . 808 . 82 LEU HD1 H -0.3200 0.2 . 809 . 82 LEU CD2 C 19.4000 0.25 . 810 . 82 LEU HD2 H -0.5400 0.2 . 811 . 82 LEU C C 175.5200 0.25 . 812 . 83 ALA N N 114.2600 0.25 . 813 . 83 ALA H H 6.7800 0.2 . 814 . 83 ALA CA C 51.2200 0.25 . 815 . 83 ALA HA H 4.5350 0.2 . 816 . 83 ALA CB C 21.9900 0.25 . 817 . 83 ALA HB H 0.8700 0.2 . 818 . 83 ALA C C 174.9600 0.25 . 819 . 84 HIS N N 116.6500 0.25 . 820 . 84 HIS H H 8.9800 0.2 . 821 . 84 HIS CA C 54.0750 0.25 . 822 . 84 HIS HA H 5.1450 0.2 . 823 . 84 HIS CB C 31.2900 0.25 . 824 . 84 HIS HB3 H 3.1000 0.2 . 825 . 84 HIS HB2 H 2.9400 0.2 . 826 . 84 HIS C C 171.3700 0.25 . 827 . 85 ALA N N 121.1500 0.25 . 828 . 85 ALA H H 8.3200 0.2 . 829 . 85 ALA CA C 50.2500 0.25 . 830 . 85 ALA HA H 5.0850 0.2 . 831 . 85 ALA CB C 23.3300 0.25 . 832 . 85 ALA HB H 1.4500 0.2 . 833 . 85 ALA C C 176.5600 0.25 . 834 . 86 PHE N N 120.8700 0.25 . 835 . 86 PHE H H 8.1000 0.2 . 836 . 86 PHE CA C 54.8400 0.25 . 837 . 86 PHE HA H 4.6400 0.2 . 838 . 86 PHE CB C 41.1000 0.25 . 839 . 86 PHE HB3 H 2.7600 0.2 . 840 . 86 PHE HB2 H 2.6700 0.2 . 841 . 86 PHE HD1 H 7.1700 0.2 . 842 . 88 PRO CA C 64.1800 0.25 . 843 . 88 PRO HA H 3.1100 0.2 . 844 . 88 PRO CB C 31.6700 0.25 . 845 . 88 PRO HB3 H 0.0200 0.2 . 846 . 88 PRO HB2 H 0.9200 0.2 . 847 . 88 PRO C C 174.4900 0.25 . 848 . 89 GLY N N 106.9000 0.25 . 849 . 89 GLY H H 5.5700 0.2 . 850 . 89 GLY CA C 44.1700 0.25 . 851 . 92 TYR CA C 59.1300 0.25 . 852 . 92 TYR HA H 4.5100 0.2 . 853 . 92 TYR CB C 35.9700 0.25 . 854 . 92 TYR HB3 H 2.4200 0.2 . 855 . 92 TYR HB2 H 2.0600 0.2 . 856 . 92 TYR CD1 C 138.7000 0.25 . 857 . 92 TYR HD1 H 6.9000 0.2 . 858 . 92 TYR HE1 H 7.1800 0.2 . 859 . 92 TYR C C 175.0400 0.25 . 860 . 93 GLY N N 105.3900 0.25 . 861 . 93 GLY H H 7.8200 0.2 . 862 . 93 GLY CA C 47.2450 0.25 . 863 . 93 GLY HA3 H 3.2800 0.2 . 864 . 93 GLY HA2 H 3.8600 0.2 . 865 . 93 GLY C C 175.0500 0.25 . 866 . 94 GLY N N 119.8700 0.25 . 867 . 94 GLY H H 8.0200 0.2 . 868 . 94 GLY CA C 46.8150 0.25 . 869 . 94 GLY HA3 H 4.7200 0.2 . 870 . 94 GLY HA2 H 4.2900 0.2 . 871 . 94 GLY C C 171.7100 0.25 . 872 . 95 ASP N N 122.7400 0.25 . 873 . 95 ASP H H 8.6000 0.2 . 874 . 95 ASP CA C 55.9800 0.25 . 875 . 95 ASP HA H 4.6100 0.2 . 876 . 95 ASP CB C 40.1800 0.25 . 877 . 95 ASP HB3 H 3.2400 0.2 . 878 . 95 ASP HB2 H 3.1000 0.2 . 879 . 95 ASP C C 173.2800 0.25 . 880 . 96 ALA N N 118.4100 0.25 . 881 . 96 ALA H H 7.9000 0.2 . 882 . 96 ALA CA C 50.9950 0.25 . 883 . 96 ALA HA H 4.9700 0.2 . 884 . 96 ALA CB C 22.7200 0.25 . 885 . 96 ALA HB H 1.2448 0.2 . 886 . 96 ALA C C 174.7200 0.25 . 887 . 97 HIS N N 120.9700 0.25 . 888 . 97 HIS H H 9.0500 0.2 . 889 . 97 HIS CA C 50.8000 0.25 . 890 . 97 HIS HA H 5.9300 0.2 . 891 . 97 HIS CB C 34.7100 0.25 . 892 . 97 HIS HB3 H 2.9800 0.2 . 893 . 97 HIS HB2 H 2.8300 0.2 . 894 . 97 HIS CD2 C 117.4000 0.25 . 895 . 97 HIS HD2 H 7.3700 0.2 . 896 . 97 HIS C C 173.6400 0.25 . 897 . 98 PHE N N 121.9700 0.25 . 898 . 98 PHE H H 8.8200 0.2 . 899 . 98 PHE CA C 56.9200 0.25 . 900 . 98 PHE HA H 4.2200 0.2 . 901 . 98 PHE CB C 42.0300 0.25 . 902 . 98 PHE HB3 H 2.1400 0.2 . 903 . 98 PHE HB2 H 1.9900 0.2 . 904 . 98 PHE CD1 C 131.9000 0.25 . 905 . 98 PHE HD1 H 6.3600 0.2 . 906 . 98 PHE CE1 C 129.7000 0.25 . 907 . 98 PHE HE1 H 6.6000 0.2 . 908 . 98 PHE CZ C 127.0000 0.25 . 909 . 98 PHE HZ H 6.4600 0.2 . 910 . 98 PHE C C 173.9300 0.25 . 911 . 99 ASP N N 122.9600 0.25 . 912 . 99 ASP H H 8.0300 0.2 . 913 . 99 ASP CA C 53.8800 0.25 . 914 . 99 ASP HA H 3.8800 0.2 . 915 . 99 ASP CB C 40.9600 0.25 . 916 . 99 ASP HB3 H 0.9848 0.2 . 917 . 99 ASP HB2 H 3.0800 0.2 . 918 . 99 ASP C C 179.1900 0.25 . 919 . 100 ASP N N 128.9800 0.25 . 920 . 100 ASP H H 10.2000 0.2 . 921 . 100 ASP CA C 53.3850 0.25 . 922 . 100 ASP HA H 5.5800 0.2 . 923 . 100 ASP CB C 40.8900 0.25 . 924 . 100 ASP HB3 H 2.9500 0.2 . 925 . 100 ASP HB2 H 2.6300 0.2 . 926 . 100 ASP C C 179.4900 0.25 . 927 . 101 ASP N N 123.8400 0.25 . 928 . 101 ASP H H 9.3500 0.2 . 929 . 101 ASP CA C 56.5750 0.25 . 930 . 101 ASP HA H 4.9800 0.2 . 931 . 101 ASP CB C 39.0600 0.25 . 932 . 101 ASP HB3 H 2.7500 0.2 . 933 . 101 ASP HB2 H 2.1400 0.2 . 934 . 101 ASP C C 177.7700 0.25 . 935 . 102 GLU N N 114.8900 0.25 . 936 . 102 GLU H H 7.3400 0.2 . 937 . 102 GLU CA C 53.1150 0.25 . 938 . 102 GLU HA H 4.7800 0.2 . 939 . 102 GLU CB C 27.0300 0.25 . 940 . 102 GLU HB3 H 1.1700 0.2 . 941 . 102 GLU HB2 H 0.5248 0.2 . 942 . 102 GLU CG C 34.3000 0.25 . 943 . 102 GLU HG3 H 1.5300 0.2 . 944 . 102 GLU HG2 H 2.6100 0.2 . 945 . 102 GLU C C 177.4800 0.25 . 946 . 103 THR N N 122.1300 0.25 . 947 . 103 THR H H 8.1400 0.2 . 948 . 103 THR CA C 61.6450 0.25 . 949 . 103 THR HA H 4.3300 0.2 . 950 . 103 THR CB C 68.7600 0.25 . 951 . 103 THR HB H 3.9400 0.2 . 952 . 103 THR CG2 C 21.1000 0.25 . 953 . 103 THR HG2 H 1.0800 0.2 . 954 . 103 THR C C 172.1400 0.25 . 955 . 104 TRP N N 132.1100 0.25 . 956 . 104 TRP H H 9.5900 0.2 . 957 . 104 TRP CA C 56.1000 0.25 . 958 . 104 TRP HA H 5.2650 0.2 . 959 . 104 TRP CB C 31.1300 0.25 . 960 . 104 TRP HB3 H 3.3800 0.2 . 961 . 104 TRP HB2 H 3.0000 0.2 . 962 . 104 TRP CD1 C 128.1000 0.25 . 963 . 104 TRP HD1 H 7.4900 0.2 . 964 . 104 TRP NE1 N 125.9500 0.25 . 965 . 104 TRP HE1 H 9.5600 0.2 . 966 . 104 TRP CE3 C 122.2000 0.25 . 967 . 104 TRP HE3 H 7.5100 0.2 . 968 . 104 TRP CZ3 C 120.8000 0.25 . 969 . 104 TRP HZ3 H 6.7500 0.2 . 970 . 104 TRP CZ2 C 115.2000 0.25 . 971 . 104 TRP HZ2 H 7.8600 0.2 . 972 . 104 TRP CH2 C 123.1000 0.25 . 973 . 104 TRP HH2 H 6.8400 0.2 . 974 . 104 TRP C C 176.3400 0.25 . 975 . 105 THR N N 113.2100 0.25 . 976 . 105 THR H H 8.7800 0.2 . 977 . 105 THR CA C 59.9800 0.25 . 978 . 105 THR HA H 4.9550 0.2 . 979 . 105 THR CB C 71.4100 0.25 . 980 . 105 THR HB H 4.2200 0.2 . 981 . 105 THR CG2 C 19.3000 0.25 . 982 . 105 THR HG2 H 0.7900 0.2 . 983 . 105 THR C C 174.4000 0.25 . 984 . 106 SER N N 115.7000 0.25 . 985 . 106 SER H H 8.6000 0.2 . 986 . 106 SER CA C 57.6450 0.25 . 987 . 106 SER HA H 4.9300 0.2 . 988 . 106 SER CB C 63.9400 0.25 . 989 . 106 SER HB3 H 4.1400 0.2 . 990 . 106 SER HB2 H 3.9700 0.2 . 991 . 106 SER C C 174.9300 0.25 . 992 . 107 SER N N 121.2100 0.25 . 993 . 107 SER H H 8.9700 0.2 . 994 . 107 SER CA C 56.9400 0.25 . 995 . 107 SER HA H 4.9500 0.2 . 996 . 107 SER CB C 65.0200 0.25 . 997 . 107 SER HB3 H 4.2700 0.2 . 998 . 107 SER HB2 H 3.9100 0.2 . 999 . 107 SER C C 172.7700 0.25 . 1000 . 108 SER CA C 57.9900 0.25 . 1001 . 108 SER HA H 4.0200 0.2 . 1002 . 108 SER CB C 63.9900 0.25 . 1003 . 108 SER HB3 H 3.8300 0.2 . 1004 . 108 SER HB2 H 3.4900 0.2 . 1005 . 108 SER C C 174.8000 0.25 . 1006 . 109 LYS N N 124.7300 0.25 . 1007 . 109 LYS H H 7.8400 0.2 . 1008 . 109 LYS CA C 55.5450 0.25 . 1009 . 109 LYS HA H 4.3050 0.2 . 1010 . 109 LYS CB C 32.0900 0.25 . 1011 . 109 LYS HB3 H 1.7600 0.2 . 1012 . 109 LYS HB2 H 1.6500 0.2 . 1013 . 109 LYS CG C 24.9000 0.25 . 1014 . 109 LYS HG3 H 1.4500 0.2 . 1015 . 109 LYS HG2 H 1.3500 0.2 . 1016 . 109 LYS CD C 28.9000 0.25 . 1017 . 109 LYS HD3 H 1.7800 0.2 . 1018 . 109 LYS HD2 H 1.6700 0.2 . 1019 . 109 LYS CE C 42.1000 0.25 . 1020 . 109 LYS HE3 H 2.9800 0.2 . 1021 . 109 LYS C C 175.1400 0.25 . 1022 . 110 GLY N N 109.8900 0.25 . 1023 . 110 GLY H H 7.9100 0.2 . 1024 . 110 GLY CA C 44.8550 0.25 . 1025 . 110 GLY HA3 H 3.7850 0.2 . 1026 . 110 GLY HA2 H 3.3900 0.2 . 1027 . 110 GLY C C 173.2800 0.25 . 1028 . 111 TYR N N 122.1600 0.25 . 1029 . 111 TYR H H 8.3200 0.2 . 1030 . 111 TYR CA C 58.3200 0.25 . 1031 . 111 TYR HA H 4.0550 0.2 . 1032 . 111 TYR CB C 40.4000 0.25 . 1033 . 111 TYR HB3 H 2.0500 0.2 . 1034 . 111 TYR HB2 H 1.5200 0.2 . 1035 . 111 TYR CD1 C 132.4000 0.25 . 1036 . 111 TYR HD1 H 5.7000 0.2 . 1037 . 111 TYR CE1 C 118.4000 0.25 . 1038 . 111 TYR HE1 H 6.3600 0.2 . 1039 . 111 TYR C C 173.7700 0.25 . 1040 . 112 ASN N N 123.6100 0.25 . 1041 . 112 ASN H H 8.5200 0.2 . 1042 . 112 ASN CA C 54.5000 0.25 . 1043 . 112 ASN HA H 4.9600 0.2 . 1044 . 112 ASN CB C 40.8600 0.25 . 1045 . 112 ASN HB3 H 3.0400 0.2 . 1046 . 112 ASN HB2 H 2.8200 0.2 . 1047 . 112 ASN C C 175.0500 0.25 . 1048 . 113 LEU N N 129.7600 0.25 . 1049 . 113 LEU H H 8.6800 0.2 . 1050 . 113 LEU CA C 58.1900 0.25 . 1051 . 113 LEU HA H 4.3400 0.2 . 1052 . 113 LEU CB C 41.8900 0.25 . 1053 . 113 LEU HB3 H 1.6100 0.2 . 1054 . 113 LEU HB2 H 1.5300 0.2 . 1055 . 113 LEU CG C 26.8000 0.25 . 1056 . 113 LEU HG H 0.8800 0.2 . 1057 . 113 LEU CD1 C 26.8000 0.25 . 1058 . 113 LEU HD1 H 0.3600 0.2 . 1059 . 113 LEU CD2 C 22.0000 0.25 . 1060 . 113 LEU HD2 H -0.1800 0.2 . 1061 . 113 LEU C C 176.6500 0.25 . 1062 . 114 PHE N N 118.4600 0.25 . 1063 . 114 PHE H H 8.5600 0.2 . 1064 . 114 PHE CA C 60.5850 0.25 . 1065 . 114 PHE HA H 4.0150 0.2 . 1066 . 114 PHE CB C 37.5400 0.25 . 1067 . 114 PHE HB3 H 3.4400 0.2 . 1068 . 114 PHE HB2 H 3.3100 0.2 . 1069 . 114 PHE CD1 C 132.7000 0.25 . 1070 . 114 PHE HD1 H 7.3100 0.2 . 1071 . 114 PHE CE1 C 130.2000 0.25 . 1072 . 114 PHE HE1 H 6.8300 0.2 . 1073 . 114 PHE CZ C 128.7000 0.25 . 1074 . 114 PHE HZ H 6.5300 0.2 . 1075 . 114 PHE C C 174.9600 0.25 . 1076 . 115 LEU N N 120.3700 0.25 . 1077 . 115 LEU H H 8.1200 0.2 . 1078 . 115 LEU CA C 57.7850 0.25 . 1079 . 115 LEU HA H 3.1850 0.2 . 1080 . 115 LEU CB C 43.3500 0.25 . 1081 . 115 LEU HB3 H 1.7500 0.2 . 1082 . 115 LEU CG C 27.2000 0.25 . 1083 . 115 LEU HG H 1.7400 0.2 . 1084 . 115 LEU CD1 C 24.9000 0.25 . 1085 . 115 LEU HD1 H 0.7600 0.2 . 1086 . 115 LEU CD2 C 24.9000 0.25 . 1087 . 115 LEU HD2 H 0.9900 0.2 . 1088 . 115 LEU C C 178.8400 0.25 . 1089 . 116 VAL N N 115.5500 0.25 . 1090 . 116 VAL H H 7.8000 0.2 . 1091 . 116 VAL CA C 65.8600 0.25 . 1092 . 116 VAL HA H 4.1300 0.2 . 1093 . 116 VAL CB C 32.0400 0.25 . 1094 . 116 VAL HB H 2.2900 0.2 . 1095 . 116 VAL CG1 C 24.1000 0.25 . 1096 . 116 VAL HG1 H 1.2500 0.2 . 1097 . 116 VAL CG2 C 22.3000 0.25 . 1098 . 116 VAL HG2 H 1.1300 0.2 . 1099 . 116 VAL C C 178.5800 0.25 . 1100 . 117 ALA N N 122.0400 0.25 . 1101 . 117 ALA H H 9.3400 0.2 . 1102 . 117 ALA CA C 55.2650 0.25 . 1103 . 117 ALA HA H 3.5400 0.2 . 1104 . 117 ALA CB C 17.7530 0.25 . 1105 . 117 ALA HB H 1.0000 0.2 . 1106 . 117 ALA C C 176.7500 0.25 . 1107 . 118 ALA N N 118.9700 0.25 . 1108 . 118 ALA H H 8.6000 0.2 . 1109 . 118 ALA CA C 56.5900 0.25 . 1110 . 118 ALA HA H 3.8050 0.2 . 1111 . 118 ALA CB C 17.0830 0.25 . 1112 . 118 ALA HB H 1.0500 0.2 . 1113 . 118 ALA C C 179.8200 0.25 . 1114 . 119 HIS N N 117.8300 0.25 . 1115 . 119 HIS H H 7.5300 0.2 . 1116 . 119 HIS CA C 58.8550 0.25 . 1117 . 119 HIS HA H 4.6000 0.2 . 1118 . 119 HIS CB C 28.7400 0.25 . 1119 . 119 HIS HB3 H 4.1600 0.2 . 1120 . 119 HIS HB2 H 3.1200 0.2 . 1121 . 119 HIS CD2 C 128.2000 0.25 . 1122 . 119 HIS HD2 H 7.0900 0.2 . 1123 . 119 HIS C C 176.4800 0.25 . 1124 . 120 GLU N N 118.0700 0.25 . 1125 . 120 GLU H H 9.1900 0.2 . 1126 . 120 GLU CA C 58.8250 0.25 . 1127 . 120 GLU HA H 3.9900 0.2 . 1128 . 120 GLU CB C 28.0200 0.25 . 1129 . 120 GLU HB3 H 2.8600 0.2 . 1130 . 120 GLU HB2 H 1.8500 0.2 . 1131 . 120 GLU CG C 33.8000 0.25 . 1132 . 120 GLU HG3 H 1.4400 0.2 . 1133 . 120 GLU HG2 H 1.0400 0.2 . 1134 . 120 GLU C C 178.1400 0.25 . 1135 . 121 PHE N N 116.9000 0.25 . 1136 . 121 PHE H H 9.1200 0.2 . 1137 . 121 PHE CA C 55.7500 0.25 . 1138 . 121 PHE HA H 4.8600 0.2 . 1139 . 121 PHE CB C 36.0200 0.25 . 1140 . 121 PHE HB3 H 2.8100 0.2 . 1141 . 121 PHE HD1 H 6.2800 0.2 . 1142 . 121 PHE CE1 C 129.0000 0.25 . 1143 . 121 PHE HE1 H 6.3800 0.2 . 1144 . 121 PHE CZ C 127.7000 0.25 . 1145 . 121 PHE HZ H 6.1000 0.2 . 1146 . 121 PHE C C 177.6100 0.25 . 1147 . 122 GLY N N 108.9000 0.25 . 1148 . 122 GLY H H 7.8100 0.2 . 1149 . 122 GLY CA C 48.4900 0.25 . 1150 . 122 GLY HA3 H 4.1750 0.2 . 1151 . 122 GLY HA2 H 2.5100 0.2 . 1152 . 122 GLY C C 177.4800 0.25 . 1153 . 123 HIS N N 121.7100 0.25 . 1154 . 123 HIS H H 7.3200 0.2 . 1155 . 123 HIS CA C 57.6150 0.25 . 1156 . 123 HIS HA H 5.5450 0.2 . 1157 . 123 HIS CB C 28.1800 0.25 . 1158 . 123 HIS HB3 H 2.8300 0.2 . 1159 . 123 HIS HB2 H 4.1200 0.2 . 1160 . 123 HIS HD2 H 7.0900 0.2 . 1161 . 123 HIS CE1 C 138.0000 0.25 . 1162 . 123 HIS HE1 H 6.4700 0.2 . 1163 . 123 HIS C C 179.4800 0.25 . 1164 . 124 SER N N 116.9500 0.25 . 1165 . 124 SER H H 9.0000 0.2 . 1166 . 124 SER CA C 63.0900 0.25 . 1167 . 124 SER HA H 4.7200 0.2 . 1168 . 124 SER HB3 H 4.3200 0.2 . 1169 . 124 SER C C 175.4200 0.25 . 1170 . 125 LEU N N 114.7100 0.25 . 1171 . 125 LEU H H 7.6000 0.2 . 1172 . 125 LEU CA C 55.0850 0.25 . 1173 . 125 LEU HA H 4.6700 0.2 . 1174 . 125 LEU CB C 43.5600 0.25 . 1175 . 125 LEU HB3 H 1.7500 0.2 . 1176 . 125 LEU CG C 26.2000 0.25 . 1177 . 125 LEU HG H 2.2000 0.2 . 1178 . 125 LEU CD1 C 24.6000 0.25 . 1179 . 125 LEU HD1 H 0.5300 0.2 . 1180 . 125 LEU CD2 C 22.2000 0.25 . 1181 . 125 LEU HD2 H 0.9800 0.2 . 1182 . 125 LEU C C 178.0600 0.25 . 1183 . 126 GLY N N 108.1400 0.25 . 1184 . 126 GLY H H 8.4000 0.2 . 1185 . 126 GLY CA C 45.1750 0.25 . 1186 . 126 GLY HA3 H 5.0600 0.2 . 1187 . 126 GLY HA2 H 3.5800 0.2 . 1188 . 126 GLY C C 172.7800 0.25 . 1189 . 127 LEU N N 120.6600 0.25 . 1190 . 127 LEU H H 8.9000 0.2 . 1191 . 127 LEU CA C 54.5500 0.25 . 1192 . 127 LEU HA H 4.6850 0.2 . 1193 . 127 LEU CB C 41.9300 0.25 . 1194 . 127 LEU HB3 H 1.5700 0.2 . 1195 . 127 LEU CG C 26.8000 0.25 . 1196 . 127 LEU HG H 1.4500 0.2 . 1197 . 127 LEU CD1 C 26.9000 0.25 . 1198 . 127 LEU HD1 H 1.0500 0.2 . 1199 . 127 LEU CD2 C 22.3000 0.25 . 1200 . 127 LEU HD2 H 0.7200 0.2 . 1201 . 127 LEU C C 175.4000 0.25 . 1202 . 128 ASP N N 123.4000 0.25 . 1203 . 128 ASP H H 8.2300 0.2 . 1204 . 128 ASP CA C 50.3200 0.25 . 1205 . 128 ASP HA H 4.0350 0.2 . 1206 . 128 ASP CB C 42.5100 0.25 . 1207 . 128 ASP HB3 H 1.1148 0.2 . 1208 . 128 ASP HB2 H 2.0200 0.2 . 1209 . 128 ASP C C 174.9400 0.25 . 1210 . 129 HIS N N 117.0000 0.25 . 1211 . 129 HIS H H 9.0600 0.2 . 1212 . 129 HIS CA C 57.2950 0.25 . 1213 . 129 HIS HA H 5.0000 0.2 . 1214 . 129 HIS CB C 29.0600 0.25 . 1215 . 129 HIS HB3 H 2.8700 0.2 . 1216 . 129 HIS CE1 C 135.7000 0.25 . 1217 . 129 HIS HE1 H 7.2600 0.2 . 1218 . 129 HIS CD2 C 125.8000 0.25 . 1219 . 129 HIS HD2 H 7.1900 0.2 . 1220 . 129 HIS C C 175.5200 0.25 . 1221 . 130 SER N N 115.7100 0.25 . 1222 . 130 SER H H 6.9900 0.2 . 1223 . 130 SER CA C 56.4550 0.25 . 1224 . 130 SER HA H 4.2150 0.2 . 1225 . 130 SER CB C 64.3500 0.25 . 1226 . 130 SER HB3 H 3.4000 0.2 . 1227 . 130 SER HB2 H 4.5400 0.2 . 1228 . 130 SER C C 175.0500 0.25 . 1229 . 131 LYS N N 122.2600 0.25 . 1230 . 131 LYS H H 8.5100 0.2 . 1231 . 131 LYS CA C 56.1600 0.25 . 1232 . 131 LYS HA H 4.6250 0.2 . 1233 . 131 LYS CB C 32.5100 0.25 . 1234 . 131 LYS HB3 H 2.0900 0.2 . 1235 . 131 LYS HB2 H 1.7400 0.2 . 1236 . 131 LYS CG C 25.5000 0.25 . 1237 . 131 LYS HG3 H 1.5100 0.2 . 1238 . 131 LYS HG2 H 1.4300 0.2 . 1239 . 131 LYS CD C 28.8000 0.25 . 1240 . 131 LYS HD3 H 1.7400 0.2 . 1241 . 131 LYS CE C 42.2000 0.25 . 1242 . 131 LYS HE3 H 3.0300 0.2 . 1243 . 131 LYS C C 175.8000 0.25 . 1244 . 132 ASP N N 124.6400 0.25 . 1245 . 132 ASP H H 8.8600 0.2 . 1246 . 132 ASP CA C 51.3100 0.25 . 1247 . 132 ASP HA H 4.7500 0.2 . 1248 . 132 ASP CB C 41.3000 0.25 . 1249 . 132 ASP HB3 H 2.9900 0.2 . 1250 . 132 ASP HB2 H 2.4700 0.2 . 1251 . 132 ASP C C 174.1700 0.25 . 1252 . 133 PRO CA C 62.5800 0.25 . 1253 . 133 PRO HA H 4.1700 0.2 . 1254 . 133 PRO CB C 31.6800 0.25 . 1255 . 133 PRO HB3 H 2.3000 0.2 . 1256 . 133 PRO HB2 H 1.5500 0.2 . 1257 . 133 PRO CG C 27.1000 0.25 . 1258 . 133 PRO HG3 H 1.8100 0.2 . 1259 . 133 PRO HG2 H 1.6800 0.2 . 1260 . 133 PRO CD C 50.7000 0.25 . 1261 . 133 PRO HD3 H 4.1400 0.2 . 1262 . 133 PRO HD2 H 3.7000 0.2 . 1263 . 133 PRO C C 171.7800 0.25 . 1264 . 134 GLY N N 106.3400 0.25 . 1265 . 134 GLY H H 8.5200 0.2 . 1266 . 134 GLY CA C 44.5050 0.25 . 1267 . 134 GLY HA3 H 4.1750 0.2 . 1268 . 134 GLY HA2 H 3.5600 0.2 . 1269 . 134 GLY C C 173.4400 0.25 . 1270 . 135 ALA N N 124.7400 0.25 . 1271 . 135 ALA H H 8.0500 0.2 . 1272 . 135 ALA CA C 51.9900 0.25 . 1273 . 135 ALA HA H 4.6100 0.2 . 1274 . 135 ALA CB C 20.0400 0.25 . 1275 . 135 ALA HB H 1.9600 0.2 . 1276 . 135 ALA C C 177.2800 0.25 . 1277 . 136 LEU N N 132.7800 0.25 . 1278 . 136 LEU H H 12.1700 0.2 . 1279 . 136 LEU CA C 58.0500 0.25 . 1280 . 136 LEU HA H 4.5400 0.2 . 1281 . 136 LEU CB C 42.0800 0.25 . 1282 . 136 LEU HB3 H 1.9500 0.2 . 1283 . 136 LEU HB2 H 1.6300 0.2 . 1284 . 136 LEU CG C 27.8000 0.25 . 1285 . 136 LEU HG H 1.7900 0.2 . 1286 . 136 LEU CD1 C 22.7000 0.25 . 1287 . 136 LEU HD1 H 1.2800 0.2 . 1288 . 136 LEU CD2 C 27.4000 0.25 . 1289 . 136 LEU HD2 H 0.9000 0.2 . 1290 . 136 LEU C C 181.3200 0.25 . 1291 . 137 MET N N 114.3200 0.25 . 1292 . 137 MET H H 9.0900 0.2 . 1293 . 137 MET CA C 53.1950 0.25 . 1294 . 137 MET HA H 4.6350 0.2 . 1295 . 137 MET CB C 27.1600 0.25 . 1296 . 137 MET HB3 H 2.6100 0.2 . 1297 . 137 MET HB2 H 2.3100 0.2 . 1298 . 137 MET CG C 30.6000 0.25 . 1299 . 137 MET HG3 H 2.7400 0.2 . 1300 . 137 MET HG2 H 3.2900 0.2 . 1301 . 137 MET CE C 11.5000 0.25 . 1302 . 137 MET HE H 0.5600 0.2 . 1303 . 137 MET C C 177.6700 0.25 . 1304 . 138 PHE N N 128.0500 0.25 . 1305 . 138 PHE H H 8.0600 0.2 . 1306 . 138 PHE CA C 57.3400 0.25 . 1307 . 138 PHE HA H 4.8900 0.2 . 1308 . 138 PHE CB C 40.0700 0.25 . 1309 . 138 PHE HB3 H 3.1900 0.2 . 1310 . 138 PHE HB2 H 1.9900 0.2 . 1311 . 138 PHE CD1 C 133.2000 0.25 . 1312 . 138 PHE HD1 H 7.2200 0.2 . 1313 . 138 PHE CE1 C 130.1000 0.25 . 1314 . 138 PHE HE1 H 6.7600 0.2 . 1315 . 138 PHE CZ C 128.6000 0.25 . 1316 . 138 PHE HZ H 6.9200 0.2 . 1317 . 138 PHE C C 176.8800 0.25 . 1318 . 139 PRO CA C 63.2600 0.25 . 1319 . 139 PRO HA H 3.6500 0.2 . 1320 . 139 PRO CB C 27.5500 0.25 . 1321 . 139 PRO HB3 H 0.7800 0.2 . 1322 . 139 PRO HB2 H 0.2000 0.2 . 1323 . 139 PRO C C 172.6300 0.25 . 1324 . 140 ILE N N 118.8400 0.25 . 1325 . 140 ILE H H 7.5200 0.2 . 1326 . 140 ILE CA C 60.0550 0.25 . 1327 . 140 ILE HA H 4.6400 0.2 . 1328 . 140 ILE CB C 40.5900 0.25 . 1329 . 140 ILE HB H 2.0000 0.2 . 1330 . 140 ILE CG1 C 28.3000 0.25 . 1331 . 140 ILE HG13 H 1.5600 0.2 . 1332 . 140 ILE HG12 H 1.2400 0.2 . 1333 . 140 ILE CG2 C 17.5000 0.25 . 1334 . 140 ILE HG2 H 1.0700 0.2 . 1335 . 140 ILE CD1 C 12.3000 0.25 . 1336 . 140 ILE HD1 H 0.9800 0.2 . 1337 . 140 ILE C C 175.4200 0.25 . 1338 . 141 TYR N N 127.4200 0.25 . 1339 . 141 TYR H H 9.2100 0.2 . 1340 . 141 TYR CA C 59.0750 0.25 . 1341 . 141 TYR HA H 4.9150 0.2 . 1342 . 141 TYR CB C 38.7500 0.25 . 1343 . 141 TYR HB3 H 3.3000 0.2 . 1344 . 141 TYR HB2 H 2.8300 0.2 . 1345 . 141 TYR CD1 C 133.9000 0.25 . 1346 . 141 TYR HD1 H 7.1300 0.2 . 1347 . 141 TYR CE1 C 118.1000 0.25 . 1348 . 141 TYR HE1 H 7.0400 0.2 . 1349 . 141 TYR C C 174.4800 0.25 . 1350 . 142 THR N N 126.2100 0.25 . 1351 . 142 THR H H 8.8100 0.2 . 1352 . 142 THR CA C 61.2850 0.25 . 1353 . 142 THR HA H 4.2650 0.2 . 1354 . 142 THR CB C 70.8000 0.25 . 1355 . 142 THR HB H 4.0300 0.2 . 1356 . 142 THR CG2 C 21.2000 0.25 . 1357 . 142 THR HG2 H 1.1900 0.2 . 1358 . 142 THR C C 172.1400 0.25 . 1359 . 143 TYR N N 126.0100 0.25 . 1360 . 143 TYR H H 8.5100 0.2 . 1361 . 143 TYR CA C 58.7300 0.25 . 1362 . 143 TYR HA H 4.3100 0.2 . 1363 . 143 TYR CB C 39.3700 0.25 . 1364 . 143 TYR HB3 H 2.9400 0.2 . 1365 . 143 TYR CD1 C 133.0000 0.25 . 1366 . 143 TYR HD1 H 7.1800 0.2 . 1367 . 143 TYR CE1 C 118.2000 0.25 . 1368 . 143 TYR HE1 H 6.8300 0.2 . 1369 . 143 TYR C C 175.3200 0.25 . 1370 . 144 THR CA C 61.3000 0.25 . 1371 . 144 THR HA H 4.2400 0.2 . 1372 . 144 THR CB C 69.7300 0.25 . 1373 . 144 THR HB H 4.2100 0.2 . 1374 . 144 THR CG2 C 21.1000 0.25 . 1375 . 144 THR HG2 H 1.2400 0.2 . 1376 . 144 THR C C 174.3300 0.25 . 1377 . 145 GLY N N 110.1700 0.25 . 1378 . 145 GLY H H 7.2400 0.2 . 1379 . 145 GLY CA C 45.7850 0.25 . 1380 . 145 GLY HA3 H 3.9200 0.2 . 1381 . 145 GLY HA2 H 3.7700 0.2 . 1382 . 145 GLY C C 174.2100 0.25 . 1383 . 146 LYS N N 120.0900 0.25 . 1384 . 146 LYS H H 7.7000 0.2 . 1385 . 146 LYS CA C 56.4900 0.25 . 1386 . 146 LYS HA H 4.3200 0.2 . 1387 . 146 LYS CB C 33.0000 0.25 . 1388 . 146 LYS HB3 H 1.9100 0.2 . 1389 . 146 LYS HB2 H 1.7600 0.2 . 1390 . 146 LYS CG C 24.8000 0.25 . 1391 . 146 LYS HG3 H 1.4600 0.2 . 1392 . 146 LYS CD C 29.0000 0.25 . 1393 . 146 LYS HD3 H 1.7400 0.2 . 1394 . 146 LYS CE C 41.9000 0.25 . 1395 . 146 LYS HE3 H 3.0500 0.2 . 1396 . 146 LYS C C 176.8000 0.25 . 1397 . 149 PHE CA C 59.2600 0.25 . 1398 . 149 PHE HA H 4.3100 0.2 . 1399 . 149 PHE CB C 40.2600 0.25 . 1400 . 149 PHE HB3 H 3.1600 0.2 . 1401 . 149 PHE HB2 H 2.9400 0.2 . 1402 . 149 PHE CD1 C 132.0000 0.25 . 1403 . 149 PHE HD1 H 7.2500 0.2 . 1404 . 149 PHE CE1 C 131.0000 0.25 . 1405 . 149 PHE HE1 H 7.2200 0.2 . 1406 . 149 PHE C C 174.0400 0.25 . 1407 . 150 MET N N 126.8800 0.25 . 1408 . 150 MET H H 7.2500 0.2 . 1409 . 150 MET CA C 53.4400 0.25 . 1410 . 150 MET HA H 4.3700 0.2 . 1411 . 150 MET CB C 34.6700 0.25 . 1412 . 150 MET HB3 H 1.8500 0.2 . 1413 . 150 MET HB2 H 1.6900 0.2 . 1414 . 150 MET CG C 31.5000 0.25 . 1415 . 150 MET HG3 H 2.3700 0.2 . 1416 . 150 MET C C 173.8000 0.25 . 1417 . 151 LEU N N 127.2200 0.25 . 1418 . 151 LEU H H 8.4000 0.2 . 1419 . 151 LEU CA C 53.3200 0.25 . 1420 . 151 LEU HA H 4.1400 0.2 . 1421 . 151 LEU CB C 42.9400 0.25 . 1422 . 151 LEU HB3 H 1.6600 0.2 . 1423 . 151 LEU HB2 H 1.3400 0.2 . 1424 . 151 LEU CG C 25.0000 0.25 . 1425 . 151 LEU HG H 0.4200 0.2 . 1426 . 151 LEU CD1 C 25.8000 0.25 . 1427 . 151 LEU HD1 H 0.8200 0.2 . 1428 . 151 LEU CD2 C 25.8000 0.25 . 1429 . 151 LEU HD2 H 0.4800 0.2 . 1430 . 151 LEU C C 174.2200 0.25 . 1431 . 152 PRO CA C 62.8900 0.25 . 1432 . 152 PRO HA H 4.3600 0.2 . 1433 . 152 PRO CB C 33.1600 0.25 . 1434 . 152 PRO HB3 H 2.3200 0.2 . 1435 . 152 PRO HB2 H 1.9300 0.2 . 1436 . 152 PRO CG C 28.7000 0.25 . 1437 . 152 PRO CD C 51.0000 0.25 . 1438 . 152 PRO C C 176.2000 0.25 . 1439 . 153 ASP N N 120.6800 0.25 . 1440 . 153 ASP H H 8.4000 0.2 . 1441 . 153 ASP CA C 57.9500 0.25 . 1442 . 153 ASP HA H 4.3300 0.2 . 1443 . 153 ASP CB C 41.2400 0.25 . 1444 . 153 ASP HB3 H 2.6900 0.2 . 1445 . 153 ASP C C 178.0200 0.25 . 1446 . 154 ASP N N 116.7900 0.25 . 1447 . 154 ASP H H 8.9000 0.2 . 1448 . 154 ASP CA C 58.8150 0.25 . 1449 . 154 ASP HA H 4.4300 0.2 . 1450 . 154 ASP CB C 43.8300 0.25 . 1451 . 154 ASP HB3 H 3.0400 0.2 . 1452 . 154 ASP HB2 H 2.3700 0.2 . 1453 . 154 ASP C C 177.3100 0.25 . 1454 . 155 ASP N N 114.5400 0.25 . 1455 . 155 ASP H H 7.1500 0.2 . 1456 . 155 ASP CA C 56.5250 0.25 . 1457 . 155 ASP HA H 4.8100 0.2 . 1458 . 155 ASP CB C 43.6400 0.25 . 1459 . 155 ASP HB3 H 2.7900 0.2 . 1460 . 155 ASP HB2 H 2.9200 0.2 . 1461 . 155 ASP C C 178.6000 0.25 . 1462 . 156 VAL N N 119.3500 0.25 . 1463 . 156 VAL H H 7.9500 0.2 . 1464 . 156 VAL CA C 66.9550 0.25 . 1465 . 156 VAL HA H 3.5750 0.2 . 1466 . 156 VAL CB C 31.7800 0.25 . 1467 . 156 VAL HB H 2.3000 0.2 . 1468 . 156 VAL CG1 C 23.3000 0.25 . 1469 . 156 VAL HG1 H 1.1000 0.2 . 1470 . 156 VAL CG2 C 21.3000 0.25 . 1471 . 156 VAL HG2 H 0.9500 0.2 . 1472 . 156 VAL C C 178.1000 0.25 . 1473 . 157 GLN N N 117.0800 0.25 . 1474 . 157 GLN H H 8.7200 0.2 . 1475 . 157 GLN CA C 58.6150 0.25 . 1476 . 157 GLN HA H 3.9050 0.2 . 1477 . 157 GLN CB C 28.1200 0.25 . 1478 . 157 GLN HB3 H 2.2000 0.2 . 1479 . 157 GLN CG C 34.3000 0.25 . 1480 . 157 GLN HG3 H 2.7000 0.2 . 1481 . 157 GLN HG2 H 2.5200 0.2 . 1482 . 157 GLN C C 179.8700 0.25 . 1483 . 158 GLY N N 108.5400 0.25 . 1484 . 158 GLY H H 8.2800 0.2 . 1485 . 158 GLY CA C 46.6500 0.25 . 1486 . 158 GLY HA3 H 2.9200 0.2 . 1487 . 158 GLY HA2 H 1.9300 0.2 . 1488 . 158 GLY C C 176.3500 0.25 . 1489 . 159 ILE N N 125.3200 0.25 . 1490 . 159 ILE H H 9.0200 0.2 . 1491 . 159 ILE CA C 61.1850 0.25 . 1492 . 159 ILE HA H 4.4150 0.2 . 1493 . 159 ILE CB C 38.7000 0.25 . 1494 . 159 ILE HB H 2.3500 0.2 . 1495 . 159 ILE CG2 C 21.1000 0.25 . 1496 . 159 ILE HG2 H 1.6300 0.2 . 1497 . 159 ILE CG1 C 30.6000 0.25 . 1498 . 159 ILE HG13 H 2.0700 0.2 . 1499 . 159 ILE HG12 H 1.8300 0.2 . 1500 . 159 ILE CD1 C 15.4000 0.25 . 1501 . 159 ILE HD1 H 1.0400 0.2 . 1502 . 159 ILE C C 178.4500 0.25 . 1503 . 160 GLN N N 122.3600 0.25 . 1504 . 160 GLN H H 8.5700 0.2 . 1505 . 160 GLN CA C 58.4000 0.25 . 1506 . 160 GLN HA H 4.2300 0.2 . 1507 . 160 GLN CB C 26.8600 0.25 . 1508 . 160 GLN HB3 H 1.7800 0.2 . 1509 . 160 GLN HB2 H 2.1800 0.2 . 1510 . 160 GLN CG C 34.6000 0.25 . 1511 . 160 GLN C C 179.4300 0.25 . 1512 . 161 SER N N 119.6500 0.25 . 1513 . 161 SER H H 7.9500 0.2 . 1514 . 161 SER CA C 61.7650 0.25 . 1515 . 161 SER HA H 4.2700 0.2 . 1516 . 161 SER CB C 61.1000 0.25 . 1517 . 161 SER HB2 H 4.0100 0.2 . 1518 . 161 SER HB3 H 4.0100 0.2 . 1519 . 161 SER C C 175.0200 0.25 . 1520 . 162 LEU N N 120.8600 0.25 . 1521 . 162 LEU H H 6.7800 0.2 . 1522 . 162 LEU CA C 56.4850 0.25 . 1523 . 162 LEU HA H 4.2050 0.2 . 1524 . 162 LEU CB C 44.6100 0.25 . 1525 . 162 LEU HB3 H 1.8400 0.2 . 1526 . 162 LEU HB2 H 0.3900 0.2 . 1527 . 162 LEU CG C 25.3000 0.25 . 1528 . 162 LEU HG H 1.6000 0.2 . 1529 . 162 LEU CD1 C 23.2000 0.25 . 1530 . 162 LEU HD1 H 0.8000 0.2 . 1531 . 162 LEU CD2 C 25.9000 0.25 . 1532 . 162 LEU HD2 H 1.0000 0.2 . 1533 . 162 LEU C C 177.6800 0.25 . 1534 . 163 TYR N N 113.9700 0.25 . 1535 . 163 TYR H H 7.6500 0.2 . 1536 . 163 TYR CA C 58.8800 0.25 . 1537 . 163 TYR HA H 4.7900 0.2 . 1538 . 163 TYR CB C 41.1800 0.25 . 1539 . 163 TYR HB3 H 3.4900 0.2 . 1540 . 163 TYR HB2 H 2.7600 0.2 . 1541 . 163 TYR CD1 C 134.2000 0.25 . 1542 . 163 TYR HD1 H 7.3900 0.2 . 1543 . 163 TYR CE1 C 117.9000 0.25 . 1544 . 163 TYR HE1 H 7.4200 0.2 . 1545 . 163 TYR C C 175.7700 0.25 . 1546 . 164 GLY N N 109.5400 0.25 . 1547 . 164 GLY H H 8.3500 0.2 . 1548 . 164 GLY CA C 44.4800 0.25 . 1549 . 164 GLY HA3 H 4.3400 0.2 . 1550 . 164 GLY HA2 H 4.0800 0.2 . 1551 . 164 GLY C C 180.3400 0.25 . stop_ save_