data_6560 #Corrected using PDB structure: 256BA # #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 # 64 G HA 3.09 2.23 # #The average CS difference between predicted and observed: #HA CA CB CO N HN #-0.03 2.03 2.22 N/A -0.32 -0.02 # #bmr6560.str.corr chemical shifts have been re-referenced with the following #offsets (these values have been added to the original bmr6560.str file): #HA CA CB CO N HN #N/A +2.13 +2.13 N/A -0.32 N/A # #The 95% confidence intervals for the above recommended offsets are: # HA CA CB CO N HN #+/-0.02 +/-0.16 +/-0.17 N/A +/-0.23 +/-0.05 # #The Correlation Coefficients between predicted and observed #chemical shifts are: #HA CA CB CO N HN #0.864 0.980 0.997 N/A 0.874 0.644 # #The RMSD between predicted and observed* (reference #corrected) chemical shifts are: #HA CA CB CO N HN #0.109 0.808 0.864 N/A 1.089 0.257 # ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; The NMR solution structure of a redesigned apocytochrome b562:Rd-apocyt b562 ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Feng H. . . 2 Takei J. . . 3 Lipsitz R. . . 4 Tjandra N. . . 5 Bai Y. . . stop_ _BMRB_accession_number 6560 _BMRB_flat_file_name bmr6560.str _Entry_type new _Submission_date 2005-03-18 _Accession_date 2005-03-31 _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' 591 '13C chemical shifts' 331 '15N chemical shifts' 110 stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_title ; Specific non-native hydrophobic interactions in a hidden folding intermediate: implications for protein folding ; _Citation_status published _Citation_type journal _MEDLINE_UI_code . _PubMed_ID 14580191 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Feng H. . . 2 Takei J. . . 3 Lipsitz R. . . 4 Tjandra N. . . 5 Bai Y. . . stop_ _Journal_abbreviation Biochemistry _Journal_volume 42 _Journal_issue 43 _Page_first 12461 _Page_last 12465 _Year 2003 loop_ _Keyword "four Helix protein" "Structural Genomics" "PSI" "Protein Structure Initiative" "Berkeley Structural Genomics Center" "BSGC" stop_ save_ ################################## # Molecular system description # ################################## save_system _Saveframe_category molecular_system _Mol_system_name "redesigned apocytochrome B562" _Abbreviation_common "redesigned apocytochrome B562" _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label "redesigned apocytochrome B562" $B562 stop_ _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Database_entry_details PDB 1YYJ ? . stop_ save_ ######################## # Monomeric polymers # ######################## save_B562 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common "redesigned apocytochrome B562" _Name_variant . _Abbreviation_common "redesigned apocytochrome B562" _Mol_thiol_state 'not present' ############################## # Polymer residue sequence # ############################## _Residue_count 106 _Mol_residue_sequence ; ADLEDNWETLNDNLKVIEKA DNAAQVKDALTKMRAAALDA QKATPPKLEDKSPDSPEMKD FRHGFDILVGQIDDALKLAN EGKVKEAQAAAEQLKTTIRA YNQKYG ; loop_ _Residue_seq_code _Residue_label 1 ALA 2 ASP 3 LEU 4 GLU 5 ASP 6 ASN 7 TRP 8 GLU 9 THR 10 LEU 11 ASN 12 ASP 13 ASN 14 LEU 15 LYS 16 VAL 17 ILE 18 GLU 19 LYS 20 ALA 21 ASP 22 ASN 23 ALA 24 ALA 25 GLN 26 VAL 27 LYS 28 ASP 29 ALA 30 LEU 31 THR 32 LYS 33 MET 34 ARG 35 ALA 36 ALA 37 ALA 38 LEU 39 ASP 40 ALA 41 GLN 42 LYS 43 ALA 44 THR 45 PRO 46 PRO 47 LYS 48 LEU 49 GLU 50 ASP 51 LYS 52 SER 53 PRO 54 ASP 55 SER 56 PRO 57 GLU 58 MET 59 LYS 60 ASP 61 PHE 62 ARG 63 HIS 64 GLY 65 PHE 66 ASP 67 ILE 68 LEU 69 VAL 70 GLY 71 GLN 72 ILE 73 ASP 74 ASP 75 ALA 76 LEU 77 LYS 78 LEU 79 ALA 80 ASN 81 GLU 82 GLY 83 LYS 84 VAL 85 LYS 86 GLU 87 ALA 88 GLN 89 ALA 90 ALA 91 ALA 92 GLU 93 GLN 94 LEU 95 LYS 96 THR 97 THR 98 ILE 99 ARG 100 ALA 101 TYR 102 ASN 103 GLN 104 LYS 105 TYR 106 GLY 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 GenBank AAN45672.1 "Soluble cytochrome B562 precursor[Shigella flexneri 2a str. 301]" 92.98 114 98 98 4e-40 REF NP_709965.1 "Soluble cytochrome B562 precursor[Shigella flexneri 2a str. 301]" 92.98 114 98 98 4e-40 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $B562 Human 9606 Eukaryota Metazoa Homon 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 $B562 "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 $B562 1.5 mM "[U-15N; U-13C]" "Sodium acetate" 50 mM . H2O 92.5 % . D2O 7.5 % . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $B562 1.5 mM "[U-13C]" "Sodium acetate" 50 mM . H2O 92.5 % . D2O 7.5 % . stop_ save_ ############################ # Computer software used # ############################ save_X-PLOR _Saveframe_category software _Name X-PLOR _Version XPLOR-NIH-2.9 loop_ _Task "structure solution" "refinement" stop_ save_ save_NMRPipe _Saveframe_category software _Name NMRPipe loop_ _Task processing stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 750 save_ ############################# # NMR applied experiments # ############################# save_NMR_applied_experiment _Saveframe_category NMR_applied_experiment _Experiment_name ; 2D HSQC 3D 13C-separated NOESY 3D 15N-separated NOESY HNHA 3D HNCACB 3D CBCA(CO)NH 3D HBHA(CO)NH ; save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 4.84 . pH temperature 298 . K pressure 1 . atm 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 . H 1 . ppm . . . . . . . . N 15 . ppm . . . . . . . . C 13 . ppm . . . . . . . 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_chemical_shift_set_1 _Saveframe_category assigned_chemical_shifts loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name "redesigned apocytochrome B562" 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 ALA HA H 4.42 . . 2 1 ALA HB H 1.52 . . 3 1 ALA CA C 51.34 . . 4 1 ALA CB C 19.25 . . 5 2 ASP H H 8.85 . . 6 2 ASP HA H 4.61 . . 7 2 ASP HB2 H 2.81 . . 8 2 ASP HB3 H 2.76 . . 9 2 ASP CA C 53.66 . . 10 2 ASP CB C 40.94 . . 11 2 ASP N N 120.05 . . 12 3 LEU H H 8.68 . . 13 3 LEU HA H 3.89 . . 14 3 LEU HB2 H 1.78 . . 15 3 LEU HB3 H 1.50 . . 16 3 LEU HG H 1.37 . . 17 3 LEU HD1 H 1.04 . . 18 3 LEU HD2 H 0.69 . . 19 3 LEU CA C 58.43 . . 20 3 LEU CB C 41.22 . . 21 3 LEU CG C 27.91 . . 22 3 LEU CD1 C 25.19 . . 23 3 LEU CD2 C 22.67 . . 24 3 LEU N N 123.21 . . 25 4 GLU H H 8.62 . . 26 4 GLU HA H 4.38 . . 27 4 GLU HB2 H 2.17 . . 28 4 GLU HB3 H 2.18 . . 29 4 GLU HG2 H 2.52 . . 30 4 GLU HG3 H 2.48 . . 31 4 GLU CA C 58.93 . . 32 4 GLU CB C 28.36 . . 33 4 GLU CG C 35.01 . . 34 4 GLU N N 115.58 . . 35 5 ASP H H 7.61 . . 36 5 ASP HA H 4.50 . . 37 5 ASP HB2 H 2.82 . . 38 5 ASP HB3 H 2.70 . . 39 5 ASP CA C 56.91 . . 40 5 ASP CB C 40.50 . . 41 5 ASP N N 118.45 . . 42 6 ASN H H 7.87 . . 43 6 ASN HA H 4.53 . . 44 6 ASN HB2 H 2.54 . . 45 6 ASN HB3 H 2.24 . . 46 6 ASN HD21 H 7.18 . . 47 6 ASN HD22 H 7.03 . . 48 6 ASN CA C 56.76 . . 49 6 ASN CB C 38.62 . . 50 6 ASN N N 118.43 . . 51 6 ASN ND2 N 113.19 . . 52 7 TRP H H 8.72 . . 53 7 TRP HA H 4.78 . . 54 7 TRP HB2 H 3.45 . . 55 7 TRP HB3 H 3.37 . . 56 7 TRP HD1 H 7.29 . . 57 7 TRP HE1 H 10.63 . . 58 7 TRP HE3 H 7.62 . . 59 7 TRP HZ2 H 7.62 . . 60 7 TRP HZ3 H 7.29 . . 61 7 TRP HH2 H 6.88 . . 62 7 TRP CA C 60.31 . . 63 7 TRP CB C 30.10 . . 64 7 TRP N N 119.30 . . 65 8 GLU H H 8.02 . . 66 8 GLU HA H 4.21 . . 67 8 GLU HB2 H 2.29 . . 68 8 GLU HB3 H 2.10 . . 69 8 GLU HG2 H 2.59 . . 70 8 GLU HG3 H 2.51 . . 71 8 GLU CA C 59.58 . . 72 8 GLU CB C 28.29 . . 73 8 GLU CG C 36.52 . . 74 8 GLU N N 118.66 . . 75 9 THR H H 8.57 . . 76 9 THR HA H 4.04 . . 77 9 THR HB H 4.26 . . 78 9 THR HG2 H 1.13 . . 79 9 THR CA C 66.67 . . 80 9 THR CB C 68.04 . . 81 9 THR CG2 C 21.11 . . 82 9 THR N N 117.39 . . 83 10 LEU H H 8.38 . . 84 10 LEU HA H 4.06 . . 85 10 LEU HB2 H 2.42 . . 86 10 LEU HB3 H 1.43 . . 87 10 LEU HG H 1.94 . . 88 10 LEU HD1 H 0.92 . . 89 10 LEU HD2 H 1.02 . . 90 10 LEU CA C 59.44 . . 91 10 LEU CB C 41.23 . . 92 10 LEU CG C 27.71 . . 93 10 LEU CD1 C 25.19 . . 94 10 LEU CD2 C 24.59 . . 95 10 LEU N N 122.47 . . 96 11 ASN H H 8.31 . . 97 11 ASN HA H 4.50 . . 98 11 ASN HB2 H 2.92 . . 99 11 ASN HB3 H 2.82 . . 100 11 ASN HD21 H 7.46 . . 101 11 ASN HD22 H 6.72 . . 102 11 ASN CA C 56.69 . . 103 11 ASN CB C 38.99 . . 104 11 ASN N N 116.03 . . 105 11 ASN ND2 N 111.98 . . 106 12 ASP H H 9.41 . . 107 12 ASP HA H 4.42 . . 108 12 ASP HB2 H 2.80 . . 109 12 ASP HB3 H 2.68 . . 110 12 ASP CA C 57.27 . . 111 12 ASP CB C 39.92 . . 112 12 ASP N N 120.24 . . 113 13 ASN H H 7.82 . . 114 13 ASN HA H 4.53 . . 115 13 ASN HB2 H 2.83 . . 116 13 ASN HB3 H 2.70 . . 117 13 ASN HD21 H 7.66 . . 118 13 ASN HD22 H 7.21 . . 119 13 ASN CA C 57.63 . . 120 13 ASN CB C 40.43 . . 121 13 ASN N N 116.37 . . 122 13 ASN ND2 N 113.21 . . 123 14 LEU H H 7.82 . . 124 14 LEU HA H 4.08 . . 125 14 LEU HB2 H 2.08 . . 126 14 LEU HB3 H 1.34 . . 127 14 LEU HG H 1.89 . . 128 14 LEU HD1 H 0.82 . . 129 14 LEU HD2 H 0.78 . . 130 14 LEU CA C 58.35 . . 131 14 LEU CB C 41.23 . . 132 14 LEU CG C 27.46 . . 133 14 LEU CD1 C 25.19 . . 134 14 LEU CD2 C 24.38 . . 135 14 LEU N N 121.80 . . 136 15 LYS H H 7.24 . . 137 15 LYS HA H 4.09 . . 138 15 LYS HB2 H 1.95 . . 139 15 LYS HG2 H 1.65 . . 140 15 LYS HG3 H 1.64 . . 141 15 LYS HD2 H 1.72 . . 142 15 LYS HE2 H 2.98 . . 143 15 LYS CA C 59.08 . . 144 15 LYS CB C 31.69 . . 145 15 LYS CG C 25.19 . . 146 15 LYS CD C 29.47 . . 147 15 LYS CE C 42.06 . . 148 15 LYS N N 118.01 . . 149 16 VAL H H 7.23 . . 150 16 VAL HA H 3.55 . . 151 16 VAL HB H 2.38 . . 152 16 VAL HG1 H 1.08 . . 153 16 VAL HG2 H 0.91 . . 154 16 VAL CA C 65.94 . . 155 16 VAL CB C 31.61 . . 156 16 VAL CG1 C 20.96 . . 157 16 VAL CG2 C 20.38 . . 158 16 VAL N N 118.25 . . 159 17 ILE H H 7.88 . . 160 17 ILE HA H 3.40 . . 161 17 ILE HB H 2.02 . . 162 17 ILE HG12 H 1.54 . . 163 17 ILE HG13 H 1.54 . . 164 17 ILE HG2 H 0.89 . . 165 17 ILE HD1 H 0.84 . . 166 17 ILE CA C 66.16 . . 167 17 ILE CB C 38.19 . . 168 17 ILE CG1 C 30.04 . . 169 17 ILE CG2 C 17.34 . . 170 17 ILE CD1 C 15.53 . . 171 17 ILE N N 118.28 . . 172 18 GLU H H 7.86 . . 173 18 GLU HA H 3.94 . . 174 18 GLU HB2 H 2.06 . . 175 18 GLU HB3 H 2.06 . . 176 18 GLU HG2 H 2.37 . . 177 18 GLU HG3 H 2.30 . . 178 18 GLU CA C 58.93 . . 179 18 GLU CB C 29.45 . . 180 18 GLU CG C 34.91 . . 181 18 GLU N N 117.40 . . 182 19 LYS H H 7.13 . . 183 19 LYS HA H 4.42 . . 184 19 LYS HB2 H 1.96 . . 185 19 LYS HB3 H 1.76 . . 186 19 LYS HG2 H 1.51 . . 187 19 LYS HD2 H 1.64 . . 188 19 LYS HE2 H 2.97 . . 189 19 LYS CA C 55.10 . . 190 19 LYS CB C 33.06 . . 191 19 LYS CG C 24.74 . . 192 19 LYS CD C 29.27 . . 193 19 LYS CE C 42.61 . . 194 19 LYS N N 113.92 . . 195 20 ALA H H 7.25 . . 196 20 ALA HA H 4.13 . . 197 20 ALA HB H 1.46 . . 198 20 ALA CA C 53.22 . . 199 20 ALA CB C 21.06 . . 200 20 ALA N N 122.85 . . 201 21 ASP H H 8.75 . . 202 21 ASP HA H 4.81 . . 203 21 ASP HB2 H 2.85 . . 204 21 ASP HB3 H 2.65 . . 205 21 ASP CA C 53.37 . . 206 21 ASP CB C 42.74 . . 207 21 ASP N N 116.03 . . 208 22 ASN H H 7.62 . . 209 22 ASN HA H 4.94 . . 210 22 ASN HB2 H 2.96 . . 211 22 ASN HB3 H 2.91 . . 212 22 ASN HD21 H 7.68 . . 213 22 ASN HD22 H 6.87 . . 214 22 ASN CA C 52.07 . . 215 22 ASN CB C 41.37 . . 216 22 ASN N N 112.57 . . 217 22 ASN ND2 N 114.88 . . 218 23 ALA H H 9.02 . . 219 23 ALA HA H 3.77 . . 220 23 ALA HB H 1.51 . . 221 23 ALA CA C 55.25 . . 222 23 ALA CB C 18.60 . . 223 23 ALA N N 121.46 . . 224 24 ALA H H 8.42 . . 225 24 ALA HA H 4.01 . . 226 24 ALA HB H 1.47 . . 227 24 ALA CA C 55.68 . . 228 24 ALA CB C 17.38 . . 229 25 GLN H H 8.02 . . 230 25 GLN HA H 4.10 . . 231 25 GLN HB2 H 1.90 . . 232 25 GLN HG2 H 2.38 . . 233 25 GLN HG3 H 2.32 . . 234 25 GLN HE21 H 7.37 . . 235 25 GLN HE22 H 7.05 . . 236 25 GLN CA C 58.35 . . 237 25 GLN CB C 29.59 . . 238 25 GLN CG C 33.80 . . 239 25 GLN N N 116.75 . . 240 25 GLN NE2 N 111.01 . . 241 26 VAL H H 7.11 . . 242 26 VAL HA H 3.47 . . 243 26 VAL HB H 2.12 . . 244 26 VAL HG1 H 1.05 . . 245 26 VAL HG2 H 0.86 . . 246 26 VAL CA C 66.67 . . 247 26 VAL CB C 31.69 . . 248 26 VAL CG1 C 21.57 . . 249 26 VAL CG2 C 20.96 . . 250 26 VAL N N 117.39 . . 251 27 LYS H H 8.73 . . 252 27 LYS HA H 3.71 . . 253 27 LYS HB2 H 1.76 . . 254 27 LYS HB3 H 1.75 . . 255 27 LYS HG2 H 1.48 . . 256 27 LYS HD2 H 1.65 . . 257 27 LYS HE2 H 2.90 . . 258 27 LYS CA C 60.31 . . 259 27 LYS CB C 32.34 . . 260 27 LYS CG C 24.74 . . 261 27 LYS CD C 30.18 . . 262 27 LYS CE C 42.06 . . 263 27 LYS N N 119.04 . . 264 28 ASP H H 8.24 . . 265 28 ASP HA H 4.32 . . 266 28 ASP HB2 H 2.74 . . 267 28 ASP HB3 H 2.58 . . 268 28 ASP CA C 57.49 . . 269 28 ASP CB C 41.08 . . 270 28 ASP N N 120.31 . . 271 29 ALA H H 7.59 . . 272 29 ALA HA H 4.17 . . 273 29 ALA HB H 1.53 . . 274 29 ALA CA C 54.88 . . 275 29 ALA CB C 19.40 . . 276 29 ALA N N 121.04 . . 277 30 LEU H H 8.51 . . 278 30 LEU HA H 4.06 . . 279 30 LEU HB2 H 2.06 . . 280 30 LEU HB3 H 1.31 . . 281 30 LEU HG H 1.87 . . 282 30 LEU HD1 H 0.92 . . 283 30 LEU HD2 H 0.70 . . 284 30 LEU CA C 57.78 . . 285 30 LEU CB C 42.53 . . 286 30 LEU CG C 27.15 . . 287 30 LEU CD1 C 25.19 . . 288 30 LEU CD2 C 26.55 . . 289 30 LEU N N 117.45 . . 290 31 THR H H 8.33 . . 291 31 THR HA H 3.76 . . 292 31 THR HB H 4.47 . . 293 31 THR HG2 H 1.27 . . 294 31 THR CA C 67.61 . . 295 31 THR CB C 69.12 . . 296 31 THR CG2 C 20.21 . . 297 31 THR N N 116.03 . . 298 32 LYS H H 7.74 . . 299 32 LYS HA H 4.05 . . 300 32 LYS HB2 H 1.72 . . 301 32 LYS HB3 H 1.72 . . 302 32 LYS HG2 H 1.46 . . 303 32 LYS HG3 H 1.40 . . 304 32 LYS HD2 H 1.63 . . 305 32 LYS HE2 H 2.98 . . 306 32 LYS HZ H 6.95 . . 307 32 LYS CA C 59.58 . . 308 32 LYS CB C 32.48 . . 309 32 LYS CG C 25.38 . . 310 32 LYS CD C 30.20 . . 311 32 LYS CE C 42.41 . . 312 32 LYS N N 122.66 . . 313 33 MET H H 8.36 . . 314 33 MET HA H 3.73 . . 315 33 MET HB2 H 2.00 . . 316 33 MET HB3 H 1.93 . . 317 33 MET HG2 H 2.38 . . 318 33 MET HE H 2.36 . . 319 33 MET CA C 59.80 . . 320 33 MET CB C 33.28 . . 321 33 MET CG C 33.35 . . 322 33 MET N N 118.20 . . 323 34 ARG H H 8.56 . . 324 34 ARG HA H 3.60 . . 325 34 ARG HB2 H 2.01 . . 326 34 ARG HG2 H 1.92 . . 327 34 ARG HD2 H 3.24 . . 328 34 ARG HD3 H 2.78 . . 329 34 ARG HE H 7.79 . . 330 34 ARG HH11 H 6.74 . . 331 34 ARG HH12 H 6.74 . . 332 34 ARG CA C 60.31 . . 333 34 ARG CB C 30.38 . . 334 34 ARG CG C 29.47 . . 335 34 ARG CD C 42.41 . . 336 34 ARG N N 120.39 . . 337 35 ALA H H 7.20 . . 338 35 ALA HA H 4.04 . . 339 35 ALA HB H 1.44 . . 340 35 ALA CA C 54.74 . . 341 35 ALA CB C 18.17 . . 342 35 ALA N N 116.96 . . 343 36 ALA H H 7.64 . . 344 36 ALA HA H 4.06 . . 345 36 ALA HB H 1.50 . . 346 36 ALA CA C 54.52 . . 347 36 ALA CB C 18.03 . . 348 36 ALA N N 120.22 . . 349 37 ALA H H 8.48 . . 350 37 ALA HA H 3.74 . . 351 37 ALA HB H 1.44 . . 352 37 ALA CA C 54.45 . . 353 37 ALA CB C 18.60 . . 354 37 ALA N N 119.80 . . 355 38 LEU H H 7.66 . . 356 38 LEU HA H 3.87 . . 357 38 LEU HB2 H 1.77 . . 358 38 LEU HB3 H 1.36 . . 359 38 LEU HG H 1.55 . . 360 38 LEU HD1 H 0.88 . . 361 38 LEU HD2 H 0.86 . . 362 38 LEU CA C 57.14 . . 363 38 LEU CB C 41.59 . . 364 38 LEU CG C 27.00 . . 365 38 LEU CD1 C 22.47 . . 366 38 LEU CD2 C 22.48 . . 367 38 LEU N N 115.34 . . 368 39 ASP H H 7.63 . . 369 39 ASP HA H 4.25 . . 370 39 ASP HB2 H 2.57 . . 371 39 ASP CA C 57.05 . . 372 39 ASP CB C 41.51 . . 373 39 ASP N N 119.21 . . 374 40 ALA H H 8.15 . . 375 40 ALA HA H 3.57 . . 376 40 ALA HB H 0.43 . . 377 40 ALA CA C 54.67 . . 378 40 ALA CB C 17.59 . . 379 40 ALA N N 123.41 . . 380 41 GLN H H 6.84 . . 381 41 GLN HA H 3.28 . . 382 41 GLN HB2 H 2.05 . . 383 41 GLN HB3 H 1.71 . . 384 41 GLN HG2 H 2.35 . . 385 41 GLN HG3 H 2.21 . . 386 41 GLN HE21 H 7.51 . . 387 41 GLN HE22 H 6.87 . . 388 41 GLN CA C 57.63 . . 389 41 GLN CB C 29.08 . . 390 41 GLN CG C 34.33 . . 391 41 GLN N N 112.02 . . 392 41 GLN NE2 N 111.98 . . 393 42 LYS H H 6.99 . . 394 42 LYS HA H 4.25 . . 395 42 LYS HB2 H 1.97 . . 396 42 LYS HB3 H 1.82 . . 397 42 LYS HG2 H 1.47 . . 398 42 LYS HD2 H 1.70 . . 399 42 LYS HE2 H 2.97 . . 400 42 LYS CA C 56.11 . . 401 42 LYS CB C 32.99 . . 402 42 LYS CG C 24.99 . . 403 42 LYS CD C 29.92 . . 404 42 LYS CE C 42.81 . . 405 42 LYS N N 113.75 . . 406 43 ALA H H 7.71 . . 407 43 ALA HA H 4.38 . . 408 43 ALA HB H 1.51 . . 409 43 ALA CA C 51.56 . . 410 43 ALA CB C 21.50 . . 411 43 ALA N N 122.79 . . 412 44 THR H H 8.18 . . 413 44 THR HA H 4.42 . . 414 44 THR HB H 3.94 . . 415 44 THR HG2 H 1.12 . . 416 44 THR CA C 59.37 . . 417 44 THR CB C 70.21 . . 418 44 THR CG2 C 19.75 . . 419 44 THR N N 114.07 . . 420 45 PRO HA H 4.34 . . 421 45 PRO HB2 H 2.26 . . 422 45 PRO HB3 H 1.98 . . 423 45 PRO HG2 H 2.08 . . 424 45 PRO HG3 H 2.08 . . 425 45 PRO HD2 H 3.87 . . 426 45 PRO HD3 H 3.86 . . 427 45 PRO CA C 65.52 . . 428 45 PRO CB C 32.00 . . 429 45 PRO CG C 29.42 . . 430 45 PRO CD C 50.71 . . 431 46 PRO HA H 4.23 . . 432 46 PRO HB2 H 2.27 . . 433 46 PRO HB3 H 1.98 . . 434 46 PRO HG2 H 2.20 . . 435 46 PRO HG3 H 2.19 . . 436 46 PRO HD2 H 3.98 . . 437 46 PRO CA C 65.36 . . 438 46 PRO CB C 32.12 . . 439 46 PRO CG C 29.42 . . 440 46 PRO CD C 50.57 . . 441 47 LYS H H 8.22 . . 442 47 LYS HA H 4.26 . . 443 47 LYS HB2 H 1.96 . . 444 47 LYS HG2 H 1.53 . . 445 47 LYS HD2 H 1.70 . . 446 47 LYS HE2 H 2.99 . . 447 47 LYS CA C 57.85 . . 448 47 LYS CB C 32.12 . . 449 47 LYS CG C 25.65 . . 450 47 LYS CD C 29.72 . . 451 47 LYS CE C 42.72 . . 452 47 LYS N N 113.27 . . 453 48 LEU H H 7.71 . . 454 48 LEU HA H 4.59 . . 455 48 LEU HB2 H 1.64 . . 456 48 LEU HB3 H 1.45 . . 457 48 LEU HG H 1.43 . . 458 48 LEU HD1 H 0.88 . . 459 48 LEU HD2 H 0.69 . . 460 48 LEU CA C 53.44 . . 461 48 LEU CB C 42.24 . . 462 48 LEU CG C 27.91 . . 463 48 LEU CD1 C 23.38 . . 464 48 LEU CD2 C 25.19 . . 465 48 LEU N N 116.34 . . 466 49 GLU HA H 4.09 . . 467 49 GLU HB2 H 2.15 . . 468 49 GLU HB3 H 2.15 . . 469 49 GLU HG2 H 2.39 . . 470 49 GLU HG3 H 2.39 . . 471 49 GLU CA C 58.72 . . 472 49 GLU CB C 29.16 . . 473 49 GLU CG C 34.71 . . 474 50 ASP H H 8.51 . . 475 50 ASP HA H 4.65 . . 476 50 ASP HB2 H 2.76 . . 477 50 ASP HB3 H 2.76 . . 478 50 ASP CA C 53.44 . . 479 50 ASP CB C 40.07 . . 480 50 ASP N N 115.69 . . 481 51 LYS H H 7.77 . . 482 51 LYS HA H 4.49 . . 483 51 LYS HB2 H 1.91 . . 484 51 LYS HB3 H 1.88 . . 485 51 LYS HG2 H 1.41 . . 486 51 LYS HG3 H 1.30 . . 487 51 LYS HD2 H 1.64 . . 488 51 LYS HD3 H 1.64 . . 489 51 LYS HE2 H 2.99 . . 490 51 LYS CA C 53.95 . . 491 51 LYS CB C 32.62 . . 492 51 LYS CG C 24.74 . . 493 51 LYS CD C 30.18 . . 494 51 LYS CE C 42.86 . . 495 51 LYS N N 119.47 . . 496 52 SER H H 8.72 . . 497 52 SER HA H 4.72 . . 498 52 SER HB2 H 4.17 . . 499 52 SER HB3 H 3.98 . . 500 52 SER CA C 56.76 . . 501 52 SER CB C 63.05 . . 502 52 SER N N 116.64 . . 503 53 PRO HA H 4.33 . . 504 53 PRO HB2 H 2.40 . . 505 53 PRO HB3 H 1.98 . . 506 53 PRO HG2 H 2.08 . . 507 53 PRO HD2 H 3.94 . . 508 53 PRO CA C 65.44 . . 509 53 PRO CB C 31.83 . . 510 53 PRO CG C 28.82 . . 511 53 PRO CD C 51.17 . . 512 54 ASP H H 7.98 . . 513 54 ASP HA H 4.83 . . 514 54 ASP HB2 H 2.83 . . 515 54 ASP HB3 H 2.64 . . 516 54 ASP CA C 52.86 . . 517 54 ASP CB C 40.86 . . 518 54 ASP N N 113.35 . . 519 55 SER H H 7.77 . . 520 55 SER HA H 4.54 . . 521 55 SER HB2 H 4.29 . . 522 55 SER HB3 H 4.29 . . 523 55 SER CA C 56.91 . . 524 55 SER CB C 62.98 . . 525 55 SER N N 115.93 . . 526 56 PRO HA H 4.34 . . 527 56 PRO HB2 H 2.40 . . 528 56 PRO HB3 H 1.98 . . 529 56 PRO HG2 H 2.08 . . 530 56 PRO HG3 H 2.08 . . 531 56 PRO HD2 H 3.94 . . 532 56 PRO CA C 66.01 . . 533 56 PRO CB C 32.19 . . 534 56 PRO CG C 28.82 . . 535 56 PRO CD C 51.78 . . 536 57 GLU HA H 4.11 . . 537 57 GLU HB2 H 2.33 . . 538 57 GLU HB3 H 1.90 . . 539 57 GLU HG2 H 2.59 . . 540 57 GLU HG3 H 2.38 . . 541 57 GLU CA C 60.74 . . 542 57 GLU CB C 29.88 . . 543 57 GLU CG C 34.25 . . 544 57 GLU N N 116.50 . . 545 58 MET H H 7.68 . . 546 58 MET HA H 4.59 . . 547 58 MET HB2 H 2.23 . . 548 58 MET HB3 H 2.08 . . 549 58 MET HG2 H 2.78 . . 550 58 MET HG3 H 2.27 . . 551 58 MET HE H 2.17 . . 552 58 MET CA C 56.26 . . 553 58 MET CB C 30.17 . . 554 58 MET CG C 32.24 . . 555 58 MET N N 118.75 . . 556 59 LYS H H 8.46 . . 557 59 LYS HA H 4.01 . . 558 59 LYS HB2 H 1.93 . . 559 59 LYS HB3 H 1.94 . . 560 59 LYS HG2 H 1.44 . . 561 59 LYS HD2 H 1.60 . . 562 59 LYS HD3 H 1.59 . . 563 59 LYS HE2 H 2.94 . . 564 59 LYS CA C 60.31 . . 565 59 LYS CB C 32.12 . . 566 59 LYS CG C 25.38 . . 567 59 LYS CD C 29.72 . . 568 59 LYS CE C 41.96 . . 569 59 LYS N N 119.80 . . 570 60 ASP H H 8.36 . . 571 60 ASP HA H 4.61 . . 572 60 ASP HB2 H 3.02 . . 573 60 ASP HB3 H 2.92 . . 574 60 ASP CA C 57.49 . . 575 60 ASP CB C 41.08 . . 576 60 ASP N N 120.51 . . 577 61 PHE H H 8.26 . . 578 61 PHE HA H 4.09 . . 579 61 PHE HB2 H 3.24 . . 580 61 PHE HB3 H 2.70 . . 581 61 PHE HD1 H 6.64 . . 582 61 PHE HD2 H 6.64 . . 583 61 PHE HE1 H 7.32 . . 584 61 PHE HE2 H 7.32 . . 585 61 PHE HZ H 6.38 . . 586 61 PHE CA C 61.25 . . 587 61 PHE CB C 38.77 . . 588 61 PHE N N 121.36 . . 589 62 ARG H H 8.48 . . 590 62 ARG HA H 3.80 . . 591 62 ARG HB2 H 1.77 . . 592 62 ARG HB3 H 1.77 . . 593 62 ARG HG2 H 1.67 . . 594 62 ARG HG3 H 1.67 . . 595 62 ARG HD2 H 2.94 . . 596 62 ARG HD3 H 2.94 . . 597 62 ARG HE H 7.52 . . 598 62 ARG HH11 H 6.57 . . 599 62 ARG CA C 61.25 . . 600 62 ARG CB C 30.37 . . 601 62 ARG CG C 28.82 . . 602 62 ARG CD C 42.41 . . 603 62 ARG N N 116.32 . . 604 63 HIS H H 8.70 . . 605 63 HIS HA H 4.60 . . 606 63 HIS HB2 H 3.56 . . 607 63 HIS HB3 H 3.45 . . 608 63 HIS HD2 H 7.39 . . 609 63 HIS HE1 H 7.74 . . 610 63 HIS CA C 58.14 . . 611 63 HIS CB C 27.93 . . 612 63 HIS N N 118.71 . . 613 64 GLY H H 8.19 . . 614 64 GLY HA2 H 3.21 . . 615 64 GLY HA3 H 3.03 . . 616 64 GLY CA C 46.43 . . 617 64 GLY N N 106.71 . . 618 65 PHE H H 6.97 . . 619 65 PHE HA H 4.10 . . 620 65 PHE HB2 H 2.85 . . 621 65 PHE HB3 H 2.63 . . 622 65 PHE HD1 H 6.70 . . 623 65 PHE HD2 H 6.70 . . 624 65 PHE HE1 H 6.38 . . 625 65 PHE HE2 H 6.38 . . 626 65 PHE HZ H 6.50 . . 627 65 PHE CA C 62.62 . . 628 65 PHE CB C 39.06 . . 629 65 PHE N N 117.43 . . 630 66 ASP H H 7.51 . . 631 66 ASP HA H 4.42 . . 632 66 ASP HB2 H 2.79 . . 633 66 ASP HB3 H 2.68 . . 634 66 ASP CA C 57.92 . . 635 66 ASP CB C 39.85 . . 636 66 ASP N N 121.26 . . 637 67 ILE H H 7.62 . . 638 67 ILE HA H 3.63 . . 639 67 ILE HB H 1.88 . . 640 67 ILE HG12 H 1.17 . . 641 67 ILE HG13 H 0.93 . . 642 67 ILE HG2 H 0.82 . . 643 67 ILE HD1 H 0.70 . . 644 67 ILE CA C 63.70 . . 645 67 ILE CB C 36.82 . . 646 67 ILE CG1 C 27.00 . . 647 67 ILE CG2 C 16.13 . . 648 67 ILE CD1 C 15.53 . . 649 67 ILE N N 120.34 . . 650 68 LEU H H 7.72 . . 651 68 LEU HA H 4.14 . . 652 68 LEU HB2 H 1.79 . . 653 68 LEU HB3 H 1.55 . . 654 68 LEU HG H 1.62 . . 655 68 LEU HD1 H 0.88 . . 656 68 LEU HD2 H 0.86 . . 657 68 LEU CA C 57.92 . . 658 68 LEU CB C 42.45 . . 659 68 LEU CG C 27.20 . . 660 68 LEU CD1 C 25.63 . . 661 68 LEU CD2 C 25.19 . . 662 68 LEU N N 120.04 . . 663 69 VAL H H 8.71 . . 664 69 VAL HA H 3.44 . . 665 69 VAL HB H 2.18 . . 666 69 VAL HG1 H 1.04 . . 667 69 VAL HG2 H 0.90 . . 668 69 VAL CA C 67.82 . . 669 69 VAL CB C 31.25 . . 670 69 VAL CG1 C 22.78 . . 671 69 VAL CG2 C 20.96 . . 672 69 VAL N N 118.71 . . 673 70 GLY H H 7.78 . . 674 70 GLY HA2 H 3.88 . . 675 70 GLY HA3 H 3.87 . . 676 70 GLY CA C 47.51 . . 677 70 GLY N N 105.62 . . 678 71 GLN H H 7.91 . . 679 71 GLN HA H 4.21 . . 680 71 GLN HB2 H 1.98 . . 681 71 GLN HG2 H 2.34 . . 682 71 GLN HG3 H 2.32 . . 683 71 GLN HE21 H 7.22 . . 684 71 GLN HE22 H 6.13 . . 685 71 GLN CA C 58.86 . . 686 71 GLN CB C 29.01 . . 687 71 GLN CG C 34.00 . . 688 71 GLN N N 120.35 . . 689 71 GLN NE2 N 107.14 . . 690 72 ILE H H 8.88 . . 691 72 ILE HA H 3.52 . . 692 72 ILE HB H 2.07 . . 693 72 ILE HG12 H 0.95 . . 694 72 ILE HG2 H 0.80 . . 695 72 ILE HD1 H 0.71 . . 696 72 ILE CA C 66.16 . . 697 72 ILE CB C 37.90 . . 698 72 ILE CG2 C 14.92 . . 699 72 ILE CD1 C 13.71 . . 700 72 ILE N N 123.57 . . 701 73 ASP H H 8.96 . . 702 73 ASP HA H 4.58 . . 703 73 ASP HB2 H 3.04 . . 704 73 ASP HB3 H 2.93 . . 705 73 ASP CA C 57.78 . . 706 73 ASP CB C 39.27 . . 707 73 ASP N N 121.57 . . 708 74 ASP H H 8.10 . . 709 74 ASP HA H 4.47 . . 710 74 ASP HB2 H 2.84 . . 711 74 ASP HB3 H 2.71 . . 712 74 ASP CA C 57.49 . . 713 74 ASP CB C 40.14 . . 714 74 ASP N N 121.77 . . 715 75 ALA H H 7.82 . . 716 75 ALA HA H 4.04 . . 717 75 ALA HB H 1.56 . . 718 75 ALA CA C 55.03 . . 719 75 ALA CB C 17.89 . . 720 75 ALA N N 123.12 . . 721 76 LEU H H 9.18 . . 722 76 LEU HA H 3.83 . . 723 76 LEU HB2 H 1.99 . . 724 76 LEU HB3 H 1.60 . . 725 76 LEU HG H 1.63 . . 726 76 LEU HD1 H 0.94 . . 727 76 LEU HD2 H 0.92 . . 728 76 LEU CA C 57.85 . . 729 76 LEU CB C 42.24 . . 730 76 LEU CG C 27.91 . . 731 76 LEU CD1 C 25.65 . . 732 76 LEU CD2 C 25.19 . . 733 76 LEU N N 121.02 . . 734 77 LYS H H 7.81 . . 735 77 LYS HA H 4.07 . . 736 77 LYS HB2 H 1.99 . . 737 77 LYS HG2 H 1.58 . . 738 77 LYS HD2 H 1.72 . . 739 77 LYS HD3 H 1.72 . . 740 77 LYS HE2 H 2.97 . . 741 77 LYS CA C 60.02 . . 742 77 LYS CB C 32.12 . . 743 77 LYS CG C 25.19 . . 744 77 LYS CD C 31.54 . . 745 77 LYS CE C 42.41 . . 746 77 LYS N N 119.79 . . 747 78 LEU H H 6.98 . . 748 78 LEU HA H 4.14 . . 749 78 LEU HB2 H 1.79 . . 750 78 LEU HB3 H 1.51 . . 751 78 LEU HG H 1.61 . . 752 78 LEU HD1 H 0.91 . . 753 78 LEU HD2 H 0.87 . . 754 78 LEU CA C 57.63 . . 755 78 LEU CB C 41.51 . . 756 78 LEU CG C 27.46 . . 757 78 LEU CD1 C 23.48 . . 758 78 LEU CD2 C 23.47 . . 759 78 LEU N N 116.47 . . 760 79 ALA H H 8.35 . . 761 79 ALA HA H 3.66 . . 762 79 ALA HB H 1.33 . . 763 79 ALA CA C 55.75 . . 764 79 ALA CB C 17.45 . . 765 79 ALA N N 121.21 . . 766 80 ASN H H 8.95 . . 767 80 ASN HA H 4.43 . . 768 80 ASN HB2 H 2.83 . . 769 80 ASN HB3 H 2.60 . . 770 80 ASN HD21 H 7.35 . . 771 80 ASN HD22 H 6.87 . . 772 80 ASN CA C 55.61 . . 773 80 ASN CB C 38.41 . . 774 80 ASN N N 117.81 . . 775 80 ASN ND2 N 110.99 . . 776 81 GLU H H 7.50 . . 777 81 GLU HA H 4.42 . . 778 81 GLU HB2 H 2.18 . . 779 81 GLU HB3 H 2.13 . . 780 81 GLU HG2 H 2.37 . . 781 81 GLU HG3 H 2.37 . . 782 81 GLU CA C 55.82 . . 783 81 GLU CB C 29.73 . . 784 81 GLU CG C 34.25 . . 785 81 GLU N N 116.95 . . 786 82 GLY H H 7.88 . . 787 82 GLY HA2 H 4.28 . . 788 82 GLY HA3 H 3.55 . . 789 82 GLY CA C 45.42 . . 790 82 GLY N N 106.66 . . 791 83 LYS H H 7.93 . . 792 83 LYS HA H 4.51 . . 793 83 LYS HB2 H 2.08 . . 794 83 LYS HB3 H 2.06 . . 795 83 LYS HG2 H 1.41 . . 796 83 LYS HG3 H 1.29 . . 797 83 LYS HD2 H 1.64 . . 798 83 LYS HE2 H 2.97 . . 799 83 LYS CA C 54.81 . . 800 83 LYS CB C 30.38 . . 801 83 LYS CG C 24.94 . . 802 83 LYS CD C 29.72 . . 803 83 LYS CE C 42.76 . . 804 83 LYS N N 123.30 . . 805 84 VAL H H 7.60 . . 806 84 VAL HA H 3.24 . . 807 84 VAL HB H 2.02 . . 808 84 VAL HG1 H 0.84 . . 809 84 VAL HG2 H 0.75 . . 810 84 VAL CA C 67.61 . . 811 84 VAL CB C 31.68 . . 812 84 VAL CG1 C 20.96 . . 813 84 VAL CG2 C 19.75 . . 814 84 VAL N N 121.61 . . 815 85 LYS H H 8.55 . . 816 85 LYS HA H 4.37 . . 817 85 LYS HB2 H 1.87 . . 818 85 LYS HB3 H 1.87 . . 819 85 LYS HG2 H 1.51 . . 820 85 LYS HD2 H 1.74 . . 821 85 LYS HE2 H 3.04 . . 822 85 LYS CA C 59.15 . . 823 85 LYS CB C 31.18 . . 824 85 LYS CG C 24.74 . . 825 85 LYS CD C 29.52 . . 826 85 LYS CE C 42.41 . . 827 85 LYS N N 119.32 . . 828 86 GLU H H 9.38 . . 829 86 GLU HA H 4.05 . . 830 86 GLU HB2 H 2.12 . . 831 86 GLU HB3 H 2.02 . . 832 86 GLU HG2 H 2.54 . . 833 86 GLU HG3 H 2.33 . . 834 86 GLU CA C 60.45 . . 835 86 GLU CB C 28.51 . . 836 86 GLU CG C 36.72 . . 837 86 GLU N N 121.02 . . 838 87 ALA H H 8.46 . . 839 87 ALA HA H 4.05 . . 840 87 ALA HB H 1.43 . . 841 87 ALA CA C 55.32 . . 842 87 ALA CB C 17.95 . . 843 87 ALA N N 123.79 . . 844 88 GLN H H 8.66 . . 845 88 GLN HA H 3.78 . . 846 88 GLN HB2 H 2.11 . . 847 88 GLN HB3 H 1.96 . . 848 88 GLN HG2 H 2.52 . . 849 88 GLN HG3 H 2.19 . . 850 88 GLN HE21 H 7.99 . . 851 88 GLN HE22 H 6.10 . . 852 88 GLN CA C 59.51 . . 853 88 GLN CB C 28.58 . . 854 88 GLN CG C 35.15 . . 855 88 GLN N N 116.30 . . 856 88 GLN NE2 N 113.42 . . 857 89 ALA H H 8.16 . . 858 89 ALA HA H 4.22 . . 859 89 ALA HB H 1.56 . . 860 89 ALA CA C 54.74 . . 861 89 ALA CB C 17.45 . . 862 89 ALA N N 122.97 . . 863 90 ALA H H 8.06 . . 864 90 ALA HA H 4.21 . . 865 90 ALA HB H 1.53 . . 866 90 ALA CA C 54.67 . . 867 90 ALA CB C 17.23 . . 868 90 ALA N N 121.60 . . 869 91 ALA H H 8.32 . . 870 91 ALA HA H 4.01 . . 871 91 ALA HB H 1.55 . . 872 91 ALA CA C 54.23 . . 873 91 ALA CB C 17.66 . . 874 91 ALA N N 120.38 . . 875 92 GLU H H 7.72 . . 876 92 GLU HA H 4.10 . . 877 92 GLU HB2 H 2.17 . . 878 92 GLU HG2 H 2.37 . . 879 92 GLU CA C 59.00 . . 880 92 GLU CB C 28.72 . . 881 92 GLU CG C 35.16 . . 882 92 GLU N N 117.25 . . 883 93 GLN H H 7.40 . . 884 93 GLN HA H 4.24 . . 885 93 GLN HB2 H 2.25 . . 886 93 GLN HB3 H 1.98 . . 887 93 GLN HG2 H 2.45 . . 888 93 GLN HE21 H 7.68 . . 889 93 GLN HE22 H 6.46 . . 890 93 GLN CA C 58.14 . . 891 93 GLN CB C 28.29 . . 892 93 GLN CG C 33.80 . . 893 93 GLN N N 116.93 . . 894 93 GLN NE2 N 111.78 . . 895 94 LEU H H 7.70 . . 896 94 LEU HA H 4.07 . . 897 94 LEU HB2 H 2.07 . . 898 94 LEU HB3 H 1.59 . . 899 94 LEU HG H 1.91 . . 900 94 LEU HD1 H 0.94 . . 901 94 LEU HD2 H 0.91 . . 902 94 LEU CA C 57.56 . . 903 94 LEU CB C 41.51 . . 904 94 LEU CG C 27.46 . . 905 94 LEU CD1 C 23.58 . . 906 94 LEU CD2 C 23.58 . . 907 94 LEU N N 118.25 . . 908 95 LYS H H 7.97 . . 909 95 LYS HA H 3.77 . . 910 95 LYS HB2 H 1.95 . . 911 95 LYS HB3 H 1.92 . . 912 95 LYS HG2 H 1.48 . . 913 95 LYS HG3 H 1.39 . . 914 95 LYS HD2 H 1.76 . . 915 95 LYS HE2 H 2.92 . . 916 95 LYS CA C 60.23 . . 917 95 LYS CB C 32.55 . . 918 95 LYS CG C 24.74 . . 919 95 LYS CD C 30.02 . . 920 95 LYS CE C 41.96 . . 921 95 LYS N N 117.83 . . 922 96 THR H H 7.57 . . 923 96 THR HA H 3.88 . . 924 96 THR HB H 4.28 . . 925 96 THR HG2 H 0.97 . . 926 96 THR CA C 66.09 . . 927 96 THR CB C 68.33 . . 928 96 THR CG2 C 21.57 . . 929 97 THR H H 7.72 . . 930 97 THR HA H 3.87 . . 931 97 THR HB H 4.27 . . 932 97 THR HG2 H 1.55 . . 933 97 THR CA C 66.23 . . 934 97 THR CB C 67.82 . . 935 97 THR CG2 C 20.78 . . 936 97 THR N N 120.04 . . 937 98 ILE H H 8.49 . . 938 98 ILE HA H 3.51 . . 939 98 ILE HB H 1.87 . . 940 98 ILE HG12 H 1.42 . . 941 98 ILE HG2 H 1.02 . . 942 98 ILE HD1 H 0.86 . . 943 98 ILE CA C 66.38 . . 944 98 ILE CB C 38.26 . . 945 98 ILE CG1 C 30.63 . . 946 98 ILE CG2 C 16.13 . . 947 98 ILE CD1 C 15.53 . . 948 98 ILE N N 120.35 . . 949 99 ARG H H 8.26 . . 950 99 ARG HA H 3.94 . . 951 99 ARG HB2 H 1.88 . . 952 99 ARG HB3 H 1.84 . . 953 99 ARG HG2 H 1.72 . . 954 99 ARG HG3 H 1.60 . . 955 99 ARG HD2 H 3.14 . . 956 99 ARG HD3 H 3.12 . . 957 99 ARG HE H 7.15 . . 958 99 ARG CA C 59.19 . . 959 99 ARG CB C 29.52 . . 960 99 ARG CG C 27.00 . . 961 99 ARG CD C 43.52 . . 962 99 ARG N N 117.72 . . 963 100 ALA H H 7.79 . . 964 100 ALA HA H 4.04 . . 965 100 ALA HB H 1.49 . . 966 100 ALA CA C 54.89 . . 967 100 ALA CB C 17.97 . . 968 100 ALA N N 120.08 . . 969 101 TYR H H 8.23 . . 970 101 TYR HA H 4.34 . . 971 101 TYR HB2 H 3.35 . . 972 101 TYR HB3 H 3.16 . . 973 101 TYR HD1 H 7.07 . . 974 101 TYR HD2 H 7.07 . . 975 101 TYR HE1 H 6.62 . . 976 101 TYR HE2 H 6.62 . . 977 101 TYR CA C 60.96 . . 978 101 TYR CB C 37.69 . . 979 101 TYR N N 117.03 . . 980 102 ASN H H 8.67 . . 981 102 ASN HA H 3.46 . . 982 102 ASN HB2 H 2.31 . . 983 102 ASN HB3 H 1.69 . . 984 102 ASN HD21 H 7.32 . . 985 102 ASN HD22 H 6.72 . . 986 102 ASN CA C 56.49 . . 987 102 ASN CB C 39.10 . . 988 102 ASN N N 120.06 . . 989 102 ASN ND2 N 111.07 . . 990 103 GLN H H 8.05 . . 991 103 GLN HA H 3.92 . . 992 103 GLN HB2 H 2.07 . . 993 103 GLN HG2 H 2.41 . . 994 103 GLN HG3 H 2.29 . . 995 103 GLN HE21 H 7.51 . . 996 103 GLN HE22 H 6.87 . . 997 103 GLN CA C 58.35 . . 998 103 GLN CB C 28.25 . . 999 103 GLN CG C 33.80 . . 1000 103 GLN N N 117.47 . . 1001 103 GLN NE2 N 111.98 . . 1002 104 LYS H H 7.44 . . 1003 104 LYS HA H 3.89 . . 1004 104 LYS HB2 H 1.49 . . 1005 104 LYS HB3 H 1.14 . . 1006 104 LYS HG2 H 1.00 . . 1007 104 LYS HG3 H 0.49 . . 1008 104 LYS HD2 H 1.39 . . 1009 104 LYS HD3 H 1.37 . . 1010 104 LYS HE2 H 2.78 . . 1011 104 LYS CA C 58.94 . . 1012 104 LYS CB C 33.73 . . 1013 104 LYS CG C 24.28 . . 1014 104 LYS CD C 29.72 . . 1015 104 LYS CE C 41.96 . . 1016 104 LYS N N 117.65 . . 1017 105 TYR H H 8.10 . . 1018 105 TYR HA H 4.84 . . 1019 105 TYR HB2 H 3.46 . . 1020 105 TYR HB3 H 3.11 . . 1021 105 TYR HD1 H 7.61 . . 1022 105 TYR HD2 H 7.61 . . 1023 105 TYR HE1 H 7.00 . . 1024 105 TYR HE2 H 7.00 . . 1025 105 TYR CA C 58.68 . . 1026 105 TYR CB C 39.88 . . 1027 105 TYR N N 113.18 . . 1028 106 GLY H H 7.79 . . 1029 106 GLY HA2 H 3.97 . . 1030 106 GLY HA3 H 3.80 . . 1031 106 GLY CA C 45.53 . . 1032 106 GLY N N 112.66 . . stop_ save_ ######################## # Coupling constants # ######################## save_coupling_constants_set_1 _Saveframe_category coupling_constants loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Spectrometer_frequency_1H 750 loop_ _Coupling_constant_code _Atom_one_residue_seq_code _Atom_one_residue_label _Atom_one_name _Atom_two_residue_seq_code _Atom_two_residue_label _Atom_two_name _Coupling_constant_value _Coupling_constant_value_error 3JHNHA 2 ASP H 2 ASP HA 6.7 0.5 3JHNHA 3 LEU H 4 LEU HA 2.7 0.5 3JHNHA 4 GLU H 5 GLU HA 4.3 0.5 3JHNHA 5 ASP H 6 ASP HA 5.7 0.5 3JHNHA 6 ASN H 9 ASN HA 5.8 0.5 3JHNHA 7 TRP H 10 TRP HA 2.9 0.5 3JHNHA 8 GLU H 11 GLU HA 4.9 0.5 3JHNHA 9 THR H 13 THR HA 3.5 0.5 3JHNHA 10 LEU H 14 LEU HA 4.2 0.5 3JHNHA 11 ASN H 15 ASN HA 4.4 0.5 3JHNHA 12 ASP H 16 ASP HA 3.9 0.5 3JHNHA 13 ASN H 17 ASN HA 5.7 0.5 3JHNHA 14 LEU H 20 LEU HA 4.0 0.5 3JHNHA 15 LYS H 21 LYS HA 4.8 0.5 3JHNHA 16 VAL H 22 VAL HA 4.5 0.5 3JHNHA 17 ILE H 24 ILE HA 3.8 0.5 3JHNHA 18 GLU H 25 GLU HA 3.8 0.5 3JHNHA 19 LYS H 27 LYS HA 9.5 0.5 3JHNHA 20 ALA H 28 ALA HA 3.4 0.5 3JHNHA 21 ASP H 30 ASP HA 10.0 0.5 3JHNHA 22 ASN H 31 ASN HA 8.3 0.5 3JHNHA 23 ALA H 34 ALA HA 3.0 0.5 3JHNHA 24 ALA H 35 ALA HA 4.5 0.5 3JHNHA 25 GLN H 36 GLN HA 4.9 0.5 3JHNHA 26 VAL H 38 VAL HA 5.8 0.5 3JHNHA 27 LYS H 39 LYS HA 3.1 0.5 3JHNHA 28 ASP H 40 ASP HA 4.2 0.5 3JHNHA 29 ALA H 41 ALA HA 4.5 0.5 3JHNHA 30 LEU H 43 LEU HA 4.0 0.5 3JHNHA 31 THR H 44 THR HA 4.2 0.5 3JHNHA 32 LYS H 47 LYS HA 4.7 0.5 3JHNHA 33 MET H 48 MET HA 4.1 0.5 3JHNHA 34 ARG H 50 ARG HA 3.0 0.5 3JHNHA 35 ALA H 51 ALA HA 4.6 0.5 3JHNHA 36 ALA H 52 ALA HA 4.7 0.5 3JHNHA 37 ALA H 54 ALA HA 3.8 0.5 3JHNHA 38 LEU H 55 LEU HA 4.8 0.5 3JHNHA 39 ASP H 57 ASP HA 6.1 0.5 3JHNHA 40 ALA H 58 ALA HA 3.3 0.5 3JHNHA 41 GLN H 59 GLN HA 3.1 0.5 3JHNHA 42 LYS H 60 LYS HA 8.8 0.5 3JHNHA 43 ALA H 61 ALA HA 6.8 0.5 3JHNHA 44 THR H 62 THR HA 9.9 0.5 3JHNHA 47 LYS H 63 LYS HA 5.7 0.5 3JHNHA 48 LEU H 65 LEU HA 5.2 0.5 3JHNHA 50 ASP H 67 ASP HA 9.0 0.5 3JHNHA 51 LYS H 68 LYS HA 6.4 0.5 3JHNHA 52 SER H 69 SER HA 4.7 0.5 3JHNHA 54 ASP H 70 ASP HA 9.8 0.5 3JHNHA 55 SER H 72 SER HA 4.3 0.5 3JHNHA 58 MET H 74 MET HA 5.7 0.5 3JHNHA 59 LYS H 75 LYS HA 3.2 0.5 3JHNHA 60 ASP H 77 ASP HA 4.3 0.5 3JHNHA 61 PHE H 78 PHE HA 3.3 0.5 3JHNHA 62 ARG H 79 ARG HA 3.8 0.5 3JHNHA 63 HIS H 81 HIS HA 3.6 0.5 3JHNHA 64 GLY H 82 GLY HA 5.4 0.5 3JHNHA 65 PHE H 83 PHE HA 6.9 0.5 3JHNHA 66 ASP H 84 ASP HA 5.9 0.5 3JHNHA 67 ILE H 85 ILE HA 4.3 0.5 3JHNHA 68 LEU H 87 LEU HA 3.3 0.5 3JHNHA 69 VAL H 90 VAL HA 4.0 0.5 3JHNHA 70 GLY H 91 GLY HA 5.9 0.5 3JHNHA 71 GLN H 92 GLN HA 5.6 0.5 3JHNHA 72 ILE H 94 ILE HA 4.9 0.5 3JHNHA 73 ASP H 95 ASP HA 3.5 0.5 3JHNHA 74 ASP H 96 ASP HA 4.7 0.5 3JHNHA 75 ALA H 96 ALA HA 5.8 0.5 3JHNHA 76 LEU H 97 LEU HA 4.0 0.5 3JHNHA 77 LYS H 98 LYS HA 4.6 0.5 3JHNHA 78 LEU H 99 LEU HA 5.0 0.5 3JHNHA 79 ALA H 101 ALA HA 4.1 0.5 3JHNHA 80 ASN H 102 ASN HA 5.0 0.5 3JHNHA 81 GLU H 104 GLU HA 8.7 0.5 3JHNHA 82 GLY H 105 GLY HA 6.6 0.5 3JHNHA 83 LYS H 105 LYS HA 9.0 0.5 3JHNHA 84 VAL H 105 VAL HA 4.0 0.5 3JHNHA 85 LYS H 105 LYS HA 5.2 0.5 3JHNHA 86 GLU H 105 GLU HA 4.5 0.5 3JHNHA 87 ALA H 105 ALA HA 5.1 0.5 3JHNHA 88 GLN H 105 GLN HA 4.8 0.5 3JHNHA 89 ALA H 105 ALA HA 4.6 0.5 3JHNHA 90 ALA H 105 ALA HA 5.0 0.5 3JHNHA 91 ALA H 105 ALA HA 4.3 0.5 3JHNHA 92 GLU H 105 GLU HA 4.7 0.5 3JHNHA 93 GLN H 105 GLN HA 6.8 0.5 3JHNHA 94 LEU H 105 LEU HA 4.6 0.5 3JHNHA 95 LYS H 105 LYS HA 3.3 0.5 3JHNHA 96 THR H 105 THR HA 4.7 0.5 3JHNHA 97 THR H 105 THR HA 3.0 0.5 3JHNHA 98 ILE H 105 ILE HA 3.1 0.5 3JHNHA 99 ARG H 105 ARG HA 4.0 0.5 3JHNHA 100 ALA H 105 ALA HA 4.1 0.5 3JHNHA 101 TYR H 105 TYR HA 5.8 0.5 3JHNHA 102 ASN H 105 ASN HA 4.3 0.5 3JHNHA 103 GLN H 105 GLN HA 5.4 0.5 3JHNHA 104 LYS H 105 LYS HA 5.6 0.5 3JHNHA 105 TYR H 105 TYR HA 9.8 0.5 3JHNHA 106 GLY H 105 GLY HA 6.5 0.5 stop_ save_