data_6779 #Corrected using PDB structure: 1ZE3D # #N.B. (Observed* = Observed shift + Offset correction) # #The average CS difference between predicted and observed: #HA CA CB CO N HN #0.08 0.80 0.89 N/A -0.14 0.06 # #bmr6779.str.corr chemical shifts have been re-referenced with the following #offsets (these values have been added to the original bmr6779.str file): #HA CA CB CO N HN #N/A +0.85 +0.85 N/A -0.14 N/A # #The 95% confidence intervals for the above recommended offsets are: # HA CA CB CO N HN #+/-0.03 +/-0.14 +/-0.16 N/A +/-0.33 +/-0.06 # #The Correlation Coefficients between predicted and observed #chemical shifts are: #HA CA CB CO N HN #0.913 0.981 0.997 N/A 0.924 0.749 # #The RMSD between predicted and observed* (reference #corrected) chemical shifts are: #HA CA CB CO N HN #0.125 0.699 0.771 N/A 1.576 0.300 # ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution Structure of the type 1 pilus assembly platform FimD(25-125) ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Nishiyama M. . . 2 Horst R. . . 3 Herrmann R. . . 4 Vetsch M. . . 5 Bettendorff P. . . 6 Ignatov O. . . 7 Grutter M. . . 8 Wuthrich K. . . 9 Glockshuber R. . . 10 Capitani G. . . stop_ _BMRB_accession_number 6779 _BMRB_flat_file_name bmr6779.str _Entry_type new _Submission_date 2005-08-17 _Accession_date 2005-08-17 _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' 525 '15N chemical shifts' 107 '13C chemical shifts' 310 stop_ loop_ _Related_BMRB_accession_number _Relationship 6629 "FimD(25-139)" stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_title ; Structural basis of chaperone-subunit complex recognition by type 1 pilus assembly platform FimD ; _Citation_status published _Citation_type journal _MEDLINE_UI_code . _PubMed_ID 15920478 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Nishiyama M. . . 2 Horst R. . . 3 Herrmann R. . . 4 Vetsch M. . . 5 Bettendorff P. . . 6 Ignatov O. . . 7 Grutter M. . . 8 Wuthrich K. . . 9 Glockshuber R. . . 10 Capitani G. . . stop_ _Journal_abbreviation "EMBO J." _Journal_volume 24 _Journal_issue 12 _Page_first 2075 _Page_last 2086 _Year 2005 loop_ _Keyword "BETA SHEET" "ALPHA HELIX" FimD stop_ save_ ################################## # Molecular system description # ################################## save_system_FimD _Saveframe_category molecular_system _Mol_system_name "Outer membrane usher protein fimD" _Abbreviation_common FimD _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label "Outer membrane usher protein FimD" $FimD stop_ _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all free' loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Database_entry_details PDB 1ZDX ? . stop_ save_ ######################## # Monomeric polymers # ######################## save_FimD _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common "FimD" _Name_variant . _Abbreviation_common FimD _Mol_thiol_state 'all free' ############################## # Polymer residue sequence # ############################## _Residue_count 101 _Mol_residue_sequence ; GQELPPGTYRVDIYLNNGYM ATRDVTFNTGDSEQGIVPCL TRAQLASMGLNTASVAGMNL LADDACVPLTTMVQDATAHL DVGQQRLNLTIPQAFMSNRA R ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 25 GLY 2 26 GLN 3 27 GLU 4 28 LEU 5 29 PRO 6 30 PRO 7 31 GLY 8 32 THR 9 33 TYR 10 34 ARG 11 35 VAL 12 36 ASP 13 37 ILE 14 38 TYR 15 39 LEU 16 40 ASN 17 41 ASN 18 42 GLY 19 43 TYR 20 44 MET 21 45 ALA 22 46 THR 23 47 ARG 24 48 ASP 25 49 VAL 26 50 THR 27 51 PHE 28 52 ASN 29 53 THR 30 54 GLY 31 55 ASP 32 56 SER 33 57 GLU 34 58 GLN 35 59 GLY 36 60 ILE 37 61 VAL 38 62 PRO 39 63 CYS 40 64 LEU 41 65 THR 42 66 ARG 43 67 ALA 44 68 GLN 45 69 LEU 46 70 ALA 47 71 SER 48 72 MET 49 73 GLY 50 74 LEU 51 75 ASN 52 76 THR 53 77 ALA 54 78 SER 55 79 VAL 56 80 ALA 57 81 GLY 58 82 MET 59 83 ASN 60 84 LEU 61 85 LEU 62 86 ALA 63 87 ASP 64 88 ASP 65 89 ALA 66 90 CYS 67 91 VAL 68 92 PRO 69 93 LEU 70 94 THR 71 95 THR 72 96 MET 73 97 VAL 74 98 GLN 75 99 ASP 76 100 ALA 77 101 THR 78 102 ALA 79 103 HIS 80 104 LEU 81 105 ASP 82 106 VAL 83 107 GLY 84 108 GLN 85 109 GLN 86 110 ARG 87 111 LEU 88 112 ASN 89 113 LEU 90 114 THR 91 115 ILE 92 116 PRO 93 117 GLN 94 118 ALA 95 119 PHE 96 120 MET 97 121 SER 98 122 ASN 99 123 ARG 100 124 ALA 101 125 ARG stop_ _Sequence_homology_query_date 2006-01-30 _Sequence_homology_query_revised_last_date 2005-12-09 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 BMRB 6629 "E. coli FimD" 87.83 115 100 100 4e-52 PDB 1ZDX "A Chain A, Solution Structure Of The Type 1Pilus Assembly Platform Fimd(25-125)" 100.00 101 100 100 4e-52 PDB 1ZDV "A Chain A, Solution Structure Of The Type 1Pilus Assembly Platform Fimd(25-139)" 87.83 115 100 100 4e-52 PDB 1ZE3 "D Chain D, Crystal Structure Of The TernaryComplex Of Fimd (N- Terminal Domain) With Fimc And ThePilin Domain Of Fimh" 80.80 125 100 100 4e-52 DBJ BAB38699.1 "export and assembly outer membraneprotein of type 1 fimbriae [Escherichia coli O157:H7]" 11.50 878 100 100 4e-52 GenBank AAA97213.1 "CG Site No. 18349 [Escherichia coli]" 11.50 878 100 100 4e-52 GenBank AAC77273.1 "outer membrane protein; export andassembly of type 1 fimbriae, interrupted [Escherichiacoli K12]" 11.50 878 100 100 4e-52 GenBank AAG59499.1 "outer membrane protein; export andassembly of type 1 fimbriae, interrupted [Escherichiacoli O157:H7 EDL933]" 11.50 878 100 100 4e-52 REF ZP_00729829.1 "COG3188: P pilus assembly protein,porin PapC [Escherichia coli E22]" 11.70 863 98 100 1e-51 REF NP_290933.1 "outer membrane protein; export andassembly of type 1 fimbriae, interrupted [Escherichiacoli O157:H7 EDL933]" 11.50 878 100 100 4e-52 REF NP_313303.1 "FimD [Escherichia coli O157:H7]" 11.50 878 100 100 4e-52 REF NP_418737.1 "outer membrane protein; export andassembly of type 1 fimbriae, interrupted [Escherichiacoli K12]" 11.50 878 100 100 4e-52 SWISS-PROT P30130 "FIMD_ECOLI Outer membrane usher protein fimDprecursor" 11.50 878 100 100 4e-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 $FimD "E. coli" 562 Eubacteria . Escherichia coli 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 $FimD '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 $FimD 2 mM "[U-13C; U-15N]" H2O 90 % . D2O 10 % . stop_ save_ ############################ # Computer software used # ############################ save_XWINNMR _Saveframe_category software _Name XWINNMR _Version 3.5 loop_ _Task collection stop_ _Details Bruker save_ save_ATHNOS/CANDID _Saveframe_category software _Name ATHNOS/CANDID loop_ _Task "structure solution" "refinement" stop_ _Details Herrmann save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AVANCE _Field_strength 900 save_ ############################# # NMR applied experiments # ############################# save_NMR_applied_experiment _Saveframe_category NMR_applied_experiment _Experiment_name ; 3D 15N-separated NOESY 3D 13C-separated NOESY ; save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.0 0.1 pH temperature 293 0.5 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 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 (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 "Outer membrane usher protein FimD" 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 GLN CA C 55.59 . . 2 2 GLN HA H 4.28 . . 3 2 GLN CB C 29.67 . . 4 2 GLN HB2 H 1.87 . . 5 2 GLN HB3 H 2.00 . . 6 2 GLN CG C 34.04 . . 7 2 GLN HG2 H 2.23 . . 8 2 GLN NE2 N 112.45 . . 9 2 GLN HE21 H 6.83 . . 10 2 GLN HE22 H 7.54 . . 11 3 GLU H H 8.55 . . 12 3 GLU N N 122.46 . . 13 3 GLU CA C 56.84 . . 14 3 GLU HA H 4.08 . . 15 3 GLU CB C 29.95 . . 16 3 GLU HB2 H 1.87 . . 17 3 GLU HB3 H 1.80 . . 18 3 GLU CG C 36.31 . . 19 3 GLU HG2 H 2.08 . . 20 3 GLU HG3 H 2.15 . . 21 4 LEU H H 8.12 . . 24 4 LEU HA H 4.58 . . 26 4 LEU HB2 H 1.20 . . 27 4 LEU HB3 H 1.46 . . 28 4 LEU CG C 27.08 . . 29 4 LEU CD1 C 26.17 . . 30 4 LEU HD1 H 0.46 . . 31 4 LEU CD2 C 23.34 . . 32 4 LEU HD2 H 0.65 . . 33 4 LEU HG H 3.06 . . 34 5 PRO CG C 26.82 . . 35 5 PRO HG2 H 1.47 . . 36 5 PRO HG3 H 1.90 . . 37 5 PRO CD C 50.22 . . 38 5 PRO HD2 H 3.46 . . 39 5 PRO HD3 H 3.63 . . 40 6 PRO CA C 63.18 . . 41 6 PRO HA H 4.16 . . 43 6 PRO HB2 H 2.12 . . 44 6 PRO HB3 H 2.17 . . 45 6 PRO CG C 27.43 . . 46 6 PRO HG2 H 1.90 . . 47 6 PRO HG3 H 1.97 . . 48 6 PRO CD C 50.24 . . 49 6 PRO HD2 H 3.58 . . 50 6 PRO HD3 H 3.46 . . 51 7 GLY H H 8.21 . . 52 7 GLY N N 107.15 . . 53 7 GLY CA C 44.83 . . 54 7 GLY HA2 H 4.07 . . 55 7 GLY HA3 H 3.82 . . 56 8 THR H H 8.43 . . 57 8 THR N N 118.18 . . 58 8 THR CA C 62.56 . . 59 8 THR HA H 4.91 . . 60 8 THR CB C 69.51 . . 61 8 THR HB H 3.68 . . 62 8 THR CG2 C 21.75 . . 63 8 THR HG2 H 0.86 . . 64 9 TYR H H 9.01 . . 65 9 TYR N N 126.79 . . 66 9 TYR CA C 56.52 . . 67 9 TYR HA H 4.58 . . 68 9 TYR CB C 41.36 . . 69 9 TYR HB2 H 2.51 . . 70 9 TYR HB3 H 2.66 . . 71 9 TYR CD1 C 134.14 . . 72 9 TYR HD1 H 6.82 . . 73 9 TYR CE1 C 131.40 . . 74 9 TYR HE1 H 7.05 . . 75 10 ARG H H 8.61 . . 76 10 ARG N N 126.24 . . 77 10 ARG CA C 56.47 . . 78 10 ARG HA H 4.57 . . 79 10 ARG CB C 28.71 . . 80 10 ARG HB2 H 1.66 . . 81 10 ARG CG C 27.40 . . 82 10 ARG HG2 H 1.26 . . 83 10 ARG HG3 H 1.12 . . 84 10 ARG CD C 42.93 . . 85 10 ARG HD2 H 2.92 . . 86 10 ARG HD3 H 3.02 . . 87 10 ARG NE N 84.96 . . 88 10 ARG HE H 7.53 . . 89 11 VAL H H 8.55 . . 90 11 VAL N N 119.48 . . 91 11 VAL CA C 58.11 . . 92 11 VAL HA H 4.83 . . 93 11 VAL CB C 35.95 . . 94 11 VAL HB H 1.82 . . 95 11 VAL CG1 C 23.30 . . 96 11 VAL HG1 H 0.52 . . 97 11 VAL CG2 C 18.59 . . 98 11 VAL HG2 H 0.87 . . 99 12 ASP H H 8.48 . . 100 12 ASP N N 119.90 . . 101 12 ASP CA C 54.00 . . 102 12 ASP HA H 5.19 . . 103 12 ASP CB C 42.59 . . 104 12 ASP HB2 H 2.99 . . 105 12 ASP HB3 H 2.68 . . 106 13 ILE H H 9.52 . . 107 13 ILE N N 124.91 . . 108 13 ILE CA C 61.97 . . 109 13 ILE HA H 4.69 . . 110 13 ILE CB C 39.15 . . 111 13 ILE HB H 1.48 . . 112 13 ILE CG2 C 17.60 . . 113 13 ILE CG1 C 28.34 . . 114 13 ILE HG12 H 1.73 . . 115 13 ILE HG13 H 0.67 . . 116 13 ILE CD1 C 13.82 . . 117 13 ILE HD1 H 0.53 . . 118 13 ILE HG2 H 0.59 . . 119 14 TYR H H 9.32 . . 120 14 TYR N N 129.10 . . 121 14 TYR CA C 56.17 . . 122 14 TYR HA H 5.00 . . 123 14 TYR CB C 41.98 . . 124 14 TYR HB2 H 2.36 . . 125 14 TYR HB3 H 3.20 . . 126 14 TYR CD1 C 133.14 . . 127 14 TYR HD1 H 6.69 . . 128 14 TYR CE1 C 133.22 . . 129 14 TYR HE1 H 6.44 . . 130 15 LEU H H 8.95 . . 131 15 LEU N N 123.08 . . 132 15 LEU CA C 53.39 . . 133 15 LEU HA H 5.11 . . 134 15 LEU CB C 44.83 . . 135 15 LEU HB2 H 1.15 . . 136 15 LEU HB3 H 1.87 . . 137 15 LEU CG C 28.71 . . 138 15 LEU CD1 C 26.17 . . 139 15 LEU HD1 H 0.79 . . 140 15 LEU CD2 C 25.50 . . 141 15 LEU HD2 H 0.67 . . 142 15 LEU HG H 1.32 . . 143 16 ASN H H 9.45 . . 144 16 ASN N N 129.23 . . 145 16 ASN CA C 54.34 . . 146 16 ASN HA H 4.49 . . 147 16 ASN CB C 35.67 . . 148 16 ASN HB2 H 2.90 . . 149 16 ASN ND2 N 109.15 . . 150 16 ASN HD21 H 7.78 . . 151 16 ASN HD22 H 7.35 . . 152 17 ASN H H 9.30 . . 153 17 ASN N N 108.06 . . 154 17 ASN CA C 55.28 . . 155 17 ASN HA H 4.18 . . 157 17 ASN HB2 H 2.99 . . 158 17 ASN HB3 H 3.03 . . 159 17 ASN ND2 N 113.01 . . 160 17 ASN HD21 H 7.47 . . 161 17 ASN HD22 H 6.78 . . 162 18 GLY H H 8.07 . . 163 18 GLY N N 108.15 . . 164 18 GLY CA C 44.28 . . 165 18 GLY HA2 H 4.59 . . 166 18 GLY HA3 H 3.48 . . 167 19 TYR H H 8.78 . . 168 19 TYR N N 127.19 . . 169 19 TYR CA C 59.39 . . 170 19 TYR HA H 2.88 . . 171 19 TYR CB C 37.59 . . 172 19 TYR HB2 H 2.50 . . 173 19 TYR HB3 H 2.42 . . 174 19 TYR CD1 C 133.24 . . 175 19 TYR HD1 H 6.44 . . 176 19 TYR CE1 C 117.98 . . 177 19 TYR HE1 H 6.37 . . 178 20 MET H H 8.40 . . 179 20 MET N N 125.21 . . 180 20 MET CA C 54.31 . . 181 20 MET HA H 4.48 . . 182 20 MET CB C 34.71 . . 183 20 MET HB2 H 1.51 . . 184 20 MET HB3 H 1.46 . . 185 20 MET CG C 32.46 . . 186 20 MET HG2 H 2.52 . . 187 20 MET HG3 H 2.32 . . 188 20 MET CE C 18.22 . . 189 20 MET HE H 1.96 . . 190 21 ALA H H 6.53 . . 191 21 ALA N N 117.05 . . 192 21 ALA CA C 52.12 . . 193 21 ALA HA H 4.07 . . 194 21 ALA CB C 21.77 . . 195 21 ALA HB H 1.08 . . 196 22 THR H H 8.65 . . 197 22 THR N N 118.61 . . 198 22 THR CA C 62.26 . . 199 22 THR HA H 5.44 . . 200 22 THR CB C 71.14 . . 201 22 THR HB H 3.77 . . 202 22 THR CG2 C 20.17 . . 203 22 THR HG2 H 1.08 . . 204 23 ARG H H 8.81 . . 205 23 ARG N N 122.41 . . 206 23 ARG CA C 54.01 . . 207 23 ARG HA H 4.55 . . 208 23 ARG CB C 34.40 . . 209 23 ARG HB2 H 1.85 . . 210 23 ARG HB3 H 1.43 . . 211 23 ARG CG C 26.48 . . 212 23 ARG HG2 H 1.27 . . 213 23 ARG HG3 H 1.18 . . 214 23 ARG CD C 43.12 . . 215 23 ARG HD2 H 2.99 . . 216 23 ARG HD3 H 2.96 . . 217 24 ASP H H 8.36 . . 218 24 ASP N N 120.77 . . 219 24 ASP CA C 54.65 . . 220 24 ASP HA H 4.85 . . 221 24 ASP CB C 40.42 . . 222 24 ASP HB2 H 2.09 . . 223 24 ASP HB3 H 2.40 . . 224 25 VAL H H 9.06 . . 225 25 VAL N N 127.29 . . 226 25 VAL CA C 61.29 . . 227 25 VAL HA H 4.12 . . 228 25 VAL CB C 35.05 . . 229 25 VAL HB H 1.95 . . 230 25 VAL CG1 C 21.73 . . 231 25 VAL HG1 H 0.24 . . 232 25 VAL CG2 C 22.71 . . 233 25 VAL HG2 H 0.68 . . 234 26 THR H H 9.29 . . 235 26 THR N N 125.91 . . 236 26 THR CA C 63.79 . . 237 26 THR HA H 4.44 . . 238 26 THR CB C 69.53 . . 239 26 THR HB H 3.85 . . 240 26 THR CG2 C 22.06 . . 241 26 THR HG2 H 0.99 . . 242 27 PHE H H 9.46 . . 243 27 PHE N N 125.76 . . 244 27 PHE CA C 55.92 . . 245 27 PHE HA H 4.99 . . 246 27 PHE CB C 41.67 . . 247 27 PHE HB2 H 2.46 . . 248 27 PHE HB3 H 3.10 . . 249 27 PHE CD1 C 133.53 . . 250 27 PHE HD1 H 7.05 . . 251 27 PHE CE1 C 134.15 . . 252 27 PHE HE1 H 6.82 . . 253 27 PHE CZ C 117.30 . . 254 27 PHE HZ H 6.31 . . 255 28 ASN H H 8.32 . . 256 28 ASN N N 119.90 . . 257 28 ASN CA C 51.49 . . 258 28 ASN HA H 5.16 . . 259 28 ASN CB C 42.32 . . 260 28 ASN HB2 H 2.44 . . 261 28 ASN HB3 H 2.77 . . 262 28 ASN ND2 N 113.74 . . 263 28 ASN HD21 H 7.75 . . 264 28 ASN HD22 H 6.89 . . 265 29 THR H H 8.86 . . 266 29 THR N N 116.37 . . 267 29 THR CA C 64.14 . . 268 29 THR HA H 4.52 . . 270 29 THR HB H 3.98 . . 271 29 THR CG2 C 22.09 . . 272 29 THR HG2 H 1.22 . . 273 30 GLY H H 7.93 . . 274 30 GLY N N 111.17 . . 275 30 GLY CA C 45.82 . . 276 30 GLY HA2 H 3.65 . . 277 30 GLY HA3 H 4.04 . . 278 31 ASP H H 8.26 . . 279 31 ASP N N 119.32 . . 280 31 ASP CA C 54.02 . . 281 31 ASP HA H 4.53 . . 282 31 ASP CB C 40.09 . . 283 31 ASP HB2 H 2.56 . . 284 31 ASP HB3 H 2.42 . . 285 32 SER H H 7.67 . . 287 32 SER CA C 57.22 . . 288 32 SER HA H 4.68 . . 289 32 SER CB C 65.75 . . 290 32 SER HB2 H 3.62 . . 291 32 SER HB3 H 4.17 . . 292 33 GLU CA C 59.36 . . 293 33 GLU HA H 4.09 . . 294 33 GLU CB C 29.64 . . 295 33 GLU HB2 H 2.05 . . 296 33 GLU HB3 H 2.25 . . 297 33 GLU CG C 36.61 . . 298 33 GLU HG2 H 2.28 . . 299 33 GLU HG3 H 2.25 . . 300 34 GLN H H 8.06 . . 301 34 GLN N N 113.47 . . 302 34 GLN CA C 56.50 . . 303 34 GLN HA H 4.42 . . 305 34 GLN HB2 H 1.92 . . 306 34 GLN HB3 H 2.03 . . 307 34 GLN CG C 35.36 . . 308 34 GLN HG2 H 2.37 . . 309 34 GLN HG3 H 2.27 . . 310 34 GLN NE2 N 114.47 . . 311 34 GLN HE21 H 7.67 . . 312 34 GLN HE22 H 7.59 . . 313 35 GLY H H 7.83 . . 314 35 GLY N N 107.99 . . 315 35 GLY CA C 45.79 . . 316 35 GLY HA2 H 3.85 . . 317 35 GLY HA3 H 4.20 . . 318 36 ILE H H 6.74 . . 319 36 ILE N N 109.58 . . 320 36 ILE CA C 58.44 . . 321 36 ILE HA H 5.22 . . 322 36 ILE CB C 43.88 . . 323 36 ILE HB H 1.54 . . 324 36 ILE CG2 C 17.95 . . 325 36 ILE CG1 C 23.93 . . 326 36 ILE HG12 H 1.02 . . 327 36 ILE HG13 H 0.68 . . 328 36 ILE CD1 C 13.52 . . 329 36 ILE HD1 H 0.10 . . 330 36 ILE HG2 H 0.60 . . 331 37 VAL H H 9.30 . . 333 37 VAL CA C 57.54 . . 334 37 VAL HA H 4.76 . . 335 37 VAL CB C 34.64 . . 336 37 VAL HB H 2.05 . . 337 37 VAL CG1 C 21.99 . . 338 37 VAL HG1 H 0.79 . . 339 37 VAL CG2 C 18.57 . . 340 37 VAL HG2 H 0.66 . . 341 38 PRO CA C 61.65 . . 342 38 PRO HA H 3.36 . . 343 38 PRO CB C 31.90 . . 344 38 PRO HB2 H 0.97 . . 345 38 PRO HB3 H 1.10 . . 346 38 PRO CG C 26.14 . . 347 38 PRO HG2 H 1.57 . . 348 38 PRO HG3 H 1.90 . . 349 38 PRO CD C 49.60 . . 350 38 PRO HD2 H 3.58 . . 351 38 PRO HD3 H 3.69 . . 352 39 CYS H H 8.34 . . 353 39 CYS N N 122.34 . . 354 39 CYS CA C 56.90 . . 355 39 CYS HA H 4.58 . . 356 39 CYS CB C 45.48 . . 357 39 CYS HB2 H 3.32 . . 358 39 CYS HB3 H 2.57 . . 359 40 LEU H H 9.12 . . 360 40 LEU N N 130.62 . . 361 40 LEU CA C 53.06 . . 362 40 LEU HA H 4.86 . . 363 40 LEU CB C 44.15 . . 364 40 LEU HB2 H 1.60 . . 365 40 LEU HB3 H 1.04 . . 366 40 LEU CG C 27.42 . . 367 40 LEU CD1 C 26.79 . . 368 40 LEU HD1 H 0.59 . . 369 40 LEU HG H 1.20 . . 370 41 THR H H 8.16 . . 371 41 THR N N 111.57 . . 372 41 THR CA C 60.25 . . 373 41 THR HA H 4.69 . . 374 41 THR CB C 71.63 . . 375 41 THR HB H 4.70 . . 376 41 THR CG2 C 21.40 . . 377 41 THR HG2 H 0.96 . . 378 42 ARG H H 9.56 . . 379 42 ARG N N 122.19 . . 380 42 ARG CA C 60.66 . . 381 42 ARG HA H 3.63 . . 382 42 ARG CB C 29.64 . . 383 42 ARG HB2 H 1.95 . . 384 42 ARG HB3 H 1.50 . . 385 42 ARG CG C 27.45 . . 386 42 ARG HG2 H 1.49 . . 387 42 ARG HG3 H 0.86 . . 388 42 ARG CD C 43.90 . . 389 42 ARG HD2 H 3.19 . . 390 42 ARG HD3 H 2.91 . . 391 43 ALA H H 8.92 . . 392 43 ALA N N 119.62 . . 393 43 ALA CA C 54.67 . . 394 43 ALA HA H 4.04 . . 395 43 ALA CB C 18.26 . . 396 43 ALA HB H 1.28 . . 397 44 GLN H H 7.62 . . 398 44 GLN N N 118.56 . . 399 44 GLN CA C 58.79 . . 400 44 GLN HA H 3.75 . . 401 44 GLN CB C 28.06 . . 402 44 GLN HB2 H 1.58 . . 403 44 GLN HB3 H 2.23 . . 404 44 GLN CG C 34.37 . . 405 44 GLN HG2 H 2.20 . . 406 44 GLN HG3 H 2.32 . . 407 44 GLN NE2 N 109.02 . . 408 44 GLN HE21 H 6.65 . . 409 44 GLN HE22 H 7.25 . . 410 45 LEU H H 8.26 . . 411 45 LEU N N 119.91 . . 412 45 LEU CA C 58.12 . . 413 45 LEU HA H 3.80 . . 414 45 LEU CB C 41.05 . . 415 45 LEU HB2 H 1.75 . . 416 45 LEU HB3 H 1.14 . . 417 45 LEU CG C 27.12 . . 418 45 LEU CD1 C 26.17 . . 419 45 LEU HD1 H 0.58 . . 420 45 LEU CD2 C 22.69 . . 421 45 LEU HD2 H 0.58 . . 422 45 LEU HG H 1.53 . . 423 46 ALA H H 8.94 . . 424 46 ALA N N 123.49 . . 425 46 ALA CA C 54.68 . . 426 46 ALA HA H 4.55 . . 427 46 ALA CB C 17.96 . . 428 46 ALA HB H 1.44 . . 429 47 SER H H 7.99 . . 430 47 SER N N 114.62 . . 431 47 SER CA C 61.29 . . 432 47 SER HA H 4.18 . . 433 47 SER CB C 62.88 . . 434 47 SER HB2 H 3.87 . . 435 47 SER HB3 H 3.91 . . 436 48 MET H H 7.17 . . 437 48 MET N N 118.60 . . 438 48 MET CA C 56.25 . . 439 48 MET HA H 4.26 . . 441 48 MET HB2 H 1.91 . . 442 48 MET HB3 H 2.20 . . 443 48 MET CG C 32.81 . . 444 48 MET HG2 H 2.69 . . 445 48 MET HG3 H 2.20 . . 446 48 MET CE C 16.86 . . 447 48 MET HE H 1.69 . . 448 49 GLY H H 7.47 . . 449 49 GLY N N 102.99 . . 450 49 GLY CA C 44.84 . . 451 49 GLY HA2 H 4.28 . . 452 49 GLY HA3 H 3.51 . . 453 50 LEU H H 7.59 . . 454 50 LEU N N 122.50 . . 455 50 LEU CA C 56.27 . . 456 50 LEU HA H 4.34 . . 457 50 LEU CB C 42.98 . . 458 50 LEU HB2 H 1.22 . . 459 50 LEU HB3 H 0.90 . . 460 50 LEU CG C 27.46 . . 461 50 LEU CD1 C 25.51 . . 462 50 LEU HD1 H 0.76 . . 463 50 LEU CD2 C 27.72 . . 464 50 LEU HD2 H 0.58 . . 465 50 LEU HG H 1.27 . . 466 51 ASN H H 9.19 . . 467 51 ASN N N 124.48 . . 468 51 ASN CA C 51.49 . . 469 51 ASN HA H 4.75 . . 470 51 ASN CB C 36.30 . . 471 51 ASN HB2 H 2.96 . . 472 51 ASN HB3 H 2.33 . . 473 51 ASN ND2 N 110.43 . . 474 51 ASN HD21 H 6.86 . . 475 51 ASN HD22 H 7.66 . . 476 52 THR H H 8.37 . . 477 52 THR N N 118.62 . . 478 52 THR CA C 65.41 . . 479 52 THR HA H 3.62 . . 480 52 THR CB C 67.69 . . 481 52 THR HB H 4.08 . . 482 52 THR CG2 C 22.36 . . 483 52 THR HG2 H 1.12 . . 484 53 ALA H H 7.69 . . 485 53 ALA N N 121.42 . . 486 53 ALA CA C 53.68 . . 487 53 ALA HA H 4.11 . . 488 53 ALA CB C 18.26 . . 489 53 ALA HB H 1.33 . . 490 54 SER H H 7.58 . . 491 54 SER N N 111.88 . . 492 54 SER CA C 59.40 . . 493 54 SER HA H 4.28 . . 494 54 SER CB C 64.44 . . 495 54 SER HB2 H 3.82 . . 496 54 SER HB3 H 4.01 . . 497 55 VAL H H 7.00 . . 498 55 VAL N N 122.48 . . 499 55 VAL CA C 60.99 . . 500 55 VAL HA H 4.04 . . 501 55 VAL CB C 32.20 . . 502 55 VAL HB H 1.97 . . 503 55 VAL CG1 C 20.77 . . 504 55 VAL HG1 H 0.65 . . 505 55 VAL CG2 C 22.69 . . 506 55 VAL HG2 H 0.64 . . 507 56 ALA H H 8.77 . . 508 56 ALA N N 132.81 . . 509 56 ALA CA C 54.07 . . 510 56 ALA HA H 4.03 . . 512 56 ALA HB H 1.30 . . 513 57 GLY H H 8.72 . . 514 57 GLY N N 109.01 . . 515 57 GLY CA C 45.78 . . 516 57 GLY HA2 H 4.14 . . 517 57 GLY HA3 H 3.51 . . 518 58 MET H H 7.91 . . 519 58 MET N N 122.76 . . 520 58 MET CA C 59.07 . . 521 58 MET HA H 3.81 . . 522 58 MET CB C 32.51 . . 523 58 MET HB2 H 2.12 . . 524 58 MET HB3 H 1.95 . . 525 58 MET CG C 34.05 . . 526 58 MET HG2 H 2.40 . . 527 58 MET HG3 H 2.34 . . 528 58 MET CE C 17.94 . . 529 58 MET HE H 1.73 . . 530 59 ASN H H 8.71 . . 531 59 ASN N N 115.47 . . 532 59 ASN CA C 54.65 . . 533 59 ASN HA H 4.22 . . 534 59 ASN CB C 36.90 . . 535 59 ASN HB2 H 2.71 . . 536 59 ASN ND2 N 112.15 . . 537 59 ASN HD21 H 7.52 . . 538 59 ASN HD22 H 6.75 . . 539 60 LEU H H 7.01 . . 540 60 LEU N N 117.26 . . 541 60 LEU CA C 54.67 . . 542 60 LEU HA H 4.16 . . 543 60 LEU CB C 42.14 . . 544 60 LEU HB2 H 1.49 . . 545 60 LEU HB3 H 1.57 . . 546 60 LEU CG C 26.79 . . 547 60 LEU CD1 C 25.19 . . 548 60 LEU HD1 H 0.80 . . 549 60 LEU CD2 C 22.36 . . 550 60 LEU HD2 H 0.67 . . 551 60 LEU HG H 1.42 . . 552 61 LEU H H 6.76 . . 553 61 LEU N N 117.79 . . 554 61 LEU CA C 54.39 . . 555 61 LEU HA H 4.10 . . 556 61 LEU CB C 42.74 . . 557 61 LEU HB2 H 1.43 . . 558 61 LEU HB3 H 1.61 . . 559 61 LEU CG C 27.13 . . 560 61 LEU CD1 C 27.41 . . 561 61 LEU HD1 H 0.86 . . 562 61 LEU CD2 C 22.79 . . 563 61 LEU HD2 H 0.72 . . 564 61 LEU HG H 1.66 . . 565 62 ALA H H 8.46 . . 566 62 ALA N N 124.20 . . 567 62 ALA CA C 52.12 . . 568 62 ALA HA H 4.25 . . 569 62 ALA CB C 19.24 . . 570 62 ALA HB H 1.40 . . 571 63 ASP H H 8.68 . . 572 63 ASP N N 119.96 . . 573 63 ASP CA C 57.18 . . 574 63 ASP HA H 4.15 . . 575 63 ASP CB C 40.84 . . 576 63 ASP HB3 H 2.49 . . 577 64 ASP H H 8.06 . . 578 64 ASP N N 112.32 . . 579 64 ASP CA C 52.54 . . 580 64 ASP HA H 4.52 . . 581 64 ASP CB C 40.10 . . 582 64 ASP HB2 H 2.45 . . 583 64 ASP HB3 H 2.68 . . 584 65 ALA H H 7.14 . . 585 65 ALA N N 122.23 . . 586 65 ALA CA C 52.16 . . 587 65 ALA HA H 4.05 . . 588 65 ALA CB C 20.09 . . 589 65 ALA HB H 1.30 . . 590 66 CYS H H 8.35 . . 591 66 CYS N N 118.05 . . 592 66 CYS CA C 53.06 . . 593 66 CYS HA H 4.14 . . 594 66 CYS CB C 40.07 . . 595 66 CYS HB2 H 3.22 . . 596 66 CYS HB3 H 2.57 . . 597 67 VAL H H 9.03 . . 599 67 VAL CA C 60.97 . . 600 67 VAL HA H 3.82 . . 601 67 VAL CB C 32.55 . . 602 67 VAL HB H 1.84 . . 603 67 VAL CG1 C 20.15 . . 604 67 VAL HG1 H 0.50 . . 605 67 VAL CG2 C 22.34 . . 606 67 VAL HG2 H 0.84 . . 607 68 PRO CA C 61.34 . . 608 68 PRO HA H 4.82 . . 609 68 PRO CB C 27.43 . . 610 68 PRO HB2 H 1.97 . . 611 68 PRO HB3 H 1.83 . . 612 68 PRO CG C 33.56 . . 613 68 PRO HG2 H 2.24 . . 614 68 PRO HG3 H 2.48 . . 615 68 PRO CD C 50.87 . . 616 68 PRO HD2 H 3.53 . . 617 68 PRO HD3 H 3.86 . . 618 69 LEU H H 7.91 . . 619 69 LEU N N 127.34 . . 620 69 LEU CA C 59.43 . . 621 69 LEU HA H 3.42 . . 622 69 LEU CB C 43.55 . . 623 69 LEU HB2 H 1.64 . . 624 69 LEU HB3 H 1.24 . . 625 69 LEU CG C 26.19 . . 626 69 LEU CD1 C 20.14 . . 627 69 LEU HD1 H 0.50 . . 628 69 LEU CD2 C 23.03 . . 629 69 LEU HD2 H 0.58 . . 630 69 LEU HG H 0.58 . . 631 70 THR H H 7.83 . . 632 70 THR N N 102.88 . . 633 70 THR CA C 63.84 . . 634 70 THR HA H 3.96 . . 635 70 THR CB C 68.28 . . 636 70 THR HB H 4.38 . . 637 70 THR CG2 C 21.73 . . 638 70 THR HG2 H 1.12 . . 639 71 THR H H 7.16 . . 640 71 THR N N 112.05 . . 641 71 THR CA C 63.22 . . 642 71 THR HA H 4.23 . . 643 71 THR CB C 69.19 . . 644 71 THR HB H 4.04 . . 645 71 THR CG2 C 21.79 . . 646 71 THR HG2 H 1.08 . . 647 72 MET H H 7.79 . . 648 72 MET N N 118.79 . . 649 72 MET CA C 57.83 . . 650 72 MET HA H 4.11 . . 651 72 MET CB C 35.60 . . 652 72 MET HB2 H 1.65 . . 653 72 MET HB3 H 2.48 . . 654 72 MET CG C 33.76 . . 655 72 MET HG2 H 2.24 . . 656 72 MET HG3 H 2.49 . . 657 72 MET CE C 17.37 . . 658 72 MET HE H 1.86 . . 659 73 VAL H H 7.60 . . 660 73 VAL N N 118.99 . . 661 73 VAL CA C 60.60 . . 662 73 VAL HA H 3.54 . . 663 73 VAL CB C 30.27 . . 664 73 VAL HB H 1.93 . . 665 73 VAL CG1 C 22.06 . . 666 73 VAL HG1 H 0.09 . . 667 73 VAL CG2 C 20.81 . . 668 73 VAL HG2 H 0.33 . . 669 74 GLN H H 7.85 . . 670 74 GLN N N 125.91 . . 671 74 GLN CA C 58.13 . . 672 74 GLN HA H 3.75 . . 673 74 GLN CB C 28.69 . . 674 74 GLN HB2 H 1.87 . . 675 74 GLN HB3 H 1.97 . . 676 74 GLN CG C 33.74 . . 677 74 GLN HG2 H 2.22 . . 678 74 GLN HG3 H 2.25 . . 679 74 GLN NE2 N 113.05 . . 680 74 GLN HE21 H 6.77 . . 681 74 GLN HE22 H 7.55 . . 682 75 ASP H H 8.50 . . 683 75 ASP N N 116.32 . . 684 75 ASP CA C 56.22 . . 685 75 ASP HA H 4.17 . . 686 75 ASP CB C 39.47 . . 687 75 ASP HB2 H 2.78 . . 688 75 ASP HB3 H 2.98 . . 689 76 ALA H H 7.97 . . 690 76 ALA N N 122.22 . . 691 76 ALA CA C 52.41 . . 692 76 ALA HA H 4.68 . . 693 76 ALA CB C 19.85 . . 694 76 ALA HB H 1.23 . . 695 77 THR H H 8.60 . . 696 77 THR N N 108.72 . . 697 77 THR CA C 60.69 . . 698 77 THR HA H 4.69 . . 699 77 THR CB C 73.02 . . 700 77 THR HB H 4.05 . . 701 77 THR CG2 C 21.10 . . 702 77 THR HG2 H 0.98 . . 703 78 ALA H H 8.52 . . 704 78 ALA N N 121.07 . . 705 78 ALA CA C 51.47 . . 706 78 ALA HA H 5.11 . . 707 78 ALA CB C 22.06 . . 708 78 ALA HB H 1.10 . . 709 79 HIS H H 8.43 . . 710 79 HIS N N 121.06 . . 711 79 HIS CA C 56.52 . . 712 79 HIS HA H 4.59 . . 713 79 HIS CB C 34.40 . . 714 79 HIS HB2 H 2.89 . . 715 79 HIS HB3 H 2.95 . . 716 79 HIS HD1 H 9.21 . . 717 79 HIS CD2 C 120.14 . . 718 79 HIS HD2 H 6.71 . . 719 79 HIS CE1 C 139.00 . . 720 79 HIS HE1 H 7.61 . . 721 80 LEU H H 8.94 . . 722 80 LEU N N 130.38 . . 723 80 LEU CA C 53.71 . . 724 80 LEU HA H 4.55 . . 725 80 LEU CB C 42.93 . . 726 80 LEU HB2 H 1.29 . . 727 80 LEU HB3 H 0.75 . . 728 80 LEU CG C 26.82 . . 729 80 LEU CD1 C 24.28 . . 730 80 LEU HD1 H -0.76 . . 731 80 LEU CD2 C 22.37 . . 732 80 LEU HD2 H 0.15 . . 733 80 LEU HG H 0.63 . . 734 81 ASP H H 9.12 . . 735 81 ASP N N 127.93 . . 736 81 ASP CA C 52.10 . . 737 81 ASP HA H 4.64 . . 738 81 ASP CB C 41.42 . . 739 81 ASP HB2 H 2.88 . . 740 81 ASP HB3 H 2.27 . . 741 82 VAL H H 8.32 . . 742 82 VAL N N 123.35 . . 743 82 VAL CA C 65.71 . . 744 82 VAL HA H 3.41 . . 746 82 VAL HB H 1.86 . . 747 82 VAL CG1 C 21.58 . . 748 82 VAL HG1 H 0.73 . . 749 83 GLY H H 8.45 . . 750 83 GLY N N 109.45 . . 751 83 GLY CA C 47.03 . . 752 83 GLY HA2 H 3.77 . . 753 83 GLY HA3 H 3.83 . . 754 84 GLN H H 7.34 . . 755 84 GLN N N 115.46 . . 756 84 GLN CA C 54.65 . . 757 84 GLN HA H 4.29 . . 758 84 GLN CB C 29.96 . . 759 84 GLN HB2 H 1.36 . . 760 84 GLN HB3 H 2.08 . . 761 84 GLN CG C 34.71 . . 762 84 GLN HG2 H 2.27 . . 763 84 GLN HG3 H 2.04 . . 764 84 GLN NE2 N 112.01 . . 765 84 GLN HE21 H 7.49 . . 766 84 GLN HE22 H 6.58 . . 767 85 GLN H H 7.79 . . 768 85 GLN N N 118.17 . . 769 85 GLN CA C 56.86 . . 770 85 GLN HA H 3.63 . . 771 85 GLN CB C 26.51 . . 772 85 GLN HB2 H 2.29 . . 773 85 GLN HB3 H 2.24 . . 774 85 GLN CG C 34.70 . . 775 85 GLN HG2 H 2.20 . . 776 85 GLN HG3 H 2.33 . . 777 85 GLN NE2 N 111.00 . . 778 85 GLN HE21 H 7.48 . . 779 85 GLN HE22 H 6.57 . . 780 86 ARG H H 7.93 . . 781 86 ARG N N 116.47 . . 782 86 ARG CA C 54.37 . . 783 86 ARG HA H 5.36 . . 784 86 ARG CB C 35.66 . . 785 86 ARG HB2 H 1.58 . . 786 86 ARG HB3 H 1.68 . . 787 86 ARG CG C 26.78 . . 788 86 ARG HG2 H 1.59 . . 789 86 ARG HG3 H 1.40 . . 790 86 ARG CD C 43.61 . . 791 86 ARG HD2 H 2.59 . . 792 86 ARG HD3 H 2.79 . . 793 86 ARG NE N 83.91 . . 794 86 ARG HE H 7.31 . . 795 87 LEU H H 9.17 . . 796 87 LEU N N 126.21 . . 797 87 LEU CA C 53.06 . . 798 87 LEU HA H 4.93 . . 799 87 LEU CB C 45.15 . . 800 87 LEU HB2 H 1.88 . . 801 87 LEU HB3 H 1.12 . . 802 87 LEU CG C 27.75 . . 803 87 LEU CD1 C 22.40 . . 804 87 LEU HD1 H 0.84 . . 805 87 LEU CD2 C 25.30 . . 806 87 LEU HD2 H 0.76 . . 807 87 LEU HG H 1.44 . . 808 88 ASN H H 9.20 . . 809 88 ASN N N 125.03 . . 810 88 ASN CA C 52.76 . . 811 88 ASN HA H 5.27 . . 812 88 ASN CB C 40.41 . . 813 88 ASN HB2 H 2.71 . . 814 88 ASN HB3 H 2.51 . . 815 88 ASN ND2 N 113.61 . . 816 88 ASN HD21 H 7.03 . . 817 88 ASN HD22 H 7.45 . . 818 89 LEU H H 9.49 . . 819 89 LEU N N 126.67 . . 820 89 LEU CA C 52.77 . . 821 89 LEU HA H 5.27 . . 822 89 LEU CB C 45.19 . . 823 89 LEU HB2 H 1.98 . . 824 89 LEU HB3 H 1.12 . . 825 89 LEU CG C 27.12 . . 826 89 LEU CD1 C 25.86 . . 827 89 LEU HD1 H 0.56 . . 828 89 LEU CD2 C 23.66 . . 829 89 LEU HD2 H 0.70 . . 830 89 LEU HG H 1.60 . . 831 90 THR H H 8.85 . . 832 90 THR N N 118.90 . . 833 90 THR CA C 61.29 . . 834 90 THR HA H 4.98 . . 835 90 THR CB C 70.47 . . 836 90 THR HB H 4.13 . . 837 90 THR CG2 C 21.11 . . 838 90 THR HG2 H 1.02 . . 839 91 ILE H H 9.23 . . 841 91 ILE CA C 57.50 . . 842 91 ILE HA H 4.42 . . 843 91 ILE CB C 42.61 . . 844 91 ILE HB H 1.77 . . 845 91 ILE CG2 C 16.98 . . 846 91 ILE CG1 C 27.73 . . 847 91 ILE HG12 H 0.92 . . 848 91 ILE HG13 H 1.34 . . 849 91 ILE CD1 C 12.89 . . 850 91 ILE HD1 H 0.63 . . 851 91 ILE HG2 H 0.83 . . 852 92 PRO CA C 63.52 . . 853 92 PRO HA H 4.29 . . 854 92 PRO CB C 32.52 . . 855 92 PRO HB2 H 1.86 . . 856 92 PRO HB3 H 2.45 . . 857 92 PRO CG C 28.10 . . 858 92 PRO HG2 H 1.87 . . 859 92 PRO HG3 H 2.51 . . 860 92 PRO CD C 52.07 . . 861 92 PRO HD2 H 3.36 . . 862 92 PRO HD3 H 3.56 . . 863 93 GLN H H 8.47 . . 864 93 GLN N N 122.18 . . 865 93 GLN CA C 58.76 . . 866 93 GLN HA H 3.62 . . 867 93 GLN CB C 28.38 . . 868 93 GLN HB2 H 1.91 . . 869 93 GLN HB3 H 1.97 . . 870 93 GLN CG C 33.47 . . 871 93 GLN HG2 H 2.35 . . 872 93 GLN NE2 N 112.63 . . 873 93 GLN HE21 H 7.51 . . 874 93 GLN HE22 H 6.83 . . 875 94 ALA H H 8.31 . . 876 94 ALA N N 119.20 . . 877 94 ALA CA C 54.08 . . 878 94 ALA HA H 3.84 . . 879 94 ALA CB C 18.07 . . 880 94 ALA HB H 0.80 . . 881 95 PHE H H 7.54 . . 882 95 PHE N N 113.73 . . 883 95 PHE CA C 56.91 . . 884 95 PHE HA H 4.77 . . 885 95 PHE CB C 39.15 . . 886 95 PHE HB2 H 2.30 . . 887 95 PHE HB3 H 3.20 . . 888 95 PHE CD1 C 132.18 . . 889 95 PHE HD1 H 7.05 . . 890 95 PHE CE1 C 132.02 . . 891 95 PHE HE1 H 7.35 . . 892 95 PHE CZ C 130.71 . . 893 95 PHE HZ H 7.27 . . 894 96 MET H H 7.52 . . 895 96 MET N N 117.02 . . 896 96 MET CA C 52.78 . . 897 96 MET HA H 4.99 . . 898 96 MET CB C 31.00 . . 899 96 MET HB3 H 2.02 . . 900 96 MET CG C 31.25 . . 901 96 MET HG2 H 2.33 . . 902 96 MET HG3 H 2.35 . . 903 96 MET CE C 15.77 . . 904 96 MET HE H 1.83 . . 905 97 SER H H 8.79 . . 907 97 SER CA C 59.07 . . 908 97 SER HA H 4.30 . . 909 97 SER CB C 63.81 . . 910 97 SER HB3 H 3.69 . . 911 98 ASN CA C 53.69 . . 912 98 ASN HA H 4.60 . . 913 98 ASN CB C 38.82 . . 914 98 ASN HB3 H 2.66 . . 915 99 ARG H H 8.17 . . 916 99 ARG N N 121.34 . . 917 99 ARG CA C 55.90 . . 918 99 ARG HA H 4.18 . . 919 99 ARG CB C 30.91 . . 920 99 ARG HB2 H 1.62 . . 921 99 ARG HB3 H 1.74 . . 922 99 ARG CG C 26.81 . . 923 99 ARG HG2 H 1.49 . . 924 99 ARG CD C 43.89 . . 925 99 ARG HD2 H 2.91 . . 926 100 ALA H H 8.25 . . 927 100 ALA N N 125.79 . . 928 100 ALA CA C 52.77 . . 929 100 ALA HA H 4.18 . . 930 100 ALA CB C 19.19 . . 931 100 ALA HB H 1.27 . . 932 101 ARG H H 7.82 . . 935 101 ARG HA H 4.02 . . 937 101 ARG HB2 H 1.58 . . 938 101 ARG HB3 H 1.72 . . 939 101 ARG CG C 27.11 . . 940 101 ARG HG2 H 1.47 . . 941 101 ARG CD C 43.56 . . 942 101 ARG HD2 H 3.06 . . stop_ save_