data_7089 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 13C, and 15N Peak Assignments of Human Macrophage Metalloelastase, in its inhibitor-free state ; _BMRB_accession_number 7089 _BMRB_flat_file_name bmr7089.str _Entry_type original _Submission_date 2006-04-26 _Accession_date 2006-04-27 _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 Bhaskaran Rajagopalan . . 2 VanDoren Steven R. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 802 "13C chemical shifts" 638 "15N chemical shifts" 166 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2007-05-02 original author . stop_ _Original_release_date 2007-05-02 save_ ############################# # Citation for this entry # ############################# save_citation_1 _Saveframe_category entry_citation _Citation_full . _Citation_title ; 1H, 13C, and 15N peak assignments and secondary structure of human macrophage metalloelastase (MMP-12) in its inhibitor-free state ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 16855860 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Bhaskaran Rajagopalan . . 2 VanDoren Steven R. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 36 _Journal_issue 'Suppl. 1' _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 55 _Page_last 55 _Year 2006 _Details . loop_ _Keyword 'Chemical Shifts' 'Inhibitor-free State' 'Matrix Metalloealstase' 'Resonance Assignments' 'Secondary Structure' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'Metalloelastase monomer' _Enzyme_commission_number E.3.4.24.65 loop_ _Mol_system_component_name _Mol_label Metalloprotease $Metalloprotease 'ZINC (II) ION, 1' $ZN 'ZINC (II) ION, 2' $ZN 'CALCIUM (II) ION, 1' $CA 'CALCIUM (II) ION, 2' $CA 'CALCIUM (II) ION, 3' $CA stop_ _System_molecular_weight 18152.7 _System_physical_state native _System_oligomer_state protein _System_paramagnetic no _System_thiol_state 'not present' loop_ _Magnetic_equivalence_ID _Magnetically_equivalent_system_component 1 Metalloprotease 2 'ZINC (II) ION, 1' 2 'ZINC (II) ION, 2' 3 'CALCIUM (II) ION, 1' 3 'CALCIUM (II) ION, 2' 3 'CALCIUM (II) ION, 3' stop_ loop_ _Biological_function 'degrades elastin and alpha1-antitrypsin' stop_ _Database_query_date . _Details 'Metalloelastase with Zinc and Calcium ions without inhibitor bound' save_ ######################## # Monomeric polymers # ######################## save_Metalloprotease _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common MMP-12 _Molecular_mass 18152.7 _Mol_thiol_state 'not present' loop_ _Biological_function 'Protease- Degrades Elastin and alpha1-antitrypsin' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 164 _Mol_residue_sequence ; FREMPGGPVWRKHYITYRIN NYTPDMNREDVDYAIRKAFQ VWSNVTPLKFSKINTGMADI LVVFARGAHGDFHAFDGKGG ILAHAFGPGSGIGGDAHFDE DEFWTTHSGGTNLFLTAVHA IGHSLGLGHSSDPKAVMFPT YKYVDINTFRLSADDIRGIQ SLYG ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 100 PHE 2 101 ARG 3 102 GLU 4 103 MET 5 104 PRO 6 105 GLY 7 106 GLY 8 107 PRO 9 108 VAL 10 109 TRP 11 110 ARG 12 111 LYS 13 112 HIS 14 113 TYR 15 114 ILE 16 115 THR 17 116 TYR 18 117 ARG 19 118 ILE 20 119 ASN 21 120 ASN 22 121 TYR 23 122 THR 24 123 PRO 25 124 ASP 26 125 MET 27 126 ASN 28 127 ARG 29 128 GLU 30 129 ASP 31 130 VAL 32 131 ASP 33 132 TYR 34 133 ALA 35 134 ILE 36 135 ARG 37 136 LYS 38 137 ALA 39 138 PHE 40 139 GLN 41 140 VAL 42 141 TRP 43 142 SER 44 143 ASN 45 144 VAL 46 145 THR 47 146 PRO 48 147 LEU 49 148 LYS 50 149 PHE 51 150 SER 52 151 LYS 53 152 ILE 54 153 ASN 55 154 THR 56 155 GLY 57 156 MET 58 157 ALA 59 158 ASP 60 159 ILE 61 160 LEU 62 161 VAL 63 162 VAL 64 163 PHE 65 164 ALA 66 165 ARG 67 166 GLY 68 167 ALA 69 168 HIS 70 169 GLY 71 170 ASP 72 171 PHE 73 172 HIS 74 173 ALA 75 174 PHE 76 175 ASP 77 176 GLY 78 177 LYS 79 178 GLY 80 179 GLY 81 180 ILE 82 181 LEU 83 182 ALA 84 183 HIS 85 184 ALA 86 185 PHE 87 186 GLY 88 187 PRO 89 188 GLY 90 189 SER 91 190 GLY 92 191 ILE 93 192 GLY 94 193 GLY 95 194 ASP 96 195 ALA 97 196 HIS 98 197 PHE 99 198 ASP 100 199 GLU 101 200 ASP 102 201 GLU 103 202 PHE 104 203 TRP 105 204 THR 106 205 THR 107 206 HIS 108 207 SER 109 208 GLY 110 209 GLY 111 210 THR 112 211 ASN 113 212 LEU 114 213 PHE 115 214 LEU 116 215 THR 117 216 ALA 118 217 VAL 119 218 HIS 120 219 ALA 121 220 ILE 122 221 GLY 123 222 HIS 124 223 SER 125 224 LEU 126 225 GLY 127 226 LEU 128 227 GLY 129 228 HIS 130 229 SER 131 230 SER 132 231 ASP 133 232 PRO 134 233 LYS 135 234 ALA 136 235 VAL 137 236 MET 138 237 PHE 139 238 PRO 140 239 THR 141 240 TYR 142 241 LYS 143 242 TYR 144 243 VAL 145 244 ASP 146 245 ILE 147 246 ASN 148 247 THR 149 248 PHE 150 249 ARG 151 250 LEU 152 251 SER 153 252 ALA 154 253 ASP 155 254 ASP 156 255 ILE 157 256 ARG 158 257 GLY 159 258 ILE 160 259 GLN 161 260 SER 162 261 LEU 163 262 TYR 164 263 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 96.34 366 99.37 99.37 1.89e-107 BMRB 6391 mmp12 100.00 165 99.39 99.39 2.67e-115 BMRB 6444 MMP12 96.34 159 98.73 98.73 9.39e-109 BMRB 7415 CAT_DOMAIN 96.34 159 99.37 99.37 3.39e-110 PDB 1JIZ "Crystal Structure Analysis Of Human Macrophage Elastase Mmp- 12" 100.00 166 99.39 99.39 3.79e-115 PDB 1JK3 "Crystal Structure Of Human Mmp-12 (Macrophage Elastase) At True Atomic Resolution" 96.34 158 100.00 100.00 8.45e-111 PDB 1OS2 "Ternary Enzyme-Product-Inhibitor Complexes Of Human Mmp12" 96.34 165 98.73 98.73 8.58e-109 PDB 1OS9 "Binary Enzyme-Product Complexes Of Human Mmp12" 96.34 165 98.73 98.73 8.58e-109 PDB 1RMZ "Crystal Structure Of The Catalytic Domain Of Human Mmp12 Complexed With The Inhibitor Nngh At 1.3 A Resolution" 96.34 159 98.73 98.73 9.39e-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" 96.34 163 99.37 99.37 4.68e-110 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" 96.34 159 99.37 99.37 4.50e-110 PDB 1UTZ "Crystal Structure Of Mmp-12 Complexed To (2r)-3-({[4-[(Pyri Din-4-Yl)phenyl]-Thien-2-Yl}carboxamido)(Phenyl)propanoic Acid" 96.34 159 99.37 99.37 4.50e-110 PDB 1Y93 "Crystal Structure Of The Catalytic Domain Of Human Mmp12 Complexed With Acetohydroxamic Acid At Atomic Resolution" 96.34 159 98.73 98.73 9.39e-109 PDB 1YCM "Solution Structure Of Matrix Metalloproteinase 12 (Mmp12) In The Presence Of N-Isobutyl-N-[4- Methoxyphenylsulfonyl]glycyl Hydr" 96.34 159 98.73 98.73 9.39e-109 PDB 1Z3J "Solution Structure Of Mmp12 In The Presence Of N-Isobutyl-N- 4-Methoxyphenylsulfonyl]glycyl Hydroxamic Acid (Nngh)" 96.34 159 98.73 98.73 9.39e-109 PDB 2HU6 "Crystal Structure Of Human Mmp-12 In Complex With Acetohydroxamic Acid And A Bicyclic Inhibitor" 96.34 159 98.73 98.73 9.39e-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 99.39 99.39 2.67e-115 PDB 2K9C "Paramagnetic Shifts In Solid-State Nmr Of Proteins To Elicit Structural Information" 92.68 152 98.68 98.68 2.01e-103 PDB 2KRJ "High-Resolution Solid-State Nmr Structure Of A 17.6 Kda Prot" 92.68 152 98.68 98.68 2.01e-103 PDB 2MLR "Membrane Bilayer Complex With Matrix Metalloproteinase-12 At Its Alpha-face" 100.00 164 100.00 100.00 6.87e-116 PDB 2MLS "Membrane Bilayer Complex With Matrix Metalloproteinase-12 At Its Beta- Face" 100.00 164 100.00 100.00 6.87e-116 PDB 2OXU "Uninhibited Form Of Human Mmp-12" 96.34 159 98.73 98.73 9.39e-109 PDB 2OXW "Human Mmp-12 Complexed With The Peptide Iag" 96.34 159 98.73 98.73 9.39e-109 PDB 2OXZ "Human Mmp-12 In Complex With Two Peptides Pqg And Iag" 96.34 159 98.73 98.73 9.39e-109 PDB 2POJ "Nmr Solution Structure Of The Inhibitor-Free State Of Macrophage Metalloelastase (Mmp-12)" 100.00 164 100.00 100.00 6.87e-116 PDB 2W0D "Does A Fast Nuclear Magnetic Resonance Spectroscopy- And X-Ray Crystallography Hybrid Approach Provide Reliable Structural Info" 96.34 164 100.00 100.00 2.16e-110 PDB 2WO8 "Mmp12 Complex With A Beta Hydroxy Carboxylic Acid" 96.34 164 99.37 99.37 4.63e-110 PDB 2WO9 "Mmp12 Complex With A Beta Hydroxy Carboxylic Acid" 96.34 164 99.37 99.37 4.63e-110 PDB 2WOA "Mmp12 Complex With A Beta Hydroxy Carboxylic Acid" 96.34 164 99.37 99.37 4.63e-110 PDB 2Z2D "Solution Structure Of Human Macrophage Elastase (Mmp-12) Catalytic Domain Complexed With A Gamma-Keto Butanoic Acid Inhibitor" 100.00 164 99.39 99.39 2.81e-115 PDB 3BA0 "Crystal Structure Of Full-Length Human Mmp-12" 96.34 365 98.73 98.73 6.47e-107 PDB 3EHX "Crystal Structure Of The Catalytic Domain Of Human Mmp12 Complexed With The Inhibitor (R)-2-(Biphenyl-4- Ylsulfonamido)-4-Methy" 96.34 158 98.73 98.73 1.12e-108 PDB 3EHY "Crystal Structure Of The Catalytic Domain Of Human Mmp12 Complexed With The Inhibitor (R)-2-(4- Methoxyphenylsulfonamido)propan" 96.34 158 98.73 98.73 1.12e-108 PDB 3F15 "Crystal Structure Of The Catalytic Domain Of Human Mmp12 Complexed With The Inhibitor (S)-N-(2,3-Dihydroxypropyl)-4- Methoxy-N-" 96.34 158 98.73 98.73 1.12e-108 PDB 3F16 "Crystal Structure Of The Catalytic Domain Of Human Mmp12 Complexed With The Inhibitor (R)-N-(3-Hydroxy-1-Nitroso-1- Oxopropan-2" 96.34 158 98.73 98.73 1.12e-108 PDB 3F17 "Crystal Structure Of The Catalytic Domain Of Human Mmp12 Complexed With The Inhibitor N-(2-Nitroso-2-Oxoethyl) Biphenyl-4-Sulfo" 96.34 158 98.73 98.73 1.12e-108 PDB 3F18 "Crystal Structure Of The Catalytic Domain Of Human Mmp12 Complexed With The Inhibitor 4-Fluoro-N-(2-Hydroxyethyl)-N- (2-Nitroso" 96.34 158 98.73 98.73 1.12e-108 PDB 3F19 "Crystal Structure Of The Catalytic Domain Of Human Mmp12 Complexed With The Inhibitor 4-Fluoro-N-(2-Nitroso-2- Oxoethyl)benzene" 96.34 158 98.73 98.73 1.12e-108 PDB 3F1A "Crystal Structure Of The Catalytic Domain Of Human Mmp12 Complexed With The Inhibitor N-(2-Nitroso-2-Oxoethyl) Benzenesulfonami" 96.34 158 98.73 98.73 1.12e-108 PDB 3LIK "Human Mmp12 In Complex With Non-Zinc Chelating Inhibitor" 96.34 159 98.73 98.73 9.39e-109 PDB 3LIL "Human Mmp12 In Complex With Non-Zinc Chelating Inhibitor" 96.34 159 98.73 98.73 9.39e-109 PDB 3LIR "Human Mmp12 In Complex With Non-Zinc Chelating Inhibitor" 96.34 159 98.73 98.73 9.39e-109 PDB 3LJG "Human Mmp12 In Complex With Non-Zinc Chelating Inhibitor" 96.34 159 98.73 98.73 9.39e-109 PDB 3LK8 "Crystal Structure Of The Catalytic Domain Of Human Mmp12 Complexed With The Inhibitor Paramethoxy-Sulfonyl-Glycine Hydroxamate" 96.34 158 98.73 98.73 1.12e-108 PDB 3LKA "Catalytic Domain Of Human Mmp-12 Complexed With Hydroxamic Acid And Paramethoxy-Sulfonyl Amide" 96.34 158 98.73 98.73 1.12e-108 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" 96.34 158 98.73 98.73 1.12e-108 PDB 3N2V "Crystal Structure Of The Catalytic Domain Of Human Mmp12 Complexed With The Inhibitor N-Hydroxy-2-(N-Hydroxyethyl)biphenyl-4- Y" 96.34 158 98.73 98.73 1.12e-108 PDB 3NX7 "Crystal Structure Of The Catalytic Domain Of Human Mmp12 Complexed With The Inhibitor N-Hydroxy-2-(N-(2-Hydroxyethyl)4- Methoxy" 96.34 158 98.73 98.73 1.12e-108 PDB 3RTS "Human Mmp-12 Catalytic Domain In Complex WithN-Hydroxy-2-(2- Phenylethylsulfonamido)acetamide" 96.34 158 98.73 98.73 1.12e-108 PDB 3RTT "Human Mmp-12 Catalytic Domain In Complex With(R)-N-Hydroxy-1- (Phenethylsulfonyl)pyrrolidine-2-Carboxamide" 96.34 158 98.73 98.73 1.12e-108 PDB 3TS4 "Human Mmp12 In Complex With L-Glutamate Motif Inhibitor" 96.34 159 98.73 98.73 9.39e-109 PDB 3TSK "Human Mmp12 In Complex With L-Glutamate Motif Inhibitor" 96.34 159 98.73 98.73 9.39e-109 PDB 3UVC "Mmp12 In A Complex With The Dimeric Adduct: 5-(5-Phenylhydantoin)-5- Phenylhydantoin" 96.34 164 100.00 100.00 2.16e-110 PDB 4EFS "Human Mmp12 In Complex With L-Glutamate Motif Inhibitor" 96.34 159 98.73 98.73 9.39e-109 PDB 4GQL "Crystal Structure Of The Catalytic Domain Of Human Mmp12 In Complex With Selective Phosphinic Inhibitor Rxp470.1" 96.34 159 98.73 98.73 9.39e-109 PDB 4GR0 "Crystal Structure Of The Catalytic Domain Of Human Mmp12 In Complex With Selective Phosphinic Inhibitor Rxp470b" 96.34 159 98.73 98.73 9.39e-109 PDB 4GR3 "Crystal Structure Of The Catalytic Domain Of Human Mmp12 In Complex With Selective Phosphinic Inhibitor Rxp470a" 96.34 159 98.73 98.73 9.39e-109 PDB 4GR8 "Crystal Structure Of The Catalytic Domain Of Human Mmp12 In Complex With Selective Phosphinic Inhibitor Rxp470c" 92.68 152 98.68 98.68 1.51e-103 PDB 4GUY "Human Mmp12 Catalytic Domain In Complex WithN-Hydroxy-2-(2-(4- Methoxyphenyl)ethylsulfonamido)acetamide" 96.34 158 98.73 98.73 1.12e-108 PDB 4H30 "Crystal Structure Of The Catalytic Domain Of Mmp-12 In Complex With A Twin Inhibitor." 96.34 159 98.73 98.73 9.39e-109 PDB 4H49 "Crystal Structure Of The Catalytic Domain Of Mmp-12 In Complex With A Twin Inhibitor." 96.34 159 98.73 98.73 9.39e-109 PDB 4H76 "Crystal Structure Of The Catalytic Domain Of Human Mmp12 In Complex With A Broad Spectrum Hydroxamate Inhibitor" 96.34 159 98.73 98.73 9.39e-109 PDB 4H84 "Crystal Structure Of The Catalytic Domain Of Human Mmp12 In Complex With A Selective Carboxylate Based Inhibitor" 96.34 159 98.73 98.73 9.39e-109 PDB 4I03 "Human Mmp12 In Complex With A Peg-linked Bifunctional L-glutamate Motif Inhibitor" 96.34 159 99.37 99.37 1.67e-109 PDB 4IJO "Unraveling Hidden Allosteric Regulatory Sites In Structurally Homologues Metalloproteases" 96.34 158 98.73 98.73 1.12e-108 DBJ BAG36675 "unnamed protein product [Homo sapiens]" 100.00 470 99.39 99.39 4.03e-113 DBJ BAJ20684 "matrix metallopeptidase 12 [synthetic construct]" 100.00 470 99.39 99.39 4.03e-113 GB AAA58658 "metalloproteinase [Homo sapiens]" 100.00 470 99.39 99.39 4.03e-113 GB AAI12302 "Matrix metalloproteinase 12, preproprotein [Homo sapiens]" 100.00 470 99.39 99.39 4.03e-113 GB AAI43774 "Matrix metallopeptidase 12 (macrophage elastase) [Homo sapiens]" 100.00 470 99.39 99.39 3.78e-113 GB AAW29944 "matrix metalloproteinase 12 (macrophage elastase) [Homo sapiens]" 100.00 470 99.39 99.39 4.03e-113 GB ADR83017 "matrix metallopeptidase 12 (macrophage elastase) [synthetic construct]" 100.00 470 99.39 99.39 4.03e-113 REF NP_002417 "macrophage metalloelastase preproprotein [Homo sapiens]" 100.00 470 99.39 99.39 4.03e-113 REF XP_003828422 "PREDICTED: macrophage metalloelastase [Pan paniscus]" 100.00 470 99.39 99.39 3.14e-113 REF XP_004052087 "PREDICTED: macrophage metalloelastase [Gorilla gorilla gorilla]" 100.00 470 99.39 99.39 3.74e-113 REF XP_508724 "PREDICTED: macrophage metalloelastase [Pan troglodytes]" 100.00 470 99.39 99.39 3.14e-113 SP P39900 "RecName: Full=Macrophage metalloelastase; Short=MME; AltName: Full=Macrophage elastase; Short=ME; Short=hME; AltName: Full=Matr" 100.00 470 99.39 99.39 4.03e-113 stop_ save_ ############# # Ligands # ############# save_ZN _Saveframe_category ligand _Mol_type non-polymer _Name_common "ZN (ZINC ION)" _BMRB_code . _PDB_code ZN _Molecular_mass 65.409 _Mol_charge 2 _Mol_paramagnetic . _Mol_aromatic no _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Fri Sep 30 15:25:14 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons ZN ZN ZN . 2 . ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ save_CA _Saveframe_category ligand _Mol_type non-polymer _Name_common "CA (CALCIUM ION)" _BMRB_code . _PDB_code CA _Molecular_mass 40.078 _Mol_charge 2 _Mol_paramagnetic . _Mol_aromatic no _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Fri Sep 30 15:25:44 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons CA CA CA . 2 . ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Metalloprotease 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 _Vendor_name _Details $Metalloprotease 'recombinant technology' 'E. coli' . . 'BL21 (DE3) RIL' Plasmid pGEXMEX-1 Promega ; 1) Foreign linker residues 'MSA' present at N-terminal end of coding frame from sub-cloning. These 3 residues could be lost from gradual autoproteolysis. 2) A Glu 219 Ala substitution was used to inactivate MMP-12's autoproteolysis without altering the structure of the protease ; 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 $assembly 0.55 mM '[U-13C; U-15N]' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $assembly 0.45 mM [U-15N] stop_ save_ ############################ # Computer software used # ############################ save_software_1 _Saveframe_category software _Name NMRPipe _Version 2.3 loop_ _Task 'Processing Spectra' stop_ _Details ; F. Delaglio, S.Grzesick, G. W. Vuister, G, Zhu, J. Pfeifer and A. Bax, (1995) J. Biomol. NMR 6, 277-293. ; save_ save_software_2 _Saveframe_category software _Name SPARKY _Version 3.106 loop_ _Task Assignment 'Peak Picking' stop_ _Details ; T.D. Goddard and D.G. Kneller, SPARKY 3, University of California, San Francisco, USA ; save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_600MHz_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details ; Triple Resonance Single-axis gradient Cryoprobe for most experiments ; save_ save_500MHz_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 500 _Details 'Triple Resonance experiments' save_ ############################# # NMR applied experiments # ############################# save_1H15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H15N HSQC' _Sample_label . save_ save_1H13C_HSQC_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H13C HSQC' _Sample_label . save_ save_HNCO_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label . save_ save_HNCA_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label . save_ save_CBCACONH_5 _Saveframe_category NMR_applied_experiment _Experiment_name CBCACONH _Sample_label . save_ save_HNCACB_6 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label . save_ save_HACACONH_7 _Saveframe_category NMR_applied_experiment _Experiment_name HACACONH _Sample_label . save_ save_HNNCAHA_8 _Saveframe_category NMR_applied_experiment _Experiment_name HNNCAHA _Sample_label . save_ save_CCONH_9 _Saveframe_category NMR_applied_experiment _Experiment_name CCONH _Sample_label . save_ save_HCCONH_10 _Saveframe_category NMR_applied_experiment _Experiment_name HCCONH _Sample_label . save_ save_HCACOCANH_11 _Saveframe_category NMR_applied_experiment _Experiment_name HCACOCANH _Sample_label . save_ save_HCCHTOCSY_12 _Saveframe_category NMR_applied_experiment _Experiment_name HCCHTOCSY _Sample_label . save_ save_CCHTOCSY_13 _Saveframe_category NMR_applied_experiment _Experiment_name CCHTOCSY _Sample_label . save_ save_HBCBCGCDHD(CEHE)_14 _Saveframe_category NMR_applied_experiment _Experiment_name HBCBCGCDHD(CEHE) _Sample_label . save_ save_15N_ed_3D_NOESY_HSQC_15 _Saveframe_category NMR_applied_experiment _Experiment_name '15N ed 3D NOESY HSQC' _Sample_label . save_ save_13C_ed_3D_NOESY_HSQC_16 _Saveframe_category NMR_applied_experiment _Experiment_name '13C ed 3D NOESY HSQC' _Sample_label . save_ ####################### # Sample conditions # ####################### save_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.6 0.05 pH temperature 299 1 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 DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 $citation_1 $citation_1 DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 $citation_1 $citation_1 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 $citation_1 $citation_1 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 . loop_ _Software_label $software_1 $software_2 stop_ loop_ _Experiment_label '1H15N HSQC' '1H13C HSQC' HNCO HNCA CBCACONH HNCACB HACACONH HNNCAHA CCONH HCCONH HCACOCANH HCCHTOCSY CCHTOCSY HBCBCGCDHD(CEHE) '15N ed 3D NOESY HSQC' '13C ed 3D NOESY HSQC' stop_ loop_ _Sample_label $sample_2 $sample_1 stop_ _Sample_conditions_label $conditions_1 _Chem_shift_reference_set_label $chemical_shift_referencing _Mol_system_component_name Metalloprotease _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 1 101 2 ARG H H 9.060 0.04 1 2 101 2 ARG HA H 4.550 0.04 1 3 101 2 ARG HB2 H 1.820 0.04 2 4 101 2 ARG HG3 H 1.670 0.04 2 5 101 2 ARG HD2 H 3.110 0.04 2 6 101 2 ARG C C 175.600 0.30 1 7 101 2 ARG CA C 57.880 0.30 1 8 101 2 ARG CB C 29.530 0.30 1 9 101 2 ARG CG C 26.900 0.30 1 10 101 2 ARG CD C 41.500 0.30 1 11 101 2 ARG N N 118.080 0.40 1 12 102 3 GLU H H 8.950 0.04 1 13 102 3 GLU HA H 4.220 0.04 1 14 102 3 GLU HB2 H 1.570 0.04 2 15 102 3 GLU HG2 H 2.360 0.04 2 16 102 3 GLU C C 173.300 0.30 1 17 102 3 GLU CA C 61.720 0.30 1 18 102 3 GLU CB C 35.300 0.30 1 19 102 3 GLU CG C 39.600 0.30 1 20 102 3 GLU N N 124.230 0.40 1 21 103 4 MET H H 7.620 0.04 1 22 103 4 MET HA H 4.690 0.04 1 23 103 4 MET HB2 H 1.470 0.04 2 24 103 4 MET HB3 H 1.690 0.04 2 25 103 4 MET CA C 53.600 0.30 1 26 103 4 MET CE C 19.000 0.30 1 27 103 4 MET N N 130.090 0.40 1 28 104 5 PRO HA H 4.350 0.04 1 29 104 5 PRO HB3 H 2.310 0.04 2 30 104 5 PRO HG3 H 1.990 0.04 2 31 104 5 PRO HD3 H 3.700 0.04 2 32 104 5 PRO C C 177.400 0.30 1 33 104 5 PRO CA C 63.540 0.30 1 34 104 5 PRO CB C 32.450 0.30 1 35 104 5 PRO CG C 27.400 0.30 1 36 104 5 PRO CD C 47.600 0.30 1 37 105 6 GLY H H 8.420 0.04 1 38 105 6 GLY HA2 H 4.380 0.04 2 39 105 6 GLY HA3 H 3.920 0.04 2 40 105 6 GLY CA C 45.360 0.30 1 41 105 6 GLY N N 109.410 0.40 1 42 106 7 GLY H H 7.960 0.04 1 43 106 7 GLY HA2 H 4.090 0.04 2 44 106 7 GLY HA3 H 3.890 0.04 2 45 106 7 GLY CA C 44.490 0.30 1 46 106 7 GLY N N 108.230 0.40 1 47 107 8 PRO HA H 3.830 0.04 1 48 107 8 PRO HB2 H 2.220 0.04 2 49 107 8 PRO HB3 H 2.000 0.04 2 50 107 8 PRO HG3 H 1.750 0.04 2 51 107 8 PRO HD2 H 3.600 0.04 2 52 107 8 PRO HD3 H 3.490 0.04 2 53 107 8 PRO CA C 64.520 0.30 1 54 107 8 PRO CB C 35.000 0.30 1 55 108 9 VAL H H 7.010 0.04 1 56 108 9 VAL HA H 4.630 0.04 1 57 108 9 VAL HB H 1.740 0.04 1 58 108 9 VAL HG1 H 0.690 0.04 2 59 108 9 VAL HG2 H 0.600 0.04 2 60 108 9 VAL CA C 59.040 0.30 1 61 108 9 VAL N N 109.090 0.40 1 62 109 10 TRP HB2 H 2.810 0.04 2 63 109 10 TRP HB3 H 2.950 0.04 2 64 109 10 TRP HD1 H 7.200 0.04 1 65 109 10 TRP HE1 H 10.100 0.04 1 66 109 10 TRP HE3 H 7.800 0.04 1 67 109 10 TRP HZ2 H 7.430 0.04 1 68 109 10 TRP HH2 H 7.190 0.04 1 69 109 10 TRP CB C 27.000 0.30 1 70 109 10 TRP CD1 C 122.500 0.30 1 71 109 10 TRP CE3 C 119.000 0.30 1 72 109 10 TRP CZ2 C 112.000 0.30 1 73 109 10 TRP CH2 C 122.300 0.30 1 74 109 10 TRP NE1 N 130.000 0.40 1 75 110 11 ARG H H 8.550 0.04 1 76 110 11 ARG HA H 4.560 0.04 1 77 110 11 ARG HB2 H 1.720 0.04 2 78 110 11 ARG HG3 H 1.560 0.04 2 79 110 11 ARG HD2 H 2.970 0.04 2 80 110 11 ARG HD3 H 3.170 0.04 2 81 110 11 ARG C C 176.500 0.30 1 82 110 11 ARG CA C 55.600 0.30 1 83 110 11 ARG CB C 28.800 0.30 1 84 110 11 ARG CG C 27.300 0.30 1 85 110 11 ARG CD C 43.300 0.30 1 86 110 11 ARG N N 118.180 0.40 1 87 111 12 LYS H H 7.530 0.04 1 88 111 12 LYS HA H 4.540 0.04 1 89 111 12 LYS HB2 H 1.970 0.04 2 90 111 12 LYS HB3 H 2.130 0.04 2 91 111 12 LYS HG2 H 1.190 0.04 2 92 111 12 LYS HG3 H 1.400 0.04 2 93 111 12 LYS HD3 H 1.750 0.04 2 94 111 12 LYS HE3 H 3.470 0.04 2 95 111 12 LYS C C 174.100 0.30 1 96 111 12 LYS CA C 54.530 0.30 1 97 111 12 LYS CB C 26.800 0.30 1 98 111 12 LYS CG C 22.500 0.30 1 99 111 12 LYS CD C 27.600 0.30 1 100 111 12 LYS N N 115.550 0.40 1 101 112 13 HIS H H 8.390 0.04 1 102 112 13 HIS HA H 4.820 0.04 1 103 112 13 HIS HB2 H 3.310 0.04 2 104 112 13 HIS HB3 H 2.800 0.04 2 105 112 13 HIS HD2 H 6.680 0.04 1 106 112 13 HIS HE1 H 8.110 0.04 1 107 112 13 HIS C C 173.300 0.30 1 108 112 13 HIS CA C 54.600 0.30 1 109 112 13 HIS CB C 31.500 0.30 1 110 112 13 HIS CD2 C 114.300 0.30 1 111 112 13 HIS CE1 C 136.300 0.30 1 112 112 13 HIS N N 114.390 0.40 1 113 113 14 TYR H H 7.000 0.04 1 114 113 14 TYR HA H 4.540 0.04 1 115 113 14 TYR HB2 H 2.860 0.04 2 116 113 14 TYR HB3 H 2.740 0.04 2 117 113 14 TYR HD1 H 7.170 0.04 1 118 113 14 TYR HE1 H 6.690 0.04 1 119 113 14 TYR C C 173.900 0.30 1 120 113 14 TYR CA C 56.850 0.30 1 121 113 14 TYR CB C 38.640 0.30 1 122 113 14 TYR CD1 C 131.100 0.30 1 123 113 14 TYR CE1 C 116.100 0.30 1 124 113 14 TYR N N 120.160 0.40 1 125 114 15 ILE H H 8.320 0.04 1 126 114 15 ILE HA H 4.180 0.04 1 127 114 15 ILE HB H 2.220 0.04 1 128 114 15 ILE HG12 H 1.370 0.04 2 129 114 15 ILE HG13 H 1.100 0.04 2 130 114 15 ILE HG2 H 0.750 0.04 1 131 114 15 ILE HD1 H 0.420 0.04 1 132 114 15 ILE C C 175.400 0.30 1 133 114 15 ILE CA C 59.030 0.30 1 134 114 15 ILE CB C 40.830 0.30 1 135 114 15 ILE CG1 C 27.900 0.30 1 136 114 15 ILE CG2 C 17.000 0.30 1 137 114 15 ILE N N 128.600 0.40 1 138 115 16 THR H H 9.270 0.04 1 139 115 16 THR HA H 5.320 0.04 1 140 115 16 THR HB H 4.110 0.04 1 141 115 16 THR HG2 H 1.100 0.04 1 142 115 16 THR C C 174.600 0.30 1 143 115 16 THR CA C 58.900 0.30 1 144 115 16 THR CB C 72.400 0.30 1 145 115 16 THR CG2 C 22.100 0.30 1 146 115 16 THR N N 117.430 0.40 1 147 116 17 TYR H H 8.660 0.04 1 148 116 17 TYR HA H 5.860 0.04 1 149 116 17 TYR HB2 H 2.960 0.04 2 150 116 17 TYR HB3 H 2.330 0.04 2 151 116 17 TYR HD1 H 6.890 0.04 1 152 116 17 TYR HE1 H 6.850 0.04 1 153 116 17 TYR C C 171.900 0.30 1 154 116 17 TYR CA C 55.190 0.30 1 155 116 17 TYR CB C 43.640 0.30 1 156 116 17 TYR CD1 C 129.600 0.30 1 157 116 17 TYR CE1 C 116.200 0.30 1 158 116 17 TYR N N 117.440 0.40 1 159 117 18 ARG H H 8.360 0.04 1 160 117 18 ARG HA H 4.700 0.04 1 161 117 18 ARG HB2 H 1.770 0.04 2 162 117 18 ARG HG3 H 1.530 0.04 2 163 117 18 ARG HD2 H 3.030 0.04 2 164 117 18 ARG C C 174.200 0.30 1 165 117 18 ARG CA C 54.740 0.30 1 166 117 18 ARG CB C 35.790 0.30 1 167 117 18 ARG CG C 27.000 0.30 1 168 117 18 ARG CD C 43.900 0.30 1 169 117 18 ARG N N 119.030 0.40 1 170 118 19 ILE H H 9.180 0.04 1 171 118 19 ILE HA H 4.340 0.04 1 172 118 19 ILE HB H 2.170 0.04 1 173 118 19 ILE HG12 H 1.760 0.04 2 174 118 19 ILE HG13 H 1.570 0.04 2 175 118 19 ILE HG2 H 0.990 0.04 1 176 118 19 ILE HD1 H 0.870 0.04 1 177 118 19 ILE C C 175.200 0.30 1 178 118 19 ILE CA C 61.550 0.30 1 179 118 19 ILE CB C 37.120 0.30 1 180 118 19 ILE CG1 C 28.000 0.30 1 181 118 19 ILE CG2 C 16.900 0.30 1 182 118 19 ILE N N 127.200 0.40 1 183 119 20 ASN H H 9.690 0.04 1 184 119 20 ASN HA H 4.340 0.04 1 185 119 20 ASN HB2 H 3.090 0.04 2 186 119 20 ASN HB3 H 2.530 0.04 2 187 119 20 ASN HD21 H 7.600 0.04 2 188 119 20 ASN HD22 H 6.990 0.04 2 189 119 20 ASN C C 173.900 0.30 1 190 119 20 ASN CA C 56.530 0.30 1 191 119 20 ASN CB C 41.990 0.30 1 192 119 20 ASN N N 128.510 0.40 1 193 119 20 ASN ND2 N 111.400 0.40 1 194 120 21 ASN H H 7.820 0.04 1 195 120 21 ASN HA H 4.670 0.04 1 196 120 21 ASN HB2 H 2.940 0.04 2 197 120 21 ASN HB3 H 3.080 0.04 2 198 120 21 ASN HD21 H 7.540 0.04 2 199 120 21 ASN HD22 H 7.050 0.04 2 200 120 21 ASN C C 169.800 0.30 1 201 120 21 ASN CA C 52.080 0.30 1 202 120 21 ASN CB C 39.030 0.30 1 203 120 21 ASN N N 113.290 0.40 1 204 120 21 ASN ND2 N 114.200 0.40 1 205 121 22 TYR H H 8.580 0.04 1 206 121 22 TYR HA H 4.110 0.04 1 207 121 22 TYR HB2 H 2.850 0.04 2 208 121 22 TYR HB3 H 2.600 0.04 2 209 121 22 TYR HD1 H 6.950 0.04 1 210 121 22 TYR HE1 H 6.850 0.04 1 211 121 22 TYR C C 176.300 0.30 1 212 121 22 TYR CA C 58.650 0.30 1 213 121 22 TYR CB C 41.170 0.30 1 214 121 22 TYR CD1 C 131.200 0.30 1 215 121 22 TYR CE1 C 115.900 0.30 1 216 121 22 TYR N N 114.590 0.40 1 217 123 24 PRO HA H 4.640 0.04 1 218 123 24 PRO HB2 H 2.110 0.04 2 219 123 24 PRO HB3 H 2.250 0.04 2 220 123 24 PRO HG2 H 1.930 0.04 2 221 123 24 PRO HG3 H 2.070 0.04 2 222 123 24 PRO HD2 H 3.590 0.04 2 223 123 24 PRO HD3 H 3.420 0.04 2 224 123 24 PRO CA C 63.000 0.30 1 225 123 24 PRO CB C 32.000 0.30 1 226 123 24 PRO CG C 27.300 0.30 1 227 123 24 PRO CD C 49.900 0.30 1 228 124 25 ASP H H 8.830 0.04 1 229 124 25 ASP HA H 4.100 0.04 1 230 124 25 ASP HB2 H 2.760 0.04 2 231 124 25 ASP HB3 H 2.550 0.04 2 232 124 25 ASP C C 175.900 0.30 1 233 124 25 ASP CA C 56.180 0.30 1 234 124 25 ASP CB C 41.800 0.30 1 235 124 25 ASP N N 121.860 0.40 1 236 125 26 MET H H 6.970 0.04 1 237 125 26 MET HA H 4.620 0.04 1 238 125 26 MET HB2 H 2.090 0.04 2 239 125 26 MET HB3 H 1.770 0.04 2 240 125 26 MET HG3 H 2.270 0.04 2 241 125 26 MET HE H 1.400 0.04 1 242 125 26 MET C C 174.900 0.30 1 243 125 26 MET CA C 53.650 0.30 1 244 125 26 MET CB C 39.350 0.30 1 245 125 26 MET CG C 31.900 0.30 1 246 125 26 MET CE C 20.800 0.30 1 247 125 26 MET N N 113.330 0.40 1 248 126 27 ASN H H 8.930 0.04 1 249 126 27 ASN HA H 4.610 0.04 1 250 126 27 ASN HB2 H 2.620 0.04 2 251 126 27 ASN HB3 H 2.860 0.04 2 252 126 27 ASN HD21 H 7.470 0.04 2 253 126 27 ASN HD22 H 6.840 0.04 2 254 126 27 ASN C C 177.300 0.30 1 255 126 27 ASN CA C 53.500 0.30 1 256 126 27 ASN CB C 38.650 0.30 1 257 126 27 ASN N N 118.800 0.40 1 258 126 27 ASN ND2 N 112.100 0.40 1 259 127 28 ARG H H 8.980 0.04 1 260 127 28 ARG HA H 4.760 0.04 1 261 127 28 ARG HB2 H 1.460 0.04 2 262 127 28 ARG HB3 H 1.360 0.04 2 263 127 28 ARG HG2 H 1.000 0.04 2 264 127 28 ARG HD2 H 3.760 0.04 2 265 127 28 ARG C C 178.000 0.30 1 266 127 28 ARG CA C 60.530 0.30 1 267 127 28 ARG CB C 30.250 0.30 1 268 127 28 ARG CG C 26.600 0.30 1 269 127 28 ARG CD C 43.600 0.30 1 270 127 28 ARG N N 126.020 0.40 1 271 128 29 GLU H H 9.090 0.04 1 272 128 29 GLU HA H 4.130 0.04 1 273 128 29 GLU HB2 H 2.000 0.04 2 274 128 29 GLU HB3 H 1.940 0.04 2 275 128 29 GLU HG2 H 2.330 0.04 2 276 128 29 GLU C C 179.400 0.30 1 277 128 29 GLU CA C 59.700 0.30 1 278 128 29 GLU CB C 28.800 0.30 1 279 128 29 GLU CG C 36.300 0.30 1 280 128 29 GLU N N 116.400 0.40 1 281 129 30 ASP H H 7.500 0.04 1 282 129 30 ASP HA H 4.660 0.04 1 283 129 30 ASP HB2 H 2.630 0.04 2 284 129 30 ASP HB3 H 2.860 0.04 2 285 129 30 ASP C C 179.200 0.30 1 286 129 30 ASP CA C 57.230 0.30 1 287 129 30 ASP CB C 41.800 0.30 1 288 129 30 ASP N N 119.790 0.40 1 289 130 31 VAL H H 7.790 0.04 1 290 130 31 VAL HA H 4.130 0.04 1 291 130 31 VAL HB H 2.320 0.04 1 292 130 31 VAL HG1 H 0.990 0.04 2 293 130 31 VAL HG2 H 0.800 0.04 2 294 130 31 VAL C C 177.400 0.30 1 295 130 31 VAL CA C 66.960 0.30 1 296 130 31 VAL CB C 31.450 0.30 1 297 130 31 VAL CG1 C 24.100 0.30 1 298 130 31 VAL CG2 C 21.500 0.30 1 299 130 31 VAL N N 123.990 0.40 1 300 131 32 ASP H H 8.420 0.04 1 301 131 32 ASP HA H 4.360 0.04 1 302 131 32 ASP HB2 H 2.820 0.04 2 303 131 32 ASP HB3 H 2.630 0.04 2 304 131 32 ASP C C 179.700 0.30 1 305 131 32 ASP CA C 58.080 0.30 1 306 131 32 ASP CB C 40.600 0.30 1 307 131 32 ASP N N 118.590 0.40 1 308 132 33 TYR H H 8.230 0.04 1 309 132 33 TYR HA H 4.200 0.04 1 310 132 33 TYR HB2 H 3.120 0.04 2 311 132 33 TYR HB3 H 3.310 0.04 2 312 132 33 TYR HD1 H 6.970 0.04 1 313 132 33 TYR HE1 H 6.730 0.04 1 314 132 33 TYR C C 176.300 0.30 1 315 132 33 TYR CA C 61.720 0.30 1 316 132 33 TYR CB C 38.860 0.30 1 317 132 33 TYR CD1 C 131.100 0.30 1 318 132 33 TYR CE1 C 116.120 0.30 1 319 132 33 TYR N N 119.720 0.40 1 320 133 34 ALA H H 8.080 0.04 1 321 133 34 ALA HA H 3.920 0.04 1 322 133 34 ALA HB H 1.500 0.04 1 323 133 34 ALA C C 179.400 0.30 1 324 133 34 ALA CA C 55.720 0.30 1 325 133 34 ALA CB C 18.800 0.30 1 326 133 34 ALA N N 121.470 0.40 1 327 134 35 ILE H H 8.090 0.04 1 328 134 35 ILE HA H 3.530 0.04 1 329 134 35 ILE HB H 2.170 0.04 1 330 134 35 ILE HG12 H 1.640 0.04 2 331 134 35 ILE HG13 H 1.500 0.04 2 332 134 35 ILE HG2 H 0.780 0.04 1 333 134 35 ILE HD1 H 0.320 0.04 1 334 134 35 ILE C C 177.300 0.30 1 335 134 35 ILE CA C 62.220 0.30 1 336 134 35 ILE CB C 35.740 0.30 1 337 134 35 ILE CG1 C 27.600 0.30 1 338 134 35 ILE CG2 C 19.100 0.30 1 339 134 35 ILE N N 114.080 0.40 1 340 135 36 ARG H H 8.290 0.04 1 341 135 36 ARG HA H 4.130 0.04 1 342 135 36 ARG HB2 H 1.780 0.04 2 343 135 36 ARG HB3 H 2.060 0.04 2 344 135 36 ARG HG2 H 1.620 0.04 2 345 135 36 ARG HG3 H 1.520 0.04 2 346 135 36 ARG HD2 H 3.330 0.04 2 347 135 36 ARG C C 179.800 0.30 1 348 135 36 ARG CA C 60.310 0.30 1 349 135 36 ARG CB C 30.540 0.30 1 350 135 36 ARG CG C 27.200 0.30 1 351 135 36 ARG CD C 44.100 0.30 1 352 135 36 ARG N N 119.830 0.40 1 353 136 37 LYS H H 8.550 0.04 1 354 136 37 LYS HA H 3.910 0.04 1 355 136 37 LYS HB2 H 2.270 0.04 2 356 136 37 LYS HB3 H 2.510 0.04 2 357 136 37 LYS HG3 H 1.290 0.04 2 358 136 37 LYS HD2 H 1.540 0.04 2 359 136 37 LYS HE3 H 2.920 0.04 2 360 136 37 LYS C C 178.700 0.30 1 361 136 37 LYS CA C 58.400 0.30 1 362 136 37 LYS CB C 31.560 0.30 1 363 136 37 LYS CG C 24.700 0.30 1 364 136 37 LYS CD C 28.100 0.30 1 365 136 37 LYS CE C 41.800 0.30 1 366 136 37 LYS N N 119.290 0.40 1 367 137 38 ALA H H 8.000 0.04 1 368 137 38 ALA HA H 3.920 0.04 1 369 137 38 ALA HB H 1.100 0.04 1 370 137 38 ALA C C 178.600 0.30 1 371 137 38 ALA CA C 55.650 0.30 1 372 137 38 ALA CB C 19.000 0.30 1 373 137 38 ALA N N 123.200 0.40 1 374 138 39 PHE H H 7.720 0.04 1 375 138 39 PHE HA H 3.750 0.04 1 376 138 39 PHE HB2 H 2.580 0.04 2 377 138 39 PHE HB3 H 2.270 0.04 2 378 138 39 PHE HD1 H 5.600 0.04 1 379 138 39 PHE HE1 H 5.900 0.04 1 380 138 39 PHE HZ H 6.400 0.04 1 381 138 39 PHE C C 178.700 0.30 1 382 138 39 PHE CA C 63.890 0.30 1 383 138 39 PHE CB C 38.670 0.30 1 384 138 39 PHE CD1 C 129.200 0.30 1 385 138 39 PHE CE1 C 127.800 0.30 1 386 138 39 PHE CZ C 124.000 0.30 1 387 138 39 PHE N N 113.900 0.40 1 388 139 40 GLN H H 8.110 0.04 1 389 139 40 GLN HA H 4.190 0.04 1 390 139 40 GLN HB2 H 2.070 0.04 2 391 139 40 GLN HB3 H 2.280 0.04 2 392 139 40 GLN HG2 H 2.460 0.04 2 393 139 40 GLN HG3 H 2.580 0.04 2 394 139 40 GLN HE21 H 6.920 0.04 2 395 139 40 GLN HE22 H 7.620 0.04 2 396 139 40 GLN C C 177.900 0.30 1 397 139 40 GLN CA C 58.540 0.30 1 398 139 40 GLN CB C 28.820 0.30 1 399 139 40 GLN CG C 34.100 0.30 1 400 139 40 GLN N N 119.100 0.40 1 401 139 40 GLN NE2 N 112.600 0.40 1 402 140 41 VAL H H 7.700 0.04 1 403 140 41 VAL HA H 3.630 0.04 1 404 140 41 VAL HB H 2.060 0.04 1 405 140 41 VAL HG1 H 1.120 0.04 2 406 140 41 VAL HG2 H 0.470 0.04 2 407 140 41 VAL C C 178.200 0.30 1 408 140 41 VAL CA C 66.070 0.30 1 409 140 41 VAL CB C 31.300 0.30 1 410 140 41 VAL CG1 C 21.700 0.30 1 411 140 41 VAL CG2 C 23.100 0.30 1 412 140 41 VAL N N 117.170 0.40 1 413 141 42 TRP H H 6.730 0.04 1 414 141 42 TRP HA H 4.370 0.04 1 415 141 42 TRP HB2 H 3.190 0.04 2 416 141 42 TRP HB3 H 3.070 0.04 2 417 141 42 TRP HD1 H 7.360 0.04 1 418 141 42 TRP HE1 H 9.920 0.04 1 419 141 42 TRP HE3 H 6.70 0.04 1 420 141 42 TRP HZ2 H 6.950 0.04 1 421 141 42 TRP HZ3 H 6.870 0.04 1 422 141 42 TRP HH2 H 6.380 0.04 1 423 141 42 TRP C C 180.700 0.30 1 424 141 42 TRP CA C 58.590 0.30 1 425 141 42 TRP CB C 30.420 0.30 1 426 141 42 TRP CD1 C 120.700 0.30 1 427 141 42 TRP CE3 C 119.00 0.30 1 428 141 42 TRP CZ2 C 114.200 0.30 1 429 141 42 TRP CZ3 C 126.00 0.30 1 430 141 42 TRP CH2 C 128.00 0.30 1 431 141 42 TRP N N 116.910 0.40 1 432 141 42 TRP NE1 N 127.600 0.40 1 433 142 43 SER H H 9.080 0.04 1 434 142 43 SER HA H 4.370 0.04 1 435 142 43 SER HB3 H 4.190 0.04 2 436 142 43 SER C C 175.700 0.30 1 437 142 43 SER CA C 61.490 0.30 1 438 142 43 SER CB C 63.720 0.30 1 439 142 43 SER N N 118.490 0.40 1 440 143 44 ASN H H 7.970 0.04 1 441 143 44 ASN HA H 4.730 0.04 1 442 143 44 ASN HB2 H 2.990 0.04 2 443 143 44 ASN HB3 H 2.840 0.04 2 444 143 44 ASN HD21 H 7.960 0.04 2 445 143 44 ASN HD22 H 6.910 0.04 2 446 143 44 ASN C C 176.700 0.30 1 447 143 44 ASN CA C 55.040 0.30 1 448 143 44 ASN CB C 39.210 0.30 1 449 143 44 ASN N N 115.220 0.40 1 450 143 44 ASN ND2 N 114.400 0.40 1 451 144 45 VAL H H 7.170 0.04 1 452 144 45 VAL HA H 4.860 0.04 1 453 144 45 VAL HB H 2.680 0.04 1 454 144 45 VAL HG1 H 1.160 0.04 2 455 144 45 VAL HG2 H 0.940 0.04 2 456 144 45 VAL C C 174.600 0.30 1 457 144 45 VAL CA C 60.440 0.30 1 458 144 45 VAL CB C 32.940 0.30 1 459 144 45 VAL CG1 C 19.200 0.30 1 460 144 45 VAL CG2 C 21.700 0.30 1 461 144 45 VAL N N 106.340 0.40 1 462 145 46 THR H H 7.490 0.04 1 463 145 46 THR HA H 4.370 0.04 1 464 145 46 THR HB H 4.010 0.04 1 465 145 46 THR HG2 H 1.450 0.04 1 466 145 46 THR C C 173.400 0.30 1 467 145 46 THR CA C 59.760 0.30 1 468 145 46 THR CB C 72.630 0.30 1 469 145 46 THR N N 110.440 0.40 1 470 146 47 PRO HA H 4.370 0.04 1 471 146 47 PRO HB3 H 2.740 0.04 2 472 146 47 PRO HG2 H 2.100 0.04 2 473 146 47 PRO HG3 H 1.970 0.04 2 474 146 47 PRO HD2 H 3.310 0.04 2 475 146 47 PRO HD3 H 3.710 0.04 2 476 146 47 PRO C C 176.100 0.30 1 477 146 47 PRO CA C 62.370 0.30 1 478 146 47 PRO CB C 31.100 0.30 1 479 146 47 PRO CG C 26.800 0.30 1 480 146 47 PRO CD C 50.700 0.30 1 481 147 48 LEU H H 7.010 0.04 1 482 147 48 LEU HA H 4.140 0.04 1 483 147 48 LEU HB2 H 1.440 0.04 2 484 147 48 LEU HB3 H 1.330 0.04 2 485 147 48 LEU HG H 1.100 0.04 1 486 147 48 LEU HD1 H 0.470 0.04 2 487 147 48 LEU HD2 H 0.270 0.04 2 488 147 48 LEU C C 176.300 0.30 1 489 147 48 LEU CA C 54.930 0.30 1 490 147 48 LEU CB C 43.230 0.30 1 491 147 48 LEU CG C 27.400 0.30 1 492 147 48 LEU CD1 C 22.000 0.30 1 493 147 48 LEU CD2 C 25.200 0.30 1 494 147 48 LEU N N 116.360 0.40 1 495 148 49 LYS H H 8.250 0.04 1 496 148 49 LYS HA H 4.270 0.04 1 497 148 49 LYS HB3 H 1.620 0.04 2 498 148 49 LYS HG3 H 1.270 0.04 2 499 148 49 LYS HD3 H 1.390 0.04 2 500 148 49 LYS HE3 H 3.310 0.04 2 501 148 49 LYS C C 175.500 0.30 1 502 148 49 LYS CA C 54.300 0.30 1 503 148 49 LYS CB C 35.400 0.30 1 504 148 49 LYS CG C 24.700 0.30 1 505 148 49 LYS CD C 28.900 0.30 1 506 148 49 LYS CE C 42.500 0.30 1 507 148 49 LYS N N 122.800 0.40 1 508 149 50 PHE H H 8.240 0.04 1 509 149 50 PHE HA H 5.700 0.04 1 510 149 50 PHE HB2 H 2.530 0.04 2 511 149 50 PHE HB3 H 2.210 0.04 2 512 149 50 PHE HD1 H 7.160 0.04 1 513 149 50 PHE HE1 H 7.040 0.04 1 514 149 50 PHE HZ H 6.800 0.04 1 515 149 50 PHE C C 176.600 0.30 1 516 149 50 PHE CA C 55.700 0.30 1 517 149 50 PHE CB C 42.070 0.30 1 518 149 50 PHE CD1 C 131.400 0.30 1 519 149 50 PHE CE1 C 130.300 0.30 1 520 149 50 PHE CZ C 126.600 0.30 1 521 149 50 PHE N N 119.370 0.40 1 522 150 51 SER H H 8.100 0.04 1 523 150 51 SER HA H 4.620 0.04 1 524 150 51 SER HB2 H 3.540 0.04 2 525 150 51 SER HB3 H 3.430 0.04 2 526 150 51 SER C C 171.100 0.30 1 527 150 51 SER CA C 56.870 0.30 1 528 150 51 SER CB C 65.800 0.30 1 529 150 51 SER N N 116.770 0.40 1 530 151 52 LYS H H 8.150 0.04 1 531 151 52 LYS HA H 4.590 0.04 1 532 151 52 LYS HB2 H 1.510 0.04 2 533 151 52 LYS HB3 H 1.420 0.04 2 534 151 52 LYS HG3 H 1.120 0.04 2 535 151 52 LYS HD2 H 1.780 0.04 2 536 151 52 LYS HE3 H 3.040 0.04 2 537 151 52 LYS C C 176.600 0.30 1 538 151 52 LYS CA C 55.500 0.30 1 539 151 52 LYS CB C 33.440 0.30 1 540 151 52 LYS CG C 25.000 0.30 1 541 151 52 LYS CD C 30.100 0.30 1 542 151 52 LYS CE C 40.500 0.30 1 543 151 52 LYS N N 127.660 0.40 1 544 152 53 ILE H H 8.750 0.04 1 545 152 53 ILE HA H 4.640 0.04 1 546 152 53 ILE HB H 1.930 0.04 1 547 152 53 ILE HG12 H 1.630 0.04 2 548 152 53 ILE HG13 H 1.120 0.04 2 549 152 53 ILE HG2 H 0.920 0.04 1 550 152 53 ILE HD1 H 0.800 0.04 1 551 152 53 ILE C C 175.400 0.30 1 552 152 53 ILE CA C 59.030 0.30 1 553 152 53 ILE CB C 38.300 0.30 1 554 152 53 ILE CG1 C 32.700 0.30 1 555 152 53 ILE CG2 C 17.300 0.30 1 556 152 53 ILE N N 123.710 0.40 1 557 153 54 ASN H H 8.840 0.04 1 558 153 54 ASN HA H 4.100 0.04 1 559 153 54 ASN HB2 H 2.910 0.04 2 560 153 54 ASN HB3 H 2.720 0.04 2 561 153 54 ASN HD21 H 7.930 0.04 2 562 153 54 ASN HD22 H 6.670 0.04 2 563 153 54 ASN C C 175.100 0.30 1 564 153 54 ASN CA C 53.850 0.30 1 565 153 54 ASN CB C 40.200 0.30 1 566 153 54 ASN N N 119.440 0.40 1 567 153 54 ASN ND2 N 110.000 0.40 1 568 154 55 THR H H 7.480 0.04 1 569 154 55 THR HA H 4.750 0.04 1 570 154 55 THR HB H 4.400 0.04 1 571 154 55 THR HG2 H 1.110 0.04 1 572 154 55 THR C C 172.600 0.30 1 573 154 55 THR CA C 60.430 0.30 1 574 154 55 THR CB C 70.900 0.30 1 575 154 55 THR CG2 C 20.800 0.30 1 576 154 55 THR N N 111.660 0.40 1 577 155 56 GLY H H 8.300 0.04 1 578 155 56 GLY HA2 H 4.150 0.04 2 579 155 56 GLY HA3 H 3.750 0.04 2 580 155 56 GLY C C 175.600 0.30 1 581 155 56 GLY CA C 44.210 0.30 1 582 155 56 GLY N N 109.870 0.40 1 583 156 57 MET H H 8.280 0.04 1 584 156 57 MET HA H 4.440 0.04 1 585 156 57 MET HB2 H 2.090 0.04 2 586 156 57 MET HB3 H 1.920 0.04 2 587 156 57 MET HG3 H 2.530 0.04 2 588 156 57 MET HE H 1.970 0.04 1 589 156 57 MET C C 175.000 0.30 1 590 156 57 MET CA C 55.300 0.30 1 591 156 57 MET CB C 31.700 0.30 1 592 156 57 MET CG C 30.200 0.30 1 593 156 57 MET CE C 20.800 0.30 1 594 156 57 MET N N 119.190 0.40 1 595 157 58 ALA H H 7.950 0.04 1 596 157 58 ALA HA H 4.550 0.04 1 597 157 58 ALA HB H 0.960 0.04 1 598 157 58 ALA C C 176.500 0.30 1 599 157 58 ALA CA C 50.080 0.30 1 600 157 58 ALA CB C 22.600 0.30 1 601 157 58 ALA N N 127.230 0.40 1 602 158 59 ASP H H 8.110 0.04 1 603 158 59 ASP HA H 4.540 0.04 1 604 158 59 ASP HB2 H 3.070 0.04 2 605 158 59 ASP C C 177.100 0.30 1 606 158 59 ASP CA C 58.070 0.30 1 607 158 59 ASP CB C 41.700 0.30 1 608 158 59 ASP N N 121.540 0.40 1 609 159 60 ILE H H 8.870 0.04 1 610 159 60 ILE HA H 4.220 0.04 1 611 159 60 ILE HB H 2.300 0.04 1 612 159 60 ILE HG12 H 1.460 0.04 2 613 159 60 ILE HG13 H 1.870 0.04 2 614 159 60 ILE HG2 H 1.140 0.04 1 615 159 60 ILE HD1 H 0.960 0.04 1 616 159 60 ILE C C 173.200 0.30 1 617 159 60 ILE CA C 61.830 0.30 1 618 159 60 ILE CB C 37.800 0.30 1 619 159 60 ILE CG2 C 19.200 0.30 1 620 159 60 ILE CD1 C 13.300 0.30 1 621 159 60 ILE N N 124.130 0.40 1 622 160 61 LEU H H 7.690 0.04 1 623 160 61 LEU HA H 5.080 0.04 1 624 160 61 LEU HB3 H 1.720 0.04 2 625 160 61 LEU HG H 1.460 0.04 1 626 160 61 LEU HD1 H 0.990 0.04 2 627 160 61 LEU HD2 H 1.140 0.04 2 628 160 61 LEU C C 175.700 0.30 1 629 160 61 LEU CA C 53.540 0.30 1 630 160 61 LEU CB C 43.600 0.30 1 631 160 61 LEU CG C 24.900 0.30 1 632 160 61 LEU CD1 C 24.200 0.30 1 633 160 61 LEU CD2 C 20.300 0.30 1 634 160 61 LEU N N 130.080 0.40 1 635 161 62 VAL H H 8.790 0.04 1 636 161 62 VAL HA H 5.220 0.04 1 637 161 62 VAL HB H 2.180 0.04 1 638 161 62 VAL HG1 H 0.880 0.04 2 639 161 62 VAL HG2 H 0.750 0.04 2 640 161 62 VAL C C 175.200 0.30 1 641 161 62 VAL CA C 61.830 0.30 1 642 161 62 VAL CB C 30.600 0.30 1 643 161 62 VAL CG1 C 20.300 0.30 1 644 161 62 VAL CG2 C 20.500 0.30 1 645 161 62 VAL N N 125.500 0.40 1 646 162 63 VAL H H 8.630 0.04 1 647 162 63 VAL HA H 4.570 0.04 1 648 162 63 VAL HB H 1.720 0.04 1 649 162 63 VAL HG1 H 0.870 0.04 2 650 162 63 VAL HG2 H 0.730 0.04 2 651 162 63 VAL C C 174.800 0.30 1 652 162 63 VAL CA C 60.720 0.30 1 653 162 63 VAL CB C 37.880 0.30 1 654 162 63 VAL CG1 C 20.900 0.30 1 655 162 63 VAL CG2 C 20.900 0.30 1 656 162 63 VAL N N 126.840 0.40 1 657 163 64 PHE H H 8.580 0.04 1 658 163 64 PHE HA H 5.370 0.04 1 659 163 64 PHE HB2 H 2.740 0.04 2 660 163 64 PHE HB3 H 3.050 0.04 2 661 163 64 PHE HD1 H 6.970 0.04 1 662 163 64 PHE HE1 H 6.500 0.04 1 663 163 64 PHE HZ H 6.060 0.04 1 664 163 64 PHE C C 176.100 0.30 1 665 163 64 PHE CA C 57.220 0.30 1 666 163 64 PHE CB C 41.030 0.30 1 667 163 64 PHE CD1 C 131.500 0.30 1 668 163 64 PHE CE1 C 129.500 0.30 1 669 163 64 PHE CZ C 127.200 0.30 1 670 163 64 PHE N N 125.680 0.40 1 671 164 65 ALA H H 9.110 0.04 1 672 164 65 ALA HA H 4.830 0.04 1 673 164 65 ALA HB H 0.910 0.04 1 674 164 65 ALA C C 174.800 0.30 1 675 164 65 ALA CA C 51.390 0.30 1 676 164 65 ALA CB C 22.900 0.30 1 677 164 65 ALA N N 126.020 0.40 1 678 165 66 ARG H H 8.840 0.04 1 679 165 66 ARG HA H 5.260 0.04 1 680 165 66 ARG HB2 H 1.920 0.04 2 681 165 66 ARG HG3 H 1.630 0.04 2 682 165 66 ARG HD2 H 3.090 0.04 2 683 165 66 ARG C C 175.700 0.30 1 684 165 66 ARG CA C 54.200 0.30 1 685 165 66 ARG CB C 34.170 0.30 1 686 165 66 ARG CG C 26.100 0.30 1 687 165 66 ARG CD C 43.400 0.30 1 688 165 66 ARG N N 118.190 0.40 1 689 166 67 GLY H H 9.530 0.04 1 690 166 67 GLY HA2 H 3.790 0.04 2 691 166 67 GLY HA3 H 3.910 0.04 2 692 166 67 GLY C C 175.500 0.30 1 693 166 67 GLY CA C 46.660 0.30 1 694 166 67 GLY N N 108.410 0.40 1 695 167 68 ALA H H 9.210 0.04 1 696 167 68 ALA HA H 4.760 0.04 1 697 167 68 ALA HB H 1.470 0.04 1 698 167 68 ALA CA C 53.340 0.30 1 699 167 68 ALA CB C 18.200 0.30 1 700 167 68 ALA N N 134.120 0.40 1 701 168 69 HIS H H 9.330 0.04 1 702 168 69 HIS HA H 4.760 0.04 1 703 168 69 HIS HB2 H 3.440 0.04 2 704 168 69 HIS HB3 H 3.170 0.04 2 705 168 69 HIS HD2 H 6.400 0.04 1 706 168 69 HIS HE1 H 6.820 0.04 1 707 168 69 HIS CD2 C 124.000 0.30 1 708 168 69 HIS CE1 C 137.600 0.30 1 709 168 69 HIS N N 120.790 0.40 1 710 169 70 GLY H H 8.600 0.04 1 711 169 70 GLY HA2 H 3.330 0.04 2 712 169 70 GLY HA3 H 3.690 0.04 2 713 169 70 GLY CA C 45.210 0.30 1 714 169 70 GLY N N 106.010 0.40 1 715 170 71 ASP H H 8.150 0.04 1 716 170 71 ASP HA H 4.250 0.04 1 717 170 71 ASP HB2 H 3.07 0.04 2 718 170 71 ASP HB3 H 2.93 0.04 2 719 170 71 ASP C C 176.300 0.30 1 720 170 71 ASP CA C 54.690 0.30 1 721 170 71 ASP CB C 42.800 0.30 1 722 170 71 ASP N N 120.950 0.40 1 723 171 72 PHE H H 8.220 0.04 1 724 171 72 PHE HA H 4.170 0.04 1 725 171 72 PHE HB2 H 2.810 0.04 2 726 171 72 PHE HB3 H 2.940 0.04 2 727 171 72 PHE HD1 H 7.030 0.04 1 728 171 72 PHE HE1 H 7.300 0.04 1 729 171 72 PHE HZ H 7.260 0.04 1 730 171 72 PHE C C 176.300 0.30 1 731 171 72 PHE CA C 54.730 0.30 1 732 171 72 PHE CB C 36.230 0.30 1 733 171 72 PHE CD1 C 130.100 0.30 1 734 171 72 PHE CE1 C 129.500 0.30 1 735 171 72 PHE CZ C 128.000 0.30 1 736 171 72 PHE N N 122.630 0.40 1 737 172 73 HIS H H 8.220 0.04 1 738 172 73 HIS HA H 4.634 0.04 1 739 172 73 HIS HB2 H 3.470 0.04 2 740 172 73 HIS HB3 H 3.060 0.04 2 741 172 73 HIS HD2 H 7.550 0.04 1 742 172 73 HIS HE1 H 8.410 0.04 1 743 172 73 HIS C C 174.700 0.30 1 744 172 73 HIS CA C 53.950 0.30 1 745 172 73 HIS CB C 26.900 0.30 1 746 172 73 HIS CD2 C 118.900 0.30 1 747 172 73 HIS CE1 C 135.000 0.30 1 748 172 73 HIS N N 122.000 0.40 1 749 173 74 ALA H H 8.300 0.04 1 750 173 74 ALA HA H 3.934 0.04 1 751 173 74 ALA HB H 1.372 0.04 1 752 173 74 ALA CA C 58.066 0.30 1 753 173 74 ALA CB C 18.600 0.30 1 754 173 74 ALA N N 123.300 0.40 1 755 174 75 PHE H H 8.270 0.04 1 756 174 75 PHE HA H 4.222 0.04 1 757 174 75 PHE HB2 H 2.92 0.04 2 758 174 75 PHE HB3 H 3.05 0.04 2 759 174 75 PHE HD1 H 7.310 0.04 1 760 174 75 PHE HE1 H 7.220 0.04 1 761 174 75 PHE HZ H 7.020 0.04 1 762 174 75 PHE C C 176.200 0.30 1 763 174 75 PHE CA C 57.430 0.30 1 764 174 75 PHE CB C 38.660 0.30 1 765 174 75 PHE CD1 C 129.500 0.30 1 766 174 75 PHE CE1 C 129.500 0.30 1 767 174 75 PHE CZ C 127.700 0.30 1 768 174 75 PHE N N 121.320 0.40 1 769 175 76 ASP H H 8.250 0.04 1 770 175 76 ASP HA H 4.880 0.04 1 771 175 76 ASP HB2 H 3.04 0.04 2 772 175 76 ASP HB3 H 3.150 0.04 2 773 175 76 ASP C C 177.300 0.30 1 774 175 76 ASP CA C 54.040 0.30 1 775 175 76 ASP CB C 41.700 0.30 1 776 175 76 ASP N N 116.500 0.40 1 777 176 77 GLY H H 8.800 0.04 1 778 176 77 GLY HA2 H 4.290 0.04 2 779 176 77 GLY HA3 H 4.450 0.04 2 780 176 77 GLY CA C 43.670 0.30 1 781 176 77 GLY N N 110.060 0.40 1 782 177 78 LYS H H 8.750 0.04 1 783 177 78 LYS HA H 3.460 0.04 1 784 177 78 LYS HB3 H 1.630 0.04 2 785 177 78 LYS HG2 H 1.330 0.04 2 786 177 78 LYS HD2 H 1.730 0.04 2 787 177 78 LYS HE3 H 2.540 0.04 2 788 177 78 LYS C C 177.900 0.30 1 789 177 78 LYS CA C 58.530 0.30 1 790 177 78 LYS CB C 32.280 0.30 1 791 177 78 LYS CG C 24.800 0.30 1 792 177 78 LYS CD C 29.300 0.30 1 793 177 78 LYS CE C 42.300 0.30 1 794 177 78 LYS N N 124.290 0.40 1 795 178 79 GLY H H 10.980 0.04 1 796 178 79 GLY HA2 H 3.560 0.04 2 797 178 79 GLY HA3 H 4.210 0.04 2 798 178 79 GLY C C 174.400 0.30 1 799 178 79 GLY CA C 43.010 0.30 1 800 178 79 GLY N N 121.280 0.40 1 801 179 80 GLY H H 8.540 0.04 1 802 179 80 GLY HA2 H 4.080 0.04 2 803 179 80 GLY HA3 H 3.470 0.04 2 804 179 80 GLY CA C 46.750 0.30 1 805 179 80 GLY N N 110.400 0.40 1 806 180 81 ILE H H 10.790 0.04 1 807 180 81 ILE HA H 3.934 0.04 1 808 180 81 ILE HB H 2.070 0.04 1 809 180 81 ILE HG12 H 1.720 0.04 2 810 180 81 ILE HG13 H 1.320 0.04 2 811 180 81 ILE HG2 H 1.200 0.04 1 812 180 81 ILE HD1 H 0.970 0.04 1 813 180 81 ILE CA C 62.350 0.30 1 814 180 81 ILE CB C 33.400 0.30 1 815 180 81 ILE CG1 C 25.000 0.30 1 816 180 81 ILE CG2 C 20.800 0.30 1 817 180 81 ILE CD1 C 17.500 0.30 1 818 180 81 ILE N N 132.140 0.40 1 819 181 82 LEU H H 8.310 0.04 1 820 181 82 LEU HA H 5.030 0.04 1 821 181 82 LEU C C 176.600 0.30 1 822 181 82 LEU CA C 52.400 0.30 1 823 181 82 LEU CB C 43.000 0.30 1 824 181 82 LEU CG C 26.900 0.30 1 825 181 82 LEU CD1 C 19.300 0.30 1 826 181 82 LEU CD2 C 22.000 0.30 1 827 181 82 LEU N N 126.600 0.40 1 828 182 83 ALA H H 8.370 0.04 1 829 182 83 ALA HA H 3.730 0.04 1 830 182 83 ALA HB H 1.500 0.04 1 831 182 83 ALA CA C 54.000 0.30 1 832 182 83 ALA CB C 17.900 0.30 1 833 182 83 ALA N N 120.930 0.40 1 834 183 84 HIS H H 8.860 0.04 1 835 183 84 HIS HA H 3.970 0.04 1 836 183 84 HIS HB2 H 3.460 0.04 2 837 183 84 HIS HB3 H 3.220 0.04 2 838 183 84 HIS HD2 H 7.130 0.04 1 839 183 84 HIS HE1 H 7.830 0.04 1 840 183 84 HIS C C 174.800 0.30 1 841 183 84 HIS CA C 55.300 0.30 1 842 183 84 HIS CB C 30.000 0.30 1 843 183 84 HIS CD2 C 120.000 0.30 1 844 183 84 HIS CE1 C 136.000 0.30 1 845 183 84 HIS N N 115.900 0.40 1 846 184 85 ALA H H 9.080 0.04 1 847 184 85 ALA HA H 4.140 0.04 1 848 184 85 ALA HB H 1.400 0.04 1 849 184 85 ALA CA C 52.150 0.30 1 850 184 85 ALA CB C 21.800 0.30 1 851 184 85 ALA N N 121.080 0.40 1 852 185 86 PHE H H 11.780 0.04 1 853 185 86 PHE HA H 4.690 0.04 1 854 185 86 PHE HB2 H 3.570 0.04 2 855 185 86 PHE HB3 H 3.300 0.04 2 856 185 86 PHE C C 180.500 0.30 1 857 185 86 PHE CA C 59.400 0.30 1 858 185 86 PHE CB C 37.000 0.30 1 859 185 86 PHE N N 135.900 0.40 1 860 186 87 GLY H H 8.320 0.04 1 861 186 87 GLY HA2 H 4.210 0.04 2 862 186 87 GLY HA3 H 4.110 0.04 2 863 186 87 GLY CA C 48.000 0.30 1 864 186 87 GLY N N 108.200 0.40 1 865 187 88 PRO CA C 63.870 0.30 1 866 187 88 PRO CB C 27.000 0.30 1 867 187 88 PRO CG C 29.100 0.30 1 868 188 89 GLY H H 5.750 0.04 1 869 188 89 GLY HA2 H 3.520 0.04 2 870 188 89 GLY HA3 H 3.920 0.04 2 871 188 89 GLY C C 179.400 0.30 1 872 188 89 GLY CA C 44.200 0.30 1 873 188 89 GLY N N 109.990 0.40 1 874 189 90 SER H H 8.090 0.04 1 875 189 90 SER HA H 4.360 0.04 1 876 189 90 SER HB2 H 3.990 0.04 2 877 189 90 SER HB3 H 4.190 0.04 2 878 189 90 SER CA C 58.850 0.30 1 879 189 90 SER CB C 64.600 0.30 1 880 189 90 SER N N 114.650 0.40 1 881 190 91 GLY H H 9.240 0.04 1 882 190 91 GLY HA2 H 3.800 0.04 2 883 190 91 GLY CA C 47.350 0.30 1 884 190 91 GLY N N 111.350 0.40 1 885 191 92 ILE H H 9.040 0.04 1 886 191 92 ILE HA H 4.020 0.04 1 887 191 92 ILE HB H 2.120 0.04 1 888 191 92 ILE HG12 H 1.460 0.04 2 889 191 92 ILE HG2 H 0.510 0.04 1 890 191 92 ILE HD1 H 0.460 0.04 1 891 191 92 ILE CA C 62.340 0.30 1 892 191 92 ILE CB C 38.000 0.30 1 893 191 92 ILE CG1 C 27.500 0.30 1 894 191 92 ILE CG2 C 22.600 0.30 1 895 191 92 ILE CD1 C 16.500 0.30 1 896 191 92 ILE N N 133.470 0.40 1 897 192 93 GLY H H 7.810 0.04 1 898 192 93 GLY HA2 H 3.800 0.04 2 899 192 93 GLY CA C 46.100 0.30 1 900 192 93 GLY N N 105.280 0.40 1 901 193 94 GLY H H 8.130 0.04 1 902 193 94 GLY HA2 H 4.290 0.04 2 903 193 94 GLY HA3 H 3.900 0.04 2 904 193 94 GLY CA C 46.400 0.30 1 905 193 94 GLY N N 115.850 0.40 1 906 194 95 ASP H H 8.280 0.04 1 907 194 95 ASP HA H 4.312 0.04 1 908 194 95 ASP HB3 H 2.990 0.04 2 909 194 95 ASP C C 175.000 0.30 1 910 194 95 ASP CA C 56.580 0.30 1 911 194 95 ASP CB C 39.500 0.30 1 912 194 95 ASP N N 122.470 0.40 1 913 195 96 ALA H H 8.630 0.04 1 914 195 96 ALA HA H 4.770 0.04 1 915 195 96 ALA HB H 1.040 0.04 1 916 195 96 ALA CA C 51.100 0.30 1 917 195 96 ALA N N 119.890 0.40 1 918 196 97 HIS H H 9.000 0.04 1 919 196 97 HIS HA H 4.810 0.04 1 920 196 97 HIS HB2 H 3.360 0.04 2 921 196 97 HIS HB3 H 2.530 0.04 2 922 196 97 HIS HD2 H 6.520 0.04 1 923 196 97 HIS HE1 H 8.460 0.04 1 924 196 97 HIS C C 172.900 0.30 1 925 196 97 HIS CA C 50.500 0.30 1 926 196 97 HIS CB C 34.100 0.30 1 927 196 97 HIS CD2 C 122.100 0.30 1 928 196 97 HIS CE1 C 140.300 0.30 1 929 196 97 HIS N N 120.880 0.40 1 930 197 98 PHE H H 9.140 0.04 1 931 197 98 PHE HA H 4.320 0.04 1 932 197 98 PHE HB2 H 2.250 0.04 2 933 197 98 PHE HB3 H 1.720 0.04 2 934 197 98 PHE HD1 H 6.250 0.04 1 935 197 98 PHE HE1 H 6.510 0.04 1 936 197 98 PHE HZ H 6.380 0.04 1 937 197 98 PHE C C 174.200 0.30 1 938 197 98 PHE CA C 57.040 0.30 1 939 197 98 PHE CB C 41.480 0.30 1 940 197 98 PHE CD1 C 129.800 0.30 1 941 197 98 PHE CE1 C 126.600 0.30 1 942 197 98 PHE CZ C 123.700 0.30 1 943 197 98 PHE N N 122.750 0.40 1 944 198 99 ASP H H 8.040 0.04 1 945 198 99 ASP HA H 4.340 0.04 1 946 198 99 ASP HB2 H 3.470 0.04 2 947 198 99 ASP HB3 H 3.120 0.04 2 948 198 99 ASP C C 179.400 0.30 1 949 198 99 ASP CA C 54.260 0.30 1 950 198 99 ASP CB C 40.500 0.30 1 951 198 99 ASP N N 122.570 0.40 1 952 199 100 GLU H H 9.560 0.04 1 953 199 100 GLU HA H 4.490 0.04 1 954 199 100 GLU HB2 H 1.740 0.04 2 955 199 100 GLU HG3 H 2.050 0.04 2 956 199 100 GLU C C 176.600 0.30 1 957 199 100 GLU CA C 56.380 0.30 1 958 199 100 GLU CB C 31.800 0.30 1 959 199 100 GLU CG C 36.400 0.30 1 960 199 100 GLU N N 130.440 0.40 1 961 200 101 ASP H H 9.080 0.04 1 962 200 101 ASP HA H 4.810 0.04 1 963 200 101 ASP HB2 H 2.560 0.04 2 964 200 101 ASP HB3 H 2.690 0.04 2 965 200 101 ASP C C 177.300 0.30 1 966 200 101 ASP CA C 56.910 0.30 1 967 200 101 ASP CB C 39.600 0.30 1 968 200 101 ASP N N 119.500 0.40 1 969 201 102 GLU H H 7.390 0.04 1 970 201 102 GLU HA H 4.470 0.04 1 971 201 102 GLU HB2 H 1.770 0.04 2 972 201 102 GLU HB3 H 1.650 0.04 2 973 201 102 GLU HG2 H 1.940 0.04 2 974 201 102 GLU C C 175.100 0.30 1 975 201 102 GLU CA C 54.020 0.30 1 976 201 102 GLU CB C 27.100 0.30 1 977 201 102 GLU CG C 35.700 0.30 1 978 201 102 GLU N N 116.700 0.40 1 979 202 103 PHE H H 8.440 0.04 1 980 202 103 PHE HA H 4.930 0.04 1 981 202 103 PHE HB2 H 2.860 0.04 2 982 202 103 PHE HB3 H 2.700 0.04 2 983 202 103 PHE HD1 H 7.080 0.04 1 984 202 103 PHE HE1 H 7.310 0.04 1 985 202 103 PHE HZ H 6.900 0.04 1 986 202 103 PHE C C 172.800 0.30 1 987 202 103 PHE CA C 55.620 0.30 1 988 202 103 PHE CB C 38.900 0.30 1 989 202 103 PHE CD1 C 129.300 0.30 1 990 202 103 PHE CE1 C 128.000 0.30 1 991 202 103 PHE CZ C 127.500 0.30 1 992 202 103 PHE N N 126.330 0.40 1 993 203 104 TRP H H 9.240 0.04 1 994 203 104 TRP HA H 5.000 0.04 1 995 203 104 TRP HB2 H 3.220 0.04 2 996 203 104 TRP HB3 H 2.570 0.04 2 997 203 104 TRP HD1 H 7.380 0.04 1 998 203 104 TRP HE1 H 10.200 0.04 1 999 203 104 TRP HE3 H 7.350 0.04 1 1000 203 104 TRP HZ2 H 7.130 0.04 1 1001 203 104 TRP HZ3 H 7.230 0.04 1 1002 203 104 TRP HH2 H 7.500 0.04 1 1003 203 104 TRP C C 176.800 0.30 1 1004 203 104 TRP CA C 56.690 0.30 1 1005 203 104 TRP CB C 31.000 0.30 1 1006 203 104 TRP CD1 C 126.100 0.30 1 1007 203 104 TRP CE3 C 116.000 0.30 1 1008 203 104 TRP CZ2 C 112.000 0.30 1 1009 203 104 TRP CZ3 C 125.000 0.30 1 1010 203 104 TRP CH2 C 122.500 0.30 1 1011 203 104 TRP N N 131.500 0.40 1 1012 203 104 TRP NE1 N 127.200 0.40 1 1013 204 105 THR H H 8.300 0.04 1 1014 204 105 THR HA H 4.400 0.04 1 1015 204 105 THR HB H 4.150 0.04 1 1016 204 105 THR HG2 H 1.110 0.04 1 1017 204 105 THR C C 176.100 0.30 1 1018 204 105 THR CA C 59.990 0.30 1 1019 204 105 THR CB C 70.680 0.30 1 1020 204 105 THR CG2 C 20.800 0.30 1 1021 204 105 THR N N 109.610 0.40 1 1022 205 106 THR H H 8.330 0.04 1 1023 205 106 THR HA H 4.600 0.04 1 1024 205 106 THR HB H 4.380 0.04 1 1025 205 106 THR HG2 H 1.340 0.04 1 1026 205 106 THR C C 175.600 0.30 1 1027 205 106 THR CA C 62.400 0.30 1 1028 205 106 THR CB C 69.400 0.30 1 1029 205 106 THR CG2 C 22.500 0.30 1 1030 205 106 THR N N 109.830 0.40 1 1031 206 107 HIS H H 8.000 0.04 1 1032 206 107 HIS HA H 4.320 0.04 1 1033 206 107 HIS HB2 H 3.470 0.04 2 1034 206 107 HIS HB3 H 3.110 0.04 2 1035 206 107 HIS HD2 H 7.170 0.04 1 1036 206 107 HIS HE1 H 7.820 0.04 1 1037 206 107 HIS C C 174.200 0.30 1 1038 206 107 HIS CA C 55.530 0.30 1 1039 206 107 HIS CB C 31.600 0.30 1 1040 206 107 HIS CD2 C 117.800 0.30 1 1041 206 107 HIS CE1 C 137.300 0.30 1 1042 206 107 HIS N N 122.640 0.40 1 1043 207 108 SER H H 7.990 0.04 1 1044 207 108 SER HA H 4.170 0.04 1 1045 207 108 SER HB2 H 3.50 0.04 2 1046 207 108 SER HB3 H 3.42 0.04 2 1047 207 108 SER C C 176.000 0.30 1 1048 207 108 SER CA C 58.800 0.30 1 1049 207 108 SER CB C 64.600 0.30 1 1050 207 108 SER N N 114.390 0.40 1 1051 208 109 GLY H H 9.020 0.04 1 1052 208 109 GLY HA2 H 3.960 0.04 2 1053 208 109 GLY HA3 H 3.740 0.04 2 1054 208 109 GLY CA C 45.300 0.30 1 1055 208 109 GLY N N 112.330 0.40 1 1056 209 110 GLY H H 8.000 0.04 1 1057 209 110 GLY HA2 H 3.840 0.04 2 1058 209 110 GLY HA3 H 4.150 0.04 2 1059 209 110 GLY C C 174.000 0.30 1 1060 209 110 GLY CA C 46.400 0.30 1 1061 209 110 GLY N N 108.040 0.40 1 1062 210 111 THR H H 9.170 0.04 1 1063 210 111 THR HA H 4.000 0.04 1 1064 210 111 THR HB H 3.790 0.04 1 1065 210 111 THR HG2 H 0.560 0.04 1 1066 210 111 THR C C 172.700 0.30 1 1067 210 111 THR CA C 62.690 0.30 1 1068 210 111 THR CB C 69.420 0.30 1 1069 210 111 THR CG2 C 21.000 0.30 1 1070 210 111 THR N N 124.630 0.40 1 1071 211 112 ASN H H 8.410 0.04 1 1072 211 112 ASN HA H 4.774 0.04 1 1073 211 112 ASN HB2 H 3.100 0.04 2 1074 211 112 ASN HB3 H 3.170 0.04 2 1075 211 112 ASN HD21 H 7.990 0.04 2 1076 211 112 ASN HD22 H 6.370 0.04 2 1077 211 112 ASN C C 176.700 0.30 1 1078 211 112 ASN CA C 55.880 0.30 1 1079 211 112 ASN CB C 41.860 0.30 1 1080 211 112 ASN N N 125.650 0.40 1 1081 211 112 ASN ND2 N 110.800 0.40 1 1082 212 113 LEU H H 8.700 0.04 1 1083 212 113 LEU HA H 4.400 0.04 1 1084 212 113 LEU HB2 H 1.860 0.04 2 1085 212 113 LEU HB3 H 1.590 0.04 2 1086 212 113 LEU HG H 1.490 0.04 1 1087 212 113 LEU HD1 H 0.800 0.04 2 1088 212 113 LEU HD2 H 1.070 0.04 2 1089 212 113 LEU C C 176.500 0.30 1 1090 212 113 LEU CA C 58.840 0.30 1 1091 212 113 LEU CB C 41.120 0.30 1 1092 212 113 LEU CG C 27.900 0.30 1 1093 212 113 LEU CD1 C 17.600 0.30 1 1094 212 113 LEU CD2 C 18.100 0.30 1 1095 212 113 LEU N N 132.060 0.40 1 1096 213 114 PHE H H 9.370 0.04 1 1097 213 114 PHE HA H 3.940 0.04 1 1098 213 114 PHE HB2 H 3.180 0.04 2 1099 213 114 PHE HB3 H 3.430 0.04 2 1100 213 114 PHE HD1 H 7.200 0.04 1 1101 213 114 PHE HE1 H 6.870 0.04 1 1102 213 114 PHE HZ H 6.500 0.04 1 1103 213 114 PHE C C 175.900 0.30 1 1104 213 114 PHE CA C 61.710 0.30 1 1105 213 114 PHE CB C 37.900 0.30 1 1106 213 114 PHE CD1 C 130.200 0.30 1 1107 213 114 PHE CE1 C 129.300 0.30 1 1108 213 114 PHE CZ C 128.900 0.30 1 1109 213 114 PHE N N 120.810 0.40 1 1110 214 115 LEU H H 9.090 0.04 1 1111 214 115 LEU HA H 4.360 0.04 1 1112 214 115 LEU HB2 H 1.820 0.04 2 1113 214 115 LEU HB3 H 1.520 0.04 2 1114 214 115 LEU HG H 1.080 0.04 1 1115 214 115 LEU HD1 H 0.450 0.04 2 1116 214 115 LEU HD2 H 0.810 0.04 2 1117 214 115 LEU C C 180.400 0.30 1 1118 214 115 LEU CA C 57.900 0.30 1 1119 214 115 LEU CB C 43.010 0.30 1 1120 214 115 LEU CG C 33.000 0.30 1 1121 214 115 LEU CD1 C 26.500 0.30 1 1122 214 115 LEU CD2 C 19.600 0.30 1 1123 214 115 LEU N N 118.040 0.40 1 1124 215 116 THR H H 7.660 0.04 1 1125 215 116 THR HA H 4.400 0.04 1 1126 215 116 THR HB H 4.080 0.04 1 1127 215 116 THR HG2 H 1.490 0.04 1 1128 215 116 THR C C 176.600 0.30 1 1129 215 116 THR CA C 67.030 0.30 1 1130 215 116 THR CB C 68.200 0.30 1 1131 215 116 THR CG2 C 21.500 0.30 1 1132 215 116 THR N N 115.530 0.40 1 1133 216 117 ALA H H 9.440 0.04 1 1134 216 117 ALA HA H 4.040 0.04 1 1135 216 117 ALA HB H 1.080 0.04 1 1136 216 117 ALA C C 178.400 0.30 1 1137 216 117 ALA CA C 55.580 0.30 1 1138 216 117 ALA CB C 17.300 0.30 1 1139 216 117 ALA N N 125.450 0.40 1 1140 217 118 VAL H H 8.560 0.04 1 1141 217 118 VAL HA H 4.580 0.04 1 1142 217 118 VAL HB H 1.560 0.04 1 1143 217 118 VAL HG1 H 0.980 0.04 2 1144 217 118 VAL HG2 H 1.110 0.04 2 1145 217 118 VAL CA C 68.030 0.30 1 1146 217 118 VAL CB C 31.200 0.30 1 1147 217 118 VAL CG1 C 23.100 0.30 1 1148 217 118 VAL CG2 C 23.600 0.30 1 1149 217 118 VAL N N 118.600 0.40 1 1150 218 119 HIS H H 6.880 0.04 1 1151 218 119 HIS HA H 4.280 0.04 1 1152 218 119 HIS HB2 H 3.070 0.04 2 1153 218 119 HIS HB3 H 3.390 0.04 2 1154 218 119 HIS HD2 H 7.060 0.04 1 1155 218 119 HIS HE1 H 7.770 0.04 1 1156 218 119 HIS C C 175.900 0.30 1 1157 218 119 HIS CA C 58.560 0.30 1 1158 218 119 HIS CB C 31.000 0.30 1 1159 218 119 HIS CD2 C 118.100 0.30 1 1160 218 119 HIS CE1 C 135.700 0.30 1 1161 218 119 HIS N N 116.930 0.40 1 1162 219 120 ALA H H 8.860 0.04 1 1163 219 120 ALA HA H 4.280 0.04 1 1164 219 120 ALA HB H 0.980 0.04 1 1165 219 120 ALA C C 178.600 0.30 1 1166 219 120 ALA CA C 56.600 0.30 1 1167 219 120 ALA CB C 18.000 0.30 1 1168 219 120 ALA N N 115.470 0.40 1 1169 220 121 ILE H H 8.920 0.04 1 1170 220 121 ILE HA H 3.550 0.04 1 1171 220 121 ILE HB H 2.350 0.04 1 1172 220 121 ILE HG12 H 1.120 0.04 2 1173 220 121 ILE HG13 H 1.450 0.04 2 1174 220 121 ILE HD1 H 1.040 0.04 1 1175 220 121 ILE C C 177.200 0.30 1 1176 220 121 ILE CA C 63.440 0.30 1 1177 220 121 ILE CB C 37.800 0.30 1 1178 220 121 ILE CG1 C 27.100 0.30 1 1179 220 121 ILE CG2 C 17.600 0.30 1 1180 220 121 ILE CD1 C 13.900 0.30 1 1181 220 121 ILE N N 115.890 0.40 1 1182 221 122 GLY H H 7.490 0.04 1 1183 221 122 GLY HA2 H 3.600 0.04 2 1184 221 122 GLY HA3 H 3.690 0.04 2 1185 221 122 GLY CA C 47.950 0.30 1 1186 221 122 GLY N N 108.560 0.40 1 1187 222 123 HIS H H 6.990 0.04 1 1188 222 123 HIS HA H 4.280 0.04 1 1189 222 123 HIS HB2 H 3.880 0.04 1 1190 222 123 HIS HB3 H 3.880 0.04 1 1191 222 123 HIS HD2 H 7.400 0.04 1 1192 222 123 HIS HE1 H 7.770 0.04 1 1193 222 123 HIS CA C 56.410 0.30 1 1194 222 123 HIS CB C 30.400 0.30 1 1195 222 123 HIS CD2 C 125.000 0.30 1 1196 222 123 HIS CE1 C 134.700 0.30 1 1197 222 123 HIS N N 118.500 0.40 1 1198 223 124 SER H H 8.460 0.04 1 1199 223 124 SER HA H 4.310 0.04 1 1200 223 124 SER HB2 H 4.050 0.04 2 1201 223 124 SER C C 175.800 0.30 1 1202 223 124 SER CA C 56.330 0.30 1 1203 223 124 SER CB C 62.360 0.30 1 1204 223 124 SER N N 122.000 0.40 1 1205 224 125 LEU H H 7.800 0.04 1 1206 224 125 LEU HA H 4.530 0.04 1 1207 224 125 LEU HB2 H 2.800 0.04 2 1208 224 125 LEU HG H 2.660 0.04 1 1209 224 125 LEU HD2 H 1.390 0.04 2 1210 224 125 LEU CA C 52.900 0.30 1 1211 224 125 LEU CB C 41.000 0.30 1 1212 224 125 LEU CG C 32.300 0.30 1 1213 224 125 LEU CD1 C 23.000 0.30 1 1214 224 125 LEU CD2 C 19.000 0.30 1 1215 224 125 LEU N N 114.580 0.40 1 1216 225 126 GLY H H 7.890 0.04 1 1217 225 126 GLY HA2 H 3.960 0.04 2 1218 225 126 GLY HA3 H 4.240 0.04 2 1219 225 126 GLY C C 176.600 0.30 1 1220 225 126 GLY CA C 46.300 0.30 1 1221 225 126 GLY N N 119.510 0.40 1 1222 226 127 LEU H H 8.130 0.04 1 1223 226 127 LEU HA H 3.960 0.04 1 1224 226 127 LEU HB3 H 2.660 0.04 2 1225 226 127 LEU HG H 1.800 0.04 1 1226 226 127 LEU HD1 H 1.500 0.04 2 1227 226 127 LEU CA C 54.000 0.30 1 1228 226 127 LEU CB C 41.800 0.30 1 1229 226 127 LEU CG C 33.000 0.30 1 1230 226 127 LEU CD1 C 31.000 0.30 1 1231 226 127 LEU N N 120.940 0.40 1 1232 227 128 GLY H H 8.830 0.04 1 1233 227 128 GLY HA2 H 3.500 0.04 2 1234 227 128 GLY HA3 H 3.600 0.04 2 1235 227 128 GLY CA C 43.700 0.30 1 1236 227 128 GLY N N 110.080 0.40 1 1237 228 129 HIS H H 8.540 0.04 1 1238 228 129 HIS HA H 5.220 0.04 1 1239 228 129 HIS HB2 H 3.050 0.04 2 1240 228 129 HIS HB3 H 3.210 0.04 2 1241 228 129 HIS HD2 H 6.650 0.04 1 1242 228 129 HIS HE1 H 8.290 0.04 1 1243 228 129 HIS CA C 56.340 0.30 1 1244 228 129 HIS CB C 30.000 0.30 1 1245 228 129 HIS CD2 C 122.500 0.30 1 1246 228 129 HIS CE1 C 139.000 0.30 1 1247 228 129 HIS N N 115.580 0.40 1 1248 229 130 SER H H 7.120 0.04 1 1249 229 130 SER HA H 4.750 0.04 1 1250 229 130 SER HB2 H 4.220 0.04 2 1251 229 130 SER C C 175.600 0.30 1 1252 229 130 SER CA C 55.580 0.30 1 1253 229 130 SER CB C 65.100 0.30 1 1254 229 130 SER N N 114.530 0.40 1 1255 230 131 SER H H 8.870 0.04 1 1256 230 131 SER HA H 4.760 0.04 1 1257 230 131 SER HB2 H 3.980 0.04 2 1258 230 131 SER HB3 H 4.090 0.04 2 1259 230 131 SER C C 173.500 0.30 1 1260 230 131 SER CA C 58.740 0.30 1 1261 230 131 SER CB C 64.220 0.30 1 1262 230 131 SER N N 120.140 0.40 1 1263 231 132 ASP H H 8.940 0.04 1 1264 231 132 ASP HA H 4.840 0.04 1 1265 231 132 ASP HB2 H 3.220 0.04 2 1266 231 132 ASP HB3 H 3.040 0.04 2 1267 231 132 ASP C C 174.900 0.30 1 1268 231 132 ASP CA C 51.430 0.30 1 1269 231 132 ASP CB C 42.500 0.30 1 1270 231 132 ASP N N 126.560 0.40 1 1271 232 133 PRO HA H 4.850 0.04 1 1272 232 133 PRO HB3 H 2.140 0.04 2 1273 232 133 PRO HD2 H 3.800 0.04 2 1274 232 133 PRO HD3 H 3.93 0.04 2 1275 232 133 PRO C C 177.800 0.30 1 1276 232 133 PRO CA C 63.200 0.30 1 1277 232 133 PRO CB C 32.000 0.30 1 1278 232 133 PRO CG C 27.400 0.30 1 1279 232 133 PRO CD C 50.70 0.30 1 1280 233 134 LYS H H 8.310 0.04 1 1281 233 134 LYS HA H 4.130 0.04 1 1282 233 134 LYS HB2 H 1.77 0.04 2 1283 233 134 LYS HB3 H 1.66 0.04 2 1284 233 134 LYS HG2 H 1.360 0.04 2 1285 233 134 LYS HD2 H 1.500 0.04 2 1286 233 134 LYS HE3 H 3.030 0.04 2 1287 233 134 LYS C C 176.800 0.30 1 1288 233 134 LYS CA C 56.440 0.30 1 1289 233 134 LYS CB C 28.700 0.30 1 1290 233 134 LYS CG C 24.200 0.30 1 1291 233 134 LYS CD C 31.900 0.30 1 1292 233 134 LYS CE C 41.100 0.30 1 1293 233 134 LYS N N 116.890 0.40 1 1294 234 135 ALA H H 8.190 0.04 1 1295 234 135 ALA HA H 4.560 0.04 1 1296 234 135 ALA HB H 1.800 0.04 1 1297 234 135 ALA C C 179.500 0.30 1 1298 234 135 ALA CA C 52.080 0.30 1 1299 234 135 ALA CB C 20.000 0.30 1 1300 234 135 ALA N N 123.950 0.40 1 1301 235 136 VAL H H 11.380 0.04 1 1302 235 136 VAL HA H 4.250 0.04 1 1303 235 136 VAL HB H 2.330 0.04 1 1304 235 136 VAL HG1 H 1.140 0.04 2 1305 235 136 VAL HG2 H 0.960 0.04 2 1306 235 136 VAL CA C 64.950 0.30 1 1307 235 136 VAL CB C 31.370 0.30 1 1308 235 136 VAL CG1 C 20.400 0.30 1 1309 235 136 VAL CG2 C 23.900 0.30 1 1310 235 136 VAL N N 131.320 0.40 1 1311 236 137 MET H H 7.910 0.04 1 1312 236 137 MET HA H 4.220 0.04 1 1313 236 137 MET HB2 H 2.180 0.04 2 1314 236 137 MET HB3 H 2.040 0.04 2 1315 236 137 MET HG2 H 2.960 0.04 2 1316 236 137 MET HE H 1.790 0.04 1 1317 236 137 MET C C 177.700 0.30 1 1318 236 137 MET CA C 53.760 0.30 1 1319 236 137 MET CB C 27.340 0.30 1 1320 236 137 MET CG C 30.500 0.30 1 1321 236 137 MET CE C 20.500 0.30 1 1322 236 137 MET N N 115.150 0.40 1 1323 237 138 PHE H H 8.010 0.04 1 1324 237 138 PHE HA H 3.860 0.04 1 1325 237 138 PHE HB2 H 3.030 0.04 2 1326 237 138 PHE HB3 H 3.210 0.04 2 1327 237 138 PHE HD1 H 7.300 0.04 1 1328 237 138 PHE HE1 H 7.360 0.04 1 1329 237 138 PHE HZ H 7.070 0.04 1 1330 237 138 PHE C C 176.800 0.30 1 1331 237 138 PHE CA C 57.840 0.30 1 1332 237 138 PHE CB C 40.250 0.30 1 1333 237 138 PHE CD1 C 129.900 0.30 1 1334 237 138 PHE CE1 C 128.900 0.30 1 1335 237 138 PHE CZ C 129.400 0.30 1 1336 237 138 PHE N N 128.350 0.40 1 1337 238 139 PRO HA H 4.330 0.04 1 1338 238 139 PRO HB3 H 2.050 0.04 2 1339 238 139 PRO HG2 H 1.560 0.04 2 1340 238 139 PRO HG3 H 1.410 0.04 2 1341 238 139 PRO HD2 H 3.510 0.04 2 1342 238 139 PRO HD3 H 3.500 0.04 2 1343 238 139 PRO C C 176.300 0.30 1 1344 238 139 PRO CA C 65.610 0.30 1 1345 238 139 PRO CB C 29.300 0.30 1 1346 238 139 PRO CG C 25.660 0.30 1 1347 238 139 PRO CD C 50.400 0.30 1 1348 239 140 THR H H 6.390 0.04 1 1349 239 140 THR HA H 4.120 0.04 1 1350 239 140 THR HB H 4.060 0.04 1 1351 239 140 THR HG2 H 1.240 0.04 1 1352 239 140 THR C C 173.500 0.30 1 1353 239 140 THR CA C 61.420 0.30 1 1354 239 140 THR CB C 69.700 0.30 1 1355 239 140 THR CG2 C 21.800 0.30 1 1356 239 140 THR N N 111.880 0.40 1 1357 240 141 TYR H H 8.410 0.04 1 1358 240 141 TYR HA H 4.280 0.04 1 1359 240 141 TYR HB2 H 2.760 0.04 2 1360 240 141 TYR HB3 H 3.020 0.04 2 1361 240 141 TYR HD1 H 7.200 0.04 1 1362 240 141 TYR HE1 H 6.980 0.04 1 1363 240 141 TYR C C 174.600 0.30 1 1364 240 141 TYR CA C 59.060 0.30 1 1365 240 141 TYR CB C 39.420 0.30 1 1366 240 141 TYR CD1 C 129.700 0.30 1 1367 240 141 TYR CE1 C 115.900 0.30 1 1368 240 141 TYR N N 127.950 0.40 1 1369 241 142 LYS H H 7.420 0.04 1 1370 241 142 LYS HA H 4.030 0.04 1 1371 241 142 LYS HB3 H 1.630 0.04 2 1372 241 142 LYS HE3 H 3.000 0.04 2 1373 241 142 LYS C C 173.700 0.30 1 1374 241 142 LYS CA C 55.360 0.30 1 1375 241 142 LYS CB C 35.010 0.30 1 1376 241 142 LYS CG C 23.900 0.30 1 1377 241 142 LYS CD C 29.300 0.30 1 1378 241 142 LYS CE C 42.400 0.30 1 1379 241 142 LYS N N 127.450 0.40 1 1380 242 143 TYR H H 8.540 0.04 1 1381 242 143 TYR HA H 3.860 0.04 1 1382 242 143 TYR HB2 H 3.050 0.04 2 1383 242 143 TYR HB3 H 2.740 0.04 2 1384 242 143 TYR HD1 H 6.990 0.04 1 1385 242 143 TYR HE1 H 6.740 0.04 1 1386 242 143 TYR C C 175.200 0.30 1 1387 242 143 TYR CA C 60.900 0.30 1 1388 242 143 TYR CB C 38.500 0.30 1 1389 242 143 TYR CD1 C 131.000 0.30 1 1390 242 143 TYR CE1 C 116.100 0.30 1 1391 242 143 TYR N N 123.250 0.40 1 1392 243 144 VAL H H 5.870 0.04 1 1393 243 144 VAL HA H 3.880 0.04 1 1394 243 144 VAL HB H 1.900 0.04 1 1395 243 144 VAL HG1 H 0.820 0.04 2 1396 243 144 VAL HG2 H 1.080 0.04 2 1397 243 144 VAL C C 172.200 0.30 1 1398 243 144 VAL CA C 59.530 0.30 1 1399 243 144 VAL CB C 35.400 0.30 1 1400 243 144 VAL CG1 C 19.500 0.30 1 1401 243 144 VAL CG2 C 21.400 0.30 1 1402 243 144 VAL N N 124.130 0.40 1 1403 244 145 ASP H H 7.850 0.04 1 1404 244 145 ASP HA H 4.280 0.04 1 1405 244 145 ASP HB2 H 2.720 0.04 2 1406 244 145 ASP HB3 H 2.740 0.04 2 1407 244 145 ASP C C 179.100 0.30 1 1408 244 145 ASP CA C 55.260 0.30 1 1409 244 145 ASP CB C 42.100 0.30 1 1410 244 145 ASP N N 118.510 0.40 1 1411 245 146 ILE H H 7.770 0.04 1 1412 245 146 ILE HA H 3.840 0.04 1 1413 245 146 ILE HB H 1.960 0.04 1 1414 245 146 ILE HG2 H 1.280 0.04 1 1415 245 146 ILE HD1 H 0.800 0.04 1 1416 245 146 ILE C C 177.400 0.30 1 1417 245 146 ILE CA C 64.650 0.30 1 1418 245 146 ILE CB C 37.900 0.30 1 1419 245 146 ILE CG2 C 18.200 0.30 1 1420 245 146 ILE CG1 C 27.000 0.30 1 1421 245 146 ILE CD1 C 14.000 0.30 1 1422 245 146 ILE N N 124.230 0.40 1 1423 246 147 ASN H H 8.590 0.04 1 1424 246 147 ASN HA H 4.580 0.04 1 1425 246 147 ASN HB2 H 2.980 0.04 2 1426 246 147 ASN HB3 H 2.840 0.04 2 1427 246 147 ASN HD21 H 7.050 0.04 2 1428 246 147 ASN HD22 H 7.950 0.04 2 1429 246 147 ASN C C 176.500 0.30 1 1430 246 147 ASN CA C 55.600 0.30 1 1431 246 147 ASN CB C 38.420 0.30 1 1432 246 147 ASN N N 118.560 0.40 1 1433 246 147 ASN ND2 N 115.000 0.40 1 1434 247 148 THR H H 7.540 0.04 1 1435 247 148 THR HA H 4.400 0.04 1 1436 247 148 THR HB H 3.830 0.04 1 1437 247 148 THR HG2 H 1.140 0.04 1 1438 247 148 THR C C 173.900 0.30 1 1439 247 148 THR CA C 60.950 0.30 1 1440 247 148 THR CB C 69.270 0.30 1 1441 247 148 THR CG2 C 21.500 0.30 1 1442 247 148 THR N N 108.860 0.40 1 1443 248 149 PHE H H 7.190 0.04 1 1444 248 149 PHE HA H 4.154 0.04 1 1445 248 149 PHE HB2 H 3.110 0.04 2 1446 248 149 PHE HB3 H 2.850 0.04 2 1447 248 149 PHE HD1 H 7.320 0.04 1 1448 248 149 PHE HE1 H 7.040 0.04 1 1449 248 149 PHE HZ H 6.970 0.04 1 1450 248 149 PHE C C 174.600 0.30 1 1451 248 149 PHE CA C 60.000 0.30 1 1452 248 149 PHE CB C 40.030 0.30 1 1453 248 149 PHE CD1 C 132.000 0.30 1 1454 248 149 PHE CE1 C 131.500 0.30 1 1455 248 149 PHE CZ C 131.100 0.30 1 1456 248 149 PHE N N 123.200 0.40 1 1457 249 150 ARG H H 7.180 0.04 1 1458 249 150 ARG HA H 4.130 0.04 1 1459 249 150 ARG HB3 H 1.660 0.04 2 1460 249 150 ARG HG3 H 1.460 0.04 2 1461 249 150 ARG HD3 H 3.090 0.04 2 1462 249 150 ARG C C 174.600 0.30 1 1463 249 150 ARG CA C 54.340 0.30 1 1464 249 150 ARG CB C 33.510 0.30 1 1465 249 150 ARG CG C 26.200 0.30 1 1466 249 150 ARG CD C 43.500 0.30 1 1467 249 150 ARG N N 126.250 0.40 1 1468 250 151 LEU H H 8.180 0.04 1 1469 250 151 LEU HA H 3.920 0.04 1 1470 250 151 LEU HB2 H 1.300 0.04 2 1471 250 151 LEU HB3 H 1.460 0.04 2 1472 250 151 LEU HG H 1.670 0.04 1 1473 250 151 LEU HD1 H 0.330 0.04 2 1474 250 151 LEU HD2 H 0.110 0.04 2 1475 250 151 LEU C C 177.000 0.30 1 1476 250 151 LEU CA C 54.970 0.30 1 1477 250 151 LEU CB C 43.100 0.30 1 1478 250 151 LEU CG C 26.900 0.30 1 1479 250 151 LEU CD1 C 22.500 0.30 1 1480 250 151 LEU N N 120.940 0.40 1 1481 251 152 SER H H 9.000 0.04 1 1482 251 152 SER HA H 4.200 0.04 1 1483 251 152 SER HB3 H 3.880 0.04 2 1484 251 152 SER C C 175.100 0.30 1 1485 251 152 SER CA C 57.830 0.30 1 1486 251 152 SER CB C 65.800 0.30 1 1487 251 152 SER N N 118.210 0.40 1 1488 252 153 ALA H H 8.860 0.04 1 1489 252 153 ALA HA H 4.540 0.04 1 1490 252 153 ALA HB H 1.500 0.04 1 1491 252 153 ALA C C 180.300 0.30 1 1492 252 153 ALA CA C 55.710 0.30 1 1493 252 153 ALA CB C 18.200 0.30 1 1494 252 153 ALA N N 123.680 0.40 1 1495 253 154 ASP H H 8.300 0.04 1 1496 253 154 ASP HA H 4.380 0.04 1 1497 253 154 ASP HB2 H 2.860 0.04 2 1498 253 154 ASP HB3 H 2.510 0.04 2 1499 253 154 ASP C C 178.600 0.30 1 1500 253 154 ASP CA C 58.360 0.30 1 1501 253 154 ASP CB C 43.800 0.30 1 1502 253 154 ASP N N 117.490 0.40 1 1503 254 155 ASP H H 7.430 0.04 1 1504 254 155 ASP HA H 4.760 0.04 1 1505 254 155 ASP HB2 H 3.090 0.04 2 1506 254 155 ASP HB3 H 2.790 0.04 2 1507 254 155 ASP C C 177.700 0.30 1 1508 254 155 ASP CA C 57.810 0.30 1 1509 254 155 ASP CB C 44.300 0.30 1 1510 254 155 ASP N N 118.830 0.40 1 1511 255 156 ILE H H 7.920 0.04 1 1512 255 156 ILE HA H 3.690 0.04 1 1513 255 156 ILE HB H 1.770 0.04 1 1514 255 156 ILE HG12 H 1.430 0.04 2 1515 255 156 ILE HG13 H 1.610 0.04 2 1516 255 156 ILE HG2 H 0.890 0.04 1 1517 255 156 ILE HD1 H 0.780 0.04 1 1518 255 156 ILE C C 177.600 0.30 1 1519 255 156 ILE CA C 65.520 0.30 1 1520 255 156 ILE CB C 38.490 0.30 1 1521 255 156 ILE CG1 C 27.200 0.30 1 1522 255 156 ILE CD1 C 17.000 0.30 1 1523 255 156 ILE N N 118.800 0.40 1 1524 256 157 ARG H H 8.480 0.04 1 1525 256 157 ARG HA H 4.130 0.04 1 1526 256 157 ARG HB2 H 1.960 0.04 2 1527 256 157 ARG HG2 H 1.760 0.04 2 1528 256 157 ARG HD2 H 3.260 0.04 2 1529 256 157 ARG C C 180.500 0.30 1 1530 256 157 ARG CA C 59.400 0.30 1 1531 256 157 ARG CB C 29.850 0.30 1 1532 256 157 ARG CG C 27.300 0.30 1 1533 256 157 ARG CD C 43.500 0.30 1 1534 256 157 ARG N N 119.230 0.40 1 1535 257 158 GLY H H 8.310 0.04 1 1536 257 158 GLY HA2 H 3.820 0.04 2 1537 257 158 GLY HA3 H 3.970 0.04 2 1538 257 158 GLY C C 177.000 0.30 1 1539 257 158 GLY CA C 47.400 0.30 1 1540 257 158 GLY N N 108.170 0.40 1 1541 258 159 ILE H H 8.580 0.04 1 1542 258 159 ILE HA H 4.530 0.04 1 1543 258 159 ILE HB H 2.170 0.04 1 1544 258 159 ILE HG13 H 1.590 0.04 2 1545 258 159 ILE HG2 H 0.890 0.04 1 1546 258 159 ILE HD1 H 0.720 0.04 1 1547 258 159 ILE C C 177.800 0.30 1 1548 258 159 ILE CA C 61.110 0.30 1 1549 258 159 ILE CB C 31.900 0.30 1 1550 258 159 ILE CG1 C 24.200 0.30 1 1551 258 159 ILE CG2 C 20.600 0.30 1 1552 258 159 ILE N N 123.360 0.40 1 1553 259 160 GLN H H 8.680 0.04 1 1554 259 160 GLN HA H 4.510 0.04 1 1555 259 160 GLN HB2 H 2.270 0.04 2 1556 259 160 GLN HB3 H 2.040 0.04 2 1557 259 160 GLN HG2 H 2.960 0.04 2 1558 259 160 GLN HG3 H 2.760 0.04 2 1559 259 160 GLN HE21 H 7.750 0.04 2 1560 259 160 GLN HE22 H 6.970 0.04 2 1561 259 160 GLN C C 179.300 0.30 1 1562 259 160 GLN CA C 58.780 0.30 1 1563 259 160 GLN CB C 27.000 0.30 1 1564 259 160 GLN CG C 35.000 0.30 1 1565 259 160 GLN N N 123.720 0.40 1 1566 259 160 GLN NE2 N 113.800 0.40 1 1567 260 161 SER H H 7.980 0.04 1 1568 260 161 SER HA H 4.290 0.04 1 1569 260 161 SER HB2 H 4.120 0.04 2 1570 260 161 SER HB3 H 4.020 0.04 2 1571 260 161 SER C C 175.100 0.30 1 1572 260 161 SER CA C 61.420 0.30 1 1573 260 161 SER CB C 62.850 0.30 1 1574 260 161 SER N N 115.850 0.40 1 1575 261 162 LEU H H 6.980 0.04 1 1576 261 162 LEU HA H 4.490 0.04 1 1577 261 162 LEU HB2 H 1.880 0.04 2 1578 261 162 LEU HB3 H 1.730 0.04 2 1579 261 162 LEU HG H 1.58 0.04 2 1580 261 162 LEU HD1 H 0.650 0.04 2 1581 261 162 LEU HD2 H 0.800 0.04 2 1582 261 162 LEU C C 177.600 0.30 1 1583 261 162 LEU CA C 56.690 0.30 1 1584 261 162 LEU CB C 43.460 0.30 1 1585 261 162 LEU CG C 26.00 0.30 1 1586 261 162 LEU CD1 C 19.700 0.30 1 1587 261 162 LEU CD2 C 23.000 0.30 1 1588 261 162 LEU N N 119.000 0.40 1 1589 262 163 TYR H H 7.750 0.04 1 1590 262 163 TYR HA H 4.710 0.04 1 1591 262 163 TYR HB2 H 2.790 0.04 2 1592 262 163 TYR HB3 H 3.110 0.04 2 1593 262 163 TYR HD1 H 7.310 0.04 1 1594 262 163 TYR HE1 H 6.860 0.04 1 1595 262 163 TYR C C 174.500 0.30 1 1596 262 163 TYR CA C 59.000 0.30 1 1597 262 163 TYR CB C 40.780 0.30 1 1598 262 163 TYR CD1 C 131.600 0.30 1 1599 262 163 TYR CE1 C 116.000 0.30 1 1600 262 163 TYR N N 114.630 0.40 1 1601 263 164 GLY H H 8.150 0.04 1 1602 263 164 GLY HA2 H 3.870 0.04 2 1603 263 164 GLY HA3 H 4.490 0.04 2 1604 263 164 GLY C C 174.600 0.30 1 1605 263 164 GLY CA C 47.400 0.30 1 1606 263 164 GLY N N 115.840 0.40 1 stop_ save_