data_5598 #Corrected using PDB structure: 1OV2A # #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 # 79 L HA 3.96 4.70 # 98 A HA 4.24 3.26 # #After reference correction, the following residues still #have a CO chemical shift difference (obs*-pred) greater than 5.0ppm: #NUM AA CS Observed* Predicted # 93 D C 176.23 181.27 # #The average CS difference between predicted and observed: #HA CA CB CO N HN #-0.05 -0.16 0.26 -0.18 -0.01 0.17 # #bmr5598.str.corr chemical shifts have been re-referenced with the following #offsets (these values have been added to the original bmr5598.str file): #HA CA CB CO N HN #N/A +0.05 +0.05 -0.18 -0.01 N/A # #The 95% confidence intervals for the above recommended offsets are: # HA CA CB CO N HN #+/-0.04 +/-0.13 +/-0.16 +/-0.19 +/-0.43 +/-0.10 # #The Correlation Coefficients between predicted and observed #chemical shifts are: #HA CA CB CO N HN #0.734 0.978 0.990 0.735 0.656 0.320 # #The RMSD between predicted and observed* (reference #corrected) chemical shifts are: #HA CA CB CO N HN #0.167 0.578 0.693 0.840 1.921 0.440 # ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 13C and 15N backbone resonance assignments of domain 1 of receptor associated protein ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Wang Yun-Xing . . stop_ _BMRB_accession_number 5598 _BMRB_flat_file_name bmr5598.str _Entry_type new _Submission_date 2002-11-25 _Accession_date 2002-11-26 _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' 627 '15N chemical shifts' 102 '13C chemical shifts' 460 stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_title ; Letter to the Editor: 1H, 13C and 15N resonance assignments of domain 1 of receptor associated protein ; _Citation_status published _Citation_type journal _MEDLINE_UI_code . _PubMed_ID . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Wu YiBing . . 2 Migliorini Molly . . 3 Yu Ping . . 4 Strickland Dudely K. . 5 Wang Yun-Xing . . stop_ _Journal_abbreviation "J. Biomol. NMR" _Journal_volume 26 _Journal_issue 2 _Page_first 187 _Page_last 188 _Year 2003 loop_ _Keyword "receptor associated protein" "domain 1" stop_ save_ ################################## # Molecular system description # ################################## save_system_D1_or_1D_of_RAP_or_RAP39 _Saveframe_category molecular_system _Mol_system_name "receptor associated protein-domain 1" _Abbreviation_common "D1 or 1D of RAP or RAP39" _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label "RAP domain 1" $Domain_1_of_RAP stop_ _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' save_ ######################## # Monomeric polymers # ######################## save_Domain_1_of_RAP _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common "receptor associated protein, domain 1" _Name_variant . _Abbreviation_common "RAP39, RAP" _Mol_thiol_state 'not present' _Details ; The first two residues are cloning artifact. ; ############################## # Polymer residue sequence # ############################## _Residue_count 102 _Mol_residue_sequence ; GSYSREKNQPKPSPKRESGE EFRMEKLNQLWEKAQRLHLP PVRLAELHADLKIQERDELA WKKLKLDGLDEDGEKEARLI RNLNVILAKYGLDGKKDART QV ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 SER 3 TYR 4 SER 5 ARG 6 GLU 7 LYS 8 ASN 9 GLN 10 PRO 11 LYS 12 PRO 13 SER 14 PRO 15 LYS 16 ARG 17 GLU 18 SER 19 GLY 20 GLU 21 GLU 22 PHE 23 ARG 24 MET 25 GLU 26 LYS 27 LEU 28 ASN 29 GLN 30 LEU 31 TRP 32 GLU 33 LYS 34 ALA 35 GLN 36 ARG 37 LEU 38 HIS 39 LEU 40 PRO 41 PRO 42 VAL 43 ARG 44 LEU 45 ALA 46 GLU 47 LEU 48 HIS 49 ALA 50 ASP 51 LEU 52 LYS 53 ILE 54 GLN 55 GLU 56 ARG 57 ASP 58 GLU 59 LEU 60 ALA 61 TRP 62 LYS 63 LYS 64 LEU 65 LYS 66 LEU 67 ASP 68 GLY 69 LEU 70 ASP 71 GLU 72 ASP 73 GLY 74 GLU 75 LYS 76 GLU 77 ALA 78 ARG 79 LEU 80 ILE 81 ARG 82 ASN 83 LEU 84 ASN 85 VAL 86 ILE 87 LEU 88 ALA 89 LYS 90 TYR 91 GLY 92 LEU 93 ASP 94 GLY 95 LYS 96 LYS 97 ASP 98 ALA 99 ARG 100 THR 101 GLN 102 VAL stop_ _Sequence_homology_query_date 2004-07-29 _Sequence_homology_query_revised_last_date 2004-07-17 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 1LRE "Receptor Associated Protein (Rap) Domain 1,Nmr, 20 Structures" 125.93 81 100 100 2e-40 PDB 1NRE "Receptor Associated Protein (Rap) Domain 1,Nmr, Minimized Average Structure" 125.93 81 100 100 2e-40 PDB 1OP1 "A Chain A, Solution Nmr Structure Of Domain1 Of Receptor Associated Protein" 124.39 82 100 100 2e-40 PDB 1OV2 "A Chain A, Ensemble Of The SolutionStructures Of Domain One Of Receptor Associated Protein" 103.03 99 100 100 2e-50 GenBank AAA51553.1 "alpha-2-macroglobulin receptor-associatedprotein" 28.57 357 99 99 4e-51 GenBank AAC67373.1 "lipoprotein receptor associated protein;alpha-2-macroglobulin receptor-associated protein [Homosapiens]" 28.57 357 99 99 4e-51 PIR A39875 "alpha-2-macroglobulin receptor-associatedprotein precursor - human" 28.57 357 99 99 4e-51 REF NP_002328.1 "low density lipoproteinreceptor-related protein associated protein 1;lipoprotein receptor associated protein; alpha-2-MRAP;alpha-2-macroglobulin receptor-associated protein 1; lowdensity lipoprotein-related protein-associated protein1; low density lipoprotein-related protein-associatedprotein 1 (alpha-2-macroglobulin receptor-associatedprotein 1) [Homo sapiens]" 28.57 357 99 99 4e-51 SWISS-PROT P30533 "AMRP_HUMAN Alpha-2-macroglobulinreceptor-associated protein precursor (Alpha-2-MRAP)(Low density lipoprotein receptor-relatedprotein-associated protein 1) (RAP)" 28.57 357 99 99 4e-51 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Domain_1_of_RAP Human 9606 Eukaryota Metazoa Homo sapiens stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name $Domain_1_of_RAP 'recombinant technology' . . . . . 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 $Domain_1_of_RAP 1.2 mM . "sodium chloride" 50 mM . stop_ save_ ####################### # Sample conditions # ####################### save_condition_1 _Saveframe_category sample_conditions loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.5 0 n/a temperature 303 0 K 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 DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 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_Shifts_of_D1_of_the_RAP _Saveframe_category assigned_chemical_shifts loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $condition_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name "RAP domain 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 2 SER CA C 58.42 . . 2 2 SER HA H 4.48 . . 3 2 SER C C 173.93 . . 4 2 SER CB C 64.00 . . 5 2 SER HB2 H 3.82 . . 6 2 SER HB3 H 3.82 . . 7 3 TYR H H 8.35 . . 8 3 TYR N N 122.35 . . 9 3 TYR CA C 58.00 . . 10 3 TYR C C 175.58 . . 11 3 TYR CB C 38.94 . . 12 3 TYR CD1 C 133.05 . . 13 3 TYR HD1 H 7.11 . . 14 3 TYR CD2 C 133.05 . . 15 3 TYR HD2 H 7.11 . . 16 3 TYR CE1 C 118.28 . . 17 3 TYR HE1 H 6.81 . . 18 3 TYR CE2 C 118.28 . . 19 3 TYR HE2 H 6.81 . . 20 4 SER H H 8.15 . . 21 4 SER N N 117.91 . . 22 4 SER CA C 58.18 . . 23 4 SER C C 174.20 . . 24 4 SER CB C 64.00 . . 25 5 ARG H H 8.34 . . 26 5 ARG N N 123.38 . . 27 5 ARG CA C 56.75 . . 28 5 ARG HA H 4.34 . . 29 5 ARG C C 176.28 . . 30 5 ARG CB C 30.74 . . 31 5 ARG HB2 H 1.79 . . 32 5 ARG HB3 H 1.83 . . 33 5 ARG CG C 27.19 . . 34 5 ARG HG2 H 1.63 . . 35 5 ARG HG3 H 1.63 . . 36 5 ARG CD C 43.39 . . 37 5 ARG HD2 H 3.20 . . 38 5 ARG HD3 H 3.20 . . 39 6 GLU H H 8.58 . . 40 6 GLU N N 122.80 . . 41 6 GLU CA C 56.75 . . 42 6 GLU HA H 4.34 . . 43 6 GLU C C 176.36 . . 44 6 GLU CB C 30.49 . . 45 6 GLU HB2 H 1.91 . . 46 6 GLU HB3 H 2.08 . . 47 7 LYS H H 8.24 . . 48 7 LYS N N 121.60 . . 49 7 LYS CA C 56.69 . . 50 7 LYS HA H 4.27 . . 51 7 LYS C C 176.15 . . 52 7 LYS CB C 33.07 . . 53 7 LYS HB2 H 1.42 . . 54 7 LYS HB3 H 1.42 . . 55 7 LYS CG C 29.10 . . 56 7 LYS HG2 H 1.68 . . 57 7 LYS HG3 H 1.68 . . 58 7 LYS CD C 24.85 . . 59 7 LYS HD2 H 1.81 . . 60 7 LYS HD3 H 1.81 . . 61 7 LYS CE C 42.22 . . 62 7 LYS HE2 H 2.99 . . 63 7 LYS HE3 H 2.99 . . 64 8 ASN H H 8.37 . . 65 8 ASN N N 119.08 . . 66 8 ASN CA C 53.54 . . 67 8 ASN HA H 4.62 . . 68 8 ASN C C 174.46 . . 69 8 ASN CB C 39.06 . . 70 8 ASN HB2 H 2.80 . . 71 8 ASN HB3 H 2.80 . . 72 9 GLN H H 7.71 . . 74 9 GLN CA C 53.45 . . 75 9 GLN HA H 4.43 . . 76 9 GLN C C 173.60 . . 77 9 GLN CB C 30.05 . . 78 10 PRO CA C 63.10 . . 79 10 PRO HA H 4.43 . . 80 10 PRO C C 176.39 . . 81 10 PRO CB C 32.20 . . 82 10 PRO HB2 H 1.88 . . 83 10 PRO HB3 H 2.01 . . 84 10 PRO CG C 27.39 . . 85 10 PRO HG2 H 2.28 . . 86 10 PRO HG3 H 2.28 . . 87 10 PRO CD C 50.68 . . 88 10 PRO HD2 H 3.65 . . 89 10 PRO HD3 H 3.78 . . 90 11 LYS H H 8.40 . . 92 11 LYS CA C 54.30 . . 93 11 LYS HA H 4.57 . . 94 11 LYS C C 174.37 . . 95 11 LYS CB C 32.58 . . 96 12 PRO CA C 62.94 . . 97 12 PRO HA H 4.44 . . 98 12 PRO C C 176.50 . . 99 12 PRO CB C 32.29 . . 100 12 PRO HB2 H 1.88 . . 101 12 PRO HB3 H 2.27 . . 102 12 PRO CG C 27.47 . . 103 12 PRO HG2 H 2.02 . . 104 12 PRO HG3 H 2.02 . . 105 12 PRO CD C 50.67 . . 106 12 PRO HD2 H 3.63 . . 107 12 PRO HD3 H 3.82 . . 108 13 SER H H 8.44 . . 110 13 SER CA C 56.52 . . 111 13 SER HA H 4.45 . . 112 13 SER C C 176.50 . . 113 13 SER CB C 63.60 . . 114 14 PRO CA C 63.25 . . 115 14 PRO HA H 4.43 . . 116 14 PRO C C 176.53 . . 117 14 PRO CB C 32.26 . . 118 14 PRO HB2 H 1.90 . . 119 14 PRO HB3 H 2.29 . . 120 14 PRO CG C 27.40 . . 121 14 PRO HG2 H 2.01 . . 122 14 PRO HG3 H 2.01 . . 123 14 PRO CD C 50.81 . . 124 14 PRO HD2 H 3.72 . . 125 14 PRO HD3 H 3.83 . . 126 15 LYS H H 8.30 . . 127 15 LYS N N 121.85 . . 128 15 LYS CA C 56.41 . . 129 15 LYS HA H 4.29 . . 130 15 LYS C C 176.29 . . 131 15 LYS CB C 33.19 . . 132 15 LYS HB2 H 1.73 . . 133 15 LYS HB3 H 1.81 . . 134 15 LYS CG C 24.76 . . 135 15 LYS HG2 H 1.40 . . 136 15 LYS HG3 H 1.40 . . 137 15 LYS CD C 29.14 . . 138 15 LYS HD2 H 1.67 . . 139 15 LYS HD3 H 1.67 . . 140 15 LYS CE C 42.23 . . 141 15 LYS HE2 H 2.98 . . 142 15 LYS HE3 H 2.98 . . 143 16 ARG H H 8.39 . . 144 16 ARG N N 123.29 . . 145 16 ARG CA C 56.66 . . 146 16 ARG HA H 4.31 . . 147 16 ARG C C 176.27 . . 148 16 ARG CB C 30.74 . . 149 16 ARG HB2 H 1.78 . . 150 16 ARG HB3 H 1.90 . . 151 16 ARG CG C 27.36 . . 152 16 ARG HG2 H 1.65 . . 153 16 ARG HG3 H 1.65 . . 154 16 ARG CD C 43.43 . . 155 16 ARG HD2 H 3.21 . . 156 16 ARG HD3 H 3.21 . . 157 17 GLU H H 8.35 . . 158 17 GLU N N 121.22 . . 159 17 GLU CA C 56.85 . . 160 17 GLU HA H 4.24 . . 161 17 GLU C C 176.46 . . 162 17 GLU CB C 30.20 . . 163 17 GLU HB2 H 1.93 . . 164 17 GLU HB3 H 2.09 . . 165 17 GLU CG C 36.68 . . 166 17 GLU HG2 H 2.27 . . 167 17 GLU HG3 H 2.27 . . 168 18 SER H H 8.37 . . 169 18 SER N N 116.32 . . 170 18 SER CA C 58.61 . . 171 18 SER HA H 4.44 . . 172 18 SER C C 174.77 . . 174 18 SER HB2 H 3.86 . . 175 18 SER HB3 H 3.91 . . 176 19 GLY H H 8.38 . . 177 19 GLY N N 110.66 . . 178 19 GLY CA C 45.38 . . 179 19 GLY HA2 H 3.95 . . 180 19 GLY HA3 H 3.99 . . 181 19 GLY C C 173.76 . . 182 20 GLU H H 8.18 . . 183 20 GLU N N 120.17 . . 184 20 GLU CA C 56.10 . . 185 20 GLU HA H 4.35 . . 186 20 GLU C C 176.24 . . 187 20 GLU CB C 30.97 . . 188 20 GLU HB2 H 2.09 . . 189 20 GLU HB3 H 2.09 . . 190 20 GLU CG C 36.46 . . 191 20 GLU HG2 H 2.22 . . 192 20 GLU HG3 H 2.22 . . 193 21 GLU H H 8.51 . . 194 21 GLU N N 123.13 . . 195 21 GLU CA C 57.79 . . 196 21 GLU HA H 3.81 . . 197 21 GLU C C 175.63 . . 198 21 GLU CB C 30.44 . . 199 21 GLU HB2 H 1.83 . . 200 21 GLU HB3 H 1.52 . . 201 21 GLU CG C 35.41 . . 202 21 GLU HG2 H 1.45 . . 203 21 GLU HG3 H 1.72 . . 204 22 PHE H H 8.61 . . 205 22 PHE N N 115.61 . . 206 22 PHE CA C 56.75 . . 207 22 PHE HA H 4.65 . . 208 22 PHE C C 176.16 . . 209 22 PHE CB C 41.64 . . 210 22 PHE HB2 H 2.60 . . 211 22 PHE HB3 H 3.17 . . 212 22 PHE CD1 C 131.94 . . 213 22 PHE HD1 H 7.05 . . 214 22 PHE CD2 C 131.94 . . 215 22 PHE HD2 H 7.05 . . 216 22 PHE CE1 C 130.60 . . 217 22 PHE HE1 H 6.36 . . 218 22 PHE CE2 C 130.60 . . 219 22 PHE HE2 H 6.36 . . 220 22 PHE CZ C 129.46 . . 221 22 PHE HZ H 6.01 . . 222 23 ARG H H 10.01 . . 223 23 ARG N N 120.86 . . 224 23 ARG CA C 56.94 . . 225 23 ARG HA H 4.25 . . 226 23 ARG C C 176.24 . . 227 23 ARG CB C 30.82 . . 228 23 ARG HB2 H 1.73 . . 229 23 ARG HB3 H 2.09 . . 230 23 ARG CG C 27.52 . . 231 23 ARG HG2 H 1.75 . . 232 23 ARG HG3 H 1.75 . . 233 23 ARG CD C 43.40 . . 234 23 ARG HD2 H 3.17 . . 235 23 ARG HD3 H 3.17 . . 236 24 MET H H 7.23 . . 237 24 MET N N 115.30 . . 238 24 MET CA C 54.52 . . 239 24 MET HA H 4.80 . . 240 24 MET C C 176.18 . . 241 24 MET CB C 34.51 . . 242 24 MET HB2 H 2.30 . . 243 24 MET HB3 H 1.85 . . 244 24 MET CG C 32.60 . . 245 24 MET HG2 H 2.68 . . 246 24 MET HG3 H 2.72 . . 247 25 GLU H H 7.71 . . 248 25 GLU N N 117.89 . . 249 25 GLU CA C 60.25 . . 250 25 GLU HA H 4.23 . . 251 25 GLU C C 178.25 . . 252 25 GLU CB C 29.64 . . 253 25 GLU HB2 H 2.07 . . 254 25 GLU HB3 H 2.20 . . 255 25 GLU CG C 35.95 . . 256 25 GLU HG2 H 2.14 . . 257 25 GLU HG3 H 2.37 . . 258 26 LYS H H 9.05 . . 259 26 LYS N N 117.11 . . 260 26 LYS CA C 59.17 . . 261 26 LYS HA H 4.14 . . 262 26 LYS C C 178.39 . . 263 26 LYS CB C 31.66 . . 264 26 LYS HB2 H 1.76 . . 265 26 LYS HB3 H 1.94 . . 266 26 LYS CG C 24.71 . . 267 26 LYS HG2 H 1.35 . . 268 26 LYS HG3 H 1.35 . . 269 26 LYS CD C 29.21 . . 270 26 LYS HD2 H 1.70 . . 271 26 LYS HD3 H 1.70 . . 272 26 LYS CE C 41.79 . . 273 26 LYS HE2 H 2.85 . . 274 26 LYS HE3 H 2.85 . . 275 27 LEU H H 6.89 . . 276 27 LEU N N 115.43 . . 277 27 LEU CA C 56.79 . . 278 27 LEU HA H 4.04 . . 279 27 LEU C C 177.91 . . 280 27 LEU CB C 39.39 . . 281 27 LEU HB2 H 0.72 . . 282 27 LEU HB3 H 1.72 . . 283 27 LEU CG C 27.43 . . 284 27 LEU CD1 C 25.68 . . 285 27 LEU HD1 H 0.88 . . 286 27 LEU CD2 C 21.96 . . 287 27 LEU HD2 H 0.66 . . 288 27 LEU HG H 1.62 . . 289 28 ASN H H 7.72 . . 290 28 ASN N N 118.10 . . 291 28 ASN CA C 57.60 . . 292 28 ASN HA H 4.81 . . 293 28 ASN C C 178.09 . . 294 28 ASN CB C 38.48 . . 295 28 ASN HB2 H 3.00 . . 296 28 ASN HB3 H 3.03 . . 297 28 ASN ND2 N 115.48 . . 298 28 ASN HD21 H 7.49 . . 299 28 ASN HD22 H 7.10 . . 300 29 GLN H H 8.49 . . 301 29 GLN N N 118.54 . . 302 29 GLN CA C 59.21 . . 303 29 GLN HA H 4.16 . . 304 29 GLN C C 179.18 . . 305 29 GLN CB C 28.29 . . 306 29 GLN HB2 H 2.10 . . 307 29 GLN HB3 H 2.21 . . 308 29 GLN CG C 34.23 . . 309 29 GLN HG2 H 2.65 . . 310 29 GLN HG3 H 2.45 . . 311 29 GLN NE2 N 111.65 . . 312 29 GLN HE21 H 6.80 . . 313 29 GLN HE22 H 7.66 . . 314 30 LEU H H 7.47 . . 315 30 LEU N N 120.84 . . 316 30 LEU CA C 58.13 . . 317 30 LEU HA H 4.11 . . 318 30 LEU C C 177.59 . . 319 30 LEU CB C 42.35 . . 320 30 LEU HB2 H 1.38 . . 321 30 LEU HB3 H 1.98 . . 322 30 LEU CD1 C 23.61 . . 323 30 LEU HD1 H 0.91 . . 324 30 LEU CD2 C 23.61 . . 325 30 LEU HD2 H 0.91 . . 326 30 LEU HG H 1.38 . . 327 31 TRP H H 8.21 . . 328 31 TRP N N 120.46 . . 329 31 TRP CA C 58.75 . . 330 31 TRP HA H 4.50 . . 331 31 TRP C C 177.83 . . 332 31 TRP CB C 30.90 . . 333 31 TRP HB2 H 3.66 . . 334 31 TRP HB3 H 3.34 . . 335 31 TRP CD1 C 127.96 . . 336 31 TRP HD1 H 7.55 . . 337 31 TRP NE1 N 129.85 . . 338 31 TRP HE1 H 10.36 . . 339 31 TRP CE3 C 120.21 . . 340 31 TRP HE3 H 7.38 . . 341 31 TRP CZ2 C 115.09 . . 342 31 TRP HZ2 H 7.52 . . 343 31 TRP CZ3 C 121.79 . . 344 31 TRP HZ3 H 7.29 . . 345 31 TRP CH2 C 125.39 . . 346 31 TRP HH2 H 7.27 . . 347 32 GLU H H 8.35 . . 348 32 GLU N N 118.26 . . 349 32 GLU CA C 59.74 . . 350 32 GLU HA H 3.88 . . 351 32 GLU C C 179.36 . . 352 32 GLU CB C 29.40 . . 353 32 GLU HB2 H 2.09 . . 354 32 GLU HB3 H 2.18 . . 355 32 GLU CG C 36.44 . . 356 32 GLU HG2 H 2.31 . . 357 32 GLU HG3 H 2.49 . . 358 33 LYS H H 7.97 . . 359 33 LYS N N 120.53 . . 360 33 LYS CA C 59.65 . . 361 33 LYS HA H 3.86 . . 362 33 LYS C C 178.48 . . 363 33 LYS CB C 32.56 . . 364 33 LYS HB2 H 2.00 . . 365 33 LYS HB3 H 2.00 . . 366 33 LYS CG C 25.47 . . 367 33 LYS HG2 H 1.37 . . 368 33 LYS HG3 H 1.53 . . 369 33 LYS CD C 29.85 . . 370 33 LYS HD2 H 1.70 . . 371 33 LYS HD3 H 1.70 . . 372 33 LYS CE C 42.31 . . 373 33 LYS HE2 H 2.96 . . 374 33 LYS HE3 H 2.96 . . 375 34 ALA H H 8.23 . . 376 34 ALA N N 120.14 . . 377 34 ALA CA C 54.87 . . 378 34 ALA HA H 3.75 . . 379 34 ALA C C 179.00 . . 380 34 ALA CB C 19.07 . . 381 34 ALA HB H 1.22 . . 382 35 GLN H H 7.34 . . 383 35 GLN N N 113.91 . . 384 35 GLN CA C 58.17 . . 385 35 GLN HA H 3.73 . . 386 35 GLN C C 178.78 . . 387 35 GLN CB C 28.91 . . 388 35 GLN HB2 H 2.03 . . 389 35 GLN HB3 H 1.87 . . 390 35 GLN CG C 33.92 . . 391 35 GLN HG2 H 1.82 . . 392 35 GLN HG3 H 1.82 . . 393 35 GLN NE2 N 110.28 . . 394 35 GLN HE21 H 5.62 . . 395 35 GLN HE22 H 5.83 . . 396 36 ARG H H 7.70 . . 397 36 ARG N N 118.94 . . 398 36 ARG CA C 57.67 . . 399 36 ARG HA H 4.08 . . 400 36 ARG C C 177.07 . . 401 36 ARG CB C 30.18 . . 402 36 ARG HB2 H 1.88 . . 403 36 ARG HB3 H 1.91 . . 404 36 ARG CG C 27.80 . . 405 36 ARG HG2 H 1.64 . . 406 36 ARG HG3 H 1.75 . . 407 36 ARG CD C 43.54 . . 408 36 ARG HD2 H 3.19 . . 409 36 ARG HD3 H 3.19 . . 410 37 LEU H H 7.37 . . 411 37 LEU N N 117.99 . . 412 37 LEU CA C 55.06 . . 413 37 LEU HA H 4.20 . . 414 37 LEU C C 176.30 . . 415 37 LEU CB C 42.32 . . 416 37 LEU HB2 H 1.63 . . 417 37 LEU HB3 H 1.75 . . 418 37 LEU CG C 27.55 . . 419 37 LEU CD1 C 22.55 . . 420 37 LEU HD1 H 0.87 . . 421 37 LEU CD2 C 22.55 . . 422 37 LEU HD2 H 0.87 . . 423 37 LEU HG H 1.62 . . 424 38 HIS H H 7.82 . . 425 38 HIS N N 114.33 . . 426 38 HIS CA C 56.07 . . 427 38 HIS HA H 4.22 . . 428 38 HIS C C 174.79 . . 429 38 HIS CB C 26.01 . . 430 38 HIS HB2 H 3.28 . . 431 38 HIS HB3 H 3.42 . . 432 38 HIS CD2 C 120.07 . . 433 38 HIS HD2 H 7.18 . . 434 38 HIS CE1 C 136.55 . . 435 38 HIS HE1 H 8.36 . . 436 39 LEU H H 7.80 . . 438 39 LEU CA C 54.33 . . 439 39 LEU HA H 4.50 . . 441 39 LEU CB C 41.68 . . 442 39 LEU HB2 H 1.37 . . 443 39 LEU HB3 H 1.52 . . 444 39 LEU CG C 28.27 . . 445 39 LEU CD1 C 25.39 . . 446 39 LEU HD1 H 1.02 . . 447 39 LEU CD2 C 23.99 . . 448 39 LEU HD2 H 1.02 . . 449 39 LEU HG H 1.87 . . 450 40 PRO CA C 61.60 . . 451 40 PRO HA H 4.80 . . 452 40 PRO CB C 31.54 . . 453 40 PRO HB2 H 2.00 . . 454 40 PRO HB3 H 2.61 . . 455 40 PRO CG C 28.08 . . 456 40 PRO HG2 H 2.17 . . 457 40 PRO HG3 H 2.27 . . 458 40 PRO CD C 50.48 . . 459 40 PRO HD2 H 4.11 . . 460 40 PRO HD3 H 3.56 . . 461 41 PRO CA C 66.73 . . 462 41 PRO HA H 4.21 . . 463 41 PRO C C 179.16 . . 464 41 PRO CB C 32.09 . . 465 41 PRO HB2 H 2.08 . . 466 41 PRO HB3 H 2.46 . . 467 41 PRO CG C 27.69 . . 468 41 PRO HG2 H 2.14 . . 469 41 PRO HG3 H 2.27 . . 470 41 PRO CD C 50.62 . . 471 41 PRO HD2 H 3.97 . . 472 41 PRO HD3 H 3.93 . . 473 42 VAL H H 8.59 . . 474 42 VAL N N 116.37 . . 475 42 VAL CA C 65.84 . . 476 42 VAL HA H 4.04 . . 477 42 VAL C C 177.51 . . 478 42 VAL CB C 31.47 . . 479 42 VAL HB H 2.16 . . 480 42 VAL CG1 C 22.03 . . 481 42 VAL HG1 H 1.09 . . 482 42 VAL CG2 C 20.82 . . 483 42 VAL HG2 H 1.02 . . 484 43 ARG H H 7.24 . . 485 43 ARG N N 120.22 . . 486 43 ARG CA C 57.70 . . 487 43 ARG HA H 4.57 . . 488 43 ARG C C 178.31 . . 489 43 ARG CB C 30.82 . . 490 43 ARG HB2 H 2.11 . . 491 43 ARG HB3 H 2.11 . . 492 43 ARG CG C 26.94 . . 493 43 ARG HG2 H 1.91 . . 494 43 ARG HG3 H 2.05 . . 495 43 ARG CD C 43.27 . . 496 43 ARG HD2 H 3.36 . . 497 43 ARG HD3 H 3.53 . . 498 44 LEU H H 8.26 . . 499 44 LEU N N 120.10 . . 500 44 LEU CA C 58.09 . . 501 44 LEU HA H 4.08 . . 502 44 LEU C C 178.58 . . 503 44 LEU CB C 41.74 . . 504 44 LEU HB2 H 1.79 . . 505 44 LEU HB3 H 1.79 . . 506 44 LEU CG C 26.63 . . 507 44 LEU CD1 C 24.39 . . 508 44 LEU HD1 H 0.56 . . 509 44 LEU CD2 C 25.61 . . 510 44 LEU HD2 H 0.69 . . 511 44 LEU HG H 1.65 . . 512 45 ALA H H 8.02 . . 513 45 ALA N N 120.38 . . 514 45 ALA CA C 55.15 . . 515 45 ALA HA H 4.30 . . 516 45 ALA C C 181.10 . . 517 45 ALA CB C 17.95 . . 518 45 ALA HB H 1.58 . . 519 46 GLU H H 7.70 . . 520 46 GLU N N 122.15 . . 521 46 GLU CA C 59.76 . . 522 46 GLU HA H 4.12 . . 523 46 GLU C C 178.66 . . 524 46 GLU CB C 29.73 . . 525 46 GLU HB2 H 2.51 . . 526 46 GLU HB3 H 2.59 . . 527 46 GLU CG C 36.79 . . 528 46 GLU HG2 H 2.43 . . 529 46 GLU HG3 H 2.72 . . 530 47 LEU H H 8.50 . . 531 47 LEU N N 121.94 . . 532 47 LEU CA C 58.32 . . 533 47 LEU HA H 3.70 . . 534 47 LEU C C 177.86 . . 535 47 LEU CB C 40.14 . . 536 47 LEU HB2 H 2.03 . . 537 47 LEU HB3 H 0.55 . . 538 47 LEU CG C 27.27 . . 539 47 LEU CD1 C 23.28 . . 540 47 LEU HD1 H 0.39 . . 541 47 LEU CD2 C 28.12 . . 542 47 LEU HD2 H 0.73 . . 543 47 LEU HG H 1.38 . . 544 48 HIS H H 8.91 . . 545 48 HIS N N 119.16 . . 546 48 HIS CA C 61.90 . . 547 48 HIS HA H 3.53 . . 548 48 HIS C C 176.60 . . 549 48 HIS CB C 29.66 . . 550 48 HIS HB2 H 3.18 . . 551 48 HIS HB3 H 3.42 . . 552 48 HIS CD2 C 117.73 . . 553 48 HIS HD2 H 5.14 . . 554 48 HIS CE1 C 136.76 . . 555 48 HIS HE1 H 7.80 . . 556 49 ALA H H 7.65 . . 557 49 ALA N N 119.33 . . 558 49 ALA CA C 55.36 . . 559 49 ALA HA H 4.18 . . 560 49 ALA C C 180.83 . . 561 49 ALA CB C 18.07 . . 562 49 ALA HB H 1.64 . . 563 50 ASP H H 8.34 . . 564 50 ASP N N 120.66 . . 565 50 ASP CA C 57.86 . . 566 50 ASP HA H 4.60 . . 567 50 ASP C C 179.90 . . 568 50 ASP CB C 40.99 . . 569 50 ASP HB2 H 2.60 . . 570 50 ASP HB3 H 2.95 . . 571 51 LEU H H 9.05 . . 572 51 LEU N N 120.46 . . 573 51 LEU CA C 57.20 . . 574 51 LEU HA H 3.90 . . 575 51 LEU C C 178.68 . . 576 51 LEU CB C 41.89 . . 577 51 LEU HB2 H 1.77 . . 578 51 LEU HB3 H 1.77 . . 579 51 LEU CG C 26.23 . . 580 51 LEU CD1 C 26.40 . . 581 51 LEU HD1 H 0.63 . . 582 51 LEU CD2 C 22.55 . . 583 51 LEU HD2 H 0.62 . . 584 51 LEU HG H 1.77 . . 585 52 LYS H H 8.34 . . 586 52 LYS N N 120.65 . . 587 52 LYS CA C 58.24 . . 588 52 LYS HA H 4.17 . . 589 52 LYS C C 180.05 . . 590 52 LYS CB C 31.75 . . 591 52 LYS HB2 H 1.83 . . 592 52 LYS HB3 H 2.16 . . 593 52 LYS CG C 24.35 . . 594 52 LYS HG2 H 1.29 . . 595 52 LYS HG3 H 1.46 . . 596 52 LYS CD C 28.42 . . 597 52 LYS HD2 H 1.60 . . 598 52 LYS HD3 H 1.60 . . 599 52 LYS CE C 41.47 . . 600 52 LYS HE2 H 2.83 . . 601 52 LYS HE3 H 2.39 . . 602 53 ILE H H 7.62 . . 603 53 ILE N N 122.62 . . 604 53 ILE CA C 64.80 . . 605 53 ILE HA H 3.73 . . 606 53 ILE C C 177.10 . . 607 53 ILE CB C 37.53 . . 608 53 ILE HB H 2.12 . . 609 53 ILE CG2 C 17.55 . . 610 53 ILE HG2 H 0.94 . . 611 53 ILE CG1 C 29.12 . . 612 53 ILE HG12 H 1.76 . . 613 53 ILE HG13 H 1.25 . . 614 53 ILE CD1 C 12.48 . . 615 53 ILE HD1 H 0.91 . . 616 54 GLN H H 7.83 . . 617 54 GLN N N 120.27 . . 618 54 GLN CA C 58.98 . . 619 54 GLN HA H 3.90 . . 620 54 GLN C C 177.61 . . 621 54 GLN CB C 26.46 . . 622 54 GLN HB2 H 2.01 . . 623 54 GLN HB3 H 2.18 . . 624 54 GLN CG C 31.63 . . 625 54 GLN HG2 H 2.17 . . 626 54 GLN HG3 H 2.43 . . 627 54 GLN NE2 N 111.97 . . 628 54 GLN HE21 H 8.76 . . 629 54 GLN HE22 H 6.55 . . 630 55 GLU H H 8.88 . . 631 55 GLU N N 119.65 . . 632 55 GLU CA C 60.30 . . 633 55 GLU HA H 3.75 . . 634 55 GLU C C 177.03 . . 635 55 GLU CB C 30.77 . . 636 55 GLU HB2 H 2.23 . . 637 55 GLU HB3 H 2.46 . . 638 55 GLU CG C 37.96 . . 639 55 GLU HG2 H 2.13 . . 640 55 GLU HG3 H 2.13 . . 641 56 ARG H H 7.75 . . 642 56 ARG N N 119.03 . . 643 56 ARG CA C 59.83 . . 644 56 ARG HA H 4.03 . . 645 56 ARG C C 179.74 . . 646 56 ARG CB C 29.71 . . 647 56 ARG HB2 H 2.09 . . 648 56 ARG HB3 H 2.24 . . 649 56 ARG CG C 26.72 . . 650 56 ARG HG2 H 1.59 . . 651 56 ARG HG3 H 1.98 . . 652 56 ARG CD C 43.57 . . 653 56 ARG HD2 H 3.23 . . 654 56 ARG HD3 H 3.29 . . 655 57 ASP H H 8.46 . . 656 57 ASP N N 121.45 . . 657 57 ASP CA C 57.48 . . 658 57 ASP HA H 4.51 . . 659 57 ASP C C 179.52 . . 660 57 ASP CB C 39.94 . . 661 57 ASP HB2 H 2.62 . . 662 57 ASP HB3 H 2.78 . . 663 58 GLU H H 9.22 . . 664 58 GLU N N 123.97 . . 665 58 GLU CA C 60.79 . . 666 58 GLU HA H 4.27 . . 667 58 GLU C C 179.51 . . 668 58 GLU CB C 29.23 . . 669 58 GLU HB2 H 2.35 . . 670 58 GLU HB3 H 2.28 . . 671 58 GLU CG C 37.34 . . 672 58 GLU HG2 H 2.35 . . 673 58 GLU HG3 H 2.52 . . 674 59 LEU H H 8.63 . . 675 59 LEU N N 120.62 . . 676 59 LEU CA C 58.23 . . 677 59 LEU HA H 4.16 . . 678 59 LEU C C 180.09 . . 679 59 LEU CB C 41.55 . . 680 59 LEU HB2 H 1.54 . . 681 59 LEU HB3 H 1.99 . . 682 59 LEU CG C 26.59 . . 683 59 LEU CD1 C 26.03 . . 684 59 LEU HD1 H 0.92 . . 685 59 LEU CD2 C 23.00 . . 686 59 LEU HD2 H 0.92 . . 687 59 LEU HG H 1.90 . . 688 60 ALA H H 8.06 . . 689 60 ALA N N 122.00 . . 690 60 ALA CA C 55.18 . . 691 60 ALA HA H 4.20 . . 692 60 ALA C C 180.52 . . 693 60 ALA CB C 18.27 . . 694 60 ALA HB H 1.62 . . 695 61 TRP H H 8.44 . . 696 61 TRP N N 120.85 . . 697 61 TRP CA C 61.39 . . 698 61 TRP HA H 4.13 . . 699 61 TRP C C 176.22 . . 700 61 TRP CB C 28.36 . . 701 61 TRP HB2 H 3.60 . . 702 61 TRP HB3 H 3.37 . . 703 61 TRP CD1 C 125.71 . . 704 61 TRP HD1 H 6.89 . . 705 61 TRP NE1 N 130.01 . . 706 61 TRP HE1 H 10.93 . . 707 61 TRP CE3 C 121.13 . . 708 61 TRP HE3 H 7.08 . . 709 61 TRP CZ2 C 113.87 . . 710 61 TRP HZ2 H 7.54 . . 711 61 TRP CZ3 C 120.83 . . 712 61 TRP HZ3 H 7.69 . . 713 61 TRP CH2 C 124.36 . . 714 61 TRP HH2 H 7.15 . . 715 62 LYS H H 8.26 . . 716 62 LYS N N 118.98 . . 717 62 LYS CA C 59.51 . . 718 62 LYS HA H 3.05 . . 719 62 LYS C C 178.41 . . 720 62 LYS CB C 32.19 . . 721 62 LYS HB2 H 1.98 . . 722 62 LYS HB3 H 1.86 . . 723 62 LYS CG C 25.10 . . 724 62 LYS HG2 H 1.50 . . 725 62 LYS HG3 H 1.73 . . 726 62 LYS CD C 29.45 . . 727 62 LYS HD2 H 1.73 . . 728 62 LYS HD3 H 1.73 . . 729 62 LYS CE C 42.10 . . 730 62 LYS HE2 H 3.00 . . 731 62 LYS HE3 H 3.00 . . 732 63 LYS H H 7.00 . . 733 63 LYS N N 116.88 . . 734 63 LYS CA C 59.02 . . 735 63 LYS HA H 3.96 . . 736 63 LYS C C 177.80 . . 737 63 LYS CB C 32.43 . . 738 63 LYS HB2 H 1.92 . . 739 63 LYS HB3 H 1.86 . . 740 63 LYS CG C 25.02 . . 741 63 LYS HG2 H 1.41 . . 742 63 LYS HG3 H 1.51 . . 743 63 LYS CD C 28.96 . . 744 63 LYS HD2 H 1.67 . . 745 63 LYS HD3 H 1.67 . . 746 63 LYS CE C 42.32 . . 747 63 LYS HE2 H 3.09 . . 748 63 LYS HE3 H 3.13 . . 749 64 LEU H H 7.40 . . 750 64 LEU N N 119.35 . . 751 64 LEU CA C 57.94 . . 752 64 LEU HA H 4.03 . . 753 64 LEU C C 179.16 . . 754 64 LEU CB C 41.44 . . 755 64 LEU HB2 H 1.30 . . 756 64 LEU HB3 H 1.90 . . 757 64 LEU CG C 26.35 . . 758 64 LEU CD1 C 26.11 . . 759 64 LEU HD1 H 0.92 . . 760 64 LEU CD2 C 23.98 . . 761 64 LEU HD2 H 0.92 . . 762 64 LEU HG H 1.66 . . 763 65 LYS H H 8.38 . . 764 65 LYS N N 119.67 . . 765 65 LYS CA C 57.34 . . 766 65 LYS HA H 3.75 . . 767 65 LYS C C 180.98 . . 768 65 LYS CB C 31.06 . . 769 65 LYS HB2 H 0.82 . . 770 65 LYS HB3 H 1.31 . . 771 65 LYS CG C 23.46 . . 772 65 LYS HG2 H 0.88 . . 773 65 LYS HG3 H 1.04 . . 774 65 LYS CD C 28.52 . . 775 65 LYS HD2 H 1.65 . . 776 65 LYS HD3 H 1.80 . . 777 65 LYS CE C 42.09 . . 778 65 LYS HE2 H 3.05 . . 779 65 LYS HE3 H 2.97 . . 780 66 LEU H H 7.74 . . 781 66 LEU N N 122.22 . . 782 66 LEU CA C 57.62 . . 783 66 LEU HA H 4.04 . . 784 66 LEU C C 178.14 . . 785 66 LEU CB C 41.64 . . 786 66 LEU HB2 H 1.63 . . 787 66 LEU HB3 H 1.79 . . 788 66 LEU CG C 26.84 . . 789 66 LEU CD1 C 23.44 . . 790 66 LEU HD1 H 0.87 . . 791 66 LEU CD2 C 23.44 . . 792 66 LEU HD2 H 0.87 . . 793 66 LEU HG H 1.72 . . 794 67 ASP H H 7.64 . . 795 67 ASP N N 118.06 . . 796 67 ASP CA C 54.80 . . 797 67 ASP HA H 4.70 . . 798 67 ASP C C 176.18 . . 800 67 ASP HB2 H 2.84 . . 801 67 ASP HB3 H 2.69 . . 802 68 GLY H H 7.75 . . 803 68 GLY N N 107.33 . . 804 68 GLY CA C 46.17 . . 805 68 GLY HA2 H 3.92 . . 806 68 GLY HA3 H 4.17 . . 807 68 GLY C C 175.29 . . 808 69 LEU H H 7.93 . . 809 69 LEU N N 119.09 . . 810 69 LEU CA C 54.57 . . 811 69 LEU HA H 4.61 . . 812 69 LEU C C 176.01 . . 813 69 LEU CB C 41.96 . . 814 69 LEU HB2 H 1.78 . . 815 69 LEU HB3 H 1.66 . . 816 69 LEU CG C 27.39 . . 817 69 LEU CD1 C 25.83 . . 818 69 LEU HD1 H 1.00 . . 819 69 LEU CD2 C 22.83 . . 820 69 LEU HD2 H 0.88 . . 821 69 LEU HG H 1.50 . . 822 70 ASP H H 8.91 . . 823 70 ASP N N 120.37 . . 824 70 ASP CA C 54.15 . . 825 70 ASP HA H 5.21 . . 826 70 ASP C C 177.36 . . 827 70 ASP CB C 43.20 . . 828 70 ASP HB2 H 2.84 . . 829 70 ASP HB3 H 2.13 . . 830 71 GLU H H 8.76 . . 831 71 GLU N N 120.66 . . 832 71 GLU CA C 59.13 . . 833 71 GLU HA H 4.06 . . 834 71 GLU C C 177.68 . . 835 71 GLU CB C 29.84 . . 836 71 GLU HB2 H 2.02 . . 837 71 GLU HB3 H 2.09 . . 838 71 GLU CG C 36.73 . . 839 71 GLU HG2 H 2.28 . . 840 71 GLU HG3 H 2.36 . . 841 72 ASP H H 8.15 . . 842 72 ASP N N 115.33 . . 843 72 ASP CA C 53.52 . . 844 72 ASP HA H 4.66 . . 845 72 ASP C C 177.46 . . 847 72 ASP HB2 H 3.02 . . 848 72 ASP HB3 H 2.73 . . 849 73 GLY H H 7.65 . . 850 73 GLY N N 108.31 . . 851 73 GLY CA C 46.36 . . 852 73 GLY HA2 H 4.10 . . 853 73 GLY HA3 H 4.24 . . 854 73 GLY C C 175.54 . . 855 74 GLU H H 8.26 . . 856 74 GLU N N 122.33 . . 857 74 GLU CA C 59.71 . . 858 74 GLU HA H 4.07 . . 859 74 GLU C C 179.55 . . 860 74 GLU CB C 29.91 . . 861 74 GLU HB2 H 2.16 . . 862 74 GLU HB3 H 2.16 . . 863 74 GLU CG C 36.47 . . 864 74 GLU HG2 H 2.16 . . 865 74 GLU HG3 H 2.34 . . 866 75 LYS H H 10.16 . . 867 75 LYS N N 121.96 . . 868 75 LYS CA C 59.65 . . 869 75 LYS HA H 4.09 . . 870 75 LYS C C 179.47 . . 871 75 LYS CB C 31.55 . . 872 75 LYS HB2 H 1.95 . . 873 75 LYS HB3 H 1.84 . . 874 75 LYS CG C 26.30 . . 875 75 LYS HG2 H 1.50 . . 876 75 LYS HG3 H 1.67 . . 877 75 LYS CD C 29.55 . . 878 75 LYS HD2 H 1.65 . . 879 75 LYS HD3 H 1.81 . . 880 75 LYS CE C 42.60 . . 881 75 LYS HE2 H 3.10 . . 882 75 LYS HE3 H 3.10 . . 883 76 GLU H H 8.61 . . 884 76 GLU N N 125.11 . . 885 76 GLU CA C 59.08 . . 886 76 GLU HA H 2.78 . . 887 76 GLU C C 177.47 . . 888 76 GLU CB C 29.49 . . 889 76 GLU HB2 H 1.92 . . 890 76 GLU HB3 H 2.07 . . 891 76 GLU CG C 35.45 . . 892 76 GLU HG2 H 1.33 . . 893 76 GLU HG3 H 1.92 . . 894 77 ALA H H 8.01 . . 895 77 ALA N N 118.99 . . 896 77 ALA CA C 55.12 . . 897 77 ALA HA H 3.94 . . 898 77 ALA C C 180.55 . . 899 77 ALA CB C 17.92 . . 900 77 ALA HB H 1.45 . . 901 78 ARG H H 7.52 . . 902 78 ARG N N 118.93 . . 903 78 ARG CA C 59.15 . . 904 78 ARG HA H 3.89 . . 905 78 ARG C C 177.48 . . 906 78 ARG CB C 30.15 . . 907 78 ARG HB2 H 1.91 . . 908 78 ARG HB3 H 1.91 . . 909 78 ARG CG C 27.55 . . 910 78 ARG HG2 H 1.63 . . 911 78 ARG HG3 H 1.77 . . 912 78 ARG CD C 43.49 . . 913 78 ARG HD2 H 3.22 . . 914 78 ARG HD3 H 3.22 . . 915 79 LEU H H 7.42 . . 916 79 LEU N N 120.35 . . 917 79 LEU CA C 58.23 . . 918 79 LEU HA H 4.01 . . 919 79 LEU C C 179.78 . . 920 79 LEU CB C 42.01 . . 921 79 LEU HB2 H 1.38 . . 922 79 LEU HB3 H 1.65 . . 923 79 LEU CG C 26.55 . . 924 79 LEU CD1 C 25.68 . . 925 79 LEU HD1 H 0.57 . . 926 79 LEU CD2 C 24.43 . . 927 79 LEU HD2 H 0.68 . . 928 79 LEU HG H 1.50 . . 929 80 ILE H H 7.71 . . 930 80 ILE N N 120.26 . . 931 80 ILE CA C 64.53 . . 932 80 ILE HA H 3.59 . . 933 80 ILE C C 178.20 . . 934 80 ILE CB C 38.28 . . 935 80 ILE HB H 1.76 . . 936 80 ILE CG2 C 16.94 . . 937 80 ILE HG2 H 0.86 . . 938 80 ILE CG1 C 28.89 . . 939 80 ILE HG12 H 1.01 . . 940 80 ILE HG13 H 1.54 . . 941 80 ILE CD1 C 13.25 . . 942 80 ILE HD1 H 0.73 . . 943 81 ARG H H 7.91 . . 944 81 ARG N N 120.62 . . 945 81 ARG CA C 59.90 . . 946 81 ARG HA H 4.05 . . 947 81 ARG C C 179.06 . . 948 81 ARG CB C 29.93 . . 949 81 ARG HB2 H 1.92 . . 950 81 ARG HB3 H 1.96 . . 951 81 ARG CG C 27.55 . . 952 81 ARG HG2 H 1.55 . . 953 81 ARG HG3 H 1.83 . . 954 81 ARG CD C 43.75 . . 955 81 ARG HD2 H 3.18 . . 956 81 ARG HD3 H 3.24 . . 957 82 ASN H H 8.40 . . 958 82 ASN N N 118.29 . . 959 82 ASN CA C 55.96 . . 960 82 ASN HA H 4.42 . . 961 82 ASN C C 178.30 . . 962 82 ASN CB C 37.59 . . 963 82 ASN HB2 H 2.97 . . 964 82 ASN HB3 H 3.03 . . 965 82 ASN ND2 N 111.60 . . 966 82 ASN HD21 H 8.32 . . 967 82 ASN HD22 H 6.69 . . 968 83 LEU H H 7.95 . . 969 83 LEU N N 122.54 . . 970 83 LEU CA C 58.04 . . 971 83 LEU HA H 4.00 . . 972 83 LEU C C 177.99 . . 973 83 LEU CB C 40.70 . . 974 83 LEU HB2 H 2.01 . . 975 83 LEU HB3 H 1.54 . . 976 83 LEU CG C 27.00 . . 977 83 LEU CD1 C 22.95 . . 978 83 LEU HD1 H 0.72 . . 979 83 LEU CD2 C 25.81 . . 980 83 LEU HD2 H 0.83 . . 981 83 LEU HG H 1.54 . . 982 84 ASN H H 8.15 . . 983 84 ASN N N 118.15 . . 984 84 ASN CA C 56.46 . . 985 84 ASN HA H 4.43 . . 986 84 ASN C C 178.74 . . 987 84 ASN CB C 37.60 . . 988 84 ASN HB2 H 3.02 . . 989 84 ASN HB3 H 2.77 . . 990 84 ASN ND2 N 111.28 . . 991 84 ASN HD21 H 6.83 . . 992 84 ASN HD22 H 7.45 . . 993 85 VAL H H 8.06 . . 994 85 VAL N N 122.75 . . 995 85 VAL CA C 66.94 . . 996 85 VAL HA H 3.71 . . 997 85 VAL C C 178.35 . . 998 85 VAL CB C 31.65 . . 999 85 VAL HB H 2.34 . . 1000 85 VAL CG1 C 22.87 . . 1001 85 VAL HG1 H 1.12 . . 1002 85 VAL CG2 C 21.05 . . 1003 85 VAL HG2 H 0.94 . . 1004 86 ILE H H 7.56 . . 1005 86 ILE N N 121.89 . . 1006 86 ILE CA C 66.26 . . 1007 86 ILE HA H 3.68 . . 1008 86 ILE C C 177.61 . . 1009 86 ILE CB C 38.25 . . 1010 86 ILE HB H 2.25 . . 1011 86 ILE CG2 C 17.36 . . 1012 86 ILE HG2 H 0.93 . . 1013 86 ILE CG1 C 29.81 . . 1014 86 ILE HG12 H 1.08 . . 1015 86 ILE HG13 H 2.00 . . 1016 86 ILE CD1 C 13.94 . . 1017 86 ILE HD1 H 0.82 . . 1018 87 LEU H H 8.50 . . 1019 87 LEU N N 117.31 . . 1020 87 LEU CA C 59.16 . . 1021 87 LEU HA H 3.91 . . 1022 87 LEU C C 179.36 . . 1023 87 LEU CB C 41.55 . . 1024 87 LEU HB2 H 1.30 . . 1025 87 LEU HB3 H 1.97 . . 1026 87 LEU CG C 26.90 . . 1027 87 LEU CD1 C 24.65 . . 1028 87 LEU HD1 H 0.82 . . 1029 87 LEU CD2 C 25.62 . . 1030 87 LEU HD2 H 0.93 . . 1031 87 LEU HG H 1.97 . . 1032 88 ALA H H 7.71 . . 1033 88 ALA N N 119.11 . . 1034 88 ALA CA C 54.41 . . 1035 88 ALA HA H 4.20 . . 1036 88 ALA C C 180.33 . . 1037 88 ALA CB C 18.50 . . 1038 88 ALA HB H 1.49 . . 1039 89 LYS H H 8.38 . . 1040 89 LYS N N 120.59 . . 1041 89 LYS CA C 59.30 . . 1042 89 LYS HA H 3.82 . . 1043 89 LYS C C 177.84 . . 1044 89 LYS CB C 33.07 . . 1045 89 LYS HB2 H 1.62 . . 1046 89 LYS HB3 H 1.77 . . 1047 89 LYS CG C 24.50 . . 1048 89 LYS HG2 H 0.30 . . 1049 89 LYS HG3 H 1.11 . . 1050 89 LYS CD C 30.10 . . 1051 89 LYS HD2 H 1.42 . . 1052 89 LYS HD3 H 1.51 . . 1053 89 LYS CE C 41.86 . . 1054 89 LYS HE2 H 2.69 . . 1055 89 LYS HE3 H 2.75 . . 1056 90 TYR H H 7.28 . . 1057 90 TYR N N 111.75 . . 1058 90 TYR CA C 58.10 . . 1059 90 TYR HA H 4.57 . . 1060 90 TYR C C 174.84 . . 1062 90 TYR HB2 H 3.35 . . 1063 90 TYR HB3 H 2.51 . . 1064 90 TYR CD1 C 134.15 . . 1065 90 TYR HD1 H 7.42 . . 1066 90 TYR CD2 C 134.15 . . 1067 90 TYR HD2 H 7.42 . . 1068 90 TYR CE1 C 117.86 . . 1069 90 TYR HE1 H 7.02 . . 1070 90 TYR CE2 C 117.86 . . 1071 90 TYR HE2 H 7.02 . . 1072 91 GLY H H 7.57 . . 1073 91 GLY N N 107.69 . . 1074 91 GLY CA C 46.94 . . 1075 91 GLY HA2 H 4.04 . . 1076 91 GLY HA3 H 4.12 . . 1077 91 GLY C C 175.76 . . 1078 92 LEU H H 8.35 . . 1079 92 LEU N N 117.80 . . 1080 92 LEU CA C 54.89 . . 1081 92 LEU HA H 4.34 . . 1082 92 LEU C C 175.52 . . 1083 92 LEU CB C 43.53 . . 1084 92 LEU HB2 H 1.75 . . 1085 92 LEU HB3 H 1.75 . . 1086 92 LEU CG C 26.35 . . 1087 92 LEU CD1 C 26.25 . . 1088 92 LEU HD1 H 0.93 . . 1089 92 LEU CD2 C 23.15 . . 1090 92 LEU HD2 H 0.79 . . 1091 92 LEU HG H 1.68 . . 1092 93 ASP H H 8.43 . . 1093 93 ASP N N 118.49 . . 1094 93 ASP CA C 53.50 . . 1095 93 ASP HA H 4.50 . . 1096 93 ASP C C 176.23 . . 1098 93 ASP HB2 H 2.48 . . 1099 93 ASP HB3 H 2.73 . . 1100 94 GLY H H 8.17 . . 1101 94 GLY N N 108.64 . . 1102 94 GLY CA C 45.65 . . 1103 94 GLY HA2 H 3.90 . . 1104 94 GLY HA3 H 3.94 . . 1105 94 GLY C C 174.13 . . 1106 95 LYS H H 8.07 . . 1107 95 LYS N N 120.73 . . 1108 95 LYS CA C 56.66 . . 1109 95 LYS HA H 4.27 . . 1110 95 LYS C C 176.04 . . 1111 95 LYS CB C 33.16 . . 1112 95 LYS HB2 H 1.38 . . 1113 95 LYS HB3 H 1.43 . . 1114 95 LYS CG C 24.89 . . 1115 95 LYS HG2 H 1.67 . . 1116 95 LYS HG3 H 1.67 . . 1117 95 LYS CD C 29.07 . . 1118 95 LYS HD2 H 1.81 . . 1119 95 LYS HD3 H 1.81 . . 1120 95 LYS CE C 42.22 . . 1121 95 LYS HE2 H 2.98 . . 1122 95 LYS HE3 H 2.98 . . 1123 96 LYS H H 8.32 . . 1124 96 LYS N N 122.17 . . 1125 96 LYS CA C 56.51 . . 1126 96 LYS HA H 4.31 . . 1127 96 LYS C C 175.74 . . 1128 96 LYS CB C 33.22 . . 1129 96 LYS HB2 H 1.40 . . 1130 96 LYS HB3 H 1.40 . . 1131 96 LYS CG C 24.69 . . 1132 96 LYS HG2 H 1.67 . . 1133 96 LYS HG3 H 1.67 . . 1134 96 LYS CD C 29.07 . . 1135 96 LYS HD2 H 1.80 . . 1136 96 LYS HD3 H 1.80 . . 1137 96 LYS CE C 42.28 . . 1138 96 LYS HE2 H 2.99 . . 1139 96 LYS HE3 H 2.99 . . 1140 97 ASP H H 8.27 . . 1141 97 ASP N N 121.56 . . 1142 97 ASP CA C 54.23 . . 1143 97 ASP HA H 4.57 . . 1144 97 ASP C C 175.82 . . 1145 97 ASP CB C 41.45 . . 1146 97 ASP HB2 H 2.63 . . 1147 97 ASP HB3 H 2.69 . . 1148 98 ALA H H 8.24 . . 1149 98 ALA N N 124.98 . . 1150 98 ALA CA C 52.84 . . 1151 98 ALA HA H 4.29 . . 1152 98 ALA C C 177.62 . . 1153 98 ALA CB C 19.28 . . 1154 98 ALA HB H 1.40 . . 1155 99 ARG H H 8.25 . . 1158 99 ARG HA H 4.27 . . 1161 99 ARG HB2 H 1.63 . . 1162 99 ARG HB3 H 1.63 . . 1163 99 ARG CG C 27.30 . . 1164 99 ARG HG2 H 1.82 . . 1165 99 ARG HG3 H 1.82 . . 1166 99 ARG CD C 43.41 . . 1167 99 ARG HD2 H 3.19 . . 1168 99 ARG HD3 H 3.19 . . 1169 101 GLN H H 8.28 . . 1170 101 GLN N N 121.14 . . 1171 101 GLN CA C 55.84 . . 1172 101 GLN HA H 4.37 . . 1173 101 GLN C C 174.78 . . 1174 101 GLN CB C 29.54 . . 1175 101 GLN HB2 H 2.73 . . 1176 101 GLN HB3 H 2.81 . . 1177 101 GLN CG C 33.91 . . 1178 101 GLN HG2 H 2.81 . . 1179 102 VAL H H 7.74 . . 1182 102 VAL HA H 4.19 . . 1185 102 VAL HB H 2.11 . . 1186 102 VAL CG1 C 20.98 . . 1187 102 VAL HG1 H 0.94 . . 1188 102 VAL CG2 C 20.98 . . 1189 102 VAL HG2 H 0.94 . . stop_ save_