data_15120 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; SOLUTION STRUCTURE OF MATRIX METALLOPROTEINASE 3 (MMP-3) IN THE PRESENCE OF N-ISOBUTYL-N-[4-METHOXYPHENYLSULFONYL]GLYCYL HYDROXAMIC ACID (NNGH) ; _BMRB_accession_number 15120 _BMRB_flat_file_name bmr15120.str _Entry_type original _Submission_date 2007-01-30 _Accession_date 2007-01-30 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details ; Three dimensional structure of the catalytic domain of matrix metalloproteinase-3 (MMP3) complexed with the non-peptidic inhibitor N-isobutyl-N-[4-methoxy-phenylsulfonyl]glycyl hydroxamic acid (NNGH) ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Alcaraz Luis A. . 2 Banci Lucia . . 3 Bertini Ivano . . 4 Cantini Francesca . . 5 Donaire Antonio . . 6 Gonnelli Leonardo . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 711 "13C chemical shifts" 336 "15N chemical shifts" 155 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-05-25 update BMRB 'update entity name' 2008-07-02 update BMRB 'complete entry citation' 2007-10-17 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_MMP3-NNGH _Saveframe_category entry_citation _Citation_full . _Citation_title 'Matrix metalloproteinase-inhibitor interaction: the solution structure of the catalytic domain of human matrix metalloproteinase-3 with different inhibitors' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 17710450 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Alcaraz Luis A. . 2 Banci Lucia . . 3 Bertini Ivano . . 4 Cantini Francesca . . 5 Donaire Antonio . . 6 Gonnelli Leonardo . . stop_ _Journal_abbreviation 'J. Biol. Inorg. Chem.' _Journal_volume 12 _Journal_issue 8 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1197 _Page_last 1206 _Year 2007 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'MMP3 complexed with NNGH' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label MMP3 $entity_1 'ZINC ION, 1' $ZN 'ZINC ION, 2' $ZN 'CALCIUM ION, 1' $CA 'CALCIUM ION, 2' $CA NNGH $NGH stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_entity_1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common MMP3 _Molecular_mass 18053.283 _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 161 _Mol_residue_sequence ; GIPKWRKTHLTYRIVNYTPD LPKDAVDSAVEKALKVWEEV TPLTFSRLYEGEADIMISFA VREHGDFYPFDGPGNVLAHA YAPGPGINGDAHFDDDEQWT KDTTGTNLFLVAAHEIGHSL GLFHSANTEALMYPLYHSLT DLTRFRLSQDDINGIQSLYG P ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 88 GLY 2 89 ILE 3 90 PRO 4 91 LYS 5 92 TRP 6 93 ARG 7 94 LYS 8 95 THR 9 96 HIS 10 97 LEU 11 98 THR 12 99 TYR 13 100 ARG 14 101 ILE 15 102 VAL 16 103 ASN 17 104 TYR 18 105 THR 19 106 PRO 20 107 ASP 21 108 LEU 22 109 PRO 23 110 LYS 24 111 ASP 25 112 ALA 26 113 VAL 27 114 ASP 28 115 SER 29 116 ALA 30 117 VAL 31 118 GLU 32 119 LYS 33 120 ALA 34 121 LEU 35 122 LYS 36 123 VAL 37 124 TRP 38 125 GLU 39 126 GLU 40 127 VAL 41 128 THR 42 129 PRO 43 130 LEU 44 131 THR 45 132 PHE 46 133 SER 47 134 ARG 48 135 LEU 49 136 TYR 50 137 GLU 51 138 GLY 52 139 GLU 53 140 ALA 54 141 ASP 55 142 ILE 56 143 MET 57 144 ILE 58 145 SER 59 146 PHE 60 147 ALA 61 148 VAL 62 149 ARG 63 150 GLU 64 151 HIS 65 152 GLY 66 153 ASP 67 154 PHE 68 155 TYR 69 156 PRO 70 157 PHE 71 158 ASP 72 159 GLY 73 160 PRO 74 161 GLY 75 162 ASN 76 163 VAL 77 164 LEU 78 165 ALA 79 166 HIS 80 167 ALA 81 168 TYR 82 169 ALA 83 170 PRO 84 171 GLY 85 172 PRO 86 173 GLY 87 174 ILE 88 175 ASN 89 176 GLY 90 177 ASP 91 178 ALA 92 179 HIS 93 180 PHE 94 181 ASP 95 182 ASP 96 183 ASP 97 184 GLU 98 185 GLN 99 186 TRP 100 187 THR 101 188 LYS 102 189 ASP 103 190 THR 104 191 THR 105 192 GLY 106 193 THR 107 194 ASN 108 195 LEU 109 196 PHE 110 197 LEU 111 198 VAL 112 199 ALA 113 200 ALA 114 201 HIS 115 202 GLU 116 203 ILE 117 204 GLY 118 205 HIS 119 206 SER 120 207 LEU 121 208 GLY 122 209 LEU 123 210 PHE 124 211 HIS 125 212 SER 126 213 ALA 127 214 ASN 128 215 THR 129 216 GLU 130 217 ALA 131 218 LEU 132 219 MET 133 220 TYR 134 221 PRO 135 222 LEU 136 223 TYR 137 224 HIS 138 225 SER 139 226 LEU 140 227 THR 141 228 ASP 142 229 LEU 143 230 THR 144 231 ARG 145 232 PHE 146 233 ARG 147 234 LEU 148 235 SER 149 236 GLN 150 237 ASP 151 238 ASP 152 239 ILE 153 240 ASN 154 241 GLY 155 242 ILE 156 243 GLN 157 244 SER 158 245 LEU 159 246 TYR 160 247 GLY 161 248 PRO stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-02-06 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 15395 MMP3 100.00 161 99.38 99.38 7.52e-113 BMRB 15396 MMP3 100.00 161 99.38 99.38 7.52e-113 BMRB 4173 STROMELYSIN-1 100.00 173 100.00 100.00 7.96e-114 BMRB 4364 stromelysin 98.76 166 99.37 99.37 1.01e-111 BMRB 4365 stromelysin 98.76 166 99.37 99.37 1.01e-111 BMRB 4366 stromelysin 98.76 166 99.37 99.37 1.01e-111 PDB 1B3D Stromelysin-1 100.00 173 100.00 100.00 7.96e-114 PDB 1B8Y "X-Ray Structure Of Human Stromelysin Catalytic Domain Complexed With Non-Peptide Inhibitors: Implications For Inhibitor Selecti" 100.00 167 100.00 100.00 6.07e-114 PDB 1BIW "Design And Synthesis Of Conformationally-Constrained Mmp Inhibitors" 100.00 173 100.00 100.00 7.96e-114 PDB 1BM6 "Solution Structure Of The Catalytic Domain Of Human Stromelysin-1 Complexed To A Potent Non-Peptidic Inhibitor, Nmr, 20 Structu" 100.00 173 100.00 100.00 7.96e-114 PDB 1BQO "Discovery Of Potent, Achiral Matrix Metalloproteinase Inhibitors" 100.00 173 100.00 100.00 7.96e-114 PDB 1C3I "Human Stromelysin-1 Catalytic Domain Complexed With Ro-26-2812" 100.00 173 100.00 100.00 7.96e-114 PDB 1C8T "Human Stromelysin-1 (E202q) Catalytic Domain Complexed With Ro-26-2812" 100.00 167 99.38 100.00 2.11e-113 PDB 1CAQ "X-Ray Structure Of Human Stromelysin Catalytic Domain Complexes With Non-Peptide Inhibitors: Implication For Inhibitor Selectiv" 100.00 168 100.00 100.00 7.48e-114 PDB 1CIZ "X-ray Structure Of Human Stromelysin Catalytic Domain Complexes With Non-peptide Inhibitors: Implication For Inhibitor Selectiv" 100.00 168 100.00 100.00 7.48e-114 PDB 1CQR "Crystal Structure Of The Stromelysin Catalytic Domain At 2.0 A Resolution" 100.00 173 100.00 100.00 7.96e-114 PDB 1D5J "Crystal Structure Of Mmp3 Complexed With A Thiazepine Based Inhibitor." 100.00 173 100.00 100.00 7.96e-114 PDB 1D7X "Crystal Structure Of Mmp3 Complexed With A Modified Proline Scaffold Based Inhibitor." 100.00 173 100.00 100.00 7.96e-114 PDB 1D8F "Crystal Structure Of Mmp3 Complexed With A Piperazine Based Inhibitor." 100.00 173 100.00 100.00 7.96e-114 PDB 1D8M "Crystal Structure Of Mmp3 Complexed With A Heterocycle- Based Inhibitor" 100.00 173 100.00 100.00 7.96e-114 PDB 1G05 "Heterocycle-Based Mmp Inhibitor With P2'substituents" 100.00 173 100.00 100.00 7.96e-114 PDB 1G49 "A Carboxylic Acid Based Inhibitor In Complex With Mmp3" 100.00 173 100.00 100.00 7.96e-114 PDB 1G4K "X-ray Structure Of A Novel Matrix Metalloproteinase Inhibitor Complexed To Stromelysin" 100.00 168 100.00 100.00 7.48e-114 PDB 1HFS "Crystal Structure Of The Catalytic Domain Of Human Fibroblast Stromelysin-1 Inhibited With The N-Carboxy-Alkyl Inhibitor L-764," 99.38 160 100.00 100.00 2.02e-113 PDB 1HY7 "A Carboxylic Acid Based Inhibitor In Complex With Mmp3" 100.00 173 100.00 100.00 7.96e-114 PDB 1OO9 "Orientation In Solution Of Mmp-3 Catalytic Domain And N- Timp-1 From Residual Dipolar Couplings" 100.00 168 100.00 100.00 7.48e-114 PDB 1QIA "Crystal Structure Of Stromelysin Catalytic Domain" 99.38 162 100.00 100.00 2.85e-113 PDB 1QIC "Crystal Structure Of Stromelysin Catalytic Domain" 99.38 161 100.00 100.00 2.26e-113 PDB 1SLM "Crystal Structure Of Fibroblast Stromelysin-1: The C-Truncated Human Proenzyme" 100.00 255 100.00 100.00 1.21e-113 PDB 1SLN "Crystal Structure Of The Catalytic Domain Of Human Fibroblast Stromelysin-1 Inhibited With The N-Carboxy-Alkyl Inhibitor L-702," 100.00 173 100.00 100.00 7.96e-114 PDB 1UEA "Mmp-3TIMP-1 Complex" 100.00 173 98.76 98.76 1.07e-111 PDB 1UMS "Stromelysin-1 Catalytic Domain With Hydrophobic Inhibitor Bound, Ph 7.0, 32oc, 20 Mm Cacl2, 15% Acetonitrile; Nmr Ensemble Of 2" 100.00 174 100.00 100.00 8.24e-114 PDB 1UMT "Stromelysin-1 Catalytic Domain With Hydrophobic Inhibitor Bound, Ph 7.0, 32oc, 20 Mm Cacl2, 15% Acetonitrile; Nmr Average Of 20" 100.00 174 100.00 100.00 8.24e-114 PDB 1USN "Crystal Structure Of The Catalytic Domain Of Human Fibroblast Stromelysin-1 Inhibited With Thiadiazole Inhibitor Pnu-142372" 99.38 165 100.00 100.00 3.15e-113 PDB 2D1O "Stromelysin-1 (Mmp-3) Complexed To A Hydroxamic Acid Inhibitor" 100.00 171 100.00 100.00 8.21e-114 PDB 2JNP "Solution Structure Of Matrix Metalloproteinase 3 (Mmp-3) In The Presence Of N-Isobutyl-N-[4- Methoxyphenylsulfonyl]glycyl Hydro" 100.00 161 100.00 100.00 2.74e-114 PDB 2JT5 "Solution Structure Of Matrix Metalloproteinase 3 (mmp-3) In The Presence Of N-hydroxy-2-[n-(2-hydroxyethyl)biphenyl-4- Sulfonam" 100.00 161 100.00 100.00 2.74e-114 PDB 2JT6 "Solution Structure Of Matrix Metalloproteinase 3 (Mmp-3) In The Presence Of 3-4'-Cyanobyphenyl-4-Yloxy)-N- Hdydroxypropionamide" 100.00 161 100.00 100.00 2.74e-114 PDB 2SRT "Catalytic Domain Of Human Stromelysin-1 At Ph 5.5 And 40oc Complexed With Inhibitor" 100.00 173 100.00 100.00 7.96e-114 PDB 2USN "Crystal Structure Of The Catalytic Domain Of Human Fibroblast Stromelysin-1 Inhibited With Thiadiazole Inhibitor Pnu-141803" 99.38 165 100.00 100.00 3.15e-113 PDB 3OHL "Catalytic Domain Of Stromelysin-1 In Complex With N-Hydroxy-2-(4- Methoxy-N-(Pyridine-3-Ylmethyl)phenylsulfonamido)acetamide" 100.00 167 100.00 100.00 6.07e-114 PDB 3OHO "Catalytic Domain Of Stromelysin-1 In Complex With N-Hydroxy-2-(4- Methylphenylsulfonamido)acetamide" 100.00 169 100.00 100.00 1.02e-113 PDB 3USN "Structure Of The Catalytic Domain Of Human Fibroblast Stromelysin-1 Inhibited With The Thiadiazole Inhibitor Ipnu-107859, Nmr, " 100.00 168 100.00 100.00 7.48e-114 PDB 4DPE "Structure Of Mmp3 Complexed With A Platinum-based Inhibitor." 100.00 173 100.00 100.00 7.96e-114 PDB 4G9L "Structure Of Mmp3 Complexed With Nngh Inhibitor" 100.00 173 100.00 100.00 7.96e-114 PDB 4JA1 "Structure Of Mmp3 Complexed With A Platinum-based Inhibitor" 100.00 173 100.00 100.00 7.96e-114 DBJ BAD97003 "matrix metalloproteinase 3 preproprotein variant [Homo sapiens]" 100.00 477 100.00 100.00 5.16e-111 DBJ BAD97011 "matrix metalloproteinase 3 preproprotein variant [Homo sapiens]" 100.00 477 100.00 100.00 5.16e-111 DBJ BAG36115 "unnamed protein product [Homo sapiens]" 100.00 477 100.00 100.00 5.50e-111 EMBL CAA28859 "preprostromelysin [Homo sapiens]" 100.00 477 100.00 100.00 5.50e-111 GB AAA00036 "prostromelysin=matrix metalloproteinase [human, Peptide, 477 aa]" 100.00 477 100.00 100.00 5.16e-111 GB AAA36321 "matrix metalloproteinase-3 [Homo sapiens]" 100.00 477 100.00 100.00 5.16e-111 GB AAB36942 "stromelysin [Homo sapiens]" 100.00 477 100.00 100.00 5.16e-111 GB AAD45887 "stromelysin catalytic domain [synthetic construct]" 100.00 174 100.00 100.00 8.24e-114 GB AAH69676 "Matrix metallopeptidase 3 (stromelysin 1, progelatinase) [Homo sapiens]" 100.00 477 100.00 100.00 5.16e-111 REF NP_002413 "stromelysin-1 preproprotein [Homo sapiens]" 100.00 477 100.00 100.00 5.50e-111 REF XP_002822450 "PREDICTED: stromelysin-1 [Pongo abelii]" 100.00 477 99.38 100.00 7.46e-111 REF XP_003253099 "PREDICTED: stromelysin-1 [Nomascus leucogenys]" 100.00 477 99.38 100.00 5.94e-111 REF XP_003828425 "PREDICTED: stromelysin-1 [Pan paniscus]" 100.00 477 100.00 100.00 4.89e-111 REF XP_004052086 "PREDICTED: stromelysin-1 [Gorilla gorilla gorilla]" 100.00 477 98.76 99.38 2.03e-109 SP P08254 "RecName: Full=Stromelysin-1; Short=SL-1; AltName: Full=Matrix metalloproteinase-3; Short=MMP-3; AltName: Full=Transin-1; Flags:" 100.00 477 100.00 100.00 5.50e-111 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 . _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Wed Dec 20 05:48:03 2006 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons ZN ZN ZN N 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 . _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Wed Dec 20 02:01:48 2006 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons CA CA CA N 2 . ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ save_NGH _Saveframe_category ligand _Mol_type non-polymer _Name_common "NGH (N-ISOBUTYL-N-[4-METHOXYPHENYLSULFONYL]GLYCYL HYDROXAMIC ACID)" _BMRB_code . _PDB_code NGH _Molecular_mass 316.373 _Mol_charge 0 _Mol_paramagnetic . _Mol_aromatic . _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Wed Dec 20 04:22:12 2006 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons C1 C1 C N 0 . ? C10 C10 C N 0 . ? C11 C11 C N 0 . ? C12 C12 C N 0 . ? C13 C13 C N 0 . ? C14 C14 C N 0 . ? C2 C2 C N 0 . ? C3 C3 C N 0 . ? C4 C4 C N 0 . ? C5 C5 C N 0 . ? C6 C6 C N 0 . ? C7 C7 C N 0 . ? C9 C9 C N 0 . ? H1 H1 H N 0 . ? H101 H101 H N 0 . ? H102 H102 H N 0 . ? H12 H12 H N 0 . ? H131 H131 H N 0 . ? H132 H132 H N 0 . ? H133 H133 H N 0 . ? H141 H141 H N 0 . ? H142 H142 H N 0 . ? H143 H143 H N 0 . ? H2 H2 H N 0 . ? H4 H4 H N 0 . ? H5 H5 H N 0 . ? H71 H71 H N 0 . ? H72 H72 H N 0 . ? H73 H73 H N 0 . ? H91 H91 H N 0 . ? H92 H92 H N 0 . ? HN1 HN1 H N 0 . ? HO4 HO4 H N 0 . ? N N N R 0 . ? N1 N1 N N 0 . ? O1 O1 O N 0 . ? O2 O2 O N 0 . ? O3 O3 O N 0 . ? O4 O4 O N 0 . ? O5 O5 O N 0 . ? S1 S1 S N 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name DOUB C1 C2 ? ? SING C1 C6 ? ? SING C1 H1 ? ? SING C2 C3 ? ? SING C2 H2 ? ? DOUB C3 C4 ? ? SING C3 O1 ? ? SING C4 C5 ? ? SING C4 H4 ? ? DOUB C5 C6 ? ? SING C5 H5 ? ? SING C6 S1 ? ? SING O1 C7 ? ? SING C7 H71 ? ? SING C7 H72 ? ? SING C7 H73 ? ? DOUB S1 O2 ? ? DOUB S1 O3 ? ? SING S1 N ? ? SING N C9 ? ? SING N C10 ? ? SING C9 C12 ? ? SING C9 H91 ? ? SING C9 H92 ? ? SING C10 C11 ? ? SING C10 H101 ? ? SING C10 H102 ? ? SING C11 N1 ? ? DOUB C11 O5 ? ? SING N1 O4 ? ? SING N1 HN1 ? ? SING O4 HO4 ? ? SING C12 C13 ? ? SING C12 C14 ? ? SING C12 H12 ? ? SING C13 H131 ? ? SING C13 H132 ? ? SING C13 H133 ? ? SING C14 H141 ? ? SING C14 H142 ? ? SING C14 H143 ? ? 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 _Gene_mnemonic $entity_1 Human 9606 Eukaryota Metazoa Homo sapiens MMP-3 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 $entity_1 'recombinant technology' . Escherichia coli BL(DE3) pET21a stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_unlabelled _Saveframe_category sample _Sample_type solution _Details 'Tris 20mM, pH 8, ZnCl2 0.1mM, CaCl2 5mM, NaCl 300mM' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $entity_1 1 mM 'natural abundance' TRIS 20 mM 'natural abundance' 'sodium chloride' 300 mM 'natural abundance' ZnCl2 0.1 mM 'natural abundance' CaCl2 5 mM 'natural abundance' stop_ save_ save_13C_15N _Saveframe_category sample _Sample_type solution _Details 'Tris 20mM, pH 8, ZnCl2 0.1mM, CaCl2 5mM, NaCl 300mM' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $entity_1 1 mM '[U-98% 13C; U-98% 15N]' TRIS 20 mM 'natural abundance' 'sodium chloride' 300 mM 'natural abundance' ZnCl2 0.1 mM 'natural abundance' CaCl2 5 mM 'natural abundance' stop_ save_ save_15N _Saveframe_category sample _Sample_type solution _Details 'Tris 20mM, pH 8, ZnCl2 0.1mM, CaCl2 5mM, NaCl 300mM' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $entity_1 1 mM '[U-99% 15N]' TRIS 20 mM 'natural abundance' 'sodium chloride' 300 mM 'natural abundance' ZnCl2 0.1 mM 'natural abundance' CaCl2 5 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version . loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection stop_ _Details . save_ save_XEASY _Saveframe_category software _Name XEASY _Version . loop_ _Vendor _Address _Electronic_address 'Bartels et al.' . . stop_ loop_ _Task 'data analysis' stop_ _Details . save_ save_CARA _Saveframe_category software _Name CARA _Version 1.2 loop_ _Vendor _Address _Electronic_address 'Keller and Wuthrich' . . stop_ loop_ _Task 'data analysis' stop_ _Details . save_ save_CYANA _Saveframe_category software _Name CYANA _Version . loop_ _Vendor _Address _Electronic_address 'Guntert, Mumenthaler and Wuthrich' . . stop_ loop_ _Task 'structure solution' stop_ _Details . save_ save_AMBER _Saveframe_category software _Name AMBER _Version 8 loop_ _Vendor _Address _Electronic_address 'Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Koll' . . stop_ loop_ _Task refinement stop_ _Details . save_ save_SPARKY _Saveframe_category software _Name SPARKY _Version 3.110 loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'chemical shift assignment' 'data analysis' stop_ _Details . save_ save_CSI _Saveframe_category software _Name CSI _Version 2.0 loop_ _Vendor _Address _Electronic_address 'Wishart, D.S. and B.D. Sykes' . . stop_ loop_ _Task 'structure solution' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 900 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 800 _Details . save_ save_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-1H_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H NOESY' _Sample_label $unlabelled save_ save_2D_1H-15N_HSQC_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $15N save_ save_2D_1H-13C_HSQC_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC' _Sample_label $13C_15N save_ save_3D_CBCA(CO)NH_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $13C_15N save_ save_3D_HNCACB_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $13C_15N save_ save_3D_(H)CCH-TOCSY_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D (H)CCH-TOCSY' _Sample_label $13C_15N save_ save_3D_1H-15N_NOESY_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $15N save_ save_3D_1H-13C_NOESY_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-13C NOESY' _Sample_label $13C_15N save_ save_3D_HNCA_9 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $13C_15N save_ save_3D_HN(CO)CA_10 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $13C_15N save_ save_Filtered_NOESY_11 _Saveframe_category NMR_applied_experiment _Experiment_name 'Filtered NOESY' _Sample_label $13C_15N save_ save_3D_HNHA_12 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNHA' _Sample_label $13C_15N save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.32 . M pH 8 . pH pressure 1 . atm temperature 298 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0.00 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 . indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-1H NOESY' '2D 1H-15N HSQC' '2D 1H-13C HSQC' '3D CBCA(CO)NH' '3D HNCACB' '3D (H)CCH-TOCSY' '3D 1H-15N NOESY' '3D 1H-13C NOESY' '3D HNCA' '3D HN(CO)CA' 'Filtered NOESY' stop_ loop_ _Sample_label $unlabelled $15N $13C_15N stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name MMP3 _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 88 1 GLY HA2 H 4.23 0.02 . 2 89 2 ILE H H 8.54 0.02 . 3 89 2 ILE HA H 3.79 0.02 . 4 89 2 ILE HB H 1.96 0.02 . 5 89 2 ILE HG12 H 1.03 0.02 . 6 89 2 ILE HG2 H 0.81 0.02 . 7 89 2 ILE N N 116.3 0.2 . 8 90 3 PRO HA H 4.08 0.02 . 9 90 3 PRO HB2 H 1.93 0.02 . 10 90 3 PRO HB3 H 2.22 0.02 . 11 90 3 PRO HG2 H 1.84 0.02 . 12 90 3 PRO HD2 H 3.23 0.02 . 13 90 3 PRO HD3 H 3.29 0.02 . 14 90 3 PRO CA C 61.2 0.2 . 15 90 3 PRO CB C 28.7 0.2 . 16 90 3 PRO CG C 24.16 0.2 . 17 90 3 PRO CD C 46.39 0.2 . 18 91 4 LYS H H 7.04 0.02 . 19 91 4 LYS HA H 3.46 0.02 . 20 91 4 LYS HB2 H 2.16 0.02 . 21 91 4 LYS HG2 H 0.85 0.02 . 22 91 4 LYS HD2 H 1.79 0.02 . 23 91 4 LYS HE2 H 3.42 0.02 . 24 91 4 LYS CA C 57.8 0.2 . 25 91 4 LYS CB C 29.8 0.2 . 26 91 4 LYS CG C 19.06 0.2 . 27 91 4 LYS CD C 24.24 0.2 . 28 91 4 LYS CE C 47.07 0.2 . 29 91 4 LYS N N 111.8 0.2 . 30 92 5 TRP H H 8.21 0.02 . 31 92 5 TRP HA H 4.34 0.02 . 32 92 5 TRP HB2 H 3.20 0.02 . 33 92 5 TRP HB3 H 3.57 0.02 . 34 92 5 TRP HD1 H 7.59 0.02 . 35 92 5 TRP HE1 H 10.01 0.02 . 36 92 5 TRP HZ2 H 7.94 0.02 . 37 92 5 TRP CA C 53.7 0.2 . 38 92 5 TRP N N 123.5 0.2 . 39 92 5 TRP NE1 N 129.4 0.2 . 40 93 6 ARG H H 7.91 0.02 . 41 93 6 ARG HA H 3.87 0.02 . 42 93 6 ARG HB2 H 1.45 0.02 . 43 93 6 ARG HG2 H 1.68 0.02 . 44 93 6 ARG HG3 H 1.8 0.02 . 45 93 6 ARG HD2 H 3.40 0.02 . 46 93 6 ARG HD3 H 2.91 0.02 . 47 93 6 ARG CA C 52.9 0.2 . 48 93 6 ARG CB C 26.4 0.2 . 49 93 6 ARG CG C 30.2 0.2 . 50 93 6 ARG CD C 37.3 0.2 . 51 93 6 ARG N N 119.6 0.2 . 52 94 7 LYS H H 7.47 0.02 . 53 94 7 LYS HA H 4.22 0.02 . 54 94 7 LYS HB2 H 2.5 0.02 . 55 94 7 LYS HG2 H 1.28 0.02 . 56 94 7 LYS HG3 H 0.99 0.02 . 57 94 7 LYS HD2 H 1.80 0.02 . 58 94 7 LYS HE2 H 2.90 0.02 . 59 94 7 LYS HE3 H 2.67 0.02 . 60 94 7 LYS CA C 53.4 0.2 . 61 94 7 LYS CB C 33.3 0.2 . 62 94 7 LYS CG C 18.85 0.2 . 63 94 7 LYS CD C 26.78 0.2 . 64 94 7 LYS CE C 43.13 0.2 . 65 94 7 LYS N N 116.7 0.2 . 66 95 8 THR H H 7.99 0.02 . 67 95 8 THR HA H 4.25 0.02 . 68 95 8 THR HG2 H 1.28 0.02 . 69 95 8 THR CA C 58.5 0.2 . 70 95 8 THR CB C 66.9 0.2 . 71 95 8 THR CG2 C 18.63 0.2 . 72 95 8 THR N N 105.3 0.2 . 73 96 9 HIS H H 7.02 0.02 . 74 96 9 HIS HA H 4.69 0.02 . 75 96 9 HIS HB2 H 2.88 0.02 . 76 96 9 HIS HB3 H 2.92 0.02 . 77 96 9 HIS CA C 51.4 0.2 . 78 96 9 HIS CB C 26.6 0.2 . 79 96 9 HIS N N 119.8 0.2 . 80 97 10 LEU H H 8.16 0.02 . 81 97 10 LEU HA H 4.99 0.02 . 82 97 10 LEU HB2 H 1.05 0.02 . 83 97 10 LEU HG H 0.69 0.02 . 84 97 10 LEU HD1 H -0.43 0.02 . 85 97 10 LEU HD2 H -0.14 0.02 . 86 97 10 LEU CA C 51.2 0.2 . 87 97 10 LEU N N 127.5 0.2 . 88 98 11 THR H H 9.24 0.02 . 89 98 11 THR HA H 5.54 0.02 . 90 98 11 THR HB H 4.01 0.02 . 91 98 11 THR HG2 H 0.75 0.02 . 92 98 11 THR CA C 55.4 0.2 . 93 98 11 THR CB C 70.3 0.2 . 94 98 11 THR N N 110.8 0.2 . 95 99 12 TYR H H 8.56 0.02 . 96 99 12 TYR HA H 5.53 0.02 . 97 99 12 TYR HB2 H 1.68 0.02 . 98 99 12 TYR HB3 H 2.67 0.02 . 99 99 12 TYR HD2 H 6.27 0.02 . 100 99 12 TYR HE1 H 7.21 0.02 . 101 99 12 TYR CA C 51.8 0.2 . 102 99 12 TYR CB C 39.3 0.2 . 103 99 12 TYR N N 117.5 0.2 . 104 100 13 ARG H H 8.15 0.02 . 105 100 13 ARG HA H 4.27 0.02 . 106 100 13 ARG HB2 H 2.09 0.02 . 107 100 13 ARG HB3 H 1.96 0.02 . 108 100 13 ARG HG2 H 1.5 0.02 . 109 100 13 ARG HG3 H 1.68 0.02 . 110 100 13 ARG HD2 H 3.22 0.02 . 111 100 13 ARG CA C 51.7 0.2 . 112 100 13 ARG CB C 32.0 0.2 . 113 100 13 ARG CG C 30.13 0.2 . 114 100 13 ARG CD C 39.58 0.2 . 115 100 13 ARG N N 119.2 0.2 . 116 101 14 ILE H H 8.32 0.02 . 117 101 14 ILE HA H 4.71 0.02 . 118 101 14 ILE HB H 1.54 0.02 . 119 101 14 ILE HG12 H 1.35 0.02 . 120 101 14 ILE HG2 H 0.1771 0.02 . 121 101 14 ILE HD1 H 0.86 0.02 . 122 101 14 ILE CA C 58.6 0.2 . 123 101 14 ILE CB C 34.3 0.2 . 124 101 14 ILE CG1 C 25.45 0.2 . 125 101 14 ILE CG2 C 14.5 0.2 . 126 101 14 ILE CD1 C 11.32 0.2 . 127 101 14 ILE N N 128.2 0.2 . 128 102 15 VAL H H 9.47 0.02 . 129 102 15 VAL HA H 3.29 0.02 . 130 102 15 VAL HB H 1.94 0.02 . 131 102 15 VAL HG1 H 0.89 0.02 . 132 102 15 VAL HG2 H 0.86 0.02 . 133 102 15 VAL CA C 63.2 0.2 . 134 102 15 VAL CB C 30 0.2 . 135 102 15 VAL CG1 C 20.68 0.2 . 136 102 15 VAL CG2 C 18.37 0.2 . 137 102 15 VAL N N 129.8 0.2 . 138 103 16 ASN H H 7.57 0.02 . 139 103 16 ASN HA H 4.68 0.02 . 140 103 16 ASN HB2 H 3.05 0.02 . 141 103 16 ASN HB3 H 2.82 0.02 . 142 103 16 ASN HD21 H 6.80 0.02 . 143 103 16 ASN HD22 H 7.45 0.02 . 144 103 16 ASN CA C 56.2 0.2 . 145 103 16 ASN CB C 36.3 0.2 . 146 103 16 ASN N N 116.1 0.2 . 147 103 16 ASN ND2 N 112.9 0.2 . 148 104 17 TYR H H 8.04 0.02 . 149 104 17 TYR HA H 4.09 0.02 . 150 104 17 TYR HB2 H 2.91 0.02 . 151 104 17 TYR CA C 57.0 0.2 . 152 104 17 TYR CB C 37.8 0.2 . 153 104 17 TYR N N 111.9 0.2 . 154 105 18 THR H H 8.42 0.02 . 155 105 18 THR HA H 3.99 0.02 . 156 105 18 THR HB H 1.94 0.02 . 157 105 18 THR HG2 H 0.31 0.02 . 158 106 19 PRO HA H 4.50 0.02 . 159 107 20 ASP H H 8.82 0.02 . 160 107 20 ASP HA H 4.06 0.02 . 161 107 20 ASP HB2 H 2.61 0.02 . 162 107 20 ASP HB3 H 2.91 0.02 . 163 107 20 ASP CA C 53.8 0.2 . 164 107 20 ASP CB C 38.7 0.2 . 165 107 20 ASP N N 121.7 0.2 . 166 108 21 LEU H H 6.92 0.02 . 167 108 21 LEU HA H 4.77 0.02 . 168 108 21 LEU HB2 H 1.07 0.02 . 169 108 21 LEU HB3 H 1.47 0.02 . 170 108 21 LEU HG H 0.44 0.02 . 171 108 21 LEU HD1 H 1.01 0.02 . 172 108 21 LEU HD2 H 0.41 0.02 . 173 108 21 LEU CA C 48.4 0.2 . 174 108 21 LEU CB C 44.5 0.2 . 175 108 21 LEU CG C 23.56 0.2 . 176 108 21 LEU CD1 C 21.84 0.2 . 177 108 21 LEU N N 116.5 0.2 . 178 109 22 PRO HA H 4.38 0.02 . 179 109 22 PRO HB2 H 2.34 0.02 . 180 109 22 PRO HB3 H 1.95 0.02 . 181 109 22 PRO CA C 59.4 0.2 . 182 109 22 PRO CB C 29.2 0.2 . 183 109 22 PRO CG C 25.24 0.2 . 184 109 22 PRO CD C 50.87 0.2 . 185 110 23 LYS H H 8.58 0.02 . 186 110 23 LYS HA H 3.79 0.02 . 187 110 23 LYS HB2 H 1.34 0.02 . 188 110 23 LYS HB3 H 1.25 0.02 . 189 110 23 LYS HG2 H 0.79 0.02 . 190 110 23 LYS HG3 H 0.55 0.02 . 191 110 23 LYS HD2 H 1.14 0.02 . 192 110 23 LYS HD3 H 1.02 0.02 . 193 110 23 LYS HE2 H 2.61 0.02 . 194 110 23 LYS HE3 H 2.52 0.02 . 195 110 23 LYS CA C 57.9 0.2 . 196 110 23 LYS CB C 29.4 0.2 . 197 110 23 LYS CG C 21.6 0.2 . 198 110 23 LYS CD C 26.51 0.2 . 199 110 23 LYS CE C 39.17 0.2 . 200 110 23 LYS N N 123.8 0.2 . 201 111 24 ASP H H 8.45 0.02 . 202 111 24 ASP HA H 4.22 0.02 . 203 111 24 ASP HB2 H 2.55 0.02 . 204 111 24 ASP HB3 H 2.69 0.02 . 205 111 24 ASP CA C 53.9 0.2 . 206 111 24 ASP CB C 37.1 0.2 . 207 111 24 ASP N N 113.6 0.2 . 208 112 25 ALA H H 7.26 0.02 . 209 112 25 ALA HA H 4.21 0.02 . 210 112 25 ALA HB H 1.47 0.02 . 211 112 25 ALA CA C 51.5 0.2 . 212 112 25 ALA CB C 16.2 0.2 . 213 112 25 ALA N N 122.4 0.2 . 214 113 26 VAL H H 7.47 0.02 . 215 113 26 VAL HA H 3.63 0.02 . 216 113 26 VAL HB H 1.94 0.02 . 217 113 26 VAL HG1 H 0.41 0.02 . 218 113 26 VAL HG2 H 0.59 0.02 . 219 113 26 VAL CA C 62.7 0.2 . 220 113 26 VAL CB C 28.6 0.2 . 221 113 26 VAL CG1 C 18.85 0.2 . 222 113 26 VAL N N 121.7 0.2 . 223 114 27 ASP H H 8.49 0.02 . 224 114 27 ASP HA H 4.07 0.02 . 225 114 27 ASP HB2 H 2.51 0.02 . 226 114 27 ASP HB3 H 2.58 0.02 . 227 114 27 ASP CA C 55.7 0.2 . 228 114 27 ASP CB C 37.1 0.2 . 229 114 27 ASP N N 119.3 0.2 . 230 115 28 SER H H 8.00 0.02 . 231 115 28 SER HA H 4.12 0.02 . 232 115 28 SER HB2 H 3.44 0.02 . 233 115 28 SER HB3 H 3.64 0.02 . 234 115 28 SER CA C 58.8 0.2 . 235 115 28 SER CB C 60.5 0.2 . 236 115 28 SER N N 112.5 0.2 . 237 116 29 ALA H H 7.63 0.02 . 238 116 29 ALA HA H 3.94 0.02 . 239 116 29 ALA HB H 1.32 0.02 . 240 116 29 ALA CA C 52.9 0.2 . 241 116 29 ALA CB C 15.5 0.2 . 242 116 29 ALA N N 124.1 0.2 . 243 117 30 VAL H H 7.94 0.02 . 244 117 30 VAL HA H 3.13 0.02 . 245 117 30 VAL HB H 2.38 0.02 . 246 117 30 VAL HG1 H 0.63 0.02 . 247 117 30 VAL HG2 H 0.41 0.02 . 248 117 30 VAL CA C 64.3 0.2 . 249 117 30 VAL CB C 28.7 0.2 . 250 117 30 VAL CG1 C 19.47 0.2 . 251 117 30 VAL CG2 C 19.4 0.2 . 252 117 30 VAL N N 115.7 0.2 . 253 118 31 GLU H H 8.33 0.02 . 254 118 31 GLU HA H 3.58 0.02 . 255 118 31 GLU HB2 H 2.07 0.02 . 256 118 31 GLU HB3 H 1.95 0.02 . 257 118 31 GLU HG2 H 2.10 0.02 . 258 118 31 GLU HG3 H 2.36 0.02 . 259 118 31 GLU CA C 57.5 0.2 . 260 118 31 GLU CB C 26.9 0.2 . 261 118 31 GLU CG C 33.99 0.2 . 262 118 31 GLU N N 118 0.2 . 263 119 32 LYS H H 8.23 0.02 . 264 119 32 LYS HA H 3.81 0.02 . 265 119 32 LYS HB2 H 1.85 0.02 . 266 119 32 LYS HB3 H 2.09 0.02 . 267 119 32 LYS HG2 H 0.90 0.02 . 268 119 32 LYS HG3 H 1.22 0.02 . 269 119 32 LYS HD2 H 1.054 0.02 . 270 119 32 LYS HD3 H 1.07 0.02 . 271 119 32 LYS HE2 H 2.35 0.02 . 272 119 32 LYS HE3 H 2.40 0.02 . 273 119 32 LYS CA C 56.8 0.2 . 274 119 32 LYS CB C 29.5 0.2 . 275 119 32 LYS CG C 26.19 0.2 . 276 119 32 LYS CD C 23.17 0.2 . 277 119 32 LYS CE C 39.09 0.2 . 278 119 32 LYS N N 119.1 0.2 . 279 120 33 ALA H H 8.03 0.02 . 280 120 33 ALA HA H 4.50 0.02 . 281 120 33 ALA HB H 0.75 0.02 . 282 120 33 ALA CA C 52.6 0.2 . 283 120 33 ALA CB C 16.3 0.2 . 284 120 33 ALA N N 123.3 0.2 . 285 122 35 LYS H H 7.78 0.02 . 286 122 35 LYS HA H 3.97 0.02 . 287 122 35 LYS HB2 H 1.90 0.02 . 288 122 35 LYS HB3 H 2.02 0.02 . 289 122 35 LYS HG2 H 1.39 0.02 . 290 122 35 LYS HG3 H 1.52 0.02 . 291 122 35 LYS HD2 H 1.63 0.02 . 292 122 35 LYS HE2 H 2.78 0.02 . 293 122 35 LYS CA C 56.2 0.2 . 294 122 35 LYS CB C 29.3 0.2 . 295 122 35 LYS CG C 22.34 0.2 . 296 122 35 LYS CD C 26.07 0.2 . 297 122 35 LYS CE C 37.48 0.2 . 298 122 35 LYS N N 118.9 0.2 . 299 123 36 VAL H H 7.35 0.02 . 300 123 36 VAL HA H 3.46 0.02 . 301 123 36 VAL HB H 1.36 0.02 . 302 123 36 VAL HG1 H 0.64 0.02 . 303 123 36 VAL HG2 H 0.79 0.02 . 304 123 36 VAL CA C 63.5 0.2 . 305 123 36 VAL CB C 28.4 0.2 . 306 123 36 VAL CG1 C 21.29 0.2 . 307 123 36 VAL CG2 C 18.67 0.2 . 308 123 36 VAL N N 115.1 0.2 . 309 124 37 TRP H H 6.58 0.02 . 310 124 37 TRP HA H 4.84 0.02 . 311 124 37 TRP HB2 H 2.92 0.02 . 312 124 37 TRP HB3 H 3.09 0.02 . 313 124 37 TRP HD1 H 7.47 0.02 . 314 124 37 TRP HE1 H 9.89 0.02 . 315 124 37 TRP HZ2 H 7.04 0.02 . 316 124 37 TRP CA C 54.8 0.2 . 317 124 37 TRP CB C 27.1 0.2 . 318 124 37 TRP N N 117.2 0.2 . 319 124 37 TRP NE1 N 126.2 0.2 . 320 125 38 GLU H H 8.43 0.02 . 321 125 38 GLU HA H 4.72 0.02 . 322 125 38 GLU HB2 H 1.99 0.02 . 323 125 38 GLU HG2 H 2.916 0.02 . 324 125 38 GLU N N 121.4 0.2 . 325 126 39 GLU H H 7.74 0.02 . 326 126 39 GLU HA H 4.09 0.02 . 327 126 39 GLU HB2 H 2.27 0.02 . 328 126 39 GLU HB3 H 2.04 0.02 . 329 126 39 GLU HG2 H 2.55 0.02 . 330 126 39 GLU N N 113.4 0.2 . 331 127 40 VAL H H 7.02 0.02 . 332 127 40 VAL HA H 4.80 0.02 . 333 127 40 VAL HB H 2.58 0.02 . 334 127 40 VAL HG1 H 1.11 0.02 . 335 127 40 VAL HG2 H 0.8 0.02 . 336 127 40 VAL N N 106.2 0.2 . 337 128 41 THR H H 7.3 0.02 . 338 128 41 THR HA H 5.42 0.02 . 339 128 41 THR HB H 4.20 0.02 . 340 128 41 THR HG2 H 1.437 0.02 . 341 128 41 THR CA C 57.4 0.2 . 342 128 41 THR CB C 69.5 0.2 . 343 128 41 THR CG2 C 21.76 0.2 . 344 128 41 THR N N 108.9 0.2 . 345 129 42 PRO HA H 5.33 0.02 . 346 129 42 PRO HB2 H 2.06 0.02 . 347 130 43 LEU H H 7.25 0.02 . 348 130 43 LEU HA H 4.39 0.02 . 349 130 43 LEU HB2 H 1.50 0.02 . 350 130 43 LEU HB3 H 1.59 0.02 . 351 130 43 LEU HG H 1.27 0.02 . 352 130 43 LEU HD1 H 0.43 0.02 . 353 130 43 LEU HD2 H 0.1565 0.02 . 354 130 43 LEU CA C 52.1 0.2 . 355 130 43 LEU CB C 39.8 0.2 . 356 130 43 LEU CG C 23.83 0.2 . 357 130 43 LEU CD1 C 22.17 0.2 . 358 130 43 LEU CD2 C 20.89 0.2 . 359 130 43 LEU N N 118.5 0.2 . 360 131 44 THR H H 8.00 0.02 . 361 131 44 THR HA H 4.43 0.02 . 362 131 44 THR HB H 4.02 0.02 . 363 131 44 THR HG2 H 0.9978 0.02 . 364 131 44 THR CA C 57.3 0.2 . 365 131 44 THR CB C 69.6 0.2 . 366 131 44 THR CG2 C 18.73 0.2 . 367 131 44 THR N N 110.2 0.2 . 368 132 45 PHE H H 8.21 0.02 . 369 132 45 PHE HA H 5.64 0.02 . 370 132 45 PHE HB2 H 2.73 0.02 . 371 132 45 PHE HB3 H 2.75 0.02 . 372 132 45 PHE HD1 H 6.964 0.02 . 373 132 45 PHE HE1 H 6.747 0.02 . 374 132 45 PHE CA C 53.4 0.2 . 375 132 45 PHE CB C 40.7 0.2 . 376 132 45 PHE N N 117.3 0.2 . 377 133 46 SER H H 8.67 0.02 . 378 133 46 SER HA H 4.74 0.02 . 379 133 46 SER HB2 H 3.58 0.02 . 380 133 46 SER HB3 H 3.80 0.02 . 381 133 46 SER CA C 54.6 0.2 . 382 133 46 SER CB C 62.7 0.2 . 383 133 46 SER N N 116.7 0.2 . 384 134 47 ARG H H 8.54 0.02 . 385 134 47 ARG HA H 4.60 0.02 . 386 134 47 ARG HB2 H 1.24 0.02 . 387 134 47 ARG HB3 H 1.42 0.02 . 388 134 47 ARG HD2 H 2.74 0.02 . 389 134 47 ARG HE H 6.11 0.02 . 390 134 47 ARG N N 125.1 0.2 . 391 135 48 LEU H H 8.45 0.02 . 392 135 48 LEU HA H 4.58 0.02 . 393 135 48 LEU HB2 H 1.50 0.02 . 394 135 48 LEU HB3 H 1.15 0.02 . 395 135 48 LEU HG H 0.7837 0.02 . 396 135 48 LEU HD1 H -0.171 0.02 . 397 135 48 LEU HD2 H -0.594 0.02 . 398 135 48 LEU CA C 50.2 0.2 . 399 135 48 LEU CB C 42.7 0.2 . 400 135 48 LEU CG C 24.62 0.2 . 401 135 48 LEU CD1 C 22.33 0.2 . 402 135 48 LEU CD2 C 20.13 0.2 . 403 135 48 LEU N N 125.2 0.2 . 404 136 49 TYR H H 9.20 0.02 . 405 136 49 TYR HA H 4.33 0.02 . 406 136 49 TYR HB2 H 3.15 0.02 . 407 136 49 TYR HB3 H 2.93 0.02 . 408 136 49 TYR HD2 H 7.072 0.02 . 409 136 49 TYR HE1 H 6.809 0.02 . 410 136 49 TYR CA C 55.5 0.2 . 411 136 49 TYR CB C 36.3 0.2 . 412 136 49 TYR N N 118.9 0.2 . 413 137 50 GLU H H 7.49 0.02 . 414 137 50 GLU HA H 4.68 0.02 . 415 137 50 GLU HB2 H 1.82 0.02 . 416 137 50 GLU HB3 H 1.99 0.02 . 417 137 50 GLU HG2 H 1.98 0.02 . 418 137 50 GLU HG3 H 2.07 0.02 . 419 137 50 GLU CA C 51.8 0.2 . 420 137 50 GLU CB C 30.1 0.2 . 421 137 50 GLU CG C 32.34 0.2 . 422 137 50 GLU N N 116.6 0.2 . 423 138 51 GLY H H 8.50 0.02 . 424 138 51 GLY HA2 H 3.95 0.02 . 425 138 51 GLY CA C 41.9 0.2 . 426 138 51 GLY N N 108.3 0.2 . 427 139 52 GLU H H 8.16 0.02 . 428 139 52 GLU HA H 4.19 0.02 . 429 139 52 GLU HB2 H 2.02 0.02 . 430 139 52 GLU HG2 H 2.138 0.02 . 431 139 52 GLU HG3 H 2.067 0.02 . 432 139 52 GLU CA C 53.6 0.2 . 433 139 52 GLU CB C 26.9 0.2 . 434 139 52 GLU CG C 33.4 0.2 . 435 139 52 GLU N N 119 0.2 . 436 140 53 ALA H H 7.98 0.02 . 437 140 53 ALA HA H 4.36 0.02 . 438 140 53 ALA HB H 1.1 0.02 . 439 140 53 ALA CA C 46.9 0.2 . 440 140 53 ALA CB C 19.0 0.2 . 441 140 53 ALA N N 131.5 0.2 . 442 141 54 ASP H H 8.27 0.02 . 443 141 54 ASP HA H 4.43 0.02 . 444 141 54 ASP CA C 56.6 0.2 . 445 141 54 ASP CB C 38.6 0.2 . 446 141 54 ASP N N 121.8 0.2 . 447 142 55 ILE H H 8.43 0.02 . 448 142 55 ILE HA H 4.37 0.02 . 449 142 55 ILE HB H 1.78 0.02 . 450 142 55 ILE HG2 H 0.89 0.02 . 451 142 55 ILE HD1 H 0.80 0.02 . 452 142 55 ILE CA C 57.9 0.2 . 453 142 55 ILE CB C 36.3 0.2 . 454 142 55 ILE CG1 C 24.03 0.2 . 455 142 55 ILE CG2 C 14.07 0.2 . 456 142 55 ILE CD1 C 10.49 0.2 . 457 142 55 ILE N N 123.5 0.2 . 458 143 56 MET H H 7.23 0.02 . 459 143 56 MET HA H 4.21 0.02 . 460 143 56 MET HB2 H 1.85 0.02 . 461 143 56 MET HB3 H 1.97 0.02 . 462 143 56 MET HE H 2.574 0.02 . 463 143 56 MET CA C 50.5 0.2 . 464 143 56 MET CB C 30.8 0.2 . 465 143 56 MET N N 126.4 0.2 . 466 144 57 ILE H H 9.17 0.02 . 467 144 57 ILE HA H 5.3 0.02 . 468 144 57 ILE HB H 1.76 0.02 . 469 144 57 ILE HG12 H 1.70 0.02 . 470 144 57 ILE HG13 H 1.07 0.02 . 471 144 57 ILE HG2 H 0.77 0.02 . 472 144 57 ILE HD1 H 0.58 0.02 . 473 144 57 ILE CA C 58.3 0.2 . 474 144 57 ILE CB C 36.8 0.2 . 475 144 57 ILE CG1 C 26.2 0.2 . 476 144 57 ILE CG2 C 14.33 0.2 . 477 144 57 ILE CD1 C 13.55 0.2 . 478 144 57 ILE N N 128.6 0.2 . 479 145 58 SER H H 8.51 0.02 . 480 145 58 SER HA H 4.96 0.02 . 481 145 58 SER HB2 H 3.67 0.02 . 482 145 58 SER HB3 H 3.17 0.02 . 483 145 58 SER CA C 54.5 0.2 . 484 145 58 SER CB C 63.5 0.2 . 485 145 58 SER N N 118.2 0.2 . 486 146 59 PHE H H 9.43 0.02 . 487 146 59 PHE HA H 5.23 0.02 . 488 146 59 PHE HB2 H 2.74 0.02 . 489 146 59 PHE HB3 H 2.65 0.02 . 490 146 59 PHE CA C 53.7 0.2 . 491 146 59 PHE CB C 39.1 0.2 . 492 146 59 PHE N N 120 0.2 . 493 147 60 ALA H H 9.26 0.02 . 494 147 60 ALA HA H 4.76 0.02 . 495 147 60 ALA HB H 0.98 0.02 . 496 147 60 ALA CA C 48.3 0.2 . 497 147 60 ALA CB C 20.5 0.2 . 498 147 60 ALA N N 125.5 0.2 . 499 148 61 VAL H H 8.16 0.02 . 500 148 61 VAL HA H 4.73 0.02 . 501 148 61 VAL HB H 2.12 0.02 . 502 148 61 VAL HG1 H 0.79 0.02 . 503 148 61 VAL HG2 H 0.83 0.02 . 504 148 61 VAL N N 111.5 0.2 . 505 149 62 ARG H H 9.61 0.02 . 506 149 62 ARG HA H 4.70 0.02 . 507 149 62 ARG HB2 H 2.10 0.02 . 508 149 62 ARG HB3 H 2.25 0.02 . 509 149 62 ARG HG2 H 1.54 0.02 . 510 149 62 ARG HG3 H 1.82 0.02 . 511 149 62 ARG HD2 H 3.179 0.02 . 512 149 62 ARG CA C 52.5 0.2 . 513 149 62 ARG CB C 26.5 0.2 . 514 149 62 ARG N N 117.3 0.2 . 515 150 63 GLU H H 7.55 0.02 . 516 150 63 GLU HA H 4.06 0.02 . 517 150 63 GLU HB2 H 1.94 0.02 . 518 150 63 GLU HB3 H 2.01 0.02 . 519 150 63 GLU HG2 H 2.263 0.02 . 520 150 63 GLU HG3 H 2.533 0.02 . 521 150 63 GLU CA C 55.4 0.2 . 522 150 63 GLU CB C 27.8 0.2 . 523 150 63 GLU CG C 34 0.2 . 524 150 63 GLU N N 124.7 0.2 . 525 151 64 HIS H H 9.29 0.02 . 526 151 64 HIS HA H 4.20 0.02 . 527 151 64 HIS HB2 H 2.95 0.02 . 528 151 64 HIS HD2 H 6.763 0.02 . 529 151 64 HIS CA C 60.4 0.2 . 530 151 64 HIS CB C 31.8 0.2 . 531 151 64 HIS N N 123.7 0.2 . 532 152 65 GLY H H 8.07 0.02 . 533 152 65 GLY HA2 H 3.88 0.02 . 534 152 65 GLY CA C 53.3 0.2 . 535 152 65 GLY N N 109 0.2 . 536 153 66 ASP H H 6.82 0.02 . 537 153 66 ASP HA H 4.69 0.02 . 538 153 66 ASP HB2 H 2.91 0.02 . 539 153 66 ASP HB3 H 2.71 0.02 . 540 153 66 ASP CB C 41.4 0.2 . 541 153 66 ASP N N 115.6 0.2 . 542 154 67 PHE H H 7.81 0.02 . 543 154 67 PHE HA H 4.05 0.02 . 544 154 67 PHE HD1 H 6.43 0.02 . 545 154 67 PHE N N 115.6 0.2 . 546 155 68 TYR H H 6.77 0.02 . 547 155 68 TYR HA H 4.45 0.02 . 548 155 68 TYR HE1 H 7.06 0.02 . 549 155 68 TYR N N 116.8 0.2 . 550 156 69 PRO HA H 3.92 0.02 . 551 156 69 PRO HB2 H 2.75 0.02 . 552 157 70 PHE H H 8.50 0.02 . 553 157 70 PHE HA H 3.99 0.02 . 554 157 70 PHE HB2 H 2.99 0.02 . 555 157 70 PHE HD1 H 6.601 0.02 . 556 157 70 PHE HE1 H 7.202 0.02 . 557 157 70 PHE N N 122.7 0.2 . 558 158 71 ASP H H 7.86 0.02 . 559 158 71 ASP HA H 4.02 0.02 . 560 158 71 ASP HB2 H 2.67 0.02 . 561 158 71 ASP CA C 50.8 0.2 . 562 158 71 ASP CB C 37.5 0.2 . 563 158 71 ASP N N 115.5 0.2 . 564 159 72 GLY H H 8.85 0.02 . 565 159 72 GLY HA2 H 3.33 0.02 . 566 159 72 GLY CA C 42.0 0.2 . 567 159 72 GLY N N 110.3 0.2 . 568 160 73 PRO HA H 3.94 0.02 . 569 161 74 GLY H H 11.3 0.02 . 570 161 74 GLY HA2 H 3.86 0.02 . 571 161 74 GLY CA C 40.6 0.2 . 572 161 74 GLY N N 119.7 0.2 . 573 162 75 ASN H H 8.79 0.02 . 574 162 75 ASN HA H 3.84 0.02 . 575 162 75 ASN HB2 H 2.56 0.02 . 576 162 75 ASN HB3 H 3.16 0.02 . 577 162 75 ASN HD21 H 6.902 0.02 . 578 162 75 ASN HD22 H 7.462 0.02 . 579 162 75 ASN CA C 52.8 0.2 . 580 162 75 ASN CB C 36.5 0.2 . 581 162 75 ASN N N 118.1 0.2 . 582 162 75 ASN ND2 N 114.1 0.2 . 583 163 76 VAL H H 9.96 0.02 . 584 163 76 VAL HA H 3.51 0.02 . 585 163 76 VAL HB H 2.20 0.02 . 586 163 76 VAL HG1 H 1.126 0.02 . 587 163 76 VAL HG2 H 0.8457 0.02 . 588 163 76 VAL CA C 60.5 0.2 . 589 163 76 VAL CB C 29.1 0.2 . 590 163 76 VAL CG1 C 18 0.2 . 591 163 76 VAL CG2 C 16.72 0.2 . 592 163 76 VAL N N 125.1 0.2 . 593 164 77 LEU H H 8.44 0.02 . 594 164 77 LEU HA H 4.57 0.02 . 595 164 77 LEU HB2 H 1.27 0.02 . 596 164 77 LEU HG H 1.75 0.02 . 597 164 77 LEU HD1 H 0.312 0.02 . 598 164 77 LEU HD2 H 0.1345 0.02 . 599 164 77 LEU N N 125.5 0.2 . 600 165 78 ALA H H 7.43 0.02 . 601 165 78 ALA HA H 3.14 0.02 . 602 165 78 ALA HB H 1.68 0.02 . 603 165 78 ALA CB C 15.6 0.2 . 604 165 78 ALA N N 114.5 0.2 . 605 166 79 HIS H H 9.07 0.02 . 606 166 79 HIS HA H 4.45 0.02 . 607 166 79 HIS HB2 H 2.92 0.02 . 608 166 79 HIS HD2 H 8.201 0.02 . 609 166 79 HIS CA C 51.4 0.2 . 610 166 79 HIS CB C 27.0 0.2 . 611 166 79 HIS N N 115.6 0.2 . 612 167 80 ALA H H 8.01 0.02 . 613 167 80 ALA HA H 4.56 0.02 . 614 167 80 ALA HB H 2.09 0.02 . 615 167 80 ALA CB C 16.4 0.2 . 616 167 80 ALA N N 121.5 0.2 . 617 168 81 TYR H H 7.97 0.02 . 618 168 81 TYR HA H 4.39 0.02 . 619 168 81 TYR HB2 H 2.62 0.02 . 620 168 81 TYR HB3 H 2.77 0.02 . 621 168 81 TYR HD1 H 6.68 0.02 . 622 168 81 TYR HE1 H 6.238 0.02 . 623 168 81 TYR CA C 55.3 0.2 . 624 168 81 TYR CB C 36.0 0.2 . 625 168 81 TYR N N 123.8 0.2 . 626 169 82 ALA H H 7.44 0.02 . 627 169 82 ALA HA H 4.7 0.02 . 628 169 82 ALA N N 119.1 0.2 . 629 170 83 PRO HA H 4.13 0.02 . 630 170 83 PRO HB2 H 1.85 0.02 . 631 170 83 PRO HG2 H 1.713 0.02 . 632 170 83 PRO HD2 H 3.511 0.02 . 633 170 83 PRO CA C 60.7 0.2 . 634 170 83 PRO CB C 29.3 0.2 . 635 170 83 PRO CG C 24.68 0.2 . 636 170 83 PRO CD C 47.46 0.2 . 637 171 84 GLY H H 6.20 0.02 . 638 171 84 GLY HA2 H 4.67 0.02 . 639 171 84 GLY CA C 43.6 0.2 . 640 171 84 GLY N N 109.5 0.2 . 641 172 85 PRO HA H 4.71 0.02 . 642 172 85 PRO HB2 H 1.94 0.02 . 643 172 85 PRO HG2 H 1.77 0.02 . 644 172 85 PRO HD2 H 3.45 0.02 . 645 172 85 PRO HD3 H 3.74 0.02 . 646 172 85 PRO CA C 60.3 0.2 . 647 172 85 PRO CB C 29.2 0.2 . 648 172 85 PRO CG C 24.53 0.2 . 649 172 85 PRO CD C 48.37 0.2 . 650 173 86 GLY H H 8.75 0.02 . 651 173 86 GLY HA2 H 3.76 0.02 . 652 173 86 GLY CA C 42.7 0.2 . 653 173 86 GLY N N 109.7 0.2 . 654 174 87 ILE H H 8.90 0.02 . 655 174 87 ILE HA H 4.03 0.02 . 656 174 87 ILE HB H 1.73 0.02 . 657 174 87 ILE HG12 H 1.32 0.02 . 658 174 87 ILE HG13 H 1.04 0.02 . 659 174 87 ILE HG2 H 0.78 0.02 . 660 174 87 ILE HD1 H 0.71 0.02 . 661 174 87 ILE CA C 58.7 0.2 . 662 174 87 ILE CB C 35.9 0.2 . 663 174 87 ILE CG1 C 24.46 0.2 . 664 174 87 ILE CG2 C 14.63 0.2 . 665 174 87 ILE CD1 C 10.44 0.2 . 666 174 87 ILE N N 131.8 0.2 . 667 175 88 ASN H H 7.15 0.02 . 668 175 88 ASN HA H 4.39 0.02 . 669 175 88 ASN HB2 H 2.06 0.02 . 670 175 88 ASN HB3 H 2.27 0.02 . 671 175 88 ASN HD21 H 6.77 0.02 . 672 175 88 ASN HD22 H 7.376 0.02 . 673 175 88 ASN CA C 53.6 0.2 . 674 175 88 ASN CB C 33.1 0.2 . 675 175 88 ASN N N 117.5 0.2 . 676 175 88 ASN ND2 N 112. 0.2 . 677 176 89 GLY H H 8.09 0.02 . 678 176 89 GLY HA2 H 4.66 0.02 . 679 176 89 GLY CA C 43.2 0.2 . 680 176 89 GLY N N 120.4 0.2 . 681 177 90 ASP H H 7.76 0.02 . 682 177 90 ASP HA H 4.41 0.02 . 683 177 90 ASP HB2 H 2.45 0.02 . 684 177 90 ASP HB3 H 2.59 0.02 . 685 177 90 ASP CA C 51.8 0.2 . 686 177 90 ASP CB C 38.2 0.2 . 687 177 90 ASP N N 123.8 0.2 . 688 178 91 ALA H H 8.21 0.02 . 689 178 91 ALA HA H 4.93 0.02 . 690 178 91 ALA HB H 1.15 0.02 . 691 178 91 ALA N N 122.4 0.2 . 692 179 92 HIS H H 9.19 0.02 . 693 179 92 HIS HA H 4.85 0.02 . 694 179 92 HIS N N 120.3 0.2 . 695 180 93 PHE H H 8.81 0.02 . 696 180 93 PHE HA H 4.74 0.02 . 697 180 93 PHE HB2 H 3.06 0.02 . 698 180 93 PHE HD1 H 6.43 0.02 . 699 180 93 PHE HD2 H 7.074 0.02 . 700 180 93 PHE HE1 H 6.572 0.02 . 701 180 93 PHE HE2 H 6.81 0.02 . 702 180 93 PHE CA C 54.5 0.2 . 703 180 93 PHE CB C 36.7 0.2 . 704 180 93 PHE N N 123.5 0.2 . 705 181 94 ASP H H 8.11 0.02 . 706 181 94 ASP HA H 4.23 0.02 . 707 181 94 ASP HB2 H 2.75 0.02 . 708 181 94 ASP HB3 H 2.71 0.02 . 709 181 94 ASP CA C 51.0 0.2 . 710 181 94 ASP CB C 36.5 0.2 . 711 181 94 ASP N N 121.8 0.2 . 712 182 95 ASP H H 9.79 0.02 . 713 182 95 ASP HA H 5.39 0.02 . 714 182 95 ASP HB2 H 2.62 0.02 . 715 182 95 ASP HB3 H 2.37 0.02 . 716 182 95 ASP CA C 50.5 0.2 . 717 182 95 ASP CB C 38.2 0.2 . 718 182 95 ASP N N 128.3 0.2 . 719 183 96 ASP H H 9.22 0.02 . 720 183 96 ASP HA H 4.73 0.02 . 721 183 96 ASP HB2 H 2.57 0.02 . 722 183 96 ASP HB3 H 2.73 0.02 . 723 183 96 ASP N N 123.8 0.2 . 724 184 97 GLU H H 7.20 0.02 . 725 184 97 GLU HA H 4.83 0.02 . 726 184 97 GLU HB2 H 2.35 0.02 . 727 184 97 GLU CA C 50.4 0.2 . 728 184 97 GLU CB C 23.4 0.2 . 729 184 97 GLU N N 115.9 0.2 . 730 185 98 GLN H H 8.38 0.02 . 731 185 98 GLN HA H 4.37 0.02 . 732 185 98 GLN HB2 H 1.85 0.02 . 733 185 98 GLN HB3 H 1.64 0.02 . 734 185 98 GLN HE21 H 7.44 0.02 . 735 185 98 GLN HE22 H 6.765 0.02 . 736 185 98 GLN CA C 50.5 0.2 . 737 185 98 GLN N N 126.3 0.2 . 738 185 98 GLN NE2 N 111.7 0.2 . 739 186 99 TRP H H 9.58 0.02 . 740 186 99 TRP HA H 4.92 0.02 . 741 186 99 TRP HB2 H 3.14 0.02 . 742 186 99 TRP HD1 H 7.421 0.02 . 743 186 99 TRP HE1 H 9.35 0.02 . 744 186 99 TRP CA C 54.2 0.2 . 745 186 99 TRP CB C 27.3 0.2 . 746 186 99 TRP N N 131.2 0.2 . 747 186 99 TRP NE1 N 126 0.2 . 748 187 100 THR H H 8.73 0.02 . 749 187 100 THR HA H 4.75 0.02 . 750 187 100 THR HB H 4.38 0.02 . 751 187 100 THR HG2 H 0.9601 0.02 . 752 187 100 THR CA C 55.9 0.2 . 753 187 100 THR CB C 70.2 0.2 . 754 187 100 THR CG2 C 19.23 0.2 . 755 187 100 THR N N 110.9 0.2 . 756 188 101 LYS H H 9.05 0.02 . 757 188 101 LYS HA H 4.38 0.02 . 758 188 101 LYS HB2 H 1.72 0.02 . 759 188 101 LYS HB3 H 1.84 0.02 . 760 188 101 LYS HG2 H 1.307 0.02 . 761 188 101 LYS HG3 H 1.396 0.02 . 762 188 101 LYS HD2 H 1.57 0.02 . 763 188 101 LYS HD3 H 1.585 0.02 . 764 188 101 LYS HE2 H 2.82 0.02 . 765 188 101 LYS HE3 H 2.88 0.02 . 766 188 101 LYS CA C 54 0.2 . 767 188 101 LYS CB C 30.5 0.2 . 768 188 101 LYS CG C 21.75 0.2 . 769 188 101 LYS CD C 26.65 0.2 . 770 188 101 LYS CE C 39.34 0.2 . 771 188 101 LYS N N 120 0.2 . 772 189 102 ASP H H 7.39 0.02 . 773 189 102 ASP HA H 4.74 0.02 . 774 189 102 ASP HB2 H 3.30 0.02 . 775 189 102 ASP HB3 H 2.68 0.02 . 776 189 102 ASP CA C 49.8 0.2 . 777 189 102 ASP CB C 39.1 0.2 . 778 189 102 ASP N N 120.4 0.2 . 779 190 103 THR H H 7.77 0.02 . 780 190 103 THR HA H 4.59 0.02 . 781 190 103 THR HB H 3.93 0.02 . 782 190 103 THR HG2 H 1.112 0.02 . 783 190 103 THR CA C 61.3 0.2 . 784 190 103 THR CB C 66.8 0.2 . 785 190 103 THR CG2 C 18.76 0.2 . 786 190 103 THR N N 128 0.2 . 787 191 104 THR H H 8.17 0.02 . 788 191 104 THR HA H 4.04 0.02 . 789 191 104 THR HB H 4.05 0.02 . 790 191 104 THR HG2 H 1.146 0.02 . 791 191 104 THR CA C 61.0 0.2 . 792 191 104 THR CB C 67.1 0.2 . 793 191 104 THR CG2 C 18.98 0.2 . 794 191 104 THR N N 114.6 0.2 . 795 192 105 GLY H H 7.26 0.02 . 796 192 105 GLY HA2 H 3.40 0.02 . 797 192 105 GLY CA C 42.3 0.2 . 798 192 105 GLY N N 112.1 0.2 . 799 193 106 THR H H 8.53 0.02 . 800 193 106 THR HA H 3.54 0.02 . 801 193 106 THR HB H 2.64 0.02 . 802 193 106 THR HG2 H 0.0539 0.02 . 803 193 106 THR CA C 59.8 0.2 . 804 193 106 THR CB C 65.0 0.2 . 805 193 106 THR CG2 C 21.63 0.2 . 806 193 106 THR N N 123.7 0.2 . 807 194 107 ASN H H 8.22 0.02 . 808 194 107 ASN HA H 4.70 0.02 . 809 194 107 ASN HB2 H 2.78 0.02 . 810 194 107 ASN HD21 H 7.705 0.02 . 811 194 107 ASN HD22 H 6.968 0.02 . 812 194 107 ASN N N 126.1 0.2 . 813 194 107 ASN ND2 N 112.4 0.2 . 814 195 108 LEU H H 7.94 0.02 . 815 195 108 LEU HA H 4.40 0.02 . 816 195 108 LEU HB2 H 2.63 0.02 . 817 195 108 LEU HB3 H 2.62 0.02 . 818 195 108 LEU HG H 1.109 0.02 . 819 195 108 LEU HD1 H 0.8375 0.02 . 820 195 108 LEU HD2 H -0.343 0.02 . 821 195 108 LEU CB C 39.2 0.2 . 822 195 108 LEU N N 128.1 0.2 . 823 196 109 PHE H H 8.33 0.02 . 824 196 109 PHE HA H 3.93 0.02 . 825 196 109 PHE HB2 H 3.28 0.02 . 826 196 109 PHE HB3 H 3.12 0.02 . 827 196 109 PHE HD1 H 7.11 0.02 . 828 196 109 PHE HE1 H 6.54 0.02 . 829 196 109 PHE CA C 58.4 0.2 . 830 196 109 PHE CB C 34.6 0.2 . 831 196 109 PHE N N 119.1 0.2 . 832 197 110 LEU H H 8.61 0.02 . 833 197 110 LEU HA H 2.98 0.02 . 834 197 110 LEU HB2 H 2.56 0.02 . 835 197 110 LEU HB3 H 1.60 0.02 . 836 197 110 LEU HG H 1.476 0.02 . 837 197 110 LEU HD1 H 0.8412 0.02 . 838 197 110 LEU HD2 H 0.509 0.02 . 839 197 110 LEU CA C 55.3 0.2 . 840 197 110 LEU CB C 40.1 0.2 . 841 197 110 LEU N N 119.8 0.2 . 842 198 111 VAL H H 7.17 0.02 . 843 198 111 VAL HA H 3.88 0.02 . 844 198 111 VAL HB H 2.20 0.02 . 845 198 111 VAL HG1 H 1.123 0.02 . 846 198 111 VAL HG2 H 0.7268 0.02 . 847 198 111 VAL CA C 63.1 0.2 . 848 198 111 VAL CB C 29.1 0.2 . 849 198 111 VAL CG1 C 24.69 0.2 . 850 198 111 VAL CG2 C 21.31 0.2 . 851 198 111 VAL N N 114.7 0.2 . 852 199 112 ALA H H 9.47 0.02 . 853 199 112 ALA HA H 3.97 0.02 . 854 199 112 ALA HB H 1.07 0.02 . 855 199 112 ALA CA C 53.1 0.2 . 856 199 112 ALA CB C 13.8 0.2 . 857 199 112 ALA N N 121.8 0.2 . 858 200 113 ALA H H 8.81 0.02 . 859 200 113 ALA HA H 3.87 0.02 . 860 200 113 ALA HB H 0.95 0.02 . 861 200 113 ALA CA C 53.9 0.2 . 862 200 113 ALA CB C 14.2 0.2 . 863 200 113 ALA N N 120.7 0.2 . 864 201 114 HIS H H 7.66 0.02 . 865 201 114 HIS HA H 4.16 0.02 . 866 201 114 HIS HB2 H 3.87 0.02 . 867 201 114 HIS N N 119.8 0.2 . 868 202 115 GLU H H 9.19 0.02 . 869 202 115 GLU HA H 3.80 0.02 . 870 202 115 GLU HB2 H 0.96 0.02 . 871 202 115 GLU HB3 H 1.69 0.02 . 872 202 115 GLU HG2 H 2.33 0.02 . 873 202 115 GLU CA C 56.3 0.2 . 874 202 115 GLU CB C 26.5 0.2 . 875 202 115 GLU CG C 31.07 0.2 . 876 202 115 GLU N N 117.4 0.2 . 877 203 116 ILE H H 9.01 0.02 . 878 203 116 ILE HA H 3.80 0.02 . 879 203 116 ILE HB H 1.86 0.02 . 880 203 116 ILE HG12 H 1.276 0.02 . 881 203 116 ILE HG2 H 0.4894 0.02 . 882 203 116 ILE HD1 H 0.3846 0.02 . 883 203 116 ILE CA C 59.1 0.2 . 884 203 116 ILE CB C 32.8 0.2 . 885 203 116 ILE CG1 C 25.03 0.2 . 886 203 116 ILE CG2 C 15.52 0.2 . 887 203 116 ILE CD1 C 6.942 0.2 . 888 203 116 ILE N N 117.6 0.2 . 889 204 117 GLY H H 7.47 0.02 . 890 204 117 GLY HA2 H 2.29 0.02 . 891 204 117 GLY CA C 43.0 0.2 . 892 204 117 GLY N N 108.3 0.2 . 893 205 118 HIS H H 7.17 0.02 . 894 205 118 HIS HA H 4.38 0.02 . 895 205 118 HIS HB2 H 3.80 0.02 . 896 205 118 HIS HB3 H 2.77 0.02 . 897 205 118 HIS N N 119.7 0.2 . 898 207 120 LEU H H 8.19 0.02 . 899 207 120 LEU HA H 3.79 0.02 . 900 207 120 LEU HB2 H 1.75 0.02 . 901 207 120 LEU HG H 1.849 0.02 . 902 207 120 LEU HD1 H 0.781 0.02 . 903 207 120 LEU HD2 H 0.781 0.02 . 904 207 120 LEU CA C 55.2 0.2 . 905 207 120 LEU CG C 25.91 0.2 . 906 207 120 LEU CD1 C 24.55 0.2 . 907 207 120 LEU CD2 C 19.54 0.2 . 908 207 120 LEU N N 109 0.2 . 909 208 121 GLY H H 8.39 0.02 . 910 208 121 GLY HA2 H 5.73 0.02 . 911 208 121 GLY CA C 55.8 0.2 . 912 208 121 GLY N N 109.3 0.2 . 913 209 122 LEU H H 8.80 0.02 . 914 209 122 LEU HA H 5.26 0.02 . 915 209 122 LEU HB2 H 1.56 0.02 . 916 209 122 LEU HG H 1.417 0.02 . 917 209 122 LEU HD1 H 0.972 0.02 . 918 209 122 LEU HD2 H 0.5462 0.02 . 919 209 122 LEU N N 122.5 0.2 . 920 210 123 PHE H H 8.50 0.02 . 921 210 123 PHE HA H 4.82 0.02 . 922 210 123 PHE N N 125.1 0.2 . 923 211 124 HIS H H 5.29 0.02 . 924 211 124 HIS HB2 H 3.44 0.02 . 925 211 124 HIS N N 107.1 0.2 . 926 212 125 SER H H 6.82 0.02 . 927 212 125 SER HA H 4.67 0.02 . 928 212 125 SER HB2 H 3.07 0.02 . 929 212 125 SER HB3 H 4.04 0.02 . 930 212 125 SER CB C 64.7 0.2 . 931 212 125 SER N N 110.9 0.2 . 932 213 126 ALA H H 8.79 0.02 . 933 213 126 ALA HA H 4.25 0.02 . 934 213 126 ALA HB H 1.64 0.02 . 935 213 126 ALA CA C 48.9 0.2 . 936 213 126 ALA CB C 16.7 0.2 . 937 213 126 ALA N N 127.3 0.2 . 938 214 127 ASN H H 8.82 0.02 . 939 214 127 ASN HA H 4.52 0.02 . 940 214 127 ASN HB2 H 3.15 0.02 . 941 214 127 ASN HD21 H 6.608 0.02 . 942 214 127 ASN N N 121.4 0.2 . 943 215 128 THR H H 8.02 0.02 . 944 215 128 THR HA H 2.36 0.02 . 945 215 128 THR HB H 3.72 0.02 . 946 215 128 THR HG2 H 0.8115 0.02 . 947 215 128 THR CA C 61.0 0.2 . 948 215 128 THR CB C 65.6 0.2 . 949 215 128 THR CG2 C 18.73 0.2 . 950 215 128 THR N N 117.2 0.2 . 951 216 129 GLU H H 8.58 0.02 . 952 216 129 GLU HA H 4.45 0.02 . 953 216 129 GLU HB2 H 2.1 0.02 . 954 216 129 GLU N N 121.7 0.2 . 955 217 130 ALA H H 7.83 0.02 . 956 217 130 ALA HA H 4.17 0.02 . 957 217 130 ALA HB H 1.4 0.02 . 958 217 130 ALA CA C 49.5 0.2 . 959 217 130 ALA CB C 16.4 0.2 . 960 217 130 ALA N N 123.2 0.2 . 961 218 131 LEU H H 11.4 0.02 . 962 218 131 LEU HA H 4.41 0.02 . 963 218 131 LEU HB2 H 1.35 0.02 . 964 218 131 LEU HB3 H 1.61 0.02 . 965 218 131 LEU HG H 1.588 0.02 . 966 218 131 LEU HD1 H 0.9787 0.02 . 967 218 131 LEU HD2 H 1.128 0.02 . 968 218 131 LEU CA C 54.1 0.2 . 969 218 131 LEU CB C 39.8 0.2 . 970 218 131 LEU CG C 24.15 0.2 . 971 218 131 LEU CD2 C 21.59 0.2 . 972 218 131 LEU N N 131.8 0.2 . 973 219 132 MET H H 8.01 0.02 . 974 219 132 MET HA H 4.57 0.02 . 975 219 132 MET HB2 H 2.6 0.02 . 976 219 132 MET HE H 0.599 0.02 . 977 219 132 MET N N 110.9 0.2 . 978 220 133 TYR H H 8.06 0.02 . 979 220 133 TYR HA H 4.85 0.02 . 980 220 133 TYR HB2 H 2.88 0.02 . 981 220 133 TYR HD1 H 7.873 0.02 . 982 220 133 TYR HE1 H 7.671 0.02 . 983 220 133 TYR CA C 53.3 0.2 . 984 220 133 TYR CB C 36.1 0.2 . 985 220 133 TYR N N 128.2 0.2 . 986 221 134 PRO HA H 3.55 0.02 . 987 221 134 PRO HB2 H 1.70 0.02 . 988 221 134 PRO HB3 H 0.78 0.02 . 989 221 134 PRO HG2 H 0.7482 0.02 . 990 221 134 PRO CA C 58.8 0.2 . 991 221 134 PRO CB C 36.1 0.2 . 992 221 134 PRO CG C 24.48 0.2 . 993 222 135 LEU H H 7.50 0.02 . 994 222 135 LEU HA H 4.44 0.02 . 995 222 135 LEU HB2 H 1.67 0.02 . 996 222 135 LEU HB3 H 1.33 0.02 . 997 222 135 LEU HG H 0.2039 0.02 . 998 222 135 LEU HD1 H 0.9782 0.02 . 999 222 135 LEU HD2 H 0.809 0.02 . 1000 222 135 LEU CA C 52.2 0.2 . 1001 222 135 LEU CB C 40.1 0.2 . 1002 222 135 LEU CG C 23.61 0.2 . 1003 222 135 LEU CD1 C 20.54 0.2 . 1004 222 135 LEU CD2 C 19.15 0.2 . 1005 222 135 LEU N N 119.5 0.2 . 1006 223 136 TYR H H 9.05 0.02 . 1007 223 136 TYR HA H 4.59 0.02 . 1008 223 136 TYR HB2 H 2.71 0.02 . 1009 223 136 TYR HB3 H 2.21 0.02 . 1010 223 136 TYR CA C 56.7 0.2 . 1011 223 136 TYR CB C 34.3 0.2 . 1012 223 136 TYR N N 128 0.2 . 1013 224 137 HIS H H 8.15 0.02 . 1014 224 137 HIS HA H 4.28 0.02 . 1015 224 137 HIS HB2 H 2.87 0.02 . 1016 224 137 HIS HD2 H 6.96 0.02 . 1017 224 137 HIS CA C 55 0.2 . 1018 224 137 HIS CB C 35.3 0.2 . 1019 224 137 HIS N N 127.5 0.2 . 1020 225 138 SER H H 7.83 0.02 . 1021 225 138 SER HA H 3.91 0.02 . 1022 225 138 SER HB2 H 3.74 0.02 . 1023 225 138 SER HB3 H 3.99 0.02 . 1024 225 138 SER CA C 55.8 0.2 . 1025 225 138 SER CB C 61.5 0.2 . 1026 225 138 SER N N 119.1 0.2 . 1027 226 139 LEU H H 7.81 0.02 . 1028 226 139 LEU HA H 4.32 0.02 . 1029 226 139 LEU HB2 H 1.42 0.02 . 1030 226 139 LEU HB3 H 1.57 0.02 . 1031 226 139 LEU HD1 H 0.7595 0.02 . 1032 226 139 LEU CA C 51.8 0.2 . 1033 226 139 LEU CB C 39.2 0.2 . 1034 226 139 LEU N N 122.1 0.2 . 1035 227 140 THR H H 7.90 0.02 . 1036 227 140 THR HA H 4.27 0.02 . 1037 227 140 THR HB H 4.10 0.02 . 1038 227 140 THR HG2 H 1.216 0.02 . 1039 227 140 THR CA C 58.8 0.2 . 1040 227 140 THR CB C 67.1 0.2 . 1041 227 140 THR N N 120.8 0.2 . 1042 228 141 ASP H H 7.96 0.02 . 1043 228 141 ASP HA H 4.63 0.02 . 1044 228 141 ASP HB2 H 2.48 0.02 . 1045 228 141 ASP HB3 H 2.57 0.02 . 1046 228 141 ASP CA C 50.2 0.2 . 1047 228 141 ASP CB C 38.2 0.2 . 1048 228 141 ASP N N 123.3 0.2 . 1049 229 142 LEU H H 8.89 0.02 . 1050 229 142 LEU HA H 4.03 0.02 . 1051 229 142 LEU HB2 H 1.66 0.02 . 1052 229 142 LEU HB3 H 1.49 0.02 . 1053 229 142 LEU HG H 1.586 0.02 . 1054 229 142 LEU HD1 H 0.9031 0.02 . 1055 229 142 LEU HD2 H 0.8175 0.02 . 1056 229 142 LEU CA C 54.1 0.2 . 1057 229 142 LEU CB C 39.2 0.2 . 1058 229 142 LEU CG C 24.21 0.2 . 1059 229 142 LEU CD1 C 22.9 0.2 . 1060 229 142 LEU CD2 C 21.1 0.2 . 1061 229 142 LEU N N 126.5 0.2 . 1062 230 143 THR H H 8.36 0.02 . 1063 230 143 THR HA H 4.06 0.02 . 1064 230 143 THR HB H 4.16 0.02 . 1065 230 143 THR HG2 H 1.176 0.02 . 1066 230 143 THR CA C 61.7 0.2 . 1067 230 143 THR CB C 66.3 0.2 . 1068 230 143 THR CG2 C 19.14 0.2 . 1069 230 143 THR N N 111.4 0.2 . 1070 232 145 PHE H H 7.27 0.02 . 1071 232 145 PHE HA H 4.12 0.02 . 1072 232 145 PHE HB2 H 3.059 0.02 . 1073 232 145 PHE HB3 H 2.79 0.02 . 1074 232 145 PHE HE2 H 6.505 0.02 . 1075 232 145 PHE CA C 57.3 0.2 . 1076 232 145 PHE CB C 37.2 0.2 . 1077 232 145 PHE N N 120.9 0.2 . 1078 233 146 ARG H H 7.06 0.02 . 1079 233 146 ARG HA H 3.84 0.02 . 1080 233 146 ARG HB2 H 1.58 0.02 . 1081 233 146 ARG HB3 H 1.37 0.02 . 1082 233 146 ARG HG2 H 1.279 0.02 . 1083 233 146 ARG HD2 H 2.995 0.02 . 1084 233 146 ARG HD3 H 3.004 0.02 . 1085 233 146 ARG CA C 51.7 0.2 . 1086 233 146 ARG CB C 30.1 0.2 . 1087 233 146 ARG CG C 22.98 0.2 . 1088 233 146 ARG CD C 40.63 0.2 . 1089 233 146 ARG N N 126.2 0.2 . 1090 234 147 LEU H H 8.33 0.02 . 1091 234 147 LEU HA H 4.41 0.02 . 1092 234 147 LEU HD1 H 0.179 0.02 . 1093 234 147 LEU HD2 H 0.192 0.02 . 1094 234 147 LEU CA C 52.4 0.2 . 1095 234 147 LEU CB C 40.5 0.2 . 1096 234 147 LEU CG C 24.62 0.2 . 1097 234 147 LEU CD1 C 22.64 0.2 . 1098 234 147 LEU CD2 C 18.29 0.2 . 1099 234 147 LEU N N 121.9 0.2 . 1100 235 148 SER H H 8.66 0.02 . 1101 235 148 SER HA H 3.74 0.02 . 1102 235 148 SER HB2 H 3.91 0.02 . 1103 235 148 SER HB3 H 4.71 0.02 . 1104 235 148 SER CA C 56.2 0.2 . 1105 235 148 SER CB C 63.1 0.2 . 1106 235 148 SER N N 118 0.2 . 1107 236 149 GLN H H 9.09 0.02 . 1108 236 149 GLN HA H 4.41 0.02 . 1109 236 149 GLN HB2 H 1.95 0.02 . 1110 236 149 GLN HB3 H 2.07 0.02 . 1111 236 149 GLN HG2 H 2.34 0.02 . 1112 236 149 GLN CA C 55.1 0.2 . 1113 236 149 GLN CB C 25.6 0.2 . 1114 236 149 GLN CG C 31.23 0.2 . 1115 236 149 GLN N N 122.4 0.2 . 1116 237 150 ASP H H 8.06 0.02 . 1117 237 150 ASP HA H 4.27 0.02 . 1118 237 150 ASP HB2 H 2.55 0.02 . 1119 237 150 ASP CA C 55.2 0.2 . 1120 237 150 ASP CB C 39.8 0.2 . 1121 237 150 ASP N N 117.9 0.2 . 1122 238 151 ASP H H 8.03 0.02 . 1123 238 151 ASP HA H 3.89 0.02 . 1124 238 151 ASP HB2 H 2.97 0.02 . 1125 238 151 ASP CA C 56.1 0.2 . 1126 238 151 ASP CB C 36.5 0.2 . 1127 238 151 ASP N N 117.7 0.2 . 1128 239 152 ILE H H 7.96 0.02 . 1129 239 152 ILE HA H 3.59 0.02 . 1130 239 152 ILE HB H 1.68 0.02 . 1131 239 152 ILE HG12 H 0.8007 0.02 . 1132 239 152 ILE HG2 H 0.7681 0.02 . 1133 239 152 ILE HD1 H 0.6474 0.02 . 1134 239 152 ILE CA C 62.7 0.2 . 1135 239 152 ILE CB C 36.4 0.2 . 1136 239 152 ILE CG1 C 27.8 0.2 . 1137 239 152 ILE CG2 C 14.23 0.2 . 1138 239 152 ILE CD1 C 10.45 0.2 . 1139 239 152 ILE N N 119.1 0.2 . 1140 240 153 ASN H H 9.11 0.02 . 1141 240 153 ASN HA H 4.36 0.02 . 1142 240 153 ASN HB2 H 2.77 0.02 . 1143 240 153 ASN HB3 H 2.85 0.02 . 1144 240 153 ASN HD21 H 7.63 0.02 . 1145 240 153 ASN HD22 H 6.965 0.02 . 1146 240 153 ASN CA C 53.2 0.2 . 1147 240 153 ASN CB C 34.8 0.2 . 1148 240 153 ASN N N 118.4 0.2 . 1149 240 153 ASN ND2 N 111.6 0.2 . 1150 241 154 GLY H H 8.19 0.02 . 1151 241 154 GLY HA2 H 3.78 0.02 . 1152 241 154 GLY CA C 44.4 0.2 . 1153 241 154 GLY N N 108.2 0.2 . 1154 242 155 ILE H H 8.53 0.02 . 1155 242 155 ILE HA H 4.27 0.02 . 1156 242 155 ILE HB H 2.09 0.02 . 1157 242 155 ILE HG12 H 1.031 0.02 . 1158 242 155 ILE HG2 H 1.228 0.02 . 1159 242 155 ILE HD1 H 0.76 0.02 . 1160 242 155 ILE CA C 60.5 0.2 . 1161 242 155 ILE CB C 28.9 0.2 . 1162 242 155 ILE CG1 C 24.81 0.2 . 1163 242 155 ILE CG2 C 19.86 0.2 . 1164 242 155 ILE CD1 C 14.82 0.2 . 1165 242 155 ILE N N 123.3 0.2 . 1166 243 156 GLN H H 8.27 0.02 . 1167 243 156 GLN HA H 4.65 0.02 . 1168 243 156 GLN HG2 H 2.956 0.02 . 1169 243 156 GLN HE21 H 6.725 0.02 . 1170 243 156 GLN HE22 H 7.666 0.02 . 1171 243 156 GLN N N 120.9 0.2 . 1172 244 157 SER H H 8.02 0.02 . 1173 244 157 SER HA H 4.52 0.02 . 1174 244 157 SER N N 117.3 0.2 . 1175 245 158 LEU H H 6.73 0.02 . 1176 245 158 LEU HA H 4.09 0.02 . 1177 245 158 LEU HB2 H 1.47 0.02 . 1178 245 158 LEU HB3 H 1.62 0.02 . 1179 245 158 LEU HG H 1.469 0.02 . 1180 245 158 LEU HD1 H 0.7247 0.02 . 1181 245 158 LEU HD2 H 0.7793 0.02 . 1182 245 158 LEU CA C 54.6 0.2 . 1183 245 158 LEU CB C 40.4 0.2 . 1184 245 158 LEU CG C 24.4 0.2 . 1185 245 158 LEU CD1 C 22.48 0.2 . 1186 245 158 LEU CD2 C 21.41 0.2 . 1187 245 158 LEU N N 118.1 0.2 . 1188 246 159 TYR H H 7.58 0.02 . 1189 246 159 TYR HA H 2.84 0.02 . 1190 246 159 TYR HB2 H 3.45 0.02 . 1191 246 159 TYR HB3 H 3.15 0.02 . 1192 246 159 TYR HD1 H 7.997 0.02 . 1193 246 159 TYR HE1 H 7.068 0.02 . 1194 246 159 TYR CA C 53.0 0.2 . 1195 246 159 TYR CB C 40.5 0.2 . 1196 246 159 TYR N N 113 0.2 . 1197 247 160 GLY H H 8.31 0.02 . 1198 247 160 GLY HA2 H 4.2 0.02 . 1199 247 160 GLY HA3 H 3.97 0.02 . 1200 247 160 GLY CA C 41.8 0.2 . 1201 247 160 GLY N N 110 0.2 . 1202 248 161 PRO HG2 H 1.819 0.02 . stop_ save_