data_6014 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 13C and 15N backbone resonance assignments of matrilysin (mmp7) complexed with a hydroxamic acid inhibitor ; _BMRB_accession_number 6014 _BMRB_flat_file_name bmr6014.str _Entry_type original _Submission_date 2003-11-20 _Accession_date 2003-11-20 _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 Ou Li . . 2 Zhang Qi . . 3 Ma Jingbiao . . 4 Wang Zhonghua . . 5 Zhang Fang . . 6 Wu Houming . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 308 "13C chemical shifts" 464 "15N chemical shifts" 147 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2005-11-21 original author . stop_ _Original_release_date 2005-11-21 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: 1H, 13C and 15N backbone resonance assignments of matrilysin (MMP7) complexed with a sulfonamide hydroxamate-type inhibitor ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 15243187 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Ou Li . . 2 Zhang Qi . . 3 Ma Jingbiao . . 4 Wu Wengen . . 5 Wang Zhonghua . . 6 Zhang Fang . . 7 Ma Dawei . . 8 Wu Houming . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 29 _Journal_issue 3 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 537 _Page_last 538 _Year 2004 _Details . save_ ################################## # Molecular system description # ################################## save_system_mmp7 _Saveframe_category molecular_system _Mol_system_name matrilysin _Abbreviation_common mmp7 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'matrilysin madw01053' $mmp7 'ZINC (II) ION' $ZN 'Hydroxamic acid inhibitor' $MDW stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_mmp7 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common matrilysin _Abbreviation_common mmp7 _Molecular_mass 19128 _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 173 _Mol_residue_sequence ; YSLFPNSPKWTSKVVTYRIV SYTRDLPHITVDRLVSKALN MWGKEIPLHFRKVVWGTADI MIGFARGAHGDSYPFDGPGN TLAHAFAPGTGLGGDAHFDE DERWTDGSSLGINFLYAATH ELGHSLGMGHSSDPNAVMYP TYGNGDPQNFKLSQDDIKGI QKLYGKRSNSRKK ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 100 TYR 2 101 SER 3 102 LEU 4 103 PHE 5 104 PRO 6 105 ASN 7 106 SER 8 107 PRO 9 108 LYS 10 109 TRP 11 110 THR 12 111 SER 13 112 LYS 14 113 VAL 15 114 VAL 16 115 THR 17 116 TYR 18 117 ARG 19 118 ILE 20 119 VAL 21 120 SER 22 121 TYR 23 122 THR 24 123 ARG 25 124 ASP 26 125 LEU 27 126 PRO 28 127 HIS 29 128 ILE 30 129 THR 31 130 VAL 32 131 ASP 33 132 ARG 34 133 LEU 35 134 VAL 36 135 SER 37 136 LYS 38 137 ALA 39 138 LEU 40 139 ASN 41 140 MET 42 141 TRP 43 142 GLY 44 143 LYS 45 144 GLU 46 145 ILE 47 146 PRO 48 147 LEU 49 148 HIS 50 149 PHE 51 150 ARG 52 151 LYS 53 152 VAL 54 153 VAL 55 154 TRP 56 155 GLY 57 156 THR 58 157 ALA 59 158 ASP 60 159 ILE 61 160 MET 62 161 ILE 63 162 GLY 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 SER 73 172 TYR 74 173 PRO 75 174 PHE 76 175 ASP 77 176 GLY 78 177 PRO 79 178 GLY 80 179 ASN 81 180 THR 82 181 LEU 83 182 ALA 84 183 HIS 85 184 ALA 86 185 PHE 87 186 ALA 88 187 PRO 89 188 GLY 90 189 THR 91 190 GLY 92 191 LEU 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 ARG 104 203 TRP 105 204 THR 106 205 ASP 107 206 GLY 108 207 SER 109 208 SER 110 209 LEU 111 210 GLY 112 211 ILE 113 212 ASN 114 213 PHE 115 214 LEU 116 215 TYR 117 216 ALA 118 217 ALA 119 218 THR 120 219 HIS 121 220 GLU 122 221 LEU 123 222 GLY 124 223 HIS 125 224 SER 126 225 LEU 127 226 GLY 128 227 MET 129 228 GLY 130 229 HIS 131 230 SER 132 231 SER 133 232 ASP 134 233 PRO 135 234 ASN 136 235 ALA 137 236 VAL 138 237 MET 139 238 TYR 140 239 PRO 141 240 THR 142 241 TYR 143 242 GLY 144 243 ASN 145 244 GLY 146 245 ASP 147 246 PRO 148 247 GLN 149 248 ASN 150 249 PHE 151 250 LYS 152 251 LEU 153 252 SER 154 253 GLN 155 254 ASP 156 255 ASP 157 256 ILE 158 257 LYS 159 258 GLY 160 259 ILE 161 260 GLN 162 261 LYS 163 262 LEU 164 263 TYR 165 264 GLY 166 265 LYS 167 266 ARG 168 267 SER 169 268 ASN 170 269 SER 171 270 ARG 172 271 LYS 173 272 LYS 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 PDB 1MMP "Matrilysin Complexed With Carboxylate Inhibitor" 98.27 170 100.00 100.00 2.55e-121 PDB 1MMQ "Matrilysin Complexed With Hydroxamate Inhibitor" 98.27 170 100.00 100.00 2.55e-121 PDB 1MMR "Matrilysin Complexed With Sulfodiimine Inhibitor" 98.27 170 100.00 100.00 2.55e-121 PDB 2DDY "Solution Structure Of Matrilysin (Mmp-7) Complexed To Constraint Conformational Sulfonamide Inhibitor" 100.00 173 100.00 100.00 8.32e-124 PDB 2Y6C "The Discovery Of Mmp7 Inhibitors Exploiting A Novel Selectivity Trigger" 94.80 165 100.00 100.00 1.03e-116 PDB 2Y6D "The Discovery Of Mmp7 Inhibitors Exploiting A Novel Selectivity Trigger" 100.00 174 100.00 100.00 1.33e-123 DBJ BAD96700 "matrix metalloproteinase 7 preproprotein variant [Homo sapiens]" 100.00 267 99.42 99.42 3.75e-123 DBJ BAI46673 "matrix metallopeptidase 7 [synthetic construct]" 100.00 267 100.00 100.00 3.29e-124 EMBL CAA30678 "unnamed protein product [Homo sapiens]" 100.00 267 100.00 100.00 3.15e-124 EMBL CAA77942 "PUMP [Homo sapiens]" 100.00 267 100.00 100.00 3.15e-124 GB AAC37543 "matrilysin [Homo sapiens]" 100.00 267 100.00 100.00 3.29e-124 GB AAH03635 "Matrix metallopeptidase 7 (matrilysin, uterine) [Homo sapiens]" 100.00 267 100.00 100.00 3.29e-124 GB AAV40839 "matrix metalloproteinase 7 (matrilysin, uterine) [Homo sapiens]" 100.00 267 100.00 100.00 3.15e-124 GB AAX36381 "matrix metalloproteinase 7 [synthetic construct]" 100.00 267 100.00 100.00 3.29e-124 GB AAX36443 "matrix metalloproteinase 7 [synthetic construct]" 100.00 267 100.00 100.00 3.29e-124 REF NP_002414 "matrilysin preproprotein [Homo sapiens]" 100.00 267 100.00 100.00 3.15e-124 REF XP_001097508 "PREDICTED: matrilysin [Macaca mulatta]" 100.00 270 98.27 98.27 1.65e-121 REF XP_002822443 "PREDICTED: matrilysin [Pongo abelii]" 100.00 267 97.69 99.42 1.38e-121 REF XP_003828431 "PREDICTED: matrilysin [Pan paniscus]" 100.00 267 99.42 100.00 3.75e-123 REF XP_003910646 "PREDICTED: LOW QUALITY PROTEIN: matrilysin [Papio anubis]" 100.00 270 98.27 98.27 1.65e-121 SP P09237 "RecName: Full=Matrilysin; AltName: Full=Matrin; AltName: Full=Matrix metalloproteinase-7; Short=MMP-7; AltName: Full=Pump-1 pro" 100.00 267 100.00 100.00 3.15e-124 stop_ save_ ############# # Ligands # ############# save_MDW _Saveframe_category ligand _Mol_type non-polymer _Name_common "MDW ((1R)-N,6-DIHYDROXY-7-METHOXY-2-[(4-METHOXYPHENYL)SULFONYL]-1,2,3,4-TETRAHYDROISOQUINOLINE-1-CARBOXAMIDE)" _BMRB_code . _PDB_code MDW _Molecular_mass 408.426 _Mol_charge 0 _Mol_paramagnetic . _Mol_aromatic yes _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Mon Jun 20 12:10:06 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons C3 C3 C . 0 . ? C2 C2 C . 0 . ? O1 O1 O . 0 . ? C7 C7 C . 0 . ? O12 O12 O . 0 . ? C13 C13 C . 0 . ? C6 C6 C . 0 . ? C5 C5 C . 0 . ? C8 C8 C . 0 . ? C14 C14 C . 0 . ? O15 O15 O . 0 . ? N16 N16 N . 0 . ? O17 O17 O . 0 . ? C4 C4 C . 0 . ? C10 C10 C . 0 . ? C11 C11 C . 0 . ? N9 N9 N . 0 . ? S18 S18 S . 0 . ? O40 O40 O . 0 . ? O41 O41 O . 0 . ? C19 C19 C . 0 . ? C20 C20 C . 0 . ? C21 C21 C . 0 . ? C22 C22 C . 0 . ? O25 O25 O . 0 . ? C26 C26 C . 0 . ? C23 C23 C . 0 . ? C24 C24 C . 0 . ? H28 H28 H . 0 . ? H27 H27 H . 0 . ? H35 H35 H . 0 . ? H36 H36 H . 0 . ? H37 H37 H . 0 . ? H29 H29 H . 0 . ? H30 H30 H . 0 . ? H38 H38 H . 0 . ? H39 H39 H . 0 . ? H31 H31 H . 0 . ? H32 H32 H . 0 . ? H33 H33 H . 0 . ? H34 H34 H . 0 . ? H48 H48 H . 0 . ? H42 H42 H . 0 . ? H45 H45 H . 0 . ? H46 H46 H . 0 . ? H47 H47 H . 0 . ? H43 H43 H . 0 . ? H44 H44 H . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name SING C3 C2 ? ? DOUB C3 C4 ? ? SING C3 H28 ? ? SING C2 O1 ? ? DOUB C2 C7 ? ? SING O1 H27 ? ? SING C7 O12 ? ? SING C7 C6 ? ? SING O12 C13 ? ? SING C13 H35 ? ? SING C13 H36 ? ? SING C13 H37 ? ? DOUB C6 C5 ? ? SING C6 H29 ? ? SING C5 C8 ? ? SING C5 C4 ? ? SING C8 C14 ? ? SING C8 N9 ? ? SING C8 H30 ? ? DOUB C14 O15 ? ? SING C14 N16 ? ? SING N16 O17 ? ? SING N16 H38 ? ? SING O17 H39 ? ? SING C4 C10 ? ? SING C10 C11 ? ? SING C10 H31 ? ? SING C10 H32 ? ? SING C11 N9 ? ? SING C11 H33 ? ? SING C11 H34 ? ? SING N9 S18 ? ? DOUB S18 O40 ? ? DOUB S18 O41 ? ? SING S18 C19 ? ? SING C19 C20 ? ? DOUB C19 C24 ? ? DOUB C20 C21 ? ? SING C20 H48 ? ? SING C21 C22 ? ? SING C21 H42 ? ? SING C22 O25 ? ? DOUB C22 C23 ? ? SING O25 C26 ? ? SING C26 H45 ? ? SING C26 H46 ? ? SING C26 H47 ? ? SING C23 C24 ? ? SING C23 H43 ? ? SING C24 H44 ? ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ 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 Mon Jun 20 12:12:44 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_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain $mmp7 'E. coli' 562 Bacteria . Escherichia coli BL21(DE3) 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 $mmp7 'recombinant technology' 'E. coli' Escherichia coli BL21DE3 plasmid pET11c 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 _Concentration_min_value _Concentration_max_value _Isotopic_labeling $mmp7 . mM 0.6 0.7 . NaCl 100 mM . . . Tris-HCl 10 mM . . . CaCl2 10 mM . . . ZnCl2 0.1 mM . . . NaN3 2 mM . . . stop_ save_ ############################ # Computer software used # ############################ save_NMRView _Saveframe_category software _Name NMRView _Version 5.0.4 loop_ _Task assignments stop_ _Details ; Johnson, B.A. and Blevins, R.A. (1994) J. Biomol. NMR, 4, 603????C614 ; save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_CBCA(CO)NH_1 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _Sample_label $sample_1 save_ save_CBCANH_2 _Saveframe_category NMR_applied_experiment _Experiment_name CBCANH _Sample_label $sample_1 save_ save_C(CO)NH_3 _Saveframe_category NMR_applied_experiment _Experiment_name C(CO)NH _Sample_label $sample_1 save_ save_HC(CO)NH_4 _Saveframe_category NMR_applied_experiment _Experiment_name HC(CO)NH _Sample_label $sample_1 save_ save_HNCO_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label $sample_1 save_ save_HCACO_6 _Saveframe_category NMR_applied_experiment _Experiment_name HCACO _Sample_label $sample_1 save_ save_HNCA_7 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label $sample_1 save_ save_HCCH-COSY_and_HCCH-TOCSY_8 _Saveframe_category NMR_applied_experiment _Experiment_name 'HCCH-COSY and HCCH-TOCSY' _Sample_label $sample_1 save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name CBCANH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name C(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name HC(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name HCACO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_8 _Saveframe_category NMR_applied_experiment _Experiment_name 'HCCH-COSY and HCCH-TOCSY' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_cond._set_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.9 0.2 pH temperature 298 1 K 'ionic strength' 0.10 0.02 M stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio _Indirect_shift_ratio_citation_label _Correction_value_citation_label H2O H 1 protons ppm 4.76 . direct . internal . 1.0 $entry_citation $entry_citation DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 $entry_citation $entry_citation DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 $entry_citation $entry_citation stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $cond._set_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'matrilysin madw01053' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 1 TYR CA C 58.62 . 1 2 . 1 TYR CB C 39.21 . 1 3 . 2 SER N N 122.68 . 1 4 . 2 SER H H 7.98 . 1 5 . 2 SER CA C 60.4 . 1 6 . 2 SER CB C 65.36 . 1 7 . 2 SER C C 175.66 . 1 8 . 2 SER HA H 4.4 . 1 9 . 3 LEU CA C 58.17 . 1 10 . 3 LEU CB C 39.94 . 1 11 . 4 PHE N N 121.7 . 1 12 . 4 PHE H H 7.78 . 1 13 . 4 PHE CA C 54.85 . 1 14 . 4 PHE CB C 35.44 . 1 15 . 4 PHE C C 173 . 1 16 . 5 PRO CA C 63.99 . 1 17 . 5 PRO CB C 32.26 . 1 18 . 5 PRO HA H 4.55 . 1 19 . 6 ASN N N 118.02 . 1 20 . 6 ASN H H 8.57 . 1 21 . 6 ASN CA C 53.69 . 1 22 . 6 ASN CB C 39.65 . 1 23 . 6 ASN C C 178.56 . 1 24 . 6 ASN HA H 4.79 . 1 25 . 7 SER N N 121.13 . 1 26 . 7 SER H H 7.99 . 1 27 . 7 SER CA C 60.44 . 1 28 . 7 SER CB C 65.42 . 1 29 . 7 SER C C 174.63 . 1 30 . 7 SER HA H 4.38 . 1 31 . 8 PRO CA C 63.75 . 1 32 . 8 PRO CB C 32.42 . 1 33 . 8 PRO HA H 4.21 . 1 34 . 9 LYS N N 114.63 . 1 35 . 9 LYS H H 7.5 . 1 36 . 9 LYS CA C 54.8 . 1 37 . 9 LYS CB C 35.26 . 1 38 . 9 LYS C C 175.04 . 1 39 . 9 LYS HA H 4.29 . 1 40 . 10 TRP N N 121.98 . 1 41 . 10 TRP H H 8.21 . 1 42 . 10 TRP CA C 57.69 . 1 43 . 10 TRP CB C 30.95 . 1 44 . 10 TRP C C 175.88 . 1 45 . 10 TRP HA H 4.56 . 1 46 . 11 THR CA C 62.27 . 1 47 . 11 THR CB C 69.34 . 1 48 . 11 THR HA H 4.46 . 1 49 . 12 SER N N 116.65 . 1 50 . 12 SER H H 7.83 . 1 51 . 12 SER CA C 57.28 . 1 52 . 12 SER CB C 65.18 . 1 53 . 12 SER C C 175.32 . 1 54 . 12 SER HA H 4.85 . 1 55 . 13 LYS N N 119.89 . 1 56 . 13 LYS H H 8.42 . 1 57 . 13 LYS CA C 60.54 . 1 58 . 13 LYS CB C 34.39 . 1 59 . 13 LYS C C 172.24 . 1 60 . 13 LYS HA H 4.32 . 1 61 . 14 VAL N N 116.95 . 1 62 . 14 VAL H H 7.54 . 1 63 . 14 VAL CA C 61.21 . 1 64 . 14 VAL CB C 34.78 . 1 65 . 14 VAL C C 176.83 . 1 66 . 14 VAL HA H 4.81 . 1 67 . 15 VAL N N 130.92 . 1 68 . 15 VAL H H 8.69 . 1 69 . 15 VAL CA C 60.95 . 1 70 . 15 VAL CB C 34.77 . 1 71 . 15 VAL C C 175.71 . 1 72 . 15 VAL HA H 4.29 . 1 73 . 16 THR N N 117.64 . 1 74 . 16 THR H H 9.12 . 1 75 . 16 THR CA C 59.37 . 1 76 . 16 THR CB C 72.71 . 1 77 . 16 THR C C 176.89 . 1 78 . 16 THR HA H 5.77 . 1 79 . 17 TYR N N 117.61 . 1 80 . 17 TYR H H 8.65 . 1 81 . 17 TYR CA C 55.73 . 1 82 . 17 TYR CB C 42.95 . 1 83 . 17 TYR C C 175.15 . 1 84 . 17 TYR HA H 5.81 . 1 85 . 18 ARG N N 119.73 . 1 86 . 18 ARG H H 8.62 . 1 87 . 18 ARG CA C 55.45 . 1 88 . 18 ARG CB C 35.67 . 1 89 . 18 ARG C C 170.16 . 1 90 . 18 ARG HA H 4.3 . 1 91 . 19 ILE N N 127.84 . 1 92 . 19 ILE H H 9.01 . 1 93 . 19 ILE CA C 61.73 . 1 94 . 19 ILE CB C 37.84 . 1 95 . 19 ILE C C 174.37 . 1 96 . 19 ILE HA H 4.76 . 1 97 . 20 VAL N N 126.53 . 1 98 . 20 VAL H H 9.58 . 1 99 . 20 VAL CA C 64.11 . 1 100 . 20 VAL CB C 33.76 . 1 101 . 20 VAL C C 176.27 . 1 102 . 20 VAL HA H 3.72 . 1 103 . 21 SER N N 112.72 . 1 104 . 21 SER H H 7.55 . 1 105 . 21 SER CA C 57.27 . 1 106 . 21 SER CB C 65.69 . 1 107 . 21 SER C C 176.83 . 1 108 . 21 SER HA H 4.88 . 1 109 . 22 TYR N N 116.95 . 1 110 . 22 TYR H H 8.41 . 1 111 . 22 TYR CA C 59.14 . 1 112 . 22 TYR CB C 41.49 . 1 113 . 22 TYR C C 169.71 . 1 114 . 22 TYR HA H 4.3 . 1 115 . 23 THR CA C 57.74 . 1 116 . 23 THR CB C 67.54 . 1 117 . 23 THR HA H 4.57 . 1 118 . 24 ARG N N 127.97 . 1 119 . 24 ARG H H 9.09 . 1 120 . 24 ARG CA C 57.83 . 1 121 . 24 ARG CB C 30.6 . 1 122 . 24 ARG C C 174.76 . 1 123 . 24 ARG HA H 4.12 . 1 124 . 25 ASP N N 120.3 . 1 125 . 25 ASP H H 8.97 . 1 126 . 25 ASP CA C 57.02 . 1 127 . 25 ASP CB C 43.06 . 1 128 . 25 ASP C C 179.75 . 1 129 . 25 ASP HA H 4.45 . 1 130 . 26 LEU N N 116.19 . 1 131 . 26 LEU H H 6.99 . 1 132 . 26 LEU CA C 51.62 . 1 133 . 26 LEU CB C 47.51 . 1 134 . 26 LEU C C 176.67 . 1 135 . 26 LEU HA H 5.06 . 1 136 . 28 HIS CA C 58.57 . 1 137 . 28 HIS CB C 29.21 . 1 138 . 28 HIS HA H 4.19 . 1 139 . 29 ILE N N 114.88 . 1 140 . 29 ILE H H 8.39 . 1 141 . 29 ILE CA C 63.74 . 1 142 . 29 ILE CB C 38.48 . 1 143 . 29 ILE C C 179.47 . 1 144 . 29 ILE HA H 4.27 . 1 145 . 30 THR N N 118.7 . 1 146 . 30 THR H H 7 . 1 147 . 30 THR CA C 66.97 . 1 148 . 30 THR CB C 68.5 . 1 149 . 30 THR C C 178.8 . 1 150 . 30 THR HA H 4.15 . 1 151 . 31 VAL N N 122.53 . 1 152 . 31 VAL H H 7.45 . 1 153 . 31 VAL CA C 68.23 . 1 154 . 31 VAL CB C 31.79 . 1 155 . 31 VAL C C 176.61 . 1 156 . 31 VAL HA H 3.51 . 1 157 . 32 ASP N N 119.52 . 1 158 . 32 ASP H H 8.72 . 1 159 . 32 ASP CA C 58.91 . 1 160 . 32 ASP CB C 41.11 . 1 161 . 32 ASP C C 178.86 . 1 162 . 32 ASP HA H 4.43 . 1 163 . 33 ARG N N 120.28 . 1 164 . 33 ARG H H 8.47 . 1 165 . 33 ARG CA C 60.08 . 1 166 . 33 ARG CB C 31.1 . 1 167 . 33 ARG C C 182.89 . 1 168 . 33 ARG HA H 4.26 . 1 169 . 34 LEU N N 120.8 . 1 170 . 34 LEU H H 8.86 . 1 171 . 34 LEU CA C 58.47 . 1 172 . 34 LEU CB C 42.34 . 1 173 . 34 LEU C C 182.17 . 1 174 . 34 LEU HA H 4.34 . 1 175 . 35 VAL N N 119.81 . 1 176 . 35 VAL H H 8.9 . 1 177 . 35 VAL CA C 68.35 . 1 178 . 35 VAL CB C 31.7 . 1 179 . 35 VAL C C 181.49 . 1 180 . 35 VAL HA H 3.51 . 1 181 . 36 SER N N 112.02 . 1 182 . 36 SER H H 7.71 . 1 183 . 36 SER CA C 62.48 . 1 184 . 36 SER C C 178.43 . 1 185 . 36 SER HA H 4.02 . 1 186 . 37 LYS N N 121.74 . 1 187 . 37 LYS H H 8.25 . 1 188 . 37 LYS CA C 60.35 . 1 189 . 37 LYS CB C 33.49 . 1 190 . 37 LYS C C 178.35 . 1 191 . 37 LYS HA H 4.19 . 1 192 . 38 ALA N N 123.24 . 1 193 . 38 ALA H H 8.39 . 1 194 . 38 ALA CA C 55.69 . 1 195 . 38 ALA CB C 20.81 . 1 196 . 38 ALA C C 180.36 . 1 197 . 38 ALA HA H 4.26 . 1 198 . 39 LEU N N 115.74 . 1 199 . 39 LEU H H 8.14 . 1 200 . 39 LEU CA C 58.26 . 1 201 . 39 LEU CB C 41.59 . 1 202 . 39 LEU C C 182.44 . 1 203 . 39 LEU HA H 3.9 . 1 204 . 40 ASN N N 116.15 . 1 205 . 40 ASN H H 8.33 . 1 206 . 40 ASN CA C 56.32 . 1 207 . 40 ASN CB C 39.38 . 1 208 . 40 ASN C C 177.39 . 1 209 . 40 ASN HA H 4.5 . 1 210 . 41 MET N N 121.22 . 1 211 . 41 MET H H 8.03 . 1 212 . 41 MET CA C 59.97 . 1 213 . 41 MET CB C 32.29 . 1 214 . 41 MET C C 179.19 . 1 215 . 41 MET HA H 4.12 . 1 216 . 42 TRP N N 116.58 . 1 217 . 42 TRP H H 6.91 . 1 218 . 42 TRP CA C 59.95 . 1 219 . 42 TRP CB C 31.42 . 1 220 . 42 TRP C C 179.81 . 1 221 . 42 TRP HA H 4.56 . 1 222 . 43 GLY N N 103.99 . 1 223 . 43 GLY H H 9.41 . 1 224 . 43 GLY CA C 47.64 . 1 225 . 43 GLY C C 177.14 . 1 226 . 43 GLY HA2 H 4.37 . 1 227 . 44 LYS N N 118.02 . 1 228 . 44 LYS H H 8.01 . 1 229 . 44 LYS CA C 57.46 . 1 230 . 44 LYS CB C 32.26 . 1 231 . 44 LYS C C 177.17 . 1 232 . 44 LYS HA H 4.27 . 1 233 . 45 GLU N N 113.11 . 1 234 . 45 GLU H H 7.88 . 1 235 . 45 GLU CA C 55.9 . 1 236 . 45 GLU CB C 31.62 . 1 237 . 45 GLU C C 179.24 . 1 238 . 45 GLU HA H 4.94 . 1 239 . 46 ILE N N 110.56 . 1 240 . 46 ILE H H 7.62 . 1 241 . 46 ILE CA C 58.88 . 1 242 . 46 ILE CB C 42.39 . 1 243 . 46 ILE C C 180.2 . 1 244 . 46 ILE HA H 5.47 . 1 245 . 47 PRO CA C 62.42 . 1 246 . 47 PRO CB C 29.84 . 1 247 . 47 PRO HA H 4.76 . 1 248 . 48 LEU N N 120.75 . 1 249 . 48 LEU H H 6.9 . 1 250 . 48 LEU CA C 55.05 . 1 251 . 48 LEU CB C 46.33 . 1 252 . 48 LEU C C 175.66 . 1 253 . 48 LEU HA H 4.45 . 1 254 . 49 HIS N N 120.13 . 1 255 . 49 HIS H H 7.82 . 1 256 . 49 HIS CA C 54.98 . 1 257 . 49 HIS CB C 33.83 . 1 258 . 49 HIS C C 174.37 . 1 259 . 49 HIS HA H 4.71 . 1 260 . 50 PHE N N 119.88 . 1 261 . 50 PHE H H 8.42 . 1 262 . 50 PHE CA C 56.81 . 1 263 . 50 PHE CB C 42.3 . 1 264 . 50 PHE C C 173.41 . 1 265 . 50 PHE HA H 5.96 . 1 266 . 51 ARG N N 123.28 . 1 267 . 51 ARG H H 8.49 . 1 268 . 51 ARG CA C 55.04 . 1 269 . 51 ARG CB C 34.75 . 1 270 . 51 ARG C C 176.56 . 1 271 . 51 ARG HA H 4.76 . 1 272 . 52 LYS N N 129.48 . 1 273 . 52 LYS H H 8.58 . 1 274 . 52 LYS CA C 56.58 . 1 275 . 52 LYS CB C 34.19 . 1 276 . 52 LYS C C 173.95 . 1 277 . 52 LYS HA H 4.45 . 1 278 . 53 VAL N N 124.8 . 1 279 . 53 VAL H H 8.81 . 1 280 . 53 VAL CA C 60.57 . 1 281 . 53 VAL CB C 35.05 . 1 282 . 53 VAL C C 177.45 . 1 283 . 53 VAL HA H 4.61 . 1 284 . 54 VAL N N 117.1 . 1 285 . 54 VAL H H 8.52 . 1 286 . 54 VAL CA C 62.53 . 1 287 . 54 VAL CB C 32.99 . 1 288 . 54 VAL C C 176.67 . 1 289 . 54 VAL HA H 4.4 . 1 290 . 55 TRP N N 119.45 . 1 291 . 55 TRP H H 7.54 . 1 292 . 55 TRP CA C 56.46 . 1 293 . 55 TRP CB C 32.73 . 1 294 . 55 TRP C C 175.21 . 1 295 . 55 TRP HA H 4.6 . 1 296 . 56 GLY N N 109.51 . 1 297 . 56 GLY H H 8.1 . 1 298 . 56 GLY CA C 45.14 . 1 299 . 56 GLY C C 175.04 . 1 300 . 56 GLY HA2 H 4.1 . 1 301 . 57 THR N N 115.53 . 1 302 . 57 THR H H 8.28 . 1 303 . 57 THR CA C 63.49 . 1 304 . 57 THR CB C 69.82 . 1 305 . 57 THR C C 173.08 . 1 306 . 57 THR HA H 4.27 . 1 307 . 58 ALA N N 129.33 . 1 308 . 58 ALA H H 8.06 . 1 309 . 58 ALA CA C 49.92 . 1 310 . 58 ALA CB C 23.69 . 1 311 . 58 ALA C C 172.35 . 1 312 . 58 ALA HA H 4.63 . 1 313 . 59 ASP N N 122.48 . 1 314 . 59 ASP H H 8.36 . 1 315 . 59 ASP CA C 58.51 . 1 316 . 59 ASP CB C 41.11 . 1 317 . 59 ASP C C 176.28 . 1 318 . 59 ASP HA H 4.5 . 1 319 . 60 ILE N N 124.74 . 1 320 . 60 ILE H H 8.85 . 1 321 . 60 ILE CA C 61.91 . 1 322 . 60 ILE CB C 39.48 . 1 323 . 60 ILE C C 179.24 . 1 324 . 60 ILE HA H 3.97 . 1 325 . 61 MET N N 126.76 . 1 326 . 61 MET H H 7.47 . 1 327 . 61 MET CA C 54.33 . 1 328 . 61 MET CB C 33.65 . 1 329 . 61 MET C C 174.59 . 1 330 . 61 MET HA H 5.33 . 1 331 . 62 ILE N N 125.27 . 1 332 . 62 ILE H H 9.28 . 1 333 . 62 ILE CA C 60.56 . 1 334 . 62 ILE CB C 41.65 . 1 335 . 62 ILE C C 177.56 . 1 336 . 62 ILE HA H 5.69 . 1 337 . 63 GLY N N 111.91 . 1 338 . 63 GLY H H 8.81 . 1 339 . 63 GLY CA C 45.91 . 1 340 . 63 GLY C C 176.05 . 1 341 . 63 GLY HA2 H 4.96 . 1 342 . 64 PHE N N 118.8 . 1 343 . 64 PHE H H 7.94 . 1 344 . 64 PHE CA C 56.42 . 1 345 . 64 PHE CB C 42.22 . 1 346 . 64 PHE C C 169.77 . 1 347 . 64 PHE HA H 5.63 . 1 348 . 65 ALA N N 123.52 . 1 349 . 65 ALA H H 9.14 . 1 350 . 65 ALA CA C 51.71 . 1 351 . 65 ALA CB C 23.58 . 1 352 . 65 ALA C C 176.16 . 1 353 . 65 ALA HA H 4.89 . 1 354 . 66 ARG N N 118.16 . 1 355 . 66 ARG H H 8.67 . 1 356 . 66 ARG CA C 54.75 . 1 357 . 66 ARG CB C 34.23 . 1 358 . 66 ARG C C 175.6 . 1 359 . 66 ARG HA H 5.24 . 1 360 . 67 GLY N N 108.5 . 1 361 . 67 GLY H H 9.29 . 1 362 . 67 GLY CA C 47.16 . 1 363 . 67 GLY C C 177.62 . 1 364 . 67 GLY HA2 H 4.35 . 1 365 . 68 ALA CA C 53.4 . 1 366 . 68 ALA CB C 18.7 . 1 367 . 68 ALA HA H 3.91 . 1 368 . 69 HIS N N 119.71 . 1 369 . 69 HIS H H 9.16 . 1 370 . 69 HIS CA C 55.7 . 1 371 . 69 HIS CB C 28.89 . 1 372 . 69 HIS C C 178.7 . 1 373 . 69 HIS HA H 5.23 . 1 374 . 70 GLY CA C 44.56 . 1 375 . 70 GLY HA2 H 4.3 . 1 376 . 71 ASP N N 116.89 . 1 377 . 71 ASP H H 7.16 . 1 378 . 71 ASP CA C 51.84 . 1 379 . 71 ASP CB C 42.14 . 1 380 . 71 ASP C C 174.1 . 1 381 . 71 ASP HA H 5.01 . 1 382 . 72 SER CA C 59.22 . 1 383 . 72 SER CB C 62.9 . 1 384 . 72 SER HA H 4.28 . 1 385 . 73 TYR N N 120 . 1 386 . 73 TYR H H 7.67 . 1 387 . 73 TYR CA C 54.67 . 1 388 . 73 TYR CB C 39.55 . 1 389 . 73 TYR C C 171.74 . 1 390 . 73 TYR HA H 4.28 . 1 391 . 74 PRO CA C 63.31 . 1 392 . 74 PRO CB C 31.4 . 1 393 . 74 PRO HA H 4.45 . 1 394 . 75 PHE N N 120.53 . 1 395 . 75 PHE H H 8.14 . 1 396 . 75 PHE CA C 58.62 . 1 397 . 75 PHE CB C 39.21 . 1 398 . 75 PHE C C 181.96 . 1 399 . 75 PHE HA H 4.3 . 1 400 . 76 ASP N N 115.76 . 1 401 . 76 ASP H H 7.94 . 1 402 . 76 ASP CA C 54.12 . 1 403 . 76 ASP CB C 42.26 . 1 404 . 76 ASP C C 175.34 . 1 405 . 76 ASP HA H 4.93 . 1 406 . 77 GLY N N 110.39 . 1 407 . 77 GLY H H 8.97 . 1 408 . 77 GLY HA2 H 4.2 . 1 409 . 77 GLY CA C 44.81 . 1 410 . 77 GLY C C 179.38 . 1 411 . 78 PRO CA C 64.17 . 1 412 . 78 PRO CB C 31.64 . 1 413 . 78 PRO HA H 4 . 1 414 . 79 GLY N N 118.69 . 1 415 . 79 GLY H H 11.12 . 1 416 . 79 GLY CA C 44.08 . 1 417 . 79 GLY C C 176.03 . 1 418 . 79 GLY HA2 H 4.5 . 1 419 . 80 ASN N N 118.03 . 1 420 . 80 ASN H H 9.01 . 1 421 . 80 ASN CA C 56.36 . 1 422 . 80 ASN CB C 38.41 . 1 423 . 80 ASN C C 174.96 . 1 424 . 80 ASN HA H 4.17 . 1 425 . 81 THR N N 123.25 . 1 426 . 81 THR H H 9.93 . 1 427 . 81 THR CA C 65.93 . 1 428 . 81 THR CB C 69.72 . 1 429 . 81 THR C C 175.18 . 1 430 . 81 THR HA H 4.47 . 1 431 . 82 LEU N N 125.53 . 1 432 . 82 LEU H H 8.51 . 1 433 . 82 LEU CA C 56.04 . 1 434 . 82 LEU CB C 44.68 . 1 435 . 82 LEU C C 175.6 . 1 436 . 82 LEU HA H 4.2 . 1 437 . 83 ALA N N 114.25 . 1 438 . 83 ALA H H 7.81 . 1 439 . 83 ALA CA C 52.53 . 1 440 . 83 ALA CB C 22.35 . 1 441 . 83 ALA C C 177.17 . 1 442 . 83 ALA HA H 4.9 . 1 443 . 84 HIS N N 116.82 . 1 444 . 84 HIS H H 9.28 . 1 445 . 84 HIS CA C 55.54 . 1 446 . 84 HIS CB C 31.41 . 1 447 . 84 HIS C C 177.06 . 1 448 . 84 HIS HA H 5.08 . 1 449 . 85 ALA N N 120.69 . 1 450 . 85 ALA H H 8.52 . 1 451 . 85 ALA CA C 51.53 . 1 452 . 85 ALA CB C 24.52 . 1 453 . 85 ALA C C 170.28 . 1 454 . 85 ALA HA H 4.97 . 1 455 . 86 PHE N N 118.58 . 1 456 . 86 PHE H H 8.02 . 1 457 . 86 PHE CA C 57.03 . 1 458 . 86 PHE CB C 42.45 . 1 459 . 86 PHE C C 175.77 . 1 460 . 86 PHE HA H 4.49 . 1 461 . 87 ALA N N 122.9 . 1 462 . 87 ALA H H 8.2 . 1 463 . 87 ALA CA C 51.03 . 1 464 . 87 ALA CB C 17.25 . 1 465 . 87 ALA C C 175.49 . 1 466 . 87 ALA HA H 4.43 . 1 467 . 88 PRO CA C 65.51 . 1 468 . 88 PRO CB C 31.94 . 1 469 . 88 PRO HA H 2.97 . 1 470 . 89 GLY N N 107 . 1 471 . 89 GLY H H 6.12 . 1 472 . 89 GLY CA C 44.59 . 1 473 . 89 GLY C C 173.44 . 1 474 . 89 GLY HA2 H 4.23 . 1 475 . 90 THR CA C 62.67 . 1 476 . 90 THR CB C 70.6 . 1 477 . 90 THR HA H 4.31 . 1 478 . 91 GLY N N 112.36 . 1 479 . 91 GLY H H 8.9 . 1 480 . 91 GLY CA C 47.87 . 1 481 . 91 GLY C C 177.91 . 1 482 . 91 GLY HA2 H 4.09 . 1 483 . 92 LEU CA C 56.3 . 1 484 . 92 LEU CB C 42.18 . 1 485 . 92 LEU HA H 4.3 . 1 486 . 93 GLY N N 102.61 . 1 487 . 93 GLY H H 7.87 . 1 488 . 93 GLY CA C 47.53 . 1 489 . 93 GLY C C 177.9 . 1 490 . 93 GLY HA2 H 3.91 . 1 491 . 94 GLY N N 120.65 . 1 492 . 94 GLY H H 7.77 . 1 493 . 94 GLY CA C 47.6 . 1 494 . 94 GLY C C 175.38 . 1 495 . 94 GLY HA2 H 4.9 . 1 496 . 95 ASP N N 123.03 . 1 497 . 95 ASP H H 8.67 . 1 498 . 95 ASP CA C 56.41 . 1 499 . 95 ASP CB C 40.67 . 1 500 . 95 ASP C C 174.66 . 1 501 . 95 ASP HA H 4.61 . 1 502 . 96 ALA N N 118.94 . 1 503 . 96 ALA H H 8.36 . 1 504 . 96 ALA CA C 51.8 . 1 505 . 96 ALA CB C 22.5 . 1 506 . 96 ALA C C 173.98 . 1 507 . 96 ALA HA H 4.97 . 1 508 . 97 HIS N N 120.57 . 1 509 . 97 HIS H H 9.33 . 1 510 . 97 HIS CA C 51.49 . 1 511 . 97 HIS CB C 34.95 . 1 512 . 97 HIS C C 175.54 . 1 513 . 97 HIS HA H 5.9 . 1 514 . 98 PHE N N 121.68 . 1 515 . 98 PHE H H 8.79 . 1 516 . 98 PHE CA C 57.11 . 1 517 . 98 PHE CB C 42.34 . 1 518 . 98 PHE C C 173.02 . 1 519 . 98 PHE HA H 4.49 . 1 520 . 99 ASP N N 122.95 . 1 521 . 99 ASP H H 8.28 . 1 522 . 99 ASP CA C 55.16 . 1 523 . 99 ASP CB C 41.24 . 1 524 . 99 ASP C C 174.03 . 1 525 . 99 ASP HA H 4.26 . 1 526 . 100 GLU N N 132.34 . 1 527 . 100 GLU H H 9.59 . 1 528 . 100 GLU CA C 56.68 . 1 529 . 100 GLU CB C 31.58 . 1 530 . 100 GLU C C 181.43 . 1 531 . 100 GLU HA H 4.24 . 1 532 . 101 ASP N N 117.83 . 1 533 . 101 ASP H H 8.94 . 1 534 . 101 ASP CA C 56.78 . 1 535 . 101 ASP CB C 40.46 . 1 536 . 101 ASP C C 177.73 . 1 537 . 101 ASP HA H 4.92 . 1 538 . 102 GLU N N 116.33 . 1 539 . 102 GLU H H 7.38 . 1 540 . 102 GLU CA C 54.07 . 1 541 . 102 GLU C C 178.57 . 1 542 . 102 GLU HA H 4.53 . 1 543 . 103 ARG N N 122.67 . 1 544 . 103 ARG H H 7.88 . 1 545 . 103 ARG CA C 54.33 . 1 546 . 103 ARG CB C 30.08 . 1 547 . 103 ARG C C 175.88 . 1 548 . 103 ARG HA H 4.52 . 1 549 . 104 TRP N N 129.45 . 1 550 . 104 TRP H H 9.04 . 1 551 . 104 TRP CA C 57.48 . 1 552 . 104 TRP CB C 31.27 . 1 553 . 104 TRP C C 174.54 . 1 554 . 104 TRP HA H 5.18 . 1 555 . 105 THR N N 112.51 . 1 556 . 105 THR H H 9.1 . 1 557 . 105 THR CA C 59.73 . 1 558 . 105 THR CB C 71.89 . 1 559 . 105 THR C C 177.56 . 1 560 . 105 THR HA H 5.08 . 1 561 . 106 ASP N N 121.47 . 1 562 . 106 ASP H H 8.58 . 1 563 . 106 ASP CA C 53.75 . 1 564 . 106 ASP CB C 42.44 . 1 565 . 106 ASP C C 172.41 . 1 566 . 106 ASP HA H 5.02 . 1 567 . 107 GLY N N 109.39 . 1 568 . 107 GLY H H 8.68 . 1 569 . 107 GLY CA C 45.83 . 1 570 . 107 GLY C C 177.96 . 1 571 . 107 GLY HA2 H 4.58 . 1 572 . 108 SER N N 114.94 . 1 573 . 108 SER H H 8.31 . 1 574 . 108 SER CA C 59.08 . 1 575 . 108 SER CB C 64.6 . 1 576 . 108 SER C C 174.87 . 1 577 . 108 SER HA H 4.86 . 1 578 . 109 SER N N 122.92 . 1 579 . 109 SER H H 8.04 . 1 580 . 109 SER CA C 60.58 . 1 581 . 109 SER CB C 65.36 . 1 582 . 109 SER C C 173.86 . 1 583 . 109 SER HA H 4.78 . 1 584 . 110 LEU CA C 55.62 . 1 585 . 110 LEU CB C 42.52 . 1 586 . 110 LEU HA H 4.49 . 1 587 . 111 GLY N N 108.69 . 1 588 . 111 GLY H H 8.03 . 1 589 . 111 GLY CA C 44.9 . 1 590 . 111 GLY C C 177.56 . 1 591 . 111 GLY HA2 H 4.1 . 1 592 . 112 ILE N N 122.55 . 1 593 . 112 ILE H H 9.04 . 1 594 . 112 ILE CA C 58.67 . 1 595 . 112 ILE CB C 35.91 . 1 596 . 112 ILE C C 171.68 . 1 597 . 112 ILE HA H 3.94 . 1 598 . 113 ASN N N 126.47 . 1 599 . 113 ASN H H 8.73 . 1 600 . 113 ASN CA C 55.21 . 1 601 . 113 ASN CB C 39.8 . 1 602 . 113 ASN C C 176.39 . 1 603 . 113 ASN HA H 4.61 . 1 604 . 114 PHE N N 129.25 . 1 605 . 114 PHE H H 9.51 . 1 606 . 114 PHE CA C 59.65 . 1 607 . 114 PHE CB C 35.82 . 1 608 . 114 PHE C C 176.72 . 1 609 . 114 PHE HA H 4.71 . 1 610 . 115 LEU N N 118.53 . 1 611 . 115 LEU H H 8.75 . 1 612 . 115 LEU CA C 59.43 . 1 613 . 115 LEU CB C 41.35 . 1 614 . 115 LEU C C 176.77 . 1 615 . 115 LEU HA H 3.97 . 1 616 . 116 TYR N N 121.52 . 1 617 . 116 TYR H H 8.13 . 1 618 . 116 TYR CA C 60.31 . 1 619 . 116 TYR CB C 38.51 . 1 620 . 116 TYR C C 177.34 . 1 621 . 116 TYR HA H 4.14 . 1 622 . 117 ALA N N 118.3 . 1 623 . 117 ALA H H 8.02 . 1 624 . 117 ALA CA C 55.4 . 1 625 . 117 ALA CB C 19.3 . 1 626 . 117 ALA C C 179.13 . 1 627 . 117 ALA HA H 4.25 . 1 628 . 118 ALA N N 119.42 . 1 629 . 118 ALA H H 9.62 . 1 630 . 118 ALA CA C 55.89 . 1 631 . 118 ALA CB C 17.17 . 1 632 . 118 ALA C C 182.94 . 1 633 . 118 ALA HA H 4.09 . 1 634 . 119 THR N N 116.26 . 1 635 . 119 THR H H 8.45 . 1 636 . 119 THR CA C 69.4 . 1 637 . 119 THR C C 174.61 . 1 638 . 119 THR HA H 4.29 . 1 639 . 120 HIS N N 121.51 . 1 640 . 120 HIS H H 7.67 . 1 641 . 120 HIS CA C 59.72 . 1 642 . 120 HIS CB C 29.09 . 1 643 . 120 HIS C C 178.68 . 1 644 . 120 HIS HA H 4.76 . 1 645 . 121 GLU N N 116.02 . 1 646 . 121 GLU H H 9.24 . 1 647 . 121 GLU CA C 59.4 . 1 648 . 121 GLU CB C 29.34 . 1 649 . 121 GLU C C 177.84 . 1 650 . 121 GLU HA H 4.04 . 1 651 . 122 LEU N N 116.57 . 1 652 . 122 LEU H H 9.13 . 1 653 . 122 LEU CA C 57 . 1 654 . 122 LEU CB C 40.09 . 1 655 . 122 LEU C C 179.92 . 1 656 . 122 LEU HA H 4.32 . 1 657 . 123 GLY N N 107.48 . 1 658 . 123 GLY H H 7.65 . 1 659 . 123 GLY CA C 48.26 . 1 660 . 123 GLY C C 179.41 . 1 661 . 123 GLY HA2 H 3.77 . 1 662 . 124 HIS N N 122.98 . 1 663 . 124 HIS H H 7.42 . 1 664 . 124 HIS CA C 58.84 . 1 665 . 124 HIS CB C 28.8 . 1 666 . 124 HIS C C 180.53 . 1 667 . 124 HIS HA H 4.29 . 1 668 . 125 SER N N 119.18 . 1 669 . 125 SER H H 8.61 . 1 670 . 125 SER CA C 63.39 . 1 671 . 125 SER C C 177.54 . 1 672 . 125 SER HA H 4.44 . 1 673 . 126 LEU N N 114.88 . 1 674 . 126 LEU H H 7.31 . 1 675 . 126 LEU CA C 55.43 . 1 676 . 126 LEU CB C 43.47 . 1 677 . 126 LEU C C 175.26 . 1 678 . 126 LEU HA H 4.01 . 1 679 . 127 GLY N N 107.65 . 1 680 . 127 GLY H H 8.33 . 1 681 . 127 GLY CA C 44.82 . 1 682 . 127 GLY C C 174.77 . 1 683 . 127 GLY HA2 H 4.76 . 1 684 . 128 MET N N 118.94 . 1 685 . 128 MET H H 8.36 . 1 686 . 128 MET CA C 54.98 . 1 687 . 128 MET CB C 32.6 . 1 688 . 128 MET C C 174.54 . 1 689 . 128 MET HA H 4.64 . 1 690 . 129 GLY N N 110.98 . 1 691 . 129 GLY H H 8.64 . 1 692 . 129 GLY CA C 43.3 . 1 693 . 129 GLY C C 179.08 . 1 694 . 129 GLY HA2 H 4.54 . 1 695 . 130 HIS N N 116.22 . 1 696 . 130 HIS H H 8.51 . 1 697 . 130 HIS CA C 55.68 . 1 698 . 130 HIS CB C 29.82 . 1 699 . 130 HIS C C 174.09 . 1 700 . 130 HIS HA H 5.2 . 1 701 . 131 SER N N 114.89 . 1 702 . 131 SER H H 7.01 . 1 703 . 131 SER CA C 55.88 . 1 704 . 131 SER CB C 65.81 . 1 705 . 131 SER C C 175.66 . 1 706 . 131 SER HA H 4.3 . 1 707 . 132 SER N N 119.71 . 1 708 . 132 SER H H 8.85 . 1 709 . 132 SER CA C 59.13 . 1 710 . 132 SER CB C 64.27 . 1 711 . 132 SER C C 176.11 . 1 712 . 132 SER HA H 4.6 . 1 713 . 133 ASP N N 126.5 . 1 714 . 133 ASP H H 9.03 . 1 715 . 133 ASP CA C 51.6 . 1 716 . 133 ASP CB C 42.55 . 1 717 . 133 ASP C C 173.3 . 1 718 . 133 ASP HA H 4.99 . 1 719 . 134 PRO CA C 62.88 . 1 720 . 134 PRO CB C 32.1 . 1 721 . 135 ASN N N 114.86 . 1 722 . 135 ASN H H 8.42 . 1 723 . 135 ASN CA C 53.87 . 1 724 . 135 ASN CB C 39.88 . 1 725 . 135 ASN C C 178.74 . 1 726 . 135 ASN HA H 4.03 . 1 727 . 136 ALA N N 124.24 . 1 728 . 136 ALA H H 8.28 . 1 729 . 136 ALA CA C 52.58 . 1 730 . 136 ALA CB C 20.43 . 1 731 . 136 ALA C C 175.54 . 1 732 . 136 ALA HA H 4.7 . 1 733 . 137 VAL N N 123.39 . 1 734 . 137 VAL H H 7.99 . 1 735 . 137 VAL CA C 63.66 . 1 736 . 137 VAL CB C 33.25 . 1 737 . 137 VAL C C 178.07 . 1 738 . 137 VAL HA H 4.03 . 1 739 . 138 MET N N 113.22 . 1 740 . 138 MET H H 7.95 . 1 741 . 138 MET CA C 53.8 . 1 742 . 138 MET CB C 28.2 . 1 743 . 138 MET C C 170.16 . 1 744 . 138 MET HA H 4.64 . 1 745 . 139 TYR N N 129.04 . 1 746 . 139 TYR H H 8.14 . 1 747 . 139 TYR CA C 57.5 . 1 748 . 139 TYR CB C 39.76 . 1 749 . 139 TYR C C 178.62 . 1 750 . 139 TYR HA H 4.24 . 1 751 . 140 PRO CA C 64.03 . 1 752 . 140 PRO CB C 28.02 . 1 753 . 141 THR N N 115.2 . 1 754 . 141 THR H H 7.46 . 1 755 . 141 THR CA C 62.21 . 1 756 . 141 THR CB C 71.56 . 1 757 . 141 THR C C 174.82 . 1 758 . 141 THR HA H 4.36 . 1 759 . 142 TYR N N 126.88 . 1 760 . 142 TYR H H 9.19 . 1 761 . 142 TYR CA C 59.51 . 1 762 . 142 TYR CB C 39.45 . 1 763 . 142 TYR C C 173.08 . 1 764 . 142 TYR HA H 4.61 . 1 765 . 143 GLY N N 116.89 . 1 766 . 143 GLY H H 8.12 . 1 767 . 143 GLY CA C 45.3 . 1 768 . 143 GLY C C 175.77 . 1 769 . 143 GLY HA2 H 4.56 . 1 770 . 144 ASN N N 123.11 . 1 771 . 144 ASN H H 7.79 . 1 772 . 144 ASN CA C 54.81 . 1 773 . 144 ASN CB C 41.55 . 1 774 . 144 ASN C C 176.89 . 1 775 . 144 ASN HA H 4.45 . 1 776 . 145 GLY N N 114.91 . 1 777 . 145 GLY H H 8.15 . 1 778 . 145 GLY CA C 45.32 . 1 779 . 145 GLY C C 177.01 . 1 780 . 145 GLY HA2 H 4.03 . 1 781 . 146 ASP N N 126.22 . 1 782 . 146 ASP H H 8.05 . 1 783 . 146 ASP CA C 56.28 . 1 784 . 146 ASP CB C 42.87 . 1 785 . 146 ASP C C 172.57 . 1 786 . 146 ASP HA H 4.51 . 1 787 . 147 PRO CA C 64.43 . 1 788 . 147 PRO CB C 32.27 . 1 789 . 148 GLN N N 116.16 . 1 790 . 148 GLN H H 8.38 . 1 791 . 148 GLN CA C 57.86 . 1 792 . 148 GLN CB C 29.97 . 1 793 . 148 GLN C C 179.31 . 1 794 . 148 GLN HA H 4.34 . 1 795 . 149 ASN N N 117.6 . 1 796 . 149 ASN H H 7.99 . 1 797 . 149 ASN CA C 53.11 . 1 798 . 149 ASN CB C 39.73 . 1 799 . 149 ASN C C 177.9 . 1 800 . 149 ASN HA H 4.92 . 1 801 . 150 PHE N N 120.87 . 1 802 . 150 PHE H H 7.66 . 1 803 . 150 PHE CA C 58.21 . 1 804 . 150 PHE CB C 40.28 . 1 805 . 150 PHE C C 173.4 . 1 806 . 150 PHE HA H 4.29 . 1 807 . 151 LYS N N 120 . 1 808 . 151 LYS H H 7.96 . 1 809 . 151 LYS CA C 54.82 . 1 810 . 151 LYS CB C 35.59 . 1 811 . 151 LYS C C 172.63 . 1 812 . 151 LYS HA H 4.86 . 1 813 . 152 LEU N N 118.03 . 1 814 . 152 LEU H H 8.11 . 1 815 . 152 LEU CA C 56.01 . 1 816 . 152 LEU CB C 42.18 . 1 817 . 152 LEU C C 175.43 . 1 818 . 152 LEU HA H 4.51 . 1 819 . 153 SER CA C 61.78 . 1 820 . 153 SER HA H 3.87 . 1 821 . 154 GLN N N 122.54 . 1 822 . 154 GLN H H 8.36 . 1 823 . 154 GLN CA C 58.53 . 1 824 . 154 GLN CB C 28.2 . 1 825 . 154 GLN C C 176.34 . 1 826 . 154 GLN HA H 4.16 . 1 827 . 155 ASP CA C 58.6 . 1 828 . 155 ASP CB C 44.3 . 1 829 . 155 ASP HA H 4.47 . 1 830 . 156 ASP N N 118.41 . 1 831 . 156 ASP H H 7.45 . 1 832 . 156 ASP CA C 57.98 . 1 833 . 156 ASP CB C 44.32 . 1 834 . 156 ASP C C 180.49 . 1 835 . 156 ASP HA H 4.45 . 1 836 . 157 ILE N N 120.08 . 1 837 . 157 ILE H H 8.24 . 1 838 . 157 ILE CA C 66.02 . 1 839 . 157 ILE CB C 39.34 . 1 840 . 157 ILE C C 179.75 . 1 841 . 157 ILE HA H 3.77 . 1 842 . 158 LYS N N 118.41 . 1 843 . 158 LYS H H 8.74 . 1 844 . 158 LYS CA C 59.8 . 1 845 . 158 LYS CB C 32.8 . 1 846 . 158 LYS C C 179.69 . 1 847 . 158 LYS HA H 4.16 . 1 848 . 159 GLY N N 105.92 . 1 849 . 159 GLY H H 8.18 . 1 850 . 159 GLY CA C 48.28 . 1 851 . 159 GLY C C 175.37 . 1 852 . 159 GLY HA2 H 3.14 . 1 853 . 160 ILE N N 124.65 . 1 854 . 160 ILE H H 8.66 . 1 855 . 160 ILE CA C 61.99 . 1 856 . 160 ILE CB C 38.3 . 1 857 . 160 ILE C C 177.51 . 1 858 . 160 ILE HA H 4.76 . 1 859 . 161 GLN N N 122.48 . 1 860 . 161 GLN H H 8.36 . 1 861 . 161 GLN CA C 49.97 . 1 862 . 161 GLN CB C 28.18 . 1 863 . 161 GLN C C 180.57 . 1 864 . 161 GLN HA H 4.5 . 1 865 . 162 LYS N N 123 . 1 866 . 162 LYS H H 8.15 . 1 867 . 162 LYS CA C 59.78 . 1 868 . 162 LYS CB C 32.77 . 1 869 . 162 LYS C C 177.69 . 1 870 . 162 LYS HA H 4.15 . 1 871 . 163 LEU N N 116.19 . 1 872 . 163 LEU H H 7 . 1 873 . 163 LEU CA C 57.83 . 1 874 . 163 LEU CB C 44.66 . 1 875 . 163 LEU C C 180.48 . 1 876 . 163 LEU HA H 4.1 . 1 877 . 164 TYR N N 111.71 . 1 878 . 164 TYR H H 7.61 . 1 879 . 164 TYR CA C 60.18 . 1 880 . 164 TYR CB C 42.08 . 1 881 . 164 TYR C C 178.91 . 1 882 . 164 TYR HA H 4.76 . 1 883 . 165 GLY N N 110.34 . 1 884 . 165 GLY H H 8.56 . 1 885 . 165 GLY CA C 44.47 . 1 886 . 165 GLY C C 177.34 . 1 887 . 165 GLY HA2 H 4.48 . 1 888 . 166 LYS N N 113.64 . 1 889 . 166 LYS H H 7.97 . 1 890 . 166 LYS CA C 55.79 . 1 891 . 166 LYS CB C 35.18 . 1 892 . 166 LYS C C 177.04 . 1 893 . 166 LYS HA H 4.94 . 1 894 . 167 ARG N N 123.24 . 1 895 . 167 ARG H H 7.86 . 1 896 . 167 ARG CA C 57.87 . 1 897 . 167 ARG CB C 31.25 . 1 898 . 167 ARG C C 179.41 . 1 899 . 167 ARG HA H 4.52 . 1 900 . 169 ASN CA C 53.53 . 1 901 . 169 ASN CB C 39.3 . 1 902 . 170 SER N N 118.87 . 1 903 . 170 SER H H 7.8 . 1 904 . 170 SER CA C 63.66 . 1 905 . 170 SER CB C 71.29 . 1 906 . 170 SER C C 175.07 . 1 907 . 171 ARG CA C 56.89 . 1 908 . 171 ARG CB C 30.38 . 1 909 . 172 LYS N N 127.06 . 1 910 . 172 LYS H H 7.92 . 1 911 . 172 LYS CA C 57.85 . 1 912 . 172 LYS CB C 32.11 . 1 913 . 172 LYS C C 176.39 . 1 914 . 172 LYS HA H 4.43 . 1 915 . 173 LYS N N 128.2 . 1 916 . 173 LYS H H 8 . 1 917 . 173 LYS CA C 58.45 . 1 918 . 173 LYS CB C 34.33 . 1 919 . 173 LYS C C 176.46 . 1 stop_ save_