data_15911 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; NMR backbone assignments of the periplasmic loop P2 of the MalF subunit of the maltose ATP binding cassette transporter ; _BMRB_accession_number 15911 _BMRB_flat_file_name bmr15911.str _Entry_type original _Submission_date 2008-08-07 _Accession_date 2008-08-07 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Jacso Tomas . . 2 Grote Mathias . . 3 Schmieder Peter . . 4 Schneider Erwin . . 5 Reif Bernd . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 157 "13C chemical shifts" 329 "15N chemical shifts" 157 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2009-05-05 update BMRB 'complete entry citation' 2008-10-02 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; The periplasmic loop P2 of the MalF subunit of the maltose ATP binding cassette transporter is sufficient to bind the maltose binding protein MalE ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 19159328 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Jacso Tomas . . 2 Grote Mathias . . 3 Daus Martin L. . 4 Schmieder Peter . . 5 Keller Sandro . . 6 Schneider Erwin . . 7 Reif Bernd . . stop_ _Journal_abbreviation Biochemistry _Journal_volume 48 _Journal_issue 10 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 2216 _Page_last 2225 _Year 2009 _Details . loop_ _Keyword 'ABC Transporter' 'Maltose Transport' 'Membrane Protein' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name MalF-P2 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label MalF-P2 $MalF-P2 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_MalF-P2 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common MalF-P2 _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 184 _Mol_residue_sequence ; MNYSSTNQLTFERAQEVLLD RSWQAGKTYNFGLYPAGDEW QLALSDGETGKNYLSDAFKF GGEQKLQLKETTAQPEGERA NLRVITQNRQALSDITAILP DGNKVMMSSLRQFSGTQPLY TLDGDGTLTNNQSGVKYRPN NQIGFYQSITADGNWGDEKL SPGYTVTTGWKNFTRVFTDE GIQK ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 92 MET 2 93 ASN 3 94 TYR 4 95 SER 5 96 SER 6 97 THR 7 98 ASN 8 99 GLN 9 100 LEU 10 101 THR 11 102 PHE 12 103 GLU 13 104 ARG 14 105 ALA 15 106 GLN 16 107 GLU 17 108 VAL 18 109 LEU 19 110 LEU 20 111 ASP 21 112 ARG 22 113 SER 23 114 TRP 24 115 GLN 25 116 ALA 26 117 GLY 27 118 LYS 28 119 THR 29 120 TYR 30 121 ASN 31 122 PHE 32 123 GLY 33 124 LEU 34 125 TYR 35 126 PRO 36 127 ALA 37 128 GLY 38 129 ASP 39 130 GLU 40 131 TRP 41 132 GLN 42 133 LEU 43 134 ALA 44 135 LEU 45 136 SER 46 137 ASP 47 138 GLY 48 139 GLU 49 140 THR 50 141 GLY 51 142 LYS 52 143 ASN 53 144 TYR 54 145 LEU 55 146 SER 56 147 ASP 57 148 ALA 58 149 PHE 59 150 LYS 60 151 PHE 61 152 GLY 62 153 GLY 63 154 GLU 64 155 GLN 65 156 LYS 66 157 LEU 67 158 GLN 68 159 LEU 69 160 LYS 70 161 GLU 71 162 THR 72 163 THR 73 164 ALA 74 165 GLN 75 166 PRO 76 167 GLU 77 168 GLY 78 169 GLU 79 170 ARG 80 171 ALA 81 172 ASN 82 173 LEU 83 174 ARG 84 175 VAL 85 176 ILE 86 177 THR 87 178 GLN 88 179 ASN 89 180 ARG 90 181 GLN 91 182 ALA 92 183 LEU 93 184 SER 94 185 ASP 95 186 ILE 96 187 THR 97 188 ALA 98 189 ILE 99 190 LEU 100 191 PRO 101 192 ASP 102 193 GLY 103 194 ASN 104 195 LYS 105 196 VAL 106 197 MET 107 198 MET 108 199 SER 109 200 SER 110 201 LEU 111 202 ARG 112 203 GLN 113 204 PHE 114 205 SER 115 206 GLY 116 207 THR 117 208 GLN 118 209 PRO 119 210 LEU 120 211 TYR 121 212 THR 122 213 LEU 123 214 ASP 124 215 GLY 125 216 ASP 126 217 GLY 127 218 THR 128 219 LEU 129 220 THR 130 221 ASN 131 222 ASN 132 223 GLN 133 224 SER 134 225 GLY 135 226 VAL 136 227 LYS 137 228 TYR 138 229 ARG 139 230 PRO 140 231 ASN 141 232 ASN 142 233 GLN 143 234 ILE 144 235 GLY 145 236 PHE 146 237 TYR 147 238 GLN 148 239 SER 149 240 ILE 150 241 THR 151 242 ALA 152 243 ASP 153 244 GLY 154 245 ASN 155 246 TRP 156 247 GLY 157 248 ASP 158 249 GLU 159 250 LYS 160 251 LEU 161 252 SER 162 253 PRO 163 254 GLY 164 255 TYR 165 256 THR 166 257 VAL 167 258 THR 168 259 THR 169 260 GLY 170 261 TRP 171 262 LYS 172 263 ASN 173 264 PHE 174 265 THR 175 266 ARG 176 267 VAL 177 268 PHE 178 269 THR 179 270 ASP 180 271 GLU 181 272 GLY 182 273 ILE 183 274 GLN 184 275 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-09-16 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 2R6G "The Crystal Structure Of The E. Coli Maltose Transporter" 99.46 514 100.00 100.00 1.72e-126 PDB 3FH6 "Crystal Structure Of The Resting State Maltose Transporter From E. Coli" 99.46 480 100.00 100.00 5.55e-127 PDB 3PUV "Crystal Structure Of An Outward-Facing Mbp-Maltose Transporter Complex Bound To Adp-Vo4" 99.46 514 100.00 100.00 1.72e-126 PDB 3PUW "Crystal Structure Of An Outward-Facing Mbp-Maltose Transporter Complex Bound To Adp-Alf4" 99.46 514 100.00 100.00 1.72e-126 PDB 3PUX "Crystal Structure Of An Outward-Facing Mbp-Maltose Transporter Complex Bound To Adp-Bef3" 99.46 514 100.00 100.00 1.72e-126 PDB 3PUY "Crystal Structure Of An Outward-Facing Mbp-Maltose Transporter Complex Bound To Amp-Pnp After Crystal Soaking Of The Pretranslo" 99.46 514 100.00 100.00 1.72e-126 PDB 3PUZ "Crystal Structure Of A Pre-Translocation State Mbp-Maltose Transporter Complex Bound To Amp-Pnp" 99.46 514 100.00 100.00 1.72e-126 PDB 3PV0 "Crystal Structure Of A Pre-Translocation State Mbp-Maltose Transporter Complex Without Nucleotide" 99.46 514 100.00 100.00 1.72e-126 PDB 3RLF "Crystal Structure Of The Maltose-Binding ProteinMALTOSE TRANSPORTER Complex In An Outward-Facing Conformation Bound To Mgamppnp" 99.46 514 100.00 100.00 1.72e-126 PDB 4JBW "Crystal Structure Of E. Coli Maltose Transporter Malfgk2 In Complex With Its Regulatory Protein Eiiaglc" 99.46 514 100.00 100.00 1.72e-126 PDB 4KHZ "Crystal Structure Of The Maltose-binding Protein/maltose Transporter Complex In An Pre-translocation Conformation Bound To Malt" 99.46 514 100.00 100.00 1.72e-126 PDB 4KI0 "Crystal Structure Of The Maltose-binding Protein/maltose Transporter Complex In An Outward-facing Conformation Bound To Maltohe" 99.46 514 100.00 100.00 1.72e-126 DBJ BAB38439 "transport system permease protein MalF [Escherichia coli O157:H7 str. Sakai]" 99.46 514 99.45 99.45 2.59e-125 DBJ BAE78035 "maltose transporter subunit [Escherichia coli str. K12 substr. W3110]" 99.46 514 100.00 100.00 1.72e-126 DBJ BAG79848 "maltose ABC transporter permease component [Escherichia coli SE11]" 99.46 514 99.45 100.00 9.96e-126 DBJ BAI57430 "maltose ABC transporter permease component [Escherichia coli SE15]" 99.46 514 98.36 99.45 1.76e-124 DBJ BAJ45745 "maltose transport system permease protein malF [Escherichia coli DH1]" 99.46 514 100.00 100.00 1.72e-126 EMBL CAP78493 "Maltose transport system permease protein malF [Escherichia coli LF82]" 99.46 514 97.81 98.36 6.07e-124 EMBL CAQ34382 "malF, subunit of maltose ABC transporter [Escherichia coli BL21(DE3)]" 99.46 514 100.00 100.00 1.72e-126 EMBL CAR01011 "maltose transporter subunit ; membrane component of ABC superfamily [Escherichia coli IAI1]" 99.46 514 100.00 100.00 1.72e-126 EMBL CAR05668 "maltose transporter subunit ; membrane component of ABC superfamily [Escherichia coli S88]" 99.46 514 98.91 99.45 2.67e-125 EMBL CAR10710 "maltose transporter subunit ; membrane component of ABC superfamily [Escherichia coli ED1a]" 99.46 514 97.27 98.36 3.51e-123 GB AAB59055 "cytoplasmic maltose-binding protein [Escherichia coli]" 99.46 514 100.00 100.00 1.72e-126 GB AAC43127 "maltose transport inner membrane protein [Escherichia coli str. K-12 substr. MG1655]" 99.46 514 100.00 100.00 1.72e-126 GB AAC77003 "maltose transporter subunit [Escherichia coli str. K-12 substr. MG1655]" 99.46 514 100.00 100.00 1.72e-126 GB AAG59232 "part of maltose permease, periplasmic [Escherichia coli O157:H7 str. EDL933]" 99.46 514 98.91 98.91 5.33e-124 GB AAN45593 "part of maltose permease [Shigella flexneri 2a str. 301]" 99.46 514 100.00 100.00 1.38e-126 REF NP_313043 "maltose transporter membrane protein [Escherichia coli O157:H7 str. Sakai]" 99.46 514 99.45 99.45 2.59e-125 REF NP_418457 "maltose transporter subunit [Escherichia coli str. K-12 substr. MG1655]" 99.46 514 100.00 100.00 1.72e-126 REF NP_709886 "maltose transporter membrane protein [Shigella flexneri 2a str. 301]" 99.46 514 100.00 100.00 1.38e-126 REF WP_001295280 "maltose ABC transporter permease [Escherichia coli]" 99.46 514 100.00 100.00 1.51e-126 REF WP_001296633 "MULTISPECIES: maltose transporter membrane protein [Enterobacteriaceae]" 99.46 514 98.91 99.45 4.50e-125 SP P02916 "RecName: Full=Maltose transport system permease protein MalF" 99.46 514 100.00 100.00 1.72e-126 SP Q7A937 "RecName: Full=Maltose transport system permease protein MalF" 99.46 514 99.45 99.45 2.59e-125 SP Q83P81 "RecName: Full=Maltose transport system permease protein MalF" 99.46 514 100.00 100.00 1.38e-126 SP Q8FB38 "RecName: Full=Maltose transport system permease protein MalF" 99.46 519 97.81 98.36 7.60e-124 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $MalF-P2 'E. coli' 562 Bacteria . 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 $MalF-P2 'recombinant technology' . Escherichia coli . pET-15 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $MalF-P2 1.0 mM '[U-100% 13C; U-100% 15N; 80% 2H]' H2O 90 % 'natural abundance' D2O 10 % '[U-100% 2H]' phosphate 20 mM 'natural abundance' NaCl 100 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version . loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection processing stop_ _Details . save_ save_CCPNMR _Saveframe_category software _Name CcpNMR _Version . loop_ _Vendor _Address _Electronic_address CCPN . . stop_ loop_ _Task 'chemical shift assignment' 'data analysis' stop_ _Details ; Vranken, W. F., Boucher, W., Stevens, T. J., Pajon, R. F. A., Llinas, M., L. Ulrich, E., Markley, J. L., Ionides, J. & Laue, E. D. (2005). The CCPN Data Model for NMR Spectroscopy: Development of a Software Pipeline. Proteins 59, 687-696. ; save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_3D_HNCA_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HNCACB_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HN(COCA)CB_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(COCA)CB' _Sample_label $sample_1 save_ save_2D_1H-15N_HSQC_4 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_2D_1H-13C_HSQC_5 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details ; 20mM phosphate 100mM NaCl ; loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 100 2 mM pH 7.4 0.2 pH pressure 1 . atm temperature 300 1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details '13C chemical shifts determined with fully deuterated protein' 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 C 13 'methyl protons' ppm 0.00 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 . indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 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) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '3D HNCA' '3D HNCACB' '3D HN(COCA)CB' '2D 1H-15N HSQC' '2D 1H-13C HSQC' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name MalF-P2 _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 94 3 TYR CA C 57.399 0.000 1 2 94 3 TYR CB C 37.862 0.000 1 3 95 4 SER H H 7.781 0.003 1 4 95 4 SER CA C 59.561 0.000 1 5 95 4 SER CB C 64.269 0.000 1 6 95 4 SER N N 122.936 0.013 1 7 99 8 GLN CA C 55.422 0.003 1 8 99 8 GLN CB C 29.715 0.021 1 9 100 9 LEU H H 8.195 0.010 1 10 100 9 LEU CA C 54.144 0.024 1 11 100 9 LEU CB C 42.558 0.020 1 12 100 9 LEU N N 123.037 0.033 1 13 101 10 THR H H 7.470 0.002 1 14 101 10 THR CA C 60.648 0.032 1 15 101 10 THR CB C 70.429 0.007 1 16 101 10 THR N N 109.802 0.040 1 17 102 11 PHE H H 9.061 0.003 1 18 102 11 PHE CA C 60.937 0.065 1 19 102 11 PHE CB C 38.217 0.009 1 20 102 11 PHE N N 122.893 0.016 1 21 103 12 GLU H H 8.865 0.006 1 22 103 12 GLU CA C 59.970 0.056 1 23 103 12 GLU CB C 27.663 0.020 1 24 103 12 GLU N N 116.370 0.026 1 25 104 13 ARG H H 7.431 0.005 1 26 104 13 ARG CA C 57.138 0.059 1 27 104 13 ARG CB C 28.793 0.002 1 28 104 13 ARG N N 119.789 0.041 1 29 105 14 ALA H H 8.412 0.003 1 30 105 14 ALA CA C 55.249 0.027 1 31 105 14 ALA CB C 16.515 0.005 1 32 105 14 ALA N N 123.883 0.023 1 33 106 15 GLN H H 8.042 0.003 1 34 106 15 GLN CA C 59.366 0.013 1 35 106 15 GLN CB C 28.827 0.005 1 36 106 15 GLN N N 115.598 0.026 1 37 107 16 GLU H H 7.409 0.004 1 38 107 16 GLU CA C 59.192 0.013 1 39 107 16 GLU CB C 28.992 0.053 1 40 107 16 GLU N N 118.441 0.017 1 41 108 17 VAL H H 7.763 0.003 1 42 108 17 VAL CA C 65.927 0.000 1 43 108 17 VAL CB C 30.526 0.000 1 44 108 17 VAL N N 120.120 0.022 1 45 111 20 ASP CA C 57.381 0.031 1 46 111 20 ASP CB C 40.719 0.001 1 47 112 21 ARG H H 8.225 0.003 1 48 112 21 ARG CA C 56.950 0.002 1 49 112 21 ARG CB C 29.504 0.026 1 50 112 21 ARG N N 121.887 0.006 1 51 113 22 SER H H 8.708 0.003 1 52 113 22 SER CA C 57.595 0.116 1 53 113 22 SER CB C 66.747 0.014 1 54 113 22 SER N N 119.019 0.023 1 55 114 23 TRP H H 9.136 0.004 1 56 114 23 TRP CA C 54.917 0.043 1 57 114 23 TRP CB C 29.884 0.053 1 58 114 23 TRP N N 120.233 0.023 1 59 115 24 GLN H H 8.451 0.003 1 60 115 24 GLN CA C 55.693 0.119 1 61 115 24 GLN CB C 27.497 0.012 1 62 115 24 GLN N N 121.329 0.062 1 63 116 25 ALA H H 7.394 0.005 1 64 116 25 ALA CA C 51.316 0.032 1 65 116 25 ALA CB C 19.204 0.020 1 66 116 25 ALA N N 127.058 0.013 1 67 117 26 GLY H H 7.959 0.003 1 68 117 26 GLY CA C 44.200 0.043 1 69 117 26 GLY N N 107.303 0.020 1 70 118 27 LYS H H 8.104 0.004 1 71 118 27 LYS CA C 56.392 0.001 1 72 118 27 LYS CB C 32.220 0.054 1 73 118 27 LYS N N 123.349 0.016 1 74 119 28 THR H H 7.771 0.003 1 75 119 28 THR CA C 60.003 0.042 1 76 119 28 THR CB C 71.269 0.027 1 77 119 28 THR N N 113.334 0.006 1 78 120 29 TYR H H 9.154 0.002 1 79 120 29 TYR CA C 56.189 0.051 1 80 120 29 TYR CB C 41.263 0.017 1 81 120 29 TYR N N 120.605 0.023 1 82 121 30 ASN H H 8.561 0.001 1 83 121 30 ASN CA C 53.480 0.000 1 84 121 30 ASN CB C 38.473 0.000 1 85 121 30 ASN N N 123.850 0.031 1 86 122 31 PHE CA C 54.505 0.059 1 87 122 31 PHE CB C 44.113 0.005 1 88 123 32 GLY H H 9.074 0.002 1 89 123 32 GLY CA C 43.482 0.058 1 90 123 32 GLY N N 109.968 0.036 1 91 124 33 LEU H H 8.622 0.005 1 92 124 33 LEU CA C 52.771 0.037 1 93 124 33 LEU CB C 44.690 0.063 1 94 124 33 LEU N N 124.614 0.024 1 95 125 34 TYR H H 9.398 0.002 1 96 125 34 TYR CA C 54.909 0.000 1 97 125 34 TYR CB C 39.743 0.000 1 98 125 34 TYR N N 123.664 0.012 1 99 126 35 PRO CA C 62.722 0.006 1 100 126 35 PRO CB C 31.190 0.034 1 101 127 36 ALA H H 7.883 0.004 1 102 127 36 ALA CA C 49.803 0.039 1 103 127 36 ALA CB C 17.251 0.023 1 104 127 36 ALA N N 129.042 0.026 1 105 128 37 GLY H H 8.533 0.002 1 106 128 37 GLY CA C 46.442 0.030 1 107 128 37 GLY N N 115.787 0.008 1 108 129 38 ASP H H 8.756 0.003 1 109 129 38 ASP CA C 53.993 0.019 1 110 129 38 ASP CB C 39.899 0.004 1 111 129 38 ASP N N 128.872 0.035 1 112 130 39 GLU H H 7.347 0.003 1 113 130 39 GLU CA C 54.246 0.072 1 114 130 39 GLU CB C 31.105 0.018 1 115 130 39 GLU N N 120.896 0.010 1 116 131 40 TRP H H 8.318 0.004 1 117 131 40 TRP CA C 55.167 0.179 1 118 131 40 TRP CB C 32.995 0.103 1 119 131 40 TRP N N 120.769 0.074 1 120 132 41 GLN H H 9.210 0.002 1 121 132 41 GLN CA C 55.339 0.050 1 122 132 41 GLN CB C 33.148 0.054 1 123 132 41 GLN N N 115.314 0.015 1 124 133 42 LEU H H 8.928 0.002 1 125 133 42 LEU CA C 53.573 0.060 1 126 133 42 LEU CB C 44.397 0.054 1 127 133 42 LEU N N 125.631 0.016 1 128 134 43 ALA H H 9.135 0.003 1 129 134 43 ALA CA C 49.644 0.033 1 130 134 43 ALA CB C 21.668 0.029 1 131 134 43 ALA N N 128.632 0.057 1 132 135 44 LEU H H 8.817 0.003 1 133 135 44 LEU CA C 53.226 0.040 1 134 135 44 LEU CB C 45.789 0.012 1 135 135 44 LEU N N 122.421 0.007 1 136 136 45 SER H H 8.864 0.005 1 137 136 45 SER CA C 56.463 0.050 1 138 136 45 SER CB C 64.845 0.016 1 139 136 45 SER N N 116.147 0.008 1 140 137 46 ASP H H 8.811 0.003 1 141 137 46 ASP CA C 52.162 0.051 1 142 137 46 ASP CB C 42.281 0.011 1 143 137 46 ASP N N 125.593 0.021 1 144 138 47 GLY H H 8.968 0.002 1 145 138 47 GLY CA C 46.023 0.040 1 146 138 47 GLY N N 115.822 0.019 1 147 139 48 GLU H H 8.329 0.002 1 148 139 48 GLU CA C 57.924 0.036 1 149 139 48 GLU CB C 29.512 0.019 1 150 139 48 GLU N N 119.870 0.011 1 151 140 49 THR H H 7.243 0.003 1 152 140 49 THR CA C 61.034 0.016 1 153 140 49 THR CB C 70.776 0.018 1 154 140 49 THR N N 105.804 0.015 1 155 141 50 GLY H H 8.192 0.004 1 156 141 50 GLY CA C 45.226 0.030 1 157 141 50 GLY N N 111.934 0.010 1 158 142 51 LYS H H 7.421 0.003 1 159 142 51 LYS CA C 56.440 0.042 1 160 142 51 LYS CB C 33.562 0.029 1 161 142 51 LYS N N 119.843 0.035 1 162 143 52 ASN H H 8.061 0.007 1 163 143 52 ASN CA C 51.803 0.028 1 164 143 52 ASN CB C 41.906 0.016 1 165 143 52 ASN N N 118.976 0.033 1 166 144 53 TYR H H 8.902 0.002 1 167 144 53 TYR CA C 55.502 0.017 1 168 144 53 TYR CB C 42.370 0.082 1 169 144 53 TYR N N 117.290 0.015 1 170 145 54 LEU H H 9.288 0.002 1 171 145 54 LEU CA C 53.434 0.106 1 172 145 54 LEU CB C 47.275 0.022 1 173 145 54 LEU N N 125.471 0.017 1 174 146 55 SER H H 9.003 0.002 1 175 146 55 SER CA C 57.803 0.031 1 176 146 55 SER CB C 65.672 0.015 1 177 146 55 SER N N 124.057 0.014 1 178 147 56 ASP H H 8.892 0.002 1 179 147 56 ASP CA C 53.954 0.036 1 180 147 56 ASP CB C 40.952 0.018 1 181 147 56 ASP N N 119.254 0.013 1 182 148 57 ALA H H 8.563 0.002 1 183 148 57 ALA CA C 52.089 0.026 1 184 148 57 ALA CB C 17.660 0.006 1 185 148 57 ALA N N 124.924 0.017 1 186 149 58 PHE H H 9.421 0.002 1 187 149 58 PHE CA C 55.675 0.043 1 188 149 58 PHE CB C 41.397 0.057 1 189 149 58 PHE N N 121.433 0.004 1 190 150 59 LYS H H 8.587 0.002 1 191 150 59 LYS CA C 53.610 0.023 1 192 150 59 LYS CB C 34.609 0.005 1 193 150 59 LYS N N 117.856 0.012 1 194 151 60 PHE H H 8.541 0.002 1 195 151 60 PHE CA C 58.215 0.054 1 196 151 60 PHE CB C 38.064 0.020 1 197 151 60 PHE N N 122.107 0.075 1 198 152 61 GLY H H 8.551 0.003 1 199 152 61 GLY CA C 46.154 0.045 1 200 152 61 GLY N N 112.402 0.025 1 201 153 62 GLY H H 8.815 0.004 1 202 153 62 GLY CA C 43.673 0.029 1 203 153 62 GLY N N 117.112 0.022 1 204 154 63 GLU H H 8.367 0.001 1 205 154 63 GLU CA C 56.582 0.044 1 206 154 63 GLU CB C 28.821 0.019 1 207 154 63 GLU N N 121.027 0.027 1 208 155 64 GLN H H 7.678 0.004 1 209 155 64 GLN CA C 54.641 0.041 1 210 155 64 GLN CB C 31.804 0.038 1 211 155 64 GLN N N 120.956 0.008 1 212 156 65 LYS H H 8.526 0.002 1 213 156 65 LYS CA C 54.217 0.081 1 214 156 65 LYS CB C 32.508 0.124 1 215 156 65 LYS N N 122.991 0.028 1 216 157 66 LEU H H 8.503 0.004 1 217 157 66 LEU CA C 52.348 0.032 1 218 157 66 LEU CB C 43.539 0.008 1 219 157 66 LEU N N 124.517 0.016 1 220 158 67 GLN H H 8.711 0.002 1 221 158 67 GLN CA C 55.174 0.021 1 222 158 67 GLN CB C 27.923 0.046 1 223 158 67 GLN N N 124.159 0.022 1 224 159 68 LEU H H 8.838 0.001 1 225 159 68 LEU CA C 53.585 0.028 1 226 159 68 LEU CB C 42.491 0.027 1 227 159 68 LEU N N 126.757 0.064 1 228 160 69 LYS H H 8.210 0.002 1 229 160 69 LYS CA C 54.045 0.105 1 230 160 69 LYS CB C 34.010 0.011 1 231 160 69 LYS N N 119.940 0.026 1 232 161 70 GLU H H 9.021 0.003 1 233 161 70 GLU CA C 56.515 0.039 1 234 161 70 GLU CB C 29.285 0.015 1 235 161 70 GLU N N 124.897 0.028 1 236 162 71 THR H H 8.267 0.003 1 237 162 71 THR CA C 59.281 0.000 1 238 162 71 THR CB C 69.780 0.000 1 239 162 71 THR N N 120.131 0.021 1 240 163 72 THR CA C 62.248 0.010 1 241 163 72 THR CB C 68.574 0.010 1 242 164 73 ALA H H 7.883 0.003 1 243 164 73 ALA CA C 50.893 0.035 1 244 164 73 ALA CB C 19.944 0.009 1 245 164 73 ALA N N 125.360 0.023 1 246 165 74 GLN H H 8.262 0.002 1 247 165 74 GLN CA C 53.257 0.000 1 248 165 74 GLN CB C 27.405 0.000 1 249 165 74 GLN N N 121.117 0.032 1 250 166 75 PRO CA C 62.247 0.026 1 251 166 75 PRO CB C 30.478 0.001 1 252 167 76 GLU H H 8.220 0.003 1 253 167 76 GLU CA C 55.928 0.041 1 254 167 76 GLU CB C 29.984 0.060 1 255 167 76 GLU N N 121.122 0.028 1 256 168 77 GLY H H 8.066 0.004 1 257 168 77 GLY CA C 43.727 0.020 1 258 168 77 GLY N N 108.633 0.018 1 259 169 78 GLU H H 8.257 0.002 1 260 169 78 GLU CA C 55.257 0.021 1 261 169 78 GLU CB C 29.981 0.017 1 262 169 78 GLU N N 120.471 0.015 1 263 170 79 ARG H H 8.179 0.006 1 264 170 79 ARG CA C 55.106 0.015 1 265 170 79 ARG CB C 29.592 0.062 1 266 170 79 ARG N N 124.787 0.036 1 267 171 80 ALA H H 8.905 0.008 1 268 171 80 ALA CA C 51.870 0.103 1 269 171 80 ALA CB C 18.558 0.017 1 270 171 80 ALA N N 125.544 0.050 1 271 172 81 ASN H H 8.255 0.001 1 272 172 81 ASN CA C 52.900 0.074 1 273 172 81 ASN CB C 38.598 0.064 1 274 172 81 ASN N N 120.067 0.004 1 275 173 82 LEU H H 7.540 0.003 1 276 173 82 LEU CA C 58.718 0.000 1 277 173 82 LEU CB C 38.490 0.000 1 278 173 82 LEU N N 125.796 0.041 1 279 175 84 VAL CA C 65.838 0.010 1 280 175 84 VAL CB C 30.843 0.033 1 281 176 85 ILE H H 7.576 0.003 1 282 176 85 ILE CA C 64.209 0.012 1 283 176 85 ILE CB C 36.019 0.016 1 284 176 85 ILE N N 120.935 0.020 1 285 177 86 THR H H 8.239 0.005 1 286 177 86 THR CA C 66.685 0.020 1 287 177 86 THR CB C 68.096 0.005 1 288 177 86 THR N N 112.964 0.018 1 289 178 87 GLN H H 8.141 0.003 1 290 178 87 GLN CA C 58.031 0.031 1 291 178 87 GLN CB C 27.807 0.047 1 292 178 87 GLN N N 121.726 0.015 1 293 179 88 ASN H H 7.037 0.005 1 294 179 88 ASN CA C 52.160 0.035 1 295 179 88 ASN CB C 38.661 0.029 1 296 179 88 ASN N N 115.293 0.014 1 297 180 89 ARG H H 6.921 0.007 1 298 180 89 ARG CA C 60.297 0.000 1 299 180 89 ARG CB C 29.154 0.000 1 300 180 89 ARG N N 121.325 0.024 1 301 181 90 GLN CA C 58.549 0.033 1 302 181 90 GLN CB C 26.630 0.015 1 303 182 91 ALA H H 7.845 0.003 1 304 182 91 ALA CA C 54.148 0.023 1 305 182 91 ALA CB C 17.745 0.006 1 306 182 91 ALA N N 122.194 0.028 1 307 183 92 LEU H H 8.001 0.005 1 308 183 92 LEU CA C 56.929 0.021 1 309 183 92 LEU CB C 41.552 0.024 1 310 183 92 LEU N N 118.716 0.029 1 311 184 93 SER H H 8.150 0.002 1 312 184 93 SER CA C 60.755 0.021 1 313 184 93 SER CB C 62.339 0.008 1 314 184 93 SER N N 117.204 0.013 1 315 185 94 ASP H H 7.035 0.004 1 316 185 94 ASP CA C 54.104 0.020 1 317 185 94 ASP CB C 40.890 0.015 1 318 185 94 ASP N N 120.270 0.017 1 319 186 95 ILE H H 7.118 0.004 1 320 186 95 ILE CA C 60.667 0.021 1 321 186 95 ILE CB C 38.256 0.011 1 322 186 95 ILE N N 121.966 0.017 1 323 187 96 THR H H 8.630 0.002 1 324 187 96 THR CA C 62.389 0.014 1 325 187 96 THR CB C 69.127 0.004 1 326 187 96 THR N N 124.643 0.017 1 327 188 97 ALA H H 8.736 0.006 1 328 188 97 ALA CA C 49.096 0.046 1 329 188 97 ALA CB C 18.765 0.036 1 330 188 97 ALA N N 130.349 0.036 1 331 189 98 ILE H H 8.551 0.002 1 332 189 98 ILE CA C 59.041 0.007 1 333 189 98 ILE CB C 37.729 0.023 1 334 189 98 ILE N N 122.451 0.051 1 335 190 99 LEU H H 8.585 0.002 1 336 190 99 LEU CA C 53.565 0.000 1 337 190 99 LEU CB C 38.559 0.000 1 338 190 99 LEU N N 127.645 0.057 1 339 191 100 PRO CA C 65.137 0.001 1 340 191 100 PRO CB C 30.739 0.014 1 341 192 101 ASP H H 7.304 0.006 1 342 192 101 ASP CA C 52.980 0.068 1 343 192 101 ASP CB C 39.327 0.007 1 344 192 101 ASP N N 113.755 0.014 1 345 193 102 GLY H H 8.262 0.003 1 346 193 102 GLY CA C 44.276 0.038 1 347 193 102 GLY N N 109.448 0.018 1 348 194 103 ASN H H 8.027 0.004 1 349 194 103 ASN CA C 54.175 0.033 1 350 194 103 ASN CB C 38.390 0.028 1 351 194 103 ASN N N 120.747 0.025 1 352 195 104 LYS H H 8.317 0.004 1 353 195 104 LYS CA C 55.044 0.089 1 354 195 104 LYS CB C 33.251 0.079 1 355 195 104 LYS N N 121.246 0.057 1 356 196 105 VAL H H 9.195 0.002 1 357 196 105 VAL CA C 58.795 0.006 1 358 196 105 VAL CB C 34.633 0.036 1 359 196 105 VAL N N 118.384 0.063 1 360 197 106 MET H H 8.347 0.002 1 361 197 106 MET CA C 54.316 0.052 1 362 197 106 MET CB C 37.351 0.012 1 363 197 106 MET N N 118.647 0.016 1 364 198 107 MET H H 9.118 0.004 1 365 198 107 MET CA C 57.738 0.016 1 366 198 107 MET CB C 32.131 0.007 1 367 198 107 MET N N 125.405 0.019 1 368 199 108 SER H H 9.052 0.005 1 369 199 108 SER CA C 57.514 0.033 1 370 199 108 SER CB C 64.329 0.017 1 371 199 108 SER N N 122.131 0.024 1 372 200 109 SER H H 8.552 0.002 1 373 200 109 SER CA C 56.712 0.030 1 374 200 109 SER CB C 64.688 0.016 1 375 200 109 SER N N 120.009 0.021 1 376 201 110 LEU H H 8.141 0.003 1 377 201 110 LEU CA C 56.622 0.059 1 378 201 110 LEU CB C 40.433 0.038 1 379 201 110 LEU N N 113.947 0.043 1 380 202 111 ARG H H 7.792 0.004 1 381 202 111 ARG CA C 54.821 0.054 1 382 202 111 ARG CB C 32.857 0.018 1 383 202 111 ARG N N 110.839 0.036 1 384 203 112 GLN H H 7.757 0.005 1 385 203 112 GLN CA C 55.326 0.055 1 386 203 112 GLN CB C 32.845 0.006 1 387 203 112 GLN N N 118.390 0.013 1 388 204 113 PHE H H 9.432 0.002 1 389 204 113 PHE CA C 55.679 0.018 1 390 204 113 PHE CB C 42.206 0.016 1 391 204 113 PHE N N 122.408 0.025 1 392 205 114 SER H H 9.445 0.003 1 393 205 114 SER CA C 56.799 0.047 1 394 205 114 SER CB C 66.009 0.011 1 395 205 114 SER N N 113.313 0.043 1 396 206 115 GLY H H 8.897 0.000 1 397 206 115 GLY CA C 45.376 0.067 1 398 206 115 GLY N N 111.032 0.000 1 399 207 116 THR H H 8.080 0.003 1 400 207 116 THR CA C 59.682 0.053 1 401 207 116 THR CB C 71.914 0.011 1 402 207 116 THR N N 111.627 0.023 1 403 208 117 GLN H H 8.485 0.003 1 404 208 117 GLN CA C 52.421 0.000 1 405 208 117 GLN CB C 30.003 0.000 1 406 208 117 GLN N N 120.698 0.062 1 407 209 118 PRO CA C 62.824 0.001 1 408 209 118 PRO CB C 31.299 0.026 1 409 210 119 LEU H H 8.306 0.003 1 410 210 119 LEU CA C 56.298 0.115 1 411 210 119 LEU CB C 42.151 0.008 1 412 210 119 LEU N N 127.832 0.019 1 413 211 120 TYR H H 8.929 0.003 1 414 211 120 TYR CA C 55.336 0.026 1 415 211 120 TYR CB C 41.939 0.013 1 416 211 120 TYR N N 114.993 0.013 1 417 212 121 THR H H 8.566 0.002 1 418 212 121 THR CA C 61.667 0.017 1 419 212 121 THR CB C 70.905 0.009 1 420 212 121 THR N N 115.854 0.012 1 421 213 122 LEU H H 8.935 0.001 1 422 213 122 LEU CA C 53.553 0.021 1 423 213 122 LEU CB C 43.321 0.004 1 424 213 122 LEU N N 130.976 0.021 1 425 214 123 ASP H H 8.721 0.002 1 426 214 123 ASP CA C 52.558 0.076 1 427 214 123 ASP CB C 42.508 0.050 1 428 214 123 ASP N N 128.389 0.043 1 429 215 124 GLY H H 8.765 0.003 1 430 215 124 GLY CA C 46.423 0.035 1 431 215 124 GLY N N 109.355 0.019 1 432 216 125 ASP H H 8.176 0.004 1 433 216 125 ASP CA C 53.030 0.042 1 434 216 125 ASP CB C 39.794 0.026 1 435 216 125 ASP N N 118.715 0.034 1 436 217 126 GLY H H 8.098 0.005 1 437 217 126 GLY CA C 44.641 0.083 1 438 217 126 GLY N N 109.243 0.028 1 439 218 127 THR H H 8.281 0.002 1 440 218 127 THR CA C 64.164 0.008 1 441 218 127 THR CB C 68.357 0.043 1 442 218 127 THR N N 120.487 0.010 1 443 219 128 LEU H H 9.235 0.002 1 444 219 128 LEU CA C 52.684 0.046 1 445 219 128 LEU CB C 44.179 0.014 1 446 219 128 LEU N N 129.480 0.034 1 447 220 129 THR H H 8.969 0.002 1 448 220 129 THR CA C 61.880 0.040 1 449 220 129 THR CB C 70.099 0.006 1 450 220 129 THR N N 120.528 0.007 1 451 221 130 ASN H H 9.274 0.002 1 452 221 130 ASN CA C 52.815 0.094 1 453 221 130 ASN CB C 38.806 0.016 1 454 221 130 ASN N N 125.896 0.036 1 455 222 131 ASN H H 9.510 0.002 1 456 222 131 ASN CA C 54.778 0.033 1 457 222 131 ASN CB C 38.589 0.008 1 458 222 131 ASN N N 127.757 0.020 1 459 223 132 GLN H H 8.362 0.002 1 460 223 132 GLN CA C 57.015 0.003 1 461 223 132 GLN CB C 27.047 0.015 1 462 223 132 GLN N N 120.516 0.025 1 463 224 133 SER H H 8.058 0.003 1 464 224 133 SER CA C 57.383 0.066 1 465 224 133 SER CB C 65.114 0.013 1 466 224 133 SER N N 113.699 0.012 1 467 225 134 GLY H H 8.308 0.003 1 468 225 134 GLY CA C 45.152 0.034 1 469 225 134 GLY N N 114.008 0.016 1 470 226 135 VAL H H 7.506 0.003 1 471 226 135 VAL CA C 63.806 0.049 1 472 226 135 VAL CB C 31.486 0.041 1 473 226 135 VAL N N 123.371 0.018 1 474 227 136 LYS H H 8.208 0.002 1 475 227 136 LYS CA C 54.804 0.059 1 476 227 136 LYS CB C 34.581 0.017 1 477 227 136 LYS N N 126.044 0.024 1 478 228 137 TYR H H 9.215 0.001 1 479 228 137 TYR CA C 55.576 0.107 1 480 228 137 TYR CB C 41.618 0.085 1 481 228 137 TYR N N 116.267 0.075 1 482 229 138 ARG H H 9.403 0.004 1 483 229 138 ARG CA C 53.263 0.000 1 484 229 138 ARG CB C 32.163 0.000 1 485 229 138 ARG N N 121.407 0.025 1 486 230 139 PRO CA C 65.990 0.025 1 487 230 139 PRO CB C 30.511 0.004 1 488 231 140 ASN H H 7.746 0.002 1 489 231 140 ASN CA C 57.982 0.006 1 490 231 140 ASN CB C 39.879 0.020 1 491 231 140 ASN N N 121.111 0.023 1 492 232 141 ASN H H 8.232 0.004 1 493 232 141 ASN CA C 56.335 0.051 1 494 232 141 ASN CB C 40.236 0.011 1 495 232 141 ASN N N 118.157 0.039 1 496 233 142 GLN H H 7.448 0.004 1 497 233 142 GLN CA C 56.740 0.000 1 498 233 142 GLN CB C 29.053 0.000 1 499 233 142 GLN N N 119.788 0.017 1 500 234 143 ILE H H 6.392 0.000 1 501 234 143 ILE N N 106.264 0.000 1 502 235 144 GLY CA C 45.225 0.039 1 503 236 145 PHE H H 6.832 0.004 1 504 236 145 PHE CA C 57.241 0.001 1 505 236 145 PHE CB C 43.113 0.017 1 506 236 145 PHE N N 112.827 0.024 1 507 237 146 TYR H H 9.717 0.000 1 508 237 146 TYR CA C 60.756 0.018 1 509 237 146 TYR CB C 38.906 0.035 1 510 237 146 TYR N N 121.644 0.004 1 511 238 147 GLN H H 9.213 0.002 1 512 238 147 GLN CA C 53.716 0.021 1 513 238 147 GLN CB C 30.835 0.007 1 514 238 147 GLN N N 126.662 0.019 1 515 239 148 SER H H 9.173 0.002 1 516 239 148 SER CA C 57.891 0.050 1 517 239 148 SER CB C 63.561 0.002 1 518 239 148 SER N N 122.521 0.013 1 519 240 149 ILE H H 7.876 0.003 1 520 240 149 ILE CA C 57.838 0.047 1 521 240 149 ILE CB C 40.427 0.024 1 522 240 149 ILE N N 114.516 0.019 1 523 241 150 THR H H 8.766 0.003 1 524 241 150 THR CA C 59.982 0.000 1 525 241 150 THR CB C 70.465 0.000 1 526 241 150 THR N N 115.124 0.012 1 527 242 151 ALA CA C 54.529 0.008 1 528 242 151 ALA CB C 17.407 0.006 1 529 243 152 ASP H H 7.726 0.004 1 530 243 152 ASP CA C 52.738 0.045 1 531 243 152 ASP CB C 39.727 0.019 1 532 243 152 ASP N N 113.780 0.010 1 533 244 153 GLY H H 7.878 0.003 1 534 244 153 GLY CA C 44.841 0.028 1 535 244 153 GLY N N 108.057 0.026 1 536 245 154 ASN H H 7.293 0.003 1 537 245 154 ASN CA C 51.869 0.035 1 538 245 154 ASN CB C 39.378 0.016 1 539 245 154 ASN N N 119.074 0.013 1 540 246 155 TRP H H 8.078 0.005 1 541 246 155 TRP CA C 57.183 0.051 1 542 246 155 TRP CB C 29.969 0.037 1 543 246 155 TRP N N 119.050 0.010 1 544 247 156 GLY H H 9.531 0.002 1 545 247 156 GLY CA C 43.006 0.038 1 546 247 156 GLY N N 114.153 0.014 1 547 248 157 ASP H H 7.876 0.002 1 548 248 157 ASP CA C 54.655 0.029 1 549 248 157 ASP CB C 41.489 0.004 1 550 248 157 ASP N N 116.196 0.013 1 551 249 158 GLU H H 7.741 0.005 1 552 249 158 GLU CA C 55.876 0.061 1 553 249 158 GLU CB C 31.079 0.026 1 554 249 158 GLU N N 121.394 0.045 1 555 250 159 LYS H H 8.508 0.002 1 556 250 159 LYS CA C 54.595 0.019 1 557 250 159 LYS CB C 32.999 0.023 1 558 250 159 LYS N N 125.660 0.012 1 559 251 160 LEU H H 8.381 0.003 1 560 251 160 LEU CA C 53.334 0.017 1 561 251 160 LEU CB C 41.403 0.013 1 562 251 160 LEU N N 122.365 0.012 1 563 252 161 SER H H 8.349 0.002 1 564 252 161 SER CA C 54.771 0.000 1 565 252 161 SER CB C 63.618 0.000 1 566 252 161 SER N N 118.677 0.014 1 567 253 162 PRO CA C 62.078 0.039 1 568 253 162 PRO CB C 34.212 0.009 1 569 254 163 GLY H H 8.040 0.005 1 570 254 163 GLY CA C 44.292 0.045 1 571 254 163 GLY N N 106.203 0.023 1 572 255 164 TYR H H 7.979 0.003 1 573 255 164 TYR CA C 54.164 0.032 1 574 255 164 TYR CB C 40.251 0.011 1 575 255 164 TYR N N 114.804 0.029 1 576 256 165 THR H H 8.363 0.002 1 577 256 165 THR CA C 61.414 0.032 1 578 256 165 THR CB C 69.562 0.008 1 579 256 165 THR N N 113.934 0.036 1 580 257 166 VAL H H 8.210 0.006 1 581 257 166 VAL CA C 61.095 0.000 1 582 257 166 VAL CB C 32.064 0.000 1 583 257 166 VAL N N 123.888 0.045 1 584 259 168 THR CA C 61.110 0.000 1 585 259 168 THR CB C 69.440 0.010 1 586 260 169 GLY H H 7.938 0.015 1 587 260 169 GLY CA C 45.629 0.000 1 588 260 169 GLY N N 117.937 0.023 1 589 261 170 TRP H H 7.796 0.000 1 590 261 170 TRP CA C 56.850 0.010 1 591 261 170 TRP CB C 28.811 0.021 1 592 261 170 TRP N N 121.607 0.014 1 593 262 171 LYS H H 7.806 0.003 1 594 262 171 LYS CA C 55.425 0.000 1 595 262 171 LYS CB C 32.218 0.000 1 596 262 171 LYS N N 123.603 0.034 1 597 263 172 ASN CA C 52.796 0.000 1 598 263 172 ASN CB C 38.292 0.000 1 599 264 173 PHE H H 7.447 0.004 1 600 264 173 PHE CA C 57.603 0.000 1 601 264 173 PHE CB C 38.594 0.567 1 602 264 173 PHE N N 125.162 0.030 1 603 265 174 THR H H 7.581 0.003 1 604 265 174 THR CA C 62.734 0.000 1 605 265 174 THR CB C 70.407 0.000 1 606 265 174 THR N N 120.963 0.025 1 607 266 175 ARG CA C 55.594 0.000 1 608 266 175 ARG CB C 30.062 0.120 1 609 267 176 VAL H H 8.155 0.004 1 610 267 176 VAL CA C 61.571 0.053 1 611 267 176 VAL CB C 31.966 0.000 1 612 267 176 VAL N N 123.502 0.002 1 613 268 177 PHE H H 8.360 0.004 1 614 268 177 PHE CA C 57.297 0.024 1 615 268 177 PHE CB C 38.938 0.027 1 616 268 177 PHE N N 125.033 0.072 1 617 269 178 THR H H 8.011 0.002 1 618 269 178 THR CA C 61.141 0.013 1 619 269 178 THR CB C 69.062 0.090 1 620 269 178 THR N N 116.300 0.011 1 621 270 179 ASP H H 8.206 0.005 1 622 270 179 ASP CA C 54.091 0.011 1 623 270 179 ASP CB C 40.529 0.009 1 624 270 179 ASP N N 123.004 0.005 1 625 271 180 GLU H H 8.291 0.002 1 626 271 180 GLU CA C 56.570 0.055 1 627 271 180 GLU CB C 29.294 0.030 1 628 271 180 GLU N N 122.019 0.028 1 629 272 181 GLY H H 8.353 0.003 1 630 272 181 GLY CA C 44.909 0.018 1 631 272 181 GLY N N 110.039 0.028 1 632 273 182 ILE H H 7.696 0.004 1 633 273 182 ILE CA C 60.555 0.022 1 634 273 182 ILE CB C 37.715 0.013 1 635 273 182 ILE N N 120.432 0.010 1 636 274 183 GLN H H 8.339 0.003 1 637 274 183 GLN CA C 55.314 0.008 1 638 274 183 GLN CB C 28.474 0.010 1 639 274 183 GLN N N 125.899 0.023 1 640 275 184 LYS H H 7.960 0.004 1 641 275 184 LYS CA C 57.214 0.000 1 642 275 184 LYS CB C 32.658 0.000 1 643 275 184 LYS N N 129.825 0.017 1 stop_ save_