data_6575 #Corrected using PDB structure: 2CIAA # #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 # 25 D HA 6.18 5.29 # #After reference correction, the following residues still #have a CB chemical shift difference (obs*-pred) greater than 5.0ppm: #NUM AA CS Observed* Predicted # 23 E CB 36.24 29.69 # #After reference correction, the following residues still #have a CO chemical shift difference (obs*-pred) greater than 5.0ppm: #NUM AA CS Observed* Predicted # 63 G C 49.69 173.74 # #After reference correction, the following residues still #have a N chemical shift difference (obs*-pred) greater than 10.0ppm: #NUM AA CS Observed* Predicted # 98 Q N 135.17 123.42 # #The average CS difference between predicted and observed: #HA CA CB CO N HN #0.13 -0.19 -0.13 2.42 0.24 0.11 # #bmr6575.str.corr chemical shifts have been re-referenced with the following #offsets (these values have been added to the original bmr6575.str file): #HA CA CB CO N HN #N/A -0.16 -0.16 +2.42 +0.24 N/A # #The 95% confidence intervals for the above recommended offsets are: # HA CA CB CO N HN #+/-0.03 +/-0.14 +/-0.16 +/-0.23 +/-0.40 +/-0.06 # #The Correlation Coefficients between predicted and observed #chemical shifts are: #HA CA CB CO N HN #0.932 0.970 0.994 0.225 0.815 0.810 # #The RMSD between predicted and observed* (reference #corrected) chemical shifts are: #HA CA CB CO N HN #0.143 0.665 0.728 1.073 1.880 0.300 # ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone and side-chain chemical shift assignments for Human Nck2 SH2 domain ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Ran Xiaoyuan ? . 2 Song Jianxing ? . stop_ _BMRB_accession_number 6575 _BMRB_flat_file_name bmr6575.str _Entry_type new _Submission_date 2005-04-01 _Accession_date 2005-04-01 _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" 425 "13C chemical shifts" 370 "15N chemical shifts" 92 stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_title ; Structural Insight into the Binding Diversity between the Tyr-phosphorylated Human EphrinBs and Nck2 SH2 Domain. ; _Citation_status published _Citation_type journal _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Ran Xiaoyuan ? . 2 Song Jianxing ? . stop_ _Journal_abbreviation "J. Biol. Chem." _Journal_volume 280 _Journal_issue 19 _Page_first 19205 _Page_last 19212 _Year 2005 save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name "Nck2 SH2 domain" _Abbreviation_common ? loop_ _Mol_system_component_name _Mol_label "Nck2 SH2 domain" $Human_Nck2_SH2_domain stop_ _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state "all free" save_ ######################## # Monomeric polymers # ######################## save_Human_Nck2_SH2_domain _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common "Nck2 SH2 domain" _Mol_thiol_state "all free" ############################## # Polymer residue sequence # ############################## _Residue_count 98 _Mol_residue_sequence ; REWYYGNVTRHQAECALNER GVEGDFLIRDSESSPSDFSV SLKASGKNKHFKVQLVDNVY CIGQRRFHTMDELVEHYKKA PIFTSEHGEKLYLVRALQ ; loop_ _Residue_seq_code _Residue_label 1 ARG 2 GLU 3 TRP 4 TYR 5 TYR 6 GLY 7 ASN 8 VAL 9 THR 10 ARG 11 HIS 12 GLN 13 ALA 14 GLU 15 CYS 16 ALA 17 LEU 18 ASN 19 GLU 20 ARG 21 GLY 22 VAL 23 GLU 24 GLY 25 ASP 26 PHE 27 LEU 28 ILE 29 ARG 30 ASP 31 SER 32 GLU 33 SER 34 SER 35 PRO 36 SER 37 ASP 38 PHE 39 SER 40 VAL 41 SER 42 LEU 43 LYS 44 ALA 45 SER 46 GLY 47 LYS 48 ASN 49 LYS 50 HIS 51 PHE 52 LYS 53 VAL 54 GLN 55 LEU 56 VAL 57 ASP 58 ASN 59 VAL 60 TYR 61 CYS 62 ILE 63 GLY 64 GLN 65 ARG 66 ARG 67 PHE 68 HIS 69 THR 70 MET 71 ASP 72 GLU 73 LEU 74 VAL 75 GLU 76 HIS 77 TYR 78 LYS 79 LYS 80 ALA 81 PRO 82 ILE 83 PHE 84 THR 85 SER 86 GLU 87 HIS 88 GLY 89 GLU 90 LYS 91 LEU 92 TYR 93 LEU 94 VAL 95 ARG 96 ALA 97 LEU 98 GLN stop_ _Sequence_homology_query_date 2005-09-22 _Sequence_homology_query_revised_last_date 2005-09-08 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 1Z3K "A Chain A, Structural Insight Into TheBinding Diversity Between The Tyr-Phosphorylated HumanEphrinbs And Nck2 Sh2 Domain" 100.00 98 100 100 3e-52 GenBank AAY24332.1 "unknown [Homo sapiens]" 32.24 304 100 100 3e-52 GenBank AAC80284.1 "Nck-2 [Homo sapiens]" 25.79 380 100 100 3e-52 GenBank AAH00103.1 "NCK adaptor protein 2, isoform A [Homosapiens]" 25.79 380 100 100 3e-52 GenBank AAH07195.1 "NCK adaptor protein 2 [Homo sapiens]" 25.79 380 100 100 3e-52 GenBank AAC04831.1 "SH2/SH3 adaptor protein NCK-beta [Homosapiens]" 25.72 381 99 100 6e-52 REF NP_001004720.1 "NCK adaptor protein 2 isoform A[Homo sapiens]" 25.79 380 100 100 3e-52 REF NP_003572.2 "NCK adaptor protein 2 isoform A [Homosapiens]" 25.79 380 100 100 3e-52 REF XP_538440.2 "PREDICTED: similar to Cytoplasmicprotein NCK2 (NCK adaptor protein 2) (SH2/SH3 adaptorprotein NCK-beta) (Nck-2) [Canis familiaris]" 25.79 380 100 100 3e-52 SWISS-PROT O43639 "NCK2_HUMAN Cytoplasmic protein NCK2 (NCKadaptor protein 2) (SH2/SH3 adaptor protein NCK-beta)(Nck-2)" 25.79 380 100 100 3e-52 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Human_Nck2_SH2_domain Human 9606 Eukaryota Metazoa Homo human 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 $Human_Nck2_SH2_domain "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 $Human_Nck2_SH2_domain ? mM ? stop_ save_ ####################### # Sample conditions # ####################### save_conditions_1 _Saveframe_category sample_conditions loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.8 0.2 pH temperature 293 0.5 K pressure 1 0.1 atm stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_referencing _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 C 13 "methyl protons" ppm 0.0 . indirect ? ? ? 0.251449530 DSS N 15 "methyl protons" ppm 0.0 . indirect ? ? ? 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # Index Value Definition # # # # 1 Unique (geminal atoms and geminal methyl # # groups with identical chemical shifts # # are assumed to be assigned to # # stereospecific atoms) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. Tyr HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. Lys HG and # # HD protons or Trp HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (Lys 12 vs. Lys 27) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_chem_shift_list_1_1 _Saveframe_category assigned_chemical_shifts loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $conditions_1 _Chem_shift_reference_set_label $chemical_shift_referencing _Mol_system_component_name "Nck2 SH2 domain" 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 1 ARG CA C 54.09 . 1 2 1 ARG CB C 30.48 . 1 3 2 GLU H H 8.86 . 1 4 2 GLU C C 175.37 . 1 5 2 GLU CA C 58.63 . 1 6 2 GLU CB C 28.91 . 1 7 2 GLU CG C 35.87 . 1 8 2 GLU N N 122.16 . 1 9 3 TRP H H 6.13 . 1 10 3 TRP HA H 4.48 . 1 11 3 TRP HB2 H 2.71 . 2 12 3 TRP HB3 H 3.46 . 2 13 3 TRP C C 176.28 . 1 14 3 TRP CA C 53.69 . 1 15 3 TRP CB C 31.12 . 1 16 3 TRP N N 109.71 . 1 17 4 TYR H H 7.51 . 1 18 4 TYR HA H 5.27 . 1 19 4 TYR HB2 H 2.51 . 2 20 4 TYR HB3 H 2.77 . 2 21 4 TYR C C 174.45 . 1 22 4 TYR CA C 57.08 . 1 23 4 TYR CB C 37.14 . 1 24 4 TYR N N 121.86 . 1 25 5 TYR H H 9.23 . 1 26 5 TYR HA H 4.16 . 1 27 5 TYR HB2 H 2.64 . 2 28 5 TYR HB3 H 2.91 . 2 29 5 TYR CA C 57.84 . 1 30 5 TYR CB C 39.84 . 1 31 5 TYR N N 130.30 . 1 32 6 GLY HA2 H 3.52 . 2 33 6 GLY HA3 H 3.32 . 2 34 6 GLY C C 174.07 . 1 35 6 GLY CA C 46.62 . 1 36 7 ASN H H 8.51 . 1 37 7 ASN HA H 4.71 . 1 38 7 ASN HB2 H 2.74 . 2 39 7 ASN C C 175.27 . 1 40 7 ASN CA C 53.34 . 1 41 7 ASN CB C 36.89 . 1 42 7 ASN N N 123.71 . 1 43 8 VAL H H 7.30 . 1 44 8 VAL HA H 4.46 . 1 45 8 VAL HB H 1.95 . 1 46 8 VAL HG1 H 0.89 . 2 47 8 VAL HG2 H 0.69 . 2 48 8 VAL C C 175.98 . 1 49 8 VAL CA C 60.08 . 1 50 8 VAL CB C 33.67 . 1 51 8 VAL CG1 C 21.80 . 1 52 8 VAL CG2 C 20.21 . 1 53 8 VAL N N 117.56 . 1 54 9 THR H H 8.51 . 1 55 9 THR HA H 4.14 . 1 56 9 THR HB H 4.67 . 1 57 9 THR HG2 H 1.20 . 1 58 9 THR C C 174.94 . 1 59 9 THR CA C 60.69 . 1 60 9 THR CB C 71.13 . 1 61 9 THR CG2 C 21.79 . 1 62 9 THR N N 114.77 . 1 63 10 ARG H H 8.97 . 1 64 10 ARG HA H 3.40 . 1 65 10 ARG HB2 H 1.73 . 2 66 10 ARG HB3 H 1.54 . 2 67 10 ARG HG2 H 0.37 . 2 68 10 ARG HG3 H 1.10 . 2 69 10 ARG HD2 H 2.76 . 2 70 10 ARG C C 178.05 . 1 71 10 ARG CA C 60.77 . 1 72 10 ARG CB C 30.08 . 1 73 10 ARG CG C 27.15 . 1 74 10 ARG CD C 43.09 . 1 75 10 ARG N N 122.42 . 1 76 11 HIS H H 8.62 . 1 77 11 HIS HA H 4.17 . 1 78 11 HIS HB2 H 2.84 . 2 79 11 HIS HB3 H 3.00 . 2 80 11 HIS C C 178.21 . 1 81 11 HIS CA C 59.65 . 1 82 11 HIS CB C 30.23 . 1 83 11 HIS N N 116.89 . 1 84 12 GLN H H 7.94 . 1 85 12 GLN HA H 3.68 . 1 86 12 GLN HB2 H 2.18 . 2 87 12 GLN HG2 H 2.24 . 2 88 12 GLN C C 179.56 . 1 89 12 GLN CA C 59.04 . 1 90 12 GLN CB C 28.79 . 1 91 12 GLN CG C 34.75 . 1 92 12 GLN N N 119.01 . 1 93 13 ALA H H 8.56 . 1 94 13 ALA HA H 3.63 . 1 95 13 ALA HB H 1.28 . 1 96 13 ALA C C 178.46 . 1 97 13 ALA CA C 54.80 . 1 98 13 ALA CB C 18.45 . 1 99 13 ALA N N 122.74 . 1 100 14 GLU H H 8.23 . 1 101 14 GLU HA H 3.57 . 1 102 14 GLU HB2 H 1.99 . 2 103 14 GLU HG2 H 2.66 . 2 104 14 GLU C C 178.07 . 1 105 14 GLU CA C 60.36 . 1 106 14 GLU CB C 28.56 . 1 107 14 GLU CG C 37.16 . 1 108 14 GLU N N 116.28 . 1 109 15 CYS H H 7.81 . 1 110 15 CYS HA H 3.88 . 1 111 15 CYS HB2 H 2.69 . 2 112 15 CYS C C 176.64 . 1 113 15 CYS CA C 63.41 . 1 114 15 CYS CB C 26.29 . 1 115 15 CYS N N 115.36 . 1 116 16 ALA H H 7.70 . 1 117 16 ALA HA H 3.89 . 1 118 16 ALA HB H 1.13 . 1 119 16 ALA C C 179.50 . 1 120 16 ALA CA C 55.24 . 1 121 16 ALA CB C 17.46 . 1 122 16 ALA N N 122.13 . 1 123 17 LEU H H 8.06 . 1 124 17 LEU HA H 3.55 . 1 125 17 LEU HB2 H 1.04 . 2 126 17 LEU HB3 H 1.69 . 2 127 17 LEU HG H 1.48 . 1 128 17 LEU HD1 H 0.30 . 2 129 17 LEU HD2 H 0.56 . 2 130 17 LEU C C 179.75 . 1 131 17 LEU CA C 57.78 . 1 132 17 LEU CB C 41.17 . 1 133 17 LEU CG C 26.38 . 1 134 17 LEU CD1 C 24.81 . 1 135 17 LEU CD2 C 22.96 . 1 136 17 LEU N N 117.17 . 1 137 18 ASN H H 8.39 . 1 138 18 ASN HA H 4.19 . 1 139 18 ASN HB2 H 2.84 . 2 140 18 ASN C C 177.84 . 1 141 18 ASN CA C 55.12 . 1 142 18 ASN CB C 37.25 . 1 143 18 ASN N N 117.17 . 1 144 19 GLU H H 8.24 . 1 145 19 GLU HA H 4.02 . 1 146 19 GLU HB2 H 1.98 . 2 147 19 GLU HG2 H 2.13 . 2 148 19 GLU HG3 H 2.33 . 2 149 19 GLU C C 178.47 . 1 150 19 GLU CA C 58.76 . 1 151 19 GLU CB C 30.48 . 1 152 19 GLU CG C 36.47 . 1 153 19 GLU N N 119.24 . 1 154 20 ARG H H 7.88 . 1 155 20 ARG HA H 4.58 . 1 156 20 ARG HB2 H 1.44 . 2 157 20 ARG HB3 H 1.71 . 2 158 20 ARG C C 176.54 . 1 159 20 ARG CA C 55.72 . 1 160 20 ARG CB C 32.48 . 1 161 20 ARG CG C 26.92 . 1 162 20 ARG CD C 43.41 . 1 163 20 ARG N N 112.72 . 1 164 21 GLY H H 7.79 . 1 165 21 GLY HA2 H 3.45 . 2 166 21 GLY HA3 H 4.68 . 2 167 21 GLY C C 173.71 . 1 168 21 GLY CA C 45.31 . 1 169 21 GLY N N 109.47 . 1 170 22 VAL H H 8.93 . 1 171 22 VAL HA H 4.30 . 1 172 22 VAL HB H 2.04 . 1 173 22 VAL HG1 H 0.82 . 2 174 22 VAL HG2 H 0.76 . 2 175 22 VAL C C 174.96 . 1 176 22 VAL CA C 59.49 . 1 177 22 VAL CB C 34.32 . 1 178 22 VAL CG1 C 21.19 . 1 179 22 VAL CG2 C 19.34 . 1 180 22 VAL N N 119.61 . 1 181 23 GLU H H 8.41 . 1 182 23 GLU HA H 4.08 . 1 183 23 GLU HB2 H 1.58 . 2 184 23 GLU C C 177.87 . 1 185 23 GLU CA C 59.35 . 1 186 23 GLU CB C 36.21 . 1 187 23 GLU CG C 36.21 . 1 188 23 GLU N N 121.29 . 1 189 24 GLY H H 8.58 . 1 190 24 GLY HA2 H 4.46 . 2 191 24 GLY HA3 H 3.80 . 2 192 24 GLY C C 174.13 . 1 193 24 GLY CA C 45.32 . 1 194 24 GLY N N 115.31 . 1 195 25 ASP H H 8.60 . 1 196 25 ASP HA H 6.05 . 1 197 25 ASP HB2 H 2.16 . 2 198 25 ASP HB3 H 2.74 . 2 199 25 ASP C C 176.51 . 1 200 25 ASP CA C 53.78 . 1 201 25 ASP CB C 41.33 . 1 202 25 ASP N N 124.91 . 1 203 26 PHE H H 8.40 . 1 204 26 PHE HA H 5.92 . 1 205 26 PHE HB2 H 2.82 . 2 206 26 PHE HB3 H 2.75 . 2 207 26 PHE C C 172.17 . 1 208 26 PHE CA C 54.88 . 1 209 26 PHE CB C 45.05 . 1 210 26 PHE N N 115.12 . 1 211 27 LEU H H 9.01 . 1 212 27 LEU HA H 4.79 . 1 213 27 LEU HB2 H 1.17 . 2 214 27 LEU HB3 H 1.31 . 2 215 27 LEU HG H 1.48 . 1 216 27 LEU HD1 H 0.45 . 2 217 27 LEU HD2 H 0.15 . 2 218 27 LEU C C 174.45 . 1 219 27 LEU CA C 53.88 . 1 220 27 LEU CB C 45.74 . 1 221 27 LEU CG C 25.09 . 1 222 27 LEU CD1 C 25.29 . 1 223 27 LEU CD2 C 26.65 . 1 224 27 LEU N N 115.35 . 1 225 28 ILE H H 9.36 . 1 226 28 ILE HA H 5.33 . 1 227 28 ILE HB H 2.27 . 1 228 28 ILE HG12 H 1.19 . 1 229 28 ILE HG13 H 1.60 . 1 230 28 ILE HG2 H 0.96 . 1 231 28 ILE HD1 H 0.40 . 1 232 28 ILE C C 173.77 . 1 233 28 ILE CA C 60.44 . 1 234 28 ILE CB C 38.49 . 1 235 28 ILE CG1 C 29.46 . 2 236 28 ILE CG2 C 17.94 . 1 237 28 ILE CD1 C 12.71 . 1 238 28 ILE N N 121.33 . 1 239 29 ARG H H 9.26 . 1 240 29 ARG HA H 5.45 . 1 241 29 ARG HB2 H 2.24 . 2 242 29 ARG HB3 H 1.22 . 2 243 29 ARG HG2 H 1.63 . 2 244 29 ARG HG3 H 1.41 . 2 245 29 ARG HD2 H 3.17 . 2 246 29 ARG HD3 H 2.30 . 2 247 29 ARG C C 174.27 . 1 248 29 ARG CA C 52.34 . 1 249 29 ARG CB C 34.56 . 1 250 29 ARG CG C 26.42 . 1 251 29 ARG CD C 43.73 . 1 252 29 ARG N N 124.16 . 1 253 30 ASP H H 8.48 . 1 254 30 ASP HA H 4.61 . 1 255 30 ASP HB2 H 2.32 . 2 256 30 ASP HB3 H 2.68 . 2 257 30 ASP C C 176.15 . 1 258 30 ASP CA C 54.55 . 1 259 30 ASP CB C 40.26 . 1 260 30 ASP N N 123.35 . 1 261 31 SER H H 7.86 . 1 262 31 SER HA H 4.34 . 1 263 31 SER HB2 H 3.73 . 2 264 31 SER HB3 H 3.46 . 2 265 31 SER C C 175.89 . 1 266 31 SER CA C 57.38 . 1 267 31 SER CB C 63.63 . 1 268 31 SER N N 116.33 . 1 269 32 GLU H H 9.54 . 1 270 32 GLU HA H 4.04 . 1 271 32 GLU HB2 H 2.01 . 2 272 32 GLU C C 177.78 . 1 273 32 GLU CA C 58.02 . 1 274 32 GLU CB C 30.34 . 1 275 32 GLU CG C 36.90 . 1 276 32 GLU N N 128.08 . 1 277 33 SER H H 8.27 . 1 278 33 SER HA H 4.21 . 1 279 33 SER HB2 H 3.71 . 2 280 33 SER C C 175.00 . 1 281 33 SER CA C 59.33 . 1 282 33 SER CB C 63.68 . 1 283 33 SER N N 113.13 . 1 284 34 SER H H 7.36 . 1 285 34 SER HA H 4.80 . 1 286 34 SER HB2 H 3.73 . 2 287 34 SER HB3 H 3.64 . 2 288 34 SER CA C 54.52 . 1 289 34 SER CB C 63.85 . 1 290 34 SER N N 116.92 . 1 291 35 PRO HA H 4.06 . 1 292 35 PRO HB2 H 1.93 . 2 293 35 PRO HB3 H 1.63 . 2 294 35 PRO HG2 H 1.46 . 2 295 35 PRO HD2 H 3.62 . 2 296 35 PRO HD3 H 3.42 . 2 297 35 PRO C C 176.78 . 1 298 35 PRO CA C 62.42 . 1 299 35 PRO CB C 31.95 . 1 300 35 PRO CG C 26.82 . 1 301 35 PRO CD C 50.61 . 1 302 36 SER H H 8.00 . 1 303 36 SER HA H 4.26 . 1 304 36 SER HB2 H 3.82 . 2 305 36 SER HB3 H 3.99 . 2 306 36 SER C C 172.62 . 1 307 36 SER CA C 59.72 . 1 308 36 SER CB C 63.55 . 1 309 36 SER N N 112.66 . 1 310 37 ASP H H 7.38 . 1 311 37 ASP HA H 5.17 . 1 312 37 ASP HB2 H 2.57 . 2 313 37 ASP HB3 H 2.90 . 2 314 37 ASP C C 175.20 . 1 315 37 ASP CA C 53.48 . 1 316 37 ASP CB C 42.98 . 1 317 37 ASP N N 119.80 . 1 318 38 PHE H H 8.91 . 1 319 38 PHE HA H 5.29 . 1 320 38 PHE HB2 H 2.50 . 2 321 38 PHE HB3 H 3.17 . 2 322 38 PHE C C 175.12 . 1 323 38 PHE CA C 56.57 . 1 324 38 PHE CB C 43.94 . 1 325 38 PHE N N 116.94 . 1 326 39 SER H H 9.44 . 1 327 39 SER HA H 5.52 . 1 328 39 SER HB2 H 3.35 . 2 329 39 SER HB3 H 3.54 . 2 330 39 SER C C 173.40 . 1 331 39 SER CA C 57.70 . 1 332 39 SER CB C 65.93 . 1 333 39 SER N N 115.86 . 1 334 40 VAL H H 9.30 . 1 335 40 VAL HA H 4.68 . 1 336 40 VAL HB H 2.05 . 1 337 40 VAL HG1 H 0.65 . 2 338 40 VAL C C 175.90 . 1 339 40 VAL CA C 60.83 . 1 340 40 VAL CB C 33.24 . 1 341 40 VAL CG1 C 21.23 . 1 342 40 VAL CG2 C 19.77 . 1 343 40 VAL N N 125.22 . 1 344 41 SER H H 9.34 . 1 345 41 SER HA H 5.20 . 1 346 41 SER HB2 H 3.34 . 2 347 41 SER C C 171.33 . 1 348 41 SER CA C 58.42 . 1 349 41 SER CB C 65.19 . 1 350 41 SER N N 124.69 . 1 351 42 LEU H H 8.94 . 1 352 42 LEU HA H 4.96 . 1 353 42 LEU HB2 H 0.97 . 2 354 42 LEU HB3 H 1.60 . 2 355 42 LEU HG H 0.61 . 1 356 42 LEU HD1 H 0.74 . 2 357 42 LEU C C 174.45 . 1 358 42 LEU CA C 52.98 . 1 359 42 LEU CB C 48.65 . 1 360 42 LEU CG C 27.32 . 1 361 42 LEU CD1 C 24.07 . 1 362 42 LEU N N 126.93 . 1 363 43 LYS H H 8.83 . 1 364 43 LYS HA H 4.66 . 1 365 43 LYS HB2 H 2.12 . 2 366 43 LYS C C 174.96 . 1 367 43 LYS CA C 55.66 . 1 368 43 LYS CB C 32.51 . 1 369 43 LYS CG C 25.15 . 1 370 43 LYS CD C 28.93 . 1 371 43 LYS CE C 42.60 . 1 372 43 LYS N N 121.75 . 1 373 44 ALA H H 8.41 . 1 374 44 ALA HA H 4.71 . 1 375 44 ALA HB H 1.23 . 1 376 44 ALA C C 175.72 . 1 377 44 ALA CA C 50.81 . 1 378 44 ALA CB C 21.85 . 1 379 44 ALA N N 133.30 . 1 380 45 SER H H 9.14 . 1 381 45 SER HA H 4.02 . 1 382 45 SER HB2 H 3.74 . 2 383 45 SER HB3 H 3.84 . 2 384 45 SER C C 175.96 . 1 385 45 SER CA C 58.92 . 1 386 45 SER CB C 62.23 . 1 387 45 SER N N 117.77 . 1 388 46 GLY H H 8.84 . 1 389 46 GLY HA2 H 4.05 . 2 390 46 GLY HA3 H 3.47 . 2 391 46 GLY C C 173.49 . 1 392 46 GLY CA C 45.93 . 1 393 46 GLY N N 113.09 . 1 394 47 LYS H H 7.46 . 1 395 47 LYS HA H 4.32 . 1 396 47 LYS HB2 H 1.56 . 2 397 47 LYS HB3 H 1.75 . 2 398 47 LYS HG2 H 1.20 . 2 399 47 LYS HD2 H 1.54 . 2 400 47 LYS HE2 H 2.84 . 2 401 47 LYS C C 174.12 . 1 402 47 LYS CA C 54.98 . 1 403 47 LYS CB C 34.47 . 1 404 47 LYS CG C 23.82 . 1 405 47 LYS CD C 29.00 . 1 406 47 LYS CE C 41.90 . 1 407 47 LYS N N 119.94 . 1 408 48 ASN H H 8.51 . 1 409 48 ASN HA H 5.01 . 1 410 48 ASN HB2 H 1.88 . 2 411 48 ASN HB3 H 2.46 . 2 412 48 ASN C C 174.53 . 1 413 48 ASN CA C 52.93 . 1 414 48 ASN CB C 39.03 . 1 415 48 ASN N N 118.40 . 1 416 49 LYS H H 8.54 . 1 417 49 LYS HA H 4.12 . 1 418 49 LYS HB2 H 1.02 . 2 419 49 LYS HG2 H 0.86 . 2 420 49 LYS HD2 H 0.96 . 2 421 49 LYS HE2 H 1.81 . 2 422 49 LYS C C 173.34 . 1 423 49 LYS CA C 53.70 . 1 424 49 LYS CB C 35.89 . 1 425 49 LYS CG C 24.16 . 1 426 49 LYS CD C 27.96 . 1 427 49 LYS CE C 40.72 . 1 428 49 LYS N N 120.67 . 1 429 49 LYS NZ N 1.95 . 1 430 50 HIS H H 7.75 . 1 431 50 HIS HA H 5.38 . 1 432 50 HIS HB2 H 2.49 . 2 433 50 HIS HB3 H 2.57 . 2 434 50 HIS C C 175.27 . 1 435 50 HIS CA C 53.89 . 1 436 50 HIS CB C 33.50 . 1 437 50 HIS N N 118.17 . 1 438 51 PHE H H 9.38 . 1 439 51 PHE HA H 4.71 . 1 440 51 PHE HB2 H 2.49 . 2 441 51 PHE C C 174.80 . 1 442 51 PHE CA C 56.10 . 1 443 51 PHE CB C 41.41 . 1 444 51 PHE N N 121.88 . 1 445 52 LYS H H 8.66 . 1 446 52 LYS HA H 4.62 . 1 447 52 LYS HB2 H 1.76 . 2 448 52 LYS HG2 H 1.44 . 2 449 52 LYS HG3 H 1.34 . 2 450 52 LYS HD2 H 1.69 . 2 451 52 LYS HD3 H 1.60 . 2 452 52 LYS HE2 H 2.86 . 2 453 52 LYS C C 175.70 . 1 454 52 LYS CA C 57.03 . 1 455 52 LYS CB C 32.80 . 1 456 52 LYS CG C 24.38 . 1 457 52 LYS CD C 28.37 . 1 458 52 LYS CE C 41.32 . 1 459 52 LYS N N 125.24 . 1 460 53 VAL H H 8.90 . 1 461 53 VAL HA H 4.55 . 1 462 53 VAL HB H 1.90 . 1 463 53 VAL HG1 H 0.86 . 2 464 53 VAL HG2 H 0.76 . 2 465 53 VAL C C 175.17 . 1 466 53 VAL CA C 60.78 . 1 467 53 VAL CB C 34.34 . 1 468 53 VAL CG1 C 22.24 . 1 469 53 VAL CG2 C 21.32 . 1 470 53 VAL N N 126.02 . 1 471 54 GLN H H 8.71 . 1 472 54 GLN HA H 4.86 . 1 473 54 GLN HB2 H 1.78 . 2 474 54 GLN HG2 H 2.23 . 2 475 54 GLN C C 175.01 . 1 476 54 GLN CA C 54.45 . 1 477 54 GLN CB C 32.66 . 1 478 54 GLN CG C 34.66 . 1 479 54 GLN N N 124.91 . 1 480 55 LEU H H 8.73 . 1 481 55 LEU HA H 4.74 . 1 482 55 LEU HB2 H 1.87 . 2 483 55 LEU HG H 1.07 . 1 484 55 LEU HD1 H 0.70 . 2 485 55 LEU HD2 H -0.07 . 2 486 55 LEU C C 176.07 . 1 487 55 LEU CA C 54.31 . 1 488 55 LEU CB C 42.10 . 1 489 55 LEU CG C 27.20 . 1 490 55 LEU CD1 C 25.78 . 1 491 55 LEU CD2 C 21.46 . 1 492 55 LEU N N 127.86 . 1 493 56 VAL H H 8.84 . 1 494 56 VAL HA H 4.04 . 1 495 56 VAL HB H 1.82 . 1 496 56 VAL HG1 H 0.70 . 2 497 56 VAL C C 175.39 . 1 498 56 VAL CA C 61.13 . 1 499 56 VAL CB C 34.19 . 1 500 56 VAL CG1 C 20.61 . 1 501 56 VAL CG2 C 20.61 . 1 502 56 VAL N N 129.51 . 1 503 57 ASP H H 9.08 . 1 504 57 ASP HA H 3.99 . 1 505 57 ASP HB2 H 2.45 . 2 506 57 ASP HB3 H 2.72 . 2 507 57 ASP C C 171.61 . 1 508 57 ASP CA C 55.62 . 1 509 57 ASP CB C 39.21 . 1 510 57 ASP N N 127.07 . 1 511 58 ASN H H 8.40 . 1 512 58 ASN HA H 3.94 . 1 513 58 ASN HB2 H 2.89 . 2 514 58 ASN C C 173.68 . 1 515 58 ASN CA C 54.73 . 1 516 58 ASN CB C 38.18 . 1 517 58 ASN N N 108.30 . 1 518 59 VAL H H 7.71 . 1 519 59 VAL HA H 4.31 . 1 520 59 VAL HB H 1.80 . 1 521 59 VAL HG1 H 0.58 . 2 522 59 VAL HG2 H 0.67 . 2 523 59 VAL C C 173.45 . 1 524 59 VAL CA C 60.30 . 1 525 59 VAL CB C 34.60 . 1 526 59 VAL CG1 C 22.19 . 1 527 59 VAL CG2 C 19.86 . 1 528 59 VAL N N 116.85 . 1 529 60 TYR H H 8.86 . 1 530 60 TYR HA H 4.61 . 1 531 60 TYR HB2 H 2.45 . 2 532 60 TYR HB3 H 2.68 . 2 533 60 TYR C C 176.20 . 1 534 60 TYR CA C 58.34 . 1 535 60 TYR CB C 38.77 . 1 536 60 TYR N N 122.07 . 1 537 61 CYS H H 9.44 . 1 538 61 CYS HA H 5.28 . 1 539 61 CYS HB2 H 2.79 . 2 540 61 CYS C C 174.34 . 1 541 61 CYS CA C 58.21 . 1 542 61 CYS CB C 30.14 . 1 543 61 CYS N N 122.04 . 1 544 62 ILE H H 8.23 . 1 545 62 ILE HA H 4.62 . 1 546 62 ILE HB H 1.96 . 1 547 62 ILE HG12 H 0.99 . 1 548 62 ILE HG13 H 1.16 . 1 549 62 ILE HG2 H 1.66 . 1 550 62 ILE HD1 H 0.49 . 1 551 62 ILE C C 175.01 . 1 552 62 ILE CA C 59.79 . 1 553 62 ILE CB C 39.60 . 1 554 62 ILE CG1 C 27.88 . 2 555 62 ILE CG2 C 15.93 . 1 556 62 ILE CD1 C 13.48 . 1 557 62 ILE N N 123.44 . 1 558 63 GLY H H 9.01 . 1 559 63 GLY HA2 H 3.85 . 2 560 63 GLY HA3 H 3.73 . 2 561 63 GLY C C 49.69 . 1 562 63 GLY CA C 47.11 . 1 563 63 GLY N N 117.44 . 1 564 66 ARG H H 7.66 . 1 565 66 ARG HA H 4.88 . 1 566 66 ARG HB2 H 1.28 . 2 567 66 ARG HG2 H 1.28 . 2 568 66 ARG HG3 H 1.38 . 2 569 66 ARG HD2 H 2.93 . 2 570 66 ARG C C 175.29 . 1 571 66 ARG CA C 54.53 . 1 572 66 ARG CB C 33.15 . 1 573 66 ARG CG C 27.16 . 1 574 66 ARG CD C 43.60 . 1 575 66 ARG N N 120.86 . 1 576 67 PHE H H 9.21 . 1 577 67 PHE HA H 4.68 . 1 578 67 PHE HB2 H 2.56 . 2 579 67 PHE HB3 H 3.24 . 2 580 67 PHE C C 175.53 . 1 581 67 PHE CA C 56.71 . 1 582 67 PHE CB C 43.26 . 1 583 67 PHE N N 119.97 . 1 584 68 HIS H H 9.57 . 1 585 68 HIS HA H 4.55 . 1 586 68 HIS HB2 H 3.37 . 2 587 68 HIS C C 175.27 . 1 588 68 HIS CA C 59.22 . 1 589 68 HIS CB C 29.89 . 1 590 68 HIS N N 120.43 . 1 591 69 THR H H 7.30 . 1 592 69 THR HA H 4.69 . 1 593 69 THR HB H 4.77 . 1 594 69 THR HG2 H 1.22 . 1 595 69 THR C C 174.15 . 1 596 69 THR CA C 58.80 . 1 597 69 THR CB C 73.42 . 1 598 69 THR CG2 C 29.44 . 1 599 69 THR N N 103.24 . 1 600 70 MET H H 8.60 . 1 601 70 MET HA H 3.64 . 1 602 70 MET HB2 H 1.57 . 2 603 70 MET HB3 H 1.48 . 2 604 70 MET HG2 H 2.28 . 2 605 70 MET C C 177.65 . 1 606 70 MET CA C 55.92 . 1 607 70 MET CB C 32.58 . 1 608 70 MET CG C 30.91 . 1 609 70 MET N N 120.62 . 1 610 71 ASP H H 7.93 . 1 611 71 ASP HA H 4.12 . 1 612 71 ASP HB2 H 2.50 . 2 613 71 ASP HB3 H 2.61 . 2 614 71 ASP C C 178.20 . 1 615 71 ASP CA C 57.13 . 1 616 71 ASP CB C 40.50 . 1 617 71 ASP N N 116.74 . 1 618 72 GLU H H 7.69 . 1 619 72 GLU HA H 3.76 . 1 620 72 GLU HB2 H 2.17 . 2 621 72 GLU HG2 H 2.28 . 2 622 72 GLU HG3 H 2.35 . 2 623 72 GLU C C 178.22 . 1 624 72 GLU CA C 58.80 . 1 625 72 GLU CB C 30.73 . 1 626 72 GLU CG C 37.10 . 1 627 72 GLU N N 118.69 . 1 628 73 LEU H H 6.58 . 1 629 73 LEU HA H 1.88 . 1 630 73 LEU HB2 H 0.76 . 2 631 73 LEU HB3 H 1.48 . 2 632 73 LEU HG H 0.68 . 1 633 73 LEU HD1 H 0.29 . 2 634 73 LEU HD2 H 1.06 . 2 635 73 LEU C C 177.19 . 1 636 73 LEU CA C 58.76 . 1 637 73 LEU CB C 41.71 . 1 638 73 LEU CG C 29.19 . 1 639 73 LEU CD1 C 22.84 . 1 640 73 LEU CD2 C 27.27 . 1 641 73 LEU N N 123.24 . 1 642 74 VAL H H 7.60 . 1 643 74 VAL HA H 2.69 . 1 644 74 VAL HB H 1.50 . 1 645 74 VAL HG1 H 0.30 . 2 646 74 VAL HG2 H -0.30 . 2 647 74 VAL C C 177.02 . 1 648 74 VAL CA C 66.26 . 1 649 74 VAL CB C 31.23 . 1 650 74 VAL CG1 C 21.34 . 1 651 74 VAL CG2 C 22.24 . 1 652 74 VAL N N 118.67 . 1 653 75 GLU H H 7.54 . 1 654 75 GLU HA H 3.67 . 1 655 75 GLU HB2 H 1.84 . 2 656 75 GLU C C 179.84 . 1 657 75 GLU CA C 58.55 . 1 658 75 GLU CB C 29.12 . 1 659 75 GLU CG C 35.89 . 1 660 75 GLU N N 114.90 . 1 661 76 HIS H H 7.82 . 1 662 76 HIS HA H 3.93 . 1 663 76 HIS HB2 H 2.86 . 2 664 76 HIS HB3 H 2.65 . 2 665 76 HIS C C 178.36 . 1 666 76 HIS CA C 60.09 . 1 667 76 HIS CB C 30.56 . 1 668 76 HIS N N 118.74 . 1 669 77 TYR H H 7.27 . 1 670 77 TYR HA H 5.28 . 1 671 77 TYR HB2 H 2.12 . 2 672 77 TYR HB3 H 3.19 . 2 673 77 TYR C C 174.87 . 1 674 77 TYR CA C 60.03 . 1 675 77 TYR CB C 36.91 . 1 676 77 TYR N N 114.90 . 1 677 78 LYS H H 7.06 . 1 678 78 LYS HA H 4.85 . 1 679 78 LYS HB2 H 1.75 . 2 680 78 LYS HG2 H 1.18 . 2 681 78 LYS HG3 H 1.56 . 2 682 78 LYS HD2 H 1.53 . 2 683 78 LYS HE2 H 2.73 . 2 684 78 LYS HE3 H 2.59 . 2 685 78 LYS C C 178.94 . 1 686 78 LYS CA C 57.43 . 1 687 78 LYS CB C 33.81 . 1 688 78 LYS CG C 24.91 . 1 689 78 LYS CD C 30.02 . 1 690 78 LYS CE C 42.00 . 1 691 78 LYS N N 116.58 . 1 692 79 LYS H H 7.00 . 1 693 79 LYS HA H 4.18 . 1 694 79 LYS HB2 H 1.50 . 2 695 79 LYS HB3 H 1.63 . 2 696 79 LYS HG2 H 1.23 . 2 697 79 LYS HD2 H 1.50 . 2 698 79 LYS HE2 H 2.82 . 2 699 79 LYS C C 174.64 . 1 700 79 LYS CA C 55.75 . 1 701 79 LYS CB C 34.37 . 1 702 79 LYS CG C 24.63 . 1 703 79 LYS CD C 28.72 . 1 704 79 LYS CE C 41.95 . 1 705 79 LYS N N 115.64 . 1 706 80 ALA H H 8.02 . 1 707 80 ALA HA H 4.71 . 1 708 80 ALA HB H 0.72 . 1 709 80 ALA CA C 48.61 . 1 710 80 ALA CB C 19.11 . 1 711 80 ALA N N 126.78 . 1 712 81 PRO HA H 3.56 . 1 713 81 PRO HB2 H 1.41 . 2 714 81 PRO HB3 H 1.06 . 2 715 81 PRO HG2 H 1.78 . 2 716 81 PRO HD2 H 3.50 . 2 717 81 PRO C C 178.33 . 1 718 81 PRO CA C 62.44 . 1 719 81 PRO CB C 31.33 . 1 720 81 PRO CG C 27.40 . 1 721 81 PRO CD C 49.15 . 1 722 82 ILE H H 8.32 . 1 723 82 ILE HA H 3.80 . 1 724 82 ILE HB H 0.83 . 1 725 82 ILE HG12 H -0.38 . 1 726 82 ILE HG13 H -0.23 . 1 727 82 ILE HG2 H -0.01 . 1 728 82 ILE HD1 H -0.46 . 1 729 82 ILE C C 173.10 . 1 730 82 ILE CA C 60.84 . 1 731 82 ILE CB C 39.60 . 1 732 82 ILE CG1 C 28.40 . 2 733 82 ILE CG2 C 13.65 . 1 734 82 ILE CD1 C 13.65 . 1 735 82 ILE N N 123.98 . 1 736 83 PHE H H 7.06 . 1 737 83 PHE HA H 4.39 . 1 738 83 PHE HB2 H 2.28 . 2 739 83 PHE HB3 H 3.09 . 2 740 83 PHE C C 172.60 . 1 741 83 PHE CA C 57.59 . 1 742 83 PHE CB C 43.44 . 1 743 83 PHE N N 120.49 . 1 744 84 THR H H 7.25 . 1 745 84 THR HA H 4.79 . 1 746 84 THR HB H 3.49 . 1 747 84 THR HG2 H 0.85 . 1 748 84 THR C C 173.26 . 1 749 84 THR CA C 60.47 . 1 750 84 THR CB C 70.30 . 1 751 84 THR CG2 C 20.33 . 1 752 84 THR N N 122.41 . 1 753 85 SER H H 8.86 . 1 754 85 SER HA H 4.25 . 1 755 85 SER HB2 H 4.00 . 2 756 85 SER HB3 H 4.41 . 2 757 85 SER CA C 56.70 . 1 758 85 SER CB C 65.79 . 1 759 85 SER N N 121.46 . 1 760 87 HIS H H 8.33 . 1 761 87 HIS HA H 4.22 . 1 762 87 HIS HB2 H 1.91 . 2 763 87 HIS HB3 H 1.24 . 2 764 87 HIS C C 175.43 . 1 765 87 HIS CA C 55.04 . 1 766 87 HIS CB C 30.53 . 1 767 87 HIS N N 120.37 . 1 768 88 GLY H H 7.78 . 1 769 88 GLY HA2 H 4.05 . 2 770 88 GLY HA3 H 3.35 . 2 771 88 GLY C C 174.28 . 1 772 88 GLY CA C 45.25 . 1 773 88 GLY N N 108.15 . 1 774 89 GLU H H 7.73 . 1 775 89 GLU HA H 4.42 . 1 776 89 GLU HB2 H 1.84 . 2 777 89 GLU HG2 H 1.95 . 2 778 89 GLU HG3 H 2.07 . 2 779 89 GLU C C 175.80 . 1 780 89 GLU CA C 56.54 . 1 781 89 GLU CB C 29.71 . 1 782 89 GLU CG C 36.18 . 1 783 89 GLU N N 120.46 . 1 784 90 LYS H H 8.54 . 1 785 90 LYS HA H 4.55 . 1 786 90 LYS HB2 H 1.15 . 2 787 90 LYS HB3 H 1.65 . 2 788 90 LYS HG2 H 1.36 . 2 789 90 LYS HG3 H 1.25 . 2 790 90 LYS HD2 H 1.54 . 2 791 90 LYS HE2 H 2.90 . 2 792 90 LYS C C 174.74 . 1 793 90 LYS CA C 56.15 . 1 794 90 LYS CB C 34.70 . 1 795 90 LYS CG C 25.35 . 1 796 90 LYS CD C 29.69 . 1 797 90 LYS CE C 41.94 . 1 798 90 LYS N N 126.01 . 1 799 91 LEU H H 8.45 . 1 800 91 LEU HA H 4.64 . 1 801 91 LEU HB2 H 1.37 . 2 802 91 LEU HB3 H 1.54 . 2 803 91 LEU HG H 1.64 . 1 804 91 LEU HD1 H 0.77 . 2 805 91 LEU HD2 H 0.84 . 2 806 91 LEU C C 174.63 . 1 807 91 LEU CA C 53.74 . 1 808 91 LEU CB C 43.32 . 1 809 91 LEU CG C 27.11 . 1 810 91 LEU CD1 C 25.43 . 1 811 91 LEU CD2 C 22.78 . 1 812 91 LEU N N 121.68 . 1 813 92 TYR H H 7.97 . 1 814 92 TYR HA H 4.49 . 1 815 92 TYR HB2 H 2.21 . 2 816 92 TYR HB3 H 2.95 . 2 817 92 TYR C C 175.63 . 1 818 92 TYR CA C 56.21 . 1 819 92 TYR CB C 41.54 . 1 820 92 TYR N N 119.36 . 1 821 93 LEU H H 7.97 . 1 822 93 LEU HA H 3.86 . 1 823 93 LEU HB2 H 0.94 . 2 824 93 LEU HB3 H 0.02 . 2 825 93 LEU HG H 1.03 . 1 826 93 LEU HD1 H -0.11 . 2 827 93 LEU HD2 H 0.01 . 2 828 93 LEU C C 176.44 . 1 829 93 LEU CA C 54.52 . 1 830 93 LEU CB C 38.39 . 1 831 93 LEU CG C 25.77 . 1 832 93 LEU CD1 C 24.78 . 1 833 93 LEU CD2 C 21.52 . 1 834 93 LEU N N 117.71 . 1 835 94 VAL H H 8.45 . 1 836 94 VAL HA H 3.95 . 1 837 94 VAL HB H 2.12 . 1 838 94 VAL HG1 H 0.90 . 2 839 94 VAL HG2 H 0.82 . 2 840 94 VAL C C 176.42 . 1 841 94 VAL CA C 65.37 . 1 842 94 VAL CB C 32.28 . 1 843 94 VAL CG1 C 21.72 . 1 844 94 VAL CG2 C 21.72 . 1 845 94 VAL N N 122.61 . 1 846 95 ARG H H 7.55 . 1 847 95 ARG HA H 4.52 . 1 848 95 ARG HB2 H 1.58 . 2 849 95 ARG HB3 H 2.03 . 2 850 95 ARG HG2 H 1.53 . 2 851 95 ARG HG3 H 1.67 . 2 852 95 ARG HD2 H 3.10 . 2 853 95 ARG HD3 H 2.89 . 2 854 95 ARG C C 172.49 . 1 855 95 ARG CA C 54.95 . 1 856 95 ARG CB C 33.69 . 1 857 95 ARG CG C 25.70 . 1 858 95 ARG CD C 43.64 . 1 859 95 ARG N N 118.16 . 1 860 96 ALA H H 8.42 . 1 861 96 ALA HA H 3.36 . 1 862 96 ALA HB H 1.00 . 1 863 96 ALA C C 177.38 . 1 864 96 ALA CA C 51.01 . 1 865 96 ALA CB C 18.48 . 1 866 96 ALA N N 126.69 . 1 867 97 LEU H H 8.33 . 1 868 97 LEU HA H 3.80 . 1 869 97 LEU HB2 H 0.77 . 2 870 97 LEU HB3 H 1.40 . 2 871 97 LEU HG H 1.56 . 1 872 97 LEU HD1 H 0.34 . 2 873 97 LEU HD2 H 0.77 . 2 874 97 LEU C C 175.02 . 1 875 97 LEU CA C 55.96 . 1 876 97 LEU CB C 42.38 . 1 877 97 LEU CG C 26.46 . 1 878 97 LEU CD1 C 26.83 . 1 879 97 LEU CD2 C 24.27 . 1 880 97 LEU N N 123.74 . 1 881 98 GLN H H 8.46 . 1 882 98 GLN HA H 4.05 . 1 883 98 GLN HB2 H 2.21 . 2 884 98 GLN HB3 H 1.82 . 2 885 98 GLN CA C 57.12 . 1 886 98 GLN CB C 30.41 . 1 887 98 GLN N N 135.17 . 1 stop_ save_