data_4553 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Assignment of 1H, 13C and 15N Resonances of the I-domain of Human Leukocyte Function Associated Antigen-1 ; _BMRB_accession_number 4553 _BMRB_flat_file_name bmr4553.str _Entry_type original _Submission_date 1999-12-10 _Accession_date 1999-12-13 _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 Kriwacki Richard W. . 2 Legge Glen B. . 3 Hommel Ulrich . . 4 Ramage Paul . . 5 Chung John . . 6 Tennant Linda L. . 7 Wright Peter E. . 8 Dyson H. Jane . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 1166 "13C chemical shifts" 690 "15N chemical shifts" 191 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2000-12-12 original BMRB . stop_ _Original_release_date 1999-12-13 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Kriwacki, R.W., Legge, G.B., Hommel, U., Ramage, P., Chung, J., Tennant, L.L., Wright, P.E., and Dyson, H.J., "Assignment of 1H, 13C and 15N Resonances of the I-domain of Human Leukocyte Function Associated Antigen-1," J. Biomol. NMR 16, 271-272 (2000). ; _Citation_title ; Assignment of 1H, 13C and 15N Resonances of the I-domain of Human Leukocyte Function Associated Antigen-1 ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 20262885 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Kriwacki Richard W. . 2 Legge Glen B. . 3 Hommel Ulrich . . 4 Ramage Paul . . 5 Chung John . . 6 Tennant Linda L. . 7 Wright Peter E. . 8 Dyson H. Jane . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of Biomolecular NMR' _Journal_volume 16 _Journal_issue 3 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 271 _Page_last 272 _Year 2000 _Details . loop_ _Keyword 'LFA-1 NMR assignment' stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref_1 _Saveframe_category citation _Citation_full ; Assignment of the 1H, 13C and 15N Resonances of the I-domain of Human Leukocyte Function Associated Antigen-1 In preparation. J. Biomol. NMR ; _Citation_title . _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 NA NA . . stop_ _Journal_abbreviation . _Journal_name_full . _Journal_volume . _Journal_issue . _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first . _Page_last . _Year . _Details . save_ save_ref_2 _Saveframe_category citation _Citation_full ; NMR solution structure of the inserted domain of human Leukocyte Function Associated Antigen-1 J. Mol. Biol. (In press) Glen B. Legge, Richard W. Kriwacki, John Chung, Ulrich Hommel|, Paul Ramage|, H. Jane Dyson and Peter E. Wright ; _Citation_title ; NMR solution structure of the inserted domain of human leukocyte function associated antigen-1. ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 10653701 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Legge 'G B' B. . 2 Kriwacki 'R W' W. . 3 Chung J . . 4 Hommel U . . 5 Ramage P . . 6 Case 'D A' A. . 7 Dyson 'H J' J. . 8 Wright 'P E' E. . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_name_full 'Journal of molecular biology' _Journal_volume 295 _Journal_issue 5 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 1251 _Page_last 1264 _Year 2000 _Details ; The interaction between the leukocyte function-associated antigen-1 (LFA-1) and the intercellular adhesion molecule is thought to be mediated primarily via the inserted domain (I-domain) in the alpha-subunit. The activation of LFA-1 is an early step in triggering the adhesion of leukocytes to target cells decorated with intercellular adhesion molecules. There is some disagreement in the literature over the respective roles of conformational changes in the I-domain and of divalent cations (Mg(2+), Mn(2+)) in the activation of LFA-1 for intercellular adhesion molecule binding. X-ray crystallographic structures of the I-domains of LFA-1 and Mac-1 in the presence and absence of cations show structural differences in the C-terminal alpha-helix; this change was proposed to represent the active and inactive conformations of the I-domain. However, more recent X-ray results have called this proposal into question. The solution structure of the Mg(2+) complex of the I-domain of LFA-1 has been determined by NMR methods, using a model-based approach to nuclear Overhauser enhancement spectroscopy peak assignment. The protein adopts the same structure in solution as that of the published I-domain X-ray structures, but the C-terminal region, where the X-ray structures are most different from each other, is different again in the solution structures. The secondary structure of this helix is well formed, but NMR relaxation data indicate that there is considerable flexibility present, probably consisting of breathing or segmental motion of the helix. The conformational diversity seen in the various X-ray structures could be explained as a result of the inherent flexibility of this C-terminal region and as a result of crystal contacts. Our NMR data are consistent with a model where the C-terminal helix has the potential flexibility to take up alternative conformations, for example, in the presence and absence of the intercellular adhesion molecule ligand. The role of divalent cations appears from our results not to be as a direct mediator of a conformational change that alters affinity for the ligand. Rather, the presence of the cation appears to be involved in some other way in ligand binding, perhaps by acting as a bridge to the ligand and by modulation of the charge of the binding surface. ; save_ save_ref_3 _Saveframe_category citation _Citation_full ; Structural Basis for LFA-1 Inhibition upon Lovastatin Binding to the CD11a I-Domain J. Kallen, K. Welzenbach, P. Ramage, D. Geyl, R. Kriwacki, G. Legge, S. Cottens,G. Weitz-Schmidt, U. Hommel Journal of Molecular Biology, Vol. 292, No. 1, Sep 1999, pp. 1-9 (doi:10.1006/jmbi.1999.3047) ; _Citation_title ; Structural basis for LFA-1 inhibition upon lovastatin binding to the CD11a I-domain. ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 10493852 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Kallen J . . 2 Welzenbach K . . 3 Ramage P . . 4 Geyl D . . 5 Kriwacki R . . 6 Legge G . . 7 Cottens S . . 8 Weitz-Schmidt G . . 9 Hommel U . . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_name_full 'Journal of molecular biology' _Journal_volume 292 _Journal_issue 1 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 1 _Page_last 9 _Year 1999 _Details ; The lymphocyte function-associated antigen (LFA-1) belongs to the family of beta2-integrins and plays an important role in T-cell activation and leukocyte migration to sites of inflammation. We report here that lovastatin, a drug clinically used for lowering cholesterol levels, inhibits the interaction of human LFA-1 with its counter-receptor intercellular adhesion molecule-1. Using nuclear magnetic resonance spectroscopy and X-ray crystallography we show that the inhibitor binds to a highly conserved domain of the LFA-1 alpha-chain called the I-domain. The first three-dimensional structure of an integrin inhibitor bound to its receptor reveals atomic details for a hitherto unknown mode of LFA-1 inhibition. It also sheds light into possible mechanisms of LFA-1 mediated signalling and will support the design of novel anti-adhesive and immunosuppressive drugs. ; save_ ################################## # Molecular system description # ################################## save_LFA-1_I-domain _Saveframe_category molecular_system _Mol_system_name 'Inserted domain of the leukocyte function associated antigen-1 in the presence of magnesium' _Abbreviation_common 'LFA-1 I-domain' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label LFA-1 $LFA-1 magnesium $entity_MG stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' _Database_query_date . _Details 'Biological_function: Leukocyte specific integrin ICAM binding (Intercellular Adhesion Molecules).' save_ ######################## # Monomeric polymers # ######################## save_LFA-1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Leukocyte Function Associated Antigen-1 Inserted-Domain' _Name_variant 'aLB2, CD11a/CD18' _Abbreviation_common 'LFA-1 I-domian' _Molecular_mass 21268 _Mol_thiol_state 'not present' _Details 'Calculated with N-terminal methionine off.' ############################## # Polymer residue sequence # ############################## _Residue_count 189 _Mol_residue_sequence ; MASKGNVDLVFLFDGSMSLQ PDEFQKILDFMKDVMKKLSN TSYQFAAVQFSTSYKTEFDF SDYVKWKDPDALLKHVKHML LLTNTFGAINYVATEVFREE LGARPDATKVLIIITDGEAT DSGNIDAAKDIIRYIIGIGK HFQTKESQETLHKFASKPAS EFVKILDTFEKLKDLFTELQ KKIYVIEGM ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 124 MET 2 125 ALA 3 126 SER 4 127 LYS 5 128 GLY 6 129 ASN 7 130 VAL 8 131 ASP 9 132 LEU 10 133 VAL 11 134 PHE 12 135 LEU 13 136 PHE 14 137 ASP 15 138 GLY 16 139 SER 17 140 MET 18 141 SER 19 142 LEU 20 143 GLN 21 144 PRO 22 145 ASP 23 146 GLU 24 147 PHE 25 148 GLN 26 149 LYS 27 150 ILE 28 151 LEU 29 152 ASP 30 153 PHE 31 154 MET 32 155 LYS 33 156 ASP 34 157 VAL 35 158 MET 36 159 LYS 37 160 LYS 38 161 LEU 39 162 SER 40 163 ASN 41 164 THR 42 165 SER 43 166 TYR 44 167 GLN 45 168 PHE 46 169 ALA 47 170 ALA 48 171 VAL 49 172 GLN 50 173 PHE 51 174 SER 52 175 THR 53 176 SER 54 177 TYR 55 178 LYS 56 179 THR 57 180 GLU 58 181 PHE 59 182 ASP 60 183 PHE 61 184 SER 62 185 ASP 63 186 TYR 64 187 VAL 65 188 LYS 66 189 TRP 67 190 LYS 68 191 ASP 69 192 PRO 70 193 ASP 71 194 ALA 72 195 LEU 73 196 LEU 74 197 LYS 75 198 HIS 76 199 VAL 77 200 LYS 78 201 HIS 79 202 MET 80 203 LEU 81 204 LEU 82 205 LEU 83 206 THR 84 207 ASN 85 208 THR 86 209 PHE 87 210 GLY 88 211 ALA 89 212 ILE 90 213 ASN 91 214 TYR 92 215 VAL 93 216 ALA 94 217 THR 95 218 GLU 96 219 VAL 97 220 PHE 98 221 ARG 99 222 GLU 100 223 GLU 101 224 LEU 102 225 GLY 103 226 ALA 104 227 ARG 105 228 PRO 106 229 ASP 107 230 ALA 108 231 THR 109 232 LYS 110 233 VAL 111 234 LEU 112 235 ILE 113 236 ILE 114 237 ILE 115 238 THR 116 239 ASP 117 240 GLY 118 241 GLU 119 242 ALA 120 243 THR 121 244 ASP 122 245 SER 123 246 GLY 124 247 ASN 125 248 ILE 126 249 ASP 127 250 ALA 128 251 ALA 129 252 LYS 130 253 ASP 131 254 ILE 132 255 ILE 133 256 ARG 134 257 TYR 135 258 ILE 136 259 ILE 137 260 GLY 138 261 ILE 139 262 GLY 140 263 LYS 141 264 HIS 142 265 PHE 143 266 GLN 144 267 THR 145 268 LYS 146 269 GLU 147 270 SER 148 271 GLN 149 272 GLU 150 273 THR 151 274 LEU 152 275 HIS 153 276 LYS 154 277 PHE 155 278 ALA 156 279 SER 157 280 LYS 158 281 PRO 159 282 ALA 160 283 SER 161 284 GLU 162 285 PHE 163 286 VAL 164 287 LYS 165 288 ILE 166 289 LEU 167 290 ASP 168 291 THR 169 292 PHE 170 293 GLU 171 294 LYS 172 295 LEU 173 296 LYS 174 297 ASP 175 298 LEU 176 299 PHE 177 300 THR 178 301 GLU 179 302 LEU 180 303 GLN 181 304 LYS 182 305 LYS 183 306 ILE 184 307 TYR 185 308 VAL 186 309 ILE 187 310 GLU 188 311 GLY 189 312 MET stop_ _Sequence_homology_query_date 2008-08-19 _Sequence_homology_query_revised_last_date 2008-08-19 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 1CQP 'Crystal Structure Analysis Of The Complex Lfa-1 (Cd11a) I- Domain LOVASTATIN AT 2.6 A RESOLUTION' 96.30 182 100.00 100.00 6.39e-101 PDB 1DGQ 'Nmr Solution Structure Of The Inserted Domain Of Human Leukocyte Function Associated Antigen-1' 99.47 188 100.00 100.00 1.16e-104 PDB 1LFA 'Cd11a I-Domain With Bound Mn++' 97.88 187 99.46 99.46 1.35e-101 PDB 1MJN 'Crystal Structure Of The Intermediate Affinity Al I Domain Mutant' 94.71 179 98.32 98.32 7.95e-97 PDB 1MQ8 'Crystal Structure Of Alphal I Domain In Complex With Icam-1' 93.65 177 98.31 98.31 2.83e-95 PDB 1MQ9 'Crystal Structure Of High Affinity Alphal I Domain With Ligand Mimetic Crystal Contact' 94.71 180 98.32 98.32 1.18e-96 PDB 1MQA 'Crystal Structure Of High Affinity Alphal I Domain In The Absence Of Ligand Or Metal' 94.71 180 98.32 98.32 1.18e-96 PDB 1RD4 'An Allosteric Inhibitor Of Lfa-1 Bound To Its I-Domain' 97.88 191 99.46 99.46 1.18e-101 PDB 1T0P ; Structural Basis Of Icam Recognition By Integrin Alpahlbeta2 Revealed In The Complex Structure Of Binding Domains Of Icam-3 And Alphalbeta2 At 1.65 A ; 92.06 175 98.85 98.85 3.69e-95 PDB 1XDD 'X-Ray Structure Of Lfa-1 I-Domain In Complex With Lfa703 At 2.2a Resolution' 99.47 188 100.00 100.00 1.16e-104 PDB 1XDG 'X-Ray Structure Of Lfa-1 I-Domain In Complex With Lfa878 At 2.1a Resolution' 99.47 188 100.00 100.00 1.16e-104 PDB 1XUO 'X-Ray Structure Of Lfa-1 I-Domain Bound To A 1,4-Diazepane- 2,5-Dione Inhibitor At 1.8a Resolution' 99.47 188 100.00 100.00 1.16e-104 PDB 1ZON 'Cd11a I-Domain Without Bound Cation' 97.88 187 99.46 99.46 1.35e-101 PDB 1ZOO 'Cd11a I-Domain With Bound Magnesium Ion' 97.88 187 99.46 99.46 1.35e-101 PDB 1ZOP 'Cd11a I-Domain With Bound Magnesium Ion' 97.88 187 99.46 99.46 1.35e-101 DBJ BAG36913 'unnamed protein product [Homo sapiens]' 97.88 1170 99.46 99.46 2.99e-104 EMBL CAA68747 'unnamed protein product [Homo sapiens]' 97.88 1170 100.00 100.00 6.49e-106 GenBank AAC31672 'leukocyte function-associated molecule-1 alpha subunit [Homo sapiens]' 97.88 1223 100.00 100.00 3.53e-106 GenBank AAQ14923 'leukocyte-associated molecule-1 alpha subunit [Pan troglodytes]' 97.88 1170 99.46 99.46 2.45e-104 GenBank AAZ38713 'integrin, alpha L (antigen CD11A (p180), lymphocyte function-associated antigen 1; alpha polypeptide) [Homo sapiens]' 97.88 1170 99.46 99.46 2.99e-104 GenBank EAW52244 ; integrin, alpha L (antigen CD11A (p180), lymphocyte function-associated antigen 1; alpha polypeptide), isoform CRA_b [Homo sapiens] ; 97.88 1223 99.46 99.46 1.65e-104 GenBank EAW52245 ; integrin, alpha L (antigen CD11A (p180), lymphocyte function-associated antigen 1; alpha polypeptide), isoform CRA_c [Homo sapiens] ; 97.88 1170 99.46 99.46 2.99e-104 REF NP_001029341 'integrin alpha L [Pan troglodytes]' 97.88 1170 99.46 99.46 2.45e-104 REF NP_002200 'integrin alpha L isoform a precursor [Homo sapiens]' 97.88 1170 99.46 99.46 2.99e-104 SWISS-PROT P20701 ; Integrin alpha-L precursor (Leukocyte adhesion glycoprotein LFA-1 alpha chain) (LFA-1A) (Leukocyte function-associated molecule 1 alpha chain) (CD11 antigen-like family member A) (CD11a antigen) ; 97.88 1170 99.46 99.46 2.99e-104 stop_ save_ ############# # Ligands # ############# save_MG _Saveframe_category ligand _Mol_type "non-polymer (NON-POLYMER)" _Name_common 'MAGNESIUM ION' _BMRB_code MG _PDB_code MG _Molecular_mass 24.305 _Mol_charge 2 _Mol_paramagnetic . _Mol_aromatic no _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons MG MG MG . 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 _Organ _Cell_line $LFA-1 Human 9606 Eukaryota Metazoa Homo sapien blood leukocytes 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_type _Vector_name _Details $LFA-1 'recombinant technology' 'E. coli' Escherichia coli BL21 (DE3)pLysS plasmid pET17b 'Refolded protein from inclusion bodies.' 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 1.2 mM '[U-13C; U-15N]' NaH2PO4 10 mM . MgSO4 10 mM . NaCl 150 mM . NaN3 0.05 % . 2H2O 5 % . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $LFA-1 1.2 mM [U-15N] stop_ save_ ############################ # Computer software used # ############################ save_FELIX _Saveframe_category software _Name FELIX _Version 97 _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 750 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 600 _Details . save_ save_NMR_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AMX _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_HNCA_1 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label . save_ save_HNCO_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label . save_ save_HN(CA)CO_3 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CA)CO _Sample_label . save_ save_HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label . save_ save_CBCA(CO)NH_5 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _Sample_label . save_ save_HBHA(CO)NH_6 _Saveframe_category NMR_applied_experiment _Experiment_name HBHA(CO)NH _Sample_label . save_ save_1H-15N_TOCSY_7 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N TOCSY' _Sample_label . save_ save_CC(CO)NH_TOSCY_8 _Saveframe_category NMR_applied_experiment _Experiment_name 'CC(CO)NH TOSCY' _Sample_label . save_ save_HCCH_COSY_9 _Saveframe_category NMR_applied_experiment _Experiment_name 'HCCH COSY' _Sample_label . save_ save_HCCH_TOCSY_10 _Saveframe_category NMR_applied_experiment _Experiment_name 'HCCH TOCSY' _Sample_label . save_ save_HCCH_TOCSY_(aromatic)_11 _Saveframe_category NMR_applied_experiment _Experiment_name 'HCCH TOCSY (aromatic)' _Sample_label . save_ save_2D_13C_HSQC_12 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 13C HSQC' _Sample_label . save_ save_3D_HB(CBCG)CDHD_13 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HB(CBCG)CDHD' _Sample_label . save_ ####################### # Sample conditions # ####################### save_condition_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.28 0.02 M pH* 7.2 0.2 n/a temperature 295 1 K stop_ save_ save_condition_2 _Saveframe_category sample_conditions _Details ; 2mM MgCl2 pH7.3 0.02% NaN3 and 5% 2H2O Protein was less affected by line broadening under these conditions. ; loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.018 0.02 M pH* 7.3 0.2 na temperature 295 1 K 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 TSP C 13 'methyl protons' ppm 0.00 external direct cylindrical external parallel 0.25144954 TSP H 1 'methyl protons' ppm 0.00 external direct cylindrical external parallel 1.00 TSP N 15 'methyl protons' ppm 0.00 external direct cylindrical external parallel 0.101329 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_lfa1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label HNCA HNCO stop_ _Sample_conditions_label $condition_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name LFA-1 _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 . 3 SER HA H 4.48 . 1 2 . 3 SER HB2 H 3.83 . 1 3 . 3 SER HB3 H 3.83 . 1 4 . 3 SER CA C 58.1 . 1 5 . 3 SER CB C 63.7 . 1 6 . 4 LYS H H 8.50 . 1 7 . 4 LYS HA H 4.31 . 1 8 . 4 LYS HB2 H 1.83 . 2 9 . 4 LYS HB3 H 1.73 . 2 10 . 4 LYS HG2 H 1.40 . 1 11 . 4 LYS HG3 H 1.40 . 1 12 . 4 LYS HD2 H 1.62 . 1 13 . 4 LYS HD3 H 1.62 . 1 14 . 4 LYS HE2 H 2.93 . 1 15 . 4 LYS HE3 H 2.93 . 1 16 . 4 LYS CA C 56.3 . 1 17 . 4 LYS CB C 32.7 . 1 18 . 4 LYS CG C 24.6 . 1 19 . 4 LYS CD C 28.8 . 1 20 . 4 LYS CE C 42.0 . 1 21 . 4 LYS N N 124.8 . 1 22 . 5 GLY H H 8.58 . 1 23 . 5 GLY HA2 H 3.93 . 2 24 . 5 GLY HA3 H 3.80 . 2 25 . 5 GLY CA C 45.1 . 1 26 . 5 GLY N N 111.1 . 1 27 . 6 ASN H H 8.21 . 1 28 . 6 ASN HA H 4.72 . 1 29 . 6 ASN HB2 H 2.59 . 2 30 . 6 ASN HB3 H 2.25 . 2 31 . 6 ASN HD21 H 7.61 . 2 32 . 6 ASN HD22 H 6.61 . 2 33 . 6 ASN CA C 52.7 . 1 34 . 6 ASN CB C 37.5 . 1 35 . 6 ASN N N 120.6 . 1 36 . 6 ASN ND2 N 113.4 . 1 37 . 7 VAL H H 6.93 . 1 38 . 7 VAL HA H 4.33 . 2 39 . 7 VAL HB H 0.66 . 2 40 . 7 VAL HG1 H 0.49 . 1 41 . 7 VAL HG2 H 0.47 . 1 42 . 7 VAL CA C 61.1 . 1 43 . 7 VAL CB C 34.4 . 1 44 . 7 VAL CG1 C 21.8 . 1 45 . 7 VAL CG2 C 20.9 . 1 46 . 7 VAL N N 124.8 . 1 47 . 8 ASP H H 8.61 . 1 48 . 8 ASP HA H 4.72 . 1 49 . 8 ASP HB2 H 2.40 . 2 50 . 8 ASP HB3 H 2.26 . 2 51 . 8 ASP CA C 52.7 . 1 52 . 8 ASP CB C 41.1 . 1 53 . 8 ASP N N 132.6 . 1 54 . 9 LEU H H 8.54 . 1 55 . 9 LEU HA H 5.40 . 1 56 . 9 LEU HB2 H 1.51 . 2 57 . 9 LEU HB3 H 1.11 . 2 58 . 9 LEU HG H 1.27 . 1 59 . 9 LEU HD1 H 0.66 . 2 60 . 9 LEU HD2 H 0.16 . 2 61 . 9 LEU CA C 54.2 . 1 62 . 9 LEU CB C 44.5 . 1 63 . 9 LEU CG C 28.0 . 1 64 . 9 LEU CD1 C 26.9 . 2 65 . 9 LEU CD2 C 23.2 . 2 66 . 9 LEU N N 128.1 . 1 67 . 10 VAL H H 9.06 . 1 68 . 10 VAL HA H 4.63 . 1 69 . 10 VAL HB H 1.83 . 1 70 . 10 VAL HG1 H 0.59 . 1 71 . 10 VAL HG2 H 0.31 . 1 72 . 10 VAL CA C 59.5 . 1 73 . 10 VAL CB C 34.3 . 1 74 . 10 VAL CG1 C 21.0 . 1 75 . 10 VAL CG2 C 24.6 . 1 76 . 10 VAL N N 125.0 . 1 77 . 11 PHE H H 8.63 . 1 78 . 11 PHE HA H 5.34 . 1 79 . 11 PHE HB2 H 3.17 . 1 80 . 11 PHE HB3 H 3.17 . 1 81 . 11 PHE HD1 H 7.17 . 1 82 . 11 PHE HD2 H 7.17 . 1 83 . 11 PHE HE1 H 7.00 . 1 84 . 11 PHE HE2 H 7.00 . 1 85 . 11 PHE HZ H 7.00 . 1 86 . 11 PHE CA C 56.7 . 1 87 . 11 PHE CB C 42.4 . 1 88 . 11 PHE CD1 C 132.4 . 1 89 . 11 PHE CD2 C 132.4 . 1 90 . 11 PHE CE1 C 131.4 . 1 91 . 11 PHE CE2 C 131.4 . 1 92 . 11 PHE CZ C 131.4 . 1 93 . 11 PHE N N 132.4 . 1 94 . 12 LEU H H 9.73 . 1 95 . 12 LEU HA H 5.76 . 1 96 . 12 LEU HB2 H 2.04 . 2 97 . 12 LEU HB3 H 1.12 . 2 98 . 12 LEU HG H 1.55 . 1 99 . 12 LEU HD1 H 0.41 . 2 100 . 12 LEU HD2 H 0.70 . 2 101 . 12 LEU CA C 52.9 . 1 102 . 12 LEU CB C 45.3 . 1 103 . 12 LEU CG C 26.9 . 1 104 . 12 LEU CD1 C 24.5 . 2 105 . 12 LEU CD2 C 24.0 . 2 106 . 12 LEU N N 130.3 . 1 107 . 13 PHE H H 9.54 . 1 108 . 13 PHE HA H 5.84 . 1 109 . 13 PHE HB2 H 2.97 . 2 110 . 13 PHE HB3 H 2.93 . 2 111 . 13 PHE HD1 H 7.00 . 1 112 . 13 PHE HD2 H 7.00 . 1 113 . 13 PHE HE1 H 6.92 . 1 114 . 13 PHE HE2 H 6.92 . 1 115 . 13 PHE HZ H 7.00 . 3 116 . 13 PHE CA C 54.9 . 1 117 . 13 PHE CB C 42.8 . 1 118 . 13 PHE CD1 C 133.7 . 1 119 . 13 PHE CD2 C 133.7 . 1 120 . 13 PHE CE1 C 131.4 . 1 121 . 13 PHE CE2 C 131.4 . 1 122 . 13 PHE CZ C 131.4 . 1 123 . 13 PHE N N 133.7 . 1 124 . 14 ASP H H 7.89 . 1 125 . 14 ASP HA H 3.29 . 1 126 . 14 ASP HB2 H 3.02 . 2 127 . 14 ASP HB3 H 2.98 . 2 128 . 14 ASP CA C 53.3 . 1 129 . 14 ASP CB C 44.4 . 1 130 . 14 ASP N N 128.6 . 1 131 . 15 GLY H H 8.33 . 1 132 . 15 GLY HA2 H 4.87 . 2 133 . 15 GLY HA3 H 4.42 . 2 134 . 15 GLY CA C 44.5 . 1 135 . 15 GLY N N 111.7 . 1 136 . 16 SER H H 9.69 . 1 137 . 16 SER HA H 4.19 . 1 138 . 16 SER HB2 H 3.89 . 1 139 . 16 SER HB3 H 3.89 . 1 140 . 16 SER HG H 8.51 . 1 141 . 16 SER CA C 58.6 . 1 142 . 16 SER CB C 66.4 . 1 143 . 16 SER N N 117.5 . 1 144 . 17 MET H H 8.72 . 1 145 . 17 MET HA H 3.79 . 1 146 . 17 MET HB2 H 2.03 . 2 147 . 17 MET HB3 H 1.93 . 2 148 . 17 MET HG2 H 2.00 . 2 149 . 17 MET HG3 H 1.77 . 2 150 . 17 MET HE H 2.01 . 1 151 . 17 MET CA C 57.0 . 1 152 . 17 MET CB C 32.9 . 1 153 . 17 MET CG C 29.9 . 1 154 . 17 MET CE C 17.4 . 1 155 . 17 MET N N 117.4 . 1 156 . 18 SER H H 6.86 . 1 157 . 18 SER HA H 4.12 . 1 158 . 18 SER HB2 H 4.14 . 2 159 . 18 SER HB3 H 3.72 . 2 160 . 18 SER HG H 10.92 . 1 161 . 18 SER CA C 58.7 . 1 162 . 18 SER CB C 61.6 . 1 163 . 18 SER N N 111.6 . 1 164 . 19 LEU H H 6.93 . 1 165 . 19 LEU HA H 4.33 . 1 166 . 19 LEU HB2 H 1.90 . 2 167 . 19 LEU HB3 H 1.24 . 2 168 . 19 LEU HG H 1.59 . 1 169 . 19 LEU HD1 H 1.06 . 2 170 . 19 LEU HD2 H 0.82 . 2 171 . 19 LEU CA C 55.4 . 1 172 . 19 LEU CB C 43.6 . 1 173 . 19 LEU CG C 27.4 . 1 174 . 19 LEU CD1 C 28.7 . 2 175 . 19 LEU CD2 C 27.6 . 2 176 . 19 LEU N N 125.5 . 1 177 . 20 GLN H H 8.92 . 1 178 . 20 GLN HA H 4.51 . 1 179 . 20 GLN HB2 H 1.53 . 1 180 . 20 GLN HB3 H 1.53 . 1 181 . 20 GLN HG2 H 2.60 . 2 182 . 20 GLN HG3 H 2.53 . 2 183 . 20 GLN HE21 H 7.56 . 2 184 . 20 GLN HE22 H 6.90 . 2 185 . 20 GLN CA C 53.5 . 1 186 . 20 GLN CB C 27.7 . 1 187 . 20 GLN CG C 33.9 . 1 188 . 20 GLN N N 123.7 . 1 189 . 20 GLN NE2 N 115.6 . 1 190 . 21 PRO HA H 4.38 . 1 191 . 21 PRO HB2 H 2.03 . 1 192 . 21 PRO HB3 H 2.48 . 1 193 . 21 PRO HG2 H 2.22 . 1 194 . 21 PRO HG3 H 2.22 . 1 195 . 21 PRO HD2 H 3.93 . 2 196 . 21 PRO HD3 H 3.85 . 2 197 . 21 PRO CA C 66.4 . 1 198 . 21 PRO CB C 31.7 . 1 199 . 21 PRO CG C 27.8 . 1 200 . 21 PRO CD C 49.7 . 1 201 . 22 ASP H H 8.78 . 1 202 . 22 ASP HA H 4.33 . 1 203 . 22 ASP HB2 H 2.58 . 2 204 . 22 ASP HB3 H 2.51 . 2 205 . 22 ASP CA C 56.1 . 1 206 . 22 ASP CB C 39.9 . 1 207 . 22 ASP N N 115.3 . 1 208 . 23 GLU H H 6.86 . 1 209 . 23 GLU HA H 3.23 . 1 210 . 23 GLU HB2 H 1.94 . 2 211 . 23 GLU HB3 H 0.40 . 2 212 . 23 GLU HG2 H 2.01 . 2 213 . 23 GLU HG3 H 1.43 . 2 214 . 23 GLU CA C 58.4 . 1 215 . 23 GLU CB C 28.6 . 1 216 . 23 GLU CG C 36.6 . 1 217 . 23 GLU N N 122.8 . 1 218 . 24 PHE H H 7.81 . 1 219 . 24 PHE HA H 3.92 . 1 220 . 24 PHE HB2 H 2.83 . 2 221 . 24 PHE HB3 H 2.41 . 2 222 . 24 PHE HD1 H 6.93 . 1 223 . 24 PHE HD2 H 6.93 . 1 224 . 24 PHE HE1 H 7.14 . 1 225 . 24 PHE HE2 H 7.14 . 1 226 . 24 PHE HZ H 7.08 . 1 227 . 24 PHE CA C 61.7 . 1 228 . 24 PHE CB C 39.1 . 1 229 . 24 PHE CD1 C 132.2 . 1 230 . 24 PHE CD2 C 132.2 . 1 231 . 24 PHE CE1 C 132.0 . 1 232 . 24 PHE CE2 C 132.0 . 1 233 . 24 PHE CZ C 130.8 . 1 234 . 24 PHE N N 119.7 . 1 235 . 25 GLN H H 7.84 . 1 236 . 25 GLN HA H 3.63 . 1 237 . 25 GLN HB2 H 2.15 . 2 238 . 25 GLN HB3 H 2.11 . 2 239 . 25 GLN HG2 H 2.32 . 2 240 . 25 GLN HG3 H 2.40 . 2 241 . 25 GLN HE21 H 7.74 . 2 242 . 25 GLN HE22 H 6.89 . 2 243 . 25 GLN CA C 58.2 . 1 244 . 25 GLN CB C 28.0 . 1 245 . 25 GLN CG C 33.2 . 1 246 . 25 GLN N N 116.3 . 1 247 . 25 GLN NE2 N 115.6 . 1 248 . 26 LYS H H 7.56 . 1 249 . 26 LYS HA H 4.04 . 1 250 . 26 LYS HB2 H 1.82 . 2 251 . 26 LYS HB3 H 1.74 . 2 252 . 26 LYS HG2 H 1.57 . 2 253 . 26 LYS HG3 H 1.41 . 2 254 . 26 LYS HD2 H 1.66 . 1 255 . 26 LYS HD3 H 1.66 . 1 256 . 26 LYS HE2 H 2.95 . 1 257 . 26 LYS HE3 H 2.95 . 1 258 . 26 LYS CA C 59.8 . 1 259 . 26 LYS CB C 32.3 . 1 260 . 26 LYS CG C 25.2 . 1 261 . 26 LYS CD C 29.5 . 1 262 . 26 LYS CE C 42.3 . 1 263 . 26 LYS N N 119.5 . 1 264 . 27 ILE H H 7.51 . 1 265 . 27 ILE HA H 3.49 . 1 266 . 27 ILE HB H 2.00 . 1 267 . 27 ILE HG12 H 1.13 . 1 268 . 27 ILE HG13 H 1.13 . 1 269 . 27 ILE HG2 H 0.74 . 1 270 . 27 ILE HD1 H 0.85 . 1 271 . 27 ILE CA C 66.5 . 1 272 . 27 ILE CB C 37.0 . 1 273 . 27 ILE CG1 C 29.0 . 1 274 . 27 ILE CG2 C 17.2 . 1 275 . 27 ILE CD1 C 16.0 . 1 276 . 27 ILE N N 122.7 . 1 277 . 28 LEU H H 7.25 . 1 278 . 28 LEU HA H 3.44 . 1 279 . 28 LEU HB2 H 1.83 . 2 280 . 28 LEU HB3 H 0.87 . 2 281 . 28 LEU HG H 1.03 . 1 282 . 28 LEU HD1 H 0.52 . 2 283 . 28 LEU HD2 H 0.09 . 2 284 . 28 LEU CA C 58.1 . 1 285 . 28 LEU CB C 40.6 . 1 286 . 28 LEU CG C 26.1 . 1 287 . 28 LEU CD1 C 25.4 . 2 288 . 28 LEU CD2 C 23.1 . 2 289 . 28 LEU N N 120.7 . 1 290 . 29 ASP H H 8.74 . 1 291 . 29 ASP HA H 4.04 . 1 292 . 29 ASP HB2 H 2.63 . 2 293 . 29 ASP HB3 H 2.59 . 2 294 . 29 ASP CA C 57.2 . 1 295 . 29 ASP CB C 40.0 . 1 296 . 29 ASP N N 119.5 . 1 297 . 30 PHE H H 7.71 . 1 298 . 30 PHE HA H 4.40 . 1 299 . 30 PHE HB2 H 3.21 . 1 300 . 30 PHE HB3 H 3.21 . 1 301 . 30 PHE HD1 H 7.28 . 1 302 . 30 PHE HD2 H 7.28 . 1 303 . 30 PHE HE1 H 7.14 . 1 304 . 30 PHE HE2 H 7.14 . 1 305 . 30 PHE HZ H 7.14 . 1 306 . 30 PHE CA C 60.1 . 1 307 . 30 PHE CB C 38.9 . 1 308 . 30 PHE CD1 C 132.2 . 1 309 . 30 PHE CD2 C 132.2 . 1 310 . 30 PHE CE1 C 131.4 . 1 311 . 30 PHE CE2 C 131.4 . 1 312 . 30 PHE CZ C 131.4 . 1 313 . 30 PHE N N 123.0 . 1 314 . 31 MET H H 7.36 . 1 315 . 31 MET HA H 2.63 . 1 316 . 31 MET HB2 H 1.69 . 2 317 . 31 MET HB3 H 0.59 . 2 318 . 31 MET HG2 H 2.20 . 2 319 . 31 MET HG3 H 0.72 . 2 320 . 31 MET HE H 1.71 . 1 321 . 31 MET CA C 59.2 . 1 322 . 31 MET CB C 33.0 . 1 323 . 31 MET CG C 30.7 . 1 324 . 31 MET CE C 17.5 . 1 325 . 31 MET N N 118.7 . 1 326 . 32 LYS H H 7.73 . 1 327 . 32 LYS HA H 3.40 . 1 328 . 32 LYS HB2 H 1.79 . 2 329 . 32 LYS HB3 H 1.50 . 2 330 . 32 LYS HG2 H 1.52 . 2 331 . 32 LYS HG3 H 0.86 . 2 332 . 32 LYS HD2 H 1.59 . 2 333 . 32 LYS HD3 H 1.50 . 2 334 . 32 LYS HE2 H 2.62 . 2 335 . 32 LYS HE3 H 2.58 . 2 336 . 32 LYS CA C 60.5 . 1 337 . 32 LYS CB C 32.6 . 1 338 . 32 LYS CG C 26.1 . 1 339 . 32 LYS CD C 29.7 . 1 340 . 32 LYS CE C 41.9 . 1 341 . 32 LYS N N 116.8 . 1 342 . 33 ASP H H 7.87 . 1 343 . 33 ASP HA H 4.12 . 1 344 . 33 ASP HB2 H 2.38 . 1 345 . 33 ASP HB3 H 2.38 . 1 346 . 33 ASP CA C 57.4 . 1 347 . 33 ASP CB C 41.1 . 1 348 . 33 ASP N N 120.3 . 1 349 . 34 VAL H H 7.72 . 1 350 . 34 VAL HA H 2.96 . 1 351 . 34 VAL HB H 1.71 . 1 352 . 34 VAL HG1 H 0.68 . 1 353 . 34 VAL HG2 H 0.28 . 1 354 . 34 VAL CA C 66.6 . 1 355 . 34 VAL CB C 31.0 . 1 356 . 34 VAL CG1 C 21.6 . 1 357 . 34 VAL CG2 C 22.9 . 1 358 . 34 VAL N N 119.3 . 1 359 . 35 MET H H 7.36 . 1 360 . 35 MET HA H 3.10 . 1 361 . 35 MET HB2 H 1.84 . 2 362 . 35 MET HB3 H 1.56 . 2 363 . 35 MET HG2 H 2.20 . 2 364 . 35 MET HG3 H 0.42 . 2 365 . 35 MET HE H 1.71 . 1 366 . 35 MET CA C 59.8 . 1 367 . 35 MET CB C 34.5 . 1 368 . 35 MET CG C 32.0 . 1 369 . 35 MET CE C 17.5 . 1 370 . 35 MET N N 115.6 . 1 371 . 36 LYS H H 8.25 . 1 372 . 36 LYS HA H 3.88 . 1 373 . 36 LYS HB2 H 1.83 . 1 374 . 36 LYS HB3 H 1.83 . 1 375 . 36 LYS HG2 H 1.58 . 2 376 . 36 LYS HG3 H 1.37 . 2 377 . 36 LYS HD2 H 1.58 . 1 378 . 36 LYS HD3 H 1.58 . 1 379 . 36 LYS HE2 H 2.83 . 2 380 . 36 LYS HE3 H 2.71 . 2 381 . 36 LYS CA C 59.9 . 1 382 . 36 LYS CB C 32.1 . 1 383 . 36 LYS CG C 26.0 . 1 384 . 36 LYS CD C 29.1 . 1 385 . 36 LYS CE C 42.0 . 1 386 . 36 LYS N N 120.1 . 1 387 . 37 LYS H H 7.88 . 1 388 . 37 LYS HA H 3.99 . 1 389 . 37 LYS HB2 H 1.48 . 2 390 . 37 LYS HB3 H 1.43 . 2 391 . 37 LYS HG2 H 1.21 . 1 392 . 37 LYS HG3 H 1.21 . 1 393 . 37 LYS HD2 H 1.10 . 1 394 . 37 LYS HD3 H 1.10 . 1 395 . 37 LYS HE2 H 2.76 . 1 396 . 37 LYS HE3 H 2.76 . 1 397 . 37 LYS CA C 58.3 . 1 398 . 37 LYS CB C 32.7 . 1 399 . 37 LYS CG C 25.9 . 1 400 . 37 LYS CD C 28.1 . 1 401 . 37 LYS CE C 42.0 . 1 402 . 37 LYS N N 120.7 . 1 403 . 38 LEU H H 7.50 . 1 404 . 38 LEU HA H 4.57 . 1 405 . 38 LEU HB2 H 1.72 . 1 406 . 38 LEU HB3 H 1.72 . 1 407 . 38 LEU HG H 1.61 . 1 408 . 38 LEU HD1 H 0.55 . 2 409 . 38 LEU HD2 H 0.66 . 2 410 . 38 LEU CA C 53.4 . 1 411 . 38 LEU CB C 40.7 . 1 412 . 38 LEU CG C 26.4 . 1 413 . 38 LEU CD1 C 24.9 . 2 414 . 38 LEU CD2 C 22.7 . 2 415 . 38 LEU N N 120.0 . 1 416 . 39 SER H H 7.27 . 1 417 . 39 SER HA H 4.33 . 1 418 . 39 SER HB2 H 4.08 . 1 419 . 39 SER HB3 H 4.08 . 1 420 . 39 SER CA C 60.4 . 1 421 . 39 SER CB C 63.6 . 1 422 . 39 SER N N 117.3 . 1 423 . 40 ASN H H 8.72 . 1 424 . 40 ASN HA H 4.96 . 1 425 . 40 ASN HB2 H 2.95 . 1 426 . 40 ASN HB3 H 2.95 . 1 427 . 40 ASN HD21 H 7.66 . 2 428 . 40 ASN HD22 H 6.86 . 2 429 . 40 ASN CA C 53.3 . 1 430 . 40 ASN CB C 37.9 . 1 431 . 40 ASN N N 121.5 . 1 432 . 40 ASN ND2 N 114.4 . 1 433 . 41 THR H H 7.95 . 1 434 . 41 THR HA H 4.77 . 1 435 . 41 THR HB H 4.63 . 1 436 . 41 THR HG2 H 1.18 . 1 437 . 41 THR CA C 61.9 . 1 438 . 41 THR CB C 71.2 . 1 439 . 41 THR CG2 C 20.8 . 1 440 . 41 THR N N 111.9 . 1 441 . 42 SER H H 8.65 . 1 442 . 42 SER HA H 4.74 . 1 443 . 42 SER HB2 H 4.01 . 1 444 . 42 SER HB3 H 4.01 . 1 445 . 42 SER CA C 58.7 . 1 446 . 42 SER CB C 63.0 . 1 447 . 42 SER N N 115.4 . 1 448 . 43 TYR H H 8.36 . 1 449 . 43 TYR HA H 5.08 . 1 450 . 43 TYR HB2 H 2.95 . 2 451 . 43 TYR HB3 H 2.07 . 2 452 . 43 TYR HD1 H 6.89 . 1 453 . 43 TYR HD2 H 6.89 . 1 454 . 43 TYR HE1 H 6.67 . 1 455 . 43 TYR HE2 H 6.67 . 1 456 . 43 TYR CA C 57.8 . 1 457 . 43 TYR CB C 39.2 . 1 458 . 43 TYR CD1 C 132.3 . 1 459 . 43 TYR CD2 C 132.3 . 1 460 . 43 TYR CE1 C 118.2 . 1 461 . 43 TYR CE2 C 118.2 . 1 462 . 43 TYR N N 125.3 . 1 463 . 44 GLN H H 8.08 . 1 464 . 44 GLN HA H 4.48 . 1 465 . 44 GLN HB2 H 2.17 . 2 466 . 44 GLN HB3 H 2.12 . 2 467 . 44 GLN HG2 H 2.37 . 2 468 . 44 GLN HG3 H 2.22 . 2 469 . 44 GLN HE21 H 6.95 . 2 470 . 44 GLN HE22 H 6.67 . 2 471 . 44 GLN CA C 54.8 . 1 472 . 44 GLN CB C 32.4 . 1 473 . 44 GLN CG C 34.2 . 1 474 . 44 GLN N N 117.4 . 1 475 . 45 PHE H H 5.48 . 1 476 . 45 PHE HA H 6.23 . 1 477 . 45 PHE HB2 H 3.16 . 2 478 . 45 PHE HB3 H 2.24 . 2 479 . 45 PHE HD1 H 6.43 . 1 480 . 45 PHE HD2 H 6.43 . 1 481 . 45 PHE HE1 H 6.98 . 1 482 . 45 PHE HE2 H 6.98 . 1 483 . 45 PHE HZ H 7.07 . 1 484 . 45 PHE CA C 56.8 . 1 485 . 45 PHE CB C 45.1 . 1 486 . 45 PHE CD1 C 133.2 . 1 487 . 45 PHE CD2 C 133.2 . 1 488 . 45 PHE CE1 C 130.4 . 1 489 . 45 PHE CE2 C 130.4 . 1 490 . 45 PHE CZ C 130.2 . 1 491 . 45 PHE N N 117.7 . 1 492 . 46 ALA H H 7.99 . 1 493 . 46 ALA HA H 3.89 . 1 494 . 46 ALA HB H 0.27 . 1 495 . 46 ALA CA C 50.5 . 1 496 . 46 ALA CB C 21.5 . 1 497 . 46 ALA N N 118.5 . 1 498 . 47 ALA H H 7.39 . 1 499 . 47 ALA HA H 5.64 . 1 500 . 47 ALA HB H 1.17 . 1 501 . 47 ALA CA C 50.8 . 1 502 . 47 ALA CB C 23.9 . 1 503 . 47 ALA N N 118.3 . 1 504 . 48 VAL H H 9.57 . 1 505 . 48 VAL HA H 4.94 . 1 506 . 48 VAL HB H 1.92 . 1 507 . 48 VAL HG1 H 1.00 . 2 508 . 48 VAL HG2 H 0.71 . 2 509 . 48 VAL CA C 59.7 . 1 510 . 48 VAL CB C 36.2 . 1 511 . 48 VAL CG1 C 22.4 . 2 512 . 48 VAL CG2 C 20.6 . 2 513 . 48 VAL N N 125.1 . 1 514 . 49 GLN H H 8.72 . 1 515 . 49 GLN HA H 3.92 . 1 516 . 49 GLN HB2 H 1.71 . 1 517 . 49 GLN HB3 H 1.71 . 1 518 . 49 GLN HG2 H 2.32 . 1 519 . 49 GLN HG3 H 2.32 . 1 520 . 49 GLN HE21 H 7.61 . 2 521 . 49 GLN HE22 H 7.48 . 2 522 . 49 GLN CA C 53.3 . 1 523 . 49 GLN CB C 30.3 . 1 524 . 49 GLN CG C 35.4 . 1 525 . 49 GLN N N 129.7 . 1 526 . 50 PHE H H 8.79 . 1 527 . 50 PHE HA H 5.61 . 1 528 . 50 PHE HB2 H 2.91 . 2 529 . 50 PHE HB3 H 2.70 . 2 530 . 50 PHE HD1 H 6.72 . 1 531 . 50 PHE HD2 H 6.72 . 1 532 . 50 PHE HE1 H 6.85 . 1 533 . 50 PHE HE2 H 6.85 . 1 534 . 50 PHE CA C 54.17 . 1 535 . 50 PHE CB C 45.5 . 1 536 . 50 PHE N N 124.8 . 1 537 . 51 SER H H 8.33 . 1 538 . 51 SER HA H 4.51 . 1 539 . 51 SER HB2 H 3.67 . 2 540 . 51 SER HB3 H 3.50 . 2 541 . 51 SER HG H 5.63 . 1 542 . 51 SER CA C 58.3 . 1 543 . 51 SER CB C 62.3 . 1 544 . 51 SER N N 117.5 . 1 545 . 52 THR H H 7.67 . 1 546 . 52 THR HA H 4.37 . 1 547 . 52 THR HB H 3.93 . 1 548 . 52 THR HG1 H 5.82 . 1 549 . 52 THR HG2 H 1.13 . 1 550 . 52 THR CA C 65.0 . 1 551 . 52 THR CB C 68.4 . 1 552 . 52 THR CG2 C 22.0 . 1 553 . 52 THR N N 124.3 . 1 554 . 53 SER H H 8.87 . 1 555 . 53 SER HA H 3.41 . 1 556 . 53 SER HB2 H 3.44 . 1 557 . 53 SER HB3 H 3.44 . 1 558 . 53 SER HG H 5.79 . 1 559 . 53 SER CA C 54.4 . 1 560 . 53 SER CB C 63.5 . 1 561 . 53 SER N N 118.9 . 1 562 . 54 TYR H H 7.14 . 1 563 . 54 TYR HA H 5.15 . 1 564 . 54 TYR HB2 H 2.12 . 2 565 . 54 TYR HB3 H 1.37 . 2 566 . 54 TYR HD1 H 6.53 . 1 567 . 54 TYR HD2 H 6.53 . 1 568 . 54 TYR HE1 H 6.69 . 1 569 . 54 TYR HE2 H 6.69 . 1 570 . 54 TYR CA C 53.7 . 1 571 . 54 TYR CB C 38.8 . 1 572 . 54 TYR CD1 C 132.7 . 1 573 . 54 TYR CD2 C 132.7 . 1 574 . 54 TYR CE1 C 118.0 . 1 575 . 54 TYR CE2 C 118.0 . 1 576 . 54 TYR N N 120.0 . 1 577 . 55 LYS H H 8.64 . 1 578 . 55 LYS HA H 4.52 . 1 579 . 55 LYS HB2 H 1.57 . 1 580 . 55 LYS HB3 H 1.42 . 1 581 . 55 LYS HG2 H 1.22 . 2 582 . 55 LYS HG3 H 0.93 . 2 583 . 55 LYS HD2 H 1.62 . 2 584 . 55 LYS HD3 H 1.51 . 2 585 . 55 LYS HE2 H 3.08 . 2 586 . 55 LYS HE3 H 2.96 . 2 587 . 55 LYS CA C 54.8 . 1 588 . 55 LYS CB C 37.9 . 1 589 . 55 LYS CG C 24.9 . 1 590 . 55 LYS CD C 29.2 . 1 591 . 55 LYS CE C 42.4 . 1 592 . 55 LYS N N 125.0 . 1 593 . 56 THR H H 9.47 . 1 594 . 56 THR HA H 4.35 . 1 595 . 56 THR HB H 4.27 . 1 596 . 56 THR HG2 H 1.06 . 1 597 . 56 THR CA C 63.5 . 1 598 . 56 THR CB C 67.8 . 1 599 . 56 THR CG2 C 22.1 . 1 600 . 56 THR N N 127.7 . 1 601 . 57 GLU H H 9.40 . 1 602 . 57 GLU HA H 4.96 . 1 603 . 57 GLU HB2 H 1.62 . 1 604 . 57 GLU HB3 H 2.26 . 1 605 . 57 GLU HG2 H 2.69 . 2 606 . 57 GLU HG3 H 2.45 . 2 607 . 57 GLU CA C 57.0 . 1 608 . 57 GLU CB C 28.8 . 1 609 . 57 GLU CG C 33.8 . 1 610 . 57 GLU N N 134.4 . 1 611 . 58 PHE H H 7.42 . 1 612 . 58 PHE HA H 4.91 . 1 613 . 58 PHE HB2 H 3.64 . 2 614 . 58 PHE HB3 H 3.36 . 2 615 . 58 PHE HD1 H 6.97 . 1 616 . 58 PHE HD2 H 6.97 . 1 617 . 58 PHE HE1 H 7.03 . 1 618 . 58 PHE HE2 H 7.03 . 1 619 . 58 PHE HZ H 6.94 . 1 620 . 58 PHE CA C 58.1 . 1 621 . 58 PHE CB C 40.1 . 1 622 . 58 PHE CD1 C 133.2 . 1 623 . 58 PHE CD2 C 133.2 . 1 624 . 58 PHE N N 111.8 . 1 625 . 59 ASP H H 9.62 . 1 626 . 59 ASP HA H 4.84 . 1 627 . 59 ASP HB2 H 3.09 . 1 628 . 59 ASP HB3 H 2.86 . 1 629 . 59 ASP CA C 52.6 . 1 630 . 59 ASP CB C 43.6 . 1 631 . 59 ASP N N 123.5 . 1 632 . 60 PHE H H 7.79 . 1 633 . 60 PHE HA H 4.99 . 1 634 . 60 PHE HB2 H 3.12 . 2 635 . 60 PHE HB3 H 3.04 . 2 636 . 60 PHE HD1 H 7.04 . 1 637 . 60 PHE HD2 H 7.04 . 1 638 . 60 PHE HE1 H 6.98 . 1 639 . 60 PHE HE2 H 6.98 . 1 640 . 60 PHE HZ H 6.90 . 1 641 . 60 PHE CA C 60.6 . 1 642 . 60 PHE CB C 38.1 . 1 643 . 60 PHE CD1 C 133.2 . 1 644 . 60 PHE CD2 C 133.2 . 1 645 . 60 PHE CE1 C 132.6 . 1 646 . 60 PHE CE2 C 132.6 . 1 647 . 60 PHE CZ C 130.3 . 1 648 . 61 SER H H 8.34 . 1 649 . 61 SER HA H 4.30 . 1 650 . 61 SER HB2 H 3.94 . 2 651 . 61 SER HB3 H 3.81 . 2 652 . 61 SER CA C 61.1 . 1 653 . 61 SER CB C 62.4 . 1 654 . 61 SER N N 115.2 . 1 655 . 62 ASP H H 8.28 . 1 656 . 62 ASP HA H 4.59 . 1 657 . 62 ASP HB2 H 3.64 . 1 658 . 62 ASP HB3 H 2.93 . 1 659 . 62 ASP CA C 57.5 . 1 660 . 62 ASP CB C 41.7 . 1 661 . 62 ASP N N 125.4 . 1 662 . 63 TYR H H 8.57 . 1 663 . 63 TYR HA H 4.06 . 1 664 . 63 TYR HB2 H 3.97 . 2 665 . 63 TYR HB3 H 3.81 . 2 666 . 63 TYR HD1 H 7.06 . 1 667 . 63 TYR HD2 H 7.06 . 1 668 . 63 TYR HE1 H 6.75 . 1 669 . 63 TYR HE2 H 6.75 . 1 670 . 63 TYR CA C 62.8 . 1 671 . 63 TYR CB C 62.8 . 1 672 . 63 TYR CD1 C 133.1 . 1 673 . 63 TYR CD2 C 133.1 . 1 674 . 63 TYR CE1 C 118.1 . 1 675 . 63 TYR CE2 C 118.1 . 1 676 . 63 TYR N N 121.6 . 1 677 . 64 VAL H H 8.40 . 1 678 . 64 VAL HA H 3.42 . 1 679 . 64 VAL HB H 2.17 . 1 680 . 64 VAL HG1 H 1.05 . 1 681 . 64 VAL HG2 H 1.29 . 1 682 . 64 VAL CA C 65.9 . 1 683 . 64 VAL CB C 31.8 . 1 684 . 64 VAL CG1 C 21.6 . 1 685 . 64 VAL CG2 C 22.7 . 1 686 . 64 VAL N N 117.7 . 1 687 . 65 LYS H H 7.52 . 1 688 . 65 LYS HA H 3.84 . 1 689 . 65 LYS HB2 H 1.64 . 2 690 . 65 LYS HB3 H 1.40 . 2 691 . 65 LYS HG2 H 0.87 . 2 692 . 65 LYS HG3 H 0.40 . 2 693 . 65 LYS HD2 H 1.34 . 1 694 . 65 LYS HD3 H 1.34 . 1 695 . 65 LYS HE2 H 2.62 . 2 696 . 65 LYS HE3 H 2.54 . 2 697 . 65 LYS CA C 58.9 . 1 698 . 65 LYS CB C 32.8 . 1 699 . 65 LYS CG C 24.3 . 1 700 . 65 LYS CD C 29.0 . 1 701 . 65 LYS CE C 41.9 . 1 702 . 65 LYS N N 119.3 . 1 703 . 66 TRP H H 7.92 . 1 704 . 66 TRP HA H 4.70 . 1 705 . 66 TRP HB2 H 2.93 . 1 706 . 66 TRP HB3 H 3.20 . 1 707 . 66 TRP HD1 H 7.38 . 1 708 . 66 TRP HE1 H 10.33 . 1 709 . 66 TRP HE3 H 7.68 . 1 710 . 66 TRP HZ2 H 7.45 . 1 711 . 66 TRP HZ3 H 7.16 . 1 712 . 66 TRP HH2 H 7.21 . 1 713 . 66 TRP CA C 58.0 . 1 714 . 66 TRP CB C 31.2 . 1 715 . 66 TRP CD1 C 128.2 . 1 716 . 66 TRP CE3 C 120.8 . 1 717 . 66 TRP CZ2 C 114.4 . 1 718 . 66 TRP CZ3 C 122.0 . 1 719 . 66 TRP CH2 C 124.6 . 1 720 . 66 TRP N N 116.5 . 1 721 . 66 TRP NE1 N 130.7 . 1 722 . 67 LYS H H 8.70 . 1 723 . 67 LYS HA H 3.23 . 1 724 . 67 LYS HB2 H 1.80 . 1 725 . 67 LYS HB3 H 1.80 . 1 726 . 67 LYS HG2 H 1.21 . 2 727 . 67 LYS HG3 H 1.07 . 2 728 . 67 LYS HD2 H 1.62 . 2 729 . 67 LYS HD3 H 1.53 . 2 730 . 67 LYS HE2 H 3.08 . 1 731 . 67 LYS HE3 H 3.08 . 1 732 . 67 LYS CA C 58.3 . 1 733 . 67 LYS CB C 31.1 . 1 734 . 67 LYS CG C 25.0 . 1 735 . 67 LYS CD C 28.9 . 1 736 . 67 LYS CE C 42.3 . 1 737 . 67 LYS N N 117.9 . 1 738 . 68 ASP H H 6.85 . 1 739 . 68 ASP HA H 4.98 . 1 740 . 68 ASP HB2 H 2.62 . 1 741 . 68 ASP HB3 H 2.62 . 1 742 . 68 ASP CA C 50.7 . 1 743 . 68 ASP CB C 42.3 . 1 744 . 68 ASP N N 117.0 . 1 745 . 69 PRO HA H 3.79 . 1 746 . 69 PRO HB2 H 1.74 . 1 747 . 69 PRO HB3 H 2.29 . 1 748 . 69 PRO HG2 H 2.00 . 2 749 . 69 PRO HG3 H 1.87 . 2 750 . 69 PRO HD2 H 3.94 . 2 751 . 69 PRO HD3 H 3.87 . 2 752 . 69 PRO CA C 64.9 . 1 753 . 69 PRO CB C 32.9 . 1 754 . 69 PRO CG C 28.3 . 1 755 . 69 PRO CD C 50.4 . 1 756 . 70 ASP H H 7.67 . 1 757 . 70 ASP HA H 4.03 . 1 758 . 70 ASP HB2 H 2.64 . 2 759 . 70 ASP HB3 H 2.46 . 2 760 . 70 ASP CA C 57.0 . 1 761 . 70 ASP CB C 40.2 . 1 762 . 70 ASP N N 114.8 . 1 763 . 71 ALA H H 7.23 . 1 764 . 71 ALA HA H 3.81 . 1 765 . 71 ALA HB H 1.11 . 1 766 . 71 ALA CA C 54.1 . 1 767 . 71 ALA CB C 18.1 . 1 768 . 71 ALA N N 123.2 . 1 769 . 72 LEU H H 7.77 . 1 770 . 72 LEU HA H 3.76 . 1 771 . 72 LEU HB2 H 1.00 . 1 772 . 72 LEU HB3 H 0.54 . 1 773 . 72 LEU HG H 1.41 . 1 774 . 72 LEU HD1 H 0.28 . 2 775 . 72 LEU HD2 H 0.66 . 2 776 . 72 LEU CA C 56.7 . 1 777 . 72 LEU CB C 41.6 . 1 778 . 72 LEU CG C 26.3 . 1 779 . 72 LEU CD1 C 26.3 . 2 780 . 72 LEU CD2 C 22.0 . 2 781 . 72 LEU N N 117.5 . 1 782 . 73 LEU H H 6.82 . 1 783 . 73 LEU HA H 4.65 . 1 784 . 73 LEU HB2 H 1.68 . 1 785 . 73 LEU HB3 H 1.48 . 1 786 . 73 LEU HG H 1.49 . 1 787 . 73 LEU HD1 H 0.64 . 2 788 . 73 LEU HD2 H 0.82 . 2 789 . 73 LEU CA C 53.5 . 1 790 . 73 LEU CB C 41.7 . 1 791 . 73 LEU CG C 26.2 . 1 792 . 73 LEU CD1 C 25.9 . 2 793 . 73 LEU CD2 C 22.8 . 2 794 . 73 LEU N N 115.2 . 1 795 . 74 LYS H H 6.88 . 1 796 . 74 LYS HA H 3.86 . 1 797 . 74 LYS HB2 H 1.86 . 2 798 . 74 LYS HB3 H 1.34 . 2 799 . 74 LYS HG2 H 1.02 . 2 800 . 74 LYS HG3 H 0.77 . 2 801 . 74 LYS HD2 H 1.43 . 1 802 . 74 LYS HD3 H 1.43 . 1 803 . 74 LYS HE2 H 2.77 . 1 804 . 74 LYS HE3 H 2.77 . 1 805 . 74 LYS CA C 58.7 . 1 806 . 74 LYS CB C 32.6 . 1 807 . 74 LYS CG C 23.5 . 1 808 . 74 LYS CD C 29.0 . 1 809 . 74 LYS CE C 41.8 . 1 810 . 74 LYS N N 121.5 . 1 811 . 75 HIS H H 8.62 . 1 812 . 75 HIS HA H 4.74 . 1 813 . 75 HIS HB2 H 2.99 . 1 814 . 75 HIS HB3 H 3.28 . 1 815 . 75 HIS HD2 H 7.03 . 1 816 . 75 HIS HE1 H 7.74 . 1 817 . 75 HIS CA C 55.2 . 1 818 . 75 HIS CB C 30.1 . 1 819 . 75 HIS CD2 C 120.6 . 1 820 . 75 HIS CE1 C 138.9 . 1 821 . 75 HIS N N 116.9 . 1 822 . 76 VAL H H 6.94 . 1 823 . 76 VAL HA H 3.70 . 1 824 . 76 VAL HB H 1.98 . 1 825 . 76 VAL HG1 H 1.22 . 1 826 . 76 VAL HG2 H 1.07 . 1 827 . 76 VAL CA C 63.9 . 1 828 . 76 VAL CB C 32.0 . 1 829 . 76 VAL CG1 C 22.7 . 1 830 . 76 VAL CG2 C 22.7 . 1 831 . 76 VAL N N 122.8 . 1 832 . 77 LYS H H 9.51 . 1 833 . 77 LYS HA H 4.67 . 1 834 . 77 LYS HB2 H 1.72 . 1 835 . 77 LYS HB3 H 1.72 . 1 836 . 77 LYS HG2 H 1.44 . 2 837 . 77 LYS HG3 H 1.35 . 2 838 . 77 LYS HD2 H 1.66 . 1 839 . 77 LYS HD3 H 1.66 . 1 840 . 77 LYS HE2 H 3.00 . 1 841 . 77 LYS HE3 H 3.00 . 1 842 . 77 LYS CA C 54.0 . 1 843 . 77 LYS CB C 34.2 . 1 844 . 77 LYS CG C 24.3 . 1 845 . 77 LYS CD C 28.8 . 1 846 . 77 LYS CE C 42.1 . 1 847 . 77 LYS N N 131.6 . 1 848 . 78 HIS H H 8.58 . 1 849 . 78 HIS HA H 4.16 . 1 850 . 78 HIS HB2 H 2.58 . 2 851 . 78 HIS HB3 H 2.00 . 2 852 . 78 HIS HD2 H 6.64 . 1 853 . 78 HIS HE1 H 7.74 . 1 854 . 78 HIS CA C 54.6 . 1 855 . 78 HIS CB C 32.0 . 1 856 . 78 HIS CD2 C 114.5 . 1 857 . 78 HIS CE1 C 138.9 . 1 858 . 78 HIS N N 130.6 . 1 859 . 79 MET H H 9.32 . 1 860 . 79 MET HA H 3.68 . 1 861 . 79 MET HB2 H 1.87 . 2 862 . 79 MET HB3 H 1.80 . 2 863 . 79 MET HG2 H 2.72 . 2 864 . 79 MET HG3 H 2.46 . 2 865 . 79 MET HE H 1.78 . 1 866 . 79 MET CA C 60.6 . 1 867 . 79 MET CB C 33.5 . 1 868 . 79 MET CG C 35.0 . 1 869 . 79 MET CE C 18.8 . 1 870 . 79 MET N N 131.8 . 1 871 . 80 LEU H H 8.37 . 1 872 . 80 LEU HA H 2.88 . 1 873 . 80 LEU HB2 H 1.51 . 1 874 . 80 LEU HB3 H 1.51 . 1 875 . 80 LEU HG H 0.07 . 1 876 . 80 LEU HD1 H 0.44 . 2 877 . 80 LEU HD2 H 0.31 . 2 878 . 80 LEU CA C 55.6 . 1 879 . 80 LEU CB C 39.2 . 1 880 . 80 LEU CG C 26.1 . 1 881 . 80 LEU CD1 C 25.5 . 2 882 . 80 LEU CD2 C 25.2 . 2 883 . 80 LEU N N 114.2 . 1 884 . 81 LEU H H 6.97 . 1 885 . 81 LEU HA H 4.84 . 1 886 . 81 LEU HB2 H 1.49 . 1 887 . 81 LEU HB3 H 1.76 . 1 888 . 81 LEU HG H 1.47 . 1 889 . 81 LEU HD1 H 0.87 . 2 890 . 81 LEU HD2 H 0.82 . 2 891 . 81 LEU CA C 54.7 . 1 892 . 81 LEU CB C 43.0 . 1 893 . 81 LEU CG C 25.5 . 1 894 . 81 LEU CD1 C 26.4 . 2 895 . 81 LEU CD2 C 22.8 . 2 896 . 81 LEU N N 122.0 . 1 897 . 82 LEU H H 7.28 . 1 898 . 82 LEU HA H 4.51 . 1 899 . 82 LEU HB2 H 1.81 . 2 900 . 82 LEU HB3 H 1.56 . 2 901 . 82 LEU HG H 1.51 . 1 902 . 82 LEU HD1 H 0.96 . 2 903 . 82 LEU HD2 H 0.82 . 2 904 . 82 LEU CA C 54.6 . 1 905 . 82 LEU CB C 39.4 . 1 906 . 82 LEU CG C 26.8 . 1 907 . 82 LEU CD1 C 25.3 . 2 908 . 82 LEU CD2 C 21.9 . 2 909 . 82 LEU N N 122.6 . 1 910 . 83 THR H H 7.82 . 1 911 . 83 THR HA H 4.34 . 1 912 . 83 THR HB H 4.43 . 1 913 . 83 THR HG1 H 5.64 . 1 914 . 83 THR HG2 H 1.34 . 1 915 . 83 THR CA C 59.7 . 1 916 . 83 THR CB C 69.8 . 1 917 . 83 THR CG2 C 22.1 . 1 918 . 83 THR N N 118.7 . 1 919 . 84 ASN H H 9.14 . 1 920 . 84 ASN HA H 5.25 . 1 921 . 84 ASN HB2 H 3.39 . 2 922 . 84 ASN HB3 H 3.11 . 2 923 . 84 ASN HD21 H 8.39 . 2 924 . 84 ASN HD22 H 7.18 . 2 925 . 84 ASN CA C 52.7 . 1 926 . 84 ASN CB C 36.4 . 1 927 . 84 ASN N N 129.8 . 1 928 . 85 THR H H 8.68 . 1 929 . 85 THR HA H 2.97 . 1 930 . 85 THR HB H 3.30 . 1 931 . 85 THR HG1 H 5.40 . 1 932 . 85 THR HG2 H 0.03 . 1 933 . 85 THR CA C 66.2 . 1 934 . 85 THR CB C 68.4 . 1 935 . 85 THR CG2 C 20.7 . 1 936 . 85 THR N N 121.0 . 1 937 . 86 PHE H H 10.43 . 1 938 . 86 PHE HA H 3.63 . 1 939 . 86 PHE HB2 H 3.04 . 1 940 . 86 PHE HB3 H 2.46 . 1 941 . 86 PHE HD1 H 7.21 . 1 942 . 86 PHE HD2 H 7.21 . 1 943 . 86 PHE HE1 H 7.34 . 1 944 . 86 PHE HE2 H 7.34 . 1 945 . 86 PHE HZ H 7.10 . 1 946 . 86 PHE CA C 64.3 . 1 947 . 86 PHE CB C 37.8 . 1 948 . 86 PHE CD1 C 133.2 . 1 949 . 86 PHE CD2 C 133.2 . 1 950 . 86 PHE CE1 C 131.7 . 1 951 . 86 PHE CE2 C 131.7 . 1 952 . 86 PHE CZ C 131.7 . 1 953 . 86 PHE N N 123.1 . 1 954 . 87 GLY H H 10.25 . 1 955 . 87 GLY HA2 H 4.16 . 2 956 . 87 GLY HA3 H 3.70 . 2 957 . 87 GLY CA C 46.3 . 1 958 . 87 GLY N N 112.1 . 1 959 . 88 ALA H H 7.96 . 1 960 . 88 ALA HA H 2.82 . 1 961 . 88 ALA HB H 0.85 . 1 962 . 88 ALA CA C 54.1 . 1 963 . 88 ALA CB C 20.6 . 1 964 . 88 ALA N N 126.6 . 1 965 . 89 ILE H H 7.87 . 1 966 . 89 ILE HA H 3.14 . 1 967 . 89 ILE HB H 1.65 . 1 968 . 89 ILE HG12 H 1.54 . 2 969 . 89 ILE HG13 H 0.33 . 2 970 . 89 ILE HG2 H 0.59 . 1 971 . 89 ILE HD1 H 0.43 . 1 972 . 89 ILE CA C 65.9 . 1 973 . 89 ILE CB C 37.6 . 1 974 . 89 ILE CG1 C 30.1 . 1 975 . 89 ILE CG2 C 17.3 . 1 976 . 89 ILE CD1 C 15.6 . 1 977 . 89 ILE N N 120.5 . 1 978 . 90 ASN H H 7.57 . 1 979 . 90 ASN HA H 4.19 . 1 980 . 90 ASN HB2 H 2.67 . 1 981 . 90 ASN HB3 H 2.67 . 1 982 . 90 ASN HD21 H 7.79 . 2 983 . 90 ASN HD22 H 7.44 . 2 984 . 90 ASN CA C 57.7 . 1 985 . 90 ASN CB C 39.0 . 1 986 . 90 ASN N N 118.7 . 1 987 . 90 ASN ND2 N 115.8 . 1 988 . 91 TYR H H 8.14 . 1 989 . 91 TYR HA H 3.94 . 1 990 . 91 TYR HB2 H 2.79 . 2 991 . 91 TYR HB3 H 2.51 . 2 992 . 91 TYR HD1 H 6.71 . 1 993 . 91 TYR HD2 H 6.71 . 1 994 . 91 TYR HE1 H 6.78 . 1 995 . 91 TYR HE2 H 6.78 . 1 996 . 91 TYR CA C 61.3 . 1 997 . 91 TYR CB C 37.7 . 1 998 . 91 TYR CD1 C 132.7 . 1 999 . 91 TYR CD2 C 132.7 . 1 1000 . 91 TYR CE1 C 118.0 . 1 1001 . 91 TYR CE2 C 118.0 . 1 1002 . 91 TYR N N 123.4 . 1 1003 . 92 VAL H H 8.15 . 1 1004 . 92 VAL HA H 3.30 . 1 1005 . 92 VAL HB H 2.28 . 1 1006 . 92 VAL HG1 H 1.00 . 1 1007 . 92 VAL HG2 H 1.17 . 1 1008 . 92 VAL CA C 66.2 . 1 1009 . 92 VAL CB C 31.1 . 1 1010 . 92 VAL CG1 C 23.3 . 1 1011 . 92 VAL CG2 C 24.6 . 1 1012 . 92 VAL N N 121.1 . 1 1013 . 93 ALA H H 8.08 . 1 1014 . 93 ALA HA H 4.10 . 1 1015 . 93 ALA HB H 1.35 . 1 1016 . 93 ALA CA C 55.2 . 1 1017 . 93 ALA CB C 18.4 . 1 1018 . 93 ALA N N 119.7 . 1 1019 . 94 THR H H 7.75 . 1 1020 . 94 THR HA H 4.35 . 1 1021 . 94 THR HB H 4.14 . 1 1022 . 94 THR HG2 H 1.19 . 1 1023 . 94 THR CA C 63.0 . 1 1024 . 94 THR CB C 70.1 . 1 1025 . 94 THR CG2 C 21.2 . 1 1026 . 94 THR N N 105.8 . 1 1027 . 95 GLU H H 8.50 . 1 1028 . 95 GLU HA H 4.44 . 1 1029 . 95 GLU HB2 H 0.75 . 1 1030 . 95 GLU HB3 H 1.59 . 1 1031 . 95 GLU HG2 H 2.02 . 1 1032 . 95 GLU HG3 H 2.02 . 1 1033 . 95 GLU CA C 55.7 . 1 1034 . 95 GLU CB C 29.5 . 1 1035 . 95 GLU CG C 35.1 . 1 1036 . 95 GLU N N 118.7 . 1 1037 . 96 VAL H H 7.07 . 1 1038 . 96 VAL HA H 4.11 . 1 1039 . 96 VAL HB H 2.13 . 1 1040 . 96 VAL HG1 H 0.35 . 1 1041 . 96 VAL HG2 H 0.66 . 1 1042 . 96 VAL CA C 64.0 . 1 1043 . 96 VAL CB C 31.9 . 1 1044 . 96 VAL CG1 C 21.4 . 1 1045 . 96 VAL CG2 C 23.4 . 1 1046 . 96 VAL N N 118.9 . 1 1047 . 97 PHE H H 7.10 . 1 1048 . 97 PHE HA H 4.59 . 1 1049 . 97 PHE HB2 H 3.26 . 2 1050 . 97 PHE HB3 H 2.76 . 2 1051 . 97 PHE HD1 H 7.20 . 1 1052 . 97 PHE HD2 H 7.20 . 1 1053 . 97 PHE HE1 H 7.15 . 4 1054 . 97 PHE HE2 H 7.15 . 4 1055 . 97 PHE HZ H 7.36 . 4 1056 . 97 PHE CA C 58.4 . 1 1057 . 97 PHE CB C 37.1 . 1 1058 . 97 PHE CD1 C 132.4 . 1 1059 . 97 PHE CD2 C 132.4 . 1 1060 . 97 PHE N N 119.7 . 1 1061 . 98 ARG H H 7.67 . 1 1062 . 98 ARG HA H 4.68 . 1 1063 . 98 ARG HB2 H 2.11 . 2 1064 . 98 ARG HB3 H 1.40 . 2 1065 . 98 ARG HG2 H 1.41 . 2 1066 . 98 ARG HG3 H 1.34 . 2 1067 . 98 ARG HD2 H 3.34 . 2 1068 . 98 ARG HD3 H 3.13 . 2 1069 . 98 ARG HE H 7.42 . 1 1070 . 98 ARG CA C 53.9 . 1 1071 . 98 ARG CB C 33.2 . 1 1072 . 98 ARG CG C 26.7 . 1 1073 . 98 ARG CD C 42.9 . 1 1074 . 98 ARG NE N 85.6 . 1 1075 . 99 GLU H H 9.54 . 1 1076 . 99 GLU HA H 4.44 . 1 1077 . 99 GLU HB2 H 2.04 . 1 1078 . 99 GLU HB3 H 2.04 . 1 1079 . 99 GLU HG2 H 2.30 . 2 1080 . 99 GLU HG3 H 2.26 . 2 1081 . 99 GLU CA C 59.3 . 1 1082 . 99 GLU CB C 29.5 . 1 1083 . 99 GLU CG C 36.4 . 1 1084 . 99 GLU N N 130.8 . 1 1085 . 100 GLU H H 10.22 . 1 1086 . 100 GLU HA H 4.18 . 1 1087 . 100 GLU HB2 H 2.06 . 2 1088 . 100 GLU HB3 H 2.00 . 2 1089 . 100 GLU HG2 H 2.41 . 1 1090 . 100 GLU HG3 H 2.41 . 1 1091 . 100 GLU CA C 59.3 . 1 1092 . 100 GLU CB C 28.3 . 1 1093 . 100 GLU CG C 36.5 . 1 1094 . 100 GLU N N 121.3 . 1 1095 . 101 LEU H H 7.37 . 1 1096 . 101 LEU HA H 4.66 . 1 1097 . 101 LEU HB2 H 2.25 . 2 1098 . 101 LEU HB3 H 1.89 . 2 1099 . 101 LEU HG H 1.57 . 1 1100 . 101 LEU HD1 H 1.08 . 2 1101 . 101 LEU HD2 H 0.96 . 2 1102 . 101 LEU CA C 54.2 . 1 1103 . 101 LEU CB C 41.6 . 1 1104 . 101 LEU CG C 27.9 . 1 1105 . 101 LEU CD1 C 25.9 . 2 1106 . 101 LEU CD2 C 22.6 . 2 1107 . 101 LEU N N 119.9 . 1 1108 . 102 GLY H H 7.86 . 1 1109 . 102 GLY HA2 H 4.39 . 2 1110 . 102 GLY HA3 H 3.72 . 2 1111 . 102 GLY CA C 45.2 . 1 1112 . 102 GLY N N 105.4 . 1 1113 . 103 ALA H H 7.53 . 1 1114 . 103 ALA HA H 3.38 . 1 1115 . 103 ALA HB H 1.15 . 1 1116 . 103 ALA CA C 52.3 . 1 1117 . 103 ALA CB C 18.5 . 1 1118 . 103 ALA N N 125.6 . 1 1119 . 104 ARG H H 10.0 . 1 1120 . 104 ARG HA H 4.60 . 1 1121 . 104 ARG HB2 H 1.74 . 1 1122 . 104 ARG HB3 H 1.74 . 1 1123 . 104 ARG HE H 7.62 . 1 1124 . 104 ARG CA C 53.5 . 1 1125 . 104 ARG CB C 30.2 . 1 1126 . 104 ARG N N 127.3 . 1 1127 . 104 ARG NE N 86.0 . 1 1128 . 105 PRO HA H 4.23 . 1 1129 . 105 PRO HB2 H 1.90 . 1 1130 . 105 PRO HB3 H 2.29 . 1 1131 . 105 PRO HG2 H 1.98 . 1 1132 . 105 PRO HG3 H 1.98 . 1 1133 . 105 PRO HD2 H 3.87 . 2 1134 . 105 PRO HD3 H 3.79 . 2 1135 . 105 PRO CA C 64.5 . 1 1136 . 105 PRO CB C 31.8 . 1 1137 . 105 PRO CG C 27.2 . 1 1138 . 105 PRO CD C 50.9 . 1 1139 . 106 ASP H H 8.20 . 1 1140 . 106 ASP HA H 4.51 . 1 1141 . 106 ASP HB2 H 2.74 . 2 1142 . 106 ASP HB3 H 2.53 . 2 1143 . 106 ASP CA C 52.8 . 1 1144 . 106 ASP CB C 40.1 . 1 1145 . 106 ASP N N 115.2 . 1 1146 . 107 ALA H H 7.20 . 1 1147 . 107 ALA HA H 4.19 . 1 1148 . 107 ALA HB H 1.02 . 1 1149 . 107 ALA CA C 51.4 . 1 1150 . 107 ALA CB C 20.3 . 1 1151 . 107 ALA N N 122.8 . 1 1152 . 108 THR H H 8.28 . 1 1153 . 108 THR HA H 3.99 . 1 1154 . 108 THR HB H 3.82 . 1 1155 . 108 THR HG1 H 5.81 . 1 1156 . 108 THR HG2 H 1.13 . 1 1157 . 108 THR CA C 63.9 . 1 1158 . 108 THR CB C 69.3 . 1 1159 . 108 THR CG2 C 21.9 . 1 1160 . 108 THR N N 121.0 . 1 1161 . 109 LYS H H 8.40 . 1 1162 . 109 LYS HA H 4.73 . 1 1163 . 109 LYS HB2 H 1.42 . 2 1164 . 109 LYS HB3 H 0.64 . 2 1165 . 109 LYS HG2 H 1.25 . 2 1166 . 109 LYS HG3 H 1.05 . 2 1167 . 109 LYS HD2 H 0.76 . 1 1168 . 109 LYS HD3 H 0.76 . 1 1169 . 109 LYS HE2 H 2.67 . 1 1170 . 109 LYS HE3 H 2.67 . 1 1171 . 109 LYS CA C 56.0 . 1 1172 . 109 LYS CB C 33.8 . 1 1173 . 109 LYS CG C 24.0 . 1 1174 . 109 LYS CD C 29.0 . 1 1175 . 109 LYS CE C 41.4 . 1 1176 . 109 LYS N N 129.7 . 1 1177 . 110 VAL H H 8.84 . 1 1178 . 110 VAL HA H 4.93 . 1 1179 . 110 VAL HB H 1.62 . 1 1180 . 110 VAL HG1 H 0.92 . 1 1181 . 110 VAL HG2 H 0.82 . 1 1182 . 110 VAL CA C 60.6 . 1 1183 . 110 VAL CB C 35.5 . 1 1184 . 110 VAL CG1 C 21.3 . 1 1185 . 110 VAL CG2 C 22.6 . 1 1186 . 110 VAL N N 125.5 . 1 1187 . 111 LEU H H 9.72 . 1 1188 . 111 LEU HA H 5.37 . 1 1189 . 111 LEU HB2 H 1.83 . 2 1190 . 111 LEU HB3 H 1.45 . 2 1191 . 111 LEU HG H 1.66 . 1 1192 . 111 LEU HD1 H 0.91 . 1 1193 . 111 LEU HD2 H 0.91 . 1 1194 . 111 LEU CA C 52.7 . 1 1195 . 111 LEU CB C 47.7 . 1 1196 . 111 LEU CG C 27.7 . 1 1197 . 111 LEU CD1 C 26.8 . 1 1198 . 111 LEU CD2 C 26.8 . 1 1199 . 111 LEU N N 131.3 . 1 1200 . 112 ILE H H 9.06 . 1 1201 . 112 ILE HA H 5.15 . 1 1202 . 112 ILE HB H 2.11 . 1 1203 . 112 ILE HG12 H 1.51 . 2 1204 . 112 ILE HG13 H 1.20 . 2 1205 . 112 ILE HG2 H 1.11 . 1 1206 . 112 ILE HD1 H 0.84 . 1 1207 . 112 ILE CA C 59.8 . 1 1208 . 112 ILE CB C 38.5 . 1 1209 . 112 ILE CG1 C 27.3 . 1 1210 . 112 ILE CG2 C 17.1 . 1 1211 . 112 ILE CD1 C 12.8 . 1 1212 . 112 ILE N N 125.7 . 1 1213 . 113 ILE H H 9.26 . 1 1214 . 113 ILE HA H 5.45 . 1 1215 . 113 ILE HB H 1.88 . 1 1216 . 113 ILE HG12 H 1.80 . 2 1217 . 113 ILE HG13 H 0.93 . 2 1218 . 113 ILE HG2 H 0.77 . 1 1219 . 113 ILE HD1 H 0.64 . 1 1220 . 113 ILE CA C 60.2 . 1 1221 . 113 ILE CB C 39.0 . 1 1222 . 113 ILE CG1 C 28.4 . 1 1223 . 113 ILE CG2 C 16.2 . 1 1224 . 113 ILE CD1 C 14.0 . 1 1225 . 113 ILE N N 129.6 . 1 1226 . 114 ILE H H 9.09 . 1 1227 . 114 ILE HA H 5.14 . 1 1228 . 114 ILE HB H 1.90 . 1 1229 . 114 ILE HG12 H 1.86 . 2 1230 . 114 ILE HG13 H 1.05 . 2 1231 . 114 ILE HG2 H 0.98 . 1 1232 . 114 ILE HD1 H 1.13 . 1 1233 . 114 ILE CA C 60.6 . 1 1234 . 114 ILE CB C 40.8 . 1 1235 . 114 ILE CG1 C 28.4 . 1 1236 . 114 ILE CG2 C 19.2 . 1 1237 . 114 ILE CD1 C 15.5 . 1 1238 . 114 ILE N N 128.7 . 1 1239 . 115 THR H H 9.35 . 1 1240 . 115 THR HA H 5.64 . 1 1241 . 115 THR HB H 4.21 . 1 1242 . 115 THR HG2 H 1.34 . 1 1243 . 115 THR CA C 59.5 . 1 1244 . 115 THR CB C 71.2 . 1 1245 . 115 THR CG2 C 17.7 . 1 1246 . 115 THR N N 121.2 . 1 1247 . 116 ASP H H 8.60 . 1 1248 . 116 ASP HA H 5.80 . 1 1249 . 116 ASP HB2 H 3.56 . 2 1250 . 116 ASP HB3 H 2.39 . 2 1251 . 116 ASP CA C 51.6 . 1 1252 . 116 ASP CB C 43.9 . 1 1253 . 116 ASP N N 127.5 . 1 1254 . 117 GLY H H 8.30 . 1 1255 . 117 GLY HA2 H 3.93 . 2 1256 . 117 GLY HA3 H 3.65 . 2 1257 . 117 GLY CA C 45.8 . 1 1258 . 117 GLY N N 115.1 . 1 1259 . 118 GLU H H 8.07 . 1 1260 . 118 GLU HA H 4.30 . 1 1261 . 118 GLU HB2 H 2.29 . 2 1262 . 118 GLU HB3 H 1.87 . 2 1263 . 118 GLU HG2 H 2.60 . 2 1264 . 118 GLU HG3 H 2.29 . 2 1265 . 118 GLU CA C 56.2 . 1 1266 . 118 GLU CB C 30.9 . 1 1267 . 118 GLU CG C 37.2 . 1 1268 . 118 GLU N N 117.2 . 1 1269 . 119 ALA H H 8.56 . 1 1270 . 119 ALA HA H 5.21 . 1 1271 . 119 ALA HB H 2.01 . 1 1272 . 119 ALA CA C 52.5 . 1 1273 . 119 ALA CB C 20.5 . 1 1274 . 119 ALA N N 123.6 . 1 1275 . 120 THR H H 9.24 . 1 1276 . 120 THR HA H 4.51 . 1 1277 . 120 THR HB H 4.80 . 1 1278 . 120 THR HG2 H 1.35 . 1 1279 . 120 THR CA C 61.0 . 1 1280 . 120 THR CB C 69.8 . 1 1281 . 120 THR CG2 C 22.6 . 1 1282 . 120 THR N N 112.2 . 1 1283 . 121 ASP H H 8.39 . 1 1284 . 121 ASP HA H 4.90 . 1 1285 . 121 ASP HB2 H 3.01 . 2 1286 . 121 ASP HB3 H 2.94 . 2 1287 . 121 ASP CA C 51.7 . 1 1288 . 121 ASP CB C 40.7 . 1 1289 . 121 ASP N N 124.4 . 1 1290 . 122 SER H H 7.45 . 1 1291 . 122 SER HA H 3.86 . 1 1292 . 122 SER HB2 H 3.56 . 1 1293 . 122 SER HB3 H 3.56 . 1 1294 . 122 SER CA C 56.7 . 1 1295 . 122 SER CB C 64.5 . 1 1296 . 122 SER N N 110.3 . 1 1297 . 123 GLY H H 6.67 . 1 1298 . 123 GLY HA2 H 4.10 . 2 1299 . 123 GLY HA3 H 3.49 . 2 1300 . 123 GLY CA C 44.7 . 1 1301 . 123 GLY N N 107.0 . 1 1302 . 124 ASN H H 8.65 . 1 1303 . 124 ASN HA H 5.00 . 1 1304 . 124 ASN HB2 H 2.81 . 2 1305 . 124 ASN HB3 H 2.68 . 2 1306 . 124 ASN HD21 H 7.71 . 2 1307 . 124 ASN HD22 H 6.92 . 2 1308 . 124 ASN CA C 52.3 . 1 1309 . 124 ASN CB C 41.9 . 1 1310 . 124 ASN N N 120.9 . 1 1311 . 124 ASN ND2 N 117.4 . 1 1312 . 125 ILE H H 8.93 . 1 1313 . 125 ILE HA H 4.94 . 1 1314 . 125 ILE HB H 2.14 . 1 1315 . 125 ILE HG12 H 1.42 . 2 1316 . 125 ILE HG13 H 1.06 . 2 1317 . 125 ILE HG2 H 0.98 . 1 1318 . 125 ILE HD1 H 0.92 . 1 1319 . 125 ILE CA C 60.1 . 1 1320 . 125 ILE CB C 38.1 . 1 1321 . 125 ILE CG1 C 15.7 . 1 1322 . 125 ILE CG2 C 27.1 . 1 1323 . 125 ILE CD1 C 19.5 . 1 1324 . 125 ILE N N 115.4 . 1 1325 . 126 ASP H H 8.90 . 1 1326 . 126 ASP HA H 4.22 . 1 1327 . 126 ASP HB2 H 2.60 . 1 1328 . 126 ASP HB3 H 2.60 . 1 1329 . 126 ASP CA C 58.0 . 1 1330 . 126 ASP CB C 39.6 . 1 1331 . 126 ASP N N 127.8 . 1 1332 . 127 ALA H H 9.00 . 1 1333 . 127 ALA HA H 4.12 . 1 1334 . 127 ALA HB H 1.34 . 1 1335 . 127 ALA CA C 53.8 . 1 1336 . 127 ALA CB C 18.0 . 1 1337 . 127 ALA N N 121.0 . 1 1338 . 128 ALA H H 7.98 . 1 1339 . 128 ALA HA H 4.42 . 1 1340 . 128 ALA HB H 1.23 . 1 1341 . 128 ALA CA C 50.1 . 1 1342 . 128 ALA CB C 19.7 . 1 1343 . 128 ALA N N 119.1 . 1 1344 . 129 LYS H H 7.25 . 1 1345 . 129 LYS HA H 3.95 . 1 1346 . 129 LYS HB2 H 3.95 . 1 1347 . 129 LYS HB3 H 3.95 . 1 1348 . 129 LYS HG2 H 1.42 . 1 1349 . 129 LYS HG3 H 1.42 . 1 1350 . 129 LYS HD2 H 1.66 . 1 1351 . 129 LYS HD3 H 1.66 . 1 1352 . 129 LYS HE2 H 2.96 . 1 1353 . 129 LYS HE3 H 2.96 . 1 1354 . 129 LYS CA C 59.5 . 1 1355 . 129 LYS CB C 32.2 . 1 1356 . 129 LYS CG C 23.8 . 1 1357 . 129 LYS CD C 29.1 . 1 1358 . 129 LYS CE C 41.8 . 1 1359 . 129 LYS N N 119.7 . 1 1360 . 130 ASP H H 8.49 . 1 1361 . 130 ASP HA H 4.62 . 1 1362 . 130 ASP HB2 H 2.69 . 2 1363 . 130 ASP HB3 H 2.50 . 2 1364 . 130 ASP CA C 54.0 . 1 1365 . 130 ASP CB C 40.1 . 1 1366 . 130 ASP N N 118.6 . 1 1367 . 131 ILE H H 7.51 . 1 1368 . 131 ILE HA H 3.74 . 1 1369 . 131 ILE HB H 1.62 . 1 1370 . 131 ILE HG12 H 1.43 . 2 1371 . 131 ILE HG13 H 0.86 . 2 1372 . 131 ILE HG2 H 0.66 . 1 1373 . 131 ILE HD1 H 0.75 . 1 1374 . 131 ILE CA C 60.4 . 1 1375 . 131 ILE CB C 39.7 . 1 1376 . 131 ILE CG1 C 26.4 . 1 1377 . 131 ILE CG2 C 18.0 . 1 1378 . 131 ILE CD1 C 13.4 . 1 1379 . 131 ILE N N 122.6 . 1 1380 . 132 ILE H H 8.44 . 1 1381 . 132 ILE HA H 3.70 . 1 1382 . 132 ILE HB H 1.97 . 1 1383 . 132 ILE HG12 H 1.61 . 2 1384 . 132 ILE HG13 H 1.14 . 2 1385 . 132 ILE HG2 H 0.89 . 1 1386 . 132 ILE HD1 H 0.81 . 1 1387 . 132 ILE CA C 61.9 . 1 1388 . 132 ILE CB C 37.4 . 1 1389 . 132 ILE CG1 C 27.5 . 1 1390 . 132 ILE CG2 C 18.0 . 1 1391 . 132 ILE CD1 C 12.5 . 1 1392 . 132 ILE N N 131.9 . 1 1393 . 133 ARG H H 8.88 . 1 1394 . 133 ARG HA H 5.20 . 1 1395 . 133 ARG HB2 H 1.84 . 2 1396 . 133 ARG HB3 H 1.59 . 2 1397 . 133 ARG HD2 H 3.08 . 1 1398 . 133 ARG HD3 H 3.08 . 1 1399 . 133 ARG HE H 6.81 . 1 1400 . 133 ARG CA C 55.2 . 1 1401 . 133 ARG CB C 31.6 . 1 1402 . 133 ARG N N 129.7 . 1 1403 . 133 ARG NE N 84.1 . 1 1404 . 134 TYR H H 8.97 . 1 1405 . 134 TYR HA H 5.53 . 1 1406 . 134 TYR HB2 H 3.10 . 2 1407 . 134 TYR HB3 H 2.86 . 2 1408 . 134 TYR HD1 H 6.97 . 1 1409 . 134 TYR HD2 H 6.97 . 1 1410 . 134 TYR HE1 H 6.54 . 1 1411 . 134 TYR HE2 H 6.54 . 1 1412 . 134 TYR CA C 56.7 . 1 1413 . 134 TYR CB C 42.0 . 1 1414 . 134 TYR CD1 C 132.7 . 1 1415 . 134 TYR CD2 C 132.7 . 1 1416 . 134 TYR CE1 C 118.1 . 1 1417 . 134 TYR CE2 C 118.1 . 1 1418 . 134 TYR CZ C 130.0 . 1 1419 . 134 TYR N N 125.9 . 1 1420 . 135 ILE H H 9.13 . 1 1421 . 135 ILE HA H 5.19 . 1 1422 . 135 ILE HB H 1.75 . 1 1423 . 135 ILE HG12 H 1.49 . 2 1424 . 135 ILE HG13 H 1.23 . 2 1425 . 135 ILE HG2 H 1.05 . 1 1426 . 135 ILE HD1 H 0.85 . 1 1427 . 135 ILE CA C 58.5 . 1 1428 . 135 ILE CB C 40.7 . 1 1429 . 135 ILE CG1 C 28.9 . 1 1430 . 135 ILE CG2 C 19.1 . 1 1431 . 135 ILE CD1 C 14.9 . 1 1432 . 135 ILE N N 125.6 . 1 1433 . 136 ILE H H 9.38 . 1 1434 . 136 ILE HA H 4.89 . 1 1435 . 136 ILE HB H 1.87 . 1 1436 . 136 ILE HG12 H 1.59 . 2 1437 . 136 ILE HG13 H 0.88 . 2 1438 . 136 ILE HG2 H 0.54 . 1 1439 . 136 ILE HD1 H 0.74 . 1 1440 . 136 ILE CA C 59.0 . 1 1441 . 136 ILE CB C 39.3 . 1 1442 . 136 ILE CG1 C 27.3 . 1 1443 . 136 ILE CG2 C 17.6 . 1 1444 . 136 ILE CD1 C 14.9 . 1 1445 . 136 ILE N N 129.3 . 1 1446 . 137 GLY H H 8.76 . 1 1447 . 137 GLY HA2 H 4.86 . 2 1448 . 137 GLY HA3 H 2.26 . 2 1449 . 137 GLY CA C 44.0 . 1 1450 . 137 GLY N N 114.8 . 1 1451 . 138 ILE H H 8.44 . 1 1452 . 138 ILE HA H 4.94 . 1 1453 . 138 ILE HB H 0.89 . 1 1454 . 138 ILE HG12 H 1.37 . 2 1455 . 138 ILE HG13 H 0.34 . 2 1456 . 138 ILE HG2 H -0.52 . 1 1457 . 138 ILE HD1 H 0.45 . 1 1458 . 138 ILE CA C 59.6 . 1 1459 . 138 ILE CB C 41.5 . 1 1460 . 138 ILE CG1 C 27.7 . 1 1461 . 138 ILE CG2 C 15.6 . 1 1462 . 138 ILE CD1 C 15.9 . 1 1463 . 138 ILE N N 123.4 . 1 1464 . 139 GLY H H 8.25 . 1 1465 . 139 GLY HA2 H 4.38 . 2 1466 . 139 GLY HA3 H 3.84 . 2 1467 . 139 GLY CA C 44.9 . 1 1468 . 139 GLY N N 111.5 . 1 1469 . 140 LYS H H 8.78 . 1 1470 . 140 LYS HA H 4.02 . 1 1471 . 140 LYS HB2 H 1.77 . 1 1472 . 140 LYS HB3 H 1.77 . 1 1473 . 140 LYS HG2 H 1.37 . 1 1474 . 140 LYS HG3 H 1.37 . 1 1475 . 140 LYS HD2 H 1.75 . 2 1476 . 140 LYS HD3 H 1.60 . 2 1477 . 140 LYS HE2 H 2.94 . 1 1478 . 140 LYS HE3 H 2.94 . 1 1479 . 140 LYS CA C 58.5 . 1 1480 . 140 LYS CB C 32.0 . 1 1481 . 140 LYS CG C 23.5 . 1 1482 . 140 LYS CD C 29.0 . 1 1483 . 140 LYS CE C 41.8 . 1 1484 . 140 LYS N N 120.1 . 1 1485 . 141 HIS H H 9.09 . 1 1486 . 141 HIS HA H 4.33 . 1 1487 . 141 HIS HB2 H 2.78 . 2 1488 . 141 HIS HB3 H 2.64 . 2 1489 . 141 HIS HD2 H 6.83 . 1 1490 . 141 HIS HE1 H 7.74 . 1 1491 . 141 HIS CA C 58.1 . 1 1492 . 141 HIS CB C 28.6 . 1 1493 . 141 HIS CD2 C 120.6 . 1 1494 . 141 HIS CE1 C 138.9 . 1 1495 . 141 HIS N N 120.3 . 1 1496 . 142 PHE H H 7.61 . 1 1497 . 142 PHE HA H 5.56 . 1 1498 . 142 PHE HB2 H 2.44 . 1 1499 . 142 PHE HB3 H 3.47 . 1 1500 . 142 PHE HD1 H 6.79 . 1 1501 . 142 PHE HD2 H 6.79 . 1 1502 . 142 PHE HE1 H 7.01 . 4 1503 . 142 PHE HE2 H 7.01 . 4 1504 . 142 PHE HZ H 7.01 . 4 1505 . 142 PHE CA C 57.0 . 1 1506 . 142 PHE CB C 38.8 . 1 1507 . 142 PHE CD1 C 131.4 . 1 1508 . 142 PHE CD2 C 131.4 . 1 1509 . 142 PHE N N 117.7 . 1 1510 . 143 GLN H H 7.40 . 1 1511 . 143 GLN HA H 4.12 . 1 1512 . 143 GLN HB2 H 2.47 . 2 1513 . 143 GLN HB3 H 2.39 . 2 1514 . 143 GLN HG2 H 2.48 . 2 1515 . 143 GLN HG3 H 2.38 . 2 1516 . 143 GLN HE21 H 6.84 . 2 1517 . 143 GLN HE22 H 7.58 . 2 1518 . 143 GLN CA C 58.1 . 1 1519 . 143 GLN CB C 29.5 . 1 1520 . 143 GLN CG C 34.3 . 1 1521 . 143 GLN N N 118.7 . 1 1522 . 143 GLN NE2 N 113.0 . 1 1523 . 144 THR H H 7.98 . 1 1524 . 144 THR HA H 4.53 . 1 1525 . 144 THR HB H 4.68 . 1 1526 . 144 THR HG2 H 1.31 . 1 1527 . 144 THR CA C 59.7 . 1 1528 . 144 THR CB C 71.1 . 1 1529 . 144 THR CG2 C 21.6 . 1 1530 . 144 THR N N 108.7 . 1 1531 . 145 LYS H H 8.96 . 1 1532 . 145 LYS HA H 3.78 . 1 1533 . 145 LYS HB2 H 1.89 . 2 1534 . 145 LYS HB3 H 1.75 . 2 1535 . 145 LYS HG2 H 1.45 . 2 1536 . 145 LYS HG3 H 1.36 . 2 1537 . 145 LYS HD2 H 1.66 . 1 1538 . 145 LYS HD3 H 1.66 . 1 1539 . 145 LYS HE2 H 3.00 . 1 1540 . 145 LYS HE3 H 3.00 . 1 1541 . 145 LYS CA C 59.3 . 1 1542 . 145 LYS CB C 31.9 . 1 1543 . 145 LYS CG C 24.3 . 1 1544 . 145 LYS CD C 28.9 . 1 1545 . 145 LYS CE C 41.9 . 1 1546 . 145 LYS N N 126.3 . 1 1547 . 146 GLU H H 9.14 . 1 1548 . 146 GLU HA H 3.96 . 1 1549 . 146 GLU HB2 H 1.92 . 1 1550 . 146 GLU HB3 H 1.92 . 1 1551 . 146 GLU HG2 H 2.46 . 2 1552 . 146 GLU HG3 H 2.27 . 2 1553 . 146 GLU CA C 60.4 . 1 1554 . 146 GLU CB C 28.4 . 1 1555 . 146 GLU CG C 36.9 . 1 1556 . 146 GLU N N 118.5 . 1 1557 . 147 SER H H 7.81 . 1 1558 . 147 SER HA H 4.30 . 1 1559 . 147 SER HB2 H 3.96 . 1 1560 . 147 SER HB3 H 3.96 . 1 1561 . 147 SER HG H 5.55 . 1 1562 . 147 SER CA C 61.7 . 1 1563 . 147 SER CB C 62.9 . 1 1564 . 147 SER N N 116.9 . 1 1565 . 148 GLN H H 7.64 . 1 1566 . 148 GLN HA H 4.18 . 1 1567 . 148 GLN HB2 H 2.04 . 2 1568 . 148 GLN HB3 H 1.95 . 2 1569 . 148 GLN HG2 H 2.31 . 2 1570 . 148 GLN HG3 H 2.22 . 2 1571 . 148 GLN HE21 H 8.15 . 2 1572 . 148 GLN HE22 H 7.80 . 2 1573 . 148 GLN CA C 56.8 . 1 1574 . 148 GLN CB C 30.6 . 1 1575 . 148 GLN CG C 36.2 . 1 1576 . 148 GLN N N 125.2 . 1 1577 . 149 GLU H H 7.85 . 1 1578 . 149 GLU HA H 2.88 . 1 1579 . 149 GLU HB2 H 1.88 . 2 1580 . 149 GLU HB3 H 1.74 . 2 1581 . 149 GLU HG2 H 2.35 . 2 1582 . 149 GLU HG3 H 1.84 . 2 1583 . 149 GLU CA C 58.2 . 1 1584 . 149 GLU CB C 28.5 . 1 1585 . 149 GLU CG C 37.1 . 1 1586 . 149 GLU N N 116.5 . 1 1587 . 150 THR H H 7.55 . 1 1588 . 150 THR HA H 4.11 . 1 1589 . 150 THR HB H 4.34 . 1 1590 . 150 THR HG2 H 1.56 . 1 1591 . 150 THR CA C 65.2 . 1 1592 . 150 THR CB C 69.0 . 1 1593 . 150 THR CG2 C 21.5 . 1 1594 . 150 THR N N 113.0 . 1 1595 . 151 LEU H H 7.35 . 1 1596 . 151 LEU HA H 4.37 . 1 1597 . 151 LEU HB2 H 2.01 . 1 1598 . 151 LEU HB3 H 1.55 . 1 1599 . 151 LEU HG H 1.70 . 1 1600 . 151 LEU HD1 H 0.07 . 2 1601 . 151 LEU HD2 H 0.90 . 2 1602 . 151 LEU CA C 55.3 . 1 1603 . 151 LEU CB C 41.1 . 1 1604 . 151 LEU CG C 26.0 . 1 1605 . 151 LEU CD1 C 24.1 . 2 1606 . 151 LEU CD2 C 20.6 . 2 1607 . 151 LEU N N 118.7 . 1 1608 . 152 HIS H H 7.76 . 1 1609 . 152 HIS HA H 4.06 . 1 1610 . 152 HIS HB2 H 3.28 . 1 1611 . 152 HIS HB3 H 3.02 . 1 1612 . 152 HIS HD2 H 6.62 . 1 1613 . 152 HIS HE1 H 7.74 . 1 1614 . 152 HIS CA C 58.3 . 1 1615 . 152 HIS CB C 30.5 . 1 1616 . 152 HIS CD2 C 117.5 . 1 1617 . 152 HIS CE1 C 138.9 . 1 1618 . 152 HIS N N 118.5 . 1 1619 . 153 LYS H H 7.54 . 1 1620 . 153 LYS HA H 4.07 . 1 1621 . 153 LYS HB2 H 1.58 . 2 1622 . 153 LYS HB3 H 1.46 . 2 1623 . 153 LYS HG2 H 1.18 . 2 1624 . 153 LYS HG3 H 0.45 . 2 1625 . 153 LYS HD2 H 1.62 . 1 1626 . 153 LYS HD3 H 1.62 . 1 1627 . 153 LYS HE2 H 3.10 . 2 1628 . 153 LYS HE3 H 2.90 . 2 1629 . 153 LYS CA C 57.4 . 1 1630 . 153 LYS CB C 31.1 . 1 1631 . 153 LYS CG C 22.5 . 1 1632 . 153 LYS CD C 29.1 . 1 1633 . 153 LYS CE C 41.5 . 1 1634 . 153 LYS N N 115.4 . 1 1635 . 154 PHE H H 7.02 . 1 1636 . 154 PHE HA H 4.49 . 1 1637 . 154 PHE HB2 H 2.94 . 2 1638 . 154 PHE HB3 H 2.75 . 2 1639 . 154 PHE HD1 H 6.73 . 1 1640 . 154 PHE HD2 H 6.73 . 1 1641 . 154 PHE HE1 H 6.71 . 4 1642 . 154 PHE HE2 H 6.71 . 4 1643 . 154 PHE HZ H 6.71 . 4 1644 . 154 PHE CA C 56.7 . 1 1645 . 154 PHE CB C 39.7 . 1 1646 . 154 PHE CD1 C 130.4 . 1 1647 . 154 PHE CD2 C 130.4 . 1 1648 . 154 PHE CE1 C 130.6 . 4 1649 . 154 PHE CE2 C 130.6 . 4 1650 . 154 PHE CZ C 130.6 . 4 1651 . 154 PHE N N 117.1 . 1 1652 . 155 ALA H H 6.94 . 1 1653 . 155 ALA HA H 4.14 . 1 1654 . 155 ALA HB H 1.46 . 1 1655 . 155 ALA CA C 51.5 . 1 1656 . 155 ALA CB C 22.5 . 1 1657 . 155 ALA N N 122.7 . 1 1658 . 156 SER H H 8.16 . 1 1659 . 156 SER HA H 4.01 . 1 1660 . 156 SER HB2 H 4.01 . 2 1661 . 156 SER HB3 H 3.07 . 2 1662 . 156 SER CA C 61.5 . 1 1663 . 156 SER CB C 61.5 . 1 1664 . 156 SER N N 120.1 . 1 1665 . 157 LYS H H 7.67 . 1 1666 . 157 LYS HA H 4.54 . 1 1667 . 157 LYS HB2 H 1.76 . 2 1668 . 157 LYS HB3 H 1.65 . 2 1669 . 157 LYS HG2 H 1.50 . 2 1670 . 157 LYS HG3 H 1.43 . 2 1671 . 157 LYS HD2 H 1.65 . 1 1672 . 157 LYS HD3 H 1.65 . 1 1673 . 157 LYS HE2 H 3.00 . 1 1674 . 157 LYS HE3 H 3.00 . 1 1675 . 157 LYS CA C 53.1 . 1 1676 . 157 LYS CB C 33.0 . 1 1677 . 157 LYS CG C 24.9 . 1 1678 . 157 LYS CD C 24.9 . 1 1679 . 157 LYS CE C 42.3 . 1 1680 . 157 LYS N N 118.3 . 1 1681 . 158 PRO HA H 4.66 . 1 1682 . 158 PRO HB2 H 2.28 . 1 1683 . 158 PRO HB3 H 2.43 . 1 1684 . 158 PRO HG2 H 1.99 . 2 1685 . 158 PRO HG3 H 1.94 . 2 1686 . 158 PRO HD2 H 3.69 . 2 1687 . 158 PRO HD3 H 3.62 . 2 1688 . 158 PRO CA C 62.0 . 1 1689 . 158 PRO CB C 34.0 . 1 1690 . 158 PRO CG C 25.0 . 1 1691 . 158 PRO CD C 50.0 . 1 1692 . 159 ALA H H 9.00 . 1 1693 . 159 ALA HA H 4.06 . 1 1694 . 159 ALA HB H 0.85 . 1 1695 . 159 ALA CA C 55.3 . 1 1696 . 159 ALA CB C 17.0 . 1 1697 . 159 ALA N N 129.1 . 1 1698 . 160 SER H H 8.12 . 1 1699 . 160 SER HA H 4.00 . 1 1700 . 160 SER HB2 H 3.86 . 1 1701 . 160 SER HB3 H 3.86 . 1 1702 . 160 SER CA C 60.5 . 1 1703 . 160 SER CB C 61.9 . 1 1704 . 160 SER N N 109.7 . 1 1705 . 161 GLU H H 7.53 . 1 1706 . 161 GLU HA H 4.24 . 1 1707 . 161 GLU HB2 H 1.70 . 2 1708 . 161 GLU HB3 H 1.54 . 2 1709 . 161 GLU HG2 H 1.89 . 1 1710 . 161 GLU HG3 H 1.89 . 1 1711 . 161 GLU CA C 56.3 . 1 1712 . 161 GLU CB C 30.8 . 1 1713 . 161 GLU CG C 35.4 . 1 1714 . 161 GLU N N 120.7 . 1 1715 . 162 PHE H H 7.17 . 1 1716 . 162 PHE HA H 4.54 . 1 1717 . 162 PHE HB2 H 4.04 . 2 1718 . 162 PHE HB3 H 2.58 . 2 1719 . 162 PHE HD1 H 6.69 . 1 1720 . 162 PHE HD2 H 6.69 . 1 1721 . 162 PHE HE1 H 6.9 . 4 1722 . 162 PHE HE2 H 6.9 . 4 1723 . 162 PHE HZ H 6.9 . 4 1724 . 162 PHE CA C 59.6 . 1 1725 . 162 PHE CB C 40.7 . 1 1726 . 162 PHE CD1 C 132.8 . 1 1727 . 162 PHE CD2 C 132.8 . 1 1728 . 162 PHE CE1 C 131.6 . 4 1729 . 162 PHE CE2 C 131.6 . 4 1730 . 162 PHE CZ C 131.6 . 4 1731 . 162 PHE N N 117.1 . 1 1732 . 163 VAL H H 7.48 . 1 1733 . 163 VAL HA H 4.71 . 1 1734 . 163 VAL HB H 1.90 . 1 1735 . 163 VAL HG1 H 0.70 . 1 1736 . 163 VAL HG2 H 0.74 . 1 1737 . 163 VAL CA C 60.9 . 1 1738 . 163 VAL CB C 32.3 . 1 1739 . 163 VAL CG1 C 21.2 . 1 1740 . 163 VAL CG2 C 22.1 . 1 1741 . 163 VAL N N 119.3 . 1 1742 . 164 LYS H H 9.24 . 1 1743 . 164 LYS HA H 4.59 . 1 1744 . 164 LYS HB2 H 1.72 . 2 1745 . 164 LYS HB3 H 1.68 . 2 1746 . 164 LYS HG2 H 1.45 . 2 1747 . 164 LYS HG3 H 1.34 . 2 1748 . 164 LYS HD2 H 1.65 . 1 1749 . 164 LYS HD3 H 1.65 . 1 1750 . 164 LYS HE2 H 3.00 . 1 1751 . 164 LYS HE3 H 3.00 . 1 1752 . 164 LYS CA C 52.8 . 1 1753 . 164 LYS CB C 34.0 . 1 1754 . 164 LYS CG C 24.0 . 1 1755 . 164 LYS CD C 27.8 . 1 1756 . 164 LYS CE C 42.0 . 1 1757 . 164 LYS N N 131.7 . 1 1758 . 165 ILE H H 8.42 . 1 1759 . 165 ILE HA H 4.96 . 1 1760 . 165 ILE HB H 1.90 . 1 1761 . 165 ILE HG12 H 1.43 . 2 1762 . 165 ILE HG13 H 1.10 . 2 1763 . 165 ILE HG2 H 0.69 . 1 1764 . 165 ILE HD1 H 0.37 . 1 1765 . 165 ILE CA C 56.7 . 1 1766 . 165 ILE CB C 36.0 . 1 1767 . 165 ILE CG1 C 25.6 . 1 1768 . 165 ILE CG2 C 16.8 . 1 1769 . 165 ILE CD1 C 9.4 . 1 1770 . 165 ILE N N 126.4 . 1 1771 . 166 LEU H H 8.92 . 1 1772 . 166 LEU HA H 4.78 . 1 1773 . 166 LEU HB2 H 1.43 . 1 1774 . 166 LEU HB3 H 1.43 . 1 1775 . 166 LEU HG H 1.43 . 1 1776 . 166 LEU HD1 H 0.55 . 2 1777 . 166 LEU HD2 H 0.70 . 2 1778 . 166 LEU CA C 52.2 . 1 1779 . 166 LEU CB C 44.6 . 1 1780 . 166 LEU CG C 26.9 . 1 1781 . 166 LEU CD1 C 25.1 . 2 1782 . 166 LEU CD2 C 23.7 . 2 1783 . 166 LEU N N 128.6 . 1 1784 . 167 ASP H H 9.01 . 1 1785 . 167 ASP HA H 4.37 . 1 1786 . 167 ASP HB2 H 2.72 . 2 1787 . 167 ASP HB3 H 2.68 . 2 1788 . 167 ASP CA C 55.6 . 1 1789 . 167 ASP CB C 39.6 . 1 1790 . 167 ASP N N 122.4 . 1 1791 . 168 THR H H 7.07 . 1 1792 . 168 THR HA H 4.77 . 1 1793 . 168 THR HB H 4.64 . 1 1794 . 168 THR HG2 H 1.19 . 1 1795 . 168 THR CA C 58.1 . 1 1796 . 168 THR CB C 71.1 . 1 1797 . 168 THR CG2 C 21.1 . 1 1798 . 168 THR N N 108.4 . 1 1799 . 169 PHE H H 8.66 . 1 1800 . 169 PHE HA H 3.80 . 1 1801 . 169 PHE HB2 H 3.16 . 1 1802 . 169 PHE HB3 H 2.88 . 1 1803 . 169 PHE HD1 H 7.27 . 1 1804 . 169 PHE HD2 H 7.27 . 1 1805 . 169 PHE HE1 H 7.15 . 4 1806 . 169 PHE HE2 H 7.15 . 4 1807 . 169 PHE HZ H 7.15 . 4 1808 . 169 PHE CA C 61.4 . 1 1809 . 169 PHE CB C 39.1 . 1 1810 . 169 PHE CD1 C 132.0 . 1 1811 . 169 PHE CD2 C 132.0 . 1 1812 . 169 PHE CE1 C 131.4 . 4 1813 . 169 PHE CE2 C 131.4 . 4 1814 . 169 PHE CZ C 131.4 . 4 1815 . 169 PHE N N 120.1 . 1 1816 . 170 GLU H H 8.64 . 1 1817 . 170 GLU HA H 4.06 . 1 1818 . 170 GLU HB2 H 2.06 . 1 1819 . 170 GLU HB3 H 2.06 . 1 1820 . 170 GLU HG2 H 2.44 . 2 1821 . 170 GLU HG3 H 2.33 . 2 1822 . 170 GLU CA C 59.1 . 1 1823 . 170 GLU CB C 29.0 . 1 1824 . 170 GLU CG C 36.6 . 1 1825 . 170 GLU N N 122.3 . 1 1826 . 171 LYS H H 7.02 . 1 1827 . 171 LYS HA H 4.24 . 1 1828 . 171 LYS HB2 H 2.06 . 2 1829 . 171 LYS HB3 H 1.83 . 2 1830 . 171 LYS HG2 H 1.67 . 2 1831 . 171 LYS HG3 H 1.55 . 2 1832 . 171 LYS HD2 H 1.92 . 1 1833 . 171 LYS HD3 H 1.92 . 1 1834 . 171 LYS HE2 H 3.02 . 1 1835 . 171 LYS HE3 H 3.02 . 1 1836 . 171 LYS CA C 56.9 . 1 1837 . 171 LYS CB C 33.3 . 1 1838 . 171 LYS CG C 25.8 . 1 1839 . 171 LYS CD C 31.9 . 1 1840 . 171 LYS CE C 42.0 . 1 1841 . 171 LYS N N 116.3 . 1 1842 . 172 LEU H H 7.41 . 1 1843 . 172 LEU HA H 3.65 . 1 1844 . 172 LEU HB2 H 1.69 . 2 1845 . 172 LEU HB3 H 1.38 . 2 1846 . 172 LEU HG H 1.29 . 1 1847 . 172 LEU HD1 H 0.66 . 2 1848 . 172 LEU HD2 H 0.12 . 2 1849 . 172 LEU CA C 57.7 . 1 1850 . 172 LEU CB C 41.3 . 1 1851 . 172 LEU CG C 26.8 . 1 1852 . 172 LEU CD1 C 24.8 . 2 1853 . 172 LEU CD2 C 22.5 . 2 1854 . 172 LEU N N 121.4 . 1 1855 . 173 LYS H H 7.48 . 1 1856 . 173 LYS HA H 4.27 . 1 1857 . 173 LYS HB2 H 1.94 . 2 1858 . 173 LYS HB3 H 1.88 . 2 1859 . 173 LYS HG2 H 1.53 . 1 1860 . 173 LYS HG3 H 1.53 . 1 1861 . 173 LYS HD2 H 1.72 . 1 1862 . 173 LYS HD3 H 1.72 . 1 1863 . 173 LYS HE2 H 3.02 . 1 1864 . 173 LYS HE3 H 3.02 . 1 1865 . 173 LYS CA C 58.4 . 1 1866 . 173 LYS CB C 32.1 . 1 1867 . 173 LYS CG C 24.1 . 1 1868 . 173 LYS CD C 29.0 . 1 1869 . 173 LYS CE C 42.0 . 1 1870 . 173 LYS N N 117.2 . 1 1871 . 174 ASP H H 7.45 . 1 1872 . 174 ASP HA H 4.93 . 1 1873 . 174 ASP HB2 H 2.58 . 1 1874 . 174 ASP HB3 H 2.92 . 1 1875 . 174 ASP CA C 54.6 . 1 1876 . 174 ASP CB C 41.6 . 1 1877 . 174 ASP N N 118.2 . 1 1878 . 175 LEU H H 7.54 . 1 1879 . 175 LEU HA H 4.36 . 1 1880 . 175 LEU HB2 H 1.91 . 2 1881 . 175 LEU HB3 H 1.68 . 2 1882 . 175 LEU HG H 1.80 . 1 1883 . 175 LEU HD1 H 0.80 . 2 1884 . 175 LEU HD2 H 0.95 . 2 1885 . 175 LEU CA C 56.4 . 1 1886 . 175 LEU CB C 42.7 . 1 1887 . 175 LEU CG C 27.1 . 1 1888 . 175 LEU CD1 C 26.0 . 2 1889 . 175 LEU CD2 C 24.2 . 2 1890 . 175 LEU N N 121.8 . 1 1891 . 176 PHE H H 8.94 . 1 1892 . 176 PHE HA H 4.02 . 1 1893 . 176 PHE HB2 H 3.30 . 2 1894 . 176 PHE HB3 H 3.09 . 2 1895 . 176 PHE HD1 H 7.05 . 1 1896 . 176 PHE HD2 H 7.05 . 1 1897 . 176 PHE HE1 H 6.97 . 4 1898 . 176 PHE HE2 H 6.97 . 4 1899 . 176 PHE HZ H 6.97 . 4 1900 . 176 PHE CA C 62.9 . 1 1901 . 176 PHE CB C 38.5 . 1 1902 . 176 PHE CD1 C 131.9 . 1 1903 . 176 PHE CD2 C 131.9 . 1 1904 . 176 PHE CE1 C 131.3 . 4 1905 . 176 PHE CE2 C 131.3 . 4 1906 . 176 PHE CZ C 131.3 . 4 1907 . 176 PHE N N 120.3 . 1 1908 . 177 THR H H 8.00 . 1 1909 . 177 THR HA H 3.73 . 1 1910 . 177 THR HB H 4.19 . 1 1911 . 177 THR HG2 H 1.27 . 1 1912 . 177 THR CA C 66.1 . 1 1913 . 177 THR CB C 68.4 . 1 1914 . 177 THR CG2 C 21.9 . 1 1915 . 177 THR N N 113.6 . 1 1916 . 178 GLU H H 7.57 . 1 1917 . 178 GLU HA H 4.10 . 1 1918 . 178 GLU HB2 H 2.07 . 1 1919 . 178 GLU HB3 H 2.07 . 1 1920 . 178 GLU HG2 H 2.27 . 2 1921 . 178 GLU HG3 H 2.16 . 2 1922 . 178 GLU CA C 58.4 . 1 1923 . 178 GLU CB C 29.7 . 1 1924 . 178 GLU CG C 35.8 . 1 1925 . 178 GLU N N 121.5 . 1 1926 . 179 LEU H H 7.94 . 1 1927 . 179 LEU HA H 3.79 . 1 1928 . 179 LEU HB2 H 1.47 . 2 1929 . 179 LEU HB3 H 1.41 . 2 1930 . 179 LEU HG H 1.50 . 1 1931 . 179 LEU HD1 H 0.67 . 1 1932 . 179 LEU HD2 H 0.67 . 1 1933 . 179 LEU CA C 57.4 . 1 1934 . 179 LEU CB C 42.0 . 1 1935 . 179 LEU CG C 26.7 . 1 1936 . 179 LEU CD1 C 24.2 . 1 1937 . 179 LEU CD2 C 24.2 . 1 1938 . 179 LEU N N 121.4 . 1 1939 . 180 GLN H H 8.31 . 1 1940 . 180 GLN HA H 3.47 . 1 1941 . 180 GLN HB2 H 1.62 . 2 1942 . 180 GLN HB3 H 1.37 . 2 1943 . 180 GLN HG2 H 1.99 . 1 1944 . 180 GLN HG3 H 1.99 . 1 1945 . 180 GLN CA C 58.7 . 1 1946 . 180 GLN CB C 27.7 . 1 1947 . 180 GLN CG C 33.6 . 1 1948 . 180 GLN N N 118.7 . 1 1949 . 180 GLN NE2 N 111.8 . 1 1950 . 181 LYS H H 7.16 . 1 1951 . 181 LYS HA H 3.95 . 1 1952 . 181 LYS HB2 H 1.83 . 2 1953 . 181 LYS HB3 H 1.34 . 2 1954 . 181 LYS HG2 H 1.01 . 2 1955 . 181 LYS HG3 H 0.77 . 2 1956 . 181 LYS HD2 H 1.44 . 1 1957 . 181 LYS HD3 H 1.44 . 1 1958 . 181 LYS HE2 H 2.77 . 1 1959 . 181 LYS HE3 H 2.77 . 1 1960 . 181 LYS CA C 58.9 . 1 1961 . 181 LYS CB C 32.8 . 1 1962 . 181 LYS CG C 24.3 . 1 1963 . 181 LYS CD C 29.0 . 1 1964 . 181 LYS CE C 41.9 . 1 1965 . 181 LYS N N 117.1 . 1 1966 . 182 LYS H H 7.44 . 1 1967 . 182 LYS HA H 4.17 . 1 1968 . 182 LYS HB2 H 1.72 . 2 1969 . 182 LYS HB3 H 1.83 . 2 1970 . 182 LYS HG2 H 1.43 . 2 1971 . 182 LYS HG3 H 1.33 . 2 1972 . 182 LYS HD2 H 1.54 . 2 1973 . 182 LYS HD3 H 1.45 . 2 1974 . 182 LYS HE2 H 2.76 . 1 1975 . 182 LYS HE3 H 2.76 . 1 1976 . 182 LYS CA C 56.5 . 1 1977 . 182 LYS CB C 31.9 . 1 1978 . 182 LYS CG C 24.0 . 1 1979 . 182 LYS CD C 28.0 . 1 1980 . 182 LYS CE C 41.8 . 1 1981 . 182 LYS N N 118.2 . 1 1982 . 183 ILE H H 7.68 . 1 1983 . 183 ILE HA H 3.93 . 1 1984 . 183 ILE HB H 1.84 . 1 1985 . 183 ILE HG12 H 1.44 . 2 1986 . 183 ILE HG13 H 1.05 . 2 1987 . 183 ILE HG2 H 0.79 . 1 1988 . 183 ILE HD1 H 0.64 . 1 1989 . 183 ILE CA C 62.6 . 1 1990 . 183 ILE CB C 37.7 . 1 1991 . 183 ILE CG1 C 27.7 . 1 1992 . 183 ILE CG2 C 17.4 . 1 1993 . 183 ILE CD1 C 12.6 . 1 1994 . 183 ILE N N 117.8 . 1 1995 . 184 TYR H H 7.77 . 1 1996 . 184 TYR HA H 4.56 . 1 1997 . 184 TYR HB2 H 3.07 . 1 1998 . 184 TYR HB3 H 3.07 . 1 1999 . 184 TYR HD1 H 6.94 . 1 2000 . 184 TYR HD2 H 6.94 . 1 2001 . 184 TYR HE1 H 6.68 . 1 2002 . 184 TYR HE2 H 6.68 . 1 2003 . 184 TYR CA C 58.4 . 1 2004 . 184 TYR CB C 38.1 . 1 2005 . 184 TYR CD1 C 132.1 . 1 2006 . 184 TYR CD2 C 132.1 . 1 2007 . 184 TYR CE1 C 118.4 . 1 2008 . 184 TYR CE2 C 118.4 . 1 2009 . 184 TYR N N 121.2 . 1 2010 . 185 VAL H H 7.54 . 1 2011 . 185 VAL HA H 4.02 . 1 2012 . 185 VAL HB H 2.13 . 1 2013 . 185 VAL HG1 H 0.93 . 1 2014 . 185 VAL HG2 H 0.93 . 1 2015 . 185 VAL CA C 62.8 . 1 2016 . 185 VAL CB C 32.1 . 1 2017 . 185 VAL CG1 C 21.0 . 1 2018 . 185 VAL CG2 C 21.0 . 1 2019 . 185 VAL N N 119.6 . 1 2020 . 186 ILE H H 7.78 . 1 2021 . 186 ILE HA H 4.08 . 1 2022 . 186 ILE HB H 1.96 . 1 2023 . 186 ILE HG12 H 1.60 . 2 2024 . 186 ILE HG13 H 1.23 . 2 2025 . 186 ILE HG2 H 0.87 . 1 2026 . 186 ILE HD1 H 0.89 . 1 2027 . 186 ILE CA C 61.7 . 1 2028 . 186 ILE CB C 38.4 . 1 2029 . 186 ILE CG1 C 27.6 . 1 2030 . 186 ILE CG2 C 17.8 . 1 2031 . 186 ILE CD1 C 13.5 . 1 2032 . 186 ILE N N 122.8 . 1 2033 . 187 GLU H H 8.14 . 1 2034 . 187 GLU HA H 4.17 . 1 2035 . 187 GLU HB2 H 2.30 . 2 2036 . 187 GLU HB3 H 2.21 . 2 2037 . 187 GLU HG2 H 2.30 . 2 2038 . 187 GLU HG3 H 2.22 . 2 2039 . 187 GLU CA C 56.8 . 1 2040 . 187 GLU CB C 30.6 . 1 2041 . 187 GLU CG C 36.2 . 1 2042 . 187 GLU N N 124.3 . 1 2043 . 188 GLY H H 7.79 . 1 2044 . 188 GLY HA2 H 3.73 . 1 2045 . 188 GLY HA3 H 3.73 . 1 2046 . 188 GLY CA C 46.0 . 1 2047 . 188 GLY N N 116.3 . 1 stop_ save_