data_6391 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 13C, and 15N chemical shift assignments for the catalytic domain of MMP-12 ; _BMRB_accession_number 6391 _BMRB_flat_file_name bmr6391.str _Entry_type original _Submission_date 2004-11-16 _Accession_date 2004-11-17 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details ; Chemical shift assignments, including side chains, for the catalytic domain of MMP-12. ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Markus Michelle A. . 2 Dwyer Brian . . 3 Wolfrom Scott . . 4 Li Jianchang . . 5 Li Wei . . 6 Malakian Karl . . 7 Wilhelm James . . 8 Tsao Desiree H.H. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 816 "13C chemical shifts" 663 "15N chemical shifts" 169 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2005-04-08 original author . stop_ _Original_release_date 2005-04-08 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; 1H, 13C, and 15N assignments of MMP-12, a key protease implicated in lung tissue remodeling ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Markus Michelle A. . 2 Dwyer Brian . . 3 Wolfrom Scott . . 4 Li Jianchang . . 5 Li Wei . . 6 Malakian Karl . . 7 Wilhelm James . . 8 Tsao Desiree H.H. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 31 _Journal_issue 3 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 260 _Page_last 260 _Year 2005 _Details . loop_ _Keyword 'chemical shift assignments' 'macrophage elastase' 'matrix metalloprotease' stop_ save_ ################################## # Molecular system description # ################################## save_assembly_mmp12 _Saveframe_category molecular_system _Mol_system_name mmp12 _Abbreviation_common mmp12 _Enzyme_commission_number 3.4.24.65 loop_ _Mol_system_component_name _Mol_label mmp12 $mmp12 inhibitor $DSV stop_ _System_molecular_weight 18342.6 _System_physical_state native _System_oligomer_state complex _System_paramagnetic no _System_thiol_state 'not present' loop_ _Biological_function 'degrades elastin' stop_ _Database_query_date . _Details 'Catalytic domain of mmp-12 with inhibitor.' save_ ######################## # Monomeric polymers # ######################## save_mmp12 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common mmp12 _Name_variant 'matrix metalloprotease 12' _Abbreviation_common 'matrix metalloprotease 12' _Molecular_mass 18342.6 _Mol_thiol_state 'not present' loop_ _Biological_function 'degrades elastin' stop_ _Details ; The residue's author sequence code corresponds to the original publication of the full-length protein sequence. ; ############################## # Polymer residue sequence # ############################## _Residue_count 165 _Mol_residue_sequence ; MFREMPGGPVWRKHYITYRI NNYTPDMNREDVDYAIRKAF QVWSNVTPLKFSKINTGMAD ILVVFARGAHGDFHAFDGKG GILAHAFGPGSGIGGDAHFD EDEFWTTHSGGTNLFLTAVH EIGHSLGLGHSSDPKAVMFP TYKYVDINTFRLSADDIRGI QSLYG ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 99 MET 2 100 PHE 3 101 ARG 4 102 GLU 5 103 MET 6 104 PRO 7 105 GLY 8 106 GLY 9 107 PRO 10 108 VAL 11 109 TRP 12 110 ARG 13 111 LYS 14 112 HIS 15 113 TYR 16 114 ILE 17 115 THR 18 116 TYR 19 117 ARG 20 118 ILE 21 119 ASN 22 120 ASN 23 121 TYR 24 122 THR 25 123 PRO 26 124 ASP 27 125 MET 28 126 ASN 29 127 ARG 30 128 GLU 31 129 ASP 32 130 VAL 33 131 ASP 34 132 TYR 35 133 ALA 36 134 ILE 37 135 ARG 38 136 LYS 39 137 ALA 40 138 PHE 41 139 GLN 42 140 VAL 43 141 TRP 44 142 SER 45 143 ASN 46 144 VAL 47 145 THR 48 146 PRO 49 147 LEU 50 148 LYS 51 149 PHE 52 150 SER 53 151 LYS 54 152 ILE 55 153 ASN 56 154 THR 57 155 GLY 58 156 MET 59 157 ALA 60 158 ASP 61 159 ILE 62 160 LEU 63 161 VAL 64 162 VAL 65 163 PHE 66 164 ALA 67 165 ARG 68 166 GLY 69 167 ALA 70 168 HIS 71 169 GLY 72 170 ASP 73 171 PHE 74 172 HIS 75 173 ALA 76 174 PHE 77 175 ASP 78 176 GLY 79 177 LYS 80 178 GLY 81 179 GLY 82 180 ILE 83 181 LEU 84 182 ALA 85 183 HIS 86 184 ALA 87 185 PHE 88 186 GLY 89 187 PRO 90 188 GLY 91 189 SER 92 190 GLY 93 191 ILE 94 192 GLY 95 193 GLY 96 194 ASP 97 195 ALA 98 196 HIS 99 197 PHE 100 198 ASP 101 199 GLU 102 200 ASP 103 201 GLU 104 202 PHE 105 203 TRP 106 204 THR 107 205 THR 108 206 HIS 109 207 SER 110 208 GLY 111 209 GLY 112 210 THR 113 211 ASN 114 212 LEU 115 213 PHE 116 214 LEU 117 215 THR 118 216 ALA 119 217 VAL 120 218 HIS 121 219 GLU 122 220 ILE 123 221 GLY 124 222 HIS 125 223 SER 126 224 LEU 127 225 GLY 128 226 LEU 129 227 GLY 130 228 HIS 131 229 SER 132 230 SER 133 231 ASP 134 232 PRO 135 233 LYS 136 234 ALA 137 235 VAL 138 236 MET 139 237 PHE 140 238 PRO 141 239 THR 142 240 TYR 143 241 LYS 144 242 TYR 145 243 VAL 146 244 ASP 147 245 ILE 148 246 ASN 149 247 THR 150 248 PHE 151 249 ARG 152 250 LEU 153 251 SER 154 252 ALA 155 253 ASP 156 254 ASP 157 255 ILE 158 256 ARG 159 257 GLY 160 258 ILE 161 259 GLN 162 260 SER 163 261 LEU 164 262 TYR 165 263 GLY stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 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 15578 FL_MMP12 95.76 366 98.73 98.73 8.63e-107 BMRB 6444 MMP12 95.76 159 99.37 99.37 1.10e-109 BMRB 7089 Metalloprotease 99.39 164 99.39 99.39 2.68e-115 BMRB 7415 CAT_DOMAIN 95.76 159 100.00 100.00 3.97e-111 PDB 1JIZ "Crystal Structure Analysis Of Human Macrophage Elastase Mmp- 12" 99.39 166 100.00 100.00 3.76e-116 PDB 1JK3 "Crystal Structure Of Human Mmp-12 (Macrophage Elastase) At True Atomic Resolution" 95.76 158 99.37 99.37 3.26e-110 PDB 1OS2 "Ternary Enzyme-Product-Inhibitor Complexes Of Human Mmp12" 95.76 165 99.37 99.37 9.30e-110 PDB 1OS9 "Binary Enzyme-Product Complexes Of Human Mmp12" 95.76 165 99.37 99.37 9.30e-110 PDB 1RMZ "Crystal Structure Of The Catalytic Domain Of Human Mmp12 Complexed With The Inhibitor Nngh At 1.3 A Resolution" 95.76 159 99.37 99.37 1.10e-109 PDB 1ROS "Crystal Structure Of Mmp-12 Complexed To 2-(1,3-Dioxo-1,3- Dihydro-2h-Isoindol-2-Yl)ethyl-4-(4-Ethoxy[1,1-Biphenyl]-4- Yl)-4-Ox" 95.76 163 100.00 100.00 4.60e-111 PDB 1UTT "Crystal Structure Of Mmp-12 Complexed To 2- (1,3-Dioxo-1,3-Dihydro-2h-Isoindol-2-Yl)ethyl-4- (4-Ethoxy[1,1-Biphenyl]-4-Yl)-4-Ox" 95.76 159 100.00 100.00 4.77e-111 PDB 1UTZ "Crystal Structure Of Mmp-12 Complexed To (2r)-3-({[4-[(Pyri Din-4-Yl)phenyl]-Thien-2-Yl}carboxamido)(Phenyl)propanoic Acid" 95.76 159 100.00 100.00 4.77e-111 PDB 1Y93 "Crystal Structure Of The Catalytic Domain Of Human Mmp12 Complexed With Acetohydroxamic Acid At Atomic Resolution" 95.76 159 99.37 99.37 1.10e-109 PDB 1YCM "Solution Structure Of Matrix Metalloproteinase 12 (Mmp12) In The Presence Of N-Isobutyl-N-[4- Methoxyphenylsulfonyl]glycyl Hydr" 95.76 159 99.37 99.37 1.10e-109 PDB 1Z3J "Solution Structure Of Mmp12 In The Presence Of N-Isobutyl-N- 4-Methoxyphenylsulfonyl]glycyl Hydroxamic Acid (Nngh)" 95.76 159 99.37 99.37 1.10e-109 PDB 2HU6 "Crystal Structure Of Human Mmp-12 In Complex With Acetohydroxamic Acid And A Bicyclic Inhibitor" 95.76 159 99.37 99.37 1.10e-109 PDB 2K2G "Solution Structure Of The Wild-Type Catalytic Domain Of Human Matrix Metalloproteinase 12 (Mmp-12) In Complex With A Tight-Bind" 100.00 165 100.00 100.00 3.32e-117 PDB 2K9C "Paramagnetic Shifts In Solid-State Nmr Of Proteins To Elicit Structural Information" 92.12 152 99.34 99.34 1.81e-104 PDB 2KRJ "High-Resolution Solid-State Nmr Structure Of A 17.6 Kda Prot" 92.12 152 99.34 99.34 1.81e-104 PDB 2MLR "Membrane Bilayer Complex With Matrix Metalloproteinase-12 At Its Alpha-face" 99.39 164 99.39 99.39 2.68e-115 PDB 2MLS "Membrane Bilayer Complex With Matrix Metalloproteinase-12 At Its Beta- Face" 99.39 164 99.39 99.39 2.68e-115 PDB 2OXU "Uninhibited Form Of Human Mmp-12" 95.76 159 99.37 99.37 1.10e-109 PDB 2OXW "Human Mmp-12 Complexed With The Peptide Iag" 95.76 159 99.37 99.37 1.10e-109 PDB 2OXZ "Human Mmp-12 In Complex With Two Peptides Pqg And Iag" 95.76 159 99.37 99.37 1.10e-109 PDB 2POJ "Nmr Solution Structure Of The Inhibitor-Free State Of Macrophage Metalloelastase (Mmp-12)" 99.39 164 99.39 99.39 2.68e-115 PDB 2W0D "Does A Fast Nuclear Magnetic Resonance Spectroscopy- And X-Ray Crystallography Hybrid Approach Provide Reliable Structural Info" 95.76 164 99.37 99.37 5.56e-110 PDB 2WO8 "Mmp12 Complex With A Beta Hydroxy Carboxylic Acid" 95.76 164 100.00 100.00 4.31e-111 PDB 2WO9 "Mmp12 Complex With A Beta Hydroxy Carboxylic Acid" 95.76 164 100.00 100.00 4.31e-111 PDB 2WOA "Mmp12 Complex With A Beta Hydroxy Carboxylic Acid" 95.76 164 100.00 100.00 4.31e-111 PDB 2Z2D "Solution Structure Of Human Macrophage Elastase (Mmp-12) Catalytic Domain Complexed With A Gamma-Keto Butanoic Acid Inhibitor" 99.39 164 100.00 100.00 3.51e-116 PDB 3BA0 "Crystal Structure Of Full-Length Human Mmp-12" 95.76 365 99.37 99.37 1.14e-107 PDB 3EHX "Crystal Structure Of The Catalytic Domain Of Human Mmp12 Complexed With The Inhibitor (R)-2-(Biphenyl-4- Ylsulfonamido)-4-Methy" 95.76 158 99.37 99.37 9.63e-110 PDB 3EHY "Crystal Structure Of The Catalytic Domain Of Human Mmp12 Complexed With The Inhibitor (R)-2-(4- Methoxyphenylsulfonamido)propan" 95.76 158 99.37 99.37 9.63e-110 PDB 3F15 "Crystal Structure Of The Catalytic Domain Of Human Mmp12 Complexed With The Inhibitor (S)-N-(2,3-Dihydroxypropyl)-4- Methoxy-N-" 95.76 158 99.37 99.37 9.63e-110 PDB 3F16 "Crystal Structure Of The Catalytic Domain Of Human Mmp12 Complexed With The Inhibitor (R)-N-(3-Hydroxy-1-Nitroso-1- Oxopropan-2" 95.76 158 99.37 99.37 9.63e-110 PDB 3F17 "Crystal Structure Of The Catalytic Domain Of Human Mmp12 Complexed With The Inhibitor N-(2-Nitroso-2-Oxoethyl) Biphenyl-4-Sulfo" 95.76 158 99.37 99.37 9.63e-110 PDB 3F18 "Crystal Structure Of The Catalytic Domain Of Human Mmp12 Complexed With The Inhibitor 4-Fluoro-N-(2-Hydroxyethyl)-N- (2-Nitroso" 95.76 158 99.37 99.37 9.63e-110 PDB 3F19 "Crystal Structure Of The Catalytic Domain Of Human Mmp12 Complexed With The Inhibitor 4-Fluoro-N-(2-Nitroso-2- Oxoethyl)benzene" 95.76 158 99.37 99.37 9.63e-110 PDB 3F1A "Crystal Structure Of The Catalytic Domain Of Human Mmp12 Complexed With The Inhibitor N-(2-Nitroso-2-Oxoethyl) Benzenesulfonami" 95.76 158 99.37 99.37 9.63e-110 PDB 3LIK "Human Mmp12 In Complex With Non-Zinc Chelating Inhibitor" 95.76 159 99.37 99.37 1.10e-109 PDB 3LIL "Human Mmp12 In Complex With Non-Zinc Chelating Inhibitor" 95.76 159 99.37 99.37 1.10e-109 PDB 3LIR "Human Mmp12 In Complex With Non-Zinc Chelating Inhibitor" 95.76 159 99.37 99.37 1.10e-109 PDB 3LJG "Human Mmp12 In Complex With Non-Zinc Chelating Inhibitor" 95.76 159 99.37 99.37 1.10e-109 PDB 3LK8 "Crystal Structure Of The Catalytic Domain Of Human Mmp12 Complexed With The Inhibitor Paramethoxy-Sulfonyl-Glycine Hydroxamate" 95.76 158 99.37 99.37 9.63e-110 PDB 3LKA "Catalytic Domain Of Human Mmp-12 Complexed With Hydroxamic Acid And Paramethoxy-Sulfonyl Amide" 95.76 158 99.37 99.37 9.63e-110 PDB 3N2U "Crystal Structure Of The Catalytic Domain Of Human Mmp12 Complexed With The Inhibitor N-Hydroxy-2-(4-Methoxy-N(2-(3,4,5-Trihydr" 95.76 158 99.37 99.37 9.63e-110 PDB 3N2V "Crystal Structure Of The Catalytic Domain Of Human Mmp12 Complexed With The Inhibitor N-Hydroxy-2-(N-Hydroxyethyl)biphenyl-4- Y" 95.76 158 99.37 99.37 9.63e-110 PDB 3NX7 "Crystal Structure Of The Catalytic Domain Of Human Mmp12 Complexed With The Inhibitor N-Hydroxy-2-(N-(2-Hydroxyethyl)4- Methoxy" 95.76 158 99.37 99.37 9.63e-110 PDB 3RTS "Human Mmp-12 Catalytic Domain In Complex WithN-Hydroxy-2-(2- Phenylethylsulfonamido)acetamide" 95.76 158 99.37 99.37 9.63e-110 PDB 3RTT "Human Mmp-12 Catalytic Domain In Complex With(R)-N-Hydroxy-1- (Phenethylsulfonyl)pyrrolidine-2-Carboxamide" 95.76 158 99.37 99.37 9.63e-110 PDB 3TS4 "Human Mmp12 In Complex With L-Glutamate Motif Inhibitor" 95.76 159 99.37 99.37 1.10e-109 PDB 3TSK "Human Mmp12 In Complex With L-Glutamate Motif Inhibitor" 95.76 159 99.37 99.37 1.10e-109 PDB 3UVC "Mmp12 In A Complex With The Dimeric Adduct: 5-(5-Phenylhydantoin)-5- Phenylhydantoin" 95.76 164 99.37 99.37 5.56e-110 PDB 4EFS "Human Mmp12 In Complex With L-Glutamate Motif Inhibitor" 95.76 159 99.37 99.37 1.10e-109 PDB 4GQL "Crystal Structure Of The Catalytic Domain Of Human Mmp12 In Complex With Selective Phosphinic Inhibitor Rxp470.1" 95.76 159 99.37 99.37 1.10e-109 PDB 4GR0 "Crystal Structure Of The Catalytic Domain Of Human Mmp12 In Complex With Selective Phosphinic Inhibitor Rxp470b" 95.76 159 99.37 99.37 1.10e-109 PDB 4GR3 "Crystal Structure Of The Catalytic Domain Of Human Mmp12 In Complex With Selective Phosphinic Inhibitor Rxp470a" 95.76 159 99.37 99.37 1.10e-109 PDB 4GR8 "Crystal Structure Of The Catalytic Domain Of Human Mmp12 In Complex With Selective Phosphinic Inhibitor Rxp470c" 92.12 152 99.34 99.34 1.59e-104 PDB 4GUY "Human Mmp12 Catalytic Domain In Complex WithN-Hydroxy-2-(2-(4- Methoxyphenyl)ethylsulfonamido)acetamide" 95.76 158 99.37 99.37 9.63e-110 PDB 4H30 "Crystal Structure Of The Catalytic Domain Of Mmp-12 In Complex With A Twin Inhibitor." 95.76 159 99.37 99.37 1.10e-109 PDB 4H49 "Crystal Structure Of The Catalytic Domain Of Mmp-12 In Complex With A Twin Inhibitor." 95.76 159 99.37 99.37 1.10e-109 PDB 4H76 "Crystal Structure Of The Catalytic Domain Of Human Mmp12 In Complex With A Broad Spectrum Hydroxamate Inhibitor" 95.76 159 99.37 99.37 1.10e-109 PDB 4H84 "Crystal Structure Of The Catalytic Domain Of Human Mmp12 In Complex With A Selective Carboxylate Based Inhibitor" 95.76 159 99.37 99.37 1.10e-109 PDB 4I03 "Human Mmp12 In Complex With A Peg-linked Bifunctional L-glutamate Motif Inhibitor" 95.76 159 98.73 98.73 8.30e-109 PDB 4IJO "Unraveling Hidden Allosteric Regulatory Sites In Structurally Homologues Metalloproteases" 95.76 158 99.37 99.37 9.63e-110 DBJ BAG36675 "unnamed protein product [Homo sapiens]" 99.39 470 100.00 100.00 5.53e-114 DBJ BAJ20684 "matrix metallopeptidase 12 [synthetic construct]" 99.39 470 100.00 100.00 5.53e-114 GB AAA58658 "metalloproteinase [Homo sapiens]" 99.39 470 100.00 100.00 6.10e-114 GB AAI12302 "Matrix metalloproteinase 12, preproprotein [Homo sapiens]" 99.39 470 100.00 100.00 5.53e-114 GB AAI43774 "Matrix metallopeptidase 12 (macrophage elastase) [Homo sapiens]" 99.39 470 100.00 100.00 5.65e-114 GB AAW29944 "matrix metalloproteinase 12 (macrophage elastase) [Homo sapiens]" 99.39 470 100.00 100.00 5.53e-114 GB ADR83017 "matrix metallopeptidase 12 (macrophage elastase) [synthetic construct]" 99.39 470 100.00 100.00 5.53e-114 REF NP_002417 "macrophage metalloelastase preproprotein [Homo sapiens]" 99.39 470 100.00 100.00 5.53e-114 REF XP_003828422 "PREDICTED: macrophage metalloelastase [Pan paniscus]" 99.39 470 100.00 100.00 4.91e-114 REF XP_004052087 "PREDICTED: macrophage metalloelastase [Gorilla gorilla gorilla]" 99.39 470 100.00 100.00 5.65e-114 REF XP_508724 "PREDICTED: macrophage metalloelastase [Pan troglodytes]" 99.39 470 100.00 100.00 4.91e-114 SP P39900 "RecName: Full=Macrophage metalloelastase; Short=MME; AltName: Full=Macrophage elastase; Short=ME; Short=hME; AltName: Full=Matr" 99.39 470 100.00 100.00 5.53e-114 stop_ save_ ############# # Ligands # ############# save_DSV _Saveframe_category ligand _Mol_type non-polymer _Name_common "DSV (N-(dibenzo[b,d]thiophen-3-ylsulfonyl)-L-valine)" _BMRB_code . _PDB_code DSV _Molecular_mass 363.451 _Mol_charge 0 _Mol_paramagnetic . _Mol_aromatic yes _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Fri Jun 17 11:42:47 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons C1 C1 C . 0 . ? C2 C2 C . 0 . ? C3 C3 C . 0 . ? C4 C4 C . 0 . ? C5 C5 C . 0 . ? C6 C6 C . 0 . ? S10 S10 S . 0 . ? C11 C11 C . 0 . ? C12 C12 C . 0 . ? CY1 CY1 C . 0 . ? CZ1 CZ1 C . 0 . ? CZ2 CZ2 C . 0 . ? CY2 CY2 C . 0 . ? S21 S21 S . 0 . ? O22 O22 O . 0 . ? O23 O23 O . 0 . ? N24 N24 N . 0 . ? C10 C10 C . 0 . ? CBC CBC C . 0 . ? CC1 CC1 C . 0 . ? CC2 CC2 C . 0 . ? C37 C37 C . 0 . ? O39 O39 O . 0 . ? O40 O40 O . 0 . ? H2 H2 H . 0 . ? H5 H5 H . 0 . ? H6 H6 H . 0 . ? HY1 HY1 H . 0 . ? HZ1 HZ1 H . 0 . ? HZ2 HZ2 H . 0 . ? HY2 HY2 H . 0 . ? HN24 HN24 H . 0 . ? HC1 HC1 H . 0 . ? HC1A HC1A H . 0 . ? HC1B HC1B H . 0 . ? HBC HBC H . 0 . ? HC2 HC2 H . 0 . ? HC2A HC2A H . 0 . ? HC2B HC2B H . 0 . ? H10 H10 H . 0 . ? HO40 HO40 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 DOUB C2 C1 ? ? SING C1 C6 ? ? SING C1 S21 ? ? SING C3 C2 ? ? SING C2 H2 ? ? SING S10 C3 ? ? DOUB C4 C3 ? ? SING C12 C4 ? ? SING C4 C5 ? ? SING H5 C5 ? ? DOUB C5 C6 ? ? SING C6 H6 ? ? SING C11 S10 ? ? DOUB CY1 C11 ? ? SING C11 C12 ? ? DOUB CY2 C12 ? ? SING CZ1 CY1 ? ? SING HY1 CY1 ? ? SING HZ1 CZ1 ? ? DOUB CZ1 CZ2 ? ? SING HZ2 CZ2 ? ? SING CZ2 CY2 ? ? SING CY2 HY2 ? ? SING N24 S21 ? ? DOUB O22 S21 ? ? DOUB S21 O23 ? ? SING HN24 N24 ? ? SING N24 C10 ? ? SING C37 C10 ? ? SING C10 CBC ? ? SING C10 H10 ? ? SING CC2 CBC ? ? SING CBC HBC ? ? SING CBC CC1 ? ? SING HC1 CC1 ? ? SING CC1 HC1A ? ? SING CC1 HC1B ? ? SING HC2 CC2 ? ? SING HC2B CC2 ? ? SING HC2A CC2 ? ? DOUB O39 C37 ? ? SING O40 C37 ? ? SING O40 HO40 ? ? 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 $mmp12 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 _Vendor_name $mmp12 'recombinant technology' 'E. coli' Escherichia coli BL21(DE3) . pET21a stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_15N_sample _Saveframe_category sample _Sample_type solution _Details '15N labelled MMP-12 (with bound inhibitor).' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $mmp12 0.2 mM [U-15N] $DSV 0.2 mM . stop_ save_ save_13C15N_sample _Saveframe_category sample _Sample_type solution _Details '13C 15N labelled MMP-12 (with bound inhibitor).' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $mmp12 0.7 mM '[U-13C; U-15N]' $DSV 0.7 mM . stop_ save_ save_13C15N_D2O_sample _Saveframe_category sample _Sample_type solution _Details '13C, 15N labelled MMP-12 (with bound inhibitor) in 2H2O.' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $mmp12 0.4 mM '[U-13C; U-15N]' $DSV 0.4 mM . D2O 100 % . stop_ save_ save_10percent_13C_sample _Saveframe_category sample _Sample_type solution _Details '10% 13C labelled MMP-12 with bound inhibitor.' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $mmp12 0.55 mM '[U-10% 13C]' $DSV 0.55 mM . stop_ save_ ############################ # Computer software used # ############################ save_peak_picking _Saveframe_category software _Name PIPP _Version 4.2.2 loop_ _Vendor _Address _Electronic_address 'Dan Garrett' . . stop_ loop_ _Task 'peak picking' stop_ _Details . save_ save_processing _Saveframe_category software _Name NMRPipe _Version 2.3 loop_ _Vendor _Address _Electronic_address 'Frank Delaglio' . . stop_ loop_ _Task 'processing spectra' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_600MHz_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details 'Triple resonance, single-axis gradient, cryoprobe for most experiments.' save_ ############################# # NMR applied experiments # ############################# save_HNCO_1 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label . save_ save_HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label . save_ save_HNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label . save_ save_CBCA(CO)NH_4 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _Sample_label . save_ save_HN(CA)CO_5 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CA)CO _Sample_label . save_ save_C(CO)NH_6 _Saveframe_category NMR_applied_experiment _Experiment_name C(CO)NH _Sample_label . save_ save_H(CCO)NH_7 _Saveframe_category NMR_applied_experiment _Experiment_name H(CCO)NH _Sample_label . save_ save_HBHA(CO)NH_8 _Saveframe_category NMR_applied_experiment _Experiment_name HBHA(CO)NH _Sample_label . save_ save_HCCH_TOCSY_9 _Saveframe_category NMR_applied_experiment _Experiment_name 'HCCH TOCSY' _Sample_label . save_ save_HACAHB_10 _Saveframe_category NMR_applied_experiment _Experiment_name HACAHB _Sample_label . save_ save_HNHB_11 _Saveframe_category NMR_applied_experiment _Experiment_name HNHB _Sample_label . save_ save_1H13C_HSQC_12 _Saveframe_category NMR_applied_experiment _Experiment_name '1H13C HSQC' _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CA)CO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name C(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name H(CCO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_8 _Saveframe_category NMR_applied_experiment _Experiment_name HBHA(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_9 _Saveframe_category NMR_applied_experiment _Experiment_name 'HCCH TOCSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_10 _Saveframe_category NMR_applied_experiment _Experiment_name HACAHB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_11 _Saveframe_category NMR_applied_experiment _Experiment_name HNHB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_12 _Saveframe_category NMR_applied_experiment _Experiment_name '1H13C HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_conditions _Saveframe_category sample_conditions _Details 'The same conditions have been used for all samples used in assignments.' loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.0 0.2 pH pressure 1 0.1 atm temperature 298 1.0 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_referencing _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 TSP C 13 'methyl carbon' ppm 0.0 external indirect . . . 0.25144954 $entry_citation $entry_citation TSP H 1 'methyl protons' ppm 0.0 external direct . . . 1.00000000 $entry_citation $entry_citation TSP N 15 nitrogen ppm 0.0 external indirect . . . 0.10132900 $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_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details 'Backbone and side chain chemical shifts for MMP-12.' loop_ _Software_label $peak_picking $processing stop_ loop_ _Experiment_label HNCO HNCA HNCACB CBCA(CO)NH HN(CA)CO C(CO)NH H(CCO)NH HBHA(CO)NH 'HCCH TOCSY' HACAHB HNHB '1H13C HSQC' stop_ _Sample_conditions_label $conditions _Chem_shift_reference_set_label $chemical_shift_referencing _Mol_system_component_name mmp12 _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 MET CA C 54.71 0.30 1 2 . 1 MET HA H 4.14 0.04 1 3 . 1 MET CB C 32.89 0.30 1 4 . 1 MET HB3 H 2.14 0.04 2 5 . 1 MET CG C 30.70 0.30 1 6 . 1 MET HG3 H 2.56 0.04 2 7 . 2 PHE C C 174.90 0.30 1 8 . 2 PHE CA C 57.81 0.30 1 9 . 2 PHE HA H 4.74 0.04 1 10 . 2 PHE CB C 39.84 0.30 1 11 . 2 PHE HB3 H 3.07 0.04 2 12 . 3 ARG N N 124.85 0.40 1 13 . 3 ARG H H 8.29 0.04 1 14 . 3 ARG C C 175.21 0.30 1 15 . 3 ARG CA C 55.72 0.30 1 16 . 3 ARG HA H 4.31 0.04 1 17 . 3 ARG CB C 31.21 0.30 1 18 . 3 ARG HB3 H 1.80 0.04 2 19 . 3 ARG HB2 H 1.70 0.04 2 20 . 3 ARG CG C 26.95 0.30 1 21 . 3 ARG HG3 H 1.60 0.04 2 22 . 3 ARG CD C 43.16 0.30 1 23 . 3 ARG HD2 H 3.19 0.04 2 24 . 4 GLU N N 123.44 0.40 1 25 . 4 GLU H H 8.37 0.04 1 26 . 4 GLU C C 175.96 0.30 1 27 . 4 GLU CA C 56.55 0.30 1 28 . 4 GLU HA H 4.17 0.04 1 29 . 4 GLU CB C 30.19 0.30 1 30 . 4 GLU HB3 H 1.92 0.04 2 31 . 4 GLU CG C 36.12 0.30 1 32 . 4 GLU HG3 H 2.37 0.04 2 33 . 5 MET N N 123.46 0.40 1 34 . 5 MET H H 8.35 0.04 1 35 . 5 MET C C 173.96 0.30 1 36 . 5 MET CA C 52.93 0.30 1 37 . 6 PRO C C 177.24 0.30 1 38 . 6 PRO CA C 63.33 0.30 1 39 . 6 PRO HA H 4.40 0.04 1 40 . 6 PRO CB C 32.06 0.30 1 41 . 6 PRO HB3 H 2.28 0.04 2 42 . 6 PRO HB2 H 1.92 0.04 2 43 . 6 PRO CG C 27.45 0.30 1 44 . 6 PRO HG3 H 2.00 0.04 2 45 . 6 PRO CD C 50.49 0.30 1 46 . 6 PRO HD3 H 3.79 0.04 2 47 . 6 PRO HD2 H 3.67 0.04 2 48 . 7 GLY N N 110.58 0.40 1 49 . 7 GLY H H 8.42 0.04 1 50 . 7 GLY C C 174.04 0.30 1 51 . 7 GLY CA C 45.12 0.30 1 52 . 7 GLY HA3 H 3.92 0.04 2 53 . 8 GLY N N 109.76 0.40 1 54 . 8 GLY H H 8.15 0.04 1 55 . 8 GLY C C 172.14 0.30 1 56 . 8 GLY CA C 43.90 0.30 1 57 . 8 GLY HA3 H 4.08 0.04 2 58 . 8 GLY HA2 H 3.96 0.04 2 59 . 9 PRO C C 175.61 0.30 1 60 . 9 PRO CA C 63.32 0.30 1 61 . 9 PRO HA H 4.39 0.04 1 62 . 9 PRO CB C 32.32 0.30 1 63 . 9 PRO HB3 H 2.12 0.04 2 64 . 9 PRO HB2 H 1.78 0.04 2 65 . 9 PRO CG C 27.23 0.30 1 66 . 9 PRO HG3 H 1.99 0.04 2 67 . 9 PRO CD C 49.59 0.30 1 68 . 9 PRO HD3 H 3.60 0.04 2 69 . 9 PRO HD2 H 3.55 0.04 2 70 . 10 VAL N N 111.64 0.40 1 71 . 10 VAL H H 7.27 0.04 1 72 . 10 VAL C C 176.37 0.30 1 73 . 10 VAL CA C 59.38 0.30 1 74 . 10 VAL HA H 4.48 0.04 1 75 . 10 VAL CB C 35.64 0.30 1 76 . 10 VAL HB H 2.20 0.04 1 77 . 10 VAL CG1 C 23.07 0.30 1 78 . 10 VAL HG1 H 0.77 0.04 2 79 . 10 VAL CG2 C 18.16 0.30 1 80 . 10 VAL HG2 H 0.70 0.04 2 81 . 11 TRP N N 123.81 0.40 1 82 . 11 TRP H H 8.21 0.04 1 83 . 11 TRP C C 176.88 0.30 1 84 . 11 TRP CA C 58.28 0.30 1 85 . 11 TRP HA H 4.52 0.04 1 86 . 11 TRP CB C 29.81 0.30 1 87 . 11 TRP HB3 H 3.49 0.04 2 88 . 11 TRP HB2 H 3.39 0.04 2 89 . 11 TRP CD1 C 126.95 0.30 1 90 . 11 TRP HD1 H 7.53 0.04 1 91 . 11 TRP CZ2 C 112.69 0.30 1 92 . 11 TRP HZ2 H 7.42 0.04 1 93 . 11 TRP NE1 N 128.27 0.40 1 94 . 11 TRP HE1 H 10.19 0.04 1 95 . 12 ARG N N 126.04 0.40 1 96 . 12 ARG H H 9.24 0.04 1 97 . 12 ARG C C 175.24 0.30 1 98 . 12 ARG CA C 55.44 0.30 1 99 . 12 ARG HA H 4.53 0.04 1 100 . 12 ARG CB C 28.68 0.30 1 101 . 12 ARG HB3 H 2.15 0.04 1 102 . 12 ARG HB2 H 1.85 0.04 1 103 . 12 ARG CG C 27.27 0.30 1 104 . 12 ARG HG3 H 1.84 0.04 2 105 . 12 ARG HG2 H 1.68 0.04 2 106 . 12 ARG CD C 43.01 0.30 1 107 . 12 ARG HD2 H 3.25 0.04 2 108 . 12 ARG NE N 86.18 0.40 1 109 . 12 ARG HE H 7.18 0.04 1 110 . 13 LYS N N 116.92 0.40 1 111 . 13 LYS H H 7.55 0.04 1 112 . 13 LYS C C 174.31 0.30 1 113 . 13 LYS CA C 54.41 0.30 1 114 . 13 LYS HA H 4.58 0.04 1 115 . 13 LYS CB C 34.08 0.30 1 116 . 13 LYS HB3 H 2.09 0.04 2 117 . 13 LYS HB2 H 2.01 0.04 2 118 . 13 LYS CG C 22.97 0.30 1 119 . 13 LYS HG3 H 1.52 0.04 2 120 . 13 LYS HG2 H 1.28 0.04 2 121 . 13 LYS CD C 30.08 0.30 1 122 . 13 LYS HD3 H 1.89 0.04 2 123 . 13 LYS HD2 H 1.81 0.04 2 124 . 13 LYS CE C 41.70 0.30 1 125 . 13 LYS HE2 H 3.07 0.04 2 126 . 14 HIS N N 115.14 0.40 1 127 . 14 HIS H H 8.48 0.04 1 128 . 14 HIS C C 172.75 0.30 1 129 . 14 HIS CA C 53.63 0.30 1 130 . 14 HIS HA H 4.88 0.04 1 131 . 14 HIS CB C 30.19 0.30 1 132 . 14 HIS HB3 H 3.46 0.04 1 133 . 14 HIS HB2 H 2.96 0.04 1 134 . 14 HIS CD2 C 116.81 0.30 1 135 . 14 HIS HD2 H 6.85 0.04 1 136 . 14 HIS CE1 C 137.24 0.30 1 137 . 14 HIS HE1 H 8.58 0.04 1 138 . 15 TYR N N 121.88 0.40 1 139 . 15 TYR H H 7.07 0.04 1 140 . 15 TYR C C 173.77 0.30 1 141 . 15 TYR CA C 56.69 0.30 1 142 . 15 TYR HA H 4.89 0.04 1 143 . 15 TYR CB C 38.32 0.30 1 144 . 15 TYR HB3 H 2.93 0.04 2 145 . 15 TYR HB2 H 2.79 0.04 2 146 . 15 TYR CD1 C 132.38 0.30 3 147 . 15 TYR HD1 H 7.02 0.04 3 148 . 15 TYR CE1 C 117.00 0.30 3 149 . 15 TYR HE1 H 6.73 0.04 3 150 . 16 ILE N N 129.78 0.40 1 151 . 16 ILE H H 8.32 0.04 1 152 . 16 ILE C C 175.22 0.30 1 153 . 16 ILE CA C 59.07 0.30 1 154 . 16 ILE HA H 4.22 0.04 1 155 . 16 ILE CB C 40.30 0.30 1 156 . 16 ILE HB H 1.36 0.04 1 157 . 16 ILE CG1 C 28.04 0.30 1 158 . 16 ILE HG13 H 0.81 0.04 2 159 . 16 ILE HG12 H 0.25 0.04 2 160 . 16 ILE CG2 C 16.83 0.30 1 161 . 16 ILE HG2 H 0.43 0.04 1 162 . 16 ILE CD1 C 12.67 0.30 1 163 . 16 ILE HD1 H 0.12 0.04 1 164 . 17 THR N N 118.65 0.40 1 165 . 17 THR H H 9.27 0.04 1 166 . 17 THR C C 174.52 0.30 1 167 . 17 THR CA C 58.65 0.30 1 168 . 17 THR HA H 5.39 0.04 1 169 . 17 THR CB C 72.59 0.30 1 170 . 17 THR HB H 4.15 0.04 1 171 . 17 THR CG2 C 21.99 0.30 1 172 . 17 THR HG2 H 1.15 0.04 1 173 . 18 TYR N N 118.69 0.40 1 174 . 18 TYR H H 8.67 0.04 1 175 . 18 TYR C C 171.77 0.30 1 176 . 18 TYR CA C 55.06 0.30 1 177 . 18 TYR HA H 5.89 0.04 1 178 . 18 TYR CB C 43.13 0.30 1 179 . 18 TYR HB3 H 2.38 0.04 1 180 . 18 TYR HB2 H 3.01 0.04 1 181 . 19 ARG N N 120.29 0.40 1 182 . 19 ARG H H 8.33 0.04 1 183 . 19 ARG C C 174.13 0.30 1 184 . 19 ARG CA C 54.65 0.30 1 185 . 19 ARG HA H 4.73 0.04 1 186 . 19 ARG CB C 35.34 0.30 1 187 . 19 ARG HB3 H 1.58 0.04 2 188 . 19 ARG CG C 27.39 0.30 1 189 . 19 ARG HG3 H 1.66 0.04 2 190 . 19 ARG CD C 43.51 0.30 1 191 . 19 ARG HD3 H 3.05 0.04 2 192 . 19 ARG HD2 H 2.92 0.04 2 193 . 19 ARG NE N 84.82 0.30 1 194 . 19 ARG HE H 7.28 0.04 1 195 . 20 ILE N N 128.45 0.40 1 196 . 20 ILE H H 9.20 0.04 1 197 . 20 ILE C C 175.09 0.30 1 198 . 20 ILE CA C 61.39 0.30 1 199 . 20 ILE HA H 4.41 0.04 1 200 . 20 ILE CB C 36.77 0.30 1 201 . 20 ILE HB H 1.81 0.04 1 202 . 20 ILE CG1 C 27.99 0.30 1 203 . 20 ILE HG13 H 1.83 0.04 2 204 . 20 ILE HG12 H 0.92 0.04 2 205 . 20 ILE CG2 C 16.76 0.30 1 206 . 20 ILE HG2 H 0.21 0.04 1 207 . 20 ILE CD1 C 13.52 0.30 1 208 . 20 ILE HD1 H 1.14 0.04 1 209 . 21 ASN N N 129.75 0.40 1 210 . 21 ASN H H 9.68 0.04 1 211 . 21 ASN C C 173.76 0.30 1 212 . 21 ASN CA C 56.26 0.30 1 213 . 21 ASN HA H 4.39 0.04 1 214 . 21 ASN CB C 41.55 0.30 1 215 . 21 ASN HB3 H 2.59 0.04 1 216 . 21 ASN HB2 H 3.15 0.04 1 217 . 21 ASN ND2 N 115.45 0.40 1 218 . 21 ASN HD21 H 7.53 0.04 2 219 . 21 ASN HD22 H 7.06 0.04 2 220 . 22 ASN N N 114.64 0.40 1 221 . 22 ASN H H 7.87 0.04 1 222 . 22 ASN C C 169.73 0.30 1 223 . 22 ASN CA C 51.97 0.30 1 224 . 22 ASN HA H 4.70 0.04 1 225 . 22 ASN CB C 38.38 0.30 1 226 . 22 ASN HB3 H 3.11 0.04 2 227 . 22 ASN HB2 H 3.02 0.04 2 228 . 22 ASN ND2 N 115.03 0.40 1 229 . 22 ASN HD21 H 7.88 0.04 2 230 . 22 ASN HD22 H 7.02 0.04 2 231 . 23 TYR N N 115.71 0.40 1 232 . 23 TYR H H 8.55 0.04 1 233 . 23 TYR C C 176.00 0.30 1 234 . 23 TYR CA C 58.74 0.30 1 235 . 23 TYR HA H 4.13 0.04 1 236 . 23 TYR CB C 40.75 0.30 1 237 . 23 TYR HB3 H 2.87 0.04 1 238 . 23 TYR HB2 H 2.65 0.04 1 239 . 23 TYR CD1 C 132.17 0.30 3 240 . 23 TYR HD1 H 6.99 0.04 3 241 . 23 TYR CE1 C 118.31 0.30 3 242 . 23 TYR HE1 H 6.91 0.04 3 243 . 24 THR CA C 58.63 0.30 1 244 . 24 THR HA H 4.38 0.04 1 245 . 24 THR CB C 66.92 0.30 1 246 . 24 THR HB H 3.46 0.04 1 247 . 24 THR CG2 C 18.83 0.30 1 248 . 24 THR HG2 H 0.53 0.04 1 249 . 25 PRO C C 177.08 0.30 1 250 . 25 PRO CA C 62.94 0.30 1 251 . 25 PRO HA H 4.69 0.04 1 252 . 25 PRO CB C 31.64 0.30 1 253 . 25 PRO HB3 H 2.28 0.04 2 254 . 25 PRO HB2 H 2.14 0.04 2 255 . 25 PRO CG C 26.69 0.30 1 256 . 25 PRO HG3 H 2.02 0.04 2 257 . 25 PRO CD C 50.30 0.30 1 258 . 25 PRO HD3 H 3.93 0.04 2 259 . 25 PRO HD2 H 3.59 0.04 2 260 . 26 ASP N N 123.15 0.40 1 261 . 26 ASP H H 8.88 0.04 1 262 . 26 ASP C C 175.73 0.30 1 263 . 26 ASP CA C 56.07 0.30 1 264 . 26 ASP HA H 4.15 0.04 1 265 . 26 ASP CB C 41.82 0.30 1 266 . 26 ASP HB3 H 2.82 0.04 1 267 . 26 ASP HB2 H 2.64 0.04 1 268 . 27 MET N N 114.47 0.40 1 269 . 27 MET H H 7.00 0.04 1 270 . 27 MET C C 174.72 0.30 1 271 . 27 MET CA C 53.34 0.30 1 272 . 27 MET HA H 4.65 0.04 1 273 . 27 MET CB C 39.13 0.30 1 274 . 27 MET HB3 H 2.30 0.04 1 275 . 27 MET HB2 H 1.48 0.04 1 276 . 27 MET CG C 31.97 0.30 1 277 . 27 MET HG3 H 2.42 0.04 2 278 . 27 MET HG2 H 2.16 0.04 2 279 . 27 MET CE C 16.55 0.30 1 280 . 27 MET HE H 1.84 0.04 1 281 . 28 ASN N N 120.02 0.40 1 282 . 28 ASN H H 8.96 0.04 1 283 . 28 ASN C C 177.21 0.30 1 284 . 28 ASN CA C 53.26 0.30 1 285 . 28 ASN HA H 4.67 0.04 1 286 . 28 ASN CB C 38.28 0.30 1 287 . 28 ASN HB3 H 2.97 0.04 2 288 . 28 ASN HB2 H 2.89 0.04 2 289 . 28 ASN ND2 N 115.12 0.40 1 290 . 28 ASN HD21 H 7.70 0.04 2 291 . 28 ASN HD22 H 7.00 0.04 2 292 . 29 ARG N N 127.16 0.40 1 293 . 29 ARG H H 8.98 0.04 1 294 . 29 ARG C C 177.95 0.30 1 295 . 29 ARG CA C 60.44 0.30 1 296 . 29 ARG HA H 3.82 0.04 1 297 . 29 ARG CB C 29.79 0.30 1 298 . 29 ARG HB3 H 1.42 0.04 1 299 . 29 ARG HB2 H 1.53 0.04 1 300 . 29 ARG CG C 26.49 0.30 1 301 . 29 ARG HG3 H 1.05 0.04 2 302 . 29 ARG CD C 43.10 0.30 1 303 . 29 ARG HD3 H 2.71 0.04 2 304 . 29 ARG HD2 H 2.64 0.04 2 305 . 29 ARG NE N 86.21 0.40 1 306 . 29 ARG HE H 6.90 0.04 1 307 . 30 GLU N N 117.53 0.40 1 308 . 30 GLU H H 9.12 0.04 1 309 . 30 GLU C C 179.29 0.30 1 310 . 30 GLU CA C 59.52 0.30 1 311 . 30 GLU HA H 4.15 0.04 1 312 . 30 GLU CB C 28.53 0.30 1 313 . 30 GLU HB3 H 2.05 0.04 2 314 . 30 GLU CG C 36.35 0.30 1 315 . 30 GLU HG3 H 2.38 0.04 2 316 . 30 GLU HG2 H 2.24 0.04 2 317 . 31 ASP N N 120.99 0.40 1 318 . 31 ASP H H 7.52 0.04 1 319 . 31 ASP C C 179.14 0.30 1 320 . 31 ASP CA C 57.11 0.30 1 321 . 31 ASP HA H 4.71 0.04 1 322 . 31 ASP CB C 40.73 0.30 1 323 . 31 ASP HB3 H 2.92 0.04 2 324 . 31 ASP HB2 H 2.71 0.04 2 325 . 32 VAL N N 125.17 0.40 1 326 . 32 VAL H H 7.80 0.04 1 327 . 32 VAL C C 177.13 0.30 1 328 . 32 VAL CA C 66.74 0.30 1 329 . 32 VAL HA H 3.60 0.04 1 330 . 32 VAL CB C 31.26 0.30 1 331 . 32 VAL HB H 2.66 0.04 1 332 . 32 VAL CG1 C 21.49 0.30 1 333 . 32 VAL HG1 H 1.00 0.04 2 334 . 32 VAL CG2 C 24.15 0.30 1 335 . 32 VAL HG2 H 1.06 0.04 2 336 . 33 ASP N N 119.63 0.40 1 337 . 33 ASP H H 8.43 0.04 1 338 . 33 ASP C C 179.56 0.30 1 339 . 33 ASP CA C 57.97 0.30 1 340 . 33 ASP HA H 4.42 0.04 1 341 . 33 ASP CB C 40.32 0.30 1 342 . 33 ASP HB3 H 2.75 0.04 1 343 . 33 ASP HB2 H 2.85 0.04 1 344 . 34 TYR N N 120.72 0.40 1 345 . 34 TYR H H 8.23 0.04 1 346 . 34 TYR C C 176.35 0.30 1 347 . 34 TYR CA C 61.60 0.30 1 348 . 34 TYR HA H 4.27 0.04 1 349 . 34 TYR CB C 38.69 0.30 1 350 . 34 TYR HB3 H 3.18 0.04 1 351 . 34 TYR HB2 H 3.39 0.04 1 352 . 34 TYR CD1 C 132.59 0.30 3 353 . 34 TYR HD1 H 7.23 0.04 3 354 . 34 TYR CE1 C 117.04 0.30 3 355 . 34 TYR HE1 H 6.79 0.04 3 356 . 35 ALA N N 122.49 0.40 1 357 . 35 ALA H H 8.13 0.04 1 358 . 35 ALA C C 179.26 0.30 1 359 . 35 ALA CA C 55.52 0.30 1 360 . 35 ALA HA H 4.01 0.04 1 361 . 35 ALA CB C 18.34 0.30 1 362 . 35 ALA HB H 1.57 0.04 1 363 . 36 ILE N N 115.16 0.40 1 364 . 36 ILE H H 8.08 0.04 1 365 . 36 ILE C C 177.14 0.30 1 366 . 36 ILE CA C 62.27 0.30 1 367 . 36 ILE HA H 3.57 0.04 1 368 . 36 ILE CB C 35.74 0.30 1 369 . 36 ILE HB H 2.20 0.04 1 370 . 36 ILE CG1 C 27.84 0.30 1 371 . 36 ILE HG13 H 1.68 0.04 2 372 . 36 ILE HG12 H 1.27 0.04 2 373 . 36 ILE CG2 C 18.82 0.30 1 374 . 36 ILE HG2 H 0.82 0.04 1 375 . 36 ILE CD1 C 8.95 0.30 1 376 . 36 ILE HD1 H 0.40 0.04 1 377 . 37 ARG N N 120.88 0.40 1 378 . 37 ARG H H 8.30 0.04 1 379 . 37 ARG C C 179.73 0.30 1 380 . 37 ARG CA C 60.15 0.30 1 381 . 37 ARG HA H 4.17 0.04 1 382 . 37 ARG CB C 30.13 0.30 1 383 . 37 ARG HB3 H 2.14 0.04 2 384 . 37 ARG HB2 H 2.04 0.04 2 385 . 37 ARG CG C 26.99 0.30 1 386 . 37 ARG HG3 H 1.85 0.04 2 387 . 37 ARG HG2 H 1.70 0.04 2 388 . 37 ARG CD C 43.76 0.30 1 389 . 37 ARG HD3 H 3.36 0.04 2 390 . 37 ARG NE N 86.61 0.40 1 391 . 37 ARG HE H 7.36 0.04 1 392 . 38 LYS N N 120.35 0.40 1 393 . 38 LYS H H 8.61 0.04 1 394 . 38 LYS C C 178.62 0.30 1 395 . 38 LYS CA C 58.35 0.30 1 396 . 38 LYS HA H 4.72 0.04 1 397 . 38 LYS CB C 31.27 0.30 1 398 . 38 LYS HB3 H 1.73 0.04 2 399 . 38 LYS CG C 24.66 0.30 1 400 . 38 LYS HG3 H 1.58 0.04 2 401 . 38 LYS HG2 H 1.35 0.04 2 402 . 38 LYS HD3 H 1.06 0.04 2 403 . 38 LYS HE3 H 3.10 0.04 2 404 . 39 ALA N N 124.56 0.40 1 405 . 39 ALA H H 8.04 0.04 1 406 . 39 ALA C C 178.57 0.30 1 407 . 39 ALA CA C 55.43 0.30 1 408 . 39 ALA HA H 3.96 0.04 1 409 . 39 ALA CB C 19.47 0.30 1 410 . 39 ALA HB H 1.15 0.04 1 411 . 40 PHE N N 115.20 0.40 1 412 . 40 PHE H H 7.72 0.04 1 413 . 40 PHE C C 178.63 0.30 1 414 . 40 PHE CA C 63.74 0.30 1 415 . 40 PHE HA H 3.77 0.04 1 416 . 40 PHE CB C 38.58 0.30 1 417 . 40 PHE HB3 H 2.71 0.04 2 418 . 40 PHE HB2 H 2.67 0.04 2 419 . 40 PHE CD1 C 131.06 0.30 3 420 . 40 PHE HD1 H 5.63 0.04 3 421 . 40 PHE CE1 C 129.89 0.30 3 422 . 40 PHE HE1 H 5.92 0.04 3 423 . 40 PHE CZ C 126.48 0.30 1 424 . 40 PHE HZ H 6.43 0.04 1 425 . 41 GLN N N 120.18 0.40 1 426 . 41 GLN H H 8.11 0.04 1 427 . 41 GLN C C 177.75 0.30 1 428 . 41 GLN CA C 58.29 0.30 1 429 . 41 GLN HA H 4.25 0.04 1 430 . 41 GLN CB C 28.50 0.30 1 431 . 41 GLN HB3 H 2.32 0.04 2 432 . 41 GLN CG C 34.12 0.30 1 433 . 41 GLN HG3 H 2.61 0.04 2 434 . 41 GLN HG2 H 2.51 0.04 2 435 . 41 GLN NE2 N 113.99 0.40 1 436 . 41 GLN HE21 H 7.65 0.04 2 437 . 41 GLN HE22 H 7.00 0.04 2 438 . 42 VAL N N 118.59 0.40 1 439 . 42 VAL H H 7.72 0.04 1 440 . 42 VAL C C 178.12 0.30 1 441 . 42 VAL CA C 66.06 0.30 1 442 . 42 VAL HA H 3.68 0.04 1 443 . 42 VAL CB C 30.97 0.30 1 444 . 42 VAL HB H 2.16 0.04 1 445 . 42 VAL CG1 C 21.86 0.30 1 446 . 42 VAL HG1 H 0.51 0.04 2 447 . 42 VAL CG2 C 22.95 0.30 1 448 . 42 VAL HG2 H 1.18 0.04 2 449 . 43 TRP N N 117.79 0.40 1 450 . 43 TRP H H 6.71 0.04 1 451 . 43 TRP C C 180.50 0.30 1 452 . 43 TRP CA C 58.28 0.30 1 453 . 43 TRP HA H 4.86 0.04 1 454 . 43 TRP CB C 30.41 0.30 1 455 . 43 TRP HB3 H 3.23 0.04 2 456 . 43 TRP HB2 H 3.11 0.04 2 457 . 43 TRP CD1 C 127.32 0.30 1 458 . 43 TRP HD1 H 6.85 0.04 1 459 . 43 TRP CE3 C 119.05 0.30 1 460 . 43 TRP HE3 H 7.39 0.04 1 461 . 43 TRP CZ3 C 120.87 0.30 1 462 . 43 TRP HZ3 H 6.76 0.04 1 463 . 43 TRP CH2 C 124.26 0.30 1 464 . 43 TRP HH2 H 6.68 0.04 1 465 . 43 TRP CZ2 C 114.36 0.30 1 466 . 43 TRP HZ2 H 7.05 0.04 1 467 . 43 TRP NE1 N 128.44 0.40 1 468 . 43 TRP HE1 H 9.80 0.04 1 469 . 44 SER N N 119.19 0.40 1 470 . 44 SER H H 9.07 0.04 1 471 . 44 SER C C 175.73 0.30 1 472 . 44 SER CA C 61.29 0.30 1 473 . 44 SER HA H 4.39 0.04 1 474 . 44 SER CB C 63.68 0.30 1 475 . 44 SER HB3 H 4.39 0.04 2 476 . 44 SER HB2 H 4.19 0.04 2 477 . 45 ASN N N 116.53 0.40 1 478 . 45 ASN H H 8.10 0.04 1 479 . 45 ASN C C 176.70 0.30 1 480 . 45 ASN CA C 54.86 0.30 1 481 . 45 ASN HA H 4.69 0.04 1 482 . 45 ASN CB C 39.04 0.30 1 483 . 45 ASN HB3 H 3.06 0.04 2 484 . 45 ASN HB2 H 2.98 0.04 2 485 . 45 ASN ND2 N 112.69 0.40 1 486 . 45 ASN HD21 H 7.64 0.04 2 487 . 45 ASN HD22 H 7.02 0.04 2 488 . 46 VAL N N 107.42 0.40 1 489 . 46 VAL H H 7.16 0.04 1 490 . 46 VAL C C 174.51 0.30 1 491 . 46 VAL CA C 60.21 0.30 1 492 . 46 VAL HA H 4.89 0.04 1 493 . 46 VAL CB C 32.51 0.30 1 494 . 46 VAL HB H 2.71 0.04 1 495 . 46 VAL CG1 C 21.63 0.30 1 496 . 46 VAL HG1 H 0.97 0.04 2 497 . 46 VAL CG2 C 19.04 0.30 1 498 . 46 VAL HG2 H 1.20 0.04 2 499 . 47 THR N N 111.69 0.40 1 500 . 47 THR H H 7.51 0.04 1 501 . 47 THR C C 173.13 0.30 1 502 . 47 THR CA C 59.89 0.30 1 503 . 47 THR HA H 5.26 0.04 1 504 . 47 THR CB C 72.28 0.30 1 505 . 47 THR HB H 4.04 0.04 1 506 . 47 THR CG2 C 24.27 0.30 1 507 . 47 THR HG2 H 1.49 0.04 1 508 . 48 PRO C C 176.01 0.30 1 509 . 48 PRO CA C 62.16 0.30 1 510 . 48 PRO HA H 4.79 0.04 1 511 . 48 PRO CB C 30.91 0.30 1 512 . 48 PRO HB3 H 2.15 0.04 2 513 . 48 PRO HB2 H 1.68 0.04 2 514 . 48 PRO CG C 26.97 0.30 1 515 . 48 PRO HG3 H 2.03 0.04 2 516 . 48 PRO HG2 H 1.40 0.04 2 517 . 48 PRO CD C 51.10 0.30 1 518 . 48 PRO HD3 H 3.76 0.04 2 519 . 48 PRO HD2 H 3.36 0.04 2 520 . 49 LEU N N 118.08 0.40 1 521 . 49 LEU H H 7.04 0.04 1 522 . 49 LEU C C 176.13 0.30 1 523 . 49 LEU CA C 54.59 0.30 1 524 . 49 LEU HA H 4.21 0.04 1 525 . 49 LEU CB C 42.96 0.30 1 526 . 49 LEU HB3 H 0.30 0.04 1 527 . 49 LEU HB2 H 1.35 0.04 1 528 . 49 LEU CG C 27.24 0.30 1 529 . 49 LEU HG H 1.02 0.04 1 530 . 49 LEU CD1 C 25.25 0.30 1 531 . 49 LEU HD1 H 0.24 0.04 2 532 . 49 LEU CD2 C 22.11 0.30 1 533 . 49 LEU HD2 H 0.48 0.04 2 534 . 50 LYS N N 123.74 0.40 1 535 . 50 LYS H H 8.16 0.04 1 536 . 50 LYS C C 173.64 0.30 1 537 . 50 LYS CA C 54.28 0.30 1 538 . 50 LYS HA H 4.32 0.04 1 539 . 50 LYS CB C 35.01 0.30 1 540 . 50 LYS HB3 H 1.67 0.04 1 541 . 50 LYS HB2 H 1.46 0.04 1 542 . 50 LYS CG C 24.70 0.30 1 543 . 50 LYS HG3 H 1.27 0.04 2 544 . 50 LYS CD C 28.57 0.30 1 545 . 50 LYS HD3 H 1.60 0.04 2 546 . 50 LYS CE C 41.99 0.30 1 547 . 50 LYS HE3 H 2.95 0.04 2 548 . 51 PHE N N 120.81 0.40 1 549 . 51 PHE H H 8.25 0.04 1 550 . 51 PHE C C 176.50 0.30 1 551 . 51 PHE CA C 55.46 0.30 1 552 . 51 PHE HA H 5.76 0.04 1 553 . 51 PHE CB C 41.54 0.30 1 554 . 51 PHE HB3 H 2.24 0.04 1 555 . 51 PHE HB2 H 2.58 0.04 1 556 . 51 PHE CD1 C 133.02 0.30 3 557 . 51 PHE HD1 H 6.94 0.04 3 558 . 52 SER N N 117.99 0.40 1 559 . 52 SER H H 8.09 0.04 1 560 . 52 SER C C 171.04 0.30 1 561 . 52 SER CA C 56.69 0.30 1 562 . 52 SER HA H 4.67 0.04 1 563 . 52 SER CB C 65.71 0.30 1 564 . 52 SER HB3 H 3.57 0.04 2 565 . 52 SER HB2 H 3.46 0.04 2 566 . 53 LYS N N 129.02 0.40 1 567 . 53 LYS H H 8.15 0.04 1 568 . 53 LYS C C 176.53 0.30 1 569 . 53 LYS CA C 55.26 0.30 1 570 . 53 LYS HA H 3.48 0.04 1 571 . 53 LYS CB C 33.22 0.30 1 572 . 53 LYS HB3 H 1.50 0.04 1 573 . 53 LYS HB2 H 1.18 0.04 1 574 . 53 LYS CG C 25.07 0.30 1 575 . 53 LYS HG3 H 0.98 0.04 2 576 . 53 LYS HG2 H 0.88 0.04 2 577 . 53 LYS CD C 29.56 0.30 1 578 . 53 LYS HD3 H 1.82 0.04 2 579 . 53 LYS HD2 H 1.60 0.04 2 580 . 53 LYS CE C 41.72 0.30 1 581 . 53 LYS HE3 H 3.11 0.04 2 582 . 54 ILE N N 124.83 0.40 1 583 . 54 ILE H H 8.77 0.04 1 584 . 54 ILE C C 175.40 0.30 1 585 . 54 ILE CA C 58.99 0.30 1 586 . 54 ILE HA H 4.68 0.04 1 587 . 54 ILE CB C 40.80 0.30 1 588 . 54 ILE HB H 1.97 0.04 1 589 . 54 ILE CG1 C 26.13 0.30 1 590 . 54 ILE HG13 H 1.19 0.04 2 591 . 54 ILE HG12 H 0.98 0.04 2 592 . 54 ILE CG2 C 17.24 0.30 1 593 . 54 ILE HG2 H 0.83 0.04 1 594 . 54 ILE CD1 C 12.78 0.30 1 595 . 54 ILE HD1 H 0.72 0.04 1 596 . 55 ASN N N 120.57 0.40 1 597 . 55 ASN H H 8.81 0.04 1 598 . 55 ASN C C 174.96 0.30 1 599 . 55 ASN CA C 53.55 0.30 1 600 . 55 ASN HA H 4.88 0.04 1 601 . 55 ASN CB C 40.00 0.30 1 602 . 55 ASN HB3 H 2.96 0.04 1 603 . 55 ASN HB2 H 2.77 0.04 1 604 . 55 ASN ND2 N 113.37 0.40 1 605 . 55 ASN HD21 H 7.47 0.04 2 606 . 55 ASN HD22 H 6.87 0.04 2 607 . 56 THR N N 112.88 0.40 1 608 . 56 THR H H 7.49 0.04 1 609 . 56 THR C C 172.60 0.30 1 610 . 56 THR CA C 60.25 0.30 1 611 . 56 THR HA H 4.46 0.04 1 612 . 56 THR CB C 70.74 0.30 1 613 . 56 THR HB H 4.14 0.04 1 614 . 56 THR CG2 C 20.90 0.30 1 615 . 56 THR HG2 H 1.16 0.04 1 616 . 57 GLY N N 111.12 0.40 1 617 . 57 GLY H H 8.29 0.04 1 618 . 57 GLY C C 173.27 0.30 1 619 . 57 GLY CA C 44.15 0.30 1 620 . 57 GLY HA3 H 4.22 0.04 2 621 . 57 GLY HA2 H 3.78 0.04 2 622 . 58 MET N N 120.33 0.40 1 623 . 58 MET H H 8.27 0.04 1 624 . 58 MET C C 174.89 0.30 1 625 . 58 MET CA C 55.11 0.30 1 626 . 58 MET HA H 4.50 0.04 1 627 . 58 MET CB C 31.89 0.30 1 628 . 58 MET HB3 H 2.59 0.04 2 629 . 58 MET HB2 H 2.01 0.04 2 630 . 58 MET CE C 16.38 0.30 1 631 . 58 MET HE H 2.14 0.04 1 632 . 59 ALA N N 128.28 0.40 1 633 . 59 ALA H H 7.93 0.04 1 634 . 59 ALA C C 176.35 0.30 1 635 . 59 ALA CA C 49.65 0.30 1 636 . 59 ALA HA H 4.58 0.04 1 637 . 59 ALA CB C 22.26 0.30 1 638 . 59 ALA HB H 1.01 0.04 1 639 . 60 ASP N N 122.64 0.40 1 640 . 60 ASP H H 8.09 0.04 1 641 . 60 ASP C C 176.87 0.30 1 642 . 60 ASP CA C 57.87 0.30 1 643 . 60 ASP HA H 4.58 0.04 1 644 . 60 ASP CB C 41.38 0.30 1 645 . 60 ASP HB3 H 2.42 0.04 1 646 . 60 ASP HB2 H 3.09 0.04 1 647 . 61 ILE N N 125.42 0.40 1 648 . 61 ILE H H 8.94 0.04 1 649 . 61 ILE C C 173.25 0.30 1 650 . 61 ILE CA C 61.65 0.30 1 651 . 61 ILE HA H 4.28 0.04 1 652 . 61 ILE CB C 39.97 0.30 1 653 . 61 ILE HB H 1.90 0.04 1 654 . 61 ILE CG1 C 26.47 0.30 1 655 . 61 ILE HG13 H 1.53 0.04 2 656 . 61 ILE HG12 H 1.34 0.04 2 657 . 61 ILE CG2 C 14.37 0.30 1 658 . 61 ILE HG2 H 1.15 0.04 1 659 . 61 ILE CD1 C 14.27 0.30 1 660 . 61 ILE HD1 H 0.94 0.04 1 661 . 62 LEU N N 131.27 0.40 1 662 . 62 LEU H H 7.58 0.04 1 663 . 62 LEU C C 175.59 0.30 1 664 . 62 LEU CA C 53.45 0.30 1 665 . 62 LEU HA H 5.07 0.04 1 666 . 62 LEU CB C 43.40 0.30 1 667 . 62 LEU HB3 H 1.52 0.04 1 668 . 62 LEU HB2 H 1.72 0.04 1 669 . 62 LEU CG C 27.35 0.30 1 670 . 62 LEU HG H 1.65 0.04 1 671 . 62 LEU CD1 C 23.98 0.30 1 672 . 62 LEU HD1 H 1.04 0.04 2 673 . 62 LEU CD2 C 25.05 0.30 1 674 . 62 LEU HD2 H 0.93 0.04 2 675 . 63 VAL N N 126.70 0.40 1 676 . 63 VAL H H 8.80 0.04 1 677 . 63 VAL C C 175.15 0.30 1 678 . 63 VAL CA C 61.74 0.30 1 679 . 63 VAL HA H 5.27 0.04 1 680 . 63 VAL CB C 32.85 0.30 1 681 . 63 VAL HB H 2.24 0.04 1 682 . 63 VAL CG1 C 20.65 0.30 1 683 . 63 VAL HG1 H 0.77 0.04 2 684 . 63 VAL CG2 C 20.19 0.30 1 685 . 63 VAL HG2 H 1.03 0.04 2 686 . 64 VAL N N 127.81 0.40 1 687 . 64 VAL H H 8.75 0.04 1 688 . 64 VAL C C 174.75 0.30 1 689 . 64 VAL CA C 60.82 0.30 1 690 . 64 VAL HA H 4.63 0.04 1 691 . 64 VAL CB C 37.26 0.30 1 692 . 64 VAL HB H 1.85 0.04 1 693 . 64 VAL CG1 C 20.87 0.30 1 694 . 64 VAL HG1 H 0.83 0.04 2 695 . 64 VAL CG2 C 21.16 0.30 1 696 . 64 VAL HG2 H 0.97 0.04 2 697 . 65 PHE N N 127.24 0.40 1 698 . 65 PHE H H 8.63 0.04 1 699 . 65 PHE C C 176.09 0.30 1 700 . 65 PHE CA C 57.00 0.30 1 701 . 65 PHE HA H 5.45 0.04 1 702 . 65 PHE CB C 40.69 0.30 1 703 . 65 PHE HB3 H 3.12 0.04 1 704 . 65 PHE HB2 H 2.83 0.04 1 705 . 65 PHE CD1 C 133.35 0.30 3 706 . 65 PHE HD1 H 7.00 0.04 3 707 . 65 PHE CE1 C 129.28 0.30 3 708 . 65 PHE HE1 H 6.12 0.04 3 709 . 65 PHE CZ C 128.30 0.30 1 710 . 65 PHE HZ H 6.30 0.04 1 711 . 66 ALA N N 127.31 0.40 1 712 . 66 ALA H H 9.17 0.04 1 713 . 66 ALA C C 174.79 0.30 1 714 . 66 ALA CA C 51.10 0.30 1 715 . 66 ALA HA H 4.89 0.04 1 716 . 66 ALA CB C 22.78 0.30 1 717 . 66 ALA HB H 1.01 0.04 1 718 . 67 ARG N N 119.44 0.40 1 719 . 67 ARG H H 8.81 0.04 1 720 . 67 ARG C C 175.82 0.30 1 721 . 67 ARG CA C 53.87 0.30 1 722 . 67 ARG HA H 5.31 0.04 1 723 . 67 ARG CB C 33.87 0.30 1 724 . 67 ARG HB3 H 1.95 0.04 2 725 . 67 ARG HB2 H 1.73 0.04 2 726 . 67 ARG CG C 26.68 0.30 1 727 . 67 ARG HG3 H 1.64 0.04 2 728 . 67 ARG CD C 43.05 0.30 1 729 . 67 ARG HD3 H 3.30 0.04 2 730 . 67 ARG NE N 85.72 0.40 1 731 . 67 ARG HE H 8.02 0.04 1 732 . 68 GLY N N 109.43 0.40 1 733 . 68 GLY H H 9.54 0.04 1 734 . 68 GLY C C 175.77 0.30 1 735 . 68 GLY CA C 46.50 0.30 1 736 . 68 GLY HA3 H 3.98 0.04 2 737 . 68 GLY HA2 H 3.84 0.04 2 738 . 69 ALA N N 135.32 0.40 1 739 . 69 ALA H H 9.21 0.04 1 740 . 69 ALA C C 176.63 0.30 1 741 . 69 ALA CA C 53.18 0.30 1 742 . 69 ALA HA H 4.37 0.04 1 743 . 69 ALA CB C 17.94 0.30 1 744 . 69 ALA HB H 1.55 0.04 1 745 . 70 HIS CA C 54.86 0.30 1 746 . 70 HIS HA H 5.08 0.04 1 747 . 70 HIS CB C 28.02 0.30 1 748 . 70 HIS HB3 H 3.40 0.04 2 749 . 70 HIS HB2 H 2.70 0.04 2 750 . 70 HIS CD2 C 126.38 0.30 1 751 . 70 HIS HD2 H 6.35 0.04 1 752 . 70 HIS CE1 C 139.99 0.30 1 753 . 70 HIS HE1 H 6.92 0.04 1 754 . 71 GLY CA C 44.31 0.30 1 755 . 71 GLY HA3 H 4.39 0.04 2 756 . 71 GLY HA2 H 3.62 0.04 2 757 . 72 ASP CA C 51.69 0.30 1 758 . 72 ASP HA H 4.59 0.04 1 759 . 72 ASP CB C 40.83 0.30 1 760 . 72 ASP HB3 H 3.23 0.04 2 761 . 72 ASP HB2 H 2.65 0.04 2 762 . 73 PHE C C 174.40 0.30 1 763 . 74 HIS N N 121.43 0.40 1 764 . 74 HIS H H 7.57 0.04 1 765 . 74 HIS C C 172.33 0.30 1 766 . 74 HIS CA C 53.66 0.30 1 767 . 74 HIS HA H 3.95 0.04 1 768 . 74 HIS CB C 29.69 0.30 1 769 . 74 HIS HB3 H 2.25 0.04 2 770 . 75 ALA N N 124.72 0.40 1 771 . 75 ALA H H 8.05 0.04 1 772 . 75 ALA C C 180.32 0.30 1 773 . 75 ALA CA C 53.49 0.30 1 774 . 75 ALA HA H 4.23 0.04 1 775 . 75 ALA CB C 18.28 0.30 1 776 . 75 ALA HB H 1.35 0.04 1 777 . 76 PHE N N 120.82 0.40 1 778 . 76 PHE H H 7.95 0.04 1 779 . 76 PHE C C 176.23 0.30 1 780 . 76 PHE CA C 57.07 0.30 1 781 . 76 PHE HA H 5.00 0.04 1 782 . 76 PHE CB C 38.33 0.30 1 783 . 76 PHE HB3 H 3.98 0.04 1 784 . 76 PHE HB2 H 3.14 0.04 1 785 . 77 ASP N N 117.64 0.40 1 786 . 77 ASP H H 8.33 0.04 1 787 . 77 ASP C C 177.25 0.30 1 788 . 77 ASP CA C 53.77 0.30 1 789 . 77 ASP HA H 4.71 0.04 1 790 . 77 ASP CB C 41.61 0.30 1 791 . 77 ASP HB3 H 3.22 0.04 2 792 . 77 ASP HB2 H 2.64 0.04 2 793 . 78 GLY N N 111.27 0.40 1 794 . 78 GLY H H 8.90 0.04 1 795 . 78 GLY C C 173.26 0.30 1 796 . 78 GLY CA C 43.75 0.30 1 797 . 78 GLY HA3 H 4.49 0.04 2 798 . 78 GLY HA2 H 4.32 0.04 2 799 . 79 LYS N N 125.67 0.40 1 800 . 79 LYS H H 8.78 0.04 1 801 . 79 LYS C C 177.62 0.30 1 802 . 79 LYS CA C 58.48 0.30 1 803 . 79 LYS HA H 3.63 0.04 1 804 . 79 LYS CB C 32.04 0.30 1 805 . 79 LYS HB3 H 1.69 0.04 2 806 . 79 LYS HB2 H 1.64 0.04 2 807 . 79 LYS CG C 24.82 0.30 1 808 . 79 LYS HG3 H 1.36 0.04 2 809 . 79 LYS CD C 29.06 0.30 1 810 . 79 LYS HD3 H 1.68 0.04 2 811 . 79 LYS CE C 41.79 0.30 1 812 . 79 LYS HE3 H 2.95 0.04 2 813 . 80 GLY N N 122.21 0.40 1 814 . 80 GLY H H 10.71 0.04 1 815 . 80 GLY C C 174.24 0.30 1 816 . 80 GLY CA C 42.92 0.30 1 817 . 80 GLY HA3 H 4.24 0.04 2 818 . 80 GLY HA2 H 3.52 0.04 2 819 . 81 GLY N N 111.53 0.40 1 820 . 81 GLY H H 8.47 0.04 1 821 . 81 GLY C C 174.99 0.30 1 822 . 81 GLY CA C 46.54 0.30 1 823 . 81 GLY HA3 H 4.11 0.04 2 824 . 81 GLY HA2 H 3.46 0.04 2 825 . 82 ILE N N 132.23 0.40 1 826 . 82 ILE H H 10.83 0.04 1 827 . 82 ILE C C 176.39 0.30 1 828 . 82 ILE CA C 62.58 0.30 1 829 . 82 ILE HA H 3.95 0.04 1 830 . 82 ILE CB C 38.03 0.30 1 831 . 82 ILE HB H 2.23 0.04 1 832 . 82 ILE CG1 C 28.35 0.30 1 833 . 82 ILE HG13 H 1.82 0.04 2 834 . 82 ILE HG12 H 1.56 0.04 2 835 . 82 ILE CG2 C 18.74 0.30 1 836 . 82 ILE HG2 H 1.43 0.04 1 837 . 82 ILE CD1 C 12.32 0.30 1 838 . 82 ILE HD1 H 1.10 0.04 1 839 . 83 LEU N N 129.43 0.40 1 840 . 83 LEU H H 8.53 0.04 1 841 . 83 LEU C C 175.87 0.30 1 842 . 83 LEU CA C 55.58 0.30 1 843 . 83 LEU HA H 4.60 0.04 1 844 . 83 LEU CB C 42.01 0.30 1 845 . 83 LEU HB3 H 1.75 0.04 1 846 . 83 LEU HB2 H 2.01 0.04 1 847 . 83 LEU CG C 26.39 0.30 1 848 . 83 LEU HG H 1.75 0.04 1 849 . 83 LEU CD1 C 24.66 0.30 1 850 . 83 LEU HD1 H 0.31 0.04 2 851 . 83 LEU CD2 C 20.87 0.30 1 852 . 83 LEU HD2 H 0.39 0.04 2 853 . 84 ALA N N 116.20 0.40 1 854 . 84 ALA H H 7.75 0.04 1 855 . 84 ALA C C 174.63 0.30 1 856 . 84 ALA CA C 51.60 0.30 1 857 . 84 ALA HA H 4.69 0.04 1 858 . 84 ALA CB C 22.38 0.30 1 859 . 84 ALA HB H 1.27 0.04 1 860 . 85 HIS N N 114.21 0.40 1 861 . 85 HIS H H 9.24 0.04 1 862 . 85 HIS C C 171.64 0.30 1 863 . 85 HIS CA C 54.21 0.30 1 864 . 85 HIS HA H 4.71 0.04 1 865 . 85 HIS CB C 30.81 0.30 1 866 . 85 HIS HB3 H 3.26 0.04 2 867 . 85 HIS HB2 H 2.91 0.04 2 868 . 85 HIS CD2 C 124.26 0.30 1 869 . 85 HIS HD2 H 6.55 0.04 1 870 . 86 ALA N N 123.74 0.40 1 871 . 86 ALA H H 8.64 0.04 1 872 . 86 ALA C C 175.72 0.30 1 873 . 86 ALA CA C 50.60 0.30 1 874 . 86 ALA HA H 5.09 0.04 1 875 . 86 ALA CB C 23.85 0.30 1 876 . 86 ALA HB H 1.28 0.04 1 877 . 87 PHE N N 121.50 0.40 1 878 . 87 PHE H H 8.07 0.04 1 879 . 87 PHE C C 175.67 0.30 1 880 . 87 PHE CA C 56.50 0.30 1 881 . 87 PHE HA H 4.29 0.04 1 882 . 87 PHE CB C 41.32 0.30 1 883 . 87 PHE HB3 H 3.04 0.04 2 884 . 87 PHE CD1 C 130.75 0.30 3 885 . 87 PHE HD1 H 7.18 0.04 3 886 . 87 PHE CE1 C 121.49 0.30 3 887 . 87 PHE HE1 H 7.87 0.04 3 888 . 87 PHE CZ C 124.63 0.30 1 889 . 87 PHE HZ H 7.50 0.04 1 890 . 88 GLY N N 106.47 0.40 1 891 . 88 GLY H H 8.25 0.04 1 892 . 88 GLY C C 171.74 0.30 1 893 . 88 GLY CA C 44.54 0.30 1 894 . 88 GLY HA3 H 4.13 0.04 2 895 . 88 GLY HA2 H 3.97 0.04 2 896 . 89 PRO C C 174.83 0.30 1 897 . 89 PRO CA C 64.07 0.30 1 898 . 89 PRO HA H 2.98 0.04 1 899 . 89 PRO CB C 31.68 0.30 1 900 . 89 PRO HB3 H 1.92 0.04 2 901 . 89 PRO HB2 H 1.82 0.04 2 902 . 89 PRO CG C 27.10 0.30 1 903 . 90 GLY N N 107.86 0.40 1 904 . 90 GLY H H 5.66 0.04 1 905 . 90 GLY C C 171.75 0.30 1 906 . 90 GLY CA C 44.12 0.30 1 907 . 90 GLY HA3 H 4.17 0.04 2 908 . 90 GLY HA2 H 3.65 0.04 2 909 . 91 SER N N 115.82 0.40 1 910 . 91 SER H H 8.40 0.04 1 911 . 91 SER C C 175.96 0.30 1 912 . 91 SER CA C 58.69 0.30 1 913 . 91 SER HA H 4.50 0.04 1 914 . 91 SER CB C 64.47 0.30 1 915 . 91 SER HB3 H 4.01 0.04 2 916 . 92 GLY N N 113.40 0.40 1 917 . 92 GLY H H 8.96 0.04 1 918 . 92 GLY C C 175.05 0.30 1 919 . 92 GLY CA C 47.05 0.30 1 920 . 92 GLY HA3 H 4.03 0.04 2 921 . 92 GLY HA2 H 3.78 0.04 2 922 . 93 ILE N N 135.28 0.40 1 923 . 93 ILE H H 9.03 0.04 1 924 . 93 ILE C C 174.24 0.30 1 925 . 93 ILE CA C 61.81 0.30 1 926 . 93 ILE HA H 4.28 0.04 1 927 . 93 ILE CB C 37.93 0.30 1 928 . 93 ILE HB H 1.52 0.04 1 929 . 93 ILE CG1 C 27.94 0.30 1 930 . 93 ILE HG13 H 0.99 0.04 2 931 . 93 ILE HG12 H 0.51 0.04 2 932 . 93 ILE CG2 C 16.37 0.30 1 933 . 93 ILE HG2 H 0.52 0.04 1 934 . 93 ILE CD1 C 14.40 0.30 1 935 . 93 ILE HD1 H 0.49 0.04 1 936 . 94 GLY N N 107.20 0.40 1 937 . 94 GLY H H 7.67 0.04 1 938 . 94 GLY C C 174.38 0.30 1 939 . 94 GLY CA C 46.76 0.30 1 940 . 94 GLY HA3 H 3.82 0.04 2 941 . 94 GLY HA2 H 3.13 0.04 2 942 . 95 GLY N N 120.79 0.40 1 943 . 95 GLY H H 7.91 0.04 1 944 . 95 GLY C C 172.03 0.30 1 945 . 95 GLY CA C 46.69 0.30 1 946 . 95 GLY HA3 H 4.65 0.04 2 947 . 95 GLY HA2 H 4.25 0.04 2 948 . 96 ASP N N 123.72 0.40 1 949 . 96 ASP H H 8.30 0.04 1 950 . 96 ASP C C 173.42 0.30 1 951 . 96 ASP CA C 56.53 0.30 1 952 . 96 ASP HA H 4.70 0.04 1 953 . 96 ASP CB C 39.58 0.30 1 954 . 96 ASP HB3 H 3.03 0.04 2 955 . 96 ASP HB2 H 2.98 0.04 2 956 . 97 ALA N N 121.09 0.40 1 957 . 97 ALA H H 8.61 0.04 1 958 . 97 ALA C C 174.63 0.30 1 959 . 97 ALA CA C 50.79 0.30 1 960 . 97 ALA HA H 4.85 0.04 1 961 . 97 ALA CB C 20.59 0.30 1 962 . 97 ALA HB H 1.05 0.04 1 963 . 98 HIS N N 122.52 0.40 1 964 . 98 HIS H H 9.30 0.04 1 965 . 98 HIS C C 172.88 0.30 1 966 . 98 HIS CA C 50.46 0.30 1 967 . 98 HIS HA H 5.94 0.04 1 968 . 98 HIS CB C 33.96 0.30 1 969 . 98 HIS HB3 H 2.57 0.04 1 970 . 98 HIS HB2 H 3.29 0.04 1 971 . 98 HIS CD2 C 116.04 0.30 1 972 . 98 HIS HD2 H 7.00 0.04 1 973 . 98 HIS CE1 C 141.63 0.30 1 974 . 98 HIS HE1 H 8.43 0.04 1 975 . 99 PHE N N 124.12 0.40 1 976 . 99 PHE H H 9.20 0.04 1 977 . 99 PHE C C 174.00 0.30 1 978 . 99 PHE CA C 56.72 0.30 1 979 . 99 PHE HA H 4.30 0.04 1 980 . 99 PHE CB C 41.02 0.30 1 981 . 99 PHE HB3 H 2.18 0.04 1 982 . 99 PHE HB2 H 1.82 0.04 1 983 . 99 PHE CD1 C 131.86 0.30 3 984 . 99 PHE HD1 H 6.30 0.04 3 985 . 99 PHE CE1 C 129.28 0.30 3 986 . 99 PHE HE1 H 6.62 0.04 3 987 . 99 PHE CZ C 125.58 0.30 1 988 . 99 PHE HZ H 6.43 0.04 1 989 . 100 ASP N N 124.23 0.40 1 990 . 100 ASP H H 8.21 0.04 1 991 . 100 ASP C C 179.46 0.30 1 992 . 100 ASP CA C 54.03 0.30 1 993 . 100 ASP HA H 4.56 0.04 1 994 . 100 ASP CB C 40.12 0.30 1 995 . 100 ASP HB3 H 3.16 0.04 2 996 . 100 ASP HB2 H 0.81 0.04 2 997 . 101 GLU N N 131.95 0.40 1 998 . 101 GLU H H 9.54 0.04 1 999 . 101 GLU C C 176.61 0.30 1 1000 . 101 GLU CA C 56.21 0.30 1 1001 . 101 GLU HA H 4.55 0.04 1 1002 . 101 GLU CB C 31.36 0.30 1 1003 . 101 GLU HB3 H 1.76 0.04 1 1004 . 101 GLU HB2 H 2.12 0.04 1 1005 . 101 GLU CG C 36.46 0.30 1 1006 . 101 GLU HG3 H 2.82 0.04 2 1007 . 101 GLU HG2 H 2.41 0.04 2 1008 . 102 ASP N N 120.66 0.40 1 1009 . 102 ASP H H 9.10 0.04 1 1010 . 102 ASP C C 177.28 0.30 1 1011 . 102 ASP CA C 56.68 0.30 1 1012 . 102 ASP HA H 4.86 0.04 1 1013 . 102 ASP CB C 39.17 0.30 1 1014 . 102 ASP HB3 H 2.75 0.04 2 1015 . 102 ASP HB2 H 2.62 0.04 2 1016 . 103 GLU N N 117.99 0.40 1 1017 . 103 GLU H H 7.47 0.04 1 1018 . 103 GLU C C 174.92 0.30 1 1019 . 103 GLU CA C 53.67 0.30 1 1020 . 103 GLU HA H 4.52 0.04 1 1021 . 103 GLU CB C 26.15 0.30 1 1022 . 103 GLU HB3 H 1.15 0.04 1 1023 . 103 GLU HB2 H 0.80 0.04 1 1024 . 103 GLU CG C 35.69 0.30 1 1025 . 103 GLU HG3 H 2.71 0.04 2 1026 . 104 PHE N N 127.58 0.40 1 1027 . 104 PHE H H 8.46 0.04 1 1028 . 104 PHE C C 172.77 0.30 1 1029 . 104 PHE CA C 55.26 0.30 1 1030 . 104 PHE HA H 5.00 0.04 1 1031 . 104 PHE CB C 38.78 0.30 1 1032 . 104 PHE HB3 H 2.94 0.04 1 1033 . 104 PHE HB2 H 2.77 0.04 1 1034 . 104 PHE CD1 C 131.32 0.30 3 1035 . 104 PHE HD1 H 7.14 0.04 3 1036 . 105 TRP N N 132.78 0.40 1 1037 . 105 TRP H H 9.27 0.04 1 1038 . 105 TRP C C 176.50 0.30 1 1039 . 105 TRP CA C 56.67 0.30 1 1040 . 105 TRP HA H 4.97 0.04 1 1041 . 105 TRP CB C 30.51 0.30 1 1042 . 105 TRP HB3 H 3.28 0.04 1 1043 . 105 TRP HB2 H 2.82 0.04 1 1044 . 105 TRP CD1 C 128.32 0.30 1 1045 . 105 TRP HD1 H 7.46 0.04 1 1046 . 105 TRP CH2 C 123.89 0.30 1 1047 . 105 TRP HH2 H 7.29 0.04 1 1048 . 105 TRP CZ2 C 116.08 0.30 1 1049 . 105 TRP HZ2 H 8.08 0.04 1 1050 . 105 TRP NE1 N 127.10 0.40 1 1051 . 105 TRP HE1 H 9.42 0.04 1 1052 . 106 THR N N 111.07 0.40 1 1053 . 106 THR H H 8.35 0.04 1 1054 . 106 THR C C 175.90 0.30 1 1055 . 106 THR CA C 59.83 0.30 1 1056 . 106 THR HA H 4.66 0.04 1 1057 . 106 THR CB C 71.81 0.30 1 1058 . 106 THR HB H 3.66 0.04 1 1059 . 106 THR CG2 C 20.56 0.30 1 1060 . 106 THR HG2 H 0.65 0.04 1 1061 . 107 THR N N 111.45 0.40 1 1062 . 107 THR H H 8.35 0.04 1 1063 . 107 THR C C 175.51 0.30 1 1064 . 107 THR CA C 62.45 0.30 1 1065 . 107 THR HA H 4.41 0.04 1 1066 . 107 THR CB C 69.25 0.30 1 1067 . 107 THR HB H 4.52 0.04 1 1068 . 107 THR CG2 C 22.45 0.30 1 1069 . 107 THR HG2 H 1.39 0.04 1 1070 . 108 HIS N N 123.92 0.40 1 1071 . 108 HIS H H 8.11 0.04 1 1072 . 108 HIS C C 174.11 0.30 1 1073 . 108 HIS CA C 55.34 0.30 1 1074 . 108 HIS HA H 5.14 0.04 1 1075 . 108 HIS CB C 30.53 0.30 1 1076 . 108 HIS HB3 H 3.27 0.04 1 1077 . 108 HIS HB2 H 3.44 0.04 1 1078 . 108 HIS CD2 C 119.59 0.30 1 1079 . 108 HIS HD2 H 7.26 0.04 1 1080 . 108 HIS CE1 C 138.46 0.30 1 1081 . 108 HIS HE1 H 8.02 0.04 1 1082 . 109 SER N N 116.32 0.40 1 1083 . 109 SER H H 8.04 0.04 1 1084 . 109 SER C C 175.39 0.30 1 1085 . 109 SER CA C 58.38 0.30 1 1086 . 109 SER HA H 3.72 0.04 1 1087 . 109 SER CB C 63.54 0.30 1 1088 . 109 SER HB3 H 3.49 0.04 1 1089 . 109 SER HB2 H 3.05 0.04 1 1090 . 110 GLY N N 115.36 0.40 1 1091 . 110 GLY H H 9.37 0.04 1 1092 . 110 GLY C C 173.75 0.30 1 1093 . 110 GLY CA C 44.96 0.30 1 1094 . 110 GLY HA3 H 4.10 0.04 2 1095 . 110 GLY HA2 H 3.89 0.04 2 1096 . 111 GLY N N 109.99 0.40 1 1097 . 111 GLY H H 7.94 0.04 1 1098 . 111 GLY C C 173.63 0.30 1 1099 . 111 GLY CA C 45.84 0.30 1 1100 . 111 GLY HA3 H 4.09 0.04 2 1101 . 111 GLY HA2 H 3.97 0.04 2 1102 . 112 THR N N 125.38 0.40 1 1103 . 112 THR H H 9.16 0.04 1 1104 . 112 THR C C 172.76 0.30 1 1105 . 112 THR CA C 62.77 0.30 1 1106 . 112 THR HA H 3.85 0.04 1 1107 . 112 THR CB C 68.47 0.30 1 1108 . 112 THR HB H 2.60 0.04 1 1109 . 112 THR CG2 C 25.19 0.30 1 1110 . 112 THR HG2 H 0.67 0.04 1 1111 . 113 ASN N N 126.92 0.40 1 1112 . 113 ASN H H 8.29 0.04 1 1113 . 113 ASN C C 176.64 0.30 1 1114 . 113 ASN CA C 55.67 0.30 1 1115 . 113 ASN HA H 4.98 0.04 1 1116 . 113 ASN CB C 41.41 0.30 1 1117 . 113 ASN HB3 H 3.21 0.04 2 1118 . 113 ASN ND2 N 112.55 0.40 1 1119 . 113 ASN HD21 H 8.14 0.04 2 1120 . 113 ASN HD22 H 6.31 0.04 2 1121 . 114 LEU N N 133.69 0.40 1 1122 . 114 LEU H H 8.75 0.04 1 1123 . 114 LEU C C 176.36 0.30 1 1124 . 114 LEU CA C 59.06 0.30 1 1125 . 114 LEU HA H 4.59 0.04 1 1126 . 114 LEU CB C 41.14 0.30 1 1127 . 114 LEU HB3 H 1.93 0.04 1 1128 . 114 LEU HB2 H 1.73 0.04 1 1129 . 114 LEU CG C 27.50 0.30 1 1130 . 114 LEU HG H 1.26 0.04 1 1131 . 114 LEU CD1 C 22.60 0.30 1 1132 . 114 LEU HD1 H 0.04 0.04 2 1133 . 114 LEU CD2 C 27.92 0.30 1 1134 . 114 LEU HD2 H 0.91 0.04 2 1135 . 115 PHE N N 121.69 0.40 1 1136 . 115 PHE H H 9.34 0.04 1 1137 . 115 PHE C C 175.65 0.30 1 1138 . 115 PHE CA C 61.39 0.30 1 1139 . 115 PHE HA H 4.06 0.04 1 1140 . 115 PHE CB C 37.88 0.30 1 1141 . 115 PHE HB3 H 3.53 0.04 2 1142 . 115 PHE HB2 H 3.27 0.04 2 1143 . 115 PHE CD1 C 132.31 0.30 3 1144 . 115 PHE HD1 H 7.36 0.04 3 1145 . 115 PHE CE1 C 130.24 0.30 3 1146 . 115 PHE HE1 H 6.63 0.04 3 1147 . 115 PHE HZ H 6.8700 0.04 1 1148 . 116 LEU N N 119.93 0.40 1 1149 . 116 LEU H H 9.26 0.04 1 1150 . 116 LEU C C 178.90 0.30 1 1151 . 116 LEU CA C 57.83 0.30 1 1152 . 116 LEU HA H 3.30 0.04 1 1153 . 116 LEU CB C 43.72 0.30 1 1154 . 116 LEU HB3 H 1.84 0.04 1 1155 . 116 LEU HB2 H 1.97 0.04 1 1156 . 116 LEU CG C 27.15 0.30 1 1157 . 116 LEU HG H 1.97 0.04 1 1158 . 116 LEU CD1 C 25.53 0.30 1 1159 . 116 LEU HD1 H 1.07 0.04 2 1160 . 116 LEU CD2 C 24.61 0.30 1 1161 . 116 LEU HD2 H 0.71 0.04 2 1162 . 117 THR N N 115.06 0.40 1 1163 . 117 THR H H 7.87 0.04 1 1164 . 117 THR C C 176.50 0.30 1 1165 . 117 THR CA C 66.62 0.30 1 1166 . 117 THR HA H 5.01 0.04 1 1167 . 117 THR CB C 68.31 0.30 1 1168 . 117 THR HB H 4.68 0.04 1 1169 . 117 THR CG2 C 22.02 0.30 1 1170 . 117 THR HG2 H 1.93 0.04 1 1171 . 118 ALA N N 125.69 0.40 1 1172 . 118 ALA H H 9.40 0.04 1 1173 . 118 ALA C C 178.23 0.30 1 1174 . 118 ALA CA C 55.87 0.30 1 1175 . 118 ALA HA H 3.96 0.04 1 1176 . 118 ALA CB C 16.88 0.30 1 1177 . 118 ALA HB H 1.16 0.04 1 1178 . 119 VAL N N 119.42 0.40 1 1179 . 119 VAL H H 8.44 0.04 1 1180 . 119 VAL C C 178.52 0.30 1 1181 . 119 VAL CA C 68.46 0.30 1 1182 . 119 VAL HA H 3.14 0.04 1 1183 . 119 VAL CB C 30.92 0.30 1 1184 . 119 VAL HB H 1.75 0.04 1 1185 . 119 VAL CG1 C 23.90 0.30 1 1186 . 119 VAL HG1 H 0.69 0.04 2 1187 . 119 VAL CG2 C 23.24 0.30 1 1188 . 119 VAL HG2 H 0.17 0.04 2 1189 . 120 HIS N N 118.11 0.40 1 1190 . 120 HIS H H 7.26 0.04 1 1191 . 120 HIS C C 175.84 0.30 1 1192 . 120 HIS CA C 59.15 0.30 1 1193 . 120 HIS HA H 3.86 0.04 1 1194 . 120 HIS CB C 28.42 0.30 1 1195 . 120 HIS HB3 H 3.04 0.04 1 1196 . 120 HIS HB2 H 2.04 0.04 1 1197 . 121 GLU N N 114.76 0.40 1 1198 . 121 GLU H H 8.60 0.04 1 1199 . 121 GLU C C 177.88 0.30 1 1200 . 121 GLU CA C 57.49 0.30 1 1201 . 121 GLU HA H 3.97 0.04 1 1202 . 121 GLU CB C 26.66 0.30 1 1203 . 121 GLU HB3 H 1.82 0.04 1 1204 . 121 GLU HB2 H 1.49 0.04 1 1205 . 121 GLU CG C 31.29 0.30 1 1206 . 122 ILE N N 119.90 0.40 1 1207 . 122 ILE H H 9.03 0.04 1 1208 . 122 ILE C C 177.37 0.30 1 1209 . 122 ILE CA C 63.77 0.30 1 1210 . 122 ILE HA H 3.56 0.04 1 1211 . 122 ILE CB C 37.09 0.30 1 1212 . 122 ILE HB H 1.42 0.04 1 1213 . 122 ILE CG1 C 29.47 0.30 1 1214 . 122 ILE HG13 H 1.09 0.04 2 1215 . 122 ILE HG12 H 0.28 0.04 2 1216 . 122 ILE CG2 C 18.67 0.30 1 1217 . 122 ILE HG2 H 0.21 0.04 1 1218 . 122 ILE CD1 C 12.10 0.30 1 1219 . 122 ILE HD1 H -0.52 0.04 1 1220 . 123 GLY N N 109.10 0.40 1 1221 . 123 GLY H H 7.46 0.04 1 1222 . 123 GLY C C 176.78 0.30 1 1223 . 123 GLY CA C 48.00 0.30 1 1224 . 123 GLY HA3 H 3.62 0.04 2 1225 . 123 GLY HA2 H 2.35 0.04 2 1226 . 124 HIS N N 120.71 0.40 1 1227 . 124 HIS H H 6.94 0.04 1 1228 . 124 HIS C C 180.11 0.30 1 1229 . 124 HIS CA C 58.28 0.30 1 1230 . 124 HIS HA H 4.70 0.04 1 1231 . 124 HIS CB C 27.42 0.30 1 1232 . 124 HIS HB3 H 3.62 0.04 2 1233 . 124 HIS HB2 H 2.62 0.04 2 1234 . 125 SER N N 124.62 0.40 1 1235 . 125 SER H H 8.95 0.04 1 1236 . 125 SER C C 175.87 0.30 1 1237 . 125 SER CA C 63.02 0.30 1 1238 . 126 LEU N N 115.53 0.40 1 1239 . 126 LEU H H 7.72 0.04 1 1240 . 126 LEU C C 177.92 0.30 1 1241 . 126 LEU CA C 54.95 0.30 1 1242 . 126 LEU HA H 4.60 0.04 1 1243 . 126 LEU CB C 42.00 0.30 1 1244 . 126 LEU HB3 H 1.69 0.04 2 1245 . 126 LEU CG C 25.51 0.30 1 1246 . 126 LEU HG H 2.00 0.04 1 1247 . 126 LEU CD1 C 24.54 0.30 1 1248 . 126 LEU HD1 H 0.32 0.04 2 1249 . 126 LEU CD2 C 21.54 0.30 1 1250 . 126 LEU HD2 H 0.85 0.04 2 1251 . 127 GLY N N 108.26 0.40 1 1252 . 127 GLY H H 8.19 0.04 1 1253 . 127 GLY C C 174.01 0.30 1 1254 . 127 GLY CA C 44.19 0.30 1 1255 . 127 GLY HA3 H 4.63 0.04 2 1256 . 127 GLY HA2 H 3.49 0.04 2 1257 . 128 LEU N N 122.40 0.40 1 1258 . 128 LEU H H 8.19 0.04 1 1259 . 128 LEU C C 177.33 0.30 1 1260 . 128 LEU CA C 55.24 0.30 1 1261 . 128 LEU HA H 4.17 0.04 1 1262 . 128 LEU CB C 42.88 0.30 1 1263 . 128 LEU HB3 H 1.41 0.04 2 1264 . 128 LEU HB2 H 1.11 0.04 2 1265 . 128 LEU CG C 26.04 0.30 1 1266 . 128 LEU HG H 1.37 0.04 1 1267 . 128 LEU CD1 C 26.20 0.30 1 1268 . 128 LEU HD1 H 0.63 0.04 2 1269 . 128 LEU CD2 C 22.90 0.30 1 1270 . 128 LEU HD2 H 0.64 0.04 2 1271 . 129 GLY N N 111.88 0.40 1 1272 . 129 GLY H H 8.13 0.04 1 1273 . 129 GLY C C 173.15 0.30 1 1274 . 129 GLY CA C 43.32 0.30 1 1275 . 129 GLY HA3 H 4.28 0.04 2 1276 . 129 GLY HA2 H 3.60 0.04 2 1277 . 130 HIS N N 116.79 0.40 1 1278 . 130 HIS H H 8.33 0.04 1 1279 . 130 HIS C C 175.08 0.30 1 1280 . 130 HIS CA C 55.21 0.30 1 1281 . 130 HIS HA H 5.51 0.04 1 1282 . 130 HIS CB C 31.23 0.30 1 1283 . 130 HIS HB3 H 3.11 0.04 2 1284 . 130 HIS CD2 C 125.55 0.30 1 1285 . 130 HIS HD2 H 7.04 0.04 1 1286 . 130 HIS CE1 C 140.27 0.30 1 1287 . 130 HIS HE1 H 8.24 0.04 1 1288 . 131 SER N N 115.60 0.40 1 1289 . 131 SER H H 7.55 0.04 1 1290 . 131 SER C C 175.25 0.30 1 1291 . 131 SER CA C 55.22 0.30 1 1292 . 131 SER HA H 4.73 0.04 1 1293 . 131 SER CB C 65.45 0.30 1 1294 . 131 SER HB3 H 4.07 0.04 2 1295 . 131 SER HB2 H 3.21 0.04 2 1296 . 132 SER N N 120.11 0.40 1 1297 . 132 SER H H 8.73 0.04 1 1298 . 132 SER C C 173.82 0.30 1 1299 . 132 SER CA C 58.22 0.30 1 1300 . 132 SER HA H 4.80 0.04 1 1301 . 132 SER CB C 64.00 0.30 1 1302 . 132 SER HB3 H 4.18 0.04 2 1303 . 132 SER HB2 H 3.97 0.04 2 1304 . 133 ASP N N 127.94 0.40 1 1305 . 133 ASP H H 8.91 0.04 1 1306 . 133 ASP C C 174.82 0.30 1 1307 . 133 ASP CA C 51.36 0.30 1 1308 . 133 ASP HA H 4.91 0.04 1 1309 . 133 ASP CB C 42.19 0.30 1 1310 . 133 ASP HB3 H 3.17 0.04 2 1311 . 133 ASP HB2 H 2.53 0.04 2 1312 . 134 PRO C C 177.95 0.30 1 1313 . 134 PRO CA C 63.31 0.30 1 1314 . 134 PRO HA H 2.97 0.04 1 1315 . 134 PRO CB C 32.00 0.30 1 1316 . 134 PRO HB3 H 1.70 0.04 2 1317 . 134 PRO HB2 H 1.60 0.04 2 1318 . 134 PRO CG C 27.17 0.30 1 1319 . 134 PRO HG3 H 1.88 0.04 2 1320 . 134 PRO HG2 H 1.61 0.04 2 1321 . 134 PRO CD C 50.82 0.30 1 1322 . 134 PRO HD3 H 4.23 0.04 2 1323 . 134 PRO HD2 H 3.93 0.04 2 1324 . 135 LYS N N 118.71 0.40 1 1325 . 135 LYS H H 8.44 0.04 1 1326 . 135 LYS C C 176.64 0.30 1 1327 . 135 LYS CA C 55.97 0.30 1 1328 . 135 LYS HA H 4.28 0.04 1 1329 . 135 LYS CB C 31.90 0.30 1 1330 . 135 LYS HB3 H 1.86 0.04 2 1331 . 135 LYS CG C 24.91 0.30 1 1332 . 135 LYS HG3 H 1.44 0.04 2 1333 . 135 LYS CD C 28.36 0.30 1 1334 . 135 LYS HD3 H 1.75 0.04 2 1335 . 135 LYS CE C 41.34 0.30 1 1336 . 135 LYS HE3 H 3.04 0.04 2 1337 . 136 ALA N N 125.59 0.40 1 1338 . 136 ALA H H 8.34 0.04 1 1339 . 136 ALA C C 179.36 0.30 1 1340 . 136 ALA CA C 52.00 0.30 1 1341 . 136 ALA HA H 4.64 0.04 1 1342 . 136 ALA CB C 19.60 0.30 1 1343 . 136 ALA HB H 1.89 0.04 1 1344 . 137 VAL N N 132.68 0.40 1 1345 . 137 VAL H H 11.48 0.04 1 1346 . 137 VAL C C 176.62 0.30 1 1347 . 137 VAL CA C 64.16 0.30 1 1348 . 137 VAL HA H 4.57 0.04 1 1349 . 137 VAL CB C 31.21 0.30 1 1350 . 137 VAL HB H 2.47 0.04 1 1351 . 137 VAL CG1 C 20.29 0.30 1 1352 . 137 VAL HG1 H 0.92 0.04 2 1353 . 137 VAL CG2 C 23.85 0.30 1 1354 . 137 VAL HG2 H 1.24 0.04 2 1355 . 138 MET N N 115.75 0.40 1 1356 . 138 MET H H 7.62 0.04 1 1357 . 138 MET C C 176.32 0.30 1 1358 . 138 MET CA C 52.58 0.30 1 1359 . 138 MET HA H 4.63 0.04 1 1360 . 138 MET CB C 26.35 0.30 1 1361 . 138 MET HB3 H 2.75 0.04 1 1362 . 138 MET HB2 H 2.51 0.04 1 1363 . 138 MET CG C 30.43 0.30 1 1364 . 138 MET HG3 H 2.66 0.04 2 1365 . 139 PHE N N 127.76 0.40 1 1366 . 139 PHE H H 7.75 0.04 1 1367 . 139 PHE C C 175.48 0.30 1 1368 . 139 PHE CA C 57.84 0.30 1 1369 . 139 PHE HA H 5.26 0.04 1 1370 . 139 PHE CB C 40.96 0.30 1 1371 . 139 PHE HB3 H 3.24 0.04 1 1372 . 139 PHE HB2 H 4.09 0.04 1 1373 . 139 PHE CD1 C 133.21 0.30 3 1374 . 139 PHE HD1 H 7.57 0.04 3 1375 . 139 PHE CE1 C 131.22 0.30 3 1376 . 139 PHE HE1 H 7.36 0.04 3 1377 . 139 PHE CZ C 130.18 0.30 1 1378 . 139 PHE HZ H 7.43 0.04 1 1379 . 140 PRO C C 175.77 0.30 1 1380 . 140 PRO CA C 64.98 0.30 1 1381 . 140 PRO HA H 3.56 0.04 1 1382 . 140 PRO CB C 32.08 0.30 1 1383 . 140 PRO HB3 H 1.77 0.04 2 1384 . 140 PRO HB2 H 1.66 0.04 2 1385 . 140 PRO CG C 27.56 0.30 1 1386 . 140 PRO HG3 H 1.49 0.04 2 1387 . 141 THR N N 113.03 0.40 1 1388 . 141 THR H H 6.86 0.04 1 1389 . 141 THR CA C 60.20 0.30 1 1390 . 141 THR HA H 4.54 0.04 1 1391 . 141 THR CB C 71.44 0.30 1 1392 . 141 THR HB H 3.95 0.04 1 1393 . 141 THR CG2 C 21.63 0.30 1 1394 . 141 THR HG2 H 1.21 0.04 1 1395 . 142 TYR N N 126.87 0.40 1 1396 . 142 TYR H H 7.74 0.04 1 1397 . 142 TYR CD1 C 132.76 0.30 3 1398 . 142 TYR HD1 H 6.52 0.04 3 1399 . 142 TYR CE1 C 117.07 0.30 3 1400 . 142 TYR HE1 H 6.81 0.04 3 1401 . 143 LYS C C 173.38 0.30 1 1402 . 143 LYS CA C 55.23 0.30 1 1403 . 143 LYS HA H 3.84 0.04 1 1404 . 143 LYS CB C 34.81 0.30 1 1405 . 143 LYS HB3 H 1.59 0.04 2 1406 . 143 LYS CG C 23.95 0.30 1 1407 . 143 LYS HG3 H 1.25 0.04 2 1408 . 143 LYS CD C 28.87 0.30 1 1409 . 143 LYS HD3 H 1.62 0.04 2 1410 . 143 LYS CE C 41.78 0.30 1 1411 . 143 LYS HE3 H 2.90 0.04 2 1412 . 144 TYR N N 124.41 0.40 1 1413 . 144 TYR H H 8.46 0.04 1 1414 . 144 TYR C C 174.88 0.30 1 1415 . 144 TYR CA C 60.60 0.30 1 1416 . 144 TYR HA H 3.75 0.04 1 1417 . 144 TYR CB C 38.41 0.30 1 1418 . 144 TYR HB3 H 2.74 0.04 1 1419 . 144 TYR HB2 H 3.06 0.04 1 1420 . 144 TYR CD1 C 132.34 0.30 3 1421 . 144 TYR HD1 H 7.00 0.04 3 1422 . 144 TYR CE1 C 118.70 0.30 3 1423 . 144 TYR HE1 H 6.82 0.04 3 1424 . 145 VAL N N 125.02 0.40 1 1425 . 145 VAL H H 5.78 0.04 1 1426 . 145 VAL C C 172.11 0.30 1 1427 . 145 VAL CA C 59.28 0.30 1 1428 . 145 VAL HA H 3.95 0.04 1 1429 . 145 VAL CB C 34.91 0.30 1 1430 . 145 VAL HB H 1.93 0.04 1 1431 . 145 VAL CG1 C 21.34 0.30 1 1432 . 145 VAL HG1 H 0.91 0.04 2 1433 . 145 VAL CG2 C 19.48 0.30 1 1434 . 145 VAL HG2 H 0.88 0.04 2 1435 . 146 ASP N N 119.75 0.40 1 1436 . 146 ASP H H 7.86 0.04 1 1437 . 146 ASP C C 179.23 0.30 1 1438 . 146 ASP CA C 55.02 0.30 1 1439 . 146 ASP HA H 4.29 0.04 1 1440 . 146 ASP CB C 41.83 0.30 1 1441 . 146 ASP HB3 H 2.79 0.04 2 1442 . 147 ILE N N 125.08 0.40 1 1443 . 147 ILE H H 7.75 0.04 1 1444 . 147 ILE C C 177.43 0.30 1 1445 . 147 ILE CA C 64.37 0.30 1 1446 . 147 ILE HA H 3.99 0.04 1 1447 . 147 ILE CB C 37.77 0.30 1 1448 . 147 ILE HB H 2.10 0.04 1 1449 . 147 ILE CG1 C 26.65 0.30 1 1450 . 147 ILE HG13 H 1.44 0.04 2 1451 . 147 ILE CG2 C 18.62 0.30 1 1452 . 147 ILE HG2 H 1.24 0.04 1 1453 . 147 ILE CD1 C 13.83 0.30 1 1454 . 147 ILE HD1 H 0.92 0.04 1 1455 . 148 ASN N N 120.13 0.40 1 1456 . 148 ASN H H 8.63 0.04 1 1457 . 148 ASN C C 176.47 0.30 1 1458 . 148 ASN CA C 55.57 0.30 1 1459 . 148 ASN HA H 4.61 0.04 1 1460 . 148 ASN CB C 38.34 0.30 1 1461 . 148 ASN HB3 H 2.88 0.04 1 1462 . 148 ASN HB2 H 3.05 0.04 1 1463 . 148 ASN ND2 N 116.24 0.40 1 1464 . 148 ASN HD21 H 8.05 0.04 2 1465 . 148 ASN HD22 H 7.09 0.04 2 1466 . 149 THR N N 109.55 0.40 1 1467 . 149 THR H H 7.51 0.04 1 1468 . 149 THR C C 173.86 0.30 1 1469 . 149 THR CA C 60.61 0.30 1 1470 . 149 THR HA H 4.49 0.04 1 1471 . 149 THR CB C 69.20 0.30 1 1472 . 149 THR HB H 4.46 0.04 1 1473 . 149 THR CG2 C 21.41 0.30 1 1474 . 149 THR HG2 H 1.15 0.04 1 1475 . 150 PHE N N 124.30 0.40 1 1476 . 150 PHE H H 7.20 0.04 1 1477 . 150 PHE C C 174.54 0.30 1 1478 . 150 PHE CA C 59.87 0.30 1 1479 . 150 PHE HA H 4.25 0.04 1 1480 . 150 PHE CB C 39.86 0.30 1 1481 . 150 PHE HB3 H 3.22 0.04 2 1482 . 150 PHE HB2 H 2.94 0.04 2 1483 . 150 PHE CD1 C 131.19 0.30 3 1484 . 150 PHE HD1 H 7.16 0.04 3 1485 . 150 PHE CE1 C 131.17 0.30 3 1486 . 150 PHE HE1 H 7.35 0.04 3 1487 . 150 PHE CZ C 128.45 0.30 1 1488 . 150 PHE HZ H 6.89 0.04 1 1489 . 151 ARG N N 127.41 0.40 1 1490 . 151 ARG H H 7.24 0.04 1 1491 . 151 ARG C C 174.51 0.30 1 1492 . 151 ARG CA C 54.24 0.30 1 1493 . 151 ARG HA H 3.96 0.04 1 1494 . 151 ARG CB C 33.19 0.30 1 1495 . 151 ARG HB3 H 1.71 0.04 1 1496 . 151 ARG HB2 H 1.53 0.04 1 1497 . 151 ARG CG C 26.09 0.30 1 1498 . 151 ARG HG3 H 1.54 0.04 2 1499 . 151 ARG HG2 H 1.46 0.04 2 1500 . 151 ARG CD C 43.22 0.30 1 1501 . 151 ARG HD3 H 3.19 0.04 2 1502 . 151 ARG HD2 H 3.12 0.04 2 1503 . 151 ARG NE N 86.74 0.40 1 1504 . 151 ARG HE H 6.98 0.04 1 1505 . 152 LEU N N 122.26 0.40 1 1506 . 152 LEU H H 8.15 0.04 1 1507 . 152 LEU C C 177.16 0.30 1 1508 . 152 LEU CA C 54.97 0.30 1 1509 . 152 LEU HA H 3.95 0.04 1 1510 . 152 LEU CB C 42.88 0.30 1 1511 . 152 LEU HB3 H 1.50 0.04 2 1512 . 152 LEU HB2 H 1.44 0.04 2 1513 . 152 LEU CG C 26.10 0.30 1 1514 . 152 LEU HG H 1.37 0.04 1 1515 . 152 LEU CD1 C 26.77 0.30 1 1516 . 152 LEU HD1 H 0.38 0.04 2 1517 . 152 LEU CD2 C 22.49 0.30 1 1518 . 152 LEU HD2 H 0.16 0.04 2 1519 . 153 SER N N 119.89 0.40 1 1520 . 153 SER H H 9.18 0.04 1 1521 . 153 SER C C 174.88 0.30 1 1522 . 153 SER CA C 57.59 0.30 1 1523 . 153 SER HA H 4.55 0.04 1 1524 . 153 SER CB C 65.89 0.30 1 1525 . 153 SER HB3 H 4.27 0.04 2 1526 . 153 SER HB2 H 3.90 0.04 2 1527 . 154 ALA N N 124.91 0.40 1 1528 . 154 ALA H H 8.90 0.04 1 1529 . 154 ALA C C 180.27 0.30 1 1530 . 154 ALA CA C 55.49 0.30 1 1531 . 154 ALA HA H 4.12 0.04 1 1532 . 154 ALA CB C 17.77 0.30 1 1533 . 154 ALA HB H 1.52 0.04 1 1534 . 155 ASP N N 118.87 0.40 1 1535 . 155 ASP H H 8.36 0.04 1 1536 . 155 ASP C C 178.72 0.30 1 1537 . 155 ASP CA C 58.08 0.30 1 1538 . 155 ASP HA H 4.48 0.04 1 1539 . 155 ASP CB C 43.05 0.30 1 1540 . 155 ASP HB3 H 2.88 0.04 1 1541 . 155 ASP HB2 H 2.58 0.04 1 1542 . 156 ASP N N 120.77 0.40 1 1543 . 156 ASP H H 7.53 0.04 1 1544 . 156 ASP C C 177.78 0.30 1 1545 . 156 ASP CA C 57.83 0.30 1 1546 . 156 ASP HA H 4.72 0.04 1 1547 . 156 ASP CB C 44.01 0.30 1 1548 . 156 ASP HB3 H 3.17 0.04 2 1549 . 156 ASP HB2 H 2.79 0.04 2 1550 . 157 ILE N N 119.85 0.40 1 1551 . 157 ILE H H 7.89 0.04 1 1552 . 157 ILE C C 177.48 0.30 1 1553 . 157 ILE CA C 65.66 0.30 1 1554 . 157 ILE HA H 3.70 0.04 1 1555 . 157 ILE CB C 38.38 0.30 1 1556 . 157 ILE HB H 1.79 0.04 1 1557 . 157 ILE CG1 C 30.73 0.30 1 1558 . 157 ILE HG13 H 1.86 0.04 2 1559 . 157 ILE HG12 H 0.85 0.04 2 1560 . 157 ILE CG2 C 16.84 0.30 1 1561 . 157 ILE HG2 H 0.95 0.04 1 1562 . 157 ILE CD1 C 12.92 0.30 1 1563 . 157 ILE HD1 H 0.83 0.04 1 1564 . 158 ARG N N 120.44 0.40 1 1565 . 158 ARG H H 8.52 0.04 1 1566 . 158 ARG C C 180.37 0.30 1 1567 . 158 ARG CA C 59.33 0.30 1 1568 . 158 ARG HA H 4.16 0.04 1 1569 . 158 ARG CB C 30.06 0.30 1 1570 . 158 ARG HB3 H 1.95 0.04 1 1571 . 158 ARG HB2 H 2.04 0.04 1 1572 . 158 ARG CG C 26.98 0.30 1 1573 . 158 ARG HG3 H 1.84 0.04 2 1574 . 158 ARG HG2 H 1.70 0.04 2 1575 . 158 ARG CD C 43.16 0.30 1 1576 . 158 ARG HD3 H 3.28 0.04 2 1577 . 158 ARG NE N 85.60 0.40 1 1578 . 158 ARG HE H 7.30 0.04 1 1579 . 159 GLY N N 108.29 0.40 1 1580 . 159 GLY H H 8.45 0.04 1 1581 . 159 GLY C C 176.78 0.30 1 1582 . 159 GLY CA C 47.35 0.30 1 1583 . 159 GLY HA3 H 3.78 0.04 2 1584 . 160 ILE N N 124.41 0.40 1 1585 . 160 ILE H H 8.56 0.04 1 1586 . 160 ILE C C 177.87 0.30 1 1587 . 160 ILE CA C 61.12 0.30 1 1588 . 160 ILE HA H 4.52 0.04 1 1589 . 160 ILE CB C 38.55 0.30 1 1590 . 160 ILE HB H 2.14 0.04 1 1591 . 160 ILE CG1 C 30.88 0.30 1 1592 . 160 ILE HG13 H 1.85 0.04 2 1593 . 160 ILE HG12 H 1.61 0.04 2 1594 . 160 ILE CG2 C 20.51 0.30 1 1595 . 160 ILE HG2 H 1.61 0.04 1 1596 . 160 ILE CD1 C 14.94 0.30 1 1597 . 160 ILE HD1 H 0.90 0.04 1 1598 . 161 GLN N N 124.92 0.40 1 1599 . 161 GLN H H 8.69 0.04 1 1600 . 161 GLN C C 179.24 0.30 1 1601 . 161 GLN CA C 58.67 0.30 1 1602 . 161 GLN HA H 4.47 0.04 1 1603 . 161 GLN CB C 27.05 0.30 1 1604 . 161 GLN HB3 H 2.03 0.04 1 1605 . 161 GLN HB2 H 2.30 0.04 1 1606 . 161 GLN CG C 34.94 0.30 1 1607 . 161 GLN HG3 H 2.99 0.04 2 1608 . 161 GLN HG2 H 2.78 0.04 2 1609 . 161 GLN NE2 N 111.29 0.40 1 1610 . 161 GLN HE21 H 7.96 0.04 2 1611 . 161 GLN HE22 H 6.68 0.04 2 1612 . 162 SER N N 116.71 0.40 1 1613 . 162 SER H H 7.99 0.04 1 1614 . 162 SER C C 174.97 0.30 1 1615 . 162 SER CA C 61.30 0.30 1 1616 . 162 SER HA H 4.30 0.04 1 1617 . 162 SER CB C 62.88 0.30 1 1618 . 162 SER HB3 H 4.07 0.04 2 1619 . 162 SER HB2 H 4.03 0.04 2 1620 . 163 LEU N N 120.17 0.40 1 1621 . 163 LEU H H 6.96 0.04 1 1622 . 163 LEU C C 177.58 0.30 1 1623 . 163 LEU CA C 56.44 0.30 1 1624 . 163 LEU HA H 4.19 0.04 1 1625 . 163 LEU CB C 43.65 0.30 1 1626 . 163 LEU HB3 H 0.85 0.04 1 1627 . 163 LEU HB2 H 1.85 0.04 1 1628 . 163 LEU CG C 26.49 0.30 1 1629 . 163 LEU HG H 1.74 0.04 1 1630 . 163 LEU CD1 C 25.49 0.30 1 1631 . 163 LEU HD1 H 0.81 0.04 2 1632 . 163 LEU CD2 C 21.84 0.30 1 1633 . 163 LEU HD2 H 0.68 0.04 2 1634 . 164 TYR N N 115.67 0.40 1 1635 . 164 TYR H H 7.74 0.04 1 1636 . 164 TYR C C 174.50 0.30 1 1637 . 164 TYR CA C 59.00 0.30 1 1638 . 164 TYR HA H 4.72 0.04 1 1639 . 164 TYR CB C 40.47 0.30 1 1640 . 164 TYR HB3 H 3.10 0.04 2 1641 . 164 TYR HB2 H 2.81 0.04 2 1642 . 164 TYR CD1 C 133.94 0.30 3 1643 . 164 TYR HD1 H 7.32 0.04 3 1644 . 165 GLY N N 116.89 0.40 1 1645 . 165 GLY H H 8.15 0.04 1 1646 . 165 GLY C C 178.27 0.30 1 1647 . 165 GLY CA C 46.08 0.30 1 1648 . 165 GLY HA3 H 3.88 0.04 2 stop_ save_