data_4553 #Corrected using PDB structure: 1XDGA # #N.B. (Observed* = Observed shift + Offset correction) # #After reference correction, the following residues still #have a HA chemical shift difference (obs*-pred) greater than 0.7ppm: #NUM AA CS Observed* Predicted # 16 S HA 4.21 4.97 # 43 Y HA 5.10 4.33 #119 A HA 5.23 4.53 #149 E HA 2.90 3.61 # #After reference correction, the following residues still #have a CB chemical shift difference (obs*-pred) greater than 5.0ppm: #NUM AA CS Observed* Predicted # 51 S CB 62.29 67.37 # 63 Y CB 62.79 38.67 # #After reference correction, the following residues still #have a N chemical shift difference (obs*-pred) greater than 10.0ppm: #NUM AA CS Observed* Predicted # 52 T N 123.21 111.60 # #After reference correction, the following residues still #have a HN chemical shift difference (obs*-pred) greater than 2.0ppm: #NUM AA CS Observed* Predicted # 7 V H 6.97 8.99 # 45 F H 5.52 8.44 #100 E H 10.26 8.26 # #The average CS difference between predicted and observed: #HA CA CB CO N HN #0.02 0.10 -0.01 N/A -1.09 0.04 # #bmr4553.str.corr chemical shifts have been re-referenced with the following #offsets (these values have been added to the original bmr4553.str file): #HA CA CB CO N HN #N/A +0.04 +0.04 N/A -1.09 N/A # #The 95% confidence intervals for the above recommended offsets are: # HA CA CB CO N HN #+/-0.02 +/-0.11 +/-0.13 N/A +/-0.26 +/-0.05 # #The Correlation Coefficients between predicted and observed #chemical shifts are: #HA CA CB CO N HN #0.906 0.967 0.984 N/A 0.868 0.710 # #The RMSD between predicted and observed* (reference #corrected) chemical shifts are: #HA CA CB CO N HN #0.162 0.765 0.861 N/A 1.738 0.341 # ####################### # 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 ; 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_ _BMRB_accession_number 4553 _BMRB_flat_file_name bmr4553.str _Entry_type new _Submission_date 1999-12-10 _Accession_date 1999-12-13 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR 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_ 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 _MEDLINE_UI_code 20262885 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 _Page_first 271 _Page_last 272 _Year 2000 loop_ _Keyword "LFA-1 NMR assignment" stop_ 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 $magnesium stop_ _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' loop_ _Biological_function ; leukocyte specific integrin ICAM binding (Intercellular Adhesion Molecules) ; stop_ loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Database_entry_details PDB 1DGQ "A Chain A, Nmr Solution Structure Of The Inserted Domain Of Human Leukocyte Function Associated Antigen-1" . PDB 1CQP "A Chain A, Crystal Structure Analysis Of The Complex Lfa-1 (Cd11a) I- Domain LOVASTATIN AT 2.6 A RESOLUTION" . PDB 1LFA "A Chain A, Cd11a I-Domain With Bound Mn++" . PDB 1ZOP "A Chain A, Cd11a I-Domain With Bound Magnesium Ion" . PDB 1ZOO "A Chain A, Cd11a I-Domain With Bound Magnesium Ion" . PDB 1ZON "Cd11a I-Domain Without Bound Cation" . stop_ 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 2004-07-29 _Sequence_homology_query_revised_last_date 2004-06-24 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 1MQ8 "B Chain B, Crystal Structure Of Alphal IDomain In Complex With Icam-1" 106.78 177 98 98 7e-93 PDB 1MJN "A Chain A, Crystal Structure Of TheIntermediate Affinity Al I Domain Mutant" 105.59 179 98 98 3e-94 PDB 1MQ9 "A Chain A, Crystal Structure Of High AffinityAlphal I Domain With Ligand Mimetic Crystal Contact" 105.00 180 98 98 6e-94 PDB 1MQA "A Chain A, Crystal Structure Of High AffinityAlphal I Domain In The Absence Of Ligand Or Metal" 105.00 180 98 98 6e-94 PDB 1CQP "A Chain A, Crystal Structure Analysis Of TheComplex Lfa-1 (Cd11a) I- Domain LOVASTATIN AT 2.6 ARESOLUTION" 103.85 182 100 100 4e-99 PDB 1LFA "A Chain A, Cd11a I-Domain With Bound Mn++" 101.07 187 99 99 2e-99 PDB 1ZON "Cd11a I-Domain Without Bound Cation" 101.07 187 99 99 2e-99 PDB 1ZOO "A Chain A, Cd11a I-Domain With Bound MagnesiumIon" 101.07 187 99 99 2e-99 PDB 1ZOP "A Chain A, Cd11a I-Domain With Bound MagnesiumIon" 101.07 187 99 99 2e-99 PDB 1DGQ "A Chain A, Nmr Solution Structure Of TheInserted Domain Of Human Leukocyte Function AssociatedAntigen-1" 100.53 188 100 100 1e-102 PDB 1RD4 "A Chain A, An Allosteric Inhibitor Of Lfa-1Bound To Its I-Domain" 98.95 191 99 99 2e-99 EMBL CAA68747.1 "unnamed protein product [Homo sapiens]" 16.15 1170 100 100 1e-101 GenBank AAH08777.1 "ITGAL protein [Homo sapiens]" 17.40 1086 98 98 3e-75 GenBank AAP88867.1 "integrin, alpha L (antigen CD11A (p180),lymphocyte function-associated antigen 1; alphapolypeptide) [synthetic construct]" 17.39 1087 98 98 3e-75 GenBank AAC31672.1 "leukocyte function-associated molecule-1alpha subunit [Homo sapiens]" 15.45 1223 100 100 1e-101 PIR S03308 "cell surface glycoprotein CD11a precursor -human" 16.15 1170 100 100 1e-101 REF NP_002200.1 "integrin alpha L precursor; antigenCD11A (p180), lymphocyte function-associated antigen 1,alpha polypeptide [Homo sapiens]" 16.15 1170 100 100 1e-101 SWISS-PROT P20701 "ITAL_HUMAN Integrin alpha-L precursor(Leukocyte adhesion glycoprotein LFA-1 alpha chain)(LFA-1A) (Leukocyte function associated molecule 1,alpha chain) (CD11a)" 16.15 1170 99 99 2e-99 stop_ save_ ############# # Ligands # ############# save_magnesium _Saveframe_category ligand _Name_common "magnesium" _Abbreviation_common Mg2+ _Mol_paramagnetic no _Mol_aromatic no loop_ _Atom_name _Atom_type _Atom_oxidation_number MG Mg +2 stop_ 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 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 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 save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 750 save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 600 save_ save_NMR_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AMX _Field_strength 500 save_ ############################# # NMR applied experiments # ############################# save_NMR_applied_experiment _Saveframe_category NMR_applied_experiment _Details ; HNCA HNCO HN(CA)CO HNCACB CBCA(CO)NH HBHA(CO)NH 1H-15N TOCSY CC(CO)NH TOSCY HCCH COSY HCCH TOCSY HCCH TOCSY (aromatic) 2D 13C HSQC 3D HB(CBCG)CDHD ; save_ ####################### # Sample conditions # ####################### save_condition_1 _Saveframe_category sample_conditions loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH* 7.2 0.2 na temperature 295 1 K 'ionic strength' 0.28 0.02 M 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 pH* 7.3 0.2 na temperature 295 1 K 'ionic strength' 0.018 0.02 M stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference 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 _Reference_correction_type TSP H 1 "methyl protons" ppm 0.00 external direct cylindrical external parallel 1.00 . TSP C 13 "methyl protons" ppm 0.00 external direct cylindrical external parallel 0.25144954 . 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 # # # # Index Value Definition # # # # 1 Unique # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups # # 3 Aromatic atoms on opposite sides of the ring # # (e.g. Tyr HE1 and HE2 protons) # # 4 Intraresidue ambiguities (e.g. Lys HG and # # HD protons) # # 5 Interresidue ambiguities (Lys 12 vs. Lys 27) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_lfa1 _Saveframe_category assigned_chemical_shifts loop_ _Sample_label $sample_1 $sample_2 stop_ _Sample_conditions_label $condition_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name LFA-1 loop_ _Atom_shift_assign_ID _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 58.14 . 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 56.34 . 1 17 4 LYS CB C 32.74 . 1 18 4 LYS CG C 24.64 . 1 19 4 LYS CD C 28.84 . 1 20 4 LYS CE C 42.04 . 1 21 4 LYS N N 123.71 . 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 45.14 . 1 26 5 GLY N N 110.01 . 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 52.74 . 1 34 6 ASN CB C 37.54 . 1 35 6 ASN N N 119.51 . 1 36 6 ASN ND2 N 113.40 . 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 61.14 . 1 43 7 VAL CB C 34.44 . 1 44 7 VAL CG1 C 21.84 . 1 45 7 VAL CG2 C 20.94 . 1 46 7 VAL N N 123.71 . 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 52.74 . 1 52 8 ASP CB C 41.14 . 1 53 8 ASP N N 131.51 . 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 54.24 . 1 62 9 LEU CB C 44.54 . 1 63 9 LEU CG C 28.04 . 1 64 9 LEU CD1 C 26.94 . 2 65 9 LEU CD2 C 23.24 . 2 66 9 LEU N N 127.01 . 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 59.54 . 1 73 10 VAL CB C 34.34 . 1 74 10 VAL CG1 C 21.04 . 1 75 10 VAL CG2 C 24.64 . 1 76 10 VAL N N 123.91 . 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 56.74 . 1 87 11 PHE CB C 42.44 . 1 88 11 PHE CD1 C 132.44 . 1 89 11 PHE CD2 C 132.44 . 1 90 11 PHE CE1 C 131.44 . 1 91 11 PHE CE2 C 131.44 . 1 92 11 PHE CZ C 131.44 . 1 93 11 PHE N N 131.31 . 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 52.94 . 1 102 12 LEU CB C 45.34 . 1 103 12 LEU CG C 26.94 . 1 104 12 LEU CD1 C 24.54 . 2 105 12 LEU CD2 C 24.04 . 2 106 12 LEU N N 129.21 . 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 54.94 . 1 118 13 PHE CD1 C 133.74 . 1 119 13 PHE CD2 C 133.74 . 1 120 13 PHE CE1 C 131.44 . 1 121 13 PHE CE2 C 131.44 . 1 122 13 PHE CZ C 131.44 . 1 123 13 PHE N N 132.61 . 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 53.34 . 1 129 14 ASP CB C 44.44 . 1 130 14 ASP N N 127.51 . 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 44.54 . 1 135 15 GLY N N 110.61 . 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 58.64 . 1 142 16 SER CB C 66.44 . 1 143 16 SER N N 116.41 . 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 57.04 . 1 152 17 MET CB C 32.94 . 1 153 17 MET CG C 29.94 . 1 154 17 MET CE C 17.44 . 1 155 17 MET N N 116.31 . 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 58.74 . 1 162 18 SER CB C 61.64 . 1 163 18 SER N N 110.51 . 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 55.44 . 1 172 19 LEU CB C 43.64 . 1 173 19 LEU CG C 27.44 . 1 174 19 LEU CD1 C 28.74 . 2 175 19 LEU CD2 C 27.64 . 2 177 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 53.54 . 1 186 20 GLN CB C 27.74 . 1 187 20 GLN CG C 33.94 . 1 188 20 GLN N N 122.61 . 1 189 20 GLN NE2 N 115.60 . 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 66.44 . 1 198 21 PRO CB C 31.74 . 1 199 21 PRO CG C 27.84 . 1 200 21 PRO CD C 49.74 . 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 56.14 . 1 206 22 ASP CB C 39.94 . 1 207 22 ASP N N 114.21 . 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 58.44 . 1 215 23 GLU CB C 28.64 . 1 216 23 GLU CG C 36.64 . 1 217 23 GLU N N 121.71 . 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 61.74 . 1 228 24 PHE CB C 39.14 . 1 229 24 PHE CD1 C 132.24 . 1 230 24 PHE CD2 C 132.24 . 1 231 24 PHE CE1 C 132.04 . 1 232 24 PHE CE2 C 132.04 . 1 233 24 PHE CZ C 130.84 . 1 234 24 PHE N N 118.61 . 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 58.24 . 1 244 25 GLN CB C 28.04 . 1 245 25 GLN CG C 33.24 . 1 246 25 GLN N N 115.21 . 1 247 25 GLN NE2 N 115.60 . 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 59.84 . 1 259 26 LYS CB C 32.34 . 1 260 26 LYS CG C 25.24 . 1 261 26 LYS CD C 29.54 . 1 262 26 LYS CE C 42.34 . 1 263 26 LYS N N 118.41 . 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 66.54 . 1 272 27 ILE CB C 37.04 . 1 273 27 ILE CG1 C 29.04 . 1 274 27 ILE CG2 C 17.24 . 1 275 27 ILE CD1 C 16.04 . 1 276 27 ILE N N 121.61 . 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 58.14 . 1 285 28 LEU CB C 40.64 . 1 286 28 LEU CG C 26.14 . 1 287 28 LEU CD1 C 25.44 . 2 288 28 LEU CD2 C 23.14 . 2 289 28 LEU N N 119.61 . 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 57.24 . 1 295 29 ASP CB C 40.04 . 1 296 29 ASP N N 118.41 . 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 60.14 . 1 307 30 PHE CB C 38.94 . 1 308 30 PHE CD1 C 132.24 . 1 309 30 PHE CD2 C 132.24 . 1 310 30 PHE CE1 C 131.44 . 1 311 30 PHE CE2 C 131.44 . 1 312 30 PHE CZ C 131.44 . 1 313 30 PHE N N 121.91 . 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 59.24 . 1 322 31 MET CB C 33.04 . 1 323 31 MET CG C 30.74 . 1 324 31 MET CE C 17.54 . 1 325 31 MET N N 117.61 . 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 60.54 . 1 337 32 LYS CB C 32.64 . 1 338 32 LYS CG C 26.14 . 1 339 32 LYS CD C 29.74 . 1 340 32 LYS CE C 41.94 . 1 341 32 LYS N N 115.71 . 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 57.44 . 1 347 33 ASP CB C 41.14 . 1 348 33 ASP N N 119.21 . 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 66.64 . 1 355 34 VAL CB C 31.04 . 1 356 34 VAL CG1 C 21.64 . 1 357 34 VAL CG2 C 22.94 . 1 358 34 VAL N N 118.21 . 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 59.84 . 1 367 35 MET CB C 34.54 . 1 368 35 MET CG C 32.04 . 1 369 35 MET CE C 17.54 . 1 370 35 MET N N 114.51 . 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 59.94 . 1 382 36 LYS CB C 32.14 . 1 383 36 LYS CG C 26.04 . 1 384 36 LYS CD C 29.14 . 1 385 36 LYS CE C 42.04 . 1 386 36 LYS N N 119.01 . 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 58.34 . 1 398 37 LYS CB C 32.74 . 1 399 37 LYS CG C 25.94 . 1 400 37 LYS CD C 28.14 . 1 401 37 LYS CE C 42.04 . 1 402 37 LYS N N 119.61 . 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 53.44 . 1 411 38 LEU CB C 40.74 . 1 412 38 LEU CG C 26.44 . 1 413 38 LEU CD1 C 24.94 . 2 414 38 LEU CD2 C 22.74 . 2 415 38 LEU N N 118.91 . 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 60.44 . 1 421 39 SER CB C 63.64 . 1 422 39 SER N N 116.21 . 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 53.34 . 1 430 40 ASN CB C 37.94 . 1 431 40 ASN N N 120.41 . 1 432 40 ASN ND2 N 114.40 . 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 61.94 . 1 438 41 THR CB C 71.24 . 1 439 41 THR CG2 C 20.84 . 1 440 41 THR N N 110.81 . 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 58.74 . 1 446 42 SER CB C 63.04 . 1 447 42 SER N N 114.31 . 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 57.84 . 1 457 43 TYR CB C 39.24 . 1 458 43 TYR CD1 C 132.34 . 1 459 43 TYR CD2 C 132.34 . 1 460 43 TYR CE1 C 118.24 . 1 461 43 TYR CE2 C 118.24 . 1 462 43 TYR N N 124.21 . 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 54.84 . 1 472 44 GLN CB C 32.44 . 1 473 44 GLN CG C 34.24 . 1 474 44 GLN N N 116.31 . 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 56.84 . 1 485 45 PHE CB C 45.14 . 1 486 45 PHE CD1 C 133.24 . 1 487 45 PHE CD2 C 133.24 . 1 488 45 PHE CE1 C 130.44 . 1 489 45 PHE CE2 C 130.44 . 1 490 45 PHE CZ C 130.24 . 1 491 45 PHE N N 116.61 . 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 50.54 . 1 496 46 ALA CB C 21.54 . 1 497 46 ALA N N 117.41 . 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 50.84 . 1 502 47 ALA CB C 23.94 . 1 503 47 ALA N N 117.21 . 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 59.74 . 1 510 48 VAL CB C 36.24 . 1 511 48 VAL CG1 C 22.44 . 2 512 48 VAL CG2 C 20.64 . 2 513 48 VAL N N 124.01 . 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 53.34 . 1 523 49 GLN CB C 30.34 . 1 524 49 GLN CG C 35.44 . 1 525 49 GLN N N 128.61 . 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 54.21 . 1 535 50 PHE CB C 45.54 . 1 536 50 PHE N N 123.71 . 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 58.34 . 1 543 51 SER CB C 62.34 . 1 544 51 SER N N 116.41 . 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 65.04 . 1 551 52 THR CB C 68.44 . 1 552 52 THR CG2 C 22.04 . 1 553 52 THR N N 123.21 . 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 54.44 . 1 560 53 SER CB C 63.54 . 1 561 53 SER N N 117.81 . 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 53.74 . 1 571 54 TYR CB C 38.84 . 1 572 54 TYR CD1 C 132.74 . 1 573 54 TYR CD2 C 132.74 . 1 574 54 TYR CE1 C 118.04 . 1 575 54 TYR CE2 C 118.04 . 1 576 54 TYR N N 118.91 . 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 54.84 . 1 588 55 LYS CB C 37.94 . 1 589 55 LYS CG C 24.94 . 1 590 55 LYS CD C 29.24 . 1 591 55 LYS CE C 42.44 . 1 592 55 LYS N N 123.91 . 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 63.54 . 1 598 56 THR CB C 67.84 . 1 599 56 THR CG2 C 22.14 . 1 600 56 THR N N 126.61 . 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 57.04 . 1 608 57 GLU CB C 28.84 . 1 609 57 GLU CG C 33.84 . 1 610 57 GLU N N 133.31 . 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 58.14 . 1 621 58 PHE CB C 40.14 . 1 622 58 PHE CD1 C 133.24 . 1 623 58 PHE CD2 C 133.24 . 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 52.64 . 1 630 59 ASP CB C 43.64 . 1 631 59 ASP N N 122.41 . 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 60.64 . 1 642 60 PHE CB C 38.14 . 1 643 60 PHE CD1 C 133.24 . 1 644 60 PHE CD2 C 133.24 . 1 645 60 PHE CE1 C 132.64 . 1 646 60 PHE CE2 C 132.64 . 1 647 60 PHE CZ C 130.34 . 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 61.14 . 1 653 61 SER CB C 62.44 . 1 654 61 SER N N 114.11 . 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 57.54 . 1 660 62 ASP CB C 41.74 . 1 661 62 ASP N N 124.31 . 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 62.84 . 1 671 63 TYR CB C 62.84 . 1 672 63 TYR CD1 C 133.14 . 1 673 63 TYR CD2 C 133.14 . 1 674 63 TYR CE1 C 118.14 . 1 675 63 TYR CE2 C 118.14 . 1 676 63 TYR N N 120.51 . 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 65.94 . 1 683 64 VAL CB C 31.84 . 1 684 64 VAL CG1 C 21.64 . 1 685 64 VAL CG2 C 22.74 . 1 686 64 VAL N N 116.61 . 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 58.94 . 1 698 65 LYS CB C 32.84 . 1 699 65 LYS CG C 24.34 . 1 700 65 LYS CD C 29.04 . 1 701 65 LYS CE C 41.94 . 1 702 65 LYS N N 118.21 . 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 58.04 . 1 714 66 TRP CB C 31.24 . 1 715 66 TRP CD1 C 128.24 . 1 716 66 TRP CE3 C 120.84 . 1 717 66 TRP CZ2 C 114.44 . 1 718 66 TRP CZ3 C 122.04 . 1 719 66 TRP CH2 C 124.64 . 1 720 66 TRP N N 115.41 . 1 721 66 TRP NE1 N 130.70 . 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 58.34 . 1 733 67 LYS CB C 31.14 . 1 734 67 LYS CG C 25.04 . 1 735 67 LYS CD C 28.94 . 1 736 67 LYS CE C 42.34 . 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 50.74 . 1 743 68 ASP CB C 42.34 . 1 744 68 ASP N N 115.91 . 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 64.94 . 1 753 69 PRO CB C 32.94 . 1 754 69 PRO CG C 28.34 . 1 755 69 PRO CD C 50.44 . 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 57.04 . 1 761 70 ASP CB C 40.24 . 1 762 70 ASP N N 113.71 . 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 54.14 . 1 767 71 ALA CB C 18.14 . 1 768 71 ALA N N 122.11 . 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 56.74 . 1 777 72 LEU CB C 41.64 . 1 778 72 LEU CG C 26.34 . 1 779 72 LEU CD1 C 26.34 . 2 780 72 LEU CD2 C 22.04 . 2 781 72 LEU N N 116.41 . 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 53.54 . 1 790 73 LEU CB C 41.74 . 1 791 73 LEU CG C 26.24 . 1 792 73 LEU CD1 C 25.94 . 2 793 73 LEU CD2 C 22.84 . 2 794 73 LEU N N 114.11 . 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 58.74 . 1 806 74 LYS CB C 32.64 . 1 807 74 LYS CG C 23.54 . 1 808 74 LYS CD C 29.04 . 1 809 74 LYS CE C 41.84 . 1 810 74 LYS N N 120.41 . 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 55.24 . 1 818 75 HIS CB C 30.14 . 1 819 75 HIS CD2 C 120.64 . 1 820 75 HIS CE1 C 138.94 . 1 821 75 HIS N N 115.81 . 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 63.94 . 1 828 76 VAL CB C 32.04 . 1 829 76 VAL CG1 C 22.74 . 1 830 76 VAL CG2 C 22.74 . 1 831 76 VAL N N 121.71 . 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 54.04 . 1 843 77 LYS CB C 34.24 . 1 844 77 LYS CG C 24.34 . 1 845 77 LYS CD C 28.84 . 1 846 77 LYS CE C 42.14 . 1 847 77 LYS N N 130.51 . 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 54.64 . 1 855 78 HIS CB C 32.04 . 1 856 78 HIS CD2 C 114.54 . 1 857 78 HIS CE1 C 138.94 . 1 858 78 HIS N N 129.51 . 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 60.64 . 1 867 79 MET CB C 33.54 . 1 868 79 MET CG C 35.04 . 1 869 79 MET CE C 18.84 . 1 870 79 MET N N 130.71 . 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 55.64 . 1 879 80 LEU CB C 39.24 . 1 880 80 LEU CG C 26.14 . 1 881 80 LEU CD1 C 25.54 . 2 882 80 LEU CD2 C 25.24 . 2 883 80 LEU N N 113.11 . 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 54.74 . 1 892 81 LEU CB C 43.04 . 1 893 81 LEU CG C 25.54 . 1 894 81 LEU CD1 C 26.44 . 2 895 81 LEU CD2 C 22.84 . 2 896 81 LEU N N 120.91 . 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 54.64 . 1 905 82 LEU CB C 39.44 . 1 906 82 LEU CG C 26.84 . 1 907 82 LEU CD1 C 25.34 . 2 908 82 LEU CD2 C 21.94 . 2 909 82 LEU N N 121.51 . 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 59.74 . 1 916 83 THR CB C 69.84 . 1 917 83 THR CG2 C 22.14 . 1 918 83 THR N N 117.61 . 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 52.74 . 1 926 84 ASN CB C 36.44 . 1 927 84 ASN N N 128.71 . 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 66.24 . 1 935 85 THR CG2 C 20.74 . 1 936 85 THR N N 119.91 . 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 64.34 . 1 947 86 PHE CB C 37.84 . 1 948 86 PHE CD1 C 133.24 . 1 949 86 PHE CD2 C 133.24 . 1 950 86 PHE CE1 C 131.74 . 1 951 86 PHE CE2 C 131.74 . 1 952 86 PHE CZ C 131.74 . 1 953 86 PHE N N 122.01 . 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 46.34 . 1 958 87 GLY N N 111.01 . 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 54.14 . 1 963 88 ALA CB C 20.64 . 1 964 88 ALA N N 125.51 . 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 65.94 . 1 973 89 ILE CB C 37.64 . 1 974 89 ILE CG1 C 30.14 . 1 975 89 ILE CG2 C 17.34 . 1 976 89 ILE CD1 C 15.64 . 1 977 89 ILE N N 119.41 . 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 57.74 . 1 985 90 ASN CB C 39.04 . 1 986 90 ASN N N 117.61 . 1 987 90 ASN ND2 N 115.80 . 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 61.34 . 1 997 91 TYR CB C 37.74 . 1 998 91 TYR CD1 C 132.74 . 1 999 91 TYR CD2 C 132.74 . 1 1000 91 TYR CE1 C 118.04 . 1 1001 91 TYR CE2 C 118.04 . 1 1002 91 TYR N N 122.31 . 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 66.24 . 1 1009 92 VAL CB C 31.14 . 1 1010 92 VAL CG1 C 23.34 . 1 1011 92 VAL CG2 C 24.64 . 1 1012 92 VAL N N 120.01 . 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 55.24 . 1 1017 93 ALA CB C 18.44 . 1 1018 93 ALA N N 118.61 . 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 63.04 . 1 1024 94 THR CB C 70.14 . 1 1025 94 THR CG2 C 21.24 . 1 1026 94 THR N N 104.71 . 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 55.74 . 1 1034 95 GLU CB C 29.54 . 1 1035 95 GLU CG C 35.14 . 1 1036 95 GLU N N 117.61 . 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 64.04 . 1 1043 96 VAL CB C 31.94 . 1 1044 96 VAL CG1 C 21.44 . 1 1045 96 VAL CG2 C 23.44 . 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 58.44 . 1 1057 97 PHE CB C 37.14 . 1 1058 97 PHE CD1 C 132.44 . 1 1059 97 PHE CD2 C 132.44 . 1 1060 97 PHE N N 118.61 . 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 53.94 . 1 1071 98 ARG CB C 33.24 . 1 1072 98 ARG CG C 26.74 . 1 1073 98 ARG CD C 42.94 . 1 1074 98 ARG NE N 85.60 . 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 59.34 . 1 1082 99 GLU CB C 29.54 . 1 1083 99 GLU CG C 36.44 . 1 1084 99 GLU N N 129.71 . 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 59.34 . 1 1093 100 GLU CG C 36.54 . 1 1094 100 GLU N N 120.21 . 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 54.24 . 1 1103 101 LEU CB C 41.64 . 1 1104 101 LEU CG C 27.94 . 1 1105 101 LEU CD1 C 25.94 . 2 1106 101 LEU CD2 C 22.64 . 2 1107 101 LEU N N 118.81 . 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 45.24 . 1 1112 102 GLY N N 104.31 . 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 52.34 . 1 1117 103 ALA CB C 18.54 . 1 1119 104 ARG H H 10.00 . 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 53.54 . 1 1125 104 ARG CB C 30.24 . 1 1126 104 ARG N N 126.21 . 1 1127 104 ARG NE N 86.00 . 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 64.54 . 1 1136 105 PRO CB C 31.84 . 1 1137 105 PRO CG C 27.24 . 1 1138 105 PRO CD C 50.94 . 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 52.84 . 1 1144 106 ASP CB C 40.14 . 1 1145 106 ASP N N 114.11 . 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 51.44 . 1 1150 107 ALA CB C 20.34 . 1 1151 107 ALA N N 121.71 . 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 63.94 . 1 1158 108 THR CB C 69.34 . 1 1159 108 THR CG2 C 21.94 . 1 1160 108 THR N N 119.91 . 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 56.04 . 1 1172 109 LYS CB C 33.84 . 1 1173 109 LYS CG C 24.04 . 1 1174 109 LYS CD C 29.04 . 1 1175 109 LYS CE C 41.44 . 1 1176 109 LYS N N 128.61 . 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 60.64 . 1 1183 110 VAL CB C 35.54 . 1 1184 110 VAL CG1 C 21.34 . 1 1185 110 VAL CG2 C 22.64 . 1 1186 110 VAL N N 124.41 . 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 52.74 . 1 1195 111 LEU CB C 47.74 . 1 1196 111 LEU CG C 27.74 . 1 1197 111 LEU CD1 C 26.84 . 1 1198 111 LEU CD2 C 26.84 . 1 1199 111 LEU N N 130.21 . 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 59.84 . 1 1208 112 ILE CB C 38.54 . 1 1209 112 ILE CG1 C 27.34 . 1 1210 112 ILE CG2 C 17.14 . 1 1211 112 ILE CD1 C 12.84 . 1 1212 112 ILE N N 124.61 . 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 60.24 . 1 1221 113 ILE CB C 39.04 . 1 1222 113 ILE CG1 C 28.44 . 1 1223 113 ILE CG2 C 16.24 . 1 1224 113 ILE CD1 C 14.04 . 1 1225 113 ILE N N 128.51 . 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 60.64 . 1 1234 114 ILE CB C 40.84 . 1 1235 114 ILE CG1 C 28.44 . 1 1236 114 ILE CG2 C 19.24 . 1 1237 114 ILE CD1 C 15.54 . 1 1238 114 ILE N N 127.61 . 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 59.54 . 1 1245 115 THR CG2 C 17.74 . 1 1246 115 THR N N 120.11 . 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 51.64 . 1 1252 116 ASP CB C 43.94 . 1 1253 116 ASP N N 126.41 . 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 45.84 . 1 1258 117 GLY N N 114.01 . 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 56.24 . 1 1266 118 GLU CB C 30.94 . 1 1267 118 GLU CG C 37.24 . 1 1268 118 GLU N N 116.11 . 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 52.54 . 1 1273 119 ALA CB C 20.54 . 1 1274 119 ALA N N 122.51 . 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 61.04 . 1 1280 120 THR CB C 69.84 . 1 1281 120 THR CG2 C 22.64 . 1 1282 120 THR N N 111.11 . 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 51.74 . 1 1289 121 ASP N N 123.31 . 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 56.74 . 1 1295 122 SER CB C 64.54 . 1 1296 122 SER N N 109.21 . 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 44.74 . 1 1301 123 GLY N N 105.91 . 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 52.34 . 1 1309 124 ASN CB C 41.94 . 1 1310 124 ASN N N 119.81 . 1 1311 124 ASN ND2 N 117.40 . 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 60.14 . 1 1320 125 ILE CB C 38.14 . 1 1321 125 ILE CG1 C 15.74 . 1 1322 125 ILE CG2 C 27.14 . 1 1323 125 ILE CD1 C 19.54 . 1 1324 125 ILE N N 114.31 . 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 58.04 . 1 1330 126 ASP CB C 39.64 . 1 1331 126 ASP N N 126.71 . 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 53.84 . 1 1336 127 ALA CB C 18.04 . 1 1337 127 ALA N N 119.91 . 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 50.14 . 1 1342 128 ALA CB C 19.74 . 1 1343 128 ALA N N 118.01 . 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 59.54 . 1 1355 129 LYS CB C 32.24 . 1 1356 129 LYS CG C 23.84 . 1 1357 129 LYS CD C 29.14 . 1 1358 129 LYS CE C 41.84 . 1 1359 129 LYS N N 118.61 . 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 54.04 . 1 1365 130 ASP CB C 40.14 . 1 1366 130 ASP N N 117.51 . 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 60.44 . 1 1375 131 ILE CB C 39.74 . 1 1376 131 ILE CG1 C 26.44 . 1 1377 131 ILE CG2 C 18.04 . 1 1378 131 ILE CD1 C 13.44 . 1 1379 131 ILE N N 121.51 . 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 61.94 . 1 1388 132 ILE CB C 37.44 . 1 1389 132 ILE CG1 C 27.54 . 1 1390 132 ILE CG2 C 18.04 . 1 1391 132 ILE CD1 C 12.54 . 1 1392 132 ILE N N 130.81 . 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 55.24 . 1 1401 133 ARG CB C 31.64 . 1 1402 133 ARG N N 128.61 . 1 1403 133 ARG NE N 84.10 . 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 56.74 . 1 1413 134 TYR CB C 42.04 . 1 1414 134 TYR CD1 C 132.74 . 1 1415 134 TYR CD2 C 132.74 . 1 1416 134 TYR CE1 C 118.14 . 1 1417 134 TYR CE2 C 118.14 . 1 1418 134 TYR CZ C 130.04 . 1 1419 134 TYR N N 124.81 . 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 58.54 . 1 1429 135 ILE CG1 C 28.94 . 1 1430 135 ILE CG2 C 19.14 . 1 1431 135 ILE CD1 C 14.94 . 1 1432 135 ILE N N 124.51 . 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 59.04 . 1 1441 136 ILE CB C 39.34 . 1 1442 136 ILE CG1 C 27.34 . 1 1443 136 ILE CG2 C 17.64 . 1 1444 136 ILE CD1 C 14.94 . 1 1445 136 ILE N N 128.21 . 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 44.04 . 1 1450 137 GLY N N 113.71 . 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 59.64 . 1 1459 138 ILE CB C 41.54 . 1 1460 138 ILE CG1 C 27.74 . 1 1461 138 ILE CG2 C 15.64 . 1 1462 138 ILE CD1 C 15.94 . 1 1463 138 ILE N N 122.31 . 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 44.94 . 1 1468 139 GLY N N 110.41 . 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 58.54 . 1 1480 140 LYS CB C 32.04 . 1 1481 140 LYS CG C 23.54 . 1 1482 140 LYS CD C 29.04 . 1 1483 140 LYS CE C 41.84 . 1 1484 140 LYS N N 119.01 . 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 58.14 . 1 1492 141 HIS CB C 28.64 . 1 1493 141 HIS CD2 C 120.64 . 1 1494 141 HIS CE1 C 138.94 . 1 1495 141 HIS N N 119.21 . 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 57.04 . 1 1506 142 PHE CB C 38.84 . 1 1507 142 PHE CD1 C 131.44 . 1 1508 142 PHE CD2 C 131.44 . 1 1509 142 PHE N N 116.61 . 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 58.14 . 1 1519 143 GLN CB C 29.54 . 1 1520 143 GLN CG C 34.34 . 1 1521 143 GLN N N 117.61 . 1 1522 143 GLN NE2 N 113.00 . 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 59.74 . 1 1528 144 THR CB C 71.14 . 1 1529 144 THR CG2 C 21.64 . 1 1530 144 THR N N 107.61 . 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 59.34 . 1 1542 145 LYS CB C 31.94 . 1 1543 145 LYS CG C 24.34 . 1 1544 145 LYS CD C 28.94 . 1 1545 145 LYS CE C 41.94 . 1 1546 145 LYS N N 125.21 . 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 60.44 . 1 1554 146 GLU CB C 28.44 . 1 1555 146 GLU CG C 36.94 . 1 1556 146 GLU N N 117.41 . 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 61.74 . 1 1563 147 SER CB C 62.94 . 1 1564 147 SER N N 115.81 . 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 56.84 . 1 1574 148 GLN CB C 30.64 . 1 1575 148 GLN CG C 36.24 . 1 1576 148 GLN N N 124.11 . 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 58.24 . 1 1584 149 GLU CB C 28.54 . 1 1585 149 GLU CG C 37.14 . 1 1586 149 GLU N N 115.41 . 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 65.24 . 1 1592 150 THR CB C 69.04 . 1 1593 150 THR CG2 C 21.54 . 1 1594 150 THR N N 111.91 . 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 55.34 . 1 1603 151 LEU CB C 41.14 . 1 1604 151 LEU CG C 26.04 . 1 1605 151 LEU CD1 C 24.14 . 2 1606 151 LEU CD2 C 20.64 . 2 1607 151 LEU N N 117.61 . 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 58.34 . 1 1615 152 HIS CB C 30.54 . 1 1616 152 HIS CD2 C 117.54 . 1 1617 152 HIS CE1 C 138.94 . 1 1618 152 HIS N N 117.41 . 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 57.44 . 1 1630 153 LYS CB C 31.14 . 1 1631 153 LYS CG C 22.54 . 1 1632 153 LYS CD C 29.14 . 1 1633 153 LYS CE C 41.54 . 1 1634 153 LYS N N 114.31 . 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 56.74 . 1 1645 154 PHE CB C 39.74 . 1 1646 154 PHE CD1 C 130.44 . 1 1647 154 PHE CD2 C 130.44 . 1 1648 154 PHE CE1 C 130.64 . 4 1649 154 PHE CE2 C 130.64 . 4 1650 154 PHE CZ C 130.64 . 4 1651 154 PHE N N 116.01 . 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 51.54 . 1 1656 155 ALA CB C 22.54 . 1 1657 155 ALA N N 121.61 . 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 61.54 . 1 1663 156 SER CB C 61.54 . 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 53.14 . 1 1676 157 LYS CB C 33.04 . 1 1677 157 LYS CG C 24.94 . 1 1678 157 LYS CD C 24.94 . 1 1679 157 LYS CE C 42.34 . 1 1680 157 LYS N N 117.21 . 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 62.04 . 1 1689 158 PRO CB C 34.04 . 1 1690 158 PRO CG C 25.04 . 1 1691 158 PRO CD C 50.04 . 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 55.34 . 1 1696 159 ALA CB C 17.04 . 1 1697 159 ALA N N 128.01 . 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 60.54 . 1 1703 160 SER CB C 61.94 . 1 1704 160 SER N N 108.61 . 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 56.34 . 1 1712 161 GLU CB C 30.84 . 1 1713 161 GLU CG C 35.44 . 1 1714 161 GLU N N 119.61 . 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 6.90 . 4 1722 162 PHE HE2 H 6.90 . 4 1723 162 PHE HZ H 6.90 . 4 1724 162 PHE CA C 59.64 . 1 1725 162 PHE CB C 40.74 . 1 1726 162 PHE CD1 C 132.84 . 1 1727 162 PHE CD2 C 132.84 . 1 1728 162 PHE CE1 C 131.64 . 4 1729 162 PHE CE2 C 131.64 . 4 1730 162 PHE CZ C 131.64 . 4 1731 162 PHE N N 116.01 . 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 60.94 . 1 1738 163 VAL CB C 32.34 . 1 1739 163 VAL CG1 C 21.24 . 1 1740 163 VAL CG2 C 22.14 . 1 1741 163 VAL N N 118.21 . 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 52.84 . 1 1753 164 LYS CB C 34.04 . 1 1754 164 LYS CG C 24.04 . 1 1755 164 LYS CD C 27.84 . 1 1756 164 LYS CE C 42.04 . 1 1757 164 LYS N N 130.61 . 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 56.74 . 1 1766 165 ILE CB C 36.04 . 1 1767 165 ILE CG1 C 25.64 . 1 1768 165 ILE CG2 C 16.84 . 1 1769 165 ILE CD1 C 9.44 . 1 1770 165 ILE N N 125.31 . 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 52.24 . 1 1779 166 LEU CB C 44.64 . 1 1780 166 LEU CG C 26.94 . 1 1781 166 LEU CD1 C 25.14 . 2 1782 166 LEU CD2 C 23.74 . 2 1783 166 LEU N N 127.51 . 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 55.64 . 1 1789 167 ASP CB C 39.64 . 1 1790 167 ASP N N 121.31 . 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 58.14 . 1 1796 168 THR CB C 71.14 . 1 1797 168 THR CG2 C 21.14 . 1 1798 168 THR N N 107.31 . 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 61.44 . 1 1809 169 PHE CB C 39.14 . 1 1810 169 PHE CD1 C 132.04 . 1 1811 169 PHE CD2 C 132.04 . 1 1812 169 PHE CE1 C 131.44 . 4 1813 169 PHE CE2 C 131.44 . 4 1814 169 PHE CZ C 131.44 . 4 1815 169 PHE N N 119.01 . 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 59.14 . 1 1823 170 GLU CB C 29.04 . 1 1824 170 GLU CG C 36.64 . 1 1825 170 GLU N N 121.21 . 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 56.94 . 1 1837 171 LYS CB C 33.34 . 1 1838 171 LYS CG C 25.84 . 1 1839 171 LYS CD C 31.94 . 1 1840 171 LYS CE C 42.04 . 1 1841 171 LYS N N 115.21 . 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 57.74 . 1 1850 172 LEU CB C 41.34 . 1 1851 172 LEU CG C 26.84 . 1 1852 172 LEU CD1 C 24.84 . 2 1853 172 LEU CD2 C 22.54 . 2 1854 172 LEU N N 120.31 . 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 58.44 . 1 1866 173 LYS CB C 32.14 . 1 1867 173 LYS CG C 24.14 . 1 1868 173 LYS CD C 29.04 . 1 1869 173 LYS CE C 42.04 . 1 1870 173 LYS N N 116.11 . 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 54.64 . 1 1876 174 ASP CB C 41.64 . 1 1877 174 ASP N N 117.11 . 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 56.44 . 1 1886 175 LEU CB C 42.74 . 1 1887 175 LEU CG C 27.14 . 1 1888 175 LEU CD1 C 26.04 . 2 1889 175 LEU CD2 C 24.24 . 2 1890 175 LEU N N 120.71 . 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 62.94 . 1 1901 176 PHE CB C 38.54 . 1 1902 176 PHE CD1 C 131.94 . 1 1903 176 PHE CD2 C 131.94 . 1 1904 176 PHE CE1 C 131.34 . 4 1905 176 PHE CE2 C 131.34 . 4 1906 176 PHE CZ C 131.34 . 4 1907 176 PHE N N 119.21 . 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 66.14 . 1 1913 177 THR CB C 68.44 . 1 1914 177 THR CG2 C 21.94 . 1 1915 177 THR N N 112.51 . 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 58.44 . 1 1923 178 GLU CB C 29.74 . 1 1924 178 GLU CG C 35.84 . 1 1925 178 GLU N N 120.41 . 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 57.44 . 1 1934 179 LEU CB C 42.04 . 1 1935 179 LEU CG C 26.74 . 1 1936 179 LEU CD1 C 24.24 . 1 1937 179 LEU CD2 C 24.24 . 1 1938 179 LEU N N 120.31 . 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 58.74 . 1 1946 180 GLN CB C 27.74 . 1 1947 180 GLN CG C 33.64 . 1 1948 180 GLN N N 117.61 . 1 1949 180 GLN NE2 N 111.80 . 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 58.94 . 1 1961 181 LYS CB C 32.84 . 1 1962 181 LYS CG C 24.34 . 1 1963 181 LYS CD C 29.04 . 1 1964 181 LYS CE C 41.94 . 1 1965 181 LYS N N 116.01 . 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 56.54 . 1 1977 182 LYS CB C 31.94 . 1 1978 182 LYS CG C 24.04 . 1 1979 182 LYS CD C 28.04 . 1 1980 182 LYS CE C 41.84 . 1 1981 182 LYS N N 117.11 . 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 62.64 . 1 1990 183 ILE CB C 37.74 . 1 1991 183 ILE CG1 C 27.74 . 1 1992 183 ILE CG2 C 17.44 . 1 1993 183 ILE CD1 C 12.64 . 1 1994 183 ILE N N 116.71 . 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 58.44 . 1 2004 184 TYR CB C 38.14 . 1 2005 184 TYR CD1 C 132.14 . 1 2006 184 TYR CD2 C 132.14 . 1 2007 184 TYR CE1 C 118.44 . 1 2008 184 TYR CE2 C 118.44 . 1 2009 184 TYR N N 120.11 . 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 62.84 . 1 2016 185 VAL CB C 32.14 . 1 2017 185 VAL CG1 C 21.04 . 1 2018 185 VAL CG2 C 21.04 . 1 2019 185 VAL N N 118.51 . 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 61.74 . 1 2029 186 ILE CG1 C 27.64 . 1 2030 186 ILE CG2 C 17.84 . 1 2031 186 ILE CD1 C 13.54 . 1 2032 186 ILE N N 121.71 . 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 2041 187 GLU CG C 36.24 . 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 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 ; 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 ; 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) ; save_