data_18941 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C, and 15N chemical shift assignments for the LFA-1 wild type I-domain ; _BMRB_accession_number 18941 _BMRB_flat_file_name bmr18941.str _Entry_type original _Submission_date 2013-01-07 _Accession_date 2013-01-07 _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 Zimmerman Tahl . . 2 Blanco Francisco J. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 305 "13C chemical shifts" 447 "15N chemical shifts" 175 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2013-01-24 original author . stop_ _Original_release_date 2013-01-24 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'ICAM-1 peptide inhibitors of T-cell adhesion bind to the allosteric site of LFA-1. An NMR characterization' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 17868072 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Zimmerman Tahl . . 2 Oyarzabal Julen . . 3 San-Sebastian Eider S. . 4 Majumdar Sumit . . 5 Tejo Bimo A. . 6 Siahaan Teruna J. . 7 Blanco Francisco J. . stop_ _Journal_abbreviation 'Chem. Biol. Drug Design' _Journal_volume 70 _Journal_issue 4 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 347 _Page_last 353 _Year 2007 _Details . loop_ _Keyword allosteric inhibitor LFA-1 NMR peptide stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'LFA-1 I-Domain' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'LFA-1 I-domain' $LFA-1_I-domain 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_LFA-1_I-domain _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common LFA-1_I-domain _Molecular_mass 20682.7 _Mol_thiol_state 'not present' loop_ _Biological_function 'Lymphocyte adhesion' stop_ _Details ; This is the inserted domain of the human alfa-L chain chain of LFA-1 (UNIPROT P20701), and the numbering used ignores the signal sequence (residues 1-26 in the unprocessed polypeptide). ; ############################## # Polymer residue sequence # ############################## _Residue_count 181 _Mol_residue_sequence ; MGNVDLVFLFDGSMSLQPDE FQKILDFMKDVMKKLSNTSY QFAAVQFSTSYKTEFDFSDY VKRKDPDALLKHVKHMLLLT NTFGAINYVATEVFREELGA RPDATKVLIIITDGEATDSG NIDAAKDIIRYIIGIGKHFQ TKESQETLHKFASKPASEFV KILDTFEKLKDLFTELQKKI Y ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 127 MET 2 128 GLY 3 129 ASN 4 130 VAL 5 131 ASP 6 132 LEU 7 133 VAL 8 134 PHE 9 135 LEU 10 136 PHE 11 137 ASP 12 138 GLY 13 139 SER 14 140 MET 15 141 SER 16 142 LEU 17 143 GLN 18 144 PRO 19 145 ASP 20 146 GLU 21 147 PHE 22 148 GLN 23 149 LYS 24 150 ILE 25 151 LEU 26 152 ASP 27 153 PHE 28 154 MET 29 155 LYS 30 156 ASP 31 157 VAL 32 158 MET 33 159 LYS 34 160 LYS 35 161 LEU 36 162 SER 37 163 ASN 38 164 THR 39 165 SER 40 166 TYR 41 167 GLN 42 168 PHE 43 169 ALA 44 170 ALA 45 171 VAL 46 172 GLN 47 173 PHE 48 174 SER 49 175 THR 50 176 SER 51 177 TYR 52 178 LYS 53 179 THR 54 180 GLU 55 181 PHE 56 182 ASP 57 183 PHE 58 184 SER 59 185 ASP 60 186 TYR 61 187 VAL 62 188 LYS 63 189 ARG 64 190 LYS 65 191 ASP 66 192 PRO 67 193 ASP 68 194 ALA 69 195 LEU 70 196 LEU 71 197 LYS 72 198 HIS 73 199 VAL 74 200 LYS 75 201 HIS 76 202 MET 77 203 LEU 78 204 LEU 79 205 LEU 80 206 THR 81 207 ASN 82 208 THR 83 209 PHE 84 210 GLY 85 211 ALA 86 212 ILE 87 213 ASN 88 214 TYR 89 215 VAL 90 216 ALA 91 217 THR 92 218 GLU 93 219 VAL 94 220 PHE 95 221 ARG 96 222 GLU 97 223 GLU 98 224 LEU 99 225 GLY 100 226 ALA 101 227 ARG 102 228 PRO 103 229 ASP 104 230 ALA 105 231 THR 106 232 LYS 107 233 VAL 108 234 LEU 109 235 ILE 110 236 ILE 111 237 ILE 112 238 THR 113 239 ASP 114 240 GLY 115 241 GLU 116 242 ALA 117 243 THR 118 244 ASP 119 245 SER 120 246 GLY 121 247 ASN 122 248 ILE 123 249 ASP 124 250 ALA 125 251 ALA 126 252 LYS 127 253 ASP 128 254 ILE 129 255 ILE 130 256 ARG 131 257 TYR 132 258 ILE 133 259 ILE 134 260 GLY 135 261 ILE 136 262 GLY 137 263 LYS 138 264 HIS 139 265 PHE 140 266 GLN 141 267 THR 142 268 LYS 143 269 GLU 144 270 SER 145 271 GLN 146 272 GLU 147 273 THR 148 274 LEU 149 275 HIS 150 276 LYS 151 277 PHE 152 278 ALA 153 279 SER 154 280 LYS 155 281 PRO 156 282 ALA 157 283 SER 158 284 GLU 159 285 PHE 160 286 VAL 161 287 LYS 162 288 ILE 163 289 LEU 164 290 ASP 165 291 THR 166 292 PHE 167 293 GLU 168 294 LYS 169 295 LEU 170 296 LYS 171 297 ASP 172 298 LEU 173 299 PHE 174 300 THR 175 301 GLU 176 302 LEU 177 303 GLN 178 304 LYS 179 305 LYS 180 306 ILE 181 307 TYR stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-06-02 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 4553 "Leukocyte Function Associated Antigen-1 Inserted-Domain" 99.45 189 99.44 99.44 6.70e-125 PDB 1CQP "Crystal Structure Analysis Of The Complex Lfa-1 (cd11a) I-domain / Lovastatin At 2.6 A Resolution" 99.45 182 99.44 99.44 1.21e-124 PDB 1DGQ "Nmr Solution Structure Of The Inserted Domain Of Human Leukocyte Function Associated Antigen-1" 99.45 188 99.44 99.44 1.12e-124 PDB 1LFA "Cd11a I-Domain With Bound Mn++" 99.45 187 100.00 100.00 7.25e-126 PDB 1MJN "Crystal Structure Of The Intermediate Affinity Al I Domain M" 98.90 179 98.88 98.88 2.42e-123 PDB 1MQ8 "Crystal Structure Of Alphal I Domain In Complex With Icam-1" 97.79 177 98.87 98.87 1.87e-121 PDB 1MQ9 "Crystal Structure Of High Affinity Alphal I Domain With Ligand Mimetic Crystal Contact" 99.45 180 98.89 98.89 4.92e-124 PDB 1MQA "Crystal Structure Of High Affinity Alphal I Domain In The Absence Of Ligand Or Metal" 99.45 180 98.89 98.89 4.92e-124 PDB 1RD4 "An Allosteric Inhibitor Of Lfa-1 Bound To Its I-Domain" 99.45 191 100.00 100.00 7.72e-126 PDB 1T0P "Structural Basis Of Icam Recognition By Integrin Alpahlbeta2 Revealed In The Complex Structure Of Binding Domains Of Icam-3 And" 96.69 175 98.29 98.29 2.52e-119 PDB 1XDD "X-ray Structure Of Lfa-1 I-domain In Complex With Lfa703 At 2.2a Resolution" 99.45 188 99.44 99.44 1.12e-124 PDB 1XDG "X-ray Structure Of Lfa-1 I-domain In Complex With Lfa878 At 2.1a Resolution" 99.45 188 99.44 99.44 1.12e-124 PDB 1XUO "X-ray Structure Of Lfa-1 I-domain Bound To A 1,4-diazepane- 2,5-dione Inhibitor At 1.8a Resolution" 99.45 188 99.44 99.44 1.12e-124 PDB 1ZON "Cd11a I-Domain Without Bound Cation" 99.45 187 100.00 100.00 7.25e-126 PDB 1ZOO "Cd11a I-Domain With Bound Magnesium Ion" 99.45 187 100.00 100.00 7.25e-126 PDB 1ZOP "Cd11a I-Domain With Bound Magnesium Ion" 99.45 187 100.00 100.00 7.25e-126 PDB 2ICA "Cd11a (Lfa1) I-Domain Complexed With Bms-587101 Aka 5-[(5s, 9r)-9-(4-Cyanophenyl)-3-(3,5-Dichlorophenyl)-1-Methyl-2,4- Dioxo-1," 98.90 183 100.00 100.00 1.00e-124 PDB 2O7N "Cd11a (Lfa1) I-Domain Complexed With 7a-[(4-Cyanophenyl) Methyl]-6-(3,5-Dichlorophenyl)-5-Oxo-2,3,5,7a-Tetrahydro- 1h-Pyrrolo[1" 98.90 183 100.00 100.00 1.00e-124 PDB 3BN3 "Crystal Structure Of Icam-5 In Complex With Al I Domain" 98.90 180 98.32 98.32 2.95e-121 PDB 3BQM "Lfa-1 I Domain Bound To Inhibitors" 99.45 182 99.44 99.44 1.21e-124 PDB 3BQN "Lfa-1 I Domain Bound To Inhibitors" 99.45 182 99.44 99.44 1.21e-124 PDB 3E2M "Lfa-1 I Domain Bound To Inhibitors" 99.45 185 99.44 99.44 1.01e-124 PDB 3EOA "Crystal Structure The Fab Fragment Of Efalizumab In Complex With Lfa-1 I Domain, Form I" 99.45 181 100.00 100.00 8.63e-126 PDB 3EOB "Crystal Structure The Fab Fragment Of Efalizumab In Complex With Lfa-1 I Domain, Form Ii" 99.45 181 100.00 100.00 8.63e-126 PDB 3F74 "Crystal Structure Of Wild Type Lfa1 I Domain" 100.00 181 99.45 99.45 1.17e-125 PDB 3F78 "Crystal Structure Of Wild Type Lfa1 I Domain Complexed With Isoflurane" 100.00 181 99.45 99.45 1.17e-125 PDB 3HI6 "Crystal Structure Of Intermediate Affinity I Domain Of Integrin Lfa-1 With The Fab Fragment Of Its Antibody Al-57" 99.45 180 98.33 98.33 2.68e-123 PDB 3M6F "Cd11a I-Domain Complexed With 6-((5s,9r)-9-(4-Cyanophenyl)-3 Dichlorophenyl)-1-Methyl-2,4-Dioxo-1,3,7- Triazaspiro[4.4]n Nicoti" 98.90 183 100.00 100.00 1.00e-124 PDB 3TCX "Structure Of Engineered Single Domain Icam-1 D1 With High-affinity Al Integrin I Domain Of Native C-terminal Helix Conformation" 98.90 180 98.88 98.88 1.38e-122 PDB 4IXD "X-ray Structure Of Lfa-1 I-domain In Complex With Ibe-667 At 1.8a Resolution" 99.45 188 99.44 99.44 1.12e-124 DBJ BAG36913 "unnamed protein product [Homo sapiens]" 99.45 1170 100.00 100.00 2.24e-118 EMBL CAA68747 "unnamed protein product [Homo sapiens]" 99.45 1170 99.44 99.44 3.85e-117 GB AAC31672 "leukocyte function-associated molecule-1 alpha subunit [Homo sapiens]" 99.45 1223 99.44 99.44 3.10e-117 GB AAQ14923 "leukocyte-associated molecule-1 alpha subunit [Pan troglodytes]" 99.45 1170 100.00 100.00 1.66e-118 GB AAZ38713 "integrin, alpha L (antigen CD11A (p180), lymphocyte function-associated antigen 1; alpha polypeptide) [Homo sapiens]" 99.45 1170 100.00 100.00 2.24e-118 GB EAW52244 "integrin, alpha L (antigen CD11A (p180), lymphocyte function-associated antigen 1; alpha polypeptide), isoform CRA_b [Homo sapi" 99.45 1223 100.00 100.00 1.63e-118 GB EAW52245 "integrin, alpha L (antigen CD11A (p180), lymphocyte function-associated antigen 1; alpha polypeptide), isoform CRA_c [Homo sapi" 99.45 1170 100.00 100.00 2.24e-118 REF NP_001029341 "integrin alpha-L [Pan troglodytes]" 99.45 1170 100.00 100.00 1.66e-118 REF NP_002200 "integrin alpha-L isoform a precursor [Homo sapiens]" 99.45 1170 100.00 100.00 2.24e-118 REF XP_001100800 "PREDICTED: integrin alpha-L [Macaca mulatta]" 99.45 843 97.78 99.44 7.70e-119 REF XP_004057549 "PREDICTED: integrin alpha-L isoform 1 [Gorilla gorilla gorilla]" 99.45 1170 100.00 100.00 1.66e-118 REF XP_005255370 "PREDICTED: integrin alpha-L isoform X1 [Homo sapiens]" 99.45 1169 100.00 100.00 2.21e-118 SP P20701 "RecName: Full=Integrin alpha-L; AltName: Full=CD11 antigen-like family member A; AltName: Full=Leukocyte adhesion glycoprotein " 99.45 1170 100.00 100.00 2.24e-118 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $LFA-1_I-domain Human 9606 Eukaryota Metazoa Homo sapiens stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Variant _Vector_name $LFA-1_I-domain 'recombinant technology' . Escherichia coli K12 BL21(DE3) pET11d stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $LFA-1_I-domain 700 uM '[U-13C; U-15N]' 'Sodium chloride' 137 mM 'natural abundance' 'sodium phosphate dibasic' 2.7 mM 'natural abundance' 'pottasium chloride' 2 mM 'natural abundance' 'pottasium sulfate monobasic' 2 mM 'natural abundance' 'Magnesium sulfate' 10 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_xwinnmr _Saveframe_category software _Name xwinnmr _Version . loop_ _Vendor _Address _Electronic_address bruker . . stop_ loop_ _Task processing stop_ _Details . save_ save_NMRpipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Frank Delaglio' . . stop_ loop_ _Task processing stop_ _Details . save_ save_NMRView _Saveframe_category software _Name NMRView _Version . loop_ _Vendor _Address _Electronic_address 'Bruce A Johnson' . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_3D_HNCO_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HN(CA)CO_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CA)CO' _Sample_label $sample_1 save_ save_3D_HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_(H)CC(CO)NH_6 _Saveframe_category NMR_applied_experiment _Experiment_name (H)CC(CO)NH _Sample_label $sample_1 save_ save_3D_HNHA_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNHA' _Sample_label $sample_1 save_ save_3D_1H-15N_NOESY_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $sample_1 save_ save_3D_1H-15N_TOCSY_9 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N TOCSY' _Sample_label $sample_1 save_ save_NMR_spectrometer_expt _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.4 . pH pressure 1 . atm temperature 295 . 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 internal indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1 DSS N 15 'methyl protons' ppm 0.00 internal 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-15N HSQC' '3D HNCO' '3D HN(CA)CO' '3D HNCACB' '3D CBCA(CO)NH' (H)CC(CO)NH '3D HNHA' '3D 1H-15N NOESY' '3D 1H-15N TOCSY' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'LFA-1 I-domain' _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 1 127 1 MET CA C 54.709 0.2 1 2 127 1 MET CB C 33.381 0.2 1 3 127 1 MET CG C 32.033 0.2 1 4 128 2 GLY H H 8.457 0.02 1 5 128 2 GLY CA C 44.941 0.2 1 6 128 2 GLY N N 109.679 0.1 1 7 129 3 ASN H H 8.544 0.02 1 8 129 3 ASN HA H 4.819 0.02 1 9 129 3 ASN CA C 53.543 0.2 1 10 129 3 ASN CB C 37.537 0.2 1 11 129 3 ASN N N 119.679 0.1 1 12 130 4 VAL H H 6.935 0.02 1 13 130 4 VAL CA C 61.469 0.2 1 14 130 4 VAL CB C 34.718 0.2 1 15 130 4 VAL N N 123.807 0.1 1 16 131 5 ASP H H 8.678 0.02 1 17 131 5 ASP HA H 4.729 0.02 1 18 131 5 ASP CA C 53.044 0.2 1 19 131 5 ASP CB C 41.279 0.2 1 20 131 5 ASP N N 131.286 0.1 1 21 132 6 LEU H H 8.592 0.02 1 22 132 6 LEU HA H 5.484 0.02 1 23 132 6 LEU CA C 54.417 0.2 1 24 132 6 LEU CB C 44.903 0.2 1 25 132 6 LEU CG C 27.741 0.2 1 26 132 6 LEU CD2 C 22.812 0.2 2 27 132 6 LEU N N 127.279 0.1 1 28 133 7 VAL H H 9.144 0.02 1 29 133 7 VAL HA H 4.665 0.02 1 30 133 7 VAL CA C 59.697 0.2 1 31 133 7 VAL CB C 34.589 0.2 1 32 133 7 VAL CG1 C 21.158 0.2 2 33 133 7 VAL CG2 C 24.801 0.2 2 34 133 7 VAL N N 124.440 0.1 1 35 134 8 PHE H H 8.663 0.02 1 36 134 8 PHE HA H 5.363 0.02 1 37 134 8 PHE CA C 55.769 0.2 1 38 134 8 PHE CB C 44.484 0.2 1 39 134 8 PHE N N 124.550 0.1 1 40 135 9 LEU H H 9.773 0.02 1 41 135 9 LEU HA H 5.797 0.02 1 42 135 9 LEU CA C 53.169 0.2 1 43 135 9 LEU CB C 45.691 0.2 1 44 135 9 LEU CG C 24.827 0.2 1 45 135 9 LEU N N 129.128 0.1 1 46 136 10 PHE H H 9.589 0.02 1 47 136 10 PHE HA H 5.887 0.02 1 48 136 10 PHE CA C 55.333 0.2 1 49 136 10 PHE CB C 43.485 0.2 1 50 136 10 PHE N N 122.550 0.1 1 51 137 11 ASP H H 7.935 0.02 1 52 137 11 ASP CA C 53.697 0.2 1 53 137 11 ASP CB C 44.661 0.2 1 54 137 11 ASP N N 127.545 0.1 1 55 138 12 GLY H H 8.379 0.02 1 56 138 12 GLY HA2 H 4.918 0.02 2 57 138 12 GLY CA C 51.970 0.2 1 58 138 12 GLY N N 110.550 0.1 1 59 139 13 SER H H 9.756 0.02 1 60 139 13 SER CA C 59.208 0.2 1 61 139 13 SER CB C 60.178 0.2 1 62 139 13 SER N N 116.418 0.1 1 63 140 14 MET H H 8.790 0.02 1 64 140 14 MET CA C 57.229 0.2 1 65 140 14 MET CB C 33.059 0.2 1 66 140 14 MET CG C 30.259 0.2 1 67 140 14 MET N N 116.353 0.1 1 68 141 15 SER H H 6.916 0.02 1 69 141 15 SER HA H 4.186 0.02 1 70 141 15 SER CA C 60.027 0.2 1 71 141 15 SER CB C 61.839 0.2 1 72 141 15 SER N N 110.515 0.1 1 73 142 16 LEU H H 6.980 0.02 1 74 142 16 LEU HA H 4.376 0.02 1 75 142 16 LEU CA C 55.658 0.2 1 76 142 16 LEU CB C 43.899 0.2 1 77 142 16 LEU CG C 28.391 0.2 1 78 142 16 LEU N N 124.535 0.1 1 79 143 17 GLN H H 8.966 0.02 1 80 143 17 GLN HA H 4.553 0.02 1 81 143 17 GLN CA C 53.774 0.2 1 82 143 17 GLN CB C 27.945 0.2 1 83 143 17 GLN N N 122.511 0.1 1 84 144 18 PRO CA C 66.754 0.2 1 85 144 18 PRO CB C 31.943 0.2 1 86 144 18 PRO CG C 28.176 0.2 1 87 144 18 PRO CD C 49.909 0.2 1 88 145 19 ASP H H 8.846 0.02 1 89 145 19 ASP HA H 4.369 0.02 1 90 145 19 ASP CA C 56.408 0.2 1 91 145 19 ASP CB C 40.150 0.2 1 92 145 19 ASP N N 114.146 0.1 1 93 146 20 GLU H H 6.898 0.02 1 94 146 20 GLU HA H 3.258 0.02 1 95 146 20 GLU CA C 58.904 0.2 1 96 146 20 GLU CB C 28.869 0.2 1 97 146 20 GLU CG C 36.808 0.2 1 98 146 20 GLU N N 121.688 0.1 1 99 147 21 PHE H H 7.867 0.02 1 100 147 21 PHE HA H 3.953 0.02 1 101 147 21 PHE CA C 62.144 0.2 1 102 147 21 PHE CB C 39.333 0.2 1 103 147 21 PHE N N 118.631 0.1 1 104 148 22 GLN H H 7.901 0.02 1 105 148 22 GLN HA H 3.653 0.02 1 106 148 22 GLN CA C 58.487 0.2 1 107 148 22 GLN CB C 28.381 0.2 1 108 148 22 GLN CG C 33.404 0.2 1 109 148 22 GLN N N 115.239 0.1 1 110 149 23 LYS H H 7.602 0.02 1 111 149 23 LYS HA H 4.036 0.02 1 112 149 23 LYS CA C 60.099 0.2 1 113 149 23 LYS CB C 32.478 0.2 1 114 149 23 LYS CD C 28.346 0.2 1 115 149 23 LYS CE C 42.572 0.2 1 116 149 23 LYS N N 118.379 0.1 1 117 150 24 ILE H H 7.621 0.02 1 118 150 24 ILE HA H 3.494 0.02 1 119 150 24 ILE HB H 2.037 0.02 1 120 150 24 ILE CA C 66.881 0.2 1 121 150 24 ILE CB C 37.390 0.2 1 122 150 24 ILE CG2 C 17.617 0.2 4 123 150 24 ILE N N 121.667 0.1 1 124 151 25 LEU H H 7.300 0.02 1 125 151 25 LEU HA H 3.455 0.02 1 126 151 25 LEU CA C 58.547 0.2 1 127 151 25 LEU CB C 40.844 0.2 1 128 151 25 LEU CD1 C 25.734 0.2 2 129 151 25 LEU CD2 C 23.237 0.2 2 130 151 25 LEU N N 119.485 0.1 1 131 152 26 ASP H H 8.785 0.02 1 132 152 26 ASP HA H 4.091 0.02 1 133 152 26 ASP CA C 57.462 0.2 1 134 152 26 ASP CB C 40.332 0.2 1 135 152 26 ASP N N 118.419 0.1 1 136 153 27 PHE H H 7.754 0.02 1 137 153 27 PHE HA H 4.359 0.02 1 138 153 27 PHE CA C 60.503 0.2 1 139 153 27 PHE CB C 39.384 0.2 1 140 153 27 PHE N N 122.000 0.1 1 141 154 28 MET H H 7.354 0.02 1 142 154 28 MET CA C 59.474 0.2 1 143 154 28 MET CB C 33.112 0.2 1 144 154 28 MET N N 117.681 0.1 1 145 155 29 LYS H H 7.752 0.02 1 146 155 29 LYS CA C 60.932 0.2 1 147 155 29 LYS CB C 32.806 0.2 1 148 155 29 LYS CG C 26.346 0.2 1 149 155 29 LYS CD C 30.069 0.2 1 150 155 29 LYS N N 115.779 0.1 1 151 156 30 ASP H H 7.922 0.02 1 152 156 30 ASP CA C 57.652 0.2 1 153 156 30 ASP CB C 41.387 0.2 1 154 156 30 ASP N N 119.203 0.1 1 155 157 31 VAL H H 7.708 0.02 1 156 157 31 VAL HA H 2.904 0.02 1 157 157 31 VAL CA C 66.878 0.2 1 158 157 31 VAL CB C 31.237 0.2 1 159 157 31 VAL N N 118.421 0.1 1 160 158 32 MET H H 7.382 0.02 1 161 158 32 MET CA C 59.929 0.2 1 162 158 32 MET CB C 34.513 0.2 1 163 158 32 MET CG C 32.190 0.2 1 164 158 32 MET N N 114.327 0.1 1 165 159 33 LYS H H 8.276 0.02 1 166 159 33 LYS CA C 60.258 0.2 1 167 159 33 LYS CB C 32.363 0.2 1 168 159 33 LYS CD C 27.958 0.2 1 169 159 33 LYS N N 119.264 0.1 1 170 160 34 LYS H H 7.942 0.02 1 171 160 34 LYS HA H 3.999 0.02 1 172 160 34 LYS CA C 58.890 0.2 1 173 160 34 LYS CB C 32.689 0.2 1 174 160 34 LYS CD C 28.542 0.2 1 175 160 34 LYS N N 119.902 0.1 1 176 161 35 LEU H H 7.604 0.02 1 177 161 35 LEU CA C 53.838 0.2 1 178 161 35 LEU CB C 41.032 0.2 1 179 161 35 LEU CD1 C 25.170 0.2 2 180 161 35 LEU N N 118.753 0.1 1 181 162 36 SER H H 7.317 0.02 1 182 162 36 SER HA H 4.371 0.02 1 183 162 36 SER CB C 63.855 0.2 1 184 162 36 SER N N 116.963 0.1 1 185 163 37 ASN H H 8.877 0.02 1 186 163 37 ASN CA C 53.400 0.2 1 187 163 37 ASN CB C 37.893 0.2 1 188 163 37 ASN N N 120.350 0.1 1 189 164 38 THR H H 8.013 0.02 1 190 164 38 THR CA C 66.755 0.2 1 191 164 38 THR N N 109.988 0.1 1 192 165 39 SER H H 8.621 0.02 1 193 165 39 SER CA C 59.120 0.2 1 194 165 39 SER CB C 63.101 0.2 1 195 165 39 SER N N 114.029 0.1 1 196 166 40 TYR H H 8.462 0.02 1 197 166 40 TYR CA C 59.021 0.2 1 198 166 40 TYR CB C 40.077 0.2 1 199 166 40 TYR N N 124.322 0.1 1 200 167 41 GLN H H 8.181 0.02 1 201 167 41 GLN HA H 4.443 0.02 1 202 167 41 GLN CA C 55.422 0.2 1 203 167 41 GLN CB C 32.562 0.2 1 204 167 41 GLN CG C 34.429 0.2 1 205 167 41 GLN N N 116.424 0.1 1 206 168 42 PHE H H 5.465 0.02 1 207 168 42 PHE HA H 6.276 0.02 1 208 168 42 PHE CA C 57.307 0.2 1 209 168 42 PHE CB C 45.439 0.2 1 210 168 42 PHE N N 116.518 0.1 1 211 169 43 ALA H H 8.033 0.02 1 212 169 43 ALA HA H 3.913 0.02 1 213 169 43 ALA CA C 50.745 0.2 1 214 169 43 ALA CB C 21.829 0.2 1 215 169 43 ALA N N 117.410 0.1 1 216 170 44 ALA H H 7.432 0.02 1 217 170 44 ALA HA H 5.668 0.02 1 218 170 44 ALA CA C 51.197 0.2 1 219 170 44 ALA CB C 24.181 0.2 1 220 170 44 ALA N N 117.220 0.1 1 221 171 45 VAL H H 9.619 0.02 1 222 171 45 VAL HA H 4.977 0.02 1 223 171 45 VAL CA C 60.015 0.2 1 224 171 45 VAL CB C 36.519 0.2 1 225 171 45 VAL N N 123.979 0.1 1 226 172 46 GLN H H 8.767 0.02 1 227 172 46 GLN HA H 3.953 0.02 1 228 172 46 GLN CA C 53.708 0.2 1 229 172 46 GLN CB C 30.538 0.2 1 230 172 46 GLN CG C 35.546 0.2 1 231 172 46 GLN N N 128.546 0.1 1 232 173 47 PHE H H 8.855 0.02 1 233 173 47 PHE HA H 5.663 0.02 1 234 173 47 PHE CA C 54.405 0.2 1 235 173 47 PHE CB C 45.888 0.2 1 236 173 47 PHE N N 123.704 0.1 1 237 174 48 SER H H 8.374 0.02 1 238 174 48 SER CA C 58.773 0.2 1 239 174 48 SER CB C 62.599 0.2 1 240 174 48 SER N N 116.393 0.1 1 241 175 49 THR H H 7.727 0.02 1 242 175 49 THR HA H 4.440 0.02 1 243 175 49 THR CA C 65.369 0.2 1 244 175 49 THR CB C 68.546 0.2 1 245 175 49 THR N N 123.154 0.1 1 246 176 50 SER H H 8.945 0.02 1 247 176 50 SER HA H 3.465 0.02 1 248 176 50 SER CA C 54.928 0.2 1 249 176 50 SER CB C 63.703 0.2 1 250 176 50 SER N N 117.788 0.1 1 251 177 51 TYR H H 7.196 0.02 1 252 177 51 TYR HA H 5.190 0.02 1 253 177 51 TYR CA C 54.646 0.2 1 254 177 51 TYR CB C 39.009 0.2 1 255 177 51 TYR N N 118.845 0.1 1 256 178 52 LYS H H 8.692 0.02 1 257 178 52 LYS HA H 4.554 0.02 1 258 178 52 LYS CA C 55.296 0.2 1 259 178 52 LYS CB C 38.301 0.2 1 260 178 52 LYS CD C 29.602 0.2 1 261 178 52 LYS CE C 42.612 0.2 1 262 178 52 LYS N N 124.006 0.1 1 263 179 53 THR H H 9.532 0.02 1 264 179 53 THR HA H 4.389 0.02 1 265 179 53 THR CA C 64.118 0.2 1 266 179 53 THR CB C 68.031 0.2 1 267 179 53 THR N N 126.435 0.1 1 268 180 54 GLU H H 9.467 0.02 1 269 180 54 GLU HA H 5.050 0.02 1 270 180 54 GLU CA C 57.450 0.2 1 271 180 54 GLU CB C 29.039 0.2 1 272 180 54 GLU CG C 33.936 0.2 1 273 180 54 GLU N N 133.187 0.1 1 274 181 55 PHE H H 7.451 0.02 1 275 181 55 PHE HA H 4.906 0.02 1 276 181 55 PHE CA C 58.438 0.2 1 277 181 55 PHE CB C 40.319 0.2 1 278 181 55 PHE N N 110.821 0.1 1 279 182 56 ASP H H 9.568 0.02 1 280 182 56 ASP HA H 4.847 0.02 1 281 182 56 ASP N N 122.226 0.1 1 282 183 57 PHE CA C 60.895 0.2 1 283 183 57 PHE CB C 50.225 0.2 1 284 184 58 SER H H 8.370 0.02 1 285 184 58 SER HA H 4.318 0.02 1 286 184 58 SER CA C 61.058 0.2 1 287 184 58 SER CB C 62.699 0.2 1 288 184 58 SER N N 113.632 0.1 1 289 185 59 ASP H H 8.222 0.02 1 290 185 59 ASP HA H 4.560 0.02 1 291 185 59 ASP CA C 57.602 0.2 1 292 185 59 ASP CB C 41.979 0.2 1 293 185 59 ASP N N 123.224 0.1 1 294 186 60 TYR H H 8.372 0.02 1 295 186 60 TYR HA H 4.072 0.02 1 296 186 60 TYR CA C 62.493 0.2 1 297 186 60 TYR CB C 39.049 0.2 1 298 186 60 TYR N N 120.311 0.1 1 299 187 61 VAL H H 8.360 0.02 1 300 187 61 VAL HA H 3.474 0.02 1 301 187 61 VAL CA C 66.337 0.2 1 302 187 61 VAL CB C 32.060 0.2 1 303 187 61 VAL N N 115.570 0.1 1 304 188 62 LYS H H 7.593 0.02 1 305 188 62 LYS HA H 4.128 0.02 1 306 188 62 LYS CA C 59.058 0.2 1 307 188 62 LYS CB C 33.560 0.2 1 308 188 62 LYS CG C 25.587 0.2 1 309 188 62 LYS CE C 42.350 0.2 1 310 188 62 LYS N N 117.188 0.1 1 311 189 63 ARG H H 7.949 0.02 1 312 189 63 ARG HA H 4.303 0.02 1 313 189 63 ARG CA C 56.821 0.2 1 314 189 63 ARG CB C 31.780 0.2 1 315 189 63 ARG CG C 27.416 0.2 1 316 189 63 ARG CD C 43.385 0.2 1 317 189 63 ARG N N 117.894 0.1 1 318 190 64 LYS H H 8.409 0.02 1 319 190 64 LYS HA H 3.524 0.02 1 320 190 64 LYS CA C 57.795 0.2 1 321 190 64 LYS CB C 31.115 0.2 1 322 190 64 LYS CG C 24.978 0.2 1 323 190 64 LYS CD C 29.629 0.2 1 324 190 64 LYS CE C 42.549 0.2 1 325 190 64 LYS N N 120.260 0.1 1 326 191 65 ASP H H 7.454 0.02 1 327 191 65 ASP HA H 4.896 0.02 1 328 191 65 ASP CA C 51.001 0.2 1 329 191 65 ASP N N 118.496 0.1 1 330 192 66 PRO CA C 65.324 0.2 1 331 192 66 PRO CB C 33.095 0.2 1 332 192 66 PRO CG C 28.609 0.2 1 333 192 66 PRO CD C 50.441 0.2 1 334 193 67 ASP H H 7.726 0.02 1 335 193 67 ASP HA H 4.080 0.02 1 336 193 67 ASP HB2 H 2.685 0.02 2 337 193 67 ASP CA C 57.149 0.2 1 338 193 67 ASP CB C 40.321 0.2 1 339 193 67 ASP N N 113.393 0.1 1 340 194 68 ALA H H 7.333 0.02 1 341 194 68 ALA HA H 4.015 0.02 1 342 194 68 ALA CA C 54.326 0.2 1 343 194 68 ALA CB C 18.577 0.2 1 344 194 68 ALA N N 121.784 0.1 1 345 195 69 LEU H H 7.970 0.02 1 346 195 69 LEU CA C 57.363 0.2 1 347 195 69 LEU CB C 42.090 0.2 1 348 195 69 LEU CG C 26.521 0.2 1 349 195 69 LEU CD2 C 21.827 0.2 2 350 195 69 LEU N N 116.952 0.1 1 351 196 70 LEU H H 6.881 0.02 1 352 196 70 LEU HA H 4.708 0.02 1 353 196 70 LEU CA C 53.765 0.2 1 354 196 70 LEU CB C 42.080 0.2 1 355 196 70 LEU CD2 C 22.925 0.2 2 356 196 70 LEU N N 113.979 0.1 1 357 197 71 LYS H H 6.999 0.02 1 358 197 71 LYS HA H 3.919 0.02 1 359 197 71 LYS CA C 59.200 0.2 1 360 197 71 LYS CB C 33.090 0.2 1 361 197 71 LYS CG C 23.868 0.2 1 362 197 71 LYS CD C 29.316 0.2 1 363 197 71 LYS CE C 42.133 0.2 1 364 197 71 LYS N N 120.638 0.1 1 365 198 72 HIS H H 8.660 0.02 1 366 198 72 HIS HA H 4.763 0.02 1 367 198 72 HIS CA C 55.604 0.2 1 368 198 72 HIS CB C 30.471 0.2 1 369 198 72 HIS N N 115.466 0.1 1 370 199 73 VAL H H 6.997 0.02 1 371 199 73 VAL HA H 3.712 0.02 1 372 199 73 VAL HB H 2.019 0.02 1 373 199 73 VAL CA C 64.438 0.2 1 374 199 73 VAL CB C 32.282 0.2 1 375 199 73 VAL N N 121.795 0.1 1 376 200 74 LYS H H 9.578 0.02 1 377 200 74 LYS HA H 4.711 0.02 1 378 200 74 LYS HG2 H 1.488 0.02 2 379 200 74 LYS CA C 54.533 0.2 1 380 200 74 LYS CB C 23.132 0.2 1 381 200 74 LYS CG C 24.444 0.2 1 382 200 74 LYS CD C 29.074 0.2 1 383 200 74 LYS CE C 42.286 0.2 1 384 200 74 LYS N N 130.550 0.1 1 385 201 75 HIS H H 8.643 0.02 1 386 201 75 HIS CA C 55.102 0.2 1 387 201 75 HIS CB C 32.429 0.2 1 388 201 75 HIS N N 129.619 0.1 1 389 202 76 MET H H 9.377 0.02 1 390 202 76 MET CA C 61.035 0.2 1 391 202 76 MET CB C 36.463 0.2 1 392 202 76 MET N N 130.749 0.1 1 393 203 77 LEU H H 8.435 0.02 1 394 203 77 LEU HA H 5.683 0.02 1 395 203 77 LEU CA C 55.793 0.2 1 396 203 77 LEU CB C 39.465 0.2 1 397 203 77 LEU CD1 C 25.618 0.2 2 398 203 77 LEU N N 113.141 0.1 1 399 204 78 LEU H H 7.024 0.02 1 400 204 78 LEU HA H 4.888 0.02 1 401 204 78 LEU CA C 55.227 0.2 1 402 204 78 LEU CB C 43.267 0.2 1 403 204 78 LEU CD1 C 26.756 0.2 2 404 204 78 LEU CD2 C 23.088 0.2 2 405 204 78 LEU N N 120.958 0.1 1 406 205 79 LEU H H 7.305 0.02 1 407 205 79 LEU HA H 4.573 0.02 1 408 205 79 LEU CA C 55.086 0.2 1 409 205 79 LEU CB C 39.577 0.2 1 410 205 79 LEU CG C 25.687 0.2 1 411 205 79 LEU N N 121.468 0.1 1 412 206 80 THR H H 7.851 0.02 1 413 206 80 THR HA H 4.362 0.02 1 414 206 80 THR CA C 60.484 0.2 1 415 206 80 THR CB C 69.984 0.2 1 416 206 80 THR N N 117.592 0.1 1 417 207 81 ASN H H 9.191 0.02 1 418 207 81 ASN HA H 5.283 0.02 1 419 207 81 ASN CA C 52.965 0.2 1 420 207 81 ASN CB C 36.605 0.2 1 421 207 81 ASN N N 128.547 0.1 1 422 208 82 THR H H 8.732 0.02 1 423 208 82 THR CA C 66.665 0.2 1 424 208 82 THR CB C 68.579 0.2 1 425 208 82 THR N N 119.700 0.1 1 426 209 83 PHE H H 10.489 0.02 1 427 209 83 PHE CA C 64.660 0.2 1 428 209 83 PHE CB C 38.099 0.2 1 429 209 83 PHE N N 122.004 0.1 1 430 210 84 GLY H H 10.305 0.02 1 431 210 84 GLY CA C 46.569 0.2 1 432 210 84 GLY N N 110.934 0.1 1 433 211 85 ALA H H 8.010 0.02 1 434 211 85 ALA HA H 2.819 0.02 1 435 211 85 ALA CA C 54.333 0.2 1 436 211 85 ALA CB C 20.865 0.2 1 437 211 85 ALA N N 125.486 0.1 1 438 212 86 ILE H H 7.931 0.02 1 439 212 86 ILE CA C 66.375 0.2 1 440 212 86 ILE CB C 37.876 0.2 1 441 212 86 ILE N N 119.431 0.1 1 442 213 87 ASN H H 7.636 0.02 1 443 213 87 ASN HA H 4.212 0.02 1 444 213 87 ASN CA C 58.057 0.2 1 445 213 87 ASN CB C 39.477 0.2 1 446 213 87 ASN N N 117.619 0.1 1 447 214 88 TYR H H 8.182 0.02 1 448 214 88 TYR HA H 3.988 0.02 1 449 214 88 TYR CA C 61.485 0.2 1 450 214 88 TYR CB C 38.322 0.2 1 451 214 88 TYR N N 122.260 0.1 1 452 215 89 VAL H H 8.191 0.02 1 453 215 89 VAL CA C 66.582 0.2 1 454 215 89 VAL CB C 31.453 0.2 1 455 215 89 VAL CG1 C 23.809 0.2 2 456 215 89 VAL CG2 C 24.751 0.2 2 457 215 89 VAL N N 120.001 0.1 1 458 216 90 ALA H H 8.133 0.02 1 459 216 90 ALA HA H 4.167 0.02 1 460 216 90 ALA CA C 55.528 0.2 1 461 216 90 ALA CB C 18.690 0.2 1 462 216 90 ALA N N 118.600 0.1 1 463 217 91 THR H H 7.806 0.02 1 464 217 91 THR HA H 4.397 0.02 1 465 217 91 THR CA C 63.250 0.2 1 466 217 91 THR CB C 70.270 0.2 1 467 217 91 THR N N 104.606 0.1 1 468 218 92 GLU H H 8.571 0.02 1 469 218 92 GLU HA H 4.467 0.02 1 470 218 92 GLU CA C 55.879 0.2 1 471 218 92 GLU CB C 38.445 0.2 1 472 218 92 GLU CG C 35.304 0.2 1 473 218 92 GLU N N 117.583 0.1 1 474 219 93 VAL H H 7.128 0.02 1 475 219 93 VAL HA H 4.150 0.02 1 476 219 93 VAL HB H 2.147 0.02 1 477 219 93 VAL CA C 64.511 0.2 1 478 219 93 VAL CB C 32.326 0.2 1 479 219 93 VAL CG1 C 21.626 0.2 2 480 219 93 VAL CG2 C 23.610 0.2 2 481 219 93 VAL N N 117.886 0.1 1 482 220 94 PHE H H 7.137 0.02 1 483 220 94 PHE HA H 4.625 0.02 1 484 220 94 PHE CA C 58.939 0.2 1 485 220 94 PHE CB C 37.326 0.2 1 486 220 94 PHE N N 118.425 0.1 1 487 221 95 ARG H H 7.716 0.02 1 488 221 95 ARG HA H 4.710 0.02 1 489 221 95 ARG CA C 54.099 0.2 1 490 221 95 ARG CB C 33.453 0.2 1 491 221 95 ARG N N 120.957 0.1 1 492 222 96 GLU H H 9.601 0.02 1 493 222 96 GLU CA C 59.560 0.2 1 494 222 96 GLU CB C 29.771 0.2 1 495 222 96 GLU CG C 36.553 0.2 1 496 222 96 GLU N N 130.017 0.1 1 497 223 97 GLU H H 10.261 0.02 1 498 223 97 GLU CA C 59.532 0.2 1 499 223 97 GLU CB C 28.573 0.2 1 500 223 97 GLU CG C 36.625 0.2 1 501 223 97 GLU N N 120.208 0.1 1 502 224 98 LEU H H 7.412 0.02 1 503 224 98 LEU HA H 4.706 0.02 1 504 224 98 LEU HB2 H 1.911 0.02 2 505 224 98 LEU CA C 54.404 0.2 1 506 224 98 LEU CB C 42.037 0.2 1 507 224 98 LEU CG C 28.041 0.2 1 508 224 98 LEU CD1 C 26.153 0.2 2 509 224 98 LEU CD2 C 22.470 0.2 2 510 224 98 LEU N N 118.735 0.1 1 511 225 99 GLY H H 7.896 0.02 1 512 225 99 GLY HA2 H 3.764 0.02 2 513 225 99 GLY CA C 45.530 0.2 1 514 225 99 GLY N N 104.180 0.1 1 515 226 100 ALA H H 7.588 0.02 1 516 226 100 ALA HA H 3.443 0.02 1 517 226 100 ALA CA C 52.624 0.2 1 518 226 100 ALA CB C 18.723 0.2 1 519 226 100 ALA N N 124.534 0.1 1 520 227 101 ARG H H 10.178 0.02 1 521 227 101 ARG HA H 4.627 0.02 1 522 227 101 ARG CA C 53.445 0.2 1 523 227 101 ARG CB C 30.654 0.2 1 524 227 101 ARG N N 126.271 0.1 1 525 228 102 PRO CA C 64.749 0.2 1 526 228 102 PRO CB C 31.973 0.2 1 527 228 102 PRO CG C 27.499 0.2 1 528 228 102 PRO CD C 50.969 0.2 1 529 229 103 ASP H H 8.227 0.02 1 530 229 103 ASP HA H 4.534 0.02 1 531 229 103 ASP CA C 53.291 0.2 1 532 229 103 ASP CB C 40.275 0.2 1 533 229 103 ASP N N 114.030 0.1 1 534 230 104 ALA H H 7.261 0.02 1 535 230 104 ALA HA H 4.175 0.02 1 536 230 104 ALA CA C 51.808 0.2 1 537 230 104 ALA CB C 20.647 0.2 1 538 230 104 ALA N N 121.884 0.1 1 539 231 105 THR H H 8.324 0.02 1 540 231 105 THR HA H 4.031 0.02 1 541 231 105 THR HB H 3.872 0.02 1 542 231 105 THR CA C 64.289 0.2 1 543 231 105 THR CB C 69.589 0.2 1 544 231 105 THR N N 119.890 0.1 1 545 232 106 LYS H H 8.422 0.02 1 546 232 106 LYS CA C 56.212 0.2 1 547 232 106 LYS CB C 34.228 0.2 1 548 232 106 LYS CG C 24.228 0.2 1 549 232 106 LYS CD C 29.365 0.2 1 550 232 106 LYS N N 128.334 0.1 1 551 233 107 VAL H H 8.912 0.02 1 552 233 107 VAL HA H 4.988 0.02 1 553 233 107 VAL CA C 61.021 0.2 1 554 233 107 VAL CB C 35.736 0.2 1 555 233 107 VAL N N 124.530 0.1 1 556 234 108 LEU H H 9.798 0.02 1 557 234 108 LEU HA H 5.456 0.02 1 558 234 108 LEU CA C 53.139 0.2 1 559 234 108 LEU CB C 48.249 0.2 1 560 234 108 LEU CG C 24.272 0.2 1 561 234 108 LEU N N 130.072 0.1 1 562 235 109 ILE H H 9.042 0.02 1 563 235 109 ILE HA H 5.092 0.02 1 564 235 109 ILE CA C 60.620 0.2 1 565 235 109 ILE CB C 39.124 0.2 1 566 235 109 ILE CG2 C 17.406 0.2 4 567 235 109 ILE N N 124.009 0.1 1 568 236 110 ILE H H 9.281 0.02 1 569 236 110 ILE HA H 5.488 0.02 1 570 236 110 ILE CA C 60.614 0.2 1 571 236 110 ILE CB C 39.267 0.2 1 572 236 110 ILE CG1 C 28.586 0.2 4 573 236 110 ILE CG2 C 16.608 0.2 4 574 236 110 ILE N N 128.550 0.1 1 575 237 111 ILE H H 9.163 0.02 1 576 237 111 ILE HA H 5.194 0.02 1 577 237 111 ILE CA C 61.005 0.2 1 578 237 111 ILE CB C 41.228 0.2 1 579 237 111 ILE CG1 C 28.815 0.2 4 580 237 111 ILE CG2 C 19.708 0.2 4 581 237 111 ILE N N 127.596 0.1 1 582 238 112 THR H H 9.437 0.02 1 583 238 112 THR HA H 5.663 0.02 1 584 238 112 THR CA C 59.846 0.2 1 585 238 112 THR CB C 71.366 0.2 1 586 238 112 THR N N 120.108 0.1 1 587 239 113 ASP H H 8.638 0.02 1 588 239 113 ASP CA C 51.902 0.2 1 589 239 113 ASP CB C 44.278 0.2 1 590 239 113 ASP N N 126.297 0.1 1 591 240 114 GLY H H 8.366 0.02 1 592 240 114 GLY CA C 46.160 0.2 1 593 240 114 GLY N N 114.029 0.1 1 594 241 115 GLU H H 8.158 0.02 1 595 241 115 GLU HA H 4.357 0.02 1 596 241 115 GLU CA C 56.592 0.2 1 597 241 115 GLU CB C 39.601 0.2 1 598 241 115 GLU CG C 37.477 0.2 1 599 241 115 GLU N N 116.094 0.1 1 600 242 116 ALA H H 8.603 0.02 1 601 242 116 ALA HA H 5.241 0.02 1 602 242 116 ALA CA C 52.871 0.2 1 603 242 116 ALA CB C 20.729 0.2 1 604 242 116 ALA N N 122.419 0.1 1 605 243 117 THR H H 9.296 0.02 1 606 243 117 THR HA H 4.553 0.02 1 607 243 117 THR CA C 61.270 0.2 1 608 243 117 THR CB C 69.959 0.2 1 609 243 117 THR N N 111.060 0.1 1 610 244 118 ASP H H 8.428 0.02 1 611 244 118 ASP HA H 4.945 0.02 1 612 244 118 ASP CA C 51.970 0.2 1 613 244 118 ASP CB C 40.993 0.2 1 614 244 118 ASP N N 123.150 0.1 1 615 245 119 SER H H 7.503 0.02 1 616 245 119 SER HA H 3.926 0.02 1 617 245 119 SER CA C 57.197 0.2 1 618 245 119 SER CB C 64.753 0.2 1 619 245 119 SER N N 109.250 0.1 1 620 246 120 GLY H H 6.743 0.02 1 621 246 120 GLY CA C 44.936 0.2 1 622 246 120 GLY N N 105.971 0.1 1 623 247 121 ASN H H 8.737 0.02 1 624 247 121 ASN HA H 5.054 0.02 1 625 247 121 ASN CA C 52.446 0.2 1 626 247 121 ASN CB C 42.294 0.2 1 627 247 121 ASN N N 119.917 0.1 1 628 248 122 ILE H H 9.003 0.02 1 629 248 122 ILE CA C 60.568 0.2 1 630 248 122 ILE CB C 38.859 0.2 1 631 248 122 ILE N N 114.177 0.1 1 632 249 123 ASP H H 8.966 0.02 1 633 249 123 ASP HA H 4.255 0.02 1 634 249 123 ASP CA C 58.334 0.2 1 635 249 123 ASP CB C 39.895 0.2 1 636 249 123 ASP N N 126.648 0.1 1 637 250 124 ALA H H 9.056 0.02 1 638 250 124 ALA HA H 4.164 0.02 1 639 250 124 ALA CA C 54.002 0.2 1 640 250 124 ALA CB C 18.219 0.2 1 641 250 124 ALA N N 119.790 0.1 1 642 251 125 ALA H H 8.052 0.02 1 643 251 125 ALA HA H 4.457 0.02 1 644 251 125 ALA CA C 50.277 0.2 1 645 251 125 ALA CB C 20.038 0.2 1 646 251 125 ALA N N 117.926 0.1 1 647 252 126 LYS H H 7.280 0.02 1 648 252 126 LYS CA C 59.836 0.2 1 649 252 126 LYS CB C 32.436 0.2 1 650 252 126 LYS CG C 23.986 0.2 1 651 252 126 LYS CD C 29.427 0.2 1 652 252 126 LYS CE C 42.077 0.2 1 653 252 126 LYS N N 118.622 0.1 1 654 253 127 ASP H H 8.528 0.02 1 655 253 127 ASP HA H 4.650 0.02 1 656 253 127 ASP HB2 H 2.543 0.02 2 657 253 127 ASP CA C 54.651 0.2 1 658 253 127 ASP CB C 40.239 0.2 1 659 253 127 ASP N N 117.304 0.1 1 660 254 128 ILE H H 7.539 0.02 1 661 254 128 ILE HA H 3.794 0.02 1 662 254 128 ILE HB H 1.683 0.02 1 663 254 128 ILE CA C 60.814 0.2 1 664 254 128 ILE CB C 40.076 0.2 1 665 254 128 ILE CG1 C 27.430 0.2 4 666 254 128 ILE CG2 C 18.431 0.2 4 667 254 128 ILE N N 121.589 0.1 1 668 255 129 ILE H H 8.498 0.02 1 669 255 129 ILE HA H 3.705 0.02 1 670 255 129 ILE CA C 58.425 0.2 1 671 255 129 ILE CB C 37.838 0.2 1 672 255 129 ILE CG1 C 27.788 0.2 4 673 255 129 ILE CG2 C 18.313 0.2 4 674 255 129 ILE N N 130.854 0.1 1 675 256 130 ARG H H 8.942 0.02 1 676 256 130 ARG CA C 59.129 0.2 1 677 256 130 ARG CB C 31.798 0.2 1 678 256 130 ARG N N 128.656 0.1 1 679 257 131 TYR H H 9.043 0.02 1 680 257 131 TYR CA C 57.139 0.2 1 681 257 131 TYR CB C 42.497 0.2 1 682 257 131 TYR N N 124.319 0.1 1 683 258 132 ILE H H 9.231 0.02 1 684 258 132 ILE CA C 58.822 0.2 1 685 258 132 ILE CB C 41.377 0.2 1 686 258 132 ILE CG2 C 19.384 0.2 4 687 258 132 ILE N N 123.591 0.1 1 688 259 133 ILE H H 9.421 0.02 1 689 259 133 ILE HA H 4.966 0.02 1 690 259 133 ILE CA C 59.204 0.2 1 691 259 133 ILE CB C 39.472 0.2 1 692 259 133 ILE CG1 C 27.736 0.2 4 693 259 133 ILE N N 128.303 0.1 1 694 260 134 GLY H H 8.822 0.02 1 695 260 134 GLY CA C 44.386 0.2 1 696 260 134 GLY N N 113.673 0.1 1 697 261 135 ILE H H 8.484 0.02 1 698 261 135 ILE HA H 4.975 0.02 1 699 261 135 ILE CA C 59.877 0.2 1 700 261 135 ILE CB C 41.935 0.2 1 701 261 135 ILE N N 122.419 0.1 1 702 262 136 GLY H H 8.326 0.02 1 703 262 136 GLY HA2 H 3.871 0.02 2 704 262 136 GLY CA C 45.197 0.2 1 705 262 136 GLY N N 110.317 0.1 1 706 263 137 LYS H H 8.838 0.02 1 707 263 137 LYS CA C 58.872 0.2 1 708 263 137 LYS CB C 32.224 0.2 1 709 263 137 LYS CG C 23.647 0.2 1 710 263 137 LYS CD C 29.196 0.2 1 711 263 137 LYS CE C 42.109 0.2 1 712 263 137 LYS N N 119.047 0.1 1 713 264 138 HIS H H 9.135 0.02 1 714 264 138 HIS HA H 4.359 0.02 1 715 264 138 HIS CA C 58.702 0.2 1 716 264 138 HIS CB C 28.900 0.2 1 717 264 138 HIS N N 119.175 0.1 1 718 265 139 PHE H H 7.683 0.02 1 719 265 139 PHE HA H 5.612 0.02 1 720 265 139 PHE CA C 57.437 0.2 1 721 265 139 PHE CB C 38.958 0.2 1 722 265 139 PHE N N 116.627 0.1 1 723 266 140 GLN H H 7.444 0.02 1 724 266 140 GLN HA H 4.160 0.02 1 725 266 140 GLN HG2 H 2.489 0.02 2 726 266 140 GLN CA C 58.620 0.2 1 727 266 140 GLN CB C 29.708 0.2 1 728 266 140 GLN CG C 32.859 0.2 1 729 266 140 GLN N N 117.675 0.1 1 730 267 141 THR H H 8.071 0.02 1 731 267 141 THR HA H 4.569 0.02 1 732 267 141 THR CA C 59.999 0.2 1 733 267 141 THR CB C 71.230 0.2 1 734 267 141 THR N N 107.604 0.1 1 735 268 142 LYS H H 9.243 0.02 1 736 268 142 LYS CA C 59.633 0.2 1 737 268 142 LYS CB C 32.207 0.2 1 738 268 142 LYS CG C 24.436 0.2 1 739 268 142 LYS CD C 29.248 0.2 1 740 268 142 LYS CE C 42.193 0.2 1 741 268 142 LYS N N 125.369 0.1 1 742 269 143 GLU H H 9.154 0.02 1 743 269 143 GLU HA H 4.003 0.02 1 744 269 143 GLU CA C 61.112 0.2 1 745 269 143 GLU CB C 28.582 0.2 1 746 269 143 GLU CG C 37.092 0.2 1 747 269 143 GLU N N 117.321 0.1 1 748 270 144 SER H H 7.864 0.02 1 749 270 144 SER HA H 4.335 0.02 1 750 270 144 SER CA C 61.284 0.2 1 751 270 144 SER CB C 63.062 0.2 1 752 270 144 SER N N 115.894 0.1 1 753 271 145 GLN H H 7.689 0.02 1 754 271 145 GLN HA H 3.797 0.02 1 755 271 145 GLN CA C 59.442 0.2 1 756 271 145 GLN CB C 27.332 0.2 1 757 271 145 GLN CG C 33.936 0.2 1 758 271 145 GLN N N 124.274 0.1 1 759 272 146 GLU H H 7.901 0.02 1 760 272 146 GLU CA C 58.607 0.2 1 761 272 146 GLU CB C 28.764 0.2 1 762 272 146 GLU CG C 37.380 0.2 1 763 272 146 GLU N N 115.240 0.1 1 764 273 147 THR H H 7.593 0.02 1 765 273 147 THR HA H 4.167 0.02 1 766 273 147 THR CA C 65.561 0.2 1 767 273 147 THR CB C 69.201 0.2 1 768 273 147 THR N N 111.676 0.1 1 769 274 148 LEU H H 7.432 0.02 1 770 274 148 LEU CA C 55.504 0.2 1 771 274 148 LEU CB C 41.463 0.2 1 772 274 148 LEU CD1 C 24.474 0.2 2 773 274 148 LEU CD2 C 20.783 0.2 2 774 274 148 LEU N N 117.223 0.1 1 775 275 149 HIS H H 7.804 0.02 1 776 275 149 HIS HA H 4.109 0.02 1 777 275 149 HIS CA C 58.844 0.2 1 778 275 149 HIS CB C 30.710 0.2 1 779 275 149 HIS N N 117.468 0.1 1 780 276 150 LYS H H 7.648 0.02 1 781 276 150 LYS HA H 4.109 0.02 1 782 276 150 LYS CA C 57.712 0.2 1 783 276 150 LYS CB C 39.352 0.2 1 784 276 150 LYS CG C 22.252 0.2 1 785 276 150 LYS CD C 29.462 0.2 1 786 276 150 LYS N N 114.311 0.1 1 787 277 151 PHE H H 7.083 0.02 1 788 277 151 PHE HA H 4.509 0.02 1 789 277 151 PHE CA C 57.338 0.2 1 790 277 151 PHE CB C 39.772 0.2 1 791 277 151 PHE N N 116.398 0.1 1 792 278 152 ALA H H 6.997 0.02 1 793 278 152 ALA HA H 4.204 0.02 1 794 278 152 ALA CA C 51.778 0.2 1 795 278 152 ALA CB C 22.986 0.2 1 796 278 152 ALA N N 121.374 0.1 1 797 279 153 SER H H 8.282 0.02 1 798 279 153 SER HA H 4.076 0.02 1 799 279 153 SER CA C 61.639 0.2 1 800 279 153 SER N N 118.834 0.1 1 801 280 154 LYS H H 7.745 0.02 1 802 280 154 LYS HA H 4.576 0.02 1 803 280 154 LYS CA C 53.533 0.2 1 804 280 154 LYS CB C 33.095 0.2 1 805 280 154 LYS N N 117.255 0.1 1 806 281 155 PRO CA C 62.702 0.2 1 807 281 155 PRO CB C 34.250 0.2 1 808 281 155 PRO CG C 25.388 0.2 1 809 282 156 ALA H H 9.075 0.02 1 810 282 156 ALA CA C 55.625 0.2 1 811 282 156 ALA CB C 17.052 0.2 1 812 282 156 ALA N N 128.012 0.1 1 813 283 157 SER H H 8.175 0.02 1 814 283 157 SER HA H 4.031 0.02 1 815 283 157 SER CA C 60.665 0.2 1 816 283 157 SER CB C 62.131 0.2 1 817 283 157 SER N N 108.678 0.1 1 818 284 158 GLU H H 7.571 0.02 1 819 284 158 GLU HA H 4.268 0.02 1 820 284 158 GLU CA C 57.000 0.2 1 821 284 158 GLU CB C 31.139 0.2 1 822 284 158 GLU CG C 35.558 0.2 1 823 284 158 GLU N N 119.932 0.1 1 824 285 159 PHE H H 7.155 0.02 1 825 285 159 PHE CA C 59.773 0.2 1 826 285 159 PHE CB C 41.043 0.2 1 827 285 159 PHE N N 115.784 0.1 1 828 286 160 VAL H H 7.664 0.02 1 829 286 160 VAL CA C 61.286 0.2 1 830 286 160 VAL CB C 32.113 0.2 1 831 286 160 VAL N N 118.369 0.1 1 832 287 161 LYS H H 9.338 0.02 1 833 287 161 LYS HA H 4.938 0.02 1 834 287 161 LYS CA C 53.160 0.2 1 835 287 161 LYS CB C 33.940 0.2 1 836 287 161 LYS CG C 24.293 0.2 1 837 287 161 LYS CD C 28.140 0.2 1 838 287 161 LYS CE C 41.890 0.2 1 839 287 161 LYS N N 130.453 0.1 1 840 288 162 ILE H H 8.480 0.02 1 841 288 162 ILE HA H 5.016 0.02 1 842 288 162 ILE CA C 57.095 0.2 1 843 288 162 ILE CB C 36.292 0.2 1 844 288 162 ILE CG1 C 25.877 0.2 4 845 288 162 ILE CG2 C 17.148 0.2 4 846 288 162 ILE N N 124.746 0.1 1 847 289 163 LEU H H 8.970 0.02 1 848 289 163 LEU HA H 4.826 0.02 1 849 289 163 LEU CA C 52.526 0.2 1 850 289 163 LEU CB C 47.311 0.2 1 851 289 163 LEU N N 127.675 0.1 1 852 290 164 ASP H H 9.073 0.02 1 853 290 164 ASP CA C 55.687 0.2 1 854 290 164 ASP CB C 39.834 0.2 1 855 290 164 ASP N N 121.371 0.1 1 856 291 165 THR H H 7.124 0.02 1 857 291 165 THR HA H 4.807 0.02 1 858 291 165 THR CA C 58.663 0.2 1 859 291 165 THR CB C 71.238 0.2 1 860 291 165 THR N N 107.345 0.1 1 861 292 166 PHE H H 8.720 0.02 1 862 292 166 PHE HA H 3.787 0.02 1 863 292 166 PHE CA C 61.653 0.2 1 864 292 166 PHE CB C 39.435 0.2 1 865 292 166 PHE N N 118.945 0.1 1 866 293 167 GLU H H 8.532 0.02 1 867 293 167 GLU HA H 4.258 0.02 1 868 293 167 GLU CA C 59.359 0.2 1 869 293 167 GLU CB C 29.162 0.2 1 870 293 167 GLU CG C 36.840 0.2 1 871 293 167 GLU N N 120.992 0.1 1 872 294 168 LYS H H 7.064 0.02 1 873 294 168 LYS HA H 4.285 0.02 1 874 294 168 LYS CA C 57.276 0.2 1 875 294 168 LYS CB C 33.484 0.2 1 876 294 168 LYS CG C 25.939 0.2 1 877 294 168 LYS N N 115.223 0.1 1 878 295 169 LEU H H 7.466 0.02 1 879 295 169 LEU CA C 57.776 0.2 1 880 295 169 LEU CB C 41.664 0.2 1 881 295 169 LEU CD1 C 24.971 0.2 2 882 295 169 LEU CD2 C 22.698 0.2 2 883 295 169 LEU N N 120.222 0.1 1 884 296 170 LYS H H 7.499 0.02 1 885 296 170 LYS HA H 4.272 0.02 1 886 296 170 LYS CA C 58.909 0.2 1 887 296 170 LYS CB C 32.125 0.2 1 888 296 170 LYS N N 116.193 0.1 1 889 297 171 ASP H H 7.513 0.02 1 890 297 171 ASP CA C 55.092 0.2 1 891 297 171 ASP CB C 41.849 0.2 1 892 297 171 ASP N N 117.257 0.1 1 893 298 172 LEU H H 7.535 0.02 1 894 298 172 LEU CA C 57.142 0.2 1 895 298 172 LEU CB C 42.872 0.2 1 896 298 172 LEU N N 120.951 0.1 1 897 299 173 PHE H H 9.188 0.02 1 898 299 173 PHE CA C 62.789 0.2 1 899 299 173 PHE CB C 38.592 0.2 1 900 299 173 PHE N N 119.264 0.1 1 901 300 174 THR H H 7.984 0.02 1 902 300 174 THR CA C 62.359 0.2 1 903 300 174 THR CB C 68.820 0.2 1 904 300 174 THR N N 112.199 0.1 1 905 301 175 GLU H H 7.631 0.02 1 906 301 175 GLU HA H 4.210 0.02 1 907 301 175 GLU CA C 57.441 0.2 1 908 301 175 GLU CB C 30.020 0.2 1 909 301 175 GLU CG C 36.065 0.2 1 910 301 175 GLU N N 119.685 0.1 1 911 302 176 LEU H H 7.851 0.02 1 912 302 176 LEU CA C 57.164 0.2 1 913 302 176 LEU CB C 42.045 0.2 1 914 302 176 LEU CG C 26.677 0.2 1 915 302 176 LEU N N 119.580 0.1 1 916 303 177 GLN H H 8.011 0.02 1 917 303 177 GLN CA C 58.204 0.2 1 918 303 177 GLN CB C 28.188 0.2 1 919 303 177 GLN N N 117.077 0.1 1 920 304 178 LYS H H 7.227 0.02 1 921 304 178 LYS N N 115.325 0.1 1 922 305 179 LYS H H 7.625 0.02 1 923 305 179 LYS N N 116.100 0.1 1 924 306 180 ILE H H 7.403 0.02 1 925 306 180 ILE N N 116.808 0.1 1 926 307 181 TYR H H 7.309 0.02 1 927 307 181 TYR N N 126.513 0.1 1 stop_ save_