data_SASDE94_MAIN # _sas_result.id 1096 _sas_result.SASBDB_code SASDE94 _sas_result.experimental_MW 14.500 _sas_result.experimental_MW_error . _sas_result.MW_standard . _sas_result.MW_standard_error . _sas_result.MW_Porod 14.500 _sas_result.MW_Porod_error . _sas_result.I0_from_PR 2.6330000000 _sas_result.I0_from_PR_error . _sas_result.I0_from_Guinier 2.6200000000 _sas_result.I0_from_Guinier_error 0.0100000000 _sas_result.Rg_from_PR 1.627 _sas_result.Rg_from_PR_error . _sas_result.Rg_from_Guinier 1.580 _sas_result.Rg_from_Guinier_error 0.040 _sas_result.D_max 6.00 _sas_result.Porod_volume 24.56 _sas_result.Porod_volume_error . _sas_result.estimated_volume . _sas_result.estimated_volume_error . _sas_result.estimated_volume_method . _sas_result.Guinier_point_min 29 _sas_result.Guinier_point_max 166 _sas_result.type_of_curve sec _sas_result.standard . _sas_result.Dmax_error . _sas_result.comments ;SEC column type: GE Healthcare S75 3.2/300; Sample Injection Concentration = 10 mg/mL; Column flow-rate = 0.1 mL/min. ; # _sas_scan.title "Tryparedoxin I109A, reduced state" _sas_scan.detc_id 16 _sas_scan.id 1096 _sas_scan.measurement_date 2018-05-31 _sas_scan.storage_temperature 20.0 _sas_scan.cell_temperature 20.0 _sas_scan.exposure_time 1.000 _sas_scan.number_of_frames . _sas_scan.unit 1/nm _sas_scan.qmin 0.0373 _sas_scan.qmax 4.9279 _sas_scan.sample_id 1056 _sas_scan.result_id 1096 _sas_scan.beam_id 10 # _sas_beam.id 10 _sas_beam.instrument_name "ESRF BM29" _sas_beam.instrument_city Grenoble _sas_beam.instrument_country France _sas_beam.shape . _sas_beam.type_of_source "X-ray synchrotron" _sas_beam.radiation_wavelength 0.099000 _sas_beam.dist_spec_to_detc 2.86900 # _sas_detc.id 16 _sas_detc.name "Pilatus 1M" _sas_detc.type Dectris _sas_detc.pixsize_x 172.000 # _sas_sample.id 1056 _sas_sample.name "Tryparedoxin I109A, reduced state" _sas_sample.ext_coefficient . _sas_sample.contrast . _sas_sample.specific_vol . _sas_sample.purity_method . _sas_sample.dry_vol . _sas_sample.sample_MW . _sas_sample.specimen_concentration . _sas_sample.concentration_method . _sas_sample.entity_id 1274 # _sas_buffer.id 676 _sas_buffer.name "10 mM HEPES pH 7.5, 50 mM NaCl" _sas_buffer.concentration . _sas_buffer.unit . _sas_buffer.pK . _sas_buffer.pH 7.500 _sas_buffer.comment . _sas_buffer.composition . _sas_buffer.sample_id 1056 # _entity.id 1274 _entity.type protein _entity.pdbx_description "Tryparedoxin I109A" _entity.formula_weight 15.775 _entity.pdbx_number_of_molecules 1 # _entity_name_com.entity_id 1274 _entity_name_com.name . # _entity_poly.entity_id 1274 _entity_poly.pdbx_seq_one_letter_code ;GSGLAKYLPGATNLLSKSGEVSLGSLVGKTVFLYFSASWCPPCRG FTPVLAEFYEKHHVAKNFEVVLISWDENESDFHDYYGKMPWLALPFDQRSTVSELGKTFG VESAPTLITINADTGAIIGTQARTRVIEDPDGANFPWPN ; # _entity_src_gen.entity_id 1274 _entity_src_gen.gene_src_common_name "Trypanosoma brucei brucei" # _struct_ref.id 1 _struct_ref.entity_id 1274 _struct_ref.db_name UniProt _struct_ref.db_code O77404 _struct_ref.details http://www.uniprot.org/uniprot/O77404 # _citation.id 419 _citation.title "Inhibitor-induced dimerization of an essential oxidoreductase from African Trypanosomes." _citation.year "2019 Jan 3" _citation.pdbx_database_id_DOI 10.1002/anie.201810470 _citation.pdbx_database_id_PubMed 30605929 # loop_ _citation_author.citation_id _citation_author.ordinal _citation_author.name 419 1 "Wagner A" 419 2 "Le TA" 419 3 "Brennich M" 419 4 "Klein P" 419 5 "Bader N" 419 6 "Diehl E" 419 7 "Paszek D" 419 8 "Weickhmann AK" 419 9 "Dirdjaja N" 419 10 "Krauth-Siegel RL" 419 11 "Engels B" 419 12 "Opatz T" 419 13 "Schindelin H" # _pdbx_contact_author.id 68 _pdbx_contact_author.name_first Martha _pdbx_contact_author.name_last Brennich _pdbx_contact_author.role . _pdbx_contact_author.address_1 EMBL _pdbx_contact_author.address_2 "European Molecular Biology Laboratory (EMBL) - Grenoble Outstation" _pdbx_contact_author.address_3 "Grenoble, France" # loop_ _sas_scan_intensity.id _sas_scan_intensity.momentum_transfer _sas_scan_intensity.intensity _sas_scan_intensity.intensity_su_counting _sas_scan_intensity.scan_id 1 3.725576E-02 -1.461951E+01 2.178967E+00 1096 2 4.194927E-02 -2.360013E+01 1.165332E+00 1096 3 4.664278E-02 -1.419823E+01 9.771361E-01 1096 4 5.133629E-02 -1.013013E+01 7.928682E-01 1096 5 5.602979E-02 -6.746533E+00 6.626768E-01 1096 6 6.072330E-02 -5.798038E+00 5.053442E-01 1096 7 6.541680E-02 -1.777797E+00 4.499861E-01 1096 8 7.011031E-02 -2.045733E+00 3.852017E-01 1096 9 7.480382E-02 -9.773397E-02 3.602177E-01 1096 10 7.949733E-02 4.562386E-01 2.979766E-01 1096 11 8.419084E-02 9.031191E-01 2.617837E-01 1096 12 8.888435E-02 8.154761E-01 2.582618E-01 1096 13 9.357785E-02 1.631816E+00 2.336855E-01 1096 14 9.827136E-02 1.910974E+00 2.103985E-01 1096 15 1.029649E-01 1.512706E+00 1.812034E-01 1096 16 1.076584E-01 1.953730E+00 1.865105E-01 1096 17 1.123519E-01 2.157713E+00 1.709788E-01 1096 18 1.170454E-01 2.263799E+00 1.554796E-01 1096 19 1.217389E-01 2.274174E+00 1.455509E-01 1096 20 1.264324E-01 1.961855E+00 1.424829E-01 1096 21 1.311259E-01 2.170077E+00 1.344049E-01 1096 22 1.358194E-01 2.521242E+00 1.303637E-01 1096 23 1.405129E-01 2.465091E+00 1.208052E-01 1096 24 1.452064E-01 2.316228E+00 1.181883E-01 1096 25 1.498999E-01 2.606455E+00 1.124720E-01 1096 26 1.545934E-01 2.284395E+00 1.097526E-01 1096 27 1.592870E-01 2.363794E+00 1.052644E-01 1096 28 1.639805E-01 2.180501E+00 9.749535E-02 1096 29 1.686740E-01 2.544288E+00 9.884534E-02 1096 30 1.733675E-01 2.551301E+00 9.702980E-02 1096 31 1.780610E-01 2.326375E+00 9.153052E-02 1096 32 1.827545E-01 2.555792E+00 8.875373E-02 1096 33 1.874480E-01 2.462449E+00 8.724047E-02 1096 34 1.921415E-01 2.708315E+00 8.728939E-02 1096 35 1.968350E-01 2.331630E+00 8.511244E-02 1096 36 2.015285E-01 2.493202E+00 8.187171E-02 1096 37 2.062220E-01 2.568210E+00 7.744782E-02 1096 38 2.109155E-01 2.426381E+00 7.889908E-02 1096 39 2.156090E-01 2.514287E+00 7.894894E-02 1096 40 2.203026E-01 2.505445E+00 7.530767E-02 1096 41 2.249961E-01 2.464354E+00 7.263001E-02 1096 42 2.296896E-01 2.349910E+00 7.322870E-02 1096 43 2.343831E-01 2.506081E+00 7.359694E-02 1096 44 2.390766E-01 2.477931E+00 7.116436E-02 1096 45 2.437701E-01 2.549691E+00 6.939934E-02 1096 46 2.484636E-01 2.526471E+00 6.953722E-02 1096 47 2.531571E-01 2.317754E+00 6.891433E-02 1096 48 2.578506E-01 2.460188E+00 6.570815E-02 1096 49 2.625441E-01 2.578146E+00 6.517117E-02 1096 50 2.672376E-01 2.378287E+00 6.547860E-02 1096 51 2.719311E-01 2.450240E+00 6.544138E-02 1096 52 2.766247E-01 2.425574E+00 6.388840E-02 1096 53 2.813182E-01 2.365723E+00 6.175750E-02 1096 54 2.860117E-01 2.593628E+00 6.087043E-02 1096 55 2.907052E-01 2.493142E+00 6.316452E-02 1096 56 2.953987E-01 2.406940E+00 6.219070E-02 1096 57 3.000922E-01 2.423810E+00 5.887286E-02 1096 58 3.047857E-01 2.432757E+00 5.905827E-02 1096 59 3.094792E-01 2.393306E+00 5.886616E-02 1096 60 3.141727E-01 2.476933E+00 6.066197E-02 1096 61 3.188662E-01 2.339989E+00 5.624254E-02 1096 62 3.235597E-01 2.490282E+00 5.723455E-02 1096 63 3.282532E-01 2.459369E+00 5.710128E-02 1096 64 3.329468E-01 2.378772E+00 5.817937E-02 1096 65 3.376403E-01 2.310479E+00 5.468722E-02 1096 66 3.423338E-01 2.446162E+00 5.592380E-02 1096 67 3.470272E-01 2.391419E+00 5.647243E-02 1096 68 3.517208E-01 2.441928E+00 5.896300E-02 1096 69 3.564143E-01 2.361491E+00 5.661329E-02 1096 70 3.611078E-01 2.494409E+00 5.771000E-02 1096 71 3.658013E-01 2.323905E+00 5.919911E-02 1096 72 3.704948E-01 2.355714E+00 6.027972E-02 1096 73 3.751883E-01 2.369282E+00 6.203521E-02 1096 74 3.798818E-01 2.232711E+00 5.863919E-02 1096 75 3.845753E-01 2.284388E+00 6.143940E-02 1096 76 3.892688E-01 2.401522E+00 6.187081E-02 1096 77 3.939623E-01 2.388345E+00 6.260823E-02 1096 78 3.986558E-01 2.284850E+00 6.153047E-02 1096 79 4.033493E-01 2.222701E+00 6.493599E-02 1096 80 4.080429E-01 2.204946E+00 6.617770E-02 1096 81 4.127364E-01 2.333581E+00 6.673320E-02 1096 82 4.174299E-01 2.270140E+00 6.875460E-02 1096 83 4.221234E-01 2.293395E+00 6.982173E-02 1096 84 4.268169E-01 2.129086E+00 7.218886E-02 1096 85 4.315104E-01 2.176813E+00 7.305400E-02 1096 86 4.362039E-01 2.209718E+00 7.342870E-02 1096 87 4.408974E-01 2.199811E+00 7.369808E-02 1096 88 4.455909E-01 2.242855E+00 7.705204E-02 1096 89 4.502844E-01 2.359088E+00 7.621620E-02 1096 90 4.549779E-01 2.181140E+00 7.697689E-02 1096 91 4.596714E-01 2.129629E+00 7.699564E-02 1096 92 4.643650E-01 2.280514E+00 7.698209E-02 1096 93 4.690585E-01 2.260910E+00 7.404693E-02 1096 94 4.737520E-01 2.212729E+00 7.234476E-02 1096 95 4.784455E-01 2.121669E+00 7.162637E-02 1096 96 4.831390E-01 2.207420E+00 7.170506E-02 1096 97 4.878325E-01 1.964197E+00 6.996116E-02 1096 98 4.925260E-01 2.094711E+00 7.093250E-02 1096 99 4.972195E-01 1.991004E+00 6.951735E-02 1096 100 5.019130E-01 2.131875E+00 6.812609E-02 1096 101 5.066065E-01 2.037657E+00 6.813013E-02 1096 102 5.113000E-01 2.101580E+00 6.957168E-02 1096 103 5.159935E-01 1.980493E+00 6.916634E-02 1096 104 5.206870E-01 2.184774E+00 6.560926E-02 1096 105 5.253805E-01 2.099500E+00 6.720545E-02 1096 106 5.300741E-01 2.124432E+00 6.843892E-02 1096 107 5.347676E-01 2.176290E+00 6.766383E-02 1096 108 5.394611E-01 2.115382E+00 6.541379E-02 1096 109 5.441546E-01 1.963411E+00 6.579594E-02 1096 110 5.488481E-01 1.948551E+00 6.590280E-02 1096 111 5.535416E-01 2.033299E+00 6.612974E-02 1096 112 5.582351E-01 1.997637E+00 6.297830E-02 1096 113 5.629286E-01 1.884040E+00 6.363140E-02 1096 114 5.676221E-01 2.012865E+00 6.378517E-02 1096 115 5.723156E-01 1.936222E+00 6.440998E-02 1096 116 5.770091E-01 1.933777E+00 6.261200E-02 1096 117 5.817026E-01 1.994233E+00 6.172350E-02 1096 118 5.863962E-01 1.914543E+00 6.238423E-02 1096 119 5.910897E-01 1.846483E+00 6.378973E-02 1096 120 5.957832E-01 1.847636E+00 6.211932E-02 1096 121 6.004767E-01 1.956864E+00 6.101531E-02 1096 122 6.051702E-01 1.966298E+00 6.095433E-02 1096 123 6.098637E-01 2.059669E+00 6.347909E-02 1096 124 6.145572E-01 1.872902E+00 6.050713E-02 1096 125 6.192507E-01 2.025638E+00 6.049322E-02 1096 126 6.239442E-01 1.812358E+00 6.095435E-02 1096 127 6.286377E-01 1.885636E+00 6.100354E-02 1096 128 6.333312E-01 1.814002E+00 6.191080E-02 1096 129 6.380248E-01 1.837382E+00 5.897727E-02 1096 130 6.427183E-01 1.796714E+00 6.104238E-02 1096 131 6.474118E-01 1.870568E+00 6.083419E-02 1096 132 6.521052E-01 1.867684E+00 6.119906E-02 1096 133 6.567987E-01 1.892859E+00 5.878557E-02 1096 134 6.614922E-01 1.854654E+00 5.950082E-02 1096 135 6.661857E-01 1.822280E+00 5.967877E-02 1096 136 6.708792E-01 1.773982E+00 6.056075E-02 1096 137 6.755728E-01 1.801727E+00 5.883866E-02 1096 138 6.802663E-01 1.857281E+00 5.852983E-02 1096 139 6.849598E-01 1.776838E+00 5.981707E-02 1096 140 6.896533E-01 1.787514E+00 5.983539E-02 1096 141 6.943468E-01 1.640230E+00 5.900169E-02 1096 142 6.990403E-01 1.690397E+00 5.731016E-02 1096 143 7.037338E-01 1.704662E+00 5.912070E-02 1096 144 7.084273E-01 1.795978E+00 5.824918E-02 1096 145 7.131208E-01 1.776502E+00 5.923465E-02 1096 146 7.178143E-01 1.654064E+00 5.722611E-02 1096 147 7.225078E-01 1.692254E+00 5.751579E-02 1096 148 7.272013E-01 1.800101E+00 5.831865E-02 1096 149 7.318948E-01 1.688369E+00 5.864234E-02 1096 150 7.365884E-01 1.626966E+00 5.654723E-02 1096 151 7.412819E-01 1.665905E+00 5.773381E-02 1096 152 7.459754E-01 1.545473E+00 5.743014E-02 1096 153 7.506689E-01 1.649537E+00 5.769953E-02 1096 154 7.553624E-01 1.680402E+00 5.701154E-02 1096 155 7.600559E-01 1.652171E+00 5.665306E-02 1096 156 7.647494E-01 1.668308E+00 5.702671E-02 1096 157 7.694429E-01 1.535822E+00 5.736559E-02 1096 158 7.741364E-01 1.598999E+00 5.674788E-02 1096 159 7.788299E-01 1.542889E+00 5.573466E-02 1096 160 7.835234E-01 1.592164E+00 5.601217E-02 1096 161 7.882170E-01 1.564690E+00 5.676378E-02 1096 162 7.929105E-01 1.571234E+00 5.689870E-02 1096 163 7.976040E-01 1.562938E+00 5.517247E-02 1096 164 8.022975E-01 1.513640E+00 5.537290E-02 1096 165 8.069910E-01 1.456678E+00 5.627458E-02 1096 166 8.116845E-01 1.484239E+00 5.615335E-02 1096 167 8.163780E-01 1.482090E+00 5.476610E-02 1096 168 8.210715E-01 1.461604E+00 5.471769E-02 1096 169 8.257650E-01 1.418873E+00 5.599608E-02 1096 170 8.304585E-01 1.423879E+00 5.505343E-02 1096 171 8.351520E-01 1.282182E+00 5.494965E-02 1096 172 8.398455E-01 1.468096E+00 5.452202E-02 1096 173 8.445390E-01 1.406638E+00 5.480847E-02 1096 174 8.492325E-01 1.398704E+00 5.524410E-02 1096 175 8.539261E-01 1.442881E+00 5.488218E-02 1096 176 8.586196E-01 1.481532E+00 5.334870E-02 1096 177 8.633131E-01 1.434800E+00 5.387971E-02 1096 178 8.680066E-01 1.310205E+00 5.504472E-02 1096 179 8.727001E-01 1.222698E+00 5.446691E-02 1096 180 8.773936E-01 1.358457E+00 5.298181E-02 1096 181 8.820871E-01 1.386439E+00 5.366599E-02 1096 182 8.867806E-01 1.371542E+00 5.414092E-02 1096 183 8.914741E-01 1.364704E+00 5.421962E-02 1096 184 8.961676E-01 1.331014E+00 5.303767E-02 1096 185 9.008611E-01 1.410893E+00 5.311894E-02 1096 186 9.055547E-01 1.300771E+00 5.339676E-02 1096 187 9.102482E-01 1.319506E+00 5.390558E-02 1096 188 9.149417E-01 1.274390E+00 5.244967E-02 1096 189 9.196352E-01 1.249387E+00 5.329193E-02 1096 190 9.243287E-01 1.394104E+00 5.274356E-02 1096 191 9.290222E-01 1.278853E+00 5.356568E-02 1096 192 9.337157E-01 1.283955E+00 5.276697E-02 1096 193 9.384092E-01 1.302673E+00 5.138277E-02 1096 194 9.431027E-01 1.240957E+00 5.287339E-02 1096 195 9.477962E-01 1.263575E+00 5.281830E-02 1096 196 9.524897E-01 1.258113E+00 5.266826E-02 1096 197 9.571832E-01 1.150415E+00 5.087576E-02 1096 198 9.618767E-01 1.255488E+00 5.234833E-02 1096 199 9.665703E-01 1.203295E+00 5.244375E-02 1096 200 9.712638E-01 1.333107E+00 5.223993E-02 1096 201 9.759573E-01 1.250161E+00 5.107122E-02 1096 202 9.806508E-01 1.113371E+00 5.138259E-02 1096 203 9.853443E-01 1.175428E+00 5.179723E-02 1096 204 9.900378E-01 1.140385E+00 5.198824E-02 1096 205 9.947313E-01 1.192583E+00 5.080430E-02 1096 206 9.994248E-01 1.220214E+00 5.075151E-02 1096 207 1.004118E+00 1.084227E+00 5.144014E-02 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1.394410E-01 1096 1017 4.805860E+00 1.418329E-01 1.433120E-01 1096 1018 4.810553E+00 1.680560E-01 1.499636E-01 1096 1019 4.815247E+00 1.941714E-01 1.469555E-01 1096 1020 4.819940E+00 1.452546E-02 1.505245E-01 1096 1021 4.824634E+00 3.393614E-01 1.565280E-01 1096 1022 4.829327E+00 4.569024E-01 1.636605E-01 1096 1023 4.834021E+00 2.704576E-01 1.586599E-01 1096 1024 4.838714E+00 1.903229E-01 1.668208E-01 1096 1025 4.843408E+00 9.882319E-02 1.726448E-01 1096 1026 4.848101E+00 1.050723E-01 1.806160E-01 1096 1027 4.852795E+00 3.287180E-01 1.778755E-01 1096 1028 4.857488E+00 1.413702E-01 1.876258E-01 1096 1029 4.862182E+00 2.302663E-01 1.962548E-01 1096 1030 4.866875E+00 2.398727E-01 1.977917E-01 1096 1031 4.871569E+00 1.381868E-01 2.049118E-01 1096 1032 4.876262E+00 2.291492E-01 2.216105E-01 1096 1033 4.880956E+00 5.138976E-01 2.294265E-01 1096 1034 4.885649E+00 2.450542E-01 2.315927E-01 1096 1035 4.890343E+00 1.586703E-01 2.524071E-01 1096 1036 4.895036E+00 7.470106E-01 2.695746E-01 1096 1037 4.899730E+00 3.810008E-02 2.773124E-01 1096 1038 4.904423E+00 -1.895666E-01 3.031102E-01 1096 1039 4.909117E+00 -8.559123E-01 3.548052E-01 1096 1040 4.913810E+00 -5.976081E-01 3.848697E-01 1096 1041 4.918504E+00 -2.513850E-01 4.036314E-01 1096 1042 4.923197E+00 6.433547E-01 5.075323E-01 1096 1043 4.927891E+00 3.130279E-01 3.061248E-01 1096 # _sas_p_of_R_details.id 1096 _sas_p_of_R_details.intensity_id 1096 _sas_p_of_R_details.software_p_of_R "GNOM 5.0" _sas_p_of_R_details.number_of_points 763 _sas_p_of_R_details.qmin 0.210916 _sas_p_of_R_details.qmax 3.78737 _sas_p_of_R_details.p_of_R_point_min 1 _sas_p_of_R_details.p_of_R_point_max 763 _sas_p_of_R_details.Rmin 0.0 _sas_p_of_R_details.Rmax 6.0 # loop_ _sas_p_of_R.id _sas_p_of_R.ordinal _sas_p_of_R.r _sas_p_of_R.P _sas_p_of_R.P_error 1096 1 0.000000E+00 0.000000E+00 0.000000E+00 1096 2 2.372000E-02 3.558000E-03 9.570000E-05 1096 3 4.743000E-02 6.918000E-03 1.810000E-04 1096 4 7.115000E-02 1.008000E-02 2.559000E-04 1096 5 9.486000E-02 1.305000E-02 3.207000E-04 1096 6 1.186000E-01 1.582000E-02 3.755000E-04 1096 7 1.423000E-01 1.841000E-02 4.206000E-04 1096 8 1.660000E-01 2.080000E-02 4.563000E-04 1096 9 1.897000E-01 2.302000E-02 4.830000E-04 1096 10 2.134000E-01 2.506000E-02 5.009000E-04 1096 11 2.372000E-01 2.692000E-02 5.107000E-04 1096 12 2.609000E-01 2.862000E-02 5.128000E-04 1096 13 2.846000E-01 3.016000E-02 5.079000E-04 1096 14 3.083000E-01 3.154000E-02 4.965000E-04 1096 15 3.320000E-01 3.277000E-02 4.794000E-04 1096 16 3.557000E-01 3.387000E-02 4.575000E-04 1096 17 3.794000E-01 3.484000E-02 4.318000E-04 1096 18 4.032000E-01 3.568000E-02 4.034000E-04 1096 19 4.269000E-01 3.641000E-02 3.738000E-04 1096 20 4.506000E-01 3.703000E-02 3.447000E-04 1096 21 4.743000E-01 3.756000E-02 3.184000E-04 1096 22 4.980000E-01 3.800000E-02 2.976000E-04 1096 23 5.217000E-01 3.836000E-02 2.850000E-04 1096 24 5.455000E-01 3.865000E-02 2.830000E-04 1096 25 5.692000E-01 3.888000E-02 2.925000E-04 1096 26 5.929000E-01 3.906000E-02 3.127000E-04 1096 27 6.166000E-01 3.920000E-02 3.416000E-04 1096 28 6.403000E-01 3.930000E-02 3.766000E-04 1096 29 6.640000E-01 3.939000E-02 4.155000E-04 1096 30 6.877000E-01 3.945000E-02 4.564000E-04 1096 31 7.115000E-01 3.951000E-02 4.979000E-04 1096 32 7.352000E-01 3.957000E-02 5.388000E-04 1096 33 7.589000E-01 3.965000E-02 5.783000E-04 1096 34 7.826000E-01 3.973000E-02 6.155000E-04 1096 35 8.063000E-01 3.985000E-02 6.500000E-04 1096 36 8.300000E-01 3.999000E-02 6.812000E-04 1096 37 8.538000E-01 4.017000E-02 7.089000E-04 1096 38 8.775000E-01 4.039000E-02 7.327000E-04 1096 39 9.012000E-01 4.066000E-02 7.525000E-04 1096 40 9.249000E-01 4.098000E-02 7.681000E-04 1096 41 9.486000E-01 4.136000E-02 7.796000E-04 1096 42 9.723000E-01 4.180000E-02 7.869000E-04 1096 43 9.960000E-01 4.230000E-02 7.900000E-04 1096 44 1.020000E+00 4.287000E-02 7.893000E-04 1096 45 1.043000E+00 4.351000E-02 7.848000E-04 1096 46 1.067000E+00 4.422000E-02 7.770000E-04 1096 47 1.091000E+00 4.499000E-02 7.661000E-04 1096 48 1.115000E+00 4.584000E-02 7.527000E-04 1096 49 1.138000E+00 4.676000E-02 7.372000E-04 1096 50 1.162000E+00 4.775000E-02 7.203000E-04 1096 51 1.186000E+00 4.880000E-02 7.026000E-04 1096 52 1.209000E+00 4.993000E-02 6.849000E-04 1096 53 1.233000E+00 5.112000E-02 6.680000E-04 1096 54 1.257000E+00 5.236000E-02 6.527000E-04 1096 55 1.281000E+00 5.367000E-02 6.398000E-04 1096 56 1.304000E+00 5.503000E-02 6.301000E-04 1096 57 1.328000E+00 5.644000E-02 6.243000E-04 1096 58 1.352000E+00 5.790000E-02 6.227000E-04 1096 59 1.375000E+00 5.940000E-02 6.257000E-04 1096 60 1.399000E+00 6.093000E-02 6.332000E-04 1096 61 1.423000E+00 6.250000E-02 6.450000E-04 1096 62 1.447000E+00 6.409000E-02 6.605000E-04 1096 63 1.470000E+00 6.569000E-02 6.792000E-04 1096 64 1.494000E+00 6.731000E-02 7.002000E-04 1096 65 1.518000E+00 6.894000E-02 7.230000E-04 1096 66 1.542000E+00 7.057000E-02 7.465000E-04 1096 67 1.565000E+00 7.219000E-02 7.703000E-04 1096 68 1.589000E+00 7.380000E-02 7.934000E-04 1096 69 1.613000E+00 7.539000E-02 8.155000E-04 1096 70 1.636000E+00 7.695000E-02 8.359000E-04 1096 71 1.660000E+00 7.848000E-02 8.541000E-04 1096 72 1.684000E+00 7.998000E-02 8.698000E-04 1096 73 1.708000E+00 8.143000E-02 8.827000E-04 1096 74 1.731000E+00 8.283000E-02 8.925000E-04 1096 75 1.755000E+00 8.418000E-02 8.992000E-04 1096 76 1.779000E+00 8.547000E-02 9.025000E-04 1096 77 1.802000E+00 8.669000E-02 9.026000E-04 1096 78 1.826000E+00 8.784000E-02 8.994000E-04 1096 79 1.850000E+00 8.891000E-02 8.932000E-04 1096 80 1.874000E+00 8.991000E-02 8.841000E-04 1096 81 1.897000E+00 9.082000E-02 8.726000E-04 1096 82 1.921000E+00 9.165000E-02 8.590000E-04 1096 83 1.945000E+00 9.238000E-02 8.437000E-04 1096 84 1.968000E+00 9.303000E-02 8.275000E-04 1096 85 1.992000E+00 9.358000E-02 8.109000E-04 1096 86 2.016000E+00 9.403000E-02 7.949000E-04 1096 87 2.040000E+00 9.438000E-02 7.801000E-04 1096 88 2.063000E+00 9.463000E-02 7.675000E-04 1096 89 2.087000E+00 9.478000E-02 7.579000E-04 1096 90 2.111000E+00 9.483000E-02 7.522000E-04 1096 91 2.134000E+00 9.478000E-02 7.511000E-04 1096 92 2.158000E+00 9.463000E-02 7.551000E-04 1096 93 2.182000E+00 9.437000E-02 7.645000E-04 1096 94 2.206000E+00 9.402000E-02 7.794000E-04 1096 95 2.229000E+00 9.357000E-02 7.994000E-04 1096 96 2.253000E+00 9.303000E-02 8.243000E-04 1096 97 2.277000E+00 9.239000E-02 8.534000E-04 1096 98 2.300000E+00 9.166000E-02 8.859000E-04 1096 99 2.324000E+00 9.085000E-02 9.212000E-04 1096 100 2.348000E+00 8.995000E-02 9.583000E-04 1096 101 2.372000E+00 8.896000E-02 9.966000E-04 1096 102 2.395000E+00 8.790000E-02 1.035000E-03 1096 103 2.419000E+00 8.677000E-02 1.074000E-03 1096 104 2.443000E+00 8.556000E-02 1.111000E-03 1096 105 2.466000E+00 8.429000E-02 1.147000E-03 1096 106 2.490000E+00 8.295000E-02 1.181000E-03 1096 107 2.514000E+00 8.156000E-02 1.212000E-03 1096 108 2.538000E+00 8.012000E-02 1.240000E-03 1096 109 2.561000E+00 7.862000E-02 1.266000E-03 1096 110 2.585000E+00 7.708000E-02 1.288000E-03 1096 111 2.609000E+00 7.551000E-02 1.306000E-03 1096 112 2.632000E+00 7.389000E-02 1.320000E-03 1096 113 2.656000E+00 7.225000E-02 1.331000E-03 1096 114 2.680000E+00 7.058000E-02 1.337000E-03 1096 115 2.704000E+00 6.889000E-02 1.340000E-03 1096 116 2.727000E+00 6.718000E-02 1.338000E-03 1096 117 2.751000E+00 6.546000E-02 1.333000E-03 1096 118 2.775000E+00 6.373000E-02 1.325000E-03 1096 119 2.798000E+00 6.199000E-02 1.313000E-03 1096 120 2.822000E+00 6.026000E-02 1.298000E-03 1096 121 2.846000E+00 5.852000E-02 1.281000E-03 1096 122 2.870000E+00 5.680000E-02 1.261000E-03 1096 123 2.893000E+00 5.508000E-02 1.239000E-03 1096 124 2.917000E+00 5.338000E-02 1.216000E-03 1096 125 2.941000E+00 5.169000E-02 1.192000E-03 1096 126 2.964000E+00 5.002000E-02 1.168000E-03 1096 127 2.988000E+00 4.837000E-02 1.144000E-03 1096 128 3.012000E+00 4.674000E-02 1.121000E-03 1096 129 3.036000E+00 4.514000E-02 1.099000E-03 1096 130 3.059000E+00 4.357000E-02 1.080000E-03 1096 131 3.083000E+00 4.203000E-02 1.064000E-03 1096 132 3.107000E+00 4.051000E-02 1.050000E-03 1096 133 3.130000E+00 3.903000E-02 1.040000E-03 1096 134 3.154000E+00 3.759000E-02 1.034000E-03 1096 135 3.178000E+00 3.617000E-02 1.032000E-03 1096 136 3.202000E+00 3.479000E-02 1.034000E-03 1096 137 3.225000E+00 3.345000E-02 1.039000E-03 1096 138 3.249000E+00 3.215000E-02 1.048000E-03 1096 139 3.273000E+00 3.088000E-02 1.060000E-03 1096 140 3.296000E+00 2.964000E-02 1.075000E-03 1096 141 3.320000E+00 2.844000E-02 1.092000E-03 1096 142 3.344000E+00 2.728000E-02 1.110000E-03 1096 143 3.368000E+00 2.616000E-02 1.130000E-03 1096 144 3.391000E+00 2.507000E-02 1.150000E-03 1096 145 3.415000E+00 2.401000E-02 1.170000E-03 1096 146 3.439000E+00 2.299000E-02 1.190000E-03 1096 147 3.462000E+00 2.201000E-02 1.209000E-03 1096 148 3.486000E+00 2.105000E-02 1.228000E-03 1096 149 3.510000E+00 2.013000E-02 1.245000E-03 1096 150 3.534000E+00 1.924000E-02 1.260000E-03 1096 151 3.557000E+00 1.839000E-02 1.274000E-03 1096 152 3.581000E+00 1.756000E-02 1.286000E-03 1096 153 3.605000E+00 1.677000E-02 1.297000E-03 1096 154 3.628000E+00 1.600000E-02 1.306000E-03 1096 155 3.652000E+00 1.526000E-02 1.313000E-03 1096 156 3.676000E+00 1.455000E-02 1.319000E-03 1096 157 3.700000E+00 1.386000E-02 1.323000E-03 1096 158 3.723000E+00 1.320000E-02 1.326000E-03 1096 159 3.747000E+00 1.257000E-02 1.329000E-03 1096 160 3.771000E+00 1.196000E-02 1.330000E-03 1096 161 3.794000E+00 1.138000E-02 1.331000E-03 1096 162 3.818000E+00 1.082000E-02 1.331000E-03 1096 163 3.842000E+00 1.028000E-02 1.332000E-03 1096 164 3.866000E+00 9.768000E-03 1.332000E-03 1096 165 3.889000E+00 9.277000E-03 1.333000E-03 1096 166 3.913000E+00 8.808000E-03 1.334000E-03 1096 167 3.937000E+00 8.361000E-03 1.336000E-03 1096 168 3.960000E+00 7.935000E-03 1.339000E-03 1096 169 3.984000E+00 7.532000E-03 1.343000E-03 1096 170 4.008000E+00 7.149000E-03 1.347000E-03 1096 171 4.032000E+00 6.787000E-03 1.353000E-03 1096 172 4.055000E+00 6.446000E-03 1.359000E-03 1096 173 4.079000E+00 6.126000E-03 1.366000E-03 1096 174 4.103000E+00 5.827000E-03 1.373000E-03 1096 175 4.126000E+00 5.548000E-03 1.381000E-03 1096 176 4.150000E+00 5.290000E-03 1.389000E-03 1096 177 4.174000E+00 5.052000E-03 1.397000E-03 1096 178 4.198000E+00 4.834000E-03 1.405000E-03 1096 179 4.221000E+00 4.636000E-03 1.413000E-03 1096 180 4.245000E+00 4.458000E-03 1.420000E-03 1096 181 4.269000E+00 4.300000E-03 1.427000E-03 1096 182 4.292000E+00 4.161000E-03 1.433000E-03 1096 183 4.316000E+00 4.042000E-03 1.438000E-03 1096 184 4.340000E+00 3.941000E-03 1.443000E-03 1096 185 4.364000E+00 3.859000E-03 1.446000E-03 1096 186 4.387000E+00 3.794000E-03 1.448000E-03 1096 187 4.411000E+00 3.748000E-03 1.450000E-03 1096 188 4.435000E+00 3.718000E-03 1.451000E-03 1096 189 4.458000E+00 3.704000E-03 1.451000E-03 1096 190 4.482000E+00 3.707000E-03 1.450000E-03 1096 191 4.506000E+00 3.724000E-03 1.449000E-03 1096 192 4.530000E+00 3.755000E-03 1.448000E-03 1096 193 4.553000E+00 3.800000E-03 1.446000E-03 1096 194 4.577000E+00 3.857000E-03 1.445000E-03 1096 195 4.601000E+00 3.925000E-03 1.444000E-03 1096 196 4.625000E+00 4.004000E-03 1.444000E-03 1096 197 4.648000E+00 4.092000E-03 1.444000E-03 1096 198 4.672000E+00 4.188000E-03 1.445000E-03 1096 199 4.696000E+00 4.290000E-03 1.447000E-03 1096 200 4.719000E+00 4.398000E-03 1.451000E-03 1096 201 4.743000E+00 4.511000E-03 1.455000E-03 1096 202 4.767000E+00 4.626000E-03 1.461000E-03 1096 203 4.791000E+00 4.743000E-03 1.469000E-03 1096 204 4.814000E+00 4.860000E-03 1.477000E-03 1096 205 4.838000E+00 4.976000E-03 1.487000E-03 1096 206 4.862000E+00 5.089000E-03 1.498000E-03 1096 207 4.885000E+00 5.199000E-03 1.510000E-03 1096 208 4.909000E+00 5.303000E-03 1.523000E-03 1096 209 4.933000E+00 5.400000E-03 1.536000E-03 1096 210 4.957000E+00 5.490000E-03 1.550000E-03 1096 211 4.980000E+00 5.571000E-03 1.564000E-03 1096 212 5.004000E+00 5.642000E-03 1.578000E-03 1096 213 5.028000E+00 5.701000E-03 1.591000E-03 1096 214 5.051000E+00 5.748000E-03 1.605000E-03 1096 215 5.075000E+00 5.782000E-03 1.618000E-03 1096 216 5.099000E+00 5.802000E-03 1.631000E-03 1096 217 5.123000E+00 5.806000E-03 1.643000E-03 1096 218 5.146000E+00 5.796000E-03 1.654000E-03 1096 219 5.170000E+00 5.769000E-03 1.665000E-03 1096 220 5.194000E+00 5.726000E-03 1.674000E-03 1096 221 5.217000E+00 5.666000E-03 1.683000E-03 1096 222 5.241000E+00 5.589000E-03 1.691000E-03 1096 223 5.265000E+00 5.495000E-03 1.699000E-03 1096 224 5.289000E+00 5.384000E-03 1.706000E-03 1096 225 5.312000E+00 5.257000E-03 1.712000E-03 1096 226 5.336000E+00 5.113000E-03 1.717000E-03 1096 227 5.360000E+00 4.954000E-03 1.722000E-03 1096 228 5.383000E+00 4.780000E-03 1.726000E-03 1096 229 5.407000E+00 4.592000E-03 1.729000E-03 1096 230 5.431000E+00 4.390000E-03 1.731000E-03 1096 231 5.455000E+00 4.177000E-03 1.732000E-03 1096 232 5.478000E+00 3.952000E-03 1.732000E-03 1096 233 5.502000E+00 3.718000E-03 1.730000E-03 1096 234 5.526000E+00 3.477000E-03 1.726000E-03 1096 235 5.549000E+00 3.228000E-03 1.719000E-03 1096 236 5.573000E+00 2.976000E-03 1.709000E-03 1096 237 5.597000E+00 2.720000E-03 1.695000E-03 1096 238 5.621000E+00 2.463000E-03 1.676000E-03 1096 239 5.644000E+00 2.208000E-03 1.652000E-03 1096 240 5.668000E+00 1.956000E-03 1.622000E-03 1096 241 5.692000E+00 1.709000E-03 1.585000E-03 1096 242 5.715000E+00 1.469000E-03 1.540000E-03 1096 243 5.739000E+00 1.239000E-03 1.485000E-03 1096 244 5.763000E+00 1.022000E-03 1.421000E-03 1096 245 5.787000E+00 8.183000E-04 1.346000E-03 1096 246 5.810000E+00 6.314000E-04 1.259000E-03 1096 247 5.834000E+00 4.634000E-04 1.159000E-03 1096 248 5.858000E+00 3.165000E-04 1.044000E-03 1096 249 5.881000E+00 1.929000E-04 9.145000E-04 1096 250 5.905000E+00 9.494000E-05 7.684000E-04 1096 251 5.929000E+00 2.463000E-05 6.050000E-04 1096 252 5.953000E+00 -1.594000E-05 4.231000E-04 1096 253 5.976000E+00 -2.478000E-05 2.218000E-04 1096 254 6.000000E+00 0.000000E+00 0.000000E+00 # loop_ _sas_p_of_R_extrapolated_intensity.id _sas_p_of_R_extrapolated_intensity.ordinal _sas_p_of_R_extrapolated_intensity.momentum_transfer _sas_p_of_R_extrapolated_intensity.intensity_reg 1096 1 0.000000E+00 2.632940E+00 1096 2 7.532700E-03 2.632800E+00 1096 3 1.506540E-02 2.632400E+00 1096 4 2.259810E-02 2.631750E+00 1096 5 3.013080E-02 2.630820E+00 1096 6 3.766350E-02 2.629640E+00 1096 7 4.519620E-02 2.628190E+00 1096 8 5.272890E-02 2.626480E+00 1096 9 6.026160E-02 2.624510E+00 1096 10 6.779430E-02 2.622280E+00 1096 11 7.532700E-02 2.619790E+00 1096 12 8.285970E-02 2.617040E+00 1096 13 9.039240E-02 2.614040E+00 1096 14 9.792510E-02 2.610770E+00 1096 15 1.054580E-01 2.607250E+00 1096 16 1.129900E-01 2.603480E+00 1096 17 1.205230E-01 2.599450E+00 1096 18 1.280560E-01 2.595170E+00 1096 19 1.355890E-01 2.590640E+00 1096 20 1.431210E-01 2.585860E+00 1096 21 1.506540E-01 2.580830E+00 1096 22 1.581870E-01 2.575550E+00 1096 23 1.657190E-01 2.570040E+00 1096 24 1.732520E-01 2.564280E+00 1096 25 1.807850E-01 2.558280E+00 1096 26 1.883170E-01 2.552040E+00 1096 27 1.958500E-01 2.545560E+00 1096 28 2.033830E-01 2.538850E+00 1096 29 2.109160E-01 2.531910E+00 1096 30 2.156090E-01 2.527470E+00 1096 31 2.203030E-01 2.522940E+00 1096 32 2.249960E-01 2.518330E+00 1096 33 2.296900E-01 2.513620E+00 1096 34 2.343830E-01 2.508830E+00 1096 35 2.390770E-01 2.503950E+00 1096 36 2.437700E-01 2.498990E+00 1096 37 2.484640E-01 2.493940E+00 1096 38 2.531570E-01 2.488810E+00 1096 39 2.578510E-01 2.483590E+00 1096 40 2.625440E-01 2.478290E+00 1096 41 2.672380E-01 2.472910E+00 1096 42 2.719310E-01 2.467450E+00 1096 43 2.766250E-01 2.461910E+00 1096 44 2.813180E-01 2.456280E+00 1096 45 2.860120E-01 2.450580E+00 1096 46 2.907050E-01 2.444790E+00 1096 47 2.953990E-01 2.438930E+00 1096 48 3.000920E-01 2.433000E+00 1096 49 3.047860E-01 2.426980E+00 1096 50 3.094790E-01 2.420890E+00 1096 51 3.141730E-01 2.414720E+00 1096 52 3.188660E-01 2.408480E+00 1096 53 3.235600E-01 2.402170E+00 1096 54 3.282530E-01 2.395780E+00 1096 55 3.329470E-01 2.389320E+00 1096 56 3.376400E-01 2.382790E+00 1096 57 3.423340E-01 2.376190E+00 1096 58 3.470270E-01 2.369520E+00 1096 59 3.517210E-01 2.362780E+00 1096 60 3.564140E-01 2.355970E+00 1096 61 3.611080E-01 2.349090E+00 1096 62 3.658010E-01 2.342150E+00 1096 63 3.704950E-01 2.335140E+00 1096 64 3.751880E-01 2.328070E+00 1096 65 3.798820E-01 2.320930E+00 1096 66 3.845750E-01 2.313730E+00 1096 67 3.892690E-01 2.306470E+00 1096 68 3.939620E-01 2.299150E+00 1096 69 3.986560E-01 2.291760E+00 1096 70 4.033490E-01 2.284320E+00 1096 71 4.080430E-01 2.276810E+00 1096 72 4.127360E-01 2.269250E+00 1096 73 4.174300E-01 2.261630E+00 1096 74 4.221230E-01 2.253960E+00 1096 75 4.268170E-01 2.246220E+00 1096 76 4.315100E-01 2.238440E+00 1096 77 4.362040E-01 2.230600E+00 1096 78 4.408970E-01 2.222700E+00 1096 79 4.455910E-01 2.214760E+00 1096 80 4.502840E-01 2.206760E+00 1096 81 4.549780E-01 2.198710E+00 1096 82 4.596710E-01 2.190620E+00 1096 83 4.643650E-01 2.182470E+00 1096 84 4.690580E-01 2.174280E+00 1096 85 4.737520E-01 2.166040E+00 1096 86 4.784460E-01 2.157760E+00 1096 87 4.831390E-01 2.149430E+00 1096 88 4.878330E-01 2.141050E+00 1096 89 4.925260E-01 2.132640E+00 1096 90 4.972190E-01 2.124180E+00 1096 91 5.019130E-01 2.115680E+00 1096 92 5.066060E-01 2.107130E+00 1096 93 5.113000E-01 2.098550E+00 1096 94 5.159930E-01 2.089930E+00 1096 95 5.206870E-01 2.081280E+00 1096 96 5.253810E-01 2.072580E+00 1096 97 5.300740E-01 2.063850E+00 1096 98 5.347680E-01 2.055090E+00 1096 99 5.394610E-01 2.046290E+00 1096 100 5.441550E-01 2.037450E+00 1096 101 5.488480E-01 2.028590E+00 1096 102 5.535420E-01 2.019690E+00 1096 103 5.582350E-01 2.010760E+00 1096 104 5.629290E-01 2.001810E+00 1096 105 5.676220E-01 1.992820E+00 1096 106 5.723160E-01 1.983810E+00 1096 107 5.770090E-01 1.974760E+00 1096 108 5.817030E-01 1.965700E+00 1096 109 5.863960E-01 1.956600E+00 1096 110 5.910900E-01 1.947490E+00 1096 111 5.957830E-01 1.938340E+00 1096 112 6.004770E-01 1.929180E+00 1096 113 6.051700E-01 1.919990E+00 1096 114 6.098640E-01 1.910790E+00 1096 115 6.145570E-01 1.901560E+00 1096 116 6.192510E-01 1.892310E+00 1096 117 6.239440E-01 1.883050E+00 1096 118 6.286380E-01 1.873760E+00 1096 119 6.333310E-01 1.864460E+00 1096 120 6.380250E-01 1.855150E+00 1096 121 6.427180E-01 1.845820E+00 1096 122 6.474120E-01 1.836470E+00 1096 123 6.521050E-01 1.827110E+00 1096 124 6.567990E-01 1.817740E+00 1096 125 6.614920E-01 1.808360E+00 1096 126 6.661860E-01 1.798960E+00 1096 127 6.708790E-01 1.789560E+00 1096 128 6.755730E-01 1.780140E+00 1096 129 6.802660E-01 1.770720E+00 1096 130 6.849600E-01 1.761290E+00 1096 131 6.896530E-01 1.751850E+00 1096 132 6.943470E-01 1.742400E+00 1096 133 6.990400E-01 1.732950E+00 1096 134 7.037340E-01 1.723500E+00 1096 135 7.084270E-01 1.714040E+00 1096 136 7.131210E-01 1.704580E+00 1096 137 7.178140E-01 1.695110E+00 1096 138 7.225080E-01 1.685650E+00 1096 139 7.272010E-01 1.676180E+00 1096 140 7.318950E-01 1.666710E+00 1096 141 7.365880E-01 1.657240E+00 1096 142 7.412820E-01 1.647780E+00 1096 143 7.459750E-01 1.638310E+00 1096 144 7.506690E-01 1.628850E+00 1096 145 7.553620E-01 1.619390E+00 1096 146 7.600560E-01 1.609930E+00 1096 147 7.647490E-01 1.600480E+00 1096 148 7.694430E-01 1.591040E+00 1096 149 7.741360E-01 1.581600E+00 1096 150 7.788300E-01 1.572170E+00 1096 151 7.835230E-01 1.562740E+00 1096 152 7.882170E-01 1.553330E+00 1096 153 7.929100E-01 1.543920E+00 1096 154 7.976040E-01 1.534520E+00 1096 155 8.022970E-01 1.525130E+00 1096 156 8.069910E-01 1.515750E+00 1096 157 8.116850E-01 1.506380E+00 1096 158 8.163780E-01 1.497030E+00 1096 159 8.210710E-01 1.487680E+00 1096 160 8.257650E-01 1.478350E+00 1096 161 8.304580E-01 1.469030E+00 1096 162 8.351520E-01 1.459730E+00 1096 163 8.398460E-01 1.450440E+00 1096 164 8.445390E-01 1.441170E+00 1096 165 8.492320E-01 1.431910E+00 1096 166 8.539260E-01 1.422670E+00 1096 167 8.586200E-01 1.413450E+00 1096 168 8.633130E-01 1.404240E+00 1096 169 8.680070E-01 1.395050E+00 1096 170 8.727000E-01 1.385880E+00 1096 171 8.773940E-01 1.376730E+00 1096 172 8.820870E-01 1.367600E+00 1096 173 8.867810E-01 1.358490E+00 1096 174 8.914740E-01 1.349400E+00 1096 175 8.961680E-01 1.340330E+00 1096 176 9.008610E-01 1.331290E+00 1096 177 9.055550E-01 1.322260E+00 1096 178 9.102480E-01 1.313260E+00 1096 179 9.149420E-01 1.304280E+00 1096 180 9.196350E-01 1.295320E+00 1096 181 9.243290E-01 1.286390E+00 1096 182 9.290220E-01 1.277480E+00 1096 183 9.337160E-01 1.268590E+00 1096 184 9.384090E-01 1.259740E+00 1096 185 9.431030E-01 1.250900E+00 1096 186 9.477960E-01 1.242100E+00 1096 187 9.524900E-01 1.233320E+00 1096 188 9.571830E-01 1.224560E+00 1096 189 9.618770E-01 1.215840E+00 1096 190 9.665700E-01 1.207140E+00 1096 191 9.712640E-01 1.198470E+00 1096 192 9.759570E-01 1.189820E+00 1096 193 9.806510E-01 1.181210E+00 1096 194 9.853440E-01 1.172620E+00 1096 195 9.900380E-01 1.164070E+00 1096 196 9.947310E-01 1.155540E+00 1096 197 9.994250E-01 1.147050E+00 1096 198 1.004120E+00 1.138580E+00 1096 199 1.008810E+00 1.130150E+00 1096 200 1.013510E+00 1.121740E+00 1096 201 1.018200E+00 1.113370E+00 1096 202 1.022890E+00 1.105030E+00 1096 203 1.027590E+00 1.096720E+00 1096 204 1.032280E+00 1.088440E+00 1096 205 1.036970E+00 1.080200E+00 1096 206 1.041670E+00 1.071990E+00 1096 207 1.046360E+00 1.063810E+00 1096 208 1.051050E+00 1.055670E+00 1096 209 1.055750E+00 1.047550E+00 1096 210 1.060440E+00 1.039480E+00 1096 211 1.065130E+00 1.031430E+00 1096 212 1.069830E+00 1.023420E+00 1096 213 1.074520E+00 1.015450E+00 1096 214 1.079220E+00 1.007510E+00 1096 215 1.083910E+00 9.996050E-01 1096 216 1.088600E+00 9.917340E-01 1096 217 1.093290E+00 9.839010E-01 1096 218 1.097990E+00 9.761020E-01 1096 219 1.102680E+00 9.683400E-01 1096 220 1.107380E+00 9.606120E-01 1096 221 1.112070E+00 9.529230E-01 1096 222 1.116760E+00 9.452680E-01 1096 223 1.121460E+00 9.376510E-01 1096 224 1.126150E+00 9.300710E-01 1096 225 1.130840E+00 9.225260E-01 1096 226 1.135540E+00 9.150180E-01 1096 227 1.140230E+00 9.075490E-01 1096 228 1.144920E+00 9.001160E-01 1096 229 1.149620E+00 8.927220E-01 1096 230 1.154310E+00 8.853640E-01 1096 231 1.159000E+00 8.780450E-01 1096 232 1.163700E+00 8.707630E-01 1096 233 1.168390E+00 8.635200E-01 1096 234 1.173080E+00 8.563140E-01 1096 235 1.177780E+00 8.491470E-01 1096 236 1.182470E+00 8.420180E-01 1096 237 1.187170E+00 8.349280E-01 1096 238 1.191860E+00 8.278760E-01 1096 239 1.196550E+00 8.208640E-01 1096 240 1.201250E+00 8.138890E-01 1096 241 1.205940E+00 8.069540E-01 1096 242 1.210630E+00 8.000570E-01 1096 243 1.215330E+00 7.932010E-01 1096 244 1.220020E+00 7.863820E-01 1096 245 1.224710E+00 7.796030E-01 1096 246 1.229410E+00 7.728630E-01 1096 247 1.234100E+00 7.661630E-01 1096 248 1.238790E+00 7.595010E-01 1096 249 1.243490E+00 7.528810E-01 1096 250 1.248180E+00 7.462980E-01 1096 251 1.252870E+00 7.397560E-01 1096 252 1.257570E+00 7.332520E-01 1096 253 1.262260E+00 7.267900E-01 1096 254 1.266960E+00 7.203670E-01 1096 255 1.271650E+00 7.139820E-01 1096 256 1.276340E+00 7.076370E-01 1096 257 1.281030E+00 7.013340E-01 1096 258 1.285730E+00 6.950680E-01 1096 259 1.290420E+00 6.888440E-01 1096 260 1.295120E+00 6.826590E-01 1096 261 1.299810E+00 6.765150E-01 1096 262 1.304500E+00 6.704090E-01 1096 263 1.309200E+00 6.643440E-01 1096 264 1.313890E+00 6.583180E-01 1096 265 1.318580E+00 6.523330E-01 1096 266 1.323280E+00 6.463870E-01 1096 267 1.327970E+00 6.404820E-01 1096 268 1.332660E+00 6.346160E-01 1096 269 1.337360E+00 6.287910E-01 1096 270 1.342050E+00 6.230050E-01 1096 271 1.346740E+00 6.172590E-01 1096 272 1.351440E+00 6.115520E-01 1096 273 1.356130E+00 6.058870E-01 1096 274 1.360820E+00 6.002600E-01 1096 275 1.365520E+00 5.946740E-01 1096 276 1.370210E+00 5.891270E-01 1096 277 1.374910E+00 5.836200E-01 1096 278 1.379600E+00 5.781520E-01 1096 279 1.384290E+00 5.727250E-01 1096 280 1.388990E+00 5.673370E-01 1096 281 1.393680E+00 5.619890E-01 1096 282 1.398370E+00 5.566800E-01 1096 283 1.403070E+00 5.514120E-01 1096 284 1.407760E+00 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712 3.416580E+00 1.493870E-01 1096 713 3.421280E+00 1.492080E-01 1096 714 3.425970E+00 1.490280E-01 1096 715 3.430660E+00 1.488480E-01 1096 716 3.435350E+00 1.486670E-01 1096 717 3.440050E+00 1.484860E-01 1096 718 3.444740E+00 1.483040E-01 1096 719 3.449440E+00 1.481210E-01 1096 720 3.454130E+00 1.479380E-01 1096 721 3.458820E+00 1.477540E-01 1096 722 3.463520E+00 1.475700E-01 1096 723 3.468210E+00 1.473850E-01 1096 724 3.472900E+00 1.471990E-01 1096 725 3.477600E+00 1.470130E-01 1096 726 3.482290E+00 1.468270E-01 1096 727 3.486980E+00 1.466390E-01 1096 728 3.491680E+00 1.464510E-01 1096 729 3.496370E+00 1.462630E-01 1096 730 3.501060E+00 1.460740E-01 1096 731 3.505760E+00 1.458840E-01 1096 732 3.510450E+00 1.456940E-01 1096 733 3.515140E+00 1.455030E-01 1096 734 3.519840E+00 1.453120E-01 1096 735 3.524530E+00 1.451190E-01 1096 736 3.529220E+00 1.449270E-01 1096 737 3.533920E+00 1.447340E-01 1096 738 3.538610E+00 1.445400E-01 1096 739 3.543310E+00 1.443450E-01 1096 740 3.548000E+00 1.441500E-01 1096 741 3.552690E+00 1.439540E-01 1096 742 3.557390E+00 1.437580E-01 1096 743 3.562080E+00 1.435610E-01 1096 744 3.566770E+00 1.433630E-01 1096 745 3.571470E+00 1.431650E-01 1096 746 3.576160E+00 1.429660E-01 1096 747 3.580850E+00 1.427660E-01 1096 748 3.585550E+00 1.425660E-01 1096 749 3.590240E+00 1.423650E-01 1096 750 3.594930E+00 1.421630E-01 1096 751 3.599630E+00 1.419610E-01 1096 752 3.604320E+00 1.417580E-01 1096 753 3.609010E+00 1.415540E-01 1096 754 3.613710E+00 1.413500E-01 1096 755 3.618400E+00 1.411450E-01 1096 756 3.623100E+00 1.409390E-01 1096 757 3.627790E+00 1.407320E-01 1096 758 3.632480E+00 1.405250E-01 1096 759 3.637180E+00 1.403170E-01 1096 760 3.641870E+00 1.401090E-01 1096 761 3.646560E+00 1.398990E-01 1096 762 3.651260E+00 1.396890E-01 1096 763 3.655950E+00 1.394780E-01 1096 764 3.660640E+00 1.392670E-01 1096 765 3.665340E+00 1.390540E-01 1096 766 3.670030E+00 1.388410E-01 1096 767 3.674720E+00 1.386280E-01 1096 768 3.679420E+00 1.384130E-01 1096 769 3.684110E+00 1.381980E-01 1096 770 3.688800E+00 1.379820E-01 1096 771 3.693500E+00 1.377650E-01 1096 772 3.698190E+00 1.375470E-01 1096 773 3.702890E+00 1.373290E-01 1096 774 3.707580E+00 1.371090E-01 1096 775 3.712270E+00 1.368890E-01 1096 776 3.716970E+00 1.366690E-01 1096 777 3.721660E+00 1.364470E-01 1096 778 3.726350E+00 1.362250E-01 1096 779 3.731050E+00 1.360020E-01 1096 780 3.735740E+00 1.357780E-01 1096 781 3.740430E+00 1.355530E-01 1096 782 3.745130E+00 1.353270E-01 1096 783 3.749820E+00 1.351010E-01 1096 784 3.754510E+00 1.348740E-01 1096 785 3.759210E+00 1.346460E-01 1096 786 3.763900E+00 1.344170E-01 1096 787 3.768590E+00 1.341880E-01 1096 788 3.773290E+00 1.339570E-01 1096 789 3.777980E+00 1.337260E-01 1096 790 3.782670E+00 1.334940E-01 1096 791 3.787370E+00 1.332610E-01 # data_SASDE94_FIT_1705 # _sas_model_fitting_details.id 1705 _sas_model_fitting_details.unit 1/A _sas_model_fitting_details.chi_square 1.18 _sas_model_fitting_details.p_value 0.389658 _sas_model_fitting_details.result_id 1096 # loop_ _sas_model_fitting.id _sas_model_fitting.ordinal _sas_model_fitting.momentum_transfer _sas_model_fitting.intensity _sas_model_fitting.fit 1705 1 1.687000E-02 2.544000E+00 2.541000E+00 1705 2 1.734000E-02 2.551000E+00 2.538000E+00 1705 3 1.781000E-02 2.326000E+00 2.534000E+00 1705 4 1.828000E-02 2.556000E+00 2.531000E+00 1705 5 1.874000E-02 2.462000E+00 2.527000E+00 1705 6 1.921000E-02 2.708000E+00 2.524000E+00 1705 7 1.968000E-02 2.332000E+00 2.520000E+00 1705 8 2.015000E-02 2.493000E+00 2.516000E+00 1705 9 2.062000E-02 2.568000E+00 2.512000E+00 1705 10 2.109000E-02 2.426000E+00 2.508000E+00 1705 11 2.156000E-02 2.514000E+00 2.504000E+00 1705 12 2.203000E-02 2.505000E+00 2.500000E+00 1705 13 2.250000E-02 2.464000E+00 2.496000E+00 1705 14 2.297000E-02 2.350000E+00 2.491000E+00 1705 15 2.344000E-02 2.506000E+00 2.487000E+00 1705 16 2.391000E-02 2.478000E+00 2.483000E+00 1705 17 2.438000E-02 2.550000E+00 2.478000E+00 1705 18 2.485000E-02 2.526000E+00 2.474000E+00 1705 19 2.532000E-02 2.318000E+00 2.469000E+00 1705 20 2.579000E-02 2.460000E+00 2.464000E+00 1705 21 2.625000E-02 2.578000E+00 2.459000E+00 1705 22 2.672000E-02 2.378000E+00 2.454000E+00 1705 23 2.719000E-02 2.450000E+00 2.449000E+00 1705 24 2.766000E-02 2.426000E+00 2.444000E+00 1705 25 2.813000E-02 2.366000E+00 2.439000E+00 1705 26 2.860000E-02 2.594000E+00 2.434000E+00 1705 27 2.907000E-02 2.493000E+00 2.428000E+00 1705 28 2.954000E-02 2.407000E+00 2.423000E+00 1705 29 3.001000E-02 2.424000E+00 2.418000E+00 1705 30 3.048000E-02 2.433000E+00 2.412000E+00 1705 31 3.095000E-02 2.393000E+00 2.406000E+00 1705 32 3.142000E-02 2.477000E+00 2.400000E+00 1705 33 3.189000E-02 2.340000E+00 2.395000E+00 1705 34 3.236000E-02 2.490000E+00 2.389000E+00 1705 35 3.283000E-02 2.459000E+00 2.383000E+00 1705 36 3.329000E-02 2.379000E+00 2.377000E+00 1705 37 3.376000E-02 2.310000E+00 2.371000E+00 1705 38 3.423000E-02 2.446000E+00 2.365000E+00 1705 39 3.470000E-02 2.391000E+00 2.359000E+00 1705 40 3.517000E-02 2.442000E+00 2.353000E+00 1705 41 3.564000E-02 2.361000E+00 2.346000E+00 1705 42 3.611000E-02 2.494000E+00 2.340000E+00 1705 43 3.658000E-02 2.324000E+00 2.333000E+00 1705 44 3.705000E-02 2.356000E+00 2.327000E+00 1705 45 3.752000E-02 2.369000E+00 2.320000E+00 1705 46 3.799000E-02 2.233000E+00 2.314000E+00 1705 47 3.846000E-02 2.284000E+00 2.307000E+00 1705 48 3.893000E-02 2.402000E+00 2.300000E+00 1705 49 3.940000E-02 2.388000E+00 2.293000E+00 1705 50 3.987000E-02 2.285000E+00 2.286000E+00 1705 51 4.033000E-02 2.223000E+00 2.279000E+00 1705 52 4.080000E-02 2.205000E+00 2.272000E+00 1705 53 4.127000E-02 2.334000E+00 2.265000E+00 1705 54 4.174000E-02 2.270000E+00 2.258000E+00 1705 55 4.221000E-02 2.293000E+00 2.251000E+00 1705 56 4.268000E-02 2.129000E+00 2.244000E+00 1705 57 4.315000E-02 2.177000E+00 2.236000E+00 1705 58 4.362000E-02 2.210000E+00 2.229000E+00 1705 59 4.409000E-02 2.200000E+00 2.222000E+00 1705 60 4.456000E-02 2.243000E+00 2.214000E+00 1705 61 4.503000E-02 2.359000E+00 2.207000E+00 1705 62 4.550000E-02 2.181000E+00 2.199000E+00 1705 63 4.597000E-02 2.130000E+00 2.191000E+00 1705 64 4.644000E-02 2.281000E+00 2.184000E+00 1705 65 4.691000E-02 2.261000E+00 2.176000E+00 1705 66 4.738000E-02 2.213000E+00 2.168000E+00 1705 67 4.784000E-02 2.122000E+00 2.160000E+00 1705 68 4.831000E-02 2.207000E+00 2.152000E+00 1705 69 4.878000E-02 1.964000E+00 2.144000E+00 1705 70 4.925000E-02 2.095000E+00 2.136000E+00 1705 71 4.972000E-02 1.991000E+00 2.129000E+00 1705 72 5.019000E-02 2.132000E+00 2.120000E+00 1705 73 5.066000E-02 2.038000E+00 2.112000E+00 1705 74 5.113000E-02 2.102000E+00 2.104000E+00 1705 75 5.160000E-02 1.980000E+00 2.096000E+00 1705 76 5.207000E-02 2.185000E+00 2.088000E+00 1705 77 5.254000E-02 2.099000E+00 2.079000E+00 1705 78 5.301000E-02 2.124000E+00 2.071000E+00 1705 79 5.348000E-02 2.176000E+00 2.063000E+00 1705 80 5.395000E-02 2.115000E+00 2.054000E+00 1705 81 5.442000E-02 1.963000E+00 2.046000E+00 1705 82 5.488000E-02 1.949000E+00 2.037000E+00 1705 83 5.535000E-02 2.033000E+00 2.029000E+00 1705 84 5.582000E-02 1.998000E+00 2.020000E+00 1705 85 5.629000E-02 1.884000E+00 2.012000E+00 1705 86 5.676000E-02 2.013000E+00 2.003000E+00 1705 87 5.723000E-02 1.936000E+00 1.994000E+00 1705 88 5.770000E-02 1.934000E+00 1.986000E+00 1705 89 5.817000E-02 1.994000E+00 1.977000E+00 1705 90 5.864000E-02 1.915000E+00 1.968000E+00 1705 91 5.911000E-02 1.846000E+00 1.959000E+00 1705 92 5.958000E-02 1.848000E+00 1.950000E+00 1705 93 6.005000E-02 1.957000E+00 1.942000E+00 1705 94 6.052000E-02 1.966000E+00 1.933000E+00 1705 95 6.099000E-02 2.060000E+00 1.924000E+00 1705 96 6.146000E-02 1.873000E+00 1.915000E+00 1705 97 6.193000E-02 2.026000E+00 1.906000E+00 1705 98 6.239000E-02 1.812000E+00 1.897000E+00 1705 99 6.286000E-02 1.886000E+00 1.888000E+00 1705 100 6.333000E-02 1.814000E+00 1.879000E+00 1705 101 6.380000E-02 1.837000E+00 1.870000E+00 1705 102 6.427000E-02 1.797000E+00 1.861000E+00 1705 103 6.474000E-02 1.871000E+00 1.852000E+00 1705 104 6.521000E-02 1.868000E+00 1.842000E+00 1705 105 6.568000E-02 1.893000E+00 1.833000E+00 1705 106 6.615000E-02 1.855000E+00 1.824000E+00 1705 107 6.662000E-02 1.822000E+00 1.815000E+00 1705 108 6.709000E-02 1.774000E+00 1.806000E+00 1705 109 6.756000E-02 1.802000E+00 1.796000E+00 1705 110 6.803000E-02 1.857000E+00 1.787000E+00 1705 111 6.850000E-02 1.777000E+00 1.778000E+00 1705 112 6.897000E-02 1.788000E+00 1.769000E+00 1705 113 6.943000E-02 1.640000E+00 1.759000E+00 1705 114 6.990000E-02 1.690000E+00 1.750000E+00 1705 115 7.037000E-02 1.705000E+00 1.741000E+00 1705 116 7.084000E-02 1.796000E+00 1.731000E+00 1705 117 7.131000E-02 1.777000E+00 1.722000E+00 1705 118 7.178000E-02 1.654000E+00 1.713000E+00 1705 119 7.225000E-02 1.692000E+00 1.703000E+00 1705 120 7.272000E-02 1.800000E+00 1.694000E+00 1705 121 7.319000E-02 1.688000E+00 1.684000E+00 1705 122 7.366000E-02 1.627000E+00 1.675000E+00 1705 123 7.413000E-02 1.666000E+00 1.666000E+00 1705 124 7.460000E-02 1.545000E+00 1.656000E+00 1705 125 7.507000E-02 1.650000E+00 1.647000E+00 1705 126 7.554000E-02 1.680000E+00 1.637000E+00 1705 127 7.601000E-02 1.652000E+00 1.628000E+00 1705 128 7.647000E-02 1.668000E+00 1.618000E+00 1705 129 7.694000E-02 1.536000E+00 1.609000E+00 1705 130 7.741000E-02 1.599000E+00 1.600000E+00 1705 131 7.788000E-02 1.543000E+00 1.590000E+00 1705 132 7.835000E-02 1.592000E+00 1.581000E+00 1705 133 7.882000E-02 1.565000E+00 1.571000E+00 1705 134 7.929000E-02 1.571000E+00 1.562000E+00 1705 135 7.976000E-02 1.563000E+00 1.552000E+00 1705 136 8.023000E-02 1.514000E+00 1.543000E+00 1705 137 8.070000E-02 1.457000E+00 1.533000E+00 1705 138 8.117000E-02 1.484000E+00 1.524000E+00 1705 139 8.164000E-02 1.482000E+00 1.515000E+00 1705 140 8.211000E-02 1.462000E+00 1.505000E+00 1705 141 8.258000E-02 1.419000E+00 1.496000E+00 1705 142 8.305000E-02 1.424000E+00 1.486000E+00 1705 143 8.352000E-02 1.282000E+00 1.477000E+00 1705 144 8.398000E-02 1.468000E+00 1.467000E+00 1705 145 8.445000E-02 1.407000E+00 1.458000E+00 1705 146 8.492000E-02 1.399000E+00 1.449000E+00 1705 147 8.539000E-02 1.443000E+00 1.439000E+00 1705 148 8.586000E-02 1.482000E+00 1.430000E+00 1705 149 8.633000E-02 1.435000E+00 1.421000E+00 1705 150 8.680000E-02 1.310000E+00 1.411000E+00 1705 151 8.727000E-02 1.223000E+00 1.402000E+00 1705 152 8.774000E-02 1.358000E+00 1.392000E+00 1705 153 8.821000E-02 1.386000E+00 1.383000E+00 1705 154 8.868000E-02 1.372000E+00 1.374000E+00 1705 155 8.915000E-02 1.365000E+00 1.365000E+00 1705 156 8.962000E-02 1.331000E+00 1.355000E+00 1705 157 9.009000E-02 1.411000E+00 1.346000E+00 1705 158 9.056000E-02 1.301000E+00 1.337000E+00 1705 159 9.102000E-02 1.320000E+00 1.328000E+00 1705 160 9.149000E-02 1.274000E+00 1.318000E+00 1705 161 9.196000E-02 1.249000E+00 1.309000E+00 1705 162 9.243000E-02 1.394000E+00 1.300000E+00 1705 163 9.290000E-02 1.279000E+00 1.291000E+00 1705 164 9.337000E-02 1.284000E+00 1.282000E+00 1705 165 9.384000E-02 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3.764000E-01 2.176000E-01 1.496000E-01 1705 768 3.769000E-01 1.152000E-01 1.495000E-01 1705 769 3.773000E-01 2.090000E-01 1.495000E-01 1705 770 3.778000E-01 1.420000E-01 1.494000E-01 1705 771 3.783000E-01 1.315000E-01 1.494000E-01 1705 772 3.787000E-01 2.709000E-01 1.493000E-01 1705 773 3.792000E-01 1.107000E-01 1.493000E-01 1705 774 3.797000E-01 2.324000E-01 1.492000E-01 1705 775 3.801000E-01 9.879000E-02 1.492000E-01 1705 776 3.806000E-01 1.004000E-01 1.492000E-01 1705 777 3.811000E-01 1.338000E-01 1.491000E-01 1705 778 3.816000E-01 5.912000E-02 1.491000E-01 1705 779 3.820000E-01 1.332000E-01 1.490000E-01 1705 780 3.825000E-01 1.615000E-01 1.490000E-01 1705 781 3.830000E-01 1.520000E-01 1.490000E-01 1705 782 3.834000E-01 1.859000E-01 1.489000E-01 1705 783 3.839000E-01 8.129000E-02 1.489000E-01 1705 784 3.844000E-01 1.245000E-01 1.489000E-01 1705 785 3.848000E-01 1.458000E-01 1.488000E-01 1705 786 3.853000E-01 8.013000E-02 1.488000E-01 1705 787 3.858000E-01 8.679000E-02 1.488000E-01 1705 788 3.862000E-01 1.160000E-01 1.487000E-01 1705 789 3.867000E-01 2.646000E-01 1.487000E-01 1705 790 3.872000E-01 1.128000E-01 1.487000E-01 1705 791 3.877000E-01 1.629000E-01 1.487000E-01 1705 792 3.881000E-01 1.174000E-01 1.486000E-01 1705 793 3.886000E-01 1.842000E-01 1.486000E-01 1705 794 3.891000E-01 9.862000E-02 1.486000E-01 1705 795 3.895000E-01 1.993000E-01 1.486000E-01 1705 796 3.900000E-01 1.879000E-01 1.485000E-01 1705 797 3.905000E-01 1.030000E-01 1.485000E-01 1705 798 3.909000E-01 2.338000E-01 1.485000E-01 1705 799 3.914000E-01 1.939000E-01 1.485000E-01 1705 800 3.919000E-01 2.033000E-01 1.484000E-01 1705 801 3.923000E-01 1.413000E-01 1.484000E-01 1705 802 3.928000E-01 1.484000E-01 1.484000E-01 1705 803 3.933000E-01 2.460000E-01 1.484000E-01 1705 804 3.938000E-01 1.387000E-01 1.484000E-01 1705 805 3.942000E-01 1.109000E-01 1.484000E-01 1705 806 3.947000E-01 9.595000E-02 1.483000E-01 1705 807 3.952000E-01 1.247000E-01 1.483000E-01 1705 808 3.956000E-01 1.655000E-01 1.483000E-01 1705 809 3.961000E-01 1.348000E-01 1.483000E-01 1705 810 3.966000E-01 1.203000E-01 1.483000E-01 1705 811 3.970000E-01 8.637000E-02 1.483000E-01 1705 812 3.975000E-01 1.815000E-01 1.483000E-01 1705 813 3.980000E-01 1.588000E-01 1.483000E-01 1705 814 3.984000E-01 1.586000E-01 1.483000E-01 1705 815 3.989000E-01 1.614000E-01 1.482000E-01 1705 816 3.994000E-01 1.627000E-01 1.482000E-01 1705 817 3.999000E-01 9.956000E-02 1.482000E-01 1705 818 4.003000E-01 1.045000E-01 1.482000E-01 1705 819 4.008000E-01 2.052000E-01 1.482000E-01 1705 820 4.013000E-01 1.193000E-01 1.482000E-01 1705 821 4.017000E-01 1.764000E-01 1.482000E-01 1705 822 4.022000E-01 2.043000E-01 1.482000E-01 1705 823 4.027000E-01 7.897000E-02 1.482000E-01 1705 824 4.031000E-01 1.281000E-01 1.482000E-01 1705 825 4.036000E-01 2.044000E-01 1.482000E-01 1705 826 4.041000E-01 9.236000E-02 1.482000E-01 1705 827 4.046000E-01 1.350000E-01 1.482000E-01 1705 828 4.050000E-01 1.547000E-01 1.482000E-01 1705 829 4.055000E-01 1.771000E-01 1.482000E-01 1705 830 4.060000E-01 1.601000E-01 1.482000E-01 1705 831 4.064000E-01 1.325000E-01 1.482000E-01 1705 832 4.069000E-01 -1.271000E-02 1.482000E-01 1705 833 4.074000E-01 1.460000E-01 1.482000E-01 1705 834 4.078000E-01 1.236000E-01 1.482000E-01 1705 835 4.083000E-01 1.368000E-01 1.482000E-01 1705 836 4.088000E-01 1.426000E-01 1.482000E-01 1705 837 4.092000E-01 1.082000E-01 1.483000E-01 1705 838 4.097000E-01 3.238000E-01 1.483000E-01 1705 839 4.102000E-01 1.343000E-01 1.483000E-01 1705 840 4.107000E-01 2.035000E-01 1.483000E-01 1705 841 4.111000E-01 6.413000E-02 1.483000E-01 1705 842 4.116000E-01 1.098000E-01 1.483000E-01 1705 843 4.121000E-01 1.017000E-01 1.483000E-01 1705 844 4.125000E-01 9.662000E-02 1.483000E-01 1705 845 4.130000E-01 1.687000E-01 1.483000E-01 1705 846 4.135000E-01 1.954000E-01 1.483000E-01 1705 847 4.139000E-01 1.523000E-01 1.484000E-01 1705 848 4.144000E-01 1.962000E-01 1.484000E-01 1705 849 4.149000E-01 1.561000E-01 1.484000E-01 1705 850 4.153000E-01 1.384000E-01 1.484000E-01 1705 851 4.158000E-01 1.257000E-01 1.484000E-01 1705 852 4.163000E-01 2.703000E-01 1.484000E-01 1705 853 4.168000E-01 1.762000E-01 1.484000E-01 1705 854 4.172000E-01 1.583000E-01 1.485000E-01 1705 855 4.177000E-01 1.585000E-01 1.485000E-01 1705 856 4.182000E-01 9.686000E-02 1.485000E-01 1705 857 4.186000E-01 2.006000E-01 1.485000E-01 1705 858 4.191000E-01 1.589000E-01 1.485000E-01 1705 859 4.196000E-01 1.295000E-01 1.485000E-01 1705 860 4.200000E-01 1.475000E-01 1.486000E-01 1705 861 4.205000E-01 7.253000E-02 1.486000E-01 1705 862 4.210000E-01 7.763000E-02 1.486000E-01 1705 863 4.214000E-01 1.574000E-01 1.486000E-01 1705 864 4.219000E-01 2.455000E-01 1.486000E-01 1705 865 4.224000E-01 7.117000E-02 1.486000E-01 1705 866 4.229000E-01 2.448000E-01 1.487000E-01 1705 867 4.233000E-01 2.803000E-01 1.487000E-01 1705 868 4.238000E-01 8.726000E-02 1.487000E-01 1705 869 4.243000E-01 1.438000E-01 1.487000E-01 1705 870 4.247000E-01 1.328000E-01 1.488000E-01 1705 871 4.252000E-01 2.189000E-01 1.488000E-01 1705 872 4.257000E-01 2.176000E-01 1.488000E-01 1705 873 4.261000E-01 1.286000E-01 1.488000E-01 1705 874 4.266000E-01 3.213000E-01 1.488000E-01 1705 875 4.271000E-01 2.029000E-01 1.489000E-01 1705 876 4.275000E-01 1.911000E-01 1.489000E-01 1705 877 4.280000E-01 1.724000E-01 1.489000E-01 1705 878 4.285000E-01 1.393000E-01 1.489000E-01 1705 879 4.290000E-01 1.062000E-01 1.490000E-01 1705 880 4.294000E-01 2.508000E-01 1.490000E-01 1705 881 4.299000E-01 2.220000E-01 1.490000E-01 1705 882 4.304000E-01 1.695000E-01 1.490000E-01 1705 883 4.308000E-01 5.982000E-02 1.490000E-01 1705 884 4.313000E-01 1.586000E-01 1.491000E-01 1705 885 4.318000E-01 1.471000E-01 1.491000E-01 1705 886 4.322000E-01 2.353000E-01 1.491000E-01 1705 887 4.327000E-01 1.642000E-01 1.491000E-01 1705 888 4.332000E-01 8.582000E-02 1.492000E-01 1705 889 4.337000E-01 1.702000E-01 1.492000E-01 1705 890 4.341000E-01 1.162000E-01 1.492000E-01 1705 891 4.346000E-01 2.401000E-01 1.492000E-01 1705 892 4.351000E-01 7.728000E-02 1.493000E-01 1705 893 4.355000E-01 3.899000E-02 1.493000E-01 1705 894 4.360000E-01 1.863000E-01 1.493000E-01 1705 895 4.365000E-01 4.241000E-02 1.494000E-01 1705 896 4.369000E-01 2.098000E-01 1.494000E-01 1705 897 4.374000E-01 1.285000E-01 1.494000E-01 1705 898 4.379000E-01 7.166000E-02 1.494000E-01 1705 899 4.383000E-01 1.582000E-01 1.495000E-01 1705 900 4.388000E-01 2.558000E-01 1.495000E-01 1705 901 4.393000E-01 2.577000E-01 1.495000E-01 1705 902 4.398000E-01 1.073000E-01 1.495000E-01 1705 903 4.402000E-01 1.553000E-01 1.496000E-01 1705 904 4.407000E-01 2.255000E-01 1.496000E-01 1705 905 4.412000E-01 1.484000E-01 1.496000E-01 1705 906 4.416000E-01 1.120000E-01 1.496000E-01 1705 907 4.421000E-01 1.454000E-01 1.497000E-01 1705 908 4.426000E-01 2.465000E-01 1.497000E-01 1705 909 4.430000E-01 1.441000E-01 1.497000E-01 1705 910 4.435000E-01 1.719000E-01 1.497000E-01 1705 911 4.440000E-01 6.829000E-02 1.498000E-01 1705 912 4.444000E-01 1.170000E-01 1.498000E-01 1705 913 4.449000E-01 2.060000E-01 1.498000E-01 1705 914 4.454000E-01 7.942000E-03 1.499000E-01 1705 915 4.459000E-01 2.194000E-01 1.499000E-01 1705 916 4.463000E-01 5.942000E-02 1.499000E-01 1705 917 4.468000E-01 1.357000E-01 1.499000E-01 1705 918 4.473000E-01 2.703000E-01 1.500000E-01 1705 919 4.477000E-01 3.302000E-02 1.500000E-01 1705 920 4.482000E-01 1.912000E-01 1.500000E-01 1705 921 4.487000E-01 2.134000E-01 1.500000E-01 1705 922 4.491000E-01 9.196000E-02 1.501000E-01 1705 923 4.496000E-01 8.287000E-02 1.501000E-01 1705 924 4.501000E-01 2.655000E-02 1.501000E-01 1705 925 4.505000E-01 1.276000E-01 1.501000E-01 1705 926 4.510000E-01 1.669000E-01 1.502000E-01 1705 927 4.515000E-01 1.725000E-01 1.502000E-01 1705 928 4.520000E-01 5.504000E-02 1.502000E-01 1705 929 4.524000E-01 3.079000E-01 1.502000E-01 1705 930 4.529000E-01 2.291000E-01 1.503000E-01 1705 931 4.534000E-01 1.248000E-01 1.503000E-01 1705 932 4.538000E-01 6.531000E-02 1.503000E-01 1705 933 4.543000E-01 1.477000E-01 1.503000E-01 1705 934 4.548000E-01 9.188000E-02 1.504000E-01 1705 935 4.552000E-01 9.793000E-02 1.504000E-01 1705 936 4.557000E-01 1.953000E-01 1.504000E-01 1705 937 4.562000E-01 6.099000E-03 1.504000E-01 1705 938 4.566000E-01 1.240000E-01 1.505000E-01 1705 939 4.571000E-01 6.744000E-02 1.505000E-01 1705 940 4.576000E-01 2.310000E-01 1.505000E-01 1705 941 4.581000E-01 2.080000E-01 1.505000E-01 1705 942 4.585000E-01 1.441000E-01 1.506000E-01 1705 943 4.590000E-01 1.401000E-01 1.506000E-01 1705 944 4.595000E-01 1.092000E-01 1.506000E-01 1705 945 4.599000E-01 3.282000E-01 1.506000E-01 1705 946 4.604000E-01 1.997000E-01 1.506000E-01 1705 947 4.609000E-01 2.686000E-01 1.507000E-01 1705 948 4.613000E-01 1.946000E-01 1.507000E-01 1705 949 4.618000E-01 2.517000E-01 1.507000E-01 1705 950 4.623000E-01 1.230000E-01 1.507000E-01 1705 951 4.628000E-01 1.633000E-02 1.508000E-01 1705 952 4.632000E-01 2.239000E-01 1.508000E-01 1705 953 4.637000E-01 1.230000E-01 1.508000E-01 1705 954 4.642000E-01 1.053000E-01 1.508000E-01 1705 955 4.646000E-01 3.478000E-01 1.508000E-01 1705 956 4.651000E-01 1.931000E-01 1.509000E-01 1705 957 4.656000E-01 1.867000E-01 1.509000E-01 1705 958 4.660000E-01 9.047000E-02 1.509000E-01 1705 959 4.665000E-01 1.164000E-01 1.509000E-01 1705 960 4.670000E-01 1.055000E-01 1.509000E-01 1705 961 4.674000E-01 6.391000E-02 1.510000E-01 1705 962 4.679000E-01 3.391000E-01 1.510000E-01 1705 963 4.684000E-01 8.925000E-02 1.510000E-01 1705 964 4.689000E-01 1.920000E-01 1.510000E-01 1705 965 4.693000E-01 1.077000E-02 1.510000E-01 1705 966 4.698000E-01 2.081000E-01 1.511000E-01 1705 967 4.703000E-01 1.943000E-03 1.511000E-01 1705 968 4.707000E-01 7.304000E-02 1.511000E-01 1705 969 4.712000E-01 8.683000E-02 1.511000E-01 1705 970 4.717000E-01 1.748000E-01 1.511000E-01 1705 971 4.721000E-01 3.331000E-02 1.511000E-01 1705 972 4.726000E-01 2.610000E-01 1.512000E-01 1705 973 4.731000E-01 -4.774000E-02 1.512000E-01 1705 974 4.735000E-01 2.423000E-01 1.512000E-01 1705 975 4.740000E-01 2.274000E-01 1.512000E-01 1705 976 4.745000E-01 4.985000E-03 1.512000E-01 1705 977 4.750000E-01 4.271000E-02 1.512000E-01 1705 978 4.754000E-01 3.084000E-01 1.513000E-01 1705 979 4.759000E-01 3.363000E-01 1.513000E-01 1705 980 4.764000E-01 2.286000E-01 1.513000E-01 1705 981 4.768000E-01 3.435000E-01 1.513000E-01 1705 982 4.773000E-01 1.119000E-01 1.513000E-01 1705 983 4.778000E-01 1.820000E-01 1.513000E-01 1705 984 4.782000E-01 6.525000E-02 1.513000E-01 1705 985 4.787000E-01 3.979000E-01 1.514000E-01 1705 986 4.792000E-01 2.408000E-01 1.514000E-01 1705 987 4.796000E-01 2.266000E-01 1.514000E-01 1705 988 4.801000E-01 1.917000E-01 1.514000E-01 1705 989 4.806000E-01 1.418000E-01 1.514000E-01 1705 990 4.811000E-01 1.681000E-01 1.514000E-01 1705 991 4.815000E-01 1.942000E-01 1.514000E-01 1705 992 4.820000E-01 1.453000E-02 1.514000E-01 1705 993 4.825000E-01 3.394000E-01 1.514000E-01 1705 994 4.829000E-01 4.569000E-01 1.515000E-01 1705 995 4.834000E-01 2.705000E-01 1.515000E-01 1705 996 4.839000E-01 1.903000E-01 1.515000E-01 1705 997 4.843000E-01 9.882000E-02 1.515000E-01 1705 998 4.848000E-01 1.051000E-01 1.515000E-01 1705 999 4.853000E-01 3.287000E-01 1.515000E-01 1705 1000 4.857000E-01 1.414000E-01 1.515000E-01 1705 1001 4.862000E-01 2.303000E-01 1.515000E-01 1705 1002 4.867000E-01 2.399000E-01 1.515000E-01 1705 1003 4.872000E-01 1.382000E-01 1.515000E-01 1705 1004 4.876000E-01 2.291000E-01 1.516000E-01 1705 1005 4.881000E-01 5.139000E-01 1.516000E-01 1705 1006 4.886000E-01 2.451000E-01 1.516000E-01 1705 1007 4.890000E-01 1.587000E-01 1.516000E-01 1705 1008 4.895000E-01 7.470000E-01 1.516000E-01 1705 1009 4.900000E-01 3.810000E-02 1.516000E-01 1705 1010 4.904000E-01 -1.896000E-01 1.516000E-01 1705 1011 4.909000E-01 -8.559000E-01 1.516000E-01 1705 1012 4.914000E-01 -5.976000E-01 1.516000E-01 1705 1013 4.919000E-01 -2.514000E-01 1.516000E-01 1705 1014 4.923000E-01 6.434000E-01 1.516000E-01 1705 1015 4.928000E-01 3.130000E-01 1.516000E-01 # data_SASDE94_MODEL_2348 # _sas_model.id 2348 _sas_model.type_of_model atomic _sas_model.version . _sas_model.symmetry . _sas_model.comment . _sas_model.fitting_id 1705 _sas_model.radius . # loop_ _atom_site.group_PDB _atom_site.id _atom_site.type_symbol _atom_site.label_atom_id _atom_site.label_alt_id _atom_site.label_comp_id _atom_site.label_asym_id _atom_site.label_entity_id _atom_site.label_seq_id _atom_site.pdbx_PDB_ins_code _atom_site.Cartn_x _atom_site.Cartn_y _atom_site.Cartn_z _atom_site.occupancy _atom_site.B_iso_or_equiv _atom_site.Cartn_x_esd _atom_site.Cartn_y_esd _atom_site.Cartn_z_esd _atom_site.occupancy_esd _atom_site.B_iso_or_equiv_esd _atom_site.pdbx_formal_charge _atom_site.auth_seq_id _atom_site.auth_comp_id _atom_site.auth_asym_id _atom_site.auth_atom_id _atom_site.pdbx_PDB_model_num ATOM 1 N N . MET A 2348 1 . 1.498 -29.784 9.466 1.00 42.34 ? ? ? ? ? . 1 MET A N 2348 ATOM 2 C CA . MET A 2348 1 . 1.362 -28.330 9.713 1.00 38.79 ? ? ? ? ? . 1 MET A CA 2348 ATOM 3 C C . MET A 2348 1 . 2.451 -27.795 10.648 1.00 34.46 ? ? ? ? ? . 1 MET A C 2348 ATOM 4 O O . MET A 2348 1 . 3.019 -28.519 11.476 1.00 28.07 ? ? ? ? ? . 1 MET A O 2348 ATOM 5 C CB . MET A 2348 1 . -0.032 -28.003 10.280 1.00 43.44 ? ? ? ? ? . 1 MET A CB 2348 ATOM 6 C CG . MET A 2348 1 . -1.163 -28.074 9.261 1.00 48.34 ? ? ? ? ? . 1 MET A CG 2348 ATOM 7 S SD . MET A 2348 1 . -1.096 -26.763 8.019 1.00 56.59 ? ? ? ? ? . 1 MET A SD 2348 ATOM 8 C CE . MET A 2348 1 . -1.944 -27.553 6.650 1.00 53.77 ? ? ? ? ? . 1 MET A CE 2348 ATOM 9 N N . SER A 2348 2 . 2.702 -26.498 10.518 1.00 31.58 ? ? ? ? ? . 2 SER A N 2348 ATOM 10 C CA . SER A 2348 2 . 3.686 -25.813 11.340 1.00 29.58 ? ? ? ? ? . 2 SER A CA 2348 ATOM 11 C C . SER A 2348 2 . 3.179 -25.647 12.742 1.00 28.87 ? ? ? ? ? . 2 SER A C 2348 ATOM 12 O O . SER A 2348 2 . 1.976 -25.688 12.985 1.00 24.92 ? ? ? ? ? . 2 SER A O 2348 ATOM 13 C CB . SER A 2348 2 . 3.985 -24.427 10.800 1.00 31.81 ? ? ? ? ? . 2 SER A CB 2348 ATOM 14 O OG . SER A 2348 2 . 2.955 -23.494 11.097 1.00 29.45 ? ? ? ? ? . 2 SER A OG 2348 ATOM 15 N N . GLY A 2348 3 . 4.105 -25.396 13.653 1.00 26.92 ? ? ? ? ? . 3 GLY A N 2348 ATOM 16 C CA . GLY A 2348 3 . 3.752 -25.062 15.022 1.00 27.19 ? ? ? ? ? . 3 GLY A CA 2348 ATOM 17 C C . GLY A 2348 3 . 3.057 -23.717 15.142 1.00 26.26 ? ? ? ? ? . 3 GLY A C 2348 ATOM 18 O O . GLY A 2348 3 . 2.392 -23.466 16.134 1.00 31.06 ? ? ? ? ? . 3 GLY A O 2348 ATOM 19 N N . LEU A 2348 4 . 3.204 -22.842 14.148 1.00 27.31 ? ? ? ? ? . 4 LEU A N 2348 ATOM 20 C CA . LEU A 2348 4 . 2.393 -21.618 14.096 1.00 28.14 ? ? ? ? ? . 4 LEU A CA 2348 ATOM 21 C C . LEU A 2348 4 . 0.907 -21.935 13.926 1.00 26.94 ? ? ? ? ? . 4 LEU A C 2348 ATOM 22 O O . LEU A 2348 4 . 0.070 -21.235 14.495 1.00 25.83 ? ? ? ? ? . 4 LEU A O 2348 ATOM 23 C CB . LEU A 2348 4 . 2.859 -20.661 12.988 1.00 31.30 ? ? ? ? ? . 4 LEU A CB 2348 ATOM 24 C CG . LEU A 2348 4 . 4.018 -19.719 13.288 1.00 32.68 ? ? ? ? ? . 4 LEU A CG 2348 ATOM 25 C CD1 . LEU A 2348 4 . 4.270 -18.858 12.063 1.00 34.49 ? ? ? ? ? . 4 LEU A CD1 2348 ATOM 26 C CD2 . LEU A 2348 4 . 3.718 -18.844 14.497 1.00 34.30 ? ? ? ? ? . 4 LEU A CD2 2348 ATOM 27 N N . ALA A 2348 5 . 0.579 -22.994 13.176 1.00 26.99 ? ? ? ? ? . 5 ALA A N 2348 ATOM 28 C CA . ALA A 2348 5 . -0.817 -23.451 13.048 1.00 29.14 ? ? ? ? ? . 5 ALA A CA 2348 ATOM 29 C C . ALA A 2348 5 . -1.502 -23.807 14.377 1.00 31.57 ? ? ? ? ? . 5 ALA A C 2348 ATOM 30 O O . ALA A 2348 5 . -2.722 -23.642 14.499 1.00 38.23 ? ? ? ? ? . 5 ALA A O 2348 ATOM 31 C CB . ALA A 2348 5 . -0.923 -24.626 12.077 1.00 32.07 ? ? ? ? ? . 5 ALA A CB 2348 ATOM 32 N N . LYS A 2348 6 . -0.746 -24.274 15.372 1.00 28.88 ? ? ? ? ? . 6 LYS A N 2348 ATOM 33 C CA . LYS A 2348 6 . -1.337 -24.554 16.690 1.00 28.76 ? ? ? ? ? . 6 LYS A CA 2348 ATOM 34 C C . LYS A 2348 6 . -1.895 -23.293 17.343 1.00 24.63 ? ? ? ? ? . 6 LYS A C 2348 ATOM 35 O O . LYS A 2348 6 . -2.853 -23.372 18.095 1.00 25.15 ? ? ? ? ? . 6 LYS A O 2348 ATOM 36 C CB . LYS A 2348 6 . -0.356 -25.256 17.646 1.00 32.13 ? ? ? ? ? . 6 LYS A CB 2348 ATOM 37 C CG . LYS A 2348 6 . 0.511 -24.341 18.526 1.00 31.95 ? ? ? ? ? . 6 LYS A CG 2348 ATOM 38 C CD . LYS A 2348 6 . 1.607 -25.092 19.277 1.00 33.12 ? ? ? ? ? . 6 LYS A CD 2348 ATOM 39 C CE . LYS A 2348 6 . 2.655 -25.712 18.350 1.00 32.32 ? ? ? ? ? . 6 LYS A CE 2348 ATOM 40 N NZ . LYS A 2348 6 . 3.554 -26.649 19.060 1.00 28.93 ? ? ? ? ? 1+ 6 LYS A NZ 2348 ATOM 41 N N . TYR A 2348 7 . -1.273 -22.149 17.060 1.00 23.51 ? ? ? ? ? . 7 TYR A N 2348 ATOM 42 C CA . TYR A 2348 7 . -1.713 -20.858 17.597 1.00 24.18 ? ? ? ? ? . 7 TYR A CA 2348 ATOM 43 C C . TYR A 2348 7 . -2.735 -20.147 16.721 1.00 25.86 ? ? ? ? ? . 7 TYR A C 2348 ATOM 44 O O . TYR A 2348 7 . -3.549 -19.381 17.235 1.00 25.45 ? ? ? ? ? . 7 TYR A O 2348 ATOM 45 C CB . TYR A 2348 7 . -0.526 -19.931 17.799 1.00 22.86 ? ? ? ? ? . 7 TYR A CB 2348 ATOM 46 C CG . TYR A 2348 7 . 0.519 -20.473 18.741 1.00 20.79 ? ? ? ? ? . 7 TYR A CG 2348 ATOM 47 C CD1 . TYR A 2348 7 . 0.199 -20.788 20.060 1.00 19.65 ? ? ? ? ? . 7 TYR A CD1 2348 ATOM 48 C CD2 . TYR A 2348 7 . 1.841 -20.635 18.325 1.00 19.30 ? ? ? ? ? . 7 TYR A CD2 2348 ATOM 49 C CE1 . TYR A 2348 7 . 1.162 -21.270 20.934 1.00 19.28 ? ? ? ? ? . 7 TYR A CE1 2348 ATOM 50 C CE2 . TYR A 2348 7 . 2.805 -21.114 19.186 1.00 19.91 ? ? ? ? ? . 7 TYR A CE2 2348 ATOM 51 C CZ . TYR A 2348 7 . 2.462 -21.430 20.493 1.00 19.68 ? ? ? ? ? . 7 TYR A CZ 2348 ATOM 52 O OH . TYR A 2348 7 . 3.427 -21.901 21.354 1.00 19.23 ? ? ? ? ? . 7 TYR A OH 2348 ATOM 53 N N . LEU A 2348 8 . -2.711 -20.410 15.413 1.00 25.61 ? ? ? ? ? . 8 LEU A N 2348 ATOM 54 C CA . LEU A 2348 8 . -3.604 -19.742 14.468 1.00 27.57 ? ? ? ? ? . 8 LEU A CA 2348 ATOM 55 C C . LEU A 2348 8 . -4.522 -20.703 13.671 1.00 30.41 ? ? ? ? ? . 8 LEU A C 2348 ATOM 56 O O . LEU A 2348 8 . -4.503 -20.676 12.444 1.00 31.20 ? ? ? ? ? . 8 LEU A O 2348 ATOM 57 C CB . LEU A 2348 8 . -2.750 -18.882 13.517 1.00 26.23 ? ? ? ? ? . 8 LEU A CB 2348 ATOM 58 C CG . LEU A 2348 8 . -1.810 -17.852 14.164 1.00 24.95 ? ? ? ? ? . 8 LEU A CG 2348 ATOM 59 C CD1 . LEU A 2348 8 . -0.828 -17.290 13.142 1.00 26.14 ? ? ? ? ? . 8 LEU A CD1 2348 ATOM 60 C CD2 . LEU A 2348 8 . -2.602 -16.730 14.822 1.00 25.27 ? ? ? ? ? . 8 LEU A CD2 2348 ATOM 61 N N A PRO A 2348 9 . -5.300 -21.558 14.376 0.49 34.84 ? ? ? ? ? . 9 PRO A N 2348 ATOM 62 N N B PRO A 2348 9 . -5.359 -21.503 14.365 0.51 33.67 ? ? ? ? ? . 9 PRO A N 2348 ATOM 63 C CA A PRO A 2348 9 . -6.293 -22.381 13.700 0.49 37.05 ? ? ? ? ? . 9 PRO A CA 2348 ATOM 64 C CA B PRO A 2348 9 . -6.175 -22.534 13.697 0.51 35.34 ? ? ? ? ? . 9 PRO A CA 2348 ATOM 65 C C A PRO A 2348 9 . -7.506 -21.519 13.432 0.49 38.35 ? ? ? ? ? . 9 PRO A C 2348 ATOM 66 C C B PRO A 2348 9 . -7.186 -22.013 12.660 0.51 36.39 ? ? ? ? ? . 9 PRO A C 2348 ATOM 67 O O A PRO A 2348 9 . -8.118 -21.001 14.366 0.49 39.55 ? ? ? ? ? . 9 PRO A O 2348 ATOM 68 O O B PRO A 2348 9 . -7.420 -22.691 11.657 0.51 37.00 ? ? ? ? ? . 9 PRO A O 2348 ATOM 69 C CB A PRO A 2348 9 . -6.624 -23.442 14.742 0.49 36.54 ? ? ? ? ? . 9 PRO A CB 2348 ATOM 70 C CB B PRO A 2348 9 . -6.909 -23.210 14.865 0.51 34.76 ? ? ? ? ? . 9 PRO A CB 2348 ATOM 71 C CG A PRO A 2348 9 . -6.535 -22.693 16.022 0.49 36.43 ? ? ? ? ? . 9 PRO A CG 2348 ATOM 72 C CG B PRO A 2348 9 . -6.953 -22.172 15.932 0.51 34.10 ? ? ? ? ? . 9 PRO A CG 2348 ATOM 73 C CD A PRO A 2348 9 . -5.375 -21.751 15.840 0.49 36.25 ? ? ? ? ? . 9 PRO A CD 2348 ATOM 74 C CD B PRO A 2348 9 . -5.641 -21.459 15.815 0.51 34.53 ? ? ? ? ? . 9 PRO A CD 2348 ATOM 75 N N A GLY A 2348 10 . -7.850 -21.363 12.165 0.49 38.66 ? ? ? ? ? . 10 GLY A N 2348 ATOM 76 N N B GLY A 2348 10 . -7.776 -20.841 12.911 0.51 35.97 ? ? ? ? ? . 10 GLY A N 2348 ATOM 77 C CA A GLY A 2348 10 . -8.786 -20.329 11.768 0.49 37.94 ? ? ? ? ? . 10 GLY A CA 2348 ATOM 78 C CA B GLY A 2348 10 . -8.733 -20.217 11.981 0.51 36.27 ? ? ? ? ? . 10 GLY A CA 2348 ATOM 79 C C A GLY A 2348 10 . -8.121 -19.416 10.757 0.49 37.83 ? ? ? ? ? . 10 GLY A C 2348 ATOM 80 C C B GLY A 2348 10 . -8.107 -19.480 10.800 0.51 37.15 ? ? ? ? ? . 10 GLY A C 2348 ATOM 81 O O A GLY A 2348 10 . -8.796 -18.870 9.876 0.49 37.03 ? ? ? ? ? . 10 GLY A O 2348 ATOM 82 O O B GLY A 2348 10 . -8.798 -19.134 9.836 0.51 37.06 ? ? ? ? ? . 10 GLY A O 2348 ATOM 83 N N . ALA A 2348 11 . -6.803 -19.231 10.888 1.00 36.15 ? ? ? ? ? . 11 ALA A N 2348 ATOM 84 C CA . ALA A 2348 11 . -6.026 -18.586 9.835 1.00 35.46 ? ? ? ? ? . 11 ALA A CA 2348 ATOM 85 C C . ALA A 2348 11 . -5.687 -19.603 8.758 1.00 36.66 ? ? ? ? ? . 11 ALA A C 2348 ATOM 86 O O . ALA A 2348 11 . -5.713 -20.816 8.988 1.00 35.61 ? ? ? ? ? . 11 ALA A O 2348 ATOM 87 C CB . ALA A 2348 11 . -4.743 -17.992 10.401 1.00 34.28 ? ? ? ? ? . 11 ALA A CB 2348 ATOM 88 N N . THR A 2348 12 . -5.403 -19.089 7.571 1.00 35.16 ? ? ? ? ? . 12 THR A N 2348 ATOM 89 C CA . THR A 2348 12 . -4.620 -19.821 6.582 1.00 34.41 ? ? ? ? ? . 12 THR A CA 2348 ATOM 90 C C . THR A 2348 12 . -3.465 -18.927 6.157 1.00 30.55 ? ? ? ? ? . 12 THR A C 2348 ATOM 91 O O . THR A 2348 12 . -2.309 -19.284 6.369 1.00 33.15 ? ? ? ? ? . 12 THR A O 2348 ATOM 92 C CB . THR A 2348 12 . -5.447 -20.322 5.371 1.00 37.60 ? ? ? ? ? . 12 THR A CB 2348 ATOM 93 C CG2 . THR A 2348 12 . -5.624 -21.844 5.441 1.00 41.25 ? ? ? ? ? . 12 THR A CG2 2348 ATOM 94 O OG1 . THR A 2348 12 . -6.745 -19.707 5.356 1.00 40.05 ? ? ? ? ? . 12 THR A OG1 2348 ATOM 95 N N . ASN A 2348 13 . -3.761 -17.760 5.589 1.00 24.01 ? ? ? ? ? . 13 ASN A N 2348 ATOM 96 C CA . ASN A 2348 13 . -2.702 -16.909 5.058 1.00 21.19 ? ? ? ? ? . 13 ASN A CA 2348 ATOM 97 C C . ASN A 2348 13 . -2.485 -15.671 5.897 1.00 19.45 ? ? ? ? ? . 13 ASN A C 2348 ATOM 98 O O . ASN A 2348 13 . -3.378 -15.222 6.620 1.00 21.50 ? ? ? ? ? . 13 ASN A O 2348 ATOM 99 C CB . ASN A 2348 13 . -2.997 -16.518 3.609 1.00 23.60 ? ? ? ? ? . 13 ASN A CB 2348 ATOM 100 C CG . ASN A 2348 13 . -3.062 -17.718 2.683 1.00 25.11 ? ? ? ? ? . 13 ASN A CG 2348 ATOM 101 N ND2 . ASN A 2348 13 . -4.029 -17.717 1.771 1.00 24.16 ? ? ? ? ? . 13 ASN A ND2 2348 ATOM 102 O OD1 . ASN A 2348 13 . -2.256 -18.644 2.795 1.00 28.41 ? ? ? ? ? . 13 ASN A OD1 2348 ATOM 103 N N . LEU A 2348 14 . -1.277 -15.134 5.781 1.00 16.54 ? ? ? ? ? . 14 LEU A N 2348 ATOM 104 C CA . LEU A 2348 14 . -0.881 -13.881 6.390 1.00 15.38 ? ? ? ? ? . 14 LEU A CA 2348 ATOM 105 C C . LEU A 2348 14 . -0.723 -12.879 5.271 1.00 15.70 ? ? ? ? ? . 14 LEU A C 2348 ATOM 106 O O . LEU A 2348 14 . -0.384 -13.251 4.152 1.00 16.70 ? ? ? ? ? . 14 LEU A O 2348 ATOM 107 C CB . LEU A 2348 14 . 0.455 -14.057 7.118 1.00 15.56 ? ? ? ? ? . 14 LEU A CB 2348 ATOM 108 C CG . LEU A 2348 14 . 0.466 -15.081 8.254 1.00 15.33 ? ? ? ? ? . 14 LEU A CG 2348 ATOM 109 C CD1 . LEU A 2348 14 . 1.865 -15.199 8.824 1.00 16.03 ? ? ? ? ? . 14 LEU A CD1 2348 ATOM 110 C CD2 . LEU A 2348 14 . -0.512 -14.706 9.360 1.00 14.84 ? ? ? ? ? . 14 LEU A CD2 2348 ATOM 111 N N . LEU A 2348 15 . -0.963 -11.610 5.571 1.00 15.63 ? ? ? ? ? . 15 LEU A N 2348 ATOM 112 C CA . LEU A 2348 15 . -0.692 -10.536 4.620 1.00 16.16 ? ? ? ? ? . 15 LEU A CA 2348 ATOM 113 C C . LEU A 2348 15 . 0.817 -10.328 4.485 1.00 16.48 ? ? ? ? ? . 15 LEU A C 2348 ATOM 114 O O . LEU A 2348 15 . 1.537 -10.488 5.458 1.00 15.72 ? ? ? ? ? . 15 LEU A O 2348 ATOM 115 C CB . LEU A 2348 15 . -1.302 -9.224 5.088 1.00 15.78 ? ? ? ? ? . 15 LEU A CB 2348 ATOM 116 C CG . LEU A 2348 15 . -2.774 -9.203 5.473 1.00 16.53 ? ? ? ? ? . 15 LEU A CG 2348 ATOM 117 C CD1 . LEU A 2348 15 . -3.169 -7.778 5.854 1.00 17.40 ? ? ? ? ? . 15 LEU A CD1 2348 ATOM 118 C CD2 . LEU A 2348 15 . -3.657 -9.742 4.356 1.00 15.86 ? ? ? ? ? . 15 LEU A CD2 2348 ATOM 119 N N . SER A 2348 16 . 1.274 -9.967 3.289 1.00 16.81 ? ? ? ? ? . 16 SER A N 2348 ATOM 120 C CA . SER A 2348 16 . 2.659 -9.490 3.089 1.00 18.19 ? ? ? ? ? . 16 SER A CA 2348 ATOM 121 C C . SER A 2348 16 . 2.617 -8.199 2.266 1.00 19.91 ? ? ? ? ? . 16 SER A C 2348 ATOM 122 O O . SER A 2348 16 . 1.553 -7.749 1.839 1.00 18.64 ? ? ? ? ? . 16 SER A O 2348 ATOM 123 C CB . SER A 2348 16 . 3.525 -10.544 2.378 1.00 19.00 ? ? ? ? ? . 16 SER A CB 2348 ATOM 124 O OG . SER A 2348 16 . 3.353 -10.503 0.969 1.00 19.59 ? ? ? ? ? . 16 SER A OG 2348 ATOM 125 N N . LYS A 2348 17 . 3.780 -7.614 2.027 1.00 21.51 ? ? ? ? ? . 17 LYS A N 2348 ATOM 126 C CA . LYS A 2348 17 . 3.855 -6.435 1.165 1.00 24.73 ? ? ? ? ? . 17 LYS A CA 2348 ATOM 127 C C . LYS A 2348 17 . 3.444 -6.732 -0.283 1.00 25.66 ? ? ? ? ? . 17 LYS A C 2348 ATOM 128 O O . LYS A 2348 17 . 3.019 -5.819 -0.983 1.00 27.03 ? ? ? ? ? . 17 LYS A O 2348 ATOM 129 C CB . LYS A 2348 17 . 5.262 -5.832 1.197 1.00 25.50 ? ? ? ? ? . 17 LYS A CB 2348 ATOM 130 C CG . LYS A 2348 17 . 5.682 -5.273 2.551 1.00 25.81 ? ? ? ? ? . 17 LYS A CG 2348 ATOM 131 C CD . LYS A 2348 17 . 4.736 -4.187 3.056 1.00 28.95 ? ? ? ? ? . 17 LYS A CD 2348 ATOM 132 C CE . LYS A 2348 17 . 3.753 -4.693 4.113 1.00 28.57 ? ? ? ? ? . 17 LYS A CE 2348 ATOM 133 N NZ . LYS A 2348 17 . 2.971 -3.562 4.702 1.00 25.15 ? ? ? ? ? 1+ 17 LYS A NZ 2348 ATOM 134 N N . SER A 2348 18 . 3.555 -7.992 -0.712 1.00 25.74 ? ? ? ? ? . 18 SER A N 2348 ATOM 135 C CA . SER A 2348 18 . 3.177 -8.416 -2.070 1.00 30.18 ? ? ? ? ? . 18 SER A CA 2348 ATOM 136 C C . SER A 2348 18 . 2.143 -9.546 -2.074 1.00 32.37 ? ? ? ? ? . 18 SER A C 2348 ATOM 137 O O . SER A 2348 18 . 2.384 -10.619 -2.635 1.00 35.88 ? ? ? ? ? . 18 SER A O 2348 ATOM 138 C CB . SER A 2348 18 . 4.431 -8.893 -2.797 1.00 31.94 ? ? ? ? ? . 18 SER A CB 2348 ATOM 139 O OG . SER A 2348 18 . 4.959 -10.040 -2.149 1.00 33.68 ? ? ? ? ? . 18 SER A OG 2348 ATOM 140 N N . GLY A 2348 19 . 0.995 -9.323 -1.452 1.00 31.20 ? ? ? ? ? . 19 GLY A N 2348 ATOM 141 C CA . GLY A 2348 19 . -0.034 -10.370 -1.395 1.00 32.15 ? ? ? ? ? . 19 GLY A CA 2348 ATOM 142 C C . GLY A 2348 19 . 0.276 -11.471 -0.382 1.00 31.51 ? ? ? ? ? . 19 GLY A C 2348 ATOM 143 O O . GLY A 2348 19 . 1.310 -11.458 0.288 1.00 33.38 ? ? ? ? ? . 19 GLY A O 2348 ATOM 144 N N . GLU A 2348 20 . -0.629 -12.434 -0.282 1.00 26.41 ? ? ? ? ? . 20 GLU A N 2348 ATOM 145 C CA . GLU A 2348 20 . -0.691 -13.290 0.884 1.00 24.83 ? ? ? ? ? . 20 GLU A CA 2348 ATOM 146 C C . GLU A 2348 20 . 0.330 -14.411 0.824 1.00 21.95 ? ? ? ? ? . 20 GLU A C 2348 ATOM 147 O O . GLU A 2348 20 . 0.679 -14.879 -0.254 1.00 20.93 ? ? ? ? ? . 20 GLU A O 2348 ATOM 148 C CB . GLU A 2348 20 . -2.102 -13.854 1.040 1.00 28.97 ? ? ? ? ? . 20 GLU A CB 2348 ATOM 149 C CG . GLU A 2348 20 . -3.156 -12.772 1.249 1.00 29.83 ? ? ? ? ? . 20 GLU A CG 2348 ATOM 150 C CD . GLU A 2348 20 . -4.539 -13.321 1.561 1.00 31.70 ? ? ? ? ? . 20 GLU A CD 2348 ATOM 151 O OE1 . GLU A 2348 20 . -4.814 -14.491 1.202 1.00 33.49 ? ? ? ? ? . 20 GLU A OE1 2348 ATOM 152 O OE2 . GLU A 2348 20 . -5.349 -12.565 2.154 1.00 34.19 ? ? ? ? ? 1- 20 GLU A OE2 2348 ATOM 153 N N . VAL A 2348 21 . 0.799 -14.822 1.996 1.00 18.14 ? ? ? ? ? . 21 VAL A N 2348 ATOM 154 C CA . VAL A 2348 21 . 1.739 -15.940 2.130 1.00 18.05 ? ? ? ? ? . 21 VAL A CA 2348 ATOM 155 C C . VAL A 2348 21 . 1.210 -16.964 3.137 1.00 16.57 ? ? ? ? ? . 21 VAL A C 2348 ATOM 156 O O . VAL A 2348 21 . 0.519 -16.610 4.089 1.00 15.65 ? ? ? ? ? . 21 VAL A O 2348 ATOM 157 C CB . VAL A 2348 21 . 3.150 -15.466 2.542 1.00 18.57 ? ? ? ? ? . 21 VAL A CB 2348 ATOM 158 C CG1 . VAL A 2348 21 . 3.672 -14.437 1.540 1.00 19.84 ? ? ? ? ? . 21 VAL A CG1 2348 ATOM 159 C CG2 . VAL A 2348 21 . 3.176 -14.922 3.970 1.00 17.16 ? ? ? ? ? . 21 VAL A CG2 2348 ATOM 160 N N . SER A 2348 22 . 1.533 -18.230 2.906 1.00 15.34 ? ? ? ? ? . 22 SER A N 2348 ATOM 161 C CA . SER A 2348 22 . 1.073 -19.315 3.767 1.00 16.37 ? ? ? ? ? . 22 SER A CA 2348 ATOM 162 C C . SER A 2348 22 . 1.872 -19.345 5.061 1.00 16.62 ? ? ? ? ? . 22 SER A C 2348 ATOM 163 O O . SER A 2348 22 . 3.000 -18.826 5.142 1.00 15.98 ? ? ? ? ? . 22 SER A O 2348 ATOM 164 C CB . SER A 2348 22 . 1.237 -20.655 3.056 1.00 17.61 ? ? ? ? ? . 22 SER A CB 2348 ATOM 165 O OG . SER A 2348 22 . 2.618 -20.887 2.815 1.00 17.06 ? ? ? ? ? . 22 SER A OG 2348 ATOM 166 N N . LEU A 2348 23 . 1.305 -19.988 6.072 1.00 17.27 ? ? ? ? ? . 23 LEU A N 2348 ATOM 167 C CA . LEU A 2348 23 . 2.058 -20.286 7.290 1.00 17.54 ? ? ? ? ? . 23 LEU A CA 2348 ATOM 168 C C . LEU A 2348 23 . 3.271 -21.187 6.998 1.00 15.71 ? ? ? ? ? . 23 LEU A C 2348 ATOM 169 O O . LEU A 2348 23 . 4.357 -20.961 7.555 1.00 15.68 ? ? ? ? ? . 23 LEU A O 2348 ATOM 170 C CB . LEU A 2348 23 . 1.158 -20.925 8.354 1.00 19.09 ? ? ? ? ? . 23 LEU A CB 2348 ATOM 171 C CG . LEU A 2348 23 . 0.047 -20.044 8.926 1.00 19.85 ? ? ? ? ? . 23 LEU A CG 2348 ATOM 172 C CD1 . LEU A 2348 23 . -0.781 -20.855 9.912 1.00 20.80 ? ? ? ? ? . 23 LEU A CD1 2348 ATOM 173 C CD2 . LEU A 2348 23 . 0.588 -18.800 9.598 1.00 20.11 ? ? ? ? ? . 23 LEU A CD2 2348 ATOM 174 N N . GLY A 2348 24 . 3.092 -22.170 6.110 1.00 14.87 ? ? ? ? ? . 24 GLY A N 2348 ATOM 175 C CA . GLY A 2348 24 . 4.183 -23.039 5.652 1.00 14.51 ? ? ? ? ? . 24 GLY A CA 2348 ATOM 176 C C . GLY A 2348 24 . 5.381 -22.325 5.024 1.00 14.47 ? ? ? ? ? . 24 GLY A C 2348 ATOM 177 O O . GLY A 2348 24 . 6.505 -22.845 5.067 1.00 12.91 ? ? ? ? ? . 24 GLY A O 2348 ATOM 178 N N . SER A 2348 25 . 5.160 -21.133 4.454 1.00 14.24 ? ? ? ? ? . 25 SER A N 2348 ATOM 179 C CA . SER A 2348 25 . 6.248 -20.339 3.852 1.00 14.58 ? ? ? ? ? . 25 SER A CA 2348 ATOM 180 C C . SER A 2348 25 . 7.295 -19.881 4.877 1.00 15.23 ? ? ? ? ? . 25 SER A C 2348 ATOM 181 O O . SER A 2348 25 . 8.425 -19.538 4.510 1.00 15.85 ? ? ? ? ? . 25 SER A O 2348 ATOM 182 C CB . SER A 2348 25 . 5.691 -19.131 3.076 1.00 14.16 ? ? ? ? ? . 25 SER A CB 2348 ATOM 183 O OG . SER A 2348 25 . 5.236 -18.112 3.943 1.00 13.91 ? ? ? ? ? . 25 SER A OG 2348 ATOM 184 N N . LEU A 2348 26 . 6.900 -19.862 6.153 1.00 15.28 ? ? ? ? ? . 26 LEU A N 2348 ATOM 185 C CA . LEU A 2348 26 . 7.770 -19.517 7.262 1.00 15.71 ? ? ? ? ? . 26 LEU A CA 2348 ATOM 186 C C . LEU A 2348 26 . 8.551 -20.698 7.831 1.00 13.64 ? ? ? ? ? . 26 LEU A C 2348 ATOM 187 O O . LEU A 2348 26 . 9.162 -20.554 8.882 1.00 12.80 ? ? ? ? ? . 26 LEU A O 2348 ATOM 188 C CB . LEU A 2348 26 . 6.938 -18.882 8.384 1.00 17.44 ? ? ? ? ? . 26 LEU A CB 2348 ATOM 189 C CG . LEU A 2348 26 . 6.047 -17.702 7.946 1.00 20.26 ? ? ? ? ? . 26 LEU A CG 2348 ATOM 190 C CD1 . LEU A 2348 26 . 5.260 -17.143 9.118 1.00 22.13 ? ? ? ? ? . 26 LEU A CD1 2348 ATOM 191 C CD2 . LEU A 2348 26 . 6.881 -16.637 7.276 1.00 23.52 ? ? ? ? ? . 26 LEU A CD2 2348 ATOM 192 N N . VAL A 2348 27 . 8.555 -21.833 7.132 1.00 13.12 ? ? ? ? ? . 27 VAL A N 2348 ATOM 193 C CA . VAL A 2348 27 . 9.321 -23.014 7.537 1.00 13.59 ? ? ? ? ? . 27 VAL A CA 2348 ATOM 194 C C . VAL A 2348 27 . 10.754 -22.634 7.923 1.00 13.89 ? ? ? ? ? . 27 VAL A C 2348 ATOM 195 O O . VAL A 2348 27 . 11.416 -21.850 7.236 1.00 13.58 ? ? ? ? ? . 27 VAL A O 2348 ATOM 196 C CB . VAL A 2348 27 . 9.281 -24.133 6.469 1.00 12.77 ? ? ? ? ? . 27 VAL A CB 2348 ATOM 197 C CG1 . VAL A 2348 27 . 9.896 -23.694 5.145 1.00 12.72 ? ? ? ? ? . 27 VAL A CG1 2348 ATOM 198 C CG2 . VAL A 2348 27 . 9.933 -25.428 6.964 1.00 13.09 ? ? ? ? ? . 27 VAL A CG2 2348 ATOM 199 N N . GLY A 2348 28 . 11.165 -23.100 9.095 1.00 14.31 ? ? ? ? ? . 28 GLY A N 2348 ATOM 200 C CA . GLY A 2348 28 . 12.540 -22.930 9.573 1.00 14.56 ? ? ? ? ? . 28 GLY A CA 2348 ATOM 201 C C . GLY A 2348 28 . 12.871 -21.574 10.159 1.00 13.61 ? ? ? ? ? . 28 GLY A C 2348 ATOM 202 O O . GLY A 2348 28 . 14.008 -21.365 10.620 1.00 13.45 ? ? ? ? ? . 28 GLY A O 2348 ATOM 203 N N . LYS A 2348 29 . 11.900 -20.657 10.167 1.00 14.17 ? ? ? ? ? . 29 LYS A N 2348 ATOM 204 C CA . LYS A 2348 29 . 12.110 -19.302 10.657 1.00 14.57 ? ? ? ? ? . 29 LYS A CA 2348 ATOM 205 C C . LYS A 2348 29 . 11.932 -19.163 12.159 1.00 14.89 ? ? ? ? ? . 29 LYS A C 2348 ATOM 206 O O . LYS A 2348 29 . 11.235 -19.949 12.797 1.00 14.69 ? ? ? ? ? . 29 LYS A O 2348 ATOM 207 C CB . LYS A 2348 29 . 11.153 -18.306 9.975 1.00 15.81 ? ? ? ? ? . 29 LYS A CB 2348 ATOM 208 C CG . LYS A 2348 29 . 11.404 -18.134 8.484 1.00 16.45 ? ? ? ? ? . 29 LYS A CG 2348 ATOM 209 C CD . LYS A 2348 29 . 12.316 -16.947 8.202 1.00 17.42 ? ? ? ? ? . 29 LYS A CD 2348 ATOM 210 C CE . LYS A 2348 29 . 12.498 -16.708 6.715 1.00 17.30 ? ? ? ? ? . 29 LYS A CE 2348 ATOM 211 N NZ . LYS A 2348 29 . 13.044 -17.885 5.999 1.00 19.11 ? ? ? ? ? 1+ 29 LYS A NZ 2348 ATOM 212 N N . THR A 2348 30 . 12.603 -18.156 12.701 1.00 14.18 ? ? ? ? ? . 30 THR A N 2348 ATOM 213 C CA . THR A 2348 30 . 12.220 -17.550 13.977 1.00 14.27 ? ? ? ? ? . 30 THR A CA 2348 ATOM 214 C C . THR A 2348 30 . 11.144 -16.525 13.641 1.00 15.54 ? ? ? ? ? . 30 THR A C 2348 ATOM 215 O O . THR A 2348 30 . 11.293 -15.738 12.701 1.00 15.21 ? ? ? ? ? . 30 THR A O 2348 ATOM 216 C CB . THR A 2348 30 . 13.423 -16.869 14.660 1.00 15.36 ? ? ? ? ? . 30 THR A CB 2348 ATOM 217 C CG2 . THR A 2348 30 . 12.991 -16.093 15.905 1.00 17.24 ? ? ? ? ? . 30 THR A CG2 2348 ATOM 218 O OG1 . THR A 2348 30 . 14.393 -17.861 15.017 1.00 15.76 ? ? ? ? ? . 30 THR A OG1 2348 ATOM 219 N N . VAL A 2348 31 . 10.046 -16.537 14.380 1.00 14.34 ? ? ? ? ? . 31 VAL A N 2348 ATOM 220 C CA . VAL A 2348 31 . 8.934 -15.639 14.093 1.00 15.79 ? ? ? ? ? . 31 VAL A CA 2348 ATOM 221 C C . VAL A 2348 31 . 8.663 -14.816 15.342 1.00 16.49 ? ? ? ? ? . 31 VAL A C 2348 ATOM 222 O O . VAL A 2348 31 . 8.590 -15.357 16.455 1.00 15.72 ? ? ? ? ? . 31 VAL A O 2348 ATOM 223 C CB . VAL A 2348 31 . 7.675 -16.424 13.645 1.00 17.31 ? ? ? ? ? . 31 VAL A CB 2348 ATOM 224 C CG1 . VAL A 2348 31 . 6.467 -15.506 13.473 1.00 19.83 ? ? ? ? ? . 31 VAL A CG1 2348 ATOM 225 C CG2 . VAL A 2348 31 . 7.959 -17.190 12.356 1.00 16.54 ? ? ? ? ? . 31 VAL A CG2 2348 ATOM 226 N N . PHE A 2348 32 . 8.564 -13.502 15.158 1.00 16.30 ? ? ? ? ? . 32 PHE A N 2348 ATOM 227 C CA . PHE A 2348 32 . 8.143 -12.616 16.214 1.00 16.84 ? ? ? ? ? . 32 PHE A CA 2348 ATOM 228 C C . PHE A 2348 32 . 6.687 -12.259 15.980 1.00 16.42 ? ? ? ? ? . 32 PHE A C 2348 ATOM 229 O O . PHE A 2348 32 . 6.341 -11.721 14.924 1.00 18.32 ? ? ? ? ? . 32 PHE A O 2348 ATOM 230 C CB . PHE A 2348 32 . 8.955 -11.336 16.217 1.00 19.26 ? ? ? ? ? . 32 PHE A CB 2348 ATOM 231 C CG . PHE A 2348 32 . 10.415 -11.530 16.494 1.00 19.00 ? ? ? ? ? . 32 PHE A CG 2348 ATOM 232 C CD1 . PHE A 2348 32 . 10.870 -11.695 17.797 1.00 19.12 ? ? ? ? ? . 32 PHE A CD1 2348 ATOM 233 C CD2 . PHE A 2348 32 . 11.344 -11.506 15.462 1.00 20.74 ? ? ? ? ? . 32 PHE A CD2 2348 ATOM 234 C CE1 . PHE A 2348 32 . 12.222 -11.839 18.070 1.00 19.85 ? ? ? ? ? . 32 PHE A CE1 2348 ATOM 235 C CE2 . PHE A 2348 32 . 12.707 -11.659 15.734 1.00 21.50 ? ? ? ? ? . 32 PHE A CE2 2348 ATOM 236 C CZ . PHE A 2348 32 . 13.134 -11.818 17.049 1.00 20.68 ? ? ? ? ? . 32 PHE A CZ 2348 ATOM 237 N N . LEU A 2348 33 . 5.849 -12.554 16.959 1.00 14.24 ? ? ? ? ? . 33 LEU A N 2348 ATOM 238 C CA . LEU A 2348 33 . 4.475 -12.091 16.982 1.00 14.81 ? ? ? ? ? . 33 LEU A CA 2348 ATOM 239 C C . LEU A 2348 33 . 4.477 -10.717 17.622 1.00 15.85 ? ? ? ? ? . 33 LEU A C 2348 ATOM 240 O O . LEU A 2348 33 . 4.880 -10.578 18.777 1.00 15.41 ? ? ? ? ? . 33 LEU A O 2348 ATOM 241 C CB . LEU A 2348 33 . 3.592 -13.056 17.779 1.00 15.00 ? ? ? ? ? . 33 LEU A CB 2348 ATOM 242 C CG . LEU A 2348 33 . 3.603 -14.485 17.239 1.00 16.27 ? ? ? ? ? . 33 LEU A CG 2348 ATOM 243 C CD1 . LEU A 2348 33 . 2.632 -15.324 18.051 1.00 17.02 ? ? ? ? ? . 33 LEU A CD1 2348 ATOM 244 C CD2 . LEU A 2348 33 . 3.259 -14.541 15.757 1.00 17.70 ? ? ? ? ? . 33 LEU A CD2 2348 ATOM 245 N N . TYR A 2348 34 . 4.035 -9.718 16.859 1.00 16.06 ? ? ? ? ? . 34 TYR A N 2348 ATOM 246 C CA . TYR A 2348 34 . 4.112 -8.329 17.268 1.00 15.69 ? ? ? ? ? . 34 TYR A CA 2348 ATOM 247 C C . TYR A 2348 34 . 2.721 -7.828 17.608 1.00 15.39 ? ? ? ? ? . 34 TYR A C 2348 ATOM 248 O O . TYR A 2348 34 . 1.965 -7.440 16.735 1.00 14.35 ? ? ? ? ? . 34 TYR A O 2348 ATOM 249 C CB . TYR A 2348 34 . 4.773 -7.466 16.198 1.00 16.16 ? ? ? ? ? . 34 TYR A CB 2348 ATOM 250 C CG . TYR A 2348 34 . 4.825 -5.977 16.516 1.00 16.03 ? ? ? ? ? . 34 TYR A CG 2348 ATOM 251 C CD1 . TYR A 2348 34 . 4.977 -5.516 17.821 1.00 16.83 ? ? ? ? ? . 34 TYR A CD1 2348 ATOM 252 C CD2 . TYR A 2348 34 . 4.769 -5.031 15.488 1.00 17.63 ? ? ? ? ? . 34 TYR A CD2 2348 ATOM 253 C CE1 . TYR A 2348 34 . 5.030 -4.159 18.098 1.00 17.21 ? ? ? ? ? . 34 TYR A CE1 2348 ATOM 254 C CE2 . TYR A 2348 34 . 4.829 -3.670 15.759 1.00 17.31 ? ? ? ? ? . 34 TYR A CE2 2348 ATOM 255 C CZ . TYR A 2348 34 . 4.965 -3.243 17.069 1.00 16.44 ? ? ? ? ? . 34 TYR A CZ 2348 ATOM 256 O OH . TYR A 2348 34 . 5.016 -1.898 17.366 1.00 17.87 ? ? ? ? ? . 34 TYR A OH 2348 ATOM 257 N N . PHE A 2348 35 . 2.438 -7.854 18.898 1.00 15.23 ? ? ? ? ? . 35 PHE A N 2348 ATOM 258 C CA . PHE A 2348 35 . 1.192 -7.354 19.477 1.00 16.74 ? ? ? ? ? . 35 PHE A CA 2348 ATOM 259 C C . PHE A 2348 35 . 1.248 -5.831 19.553 1.00 16.39 ? ? ? ? ? . 35 PHE A C 2348 ATOM 260 O O . PHE A 2348 35 . 2.115 -5.268 20.223 1.00 17.11 ? ? ? ? ? . 35 PHE A O 2348 ATOM 261 C CB . PHE A 2348 35 . 0.966 -7.980 20.843 1.00 17.16 ? ? ? ? ? . 35 PHE A CB 2348 ATOM 262 C CG . PHE A 2348 35 . 0.735 -9.454 20.782 1.00 18.26 ? ? ? ? ? . 35 PHE A CG 2348 ATOM 263 C CD1 . PHE A 2348 35 . 1.802 -10.330 20.795 1.00 18.94 ? ? ? ? ? . 35 PHE A CD1 2348 ATOM 264 C CD2 . PHE A 2348 35 . -0.552 -9.974 20.684 1.00 19.43 ? ? ? ? ? . 35 PHE A CD2 2348 ATOM 265 C CE1 . PHE A 2348 35 . 1.605 -11.695 20.708 1.00 19.02 ? ? ? ? ? . 35 PHE A CE1 2348 ATOM 266 C CE2 . PHE A 2348 35 . -0.759 -11.344 20.614 1.00 19.14 ? ? ? ? ? . 35 PHE A CE2 2348 ATOM 267 C CZ . PHE A 2348 35 . 0.321 -12.205 20.626 1.00 19.19 ? ? ? ? ? . 35 PHE A CZ 2348 ATOM 268 N N . SER A 2348 36 . 0.344 -5.181 18.822 1.00 17.49 ? ? ? ? ? . 36 SER A N 2348 ATOM 269 C CA . SER A 2348 36 . 0.415 -3.732 18.583 1.00 18.12 ? ? ? ? ? . 36 SER A CA 2348 ATOM 270 C C . SER A 2348 36 . -0.954 -3.153 18.254 1.00 17.25 ? ? ? ? ? . 36 SER A C 2348 ATOM 271 O O . SER A 2348 36 . -1.942 -3.878 18.155 1.00 16.75 ? ? ? ? ? . 36 SER A O 2348 ATOM 272 C CB . SER A 2348 36 . 1.391 -3.425 17.436 1.00 19.11 ? ? ? ? ? . 36 SER A CB 2348 ATOM 273 O OG . SER A 2348 36 . 1.744 -2.041 17.380 1.00 20.12 ? ? ? ? ? . 36 SER A OG 2348 ATOM 274 N N . ALA A 2348 37 . -0.999 -1.835 18.129 1.00 16.02 ? ? ? ? ? . 37 ALA A N 2348 ATOM 275 C CA . ALA A 2348 37 . -2.210 -1.132 17.705 1.00 17.21 ? ? ? ? ? . 37 ALA A CA 2348 ATOM 276 C C . ALA A 2348 37 . -1.822 0.227 17.163 1.00 16.58 ? ? ? ? ? . 37 ALA A C 2348 ATOM 277 O O . ALA A 2348 37 . -0.894 0.865 17.681 1.00 16.07 ? ? ? ? ? . 37 ALA A O 2348 ATOM 278 C CB . ALA A 2348 37 . -3.176 -0.987 18.865 1.00 16.09 ? ? ? ? ? . 37 ALA A CB 2348 ATOM 279 N N . SER A 2348 38 . -2.538 0.673 16.134 1.00 16.09 ? ? ? ? ? . 38 SER A N 2348 ATOM 280 C CA . SER A 2348 38 . -2.180 1.894 15.393 1.00 15.94 ? ? ? ? ? . 38 SER A CA 2348 ATOM 281 C C . SER A 2348 38 . -2.215 3.154 16.234 1.00 16.06 ? ? ? ? ? . 38 SER A C 2348 ATOM 282 O O . SER A 2348 38 . -1.492 4.108 15.933 1.00 15.57 ? ? ? ? ? . 38 SER A O 2348 ATOM 283 C CB . SER A 2348 38 . -3.111 2.110 14.198 1.00 15.53 ? ? ? ? ? . 38 SER A CB 2348 ATOM 284 O OG . SER A 2348 38 . -4.417 2.483 14.611 1.00 13.61 ? ? ? ? ? . 38 SER A OG 2348 ATOM 285 N N . TRP A 2348 39 . -3.083 3.153 17.250 1.00 14.29 ? ? ? ? ? . 39 TRP A N 2348 ATOM 286 C CA . TRP A 2348 39 . -3.327 4.323 18.102 1.00 15.81 ? ? ? ? ? . 39 TRP A CA 2348 ATOM 287 C C . TRP A 2348 39 . -2.576 4.292 19.439 1.00 15.54 ? ? ? ? ? . 39 TRP A C 2348 ATOM 288 O O . TRP A 2348 39 . -2.677 5.230 20.197 1.00 14.28 ? ? ? ? ? . 39 TRP A O 2348 ATOM 289 C CB . TRP A 2348 39 . -4.835 4.560 18.336 1.00 16.03 ? ? ? ? ? . 39 TRP A CB 2348 ATOM 290 C CG . TRP A 2348 39 . -5.696 3.342 18.284 1.00 17.02 ? ? ? ? ? . 39 TRP A CG 2348 ATOM 291 C CD1 . TRP A 2348 39 . -6.597 3.017 17.301 1.00 16.62 ? ? ? ? ? . 39 TRP A CD1 2348 ATOM 292 C CD2 . TRP A 2348 39 . -5.734 2.265 19.233 1.00 17.48 ? ? ? ? ? . 39 TRP A CD2 2348 ATOM 293 C CE2 . TRP A 2348 39 . -6.689 1.329 18.758 1.00 16.65 ? ? ? ? ? . 39 TRP A CE2 2348 ATOM 294 C CE3 . TRP A 2348 39 . -5.061 2.002 20.438 1.00 17.08 ? ? ? ? ? . 39 TRP A CE3 2348 ATOM 295 N NE1 . TRP A 2348 39 . -7.186 1.815 17.579 1.00 16.89 ? ? ? ? ? . 39 TRP A NE1 2348 ATOM 296 C CZ2 . TRP A 2348 39 . -6.978 0.143 19.435 1.00 17.13 ? ? ? ? ? . 39 TRP A CZ2 2348 ATOM 297 C CZ3 . TRP A 2348 39 . -5.351 0.824 21.116 1.00 17.20 ? ? ? ? ? . 39 TRP A CZ3 2348 ATOM 298 C CH2 . TRP A 2348 39 . -6.305 -0.098 20.607 1.00 17.58 ? ? ? ? ? . 39 TRP A CH2 2348 ATOM 299 N N A CYS A 2348 40 . -1.820 3.233 19.710 0.50 15.53 ? ? ? ? ? . 40 CYS A N 2348 ATOM 300 N N B CYS A 2348 40 . -1.828 3.220 19.708 0.50 15.76 ? ? ? ? ? . 40 CYS A N 2348 ATOM 301 C CA A CYS A 2348 40 . -1.099 3.113 20.973 0.50 15.94 ? ? ? ? ? . 40 CYS A CA 2348 ATOM 302 C CA B CYS A 2348 40 . -1.048 3.086 20.945 0.50 16.31 ? ? ? ? ? . 40 CYS A CA 2348 ATOM 303 C C A CYS A 2348 40 . 0.252 3.841 20.875 0.50 15.63 ? ? ? ? ? . 40 CYS A C 2348 ATOM 304 C C B CYS A 2348 40 . 0.259 3.881 20.821 0.50 15.84 ? ? ? ? ? . 40 CYS A C 2348 ATOM 305 O O A CYS A 2348 40 . 1.104 3.413 20.104 0.50 15.01 ? ? ? ? ? . 40 CYS A O 2348 ATOM 306 O O B CYS A 2348 40 . 1.084 3.541 19.979 0.50 15.24 ? ? ? ? ? . 40 CYS A O 2348 ATOM 307 C CB A CYS A 2348 40 . -0.881 1.639 21.293 0.50 17.19 ? ? ? ? ? . 40 CYS A CB 2348 ATOM 308 C CB B CYS A 2348 40 . -0.732 1.603 21.194 0.50 17.85 ? ? ? ? ? . 40 CYS A CB 2348 ATOM 309 S SG A CYS A 2348 40 . -0.070 1.366 22.877 0.50 18.83 ? ? ? ? ? . 40 CYS A SG 2348 ATOM 310 S SG B CYS A 2348 40 . 0.692 1.280 22.270 0.50 20.15 ? ? ? ? ? . 40 CYS A SG 2348 ATOM 311 N N . PRO A 2348 41 . 0.452 4.940 21.641 1.00 15.67 ? ? ? ? ? . 41 PRO A N 2348 ATOM 312 C CA . PRO A 2348 41 . 1.703 5.735 21.475 1.00 16.29 ? ? ? ? ? . 41 PRO A CA 2348 ATOM 313 C C . PRO A 2348 41 . 3.027 4.964 21.556 1.00 17.16 ? ? ? ? ? . 41 PRO A C 2348 ATOM 314 O O . PRO A 2348 41 . 3.835 5.088 20.625 1.00 16.58 ? ? ? ? ? . 41 PRO A O 2348 ATOM 315 C CB . PRO A 2348 41 . 1.589 6.838 22.534 1.00 16.29 ? ? ? ? ? . 41 PRO A CB 2348 ATOM 316 C CG . PRO A 2348 41 . 0.113 6.972 22.756 1.00 17.02 ? ? ? ? ? . 41 PRO A CG 2348 ATOM 317 C CD . PRO A 2348 41 . -0.466 5.598 22.594 1.00 16.25 ? ? ? ? ? . 41 PRO A CD 2348 ATOM 318 N N . PRO A 2348 42 . 3.238 4.137 22.603 1.00 16.73 ? ? ? ? ? . 42 PRO A N 2348 ATOM 319 C CA . PRO A 2348 42 . 4.509 3.413 22.587 1.00 16.97 ? ? ? ? ? . 42 PRO A CA 2348 ATOM 320 C C . PRO A 2348 42 . 4.682 2.470 21.399 1.00 17.31 ? ? ? ? ? . 42 PRO A C 2348 ATOM 321 O O . PRO A 2348 42 . 5.815 2.236 21.007 1.00 18.01 ? ? ? ? ? . 42 PRO A O 2348 ATOM 322 C CB . PRO A 2348 42 . 4.524 2.635 23.913 1.00 18.24 ? ? ? ? ? . 42 PRO A CB 2348 ATOM 323 C CG . PRO A 2348 42 . 3.144 2.716 24.442 1.00 20.34 ? ? ? ? ? . 42 PRO A CG 2348 ATOM 324 C CD . PRO A 2348 42 . 2.500 3.930 23.859 1.00 17.99 ? ? ? ? ? . 42 PRO A CD 2348 ATOM 325 N N . CYS A 2348 43 . 3.583 1.953 20.830 1.00 17.08 ? ? ? ? ? . 43 CYS A N 2348 ATOM 326 C CA . CYS A 2348 43 . 3.654 1.131 19.615 1.00 17.71 ? ? ? ? ? . 43 CYS A CA 2348 ATOM 327 C C . CYS A 2348 43 . 4.071 1.965 18.412 1.00 18.28 ? ? ? ? ? . 43 CYS A C 2348 ATOM 328 O O . CYS A 2348 43 . 4.896 1.539 17.592 1.00 17.92 ? ? ? ? ? . 43 CYS A O 2348 ATOM 329 C CB . CYS A 2348 43 . 2.302 0.486 19.283 1.00 16.62 ? ? ? ? ? . 43 CYS A CB 2348 ATOM 330 S SG . CYS A 2348 43 . 1.804 -0.806 20.436 1.00 17.97 ? ? ? ? ? . 43 CYS A SG 2348 ATOM 331 N N . ARG A 2348 44 . 3.472 3.148 18.300 1.00 18.14 ? ? ? ? ? . 44 ARG A N 2348 ATOM 332 C CA . ARG A 2348 44 . 3.794 4.048 17.197 1.00 19.48 ? ? ? ? ? . 44 ARG A CA 2348 ATOM 333 C C . ARG A 2348 44 . 5.273 4.436 17.232 1.00 18.72 ? ? ? ? ? . 44 ARG A C 2348 ATOM 334 O O . ARG A 2348 44 . 5.871 4.609 16.184 1.00 18.31 ? ? ? ? ? . 44 ARG A O 2348 ATOM 335 C CB . ARG A 2348 44 . 2.889 5.272 17.211 1.00 19.31 ? ? ? ? ? . 44 ARG A CB 2348 ATOM 336 C CG . ARG A 2348 44 . 1.429 4.933 16.938 1.00 20.47 ? ? ? ? ? . 44 ARG A CG 2348 ATOM 337 C CD . ARG A 2348 44 . 0.501 5.909 17.620 1.00 25.71 ? ? ? ? ? . 44 ARG A CD 2348 ATOM 338 N NE . ARG A 2348 44 . 0.489 7.222 16.986 1.00 27.26 ? ? ? ? ? . 44 ARG A NE 2348 ATOM 339 C CZ . ARG A 2348 44 . -0.417 7.656 16.109 1.00 32.49 ? ? ? ? ? . 44 ARG A CZ 2348 ATOM 340 N NH1 . ARG A 2348 44 . -1.424 6.879 15.692 1.00 36.29 ? ? ? ? ? 1+ 44 ARG A NH1 2348 ATOM 341 N NH2 . ARG A 2348 44 . -0.309 8.895 15.634 1.00 31.30 ? ? ? ? ? . 44 ARG A NH2 2348 ATOM 342 N N . GLY A 2348 45 . 5.852 4.549 18.432 1.00 16.87 ? ? ? ? ? . 45 GLY A N 2348 ATOM 343 C CA . GLY A 2348 45 . 7.291 4.825 18.587 1.00 16.30 ? ? ? ? ? . 45 GLY A CA 2348 ATOM 344 C C . GLY A 2348 45 . 8.197 3.625 18.399 1.00 17.31 ? ? ? ? ? . 45 GLY A C 2348 ATOM 345 O O . GLY A 2348 45 . 9.343 3.761 17.968 1.00 16.80 ? ? ? ? ? . 45 GLY A O 2348 ATOM 346 N N . PHE A 2348 46 . 7.690 2.440 18.711 1.00 17.16 ? ? ? ? ? . 46 PHE A N 2348 ATOM 347 C CA . PHE A 2348 46 . 8.479 1.220 18.586 1.00 16.13 ? ? ? ? ? . 46 PHE A CA 2348 ATOM 348 C C . PHE A 2348 46 . 8.512 0.651 17.162 1.00 16.60 ? ? ? ? ? . 46 PHE A C 2348 ATOM 349 O O . PHE A 2348 46 . 9.535 0.198 16.710 1.00 16.70 ? ? ? ? ? . 46 PHE A O 2348 ATOM 350 C CB . PHE A 2348 46 . 7.967 0.150 19.541 1.00 15.86 ? ? ? ? ? . 46 PHE A CB 2348 ATOM 351 C CG . PHE A 2348 46 . 8.771 -1.108 19.489 1.00 16.05 ? ? ? ? ? . 46 PHE A CG 2348 ATOM 352 C CD1 . PHE A 2348 46 . 10.130 -1.082 19.799 1.00 17.33 ? ? ? ? ? . 46 PHE A CD1 2348 ATOM 353 C CD2 . PHE A 2348 46 . 8.199 -2.300 19.084 1.00 17.49 ? ? ? ? ? . 46 PHE A CD2 2348 ATOM 354 C CE1 . PHE A 2348 46 . 10.889 -2.235 19.714 1.00 18.28 ? ? ? ? ? . 46 PHE A CE1 2348 ATOM 355 C CE2 . PHE A 2348 46 . 8.954 -3.462 19.011 1.00 17.09 ? ? ? ? ? . 46 PHE A CE2 2348 ATOM 356 C CZ . PHE A 2348 46 . 10.300 -3.424 19.324 1.00 17.72 ? ? ? ? ? . 46 PHE A CZ 2348 ATOM 357 N N . THR A 2348 47 . 7.376 0.671 16.476 1.00 16.70 ? ? ? ? ? . 47 THR A N 2348 ATOM 358 C CA . THR A 2348 47 . 7.269 0.187 15.102 1.00 15.83 ? ? ? ? ? . 47 THR A CA 2348 ATOM 359 C C . THR A 2348 47 . 8.421 0.636 14.151 1.00 16.94 ? ? ? ? ? . 47 THR A C 2348 ATOM 360 O O . THR A 2348 47 . 9.011 -0.218 13.479 1.00 16.96 ? ? ? ? ? . 47 THR A O 2348 ATOM 361 C CB . THR A 2348 47 . 5.867 0.510 14.547 1.00 16.66 ? ? ? ? ? . 47 THR A CB 2348 ATOM 362 C CG2 . THR A 2348 47 . 5.752 0.297 13.034 1.00 16.80 ? ? ? ? ? . 47 THR A CG2 2348 ATOM 363 O OG1 . THR A 2348 47 . 4.915 -0.318 15.229 1.00 18.14 ? ? ? ? ? . 47 THR A OG1 2348 ATOM 364 N N . PRO A 2348 48 . 8.758 1.947 14.112 1.00 16.14 ? ? ? ? ? . 48 PRO A N 2348 ATOM 365 C CA . PRO A 2348 48 . 9.871 2.352 13.228 1.00 15.16 ? ? ? ? ? . 48 PRO A CA 2348 ATOM 366 C C . PRO A 2348 48 . 11.242 1.798 13.654 1.00 15.43 ? ? ? ? ? . 48 PRO A C 2348 ATOM 367 O O . PRO A 2348 48 . 12.110 1.557 12.800 1.00 15.62 ? ? ? ? ? . 48 PRO A O 2348 ATOM 368 C CB . PRO A 2348 48 . 9.825 3.888 13.265 1.00 15.95 ? ? ? ? ? . 48 PRO A CB 2348 ATOM 369 C CG . PRO A 2348 48 . 9.028 4.237 14.475 1.00 16.18 ? ? ? ? ? . 48 PRO A CG 2348 ATOM 370 C CD . PRO A 2348 48 . 8.057 3.109 14.670 1.00 16.84 ? ? ? ? ? . 48 PRO A CD 2348 ATOM 371 N N . VAL A 2348 49 . 11.421 1.568 14.952 1.00 15.24 ? ? ? ? ? . 49 VAL A N 2348 ATOM 372 C CA . VAL A 2348 49 . 12.653 0.979 15.497 1.00 15.00 ? ? ? ? ? . 49 VAL A CA 2348 ATOM 373 C C . VAL A 2348 49 . 12.738 -0.490 15.080 1.00 16.44 ? ? ? ? ? . 49 VAL A C 2348 ATOM 374 O O . VAL A 2348 49 . 13.785 -0.970 14.589 1.00 17.54 ? ? ? ? ? . 49 VAL A O 2348 ATOM 375 C CB . VAL A 2348 49 . 12.683 1.119 17.046 1.00 14.01 ? ? ? ? ? . 49 VAL A CB 2348 ATOM 376 C CG1 . VAL A 2348 49 . 13.850 0.377 17.659 1.00 13.62 ? ? ? ? ? . 49 VAL A CG1 2348 ATOM 377 C CG2 . VAL A 2348 49 . 12.703 2.591 17.436 1.00 13.12 ? ? ? ? ? . 49 VAL A CG2 2348 ATOM 378 N N . LEU A 2348 50 . 11.629 -1.205 15.264 1.00 16.04 ? ? ? ? ? . 50 LEU A N 2348 ATOM 379 C CA . LEU A 2348 50 . 11.549 -2.607 14.859 1.00 16.65 ? ? ? ? ? . 50 LEU A CA 2348 ATOM 380 C C . LEU A 2348 50 . 11.728 -2.754 13.346 1.00 16.14 ? ? ? ? ? . 50 LEU A C 2348 ATOM 381 O O . LEU A 2348 50 . 12.392 -3.689 12.896 1.00 17.52 ? ? ? ? ? . 50 LEU A O 2348 ATOM 382 C CB . LEU A 2348 50 . 10.228 -3.235 15.291 1.00 17.24 ? ? ? ? ? . 50 LEU A CB 2348 ATOM 383 C CG . LEU A 2348 50 . 10.134 -4.760 15.088 1.00 18.60 ? ? ? ? ? . 50 LEU A CG 2348 ATOM 384 C CD1 . LEU A 2348 50 . 11.292 -5.525 15.736 1.00 18.52 ? ? ? ? ? . 50 LEU A CD1 2348 ATOM 385 C CD2 . LEU A 2348 50 . 8.808 -5.265 15.625 1.00 20.67 ? ? ? ? ? . 50 LEU A CD2 2348 ATOM 386 N N . ALA A 2348 51 . 11.158 -1.827 12.578 1.00 15.16 ? ? ? ? ? . 51 ALA A N 2348 ATOM 387 C CA . ALA A 2348 51 . 11.350 -1.791 11.114 1.00 16.39 ? ? ? ? ? . 51 ALA A CA 2348 ATOM 388 C C . ALA A 2348 51 . 12.807 -1.689 10.702 1.00 16.39 ? ? ? ? ? . 51 ALA A C 2348 ATOM 389 O O . ALA A 2348 51 . 13.234 -2.388 9.789 1.00 16.12 ? ? ? ? ? . 51 ALA A O 2348 ATOM 390 C CB . ALA A 2348 51 . 10.558 -0.659 10.489 1.00 16.94 ? ? ? ? ? . 51 ALA A CB 2348 ATOM 391 N N . GLU A 2348 52 . 13.571 -0.833 11.380 1.00 15.83 ? ? ? ? ? . 52 GLU A N 2348 ATOM 392 C CA . GLU A 2348 52 . 15.018 -0.741 11.136 1.00 17.29 ? ? ? ? ? . 52 GLU A CA 2348 ATOM 393 C C . GLU A 2348 52 . 15.738 -2.056 11.452 1.00 16.77 ? ? ? ? ? . 52 GLU A C 2348 ATOM 394 O O . GLU A 2348 52 . 16.547 -2.538 10.644 1.00 17.83 ? ? ? ? ? . 52 GLU A O 2348 ATOM 395 C CB . GLU A 2348 52 . 15.655 0.398 11.929 1.00 19.04 ? ? ? ? ? . 52 GLU A CB 2348 ATOM 396 C CG . GLU A 2348 52 . 15.197 1.779 11.502 1.00 23.10 ? ? ? ? ? . 52 GLU A CG 2348 ATOM 397 C CD . GLU A 2348 52 . 15.652 2.158 10.111 1.00 27.07 ? ? ? ? ? . 52 GLU A CD 2348 ATOM 398 O OE1 . GLU A 2348 52 . 16.805 1.871 9.753 1.00 26.53 ? ? ? ? ? . 52 GLU A OE1 2348 ATOM 399 O OE2 . GLU A 2348 52 . 14.838 2.741 9.372 1.00 35.08 ? ? ? ? ? 1- 52 GLU A OE2 2348 ATOM 400 N N . PHE A 2348 53 . 15.440 -2.626 12.617 1.00 17.09 ? ? ? ? ? . 53 PHE A N 2348 ATOM 401 C CA . PHE A 2348 53 . 15.961 -3.927 13.008 1.00 17.72 ? ? ? ? ? . 53 PHE A CA 2348 ATOM 402 C C . PHE A 2348 53 . 15.659 -5.004 11.960 1.00 18.04 ? ? ? ? ? . 53 PHE A C 2348 ATOM 403 O O . PHE A 2348 53 . 16.544 -5.765 11.559 1.00 17.15 ? ? ? ? ? . 53 PHE A O 2348 ATOM 404 C CB . PHE A 2348 53 . 15.394 -4.344 14.367 1.00 17.66 ? ? ? ? ? . 53 PHE A CB 2348 ATOM 405 C CG . PHE A 2348 53 . 16.073 -5.523 14.955 1.00 17.72 ? ? ? ? ? . 53 PHE A CG 2348 ATOM 406 C CD1 . PHE A 2348 53 . 17.204 -5.365 15.759 1.00 19.84 ? ? ? ? ? . 53 PHE A CD1 2348 ATOM 407 C CD2 . PHE A 2348 53 . 15.613 -6.800 14.692 1.00 18.67 ? ? ? ? ? . 53 PHE A CD2 2348 ATOM 408 C CE1 . PHE A 2348 53 . 17.855 -6.470 16.294 1.00 18.69 ? ? ? ? ? . 53 PHE A CE1 2348 ATOM 409 C CE2 . PHE A 2348 53 . 16.250 -7.909 15.237 1.00 19.49 ? ? ? ? ? . 53 PHE A CE2 2348 ATOM 410 C CZ . PHE A 2348 53 . 17.381 -7.740 16.022 1.00 19.50 ? ? ? ? ? . 53 PHE A CZ 2348 ATOM 411 N N . TYR A 2348 54 . 14.402 -5.066 11.538 1.00 18.62 ? ? ? ? ? . 54 TYR A N 2348 ATOM 412 C CA . TYR A 2348 54 . 13.957 -5.985 10.484 1.00 16.78 ? ? ? ? ? . 54 TYR A CA 2348 ATOM 413 C C . TYR A 2348 54 . 14.740 -5.808 9.197 1.00 17.12 ? ? ? ? ? . 54 TYR A C 2348 ATOM 414 O O . TYR A 2348 54 . 15.274 -6.777 8.637 1.00 16.38 ? ? ? ? ? . 54 TYR A O 2348 ATOM 415 C CB . TYR A 2348 54 . 12.465 -5.744 10.204 1.00 17.54 ? ? ? ? ? . 54 TYR A CB 2348 ATOM 416 C CG . TYR A 2348 54 . 11.834 -6.704 9.220 1.00 17.88 ? ? ? ? ? . 54 TYR A CG 2348 ATOM 417 C CD1 . TYR A 2348 54 . 11.284 -7.902 9.655 1.00 17.99 ? ? ? ? ? . 54 TYR A CD1 2348 ATOM 418 C CD2 . TYR A 2348 54 . 11.783 -6.414 7.859 1.00 18.12 ? ? ? ? ? . 54 TYR A CD2 2348 ATOM 419 C CE1 . TYR A 2348 54 . 10.703 -8.787 8.776 1.00 17.40 ? ? ? ? ? . 54 TYR A CE1 2348 ATOM 420 C CE2 . TYR A 2348 54 . 11.201 -7.294 6.965 1.00 18.18 ? ? ? ? ? . 54 TYR A CE2 2348 ATOM 421 C CZ . TYR A 2348 54 . 10.656 -8.477 7.430 1.00 18.40 ? ? ? ? ? . 54 TYR A CZ 2348 ATOM 422 O OH . TYR A 2348 54 . 10.066 -9.352 6.548 1.00 18.64 ? ? ? ? ? . 54 TYR A OH 2348 ATOM 423 N N . GLU A 2348 55 . 14.825 -4.567 8.729 1.00 18.35 ? ? ? ? ? . 55 GLU A N 2348 ATOM 424 C CA . GLU A 2348 55 . 15.479 -4.298 7.450 1.00 19.54 ? ? ? ? ? . 55 GLU A CA 2348 ATOM 425 C C . GLU A 2348 55 . 16.941 -4.728 7.457 1.00 17.47 ? ? ? ? ? . 55 GLU A C 2348 ATOM 426 O O . GLU A 2348 55 . 17.426 -5.225 6.444 1.00 16.00 ? ? ? ? ? . 55 GLU A O 2348 ATOM 427 C CB . GLU A 2348 55 . 15.344 -2.832 7.037 1.00 23.35 ? ? ? ? ? . 55 GLU A CB 2348 ATOM 428 C CG . GLU A 2348 55 . 13.904 -2.394 6.757 1.00 27.78 ? ? ? ? ? . 55 GLU A CG 2348 ATOM 429 C CD . GLU A 2348 55 . 13.379 -2.755 5.374 1.00 33.34 ? ? ? ? ? . 55 GLU A CD 2348 ATOM 430 O OE1 . GLU A 2348 55 . 13.957 -3.640 4.695 1.00 38.81 ? ? ? ? ? . 55 GLU A OE1 2348 ATOM 431 O OE2 . GLU A 2348 55 . 12.365 -2.144 4.970 1.00 33.79 ? ? ? ? ? 1- 55 GLU A OE2 2348 ATOM 432 N N . LYS A 2348 56 . 17.630 -4.527 8.582 1.00 17.29 ? ? ? ? ? . 56 LYS A N 2348 ATOM 433 C CA . LYS A 2348 56 . 19.040 -4.884 8.705 1.00 17.51 ? ? ? ? ? . 56 LYS A CA 2348 ATOM 434 C C . LYS A 2348 56 . 19.255 -6.396 8.816 1.00 15.74 ? ? ? ? ? . 56 LYS A C 2348 ATOM 435 O O . LYS A 2348 56 . 20.181 -6.935 8.183 1.00 16.74 ? ? ? ? ? . 56 LYS A O 2348 ATOM 436 C CB . LYS A 2348 56 . 19.699 -4.158 9.902 1.00 20.10 ? ? ? ? ? . 56 LYS A CB 2348 ATOM 437 C CG . LYS A 2348 56 . 21.202 -4.417 10.024 1.00 22.06 ? ? ? ? ? . 56 LYS A CG 2348 ATOM 438 C CD . LYS A 2348 56 . 21.921 -3.570 11.086 1.00 24.35 ? ? ? ? ? . 56 LYS A CD 2348 ATOM 439 C CE . LYS A 2348 56 . 23.451 -3.707 10.942 1.00 26.58 ? ? ? ? ? . 56 LYS A CE 2348 ATOM 440 N NZ . LYS A 2348 56 . 24.320 -2.988 11.937 1.00 24.67 ? ? ? ? ? 1+ 56 LYS A NZ 2348 ATOM 441 N N . HIS A 2348 57 . 18.415 -7.076 9.599 1.00 14.57 ? ? ? ? ? . 57 HIS A N 2348 ATOM 442 C CA . HIS A 2348 57 . 18.718 -8.424 10.085 1.00 15.29 ? ? ? ? ? . 57 HIS A CA 2348 ATOM 443 C C . HIS A 2348 57 . 17.814 -9.569 9.624 1.00 15.31 ? ? ? ? ? . 57 HIS A C 2348 ATOM 444 O O . HIS A 2348 57 . 18.170 -10.726 9.880 1.00 16.33 ? ? ? ? ? . 57 HIS A O 2348 ATOM 445 C CB . HIS A 2348 57 . 18.690 -8.468 11.612 1.00 15.83 ? ? ? ? ? . 57 HIS A CB 2348 ATOM 446 C CG . HIS A 2348 57 . 19.586 -7.481 12.281 1.00 16.66 ? ? ? ? ? . 57 HIS A CG 2348 ATOM 447 C CD2 . HIS A 2348 57 . 19.312 -6.513 13.190 1.00 18.19 ? ? ? ? ? . 57 HIS A CD2 2348 ATOM 448 N ND1 . HIS A 2348 57 . 20.944 -7.457 12.094 1.00 16.54 ? ? ? ? ? . 57 HIS A ND1 2348 ATOM 449 C CE1 . HIS A 2348 57 . 21.471 -6.502 12.836 1.00 18.76 ? ? ? ? ? . 57 HIS A CE1 2348 ATOM 450 N NE2 . HIS A 2348 57 . 20.502 -5.918 13.519 1.00 17.63 ? ? ? ? ? . 57 HIS A NE2 2348 ATOM 451 N N . HIS A 2348 58 . 16.668 -9.294 8.996 1.00 15.07 ? ? ? ? ? . 58 HIS A N 2348 ATOM 452 C CA . HIS A 2348 58 . 15.663 -10.363 8.809 1.00 15.32 ? ? ? ? ? . 58 HIS A CA 2348 ATOM 453 C C . HIS A 2348 58 . 16.142 -11.508 7.916 1.00 15.60 ? ? ? ? ? . 58 HIS A C 2348 ATOM 454 O O . HIS A 2348 58 . 15.814 -12.666 8.172 1.00 16.71 ? ? ? ? ? . 58 HIS A O 2348 ATOM 455 C CB . HIS A 2348 58 . 14.270 -9.838 8.384 1.00 16.50 ? ? ? ? ? . 58 HIS A CB 2348 ATOM 456 C CG . HIS A 2348 58 . 14.110 -9.576 6.917 1.00 16.28 ? ? ? ? ? . 58 HIS A CG 2348 ATOM 457 C CD2 . HIS A 2348 58 . 13.530 -10.314 5.939 1.00 17.28 ? ? ? ? ? . 58 HIS A CD2 2348 ATOM 458 N ND1 . HIS A 2348 58 . 14.514 -8.401 6.318 1.00 18.08 ? ? ? ? ? . 58 HIS A ND1 2348 ATOM 459 C CE1 . HIS A 2348 58 . 14.236 -8.449 5.025 1.00 19.03 ? ? ? ? ? . 58 HIS A CE1 2348 ATOM 460 N NE2 . HIS A 2348 58 . 13.622 -9.592 4.773 1.00 19.90 ? ? ? ? ? . 58 HIS A NE2 2348 ATOM 461 N N . VAL A 2348 59 . 16.953 -11.183 6.909 1.00 14.27 ? ? ? ? ? . 59 VAL A N 2348 ATOM 462 C CA . VAL A 2348 59 . 17.521 -12.205 6.060 1.00 14.71 ? ? ? ? ? . 59 VAL A CA 2348 ATOM 463 C C . VAL A 2348 59 . 18.661 -12.908 6.783 1.00 14.94 ? ? ? ? ? . 59 VAL A C 2348 ATOM 464 O O . VAL A 2348 59 . 18.645 -14.134 6.937 1.00 14.29 ? ? ? ? ? . 59 VAL A O 2348 ATOM 465 C CB . VAL A 2348 59 . 17.994 -11.612 4.722 1.00 14.66 ? ? ? ? ? . 59 VAL A CB 2348 ATOM 466 C CG1 . VAL A 2348 59 . 18.666 -12.682 3.873 1.00 14.25 ? ? ? ? ? . 59 VAL A CG1 2348 ATOM 467 C CG2 . VAL A 2348 59 . 16.805 -10.993 3.980 1.00 14.94 ? ? ? ? ? . 59 VAL A CG2 2348 ATOM 468 N N . ALA A 2348 60 . 19.645 -12.144 7.246 1.00 15.73 ? ? ? ? ? . 60 ALA A N 2348 ATOM 469 C CA . ALA A 2348 60 . 20.864 -12.747 7.823 1.00 17.51 ? ? ? ? ? . 60 ALA A CA 2348 ATOM 470 C C . ALA A 2348 60 . 20.557 -13.591 9.054 1.00 16.03 ? ? ? ? ? . 60 ALA A C 2348 ATOM 471 O O . ALA A 2348 60 . 21.143 -14.653 9.242 1.00 15.29 ? ? ? ? ? . 60 ALA A O 2348 ATOM 472 C CB . ALA A 2348 60 . 21.898 -11.674 8.149 1.00 18.78 ? ? ? ? ? . 60 ALA A CB 2348 ATOM 473 N N . LYS A 2348 61 . 19.598 -13.149 9.864 1.00 14.83 ? ? ? ? ? . 61 LYS A N 2348 ATOM 474 C CA . LYS A 2348 61 . 19.226 -13.871 11.088 1.00 15.73 ? ? ? ? ? . 61 LYS A CA 2348 ATOM 475 C C . LYS A 2348 61 . 17.927 -14.693 10.936 1.00 17.18 ? ? ? ? ? . 61 LYS A C 2348 ATOM 476 O O . LYS A 2348 61 . 17.409 -15.236 11.923 1.00 18.10 ? ? ? ? ? . 61 LYS A O 2348 ATOM 477 C CB . LYS A 2348 61 . 19.132 -12.891 12.265 1.00 15.99 ? ? ? ? ? . 61 LYS A CB 2348 ATOM 478 C CG . LYS A 2348 61 . 20.452 -12.166 12.504 1.00 18.28 ? ? ? ? ? . 61 LYS A CG 2348 ATOM 479 C CD . LYS A 2348 61 . 20.439 -11.283 13.741 1.00 20.10 ? ? ? ? ? . 61 LYS A CD 2348 ATOM 480 C CE . LYS A 2348 61 . 21.754 -10.505 13.895 1.00 20.17 ? ? ? ? ? . 61 LYS A CE 2348 ATOM 481 N NZ . LYS A 2348 61 . 22.893 -11.355 14.328 1.00 19.55 ? ? ? ? ? 1+ 61 LYS A NZ 2348 ATOM 482 N N . ASN A 2348 62 . 17.428 -14.784 9.701 1.00 16.86 ? ? ? ? ? . 62 ASN A N 2348 ATOM 483 C CA . ASN A 2348 62 . 16.360 -15.705 9.305 1.00 16.87 ? ? ? ? ? . 62 ASN A CA 2348 ATOM 484 C C . ASN A 2348 62 . 15.135 -15.622 10.221 1.00 16.20 ? ? ? ? ? . 62 ASN A C 2348 ATOM 485 O O . ASN A 2348 62 . 14.743 -16.606 10.871 1.00 15.82 ? ? ? ? ? . 62 ASN A O 2348 ATOM 486 C CB . ASN A 2348 62 . 16.895 -17.137 9.242 1.00 17.98 ? ? ? ? ? . 62 ASN A CB 2348 ATOM 487 C CG . ASN A 2348 62 . 15.989 -18.059 8.453 1.00 17.03 ? ? ? ? ? . 62 ASN A CG 2348 ATOM 488 N ND2 . ASN A 2348 62 . 15.720 -19.247 8.994 1.00 15.43 ? ? ? ? ? . 62 ASN A ND2 2348 ATOM 489 O OD1 . ASN A 2348 62 . 15.544 -17.708 7.365 1.00 16.98 ? ? ? ? ? . 62 ASN A OD1 2348 ATOM 490 N N . PHE A 2348 63 . 14.555 -14.436 10.284 1.00 15.83 ? ? ? ? ? . 63 PHE A N 2348 ATOM 491 C CA . PHE A 2348 63 . 13.315 -14.245 11.005 1.00 15.98 ? ? ? ? ? . 63 PHE A CA 2348 ATOM 492 C C . PHE A 2348 63 . 12.272 -13.479 10.209 1.00 16.65 ? ? ? ? ? . 63 PHE A C 2348 ATOM 493 O O . PHE A 2348 63 . 12.540 -12.876 9.147 1.00 14.62 ? ? ? ? ? . 63 PHE A O 2348 ATOM 494 C CB . PHE A 2348 63 . 13.555 -13.608 12.392 1.00 15.93 ? ? ? ? ? . 63 PHE A CB 2348 ATOM 495 C CG . PHE A 2348 63 . 14.065 -12.191 12.351 1.00 16.47 ? ? ? ? ? . 63 PHE A CG 2348 ATOM 496 C CD1 . PHE A 2348 63 . 13.192 -11.131 12.154 1.00 17.02 ? ? ? ? ? . 63 PHE A CD1 2348 ATOM 497 C CD2 . PHE A 2348 63 . 15.419 -11.914 12.539 1.00 17.98 ? ? ? ? ? . 63 PHE A CD2 2348 ATOM 498 C CE1 . PHE A 2348 63 . 13.646 -9.823 12.123 1.00 16.99 ? ? ? ? ? . 63 PHE A CE1 2348 ATOM 499 C CE2 . PHE A 2348 63 . 15.874 -10.605 12.516 1.00 17.17 ? ? ? ? ? . 63 PHE A CE2 2348 ATOM 500 C CZ . PHE A 2348 63 . 14.992 -9.562 12.310 1.00 17.23 ? ? ? ? ? . 63 PHE A CZ 2348 ATOM 501 N N . GLU A 2348 64 . 11.065 -13.521 10.753 1.00 16.63 ? ? ? ? ? . 64 GLU A N 2348 ATOM 502 C CA . GLU A 2348 64 . 9.931 -12.790 10.211 1.00 16.06 ? ? ? ? ? . 64 GLU A CA 2348 ATOM 503 C C . GLU A 2348 64 . 9.161 -12.165 11.375 1.00 16.89 ? ? ? ? ? . 64 GLU A C 2348 ATOM 504 O O . GLU A 2348 64 . 9.251 -12.634 12.498 1.00 16.07 ? ? ? ? ? . 64 GLU A O 2348 ATOM 505 C CB . GLU A 2348 64 . 9.043 -13.756 9.433 1.00 17.67 ? ? ? ? ? . 64 GLU A CB 2348 ATOM 506 C CG . GLU A 2348 64 . 7.934 -13.109 8.651 1.00 20.12 ? ? ? ? ? . 64 GLU A CG 2348 ATOM 507 C CD . GLU A 2348 64 . 8.458 -12.085 7.676 1.00 20.42 ? ? ? ? ? . 64 GLU A CD 2348 ATOM 508 O OE1 . GLU A 2348 64 . 8.489 -10.901 8.045 1.00 19.99 ? ? ? ? ? . 64 GLU A OE1 2348 ATOM 509 O OE2 . GLU A 2348 64 . 8.839 -12.477 6.559 1.00 20.73 ? ? ? ? ? 1- 64 GLU A OE2 2348 ATOM 510 N N . VAL A 2348 65 . 8.413 -11.107 11.097 1.00 16.69 ? ? ? ? ? . 65 VAL A N 2348 ATOM 511 C CA . VAL A 2348 65 . 7.578 -10.458 12.100 1.00 15.86 ? ? ? ? ? . 65 VAL A CA 2348 ATOM 512 C C . VAL A 2348 65 . 6.140 -10.529 11.600 1.00 14.98 ? ? ? ? ? . 65 VAL A C 2348 ATOM 513 O O . VAL A 2348 65 . 5.879 -10.397 10.391 1.00 14.44 ? ? ? ? ? . 65 VAL A O 2348 ATOM 514 C CB . VAL A 2348 65 . 8.066 -9.013 12.345 1.00 17.34 ? ? ? ? ? . 65 VAL A CB 2348 ATOM 515 C CG1 . VAL A 2348 65 . 7.112 -8.225 13.239 1.00 18.32 ? ? ? ? ? . 65 VAL A CG1 2348 ATOM 516 C CG2 . VAL A 2348 65 . 9.464 -9.038 12.945 1.00 18.63 ? ? ? ? ? . 65 VAL A CG2 2348 ATOM 517 N N . VAL A 2348 66 . 5.212 -10.798 12.517 1.00 14.94 ? ? ? ? ? . 66 VAL A N 2348 ATOM 518 C CA . VAL A 2348 66 . 3.791 -10.901 12.186 1.00 15.77 ? ? ? ? ? . 66 VAL A CA 2348 ATOM 519 C C . VAL A 2348 66 . 3.013 -9.926 13.068 1.00 16.12 ? ? ? ? ? . 66 VAL A C 2348 ATOM 520 O O . VAL A 2348 66 . 2.954 -10.091 14.287 1.00 18.95 ? ? ? ? ? . 66 VAL A O 2348 ATOM 521 C CB . VAL A 2348 66 . 3.248 -12.327 12.365 1.00 15.17 ? ? ? ? ? . 66 VAL A CB 2348 ATOM 522 C CG1 . VAL A 2348 66 . 1.807 -12.407 11.883 1.00 14.64 ? ? ? ? ? . 66 VAL A CG1 2348 ATOM 523 C CG2 . VAL A 2348 66 . 4.127 -13.332 11.615 1.00 15.43 ? ? ? ? ? . 66 VAL A CG2 2348 ATOM 524 N N . LEU A 2348 67 . 2.413 -8.925 12.441 1.00 14.97 ? ? ? ? ? . 67 LEU A N 2348 ATOM 525 C CA . LEU A 2348 67 . 1.558 -7.976 13.155 1.00 15.42 ? ? ? ? ? . 67 LEU A CA 2348 ATOM 526 C C . LEU A 2348 67 . 0.311 -8.673 13.669 1.00 14.43 ? ? ? ? ? . 67 LEU A C 2348 ATOM 527 O O . LEU A 2348 67 . -0.406 -9.315 12.914 1.00 15.61 ? ? ? ? ? . 67 LEU A O 2348 ATOM 528 C CB . LEU A 2348 67 . 1.134 -6.830 12.239 1.00 16.16 ? ? ? ? ? . 67 LEU A CB 2348 ATOM 529 C CG . LEU A 2348 67 . 0.138 -5.813 12.822 1.00 16.89 ? ? ? ? ? . 67 LEU A CG 2348 ATOM 530 C CD1 . LEU A 2348 67 . 0.748 -5.117 14.038 1.00 18.06 ? ? ? ? ? . 67 LEU A CD1 2348 ATOM 531 C CD2 . LEU A 2348 67 . -0.302 -4.804 11.764 1.00 16.86 ? ? ? ? ? . 67 LEU A CD2 2348 ATOM 532 N N . ILE A 2348 68 . 0.069 -8.515 14.959 1.00 16.21 ? ? ? ? ? . 68 ILE A N 2348 ATOM 533 C CA . ILE A 2348 68 . -1.140 -8.969 15.618 1.00 16.24 ? ? ? ? ? . 68 ILE A CA 2348 ATOM 534 C C . ILE A 2348 68 . -1.759 -7.692 16.195 1.00 16.84 ? ? ? ? ? . 68 ILE A C 2348 ATOM 535 O O . ILE A 2348 68 . -1.309 -7.202 17.220 1.00 16.78 ? ? ? ? ? . 68 ILE A O 2348 ATOM 536 C CB . ILE A 2348 68 . -0.842 -9.969 16.752 1.00 15.81 ? ? ? ? ? . 68 ILE A CB 2348 ATOM 537 C CG1 . ILE A 2348 68 . 0.100 -11.106 16.287 1.00 15.85 ? ? ? ? ? . 68 ILE A CG1 2348 ATOM 538 C CG2 . ILE A 2348 68 . -2.143 -10.534 17.291 1.00 16.11 ? ? ? ? ? . 68 ILE A CG2 2348 ATOM 539 C CD1 . ILE A 2348 68 . -0.444 -11.963 15.172 1.00 15.85 ? ? ? ? ? . 68 ILE A CD1 2348 ATOM 540 N N . SER A 2348 69 . -2.769 -7.158 15.519 1.00 18.12 ? ? ? ? ? . 69 SER A N 2348 ATOM 541 C CA . SER A 2348 69 . -3.262 -5.825 15.839 1.00 18.34 ? ? ? ? ? . 69 SER A CA 2348 ATOM 542 C C . SER A 2348 69 . -4.568 -5.818 16.640 1.00 17.36 ? ? ? ? ? . 69 SER A C 2348 ATOM 543 O O . SER A 2348 69 . -5.517 -6.553 16.339 1.00 15.89 ? ? ? ? ? . 69 SER A O 2348 ATOM 544 C CB . SER A 2348 69 . -3.454 -5.013 14.563 1.00 20.93 ? ? ? ? ? . 69 SER A CB 2348 ATOM 545 O OG . SER A 2348 69 . -3.970 -3.726 14.871 1.00 22.79 ? ? ? ? ? . 69 SER A OG 2348 ATOM 546 N N . TRP A 2348 70 . -4.612 -4.932 17.630 1.00 17.71 ? ? ? ? ? . 70 TRP A N 2348 ATOM 547 C CA . TRP A 2348 70 . -5.849 -4.612 18.370 1.00 17.54 ? ? ? ? ? . 70 TRP A CA 2348 ATOM 548 C C . TRP A 2348 70 . -6.788 -3.654 17.619 1.00 16.23 ? ? ? ? ? . 70 TRP A C 2348 ATOM 549 O O . TRP A 2348 70 . -7.870 -3.325 18.129 1.00 15.84 ? ? ? ? ? . 70 TRP A O 2348 ATOM 550 C CB . TRP A 2348 70 . -5.522 -4.043 19.773 1.00 18.64 ? ? ? ? ? . 70 TRP A CB 2348 ATOM 551 C CG . TRP A 2348 70 . -5.764 -5.026 20.876 1.00 18.49 ? ? ? ? ? . 70 TRP A CG 2348 ATOM 552 C CD1 . TRP A 2348 70 . -6.897 -5.175 21.635 1.00 20.30 ? ? ? ? ? . 70 TRP A CD1 2348 ATOM 553 C CD2 . TRP A 2348 70 . -4.846 -6.010 21.326 1.00 19.25 ? ? ? ? ? . 70 TRP A CD2 2348 ATOM 554 C CE2 . TRP A 2348 70 . -5.481 -6.736 22.357 1.00 20.72 ? ? ? ? ? . 70 TRP A CE2 2348 ATOM 555 C CE3 . TRP A 2348 70 . -3.546 -6.347 20.958 1.00 20.16 ? ? ? ? ? . 70 TRP A CE3 2348 ATOM 556 N NE1 . TRP A 2348 70 . -6.733 -6.207 22.522 1.00 19.85 ? ? ? ? ? . 70 TRP A NE1 2348 ATOM 557 C CZ2 . TRP A 2348 70 . -4.852 -7.783 23.021 1.00 20.72 ? ? ? ? ? . 70 TRP A CZ2 2348 ATOM 558 C CZ3 . TRP A 2348 70 . -2.918 -7.378 21.619 1.00 21.27 ? ? ? ? ? . 70 TRP A CZ3 2348 ATOM 559 C CH2 . TRP A 2348 70 . -3.570 -8.090 22.638 1.00 22.10 ? ? ? ? ? . 70 TRP A CH2 2348 ATOM 560 N N . ASP A 2348 71 . -6.400 -3.183 16.430 1.00 14.95 ? ? ? ? ? . 71 ASP A N 2348 ATOM 561 C CA . ASP A 2348 71 . -7.261 -2.280 15.672 1.00 15.71 ? ? ? ? ? . 71 ASP A CA 2348 ATOM 562 C C . ASP A 2348 71 . -8.605 -2.930 15.328 1.00 14.08 ? ? ? ? ? . 71 ASP A C 2348 ATOM 563 O O . ASP A 2348 71 . -8.633 -4.074 14.887 1.00 13.83 ? ? ? ? ? . 71 ASP A O 2348 ATOM 564 C CB . ASP A 2348 71 . -6.575 -1.838 14.377 1.00 16.40 ? ? ? ? ? . 71 ASP A CB 2348 ATOM 565 C CG . ASP A 2348 71 . -5.488 -0.813 14.617 1.00 16.78 ? ? ? ? ? . 71 ASP A CG 2348 ATOM 566 O OD1 . ASP A 2348 71 . -5.861 0.357 14.863 1.00 16.06 ? ? ? ? ? . 71 ASP A OD1 2348 ATOM 567 O OD2 . ASP A 2348 71 . -4.277 -1.173 14.553 1.00 18.80 ? ? ? ? ? 1- 71 ASP A OD2 2348 ATOM 568 N N . GLU A 2348 72 . -9.689 -2.197 15.550 1.00 13.55 ? ? ? ? ? . 72 GLU A N 2348 ATOM 569 C CA A GLU A 2348 72 . -11.051 -2.601 15.169 0.66 14.70 ? ? ? ? ? . 72 GLU A CA 2348 ATOM 570 C CA B GLU A 2348 72 . -11.003 -2.662 15.116 0.34 14.17 ? ? ? ? ? . 72 GLU A CA 2348 ATOM 571 C C . GLU A 2348 72 . -11.544 -1.845 13.940 1.00 14.43 ? ? ? ? ? . 72 GLU A C 2348 ATOM 572 O O . GLU A 2348 72 . -12.612 -2.162 13.403 1.00 15.02 ? ? ? ? ? . 72 GLU A O 2348 ATOM 573 C CB A GLU A 2348 72 . -12.032 -2.365 16.325 0.66 15.58 ? ? ? ? ? . 72 GLU A CB 2348 ATOM 574 C CB B GLU A 2348 72 . -11.951 -2.732 16.315 0.34 14.14 ? ? ? ? ? . 72 GLU A CB 2348 ATOM 575 C CG A GLU A 2348 72 . -11.825 -3.284 17.523 0.66 17.74 ? ? ? ? ? . 72 GLU A CG 2348 ATOM 576 C CG B GLU A 2348 72 . -11.456 -3.763 17.335 0.34 14.63 ? ? ? ? ? . 72 GLU A CG 2348 ATOM 577 C CD A GLU A 2348 72 . -12.840 -3.071 18.643 0.66 18.62 ? ? ? ? ? . 72 GLU A CD 2348 ATOM 578 C CD B GLU A 2348 72 . -12.487 -4.156 18.381 0.34 15.00 ? ? ? ? ? . 72 GLU A CD 2348 ATOM 579 O OE1 A GLU A 2348 72 . -13.397 -1.946 18.785 0.66 20.42 ? ? ? ? ? . 72 GLU A OE1 2348 ATOM 580 O OE2 A GLU A 2348 72 . -13.078 -4.039 19.399 0.66 18.80 ? ? ? ? ? 1- 72 GLU A OE2 2348 ATOM 581 O OE1 B GLU A 2348 72 . -13.558 -3.519 18.446 0.34 15.59 ? ? ? ? ? . 72 GLU A OE1 2348 ATOM 582 O OE2 B GLU A 2348 72 . -12.220 -5.118 19.141 0.34 14.77 ? ? ? ? ? 1- 72 GLU A OE2 2348 ATOM 583 N N . ASN A 2348 73 . -10.789 -0.830 13.505 1.00 14.08 ? ? ? ? ? . 73 ASN A N 2348 ATOM 584 C CA . ASN A 2348 73 . -11.154 -0.041 12.336 1.00 14.22 ? ? ? ? ? . 73 ASN A CA 2348 ATOM 585 C C . ASN A 2348 73 . -10.271 -0.425 11.153 1.00 13.82 ? ? ? ? ? . 73 ASN A C 2348 ATOM 586 O O . ASN A 2348 73 . -9.048 -0.290 11.203 1.00 13.41 ? ? ? ? ? . 73 ASN A O 2348 ATOM 587 C CB . ASN A 2348 73 . -11.065 1.455 12.613 1.00 15.75 ? ? ? ? ? . 73 ASN A CB 2348 ATOM 588 C CG . ASN A 2348 73 . -11.382 2.282 11.378 1.00 16.44 ? ? ? ? ? . 73 ASN A CG 2348 ATOM 589 N ND2 . ASN A 2348 73 . -12.576 2.835 11.326 1.00 16.80 ? ? ? ? ? . 73 ASN A ND2 2348 ATOM 590 O OD1 . ASN A 2348 73 . -10.571 2.366 10.456 1.00 17.63 ? ? ? ? ? . 73 ASN A OD1 2348 ATOM 591 N N . GLU A 2348 74 . -10.908 -0.880 10.082 1.00 12.83 ? ? ? ? ? . 74 GLU A N 2348 ATOM 592 C CA . GLU A 2348 74 . -10.164 -1.428 8.942 1.00 13.34 ? ? ? ? ? . 74 GLU A CA 2348 ATOM 593 C C . GLU A 2348 74 . -9.264 -0.399 8.251 1.00 12.42 ? ? ? ? ? . 74 GLU A C 2348 ATOM 594 O O . GLU A 2348 74 . -8.163 -0.752 7.810 1.00 12.27 ? ? ? ? ? . 74 GLU A O 2348 ATOM 595 C CB . GLU A 2348 74 . -11.098 -2.104 7.937 1.00 13.28 ? ? ? ? ? . 74 GLU A CB 2348 ATOM 596 C CG . GLU A 2348 74 . -10.322 -2.877 6.864 1.00 14.42 ? ? ? ? ? . 74 GLU A CG 2348 ATOM 597 C CD . GLU A 2348 74 . -11.098 -3.992 6.185 1.00 15.31 ? ? ? ? ? . 74 GLU A CD 2348 ATOM 598 O OE1 . GLU A 2348 74 . -12.342 -4.043 6.291 1.00 16.61 ? ? ? ? ? . 74 GLU A OE1 2348 ATOM 599 O OE2 . GLU A 2348 74 . -10.428 -4.814 5.521 1.00 16.63 ? ? ? ? ? 1- 74 GLU A OE2 2348 ATOM 600 N N A SER A 2348 75 . -9.716 0.852 8.158 0.50 12.08 ? ? ? ? ? . 75 SER A N 2348 ATOM 601 N N B SER A 2348 75 . -9.720 0.852 8.162 0.50 12.17 ? ? ? ? ? . 75 SER A N 2348 ATOM 602 C CA A SER A 2348 75 . -8.889 1.908 7.555 0.50 12.63 ? ? ? ? ? . 75 SER A CA 2348 ATOM 603 C CA B SER A 2348 75 . -8.902 1.929 7.582 0.50 12.79 ? ? ? ? ? . 75 SER A CA 2348 ATOM 604 C C A SER A 2348 75 . -7.615 2.172 8.375 0.50 12.99 ? ? ? ? ? . 75 SER A C 2348 ATOM 605 C C B SER A 2348 75 . -7.614 2.148 8.378 0.50 13.06 ? ? ? ? ? . 75 SER A C 2348 ATOM 606 O O A SER A 2348 75 . -6.534 2.346 7.802 0.50 12.87 ? ? ? ? ? . 75 SER A O 2348 ATOM 607 O O B SER A 2348 75 . -6.530 2.275 7.797 0.50 12.91 ? ? ? ? ? . 75 SER A O 2348 ATOM 608 C CB A SER A 2348 75 . -9.691 3.193 7.344 0.50 12.19 ? ? ? ? ? . 75 SER A CB 2348 ATOM 609 C CB B SER A 2348 75 . -9.687 3.235 7.505 0.50 12.53 ? ? ? ? ? . 75 SER A CB 2348 ATOM 610 O OG A SER A 2348 75 . -9.929 3.865 8.562 0.50 12.51 ? ? ? ? ? . 75 SER A OG 2348 ATOM 611 O OG B SER A 2348 75 . -11.042 2.992 7.190 0.50 12.90 ? ? ? ? ? . 75 SER A OG 2348 ATOM 612 N N . ASP A 2348 76 . -7.737 2.174 9.705 1.00 13.63 ? ? ? ? ? . 76 ASP A N 2348 ATOM 613 C CA . ASP A 2348 76 . -6.574 2.273 10.604 1.00 14.12 ? ? ? ? ? . 76 ASP A CA 2348 ATOM 614 C C . ASP A 2348 76 . -5.635 1.088 10.406 1.00 14.27 ? ? ? ? ? . 76 ASP A C 2348 ATOM 615 O O . ASP A 2348 76 . -4.413 1.264 10.305 1.00 15.60 ? ? ? ? ? . 76 ASP A O 2348 ATOM 616 C CB . ASP A 2348 76 . -6.999 2.328 12.092 1.00 15.22 ? ? ? ? ? . 76 ASP A CB 2348 ATOM 617 C CG . ASP A 2348 76 . -7.739 3.609 12.471 1.00 17.74 ? ? ? ? ? . 76 ASP A CG 2348 ATOM 618 O OD1 . ASP A 2348 76 . -7.583 4.650 11.792 1.00 18.03 ? ? ? ? ? . 76 ASP A OD1 2348 ATOM 619 O OD2 . ASP A 2348 76 . -8.511 3.555 13.461 1.00 18.66 ? ? ? ? ? 1- 76 ASP A OD2 2348 ATOM 620 N N . PHE A 2348 77 . -6.198 -0.116 10.328 1.00 13.52 ? ? ? ? ? . 77 PHE A N 2348 ATOM 621 C CA . PHE A 2348 77 . -5.377 -1.318 10.207 1.00 14.12 ? ? ? ? ? . 77 PHE A CA 2348 ATOM 622 C C . PHE A 2348 77 . -4.500 -1.258 8.952 1.00 13.79 ? ? ? ? ? . 77 PHE A C 2348 ATOM 623 O O . PHE A 2348 77 . -3.297 -1.442 9.049 1.00 14.65 ? ? ? ? ? . 77 PHE A O 2348 ATOM 624 C CB . PHE A 2348 77 . -6.250 -2.570 10.169 1.00 14.39 ? ? ? ? ? . 77 PHE A CB 2348 ATOM 625 C CG . PHE A 2348 77 . -5.489 -3.825 9.863 1.00 14.28 ? ? ? ? ? . 77 PHE A CG 2348 ATOM 626 C CD1 . PHE A 2348 77 . -4.882 -4.561 10.885 1.00 14.15 ? ? ? ? ? . 77 PHE A CD1 2348 ATOM 627 C CD2 . PHE A 2348 77 . -5.389 -4.282 8.545 1.00 13.66 ? ? ? ? ? . 77 PHE A CD2 2348 ATOM 628 C CE1 . PHE A 2348 77 . -4.198 -5.736 10.592 1.00 14.66 ? ? ? ? ? . 77 PHE A CE1 2348 ATOM 629 C CE2 . PHE A 2348 77 . -4.715 -5.450 8.263 1.00 14.31 ? ? ? ? ? . 77 PHE A CE2 2348 ATOM 630 C CZ . PHE A 2348 77 . -4.106 -6.167 9.277 1.00 13.75 ? ? ? ? ? . 77 PHE A CZ 2348 ATOM 631 N N . HIS A 2348 78 . -5.105 -0.968 7.800 1.00 13.17 ? ? ? ? ? . 78 HIS A N 2348 ATOM 632 C CA . HIS A 2348 78 . -4.363 -1.017 6.526 1.00 15.15 ? ? ? ? ? . 78 HIS A CA 2348 ATOM 633 C C . HIS A 2348 78 . -3.291 0.066 6.463 1.00 16.44 ? ? ? ? ? . 78 HIS A C 2348 ATOM 634 O O . HIS A 2348 78 . -2.177 -0.197 6.034 1.00 18.01 ? ? ? ? ? . 78 HIS A O 2348 ATOM 635 C CB . HIS A 2348 78 . -5.293 -0.947 5.327 1.00 15.24 ? ? ? ? ? . 78 HIS A CB 2348 ATOM 636 C CG . HIS A 2348 78 . -6.138 -2.171 5.161 1.00 16.20 ? ? ? ? ? . 78 HIS A CG 2348 ATOM 637 C CD2 . HIS A 2348 78 . -7.474 -2.321 5.042 1.00 16.05 ? ? ? ? ? . 78 HIS A CD2 2348 ATOM 638 N ND1 . HIS A 2348 78 . -5.603 -3.438 5.092 1.00 16.80 ? ? ? ? ? . 78 HIS A ND1 2348 ATOM 639 C CE1 . HIS A 2348 78 . -6.577 -4.317 4.956 1.00 16.55 ? ? ? ? ? . 78 HIS A CE1 2348 ATOM 640 N NE2 . HIS A 2348 78 . -7.722 -3.664 4.911 1.00 16.79 ? ? ? ? ? . 78 HIS A NE2 2348 ATOM 641 N N . ASP A 2348 79 . -3.634 1.265 6.931 1.00 16.68 ? ? ? ? ? . 79 ASP A N 2348 ATOM 642 C CA . ASP A 2348 79 . -2.676 2.375 7.024 1.00 16.83 ? ? ? ? ? . 79 ASP A CA 2348 ATOM 643 C C . ASP A 2348 79 . -1.470 2.068 7.917 1.00 15.94 ? ? ? ? ? . 79 ASP A C 2348 ATOM 644 O O . ASP A 2348 79 . -0.336 2.356 7.523 1.00 17.28 ? ? ? ? ? . 79 ASP A O 2348 ATOM 645 C CB . ASP A 2348 79 . -3.376 3.617 7.558 1.00 17.23 ? ? ? ? ? . 79 ASP A CB 2348 ATOM 646 C CG . ASP A 2348 79 . -2.424 4.781 7.759 1.00 20.48 ? ? ? ? ? . 79 ASP A CG 2348 ATOM 647 O OD1 . ASP A 2348 79 . -2.084 5.421 6.759 1.00 20.77 ? ? ? ? ? . 79 ASP A OD1 2348 ATOM 648 O OD2 . ASP A 2348 79 . -2.011 5.037 8.914 1.00 25.19 ? ? ? ? ? 1- 79 ASP A OD2 2348 ATOM 649 N N . TYR A 2348 80 . -1.730 1.494 9.099 1.00 14.61 ? ? ? ? ? . 80 TYR A N 2348 ATOM 650 C CA . TYR A 2348 80 . -0.697 1.179 10.096 1.00 17.20 ? ? ? ? ? . 80 TYR A CA 2348 ATOM 651 C C . TYR A 2348 80 . 0.221 0.072 9.590 1.00 17.19 ? ? ? ? ? . 80 TYR A C 2348 ATOM 652 O O . TYR A 2348 80 . 1.447 0.196 9.633 1.00 16.67 ? ? ? ? ? . 80 TYR A O 2348 ATOM 653 C CB . TYR A 2348 80 . -1.340 0.758 11.427 1.00 18.55 ? ? ? ? ? . 80 TYR A CB 2348 ATOM 654 C CG . TYR A 2348 80 . -0.396 0.484 12.583 1.00 18.63 ? ? ? ? ? . 80 TYR A CG 2348 ATOM 655 C CD1 . TYR A 2348 80 . 0.683 1.323 12.833 1.00 23.04 ? ? ? ? ? . 80 TYR A CD1 2348 ATOM 656 C CD2 . TYR A 2348 80 . -0.627 -0.565 13.480 1.00 20.76 ? ? ? ? ? . 80 TYR A CD2 2348 ATOM 657 C CE1 . TYR A 2348 80 . 1.538 1.105 13.894 1.00 22.93 ? ? ? ? ? . 80 TYR A CE1 2348 ATOM 658 C CE2 . TYR A 2348 80 . 0.226 -0.795 14.558 1.00 21.46 ? ? ? ? ? . 80 TYR A CE2 2348 ATOM 659 C CZ . TYR A 2348 80 . 1.316 0.057 14.752 1.00 22.68 ? ? ? ? ? . 80 TYR A CZ 2348 ATOM 660 O OH . TYR A 2348 80 . 2.212 -0.095 15.781 1.00 22.57 ? ? ? ? ? . 80 TYR A OH 2348 ATOM 661 N N . TYR A 2348 81 . -0.381 -1.002 9.092 1.00 17.50 ? ? ? ? ? . 81 TYR A N 2348 ATOM 662 C CA . TYR A 2348 81 . 0.379 -2.102 8.498 1.00 16.24 ? ? ? ? ? . 81 TYR A CA 2348 ATOM 663 C C . TYR A 2348 81 . 1.140 -1.652 7.227 1.00 18.13 ? ? ? ? ? . 81 TYR A C 2348 ATOM 664 O O . TYR A 2348 81 . 2.207 -2.185 6.913 1.00 15.85 ? ? ? ? ? . 81 TYR A O 2348 ATOM 665 C CB . TYR A 2348 81 . -0.539 -3.302 8.214 1.00 16.74 ? ? ? ? ? . 81 TYR A CB 2348 ATOM 666 C CG . TYR A 2348 81 . 0.157 -4.417 7.487 1.00 15.44 ? ? ? ? ? . 81 TYR A CG 2348 ATOM 667 C CD1 . TYR A 2348 81 . 1.326 -4.962 7.996 1.00 15.29 ? ? ? ? ? . 81 TYR A CD1 2348 ATOM 668 C CD2 . TYR A 2348 81 . -0.327 -4.903 6.270 1.00 16.27 ? ? ? ? ? . 81 TYR A CD2 2348 ATOM 669 C CE1 . TYR A 2348 81 . 1.991 -5.974 7.330 1.00 16.12 ? ? ? ? ? . 81 TYR A CE1 2348 ATOM 670 C CE2 . TYR A 2348 81 . 0.337 -5.915 5.598 1.00 16.03 ? ? ? ? ? . 81 TYR A CE2 2348 ATOM 671 C CZ . TYR A 2348 81 . 1.494 -6.446 6.138 1.00 15.55 ? ? ? ? ? . 81 TYR A CZ 2348 ATOM 672 O OH . TYR A 2348 81 . 2.175 -7.436 5.481 1.00 15.91 ? ? ? ? ? . 81 TYR A OH 2348 ATOM 673 N N . GLY A 2348 82 . 0.590 -0.673 6.520 1.00 17.41 ? ? ? ? ? . 82 GLY A N 2348 ATOM 674 C CA . GLY A 2348 82 . 1.289 0.024 5.435 1.00 18.28 ? ? ? ? ? . 82 GLY A CA 2348 ATOM 675 C C . GLY A 2348 82 . 2.637 0.633 5.811 1.00 20.09 ? ? ? ? ? . 82 GLY A C 2348 ATOM 676 O O . GLY A 2348 82 . 3.493 0.785 4.952 1.00 24.29 ? ? ? ? ? . 82 GLY A O 2348 ATOM 677 N N . LYS A 2348 83 . 2.831 0.980 7.081 1.00 22.68 ? ? ? ? ? . 83 LYS A N 2348 ATOM 678 C CA . LYS A 2348 83 . 4.127 1.471 7.568 1.00 25.21 ? ? ? ? ? . 83 LYS A CA 2348 ATOM 679 C C . LYS A 2348 83 . 5.180 0.368 7.755 1.00 24.73 ? ? ? ? ? . 83 LYS A C 2348 ATOM 680 O O . LYS A 2348 83 . 6.347 0.694 7.939 1.00 27.09 ? ? ? ? ? . 83 LYS A O 2348 ATOM 681 C CB . LYS A 2348 83 . 3.966 2.226 8.900 1.00 27.32 ? ? ? ? ? . 83 LYS A CB 2348 ATOM 682 C CG . LYS A 2348 83 . 3.068 3.460 8.822 1.00 28.44 ? ? ? ? ? . 83 LYS A CG 2348 ATOM 683 C CD . LYS A 2348 83 . 2.696 3.960 10.213 1.00 29.59 ? ? ? ? ? . 83 LYS A CD 2348 ATOM 684 C CE . LYS A 2348 83 . 1.544 4.950 10.191 1.00 32.72 ? ? ? ? ? . 83 LYS A CE 2348 ATOM 685 N NZ . LYS A 2348 83 . 2.009 6.314 9.830 1.00 33.48 ? ? ? ? ? 1+ 83 LYS A NZ 2348 ATOM 686 N N . MET A 2348 84 . 4.781 -0.911 7.691 1.00 19.28 ? ? ? ? ? . 84 MET A N 2348 ATOM 687 C CA . MET A 2348 84 . 5.594 -2.020 8.159 1.00 17.95 ? ? ? ? ? . 84 MET A CA 2348 ATOM 688 C C . MET A 2348 84 . 6.094 -2.867 6.992 1.00 17.98 ? ? ? ? ? . 84 MET A C 2348 ATOM 689 O O . MET A 2348 84 . 5.361 -3.039 6.022 1.00 18.70 ? ? ? ? ? . 84 MET A O 2348 ATOM 690 C CB . MET A 2348 84 . 4.741 -2.887 9.073 1.00 18.33 ? ? ? ? ? . 84 MET A CB 2348 ATOM 691 C CG . MET A 2348 84 . 4.178 -2.120 10.259 1.00 17.16 ? ? ? ? ? . 84 MET A CG 2348 ATOM 692 S SD . MET A 2348 84 . 3.073 -3.159 11.216 1.00 18.23 ? ? ? ? ? . 84 MET A SD 2348 ATOM 693 C CE . MET A 2348 84 . 2.572 -2.030 12.508 1.00 19.33 ? ? ? ? ? . 84 MET A CE 2348 ATOM 694 N N . PRO A 2348 85 . 7.327 -3.413 7.084 1.00 15.09 ? ? ? ? ? . 85 PRO A N 2348 ATOM 695 C CA . PRO A 2348 85 . 7.898 -4.245 6.004 1.00 14.89 ? ? ? ? ? . 85 PRO A CA 2348 ATOM 696 C C . PRO A 2348 85 . 7.578 -5.746 6.060 1.00 14.31 ? ? ? ? ? . 85 PRO A C 2348 ATOM 697 O O . PRO A 2348 85 . 7.878 -6.490 5.111 1.00 16.07 ? ? ? ? ? . 85 PRO A O 2348 ATOM 698 C CB . PRO A 2348 85 . 9.418 -4.058 6.204 1.00 13.50 ? ? ? ? ? . 85 PRO A CB 2348 ATOM 699 C CG . PRO A 2348 85 . 9.557 -3.858 7.671 1.00 14.27 ? ? ? ? ? . 85 PRO A CG 2348 ATOM 700 C CD . PRO A 2348 85 . 8.354 -3.051 8.079 1.00 14.84 ? ? ? ? ? . 85 PRO A CD 2348 ATOM 701 N N . TRP A 2348 86 . 7.021 -6.177 7.179 1.00 14.39 ? ? ? ? ? . 86 TRP A N 2348 ATOM 702 C CA . TRP A 2348 86 . 6.848 -7.584 7.527 1.00 15.05 ? ? ? ? ? . 86 TRP A CA 2348 ATOM 703 C C . TRP A 2348 86 . 5.414 -8.087 7.212 1.00 14.93 ? ? ? ? ? . 86 TRP A C 2348 ATOM 704 O O . TRP A 2348 86 . 4.763 -7.552 6.308 1.00 15.89 ? ? ? ? ? . 86 TRP A O 2348 ATOM 705 C CB . TRP A 2348 86 . 7.249 -7.774 8.986 1.00 16.09 ? ? ? ? ? . 86 TRP A CB 2348 ATOM 706 C CG . TRP A 2348 86 . 6.594 -6.805 9.948 1.00 16.38 ? ? ? ? ? . 86 TRP A CG 2348 ATOM 707 C CD1 . TRP A 2348 86 . 5.277 -6.720 10.275 1.00 16.39 ? ? ? ? ? . 86 TRP A CD1 2348 ATOM 708 C CD2 . TRP A 2348 86 . 7.254 -5.759 10.661 1.00 16.60 ? ? ? ? ? . 86 TRP A CD2 2348 ATOM 709 C CE2 . TRP A 2348 86 . 6.275 -5.092 11.428 1.00 16.59 ? ? ? ? ? . 86 TRP A CE2 2348 ATOM 710 C CE3 . TRP A 2348 86 . 8.580 -5.340 10.752 1.00 17.11 ? ? ? ? ? . 86 TRP A CE3 2348 ATOM 711 N NE1 . TRP A 2348 86 . 5.074 -5.703 11.176 1.00 17.10 ? ? ? ? ? . 86 TRP A NE1 2348 ATOM 712 C CZ2 . TRP A 2348 86 . 6.576 -4.003 12.239 1.00 16.34 ? ? ? ? ? . 86 TRP A CZ2 2348 ATOM 713 C CZ3 . TRP A 2348 86 . 8.880 -4.259 11.571 1.00 16.26 ? ? ? ? ? . 86 TRP A CZ3 2348 ATOM 714 C CH2 . TRP A 2348 86 . 7.883 -3.601 12.300 1.00 16.70 ? ? ? ? ? . 86 TRP A CH2 2348 ATOM 715 N N . LEU A 2348 87 . 4.947 -9.122 7.918 1.00 14.24 ? ? ? ? ? . 87 LEU A N 2348 ATOM 716 C CA . LEU A 2348 87 . 3.666 -9.781 7.638 1.00 14.03 ? ? ? ? ? . 87 LEU A CA 2348 ATOM 717 C C . LEU A 2348 87 . 2.585 -9.335 8.606 1.00 13.87 ? ? ? ? ? . 87 LEU A C 2348 ATOM 718 O O . LEU A 2348 87 . 2.870 -8.625 9.570 1.00 15.16 ? ? ? ? ? . 87 LEU A O 2348 ATOM 719 C CB . LEU A 2348 87 . 3.834 -11.298 7.738 1.00 14.67 ? ? ? ? ? . 87 LEU A CB 2348 ATOM 720 C CG . LEU A 2348 87 . 4.941 -11.933 6.902 1.00 15.26 ? ? ? ? ? . 87 LEU A CG 2348 ATOM 721 C CD1 . LEU A 2348 87 . 4.898 -13.451 7.044 1.00 17.71 ? ? ? ? ? . 87 LEU A CD1 2348 ATOM 722 C CD2 . LEU A 2348 87 . 4.848 -11.552 5.423 1.00 15.24 ? ? ? ? ? . 87 LEU A CD2 2348 ATOM 723 N N . ALA A 2348 88 . 1.338 -9.735 8.355 1.00 14.07 ? ? ? ? ? . 88 ALA A N 2348 ATOM 724 C CA . ALA A 2348 88 . 0.243 -9.403 9.270 1.00 13.95 ? ? ? ? ? . 88 ALA A CA 2348 ATOM 725 C C . ALA A 2348 88 . -0.837 -10.476 9.311 1.00 14.05 ? ? ? ? ? . 88 ALA A C 2348 ATOM 726 O O . ALA A 2348 88 . -1.203 -11.084 8.292 1.00 13.51 ? ? ? ? ? . 88 ALA A O 2348 ATOM 727 C CB . ALA A 2348 88 . -0.376 -8.068 8.919 1.00 14.60 ? ? ? ? ? . 88 ALA A CB 2348 ATOM 728 N N . LEU A 2348 89 . -1.325 -10.720 10.521 1.00 14.21 ? ? ? ? ? . 89 LEU A N 2348 ATOM 729 C CA . LEU A 2348 89 . -2.521 -11.514 10.693 1.00 14.62 ? ? ? ? ? . 89 LEU A CA 2348 ATOM 730 C C . LEU A 2348 89 . -3.619 -10.667 10.045 1.00 15.33 ? ? ? ? ? . 89 LEU A C 2348 ATOM 731 O O . LEU A 2348 89 . -3.754 -9.482 10.397 1.00 16.78 ? ? ? ? ? . 89 LEU A O 2348 ATOM 732 C CB . LEU A 2348 89 . -2.799 -11.754 12.179 1.00 15.84 ? ? ? ? ? . 89 LEU A CB 2348 ATOM 733 C CG . LEU A 2348 89 . -4.017 -12.623 12.472 1.00 17.67 ? ? ? ? ? . 89 LEU A CG 2348 ATOM 734 C CD1 . LEU A 2348 89 . -3.789 -14.077 12.038 1.00 17.19 ? ? ? ? ? . 89 LEU A CD1 2348 ATOM 735 C CD2 . LEU A 2348 89 . -4.381 -12.542 13.948 1.00 18.01 ? ? ? ? ? . 89 LEU A CD2 2348 ATOM 736 N N . PRO A 2348 90 . -4.369 -11.236 9.079 1.00 15.61 ? ? ? ? ? . 90 PRO A N 2348 ATOM 737 C CA . PRO A 2348 90 . -5.337 -10.408 8.338 1.00 15.39 ? ? ? ? ? . 90 PRO A CA 2348 ATOM 738 C C . PRO A 2348 90 . -6.419 -9.804 9.235 1.00 16.09 ? ? ? ? ? . 90 PRO A C 2348 ATOM 739 O O . PRO A 2348 90 . -6.743 -10.365 10.289 1.00 17.53 ? ? ? ? ? . 90 PRO A O 2348 ATOM 740 C CB . PRO A 2348 90 . -5.942 -11.382 7.316 1.00 15.62 ? ? ? ? ? . 90 PRO A CB 2348 ATOM 741 C CG . PRO A 2348 90 . -5.047 -12.581 7.294 1.00 15.55 ? ? ? ? ? . 90 PRO A CG 2348 ATOM 742 C CD . PRO A 2348 90 . -4.440 -12.653 8.660 1.00 15.71 ? ? ? ? ? . 90 PRO A CD 2348 ATOM 743 N N . PHE A 2348 91 . -6.969 -8.674 8.808 1.00 15.01 ? ? ? ? ? . 91 PHE A N 2348 ATOM 744 C CA . PHE A 2348 91 . -8.012 -7.972 9.554 1.00 15.12 ? ? ? ? ? . 91 PHE A CA 2348 ATOM 745 C C . PHE A 2348 91 . -9.234 -8.855 9.838 1.00 14.96 ? ? ? ? ? . 91 PHE A C 2348 ATOM 746 O O . PHE A 2348 91 . -9.821 -8.765 10.919 1.00 14.30 ? ? ? ? ? . 91 PHE A O 2348 ATOM 747 C CB . PHE A 2348 91 . -8.419 -6.696 8.808 1.00 14.17 ? ? ? ? ? . 91 PHE A CB 2348 ATOM 748 C CG . PHE A 2348 91 . -9.368 -5.827 9.575 1.00 14.33 ? ? ? ? ? . 91 PHE A CG 2348 ATOM 749 C CD1 . PHE A 2348 91 . -8.907 -5.015 10.596 1.00 14.03 ? ? ? ? ? . 91 PHE A CD1 2348 ATOM 750 C CD2 . PHE A 2348 91 . -10.718 -5.837 9.293 1.00 14.08 ? ? ? ? ? . 91 PHE A CD2 2348 ATOM 751 C CE1 . PHE A 2348 91 . -9.778 -4.214 11.312 1.00 14.13 ? ? ? ? ? . 91 PHE A CE1 2348 ATOM 752 C CE2 . PHE A 2348 91 . -11.593 -5.031 10.000 1.00 14.14 ? ? ? ? ? . 91 PHE A CE2 2348 ATOM 753 C CZ . PHE A 2348 91 . -11.125 -4.227 11.017 1.00 13.32 ? ? ? ? ? . 91 PHE A CZ 2348 ATOM 754 N N . ASP A 2348 92 . -9.589 -9.745 8.906 1.00 15.56 ? ? ? ? ? . 92 ASP A N 2348 ATOM 755 C CA . ASP A 2348 92 . -10.703 -10.677 9.134 1.00 17.16 ? ? ? ? ? . 92 ASP A CA 2348 ATOM 756 C C . ASP A 2348 92 . -10.492 -11.723 10.253 1.00 16.55 ? ? ? ? ? . 92 ASP A C 2348 ATOM 757 O O . ASP A 2348 92 . -11.442 -12.405 10.630 1.00 15.77 ? ? ? ? ? . 92 ASP A O 2348 ATOM 758 C CB . ASP A 2348 92 . -11.183 -11.323 7.817 1.00 19.89 ? ? ? ? ? . 92 ASP A CB 2348 ATOM 759 C CG . ASP A 2348 92 . -10.238 -12.389 7.264 1.00 22.49 ? ? ? ? ? . 92 ASP A CG 2348 ATOM 760 O OD1 . ASP A 2348 92 . -9.083 -12.505 7.702 1.00 25.02 ? ? ? ? ? . 92 ASP A OD1 2348 ATOM 761 O OD2 . ASP A 2348 92 . -10.682 -13.123 6.358 1.00 28.11 ? ? ? ? ? 1- 92 ASP A OD2 2348 ATOM 762 N N . GLN A 2348 93 . -9.265 -11.838 10.772 1.00 18.68 ? ? ? ? ? . 93 GLN A N 2348 ATOM 763 C CA . GLN A 2348 93 . -8.950 -12.682 11.938 1.00 19.24 ? ? ? ? ? . 93 GLN A CA 2348 ATOM 764 C C . GLN A 2348 93 . -8.865 -11.918 13.267 1.00 19.92 ? ? ? ? ? . 93 GLN A C 2348 ATOM 765 O O . GLN A 2348 93 . -8.488 -12.498 14.294 1.00 19.87 ? ? ? ? ? . 93 GLN A O 2348 ATOM 766 C CB . GLN A 2348 93 . -7.613 -13.387 11.705 1.00 21.09 ? ? ? ? ? . 93 GLN A CB 2348 ATOM 767 C CG . GLN A 2348 93 . -7.585 -14.287 10.491 1.00 22.02 ? ? ? ? ? . 93 GLN A CG 2348 ATOM 768 C CD . GLN A 2348 93 . -8.625 -15.367 10.592 1.00 22.70 ? ? ? ? ? . 93 GLN A CD 2348 ATOM 769 N NE2 . GLN A 2348 93 . -9.587 -15.348 9.687 1.00 24.75 ? ? ? ? ? . 93 GLN A NE2 2348 ATOM 770 O OE1 . GLN A 2348 93 . -8.582 -16.194 11.502 1.00 26.33 ? ? ? ? ? . 93 GLN A OE1 2348 ATOM 771 N N . ARG A 2348 94 . -9.195 -10.629 13.268 1.00 18.83 ? ? ? ? ? . 94 ARG A N 2348 ATOM 772 C CA . ARG A 2348 94 . -9.008 -9.798 14.473 1.00 18.44 ? ? ? ? ? . 94 ARG A CA 2348 ATOM 773 C C . ARG A 2348 94 . -9.787 -10.249 15.731 1.00 20.01 ? ? ? ? ? . 94 ARG A C 2348 ATOM 774 O O . ARG A 2348 94 . -9.382 -9.946 16.856 1.00 21.06 ? ? ? ? ? . 94 ARG A O 2348 ATOM 775 C CB . ARG A 2348 94 . -9.362 -8.352 14.163 1.00 18.84 ? ? ? ? ? . 94 ARG A CB 2348 ATOM 776 C CG . ARG A 2348 94 . -10.833 -8.137 13.869 1.00 17.70 ? ? ? ? ? . 94 ARG A CG 2348 ATOM 777 C CD . ARG A 2348 94 . -11.074 -6.817 13.167 1.00 17.62 ? ? ? ? ? . 94 ARG A CD 2348 ATOM 778 N NE . ARG A 2348 94 . -12.479 -6.584 12.868 1.00 16.14 ? ? ? ? ? . 94 ARG A NE 2348 ATOM 779 C CZ . ARG A 2348 94 . -13.172 -7.168 11.890 1.00 15.93 ? ? ? ? ? . 94 ARG A CZ 2348 ATOM 780 N NH1 . ARG A 2348 94 . -12.618 -8.075 11.077 1.00 15.88 ? ? ? ? ? 1+ 94 ARG A NH1 2348 ATOM 781 N NH2 . ARG A 2348 94 . -14.447 -6.844 11.720 1.00 15.41 ? ? ? ? ? . 94 ARG A NH2 2348 ATOM 782 N N . SER A 2348 95 . -10.894 -10.966 15.554 1.00 18.52 ? ? ? ? ? . 95 SER A N 2348 ATOM 783 C CA . SER A 2348 95 . -11.631 -11.517 16.704 1.00 19.63 ? ? ? ? ? . 95 SER A CA 2348 ATOM 784 C C . SER A 2348 95 . -10.806 -12.529 17.529 1.00 20.04 ? ? ? ? ? . 95 SER A C 2348 ATOM 785 O O . SER A 2348 95 . -11.153 -12.802 18.675 1.00 23.68 ? ? ? ? ? . 95 SER A O 2348 ATOM 786 C CB . SER A 2348 95 . -12.957 -12.140 16.257 1.00 19.52 ? ? ? ? ? . 95 SER A CB 2348 ATOM 787 O OG . SER A 2348 95 . -12.750 -13.290 15.451 1.00 19.99 ? ? ? ? ? . 95 SER A OG 2348 ATOM 788 N N . THR A 2348 96 . -9.726 -13.065 16.955 1.00 18.79 ? ? ? ? ? . 96 THR A N 2348 ATOM 789 C CA . THR A 2348 96 . -8.848 -14.022 17.638 1.00 19.20 ? ? ? ? ? . 96 THR A CA 2348 ATOM 790 C C . THR A 2348 96 . -7.699 -13.365 18.408 1.00 18.18 ? ? ? ? ? . 96 THR A C 2348 ATOM 791 O O . THR A 2348 96 . -7.004 -14.049 19.141 1.00 18.92 ? ? ? ? ? . 96 THR A O 2348 ATOM 792 C CB . THR A 2348 96 . -8.234 -15.045 16.647 1.00 18.50 ? ? ? ? ? . 96 THR A CB 2348 ATOM 793 C CG2 . THR A 2348 96 . -9.306 -15.722 15.827 1.00 19.51 ? ? ? ? ? . 96 THR A CG2 2348 ATOM 794 O OG1 . THR A 2348 96 . -7.308 -14.396 15.773 1.00 17.89 ? ? ? ? ? . 96 THR A OG1 2348 ATOM 795 N N . VAL A 2348 97 . -7.509 -12.050 18.253 1.00 17.87 ? ? ? ? ? . 97 VAL A N 2348 ATOM 796 C CA . VAL A 2348 97 . -6.369 -11.333 18.837 1.00 17.37 ? ? ? ? ? . 97 VAL A CA 2348 ATOM 797 C C . VAL A 2348 97 . -6.320 -11.387 20.366 1.00 17.80 ? ? ? ? ? . 97 VAL A C 2348 ATOM 798 O O . VAL A 2348 97 . -5.255 -11.611 20.940 1.00 20.08 ? ? ? ? ? . 97 VAL A O 2348 ATOM 799 C CB . VAL A 2348 97 . -6.303 -9.861 18.321 1.00 17.84 ? ? ? ? ? . 97 VAL A CB 2348 ATOM 800 C CG1 . VAL A 2348 97 . -5.371 -8.987 19.152 1.00 19.58 ? ? ? ? ? . 97 VAL A CG1 2348 ATOM 801 C CG2 . VAL A 2348 97 . -5.879 -9.848 16.855 1.00 18.67 ? ? ? ? ? . 97 VAL A CG2 2348 ATOM 802 N N . SER A 2348 98 . -7.446 -11.187 21.024 1.00 18.78 ? ? ? ? ? . 98 SER A N 2348 ATOM 803 C CA . SER A 2348 98 . -7.464 -11.238 22.490 1.00 21.28 ? ? ? ? ? . 98 SER A CA 2348 ATOM 804 C C . SER A 2348 98 . -7.035 -12.609 23.030 1.00 18.77 ? ? ? ? ? . 98 SER A C 2348 ATOM 805 O O . SER A 2348 98 . -6.158 -12.685 23.897 1.00 18.08 ? ? ? ? ? . 98 SER A O 2348 ATOM 806 C CB . SER A 2348 98 . -8.832 -10.833 23.032 1.00 25.06 ? ? ? ? ? . 98 SER A CB 2348 ATOM 807 O OG . SER A 2348 98 . -9.007 -9.449 22.802 1.00 31.85 ? ? ? ? ? . 98 SER A OG 2348 ATOM 808 N N . GLU A 2348 99 . -7.616 -13.681 22.496 1.00 19.69 ? ? ? ? ? . 99 GLU A N 2348 ATOM 809 C CA . GLU A 2348 99 . -7.262 -15.038 22.954 1.00 21.24 ? ? ? ? ? . 99 GLU A CA 2348 ATOM 810 C C . GLU A 2348 99 . -5.793 -15.374 22.682 1.00 17.41 ? ? ? ? ? . 99 GLU A C 2348 ATOM 811 O O . GLU A 2348 99 . -5.151 -16.025 23.503 1.00 15.18 ? ? ? ? ? . 99 GLU A O 2348 ATOM 812 C CB . GLU A 2348 99 . -8.204 -16.125 22.399 1.00 26.09 ? ? ? ? ? . 99 GLU A CB 2348 ATOM 813 C CG . GLU A 2348 99 . -9.552 -16.237 23.134 1.00 32.76 ? ? ? ? ? . 99 GLU A CG 2348 ATOM 814 C CD . GLU A 2348 99 . -9.435 -16.520 24.639 1.00 38.23 ? ? ? ? ? . 99 GLU A CD 2348 ATOM 815 O OE1 . GLU A 2348 99 . -10.112 -15.830 25.435 1.00 38.21 ? ? ? ? ? . 99 GLU A OE1 2348 ATOM 816 O OE2 . GLU A 2348 99 . -8.659 -17.420 25.035 1.00 43.04 ? ? ? ? ? 1- 99 GLU A OE2 2348 ATOM 817 N N A LEU A 2348 100 . -5.267 -14.922 21.547 0.62 17.52 ? ? ? ? ? . 100 LEU A N 2348 ATOM 818 N N B LEU A 2348 100 . -5.274 -14.931 21.535 0.38 17.54 ? ? ? ? ? . 100 LEU A N 2348 ATOM 819 C CA A LEU A 2348 100 . -3.843 -15.073 21.262 0.62 17.97 ? ? ? ? ? . 100 LEU A CA 2348 ATOM 820 C CA B LEU A 2348 100 . -3.842 -15.024 21.233 0.38 17.83 ? ? ? ? ? . 100 LEU A CA 2348 ATOM 821 C C A LEU A 2348 100 . -2.991 -14.334 22.306 0.62 17.34 ? ? ? ? ? . 100 LEU A C 2348 ATOM 822 C C B LEU A 2348 100 . -2.996 -14.330 22.297 0.38 17.23 ? ? ? ? ? . 100 LEU A C 2348 ATOM 823 O O A LEU A 2348 100 . -2.009 -14.887 22.811 0.62 17.52 ? ? ? ? ? . 100 LEU A O 2348 ATOM 824 O O B LEU A 2348 100 . -2.015 -14.895 22.788 0.38 17.39 ? ? ? ? ? . 100 LEU A O 2348 ATOM 825 C CB A LEU A 2348 100 . -3.512 -14.591 19.845 0.62 17.99 ? ? ? ? ? . 100 LEU A CB 2348 ATOM 826 C CB B LEU A 2348 100 . -3.539 -14.408 19.866 0.38 17.92 ? ? ? ? ? . 100 LEU A CB 2348 ATOM 827 C CG A LEU A 2348 100 . -2.154 -15.017 19.286 0.62 18.53 ? ? ? ? ? . 100 LEU A CG 2348 ATOM 828 C CG B LEU A 2348 100 . -3.832 -15.294 18.660 0.38 18.30 ? ? ? ? ? . 100 LEU A CG 2348 ATOM 829 C CD1 A LEU A 2348 100 . -2.036 -16.528 19.154 0.62 18.85 ? ? ? ? ? . 100 LEU A CD1 2348 ATOM 830 C CD2 A LEU A 2348 100 . -1.922 -14.346 17.940 0.62 18.72 ? ? ? ? ? . 100 LEU A CD2 2348 ATOM 831 C CD1 B LEU A 2348 100 . -3.529 -14.555 17.366 0.38 18.21 ? ? ? ? ? . 100 LEU A CD1 2348 ATOM 832 C CD2 B LEU A 2348 100 . -3.032 -16.584 18.760 0.38 18.99 ? ? ? ? ? . 100 LEU A CD2 2348 ATOM 833 N N . GLY A 2348 101 . -3.394 -13.112 22.652 1.00 16.30 ? ? ? ? ? . 101 GLY A N 2348 ATOM 834 C CA . GLY A 2348 101 . -2.751 -12.353 23.730 1.00 17.07 ? ? ? ? ? . 101 GLY A CA 2348 ATOM 835 C C . GLY A 2348 101 . -2.761 -13.100 25.058 1.00 16.31 ? ? ? ? ? . 101 GLY A C 2348 ATOM 836 O O . GLY A 2348 101 . -1.743 -13.175 25.749 1.00 16.49 ? ? ? ? ? . 101 GLY A O 2348 ATOM 837 N N . LYS A 2348 102 . -3.894 -13.712 25.373 1.00 16.43 ? ? ? ? ? . 102 LYS A N 2348 ATOM 838 C CA . LYS A 2348 102 . -4.015 -14.519 26.581 1.00 18.92 ? ? ? ? ? . 102 LYS A CA 2348 ATOM 839 C C . LYS A 2348 102 . -3.185 -15.794 26.544 1.00 17.88 ? ? ? ? ? . 102 LYS A C 2348 ATOM 840 O O . LYS A 2348 102 . -2.693 -16.236 27.592 1.00 17.27 ? ? ? ? ? . 102 LYS A O 2348 ATOM 841 C CB . LYS A 2348 102 . -5.471 -14.864 26.852 1.00 20.65 ? ? ? ? ? . 102 LYS A CB 2348 ATOM 842 C CG . LYS A 2348 102 . -6.288 -13.651 27.240 1.00 23.12 ? ? ? ? ? . 102 LYS A CG 2348 ATOM 843 C CD . LYS A 2348 102 . -7.765 -13.982 27.284 1.00 26.40 ? ? ? ? ? . 102 LYS A CD 2348 ATOM 844 C CE . LYS A 2348 102 . -8.599 -12.716 27.350 1.00 30.33 ? ? ? ? ? . 102 LYS A CE 2348 ATOM 845 N NZ . LYS A 2348 102 . -10.031 -13.013 27.641 1.00 32.61 ? ? ? ? ? 1+ 102 LYS A NZ 2348 ATOM 846 N N . THR A 2348 103 . -3.048 -16.401 25.367 1.00 16.42 ? ? ? ? ? . 103 THR A N 2348 ATOM 847 C CA . THR A 2348 103 . -2.195 -17.586 25.218 1.00 17.78 ? ? ? ? ? . 103 THR A CA 2348 ATOM 848 C C . THR A 2348 103 . -0.744 -17.326 25.664 1.00 17.24 ? ? ? ? ? . 103 THR A C 2348 ATOM 849 O O . THR A 2348 103 . -0.141 -18.175 26.318 1.00 18.04 ? ? ? ? ? . 103 THR A O 2348 ATOM 850 C CB . THR A 2348 103 . -2.246 -18.126 23.775 1.00 18.81 ? ? ? ? ? . 103 THR A CB 2348 ATOM 851 C CG2 . THR A 2348 103 . -1.316 -19.326 23.587 1.00 20.17 ? ? ? ? ? . 103 THR A CG2 2348 ATOM 852 O OG1 . THR A 2348 103 . -3.593 -18.515 23.477 1.00 20.80 ? ? ? ? ? . 103 THR A OG1 2348 ATOM 853 N N . PHE A 2348 104 . -0.216 -16.152 25.328 1.00 19.05 ? ? ? ? ? . 104 PHE A N 2348 ATOM 854 C CA . PHE A 2348 104 . 1.181 -15.790 25.614 1.00 19.38 ? ? ? ? ? . 104 PHE A CA 2348 ATOM 855 C C . PHE A 2348 104 . 1.370 -14.884 26.835 1.00 20.42 ? ? ? ? ? . 104 PHE A C 2348 ATOM 856 O O . PHE A 2348 104 . 2.509 -14.490 27.138 1.00 21.98 ? ? ? ? ? . 104 PHE A O 2348 ATOM 857 C CB . PHE A 2348 104 . 1.800 -15.141 24.379 1.00 19.21 ? ? ? ? ? . 104 PHE A CB 2348 ATOM 858 C CG . PHE A 2348 104 . 1.787 -16.032 23.169 1.00 18.31 ? ? ? ? ? . 104 PHE A CG 2348 ATOM 859 C CD1 . PHE A 2348 104 . 2.515 -17.212 23.163 1.00 18.08 ? ? ? ? ? . 104 PHE A CD1 2348 ATOM 860 C CD2 . PHE A 2348 104 . 1.042 -15.701 22.042 1.00 18.77 ? ? ? ? ? . 104 PHE A CD2 2348 ATOM 861 C CE1 . PHE A 2348 104 . 2.515 -18.044 22.052 1.00 19.62 ? ? ? ? ? . 104 PHE A CE1 2348 ATOM 862 C CE2 . PHE A 2348 104 . 1.023 -16.536 20.933 1.00 19.73 ? ? ? ? ? . 104 PHE A CE2 2348 ATOM 863 C CZ . PHE A 2348 104 . 1.766 -17.706 20.933 1.00 19.63 ? ? ? ? ? . 104 PHE A CZ 2348 ATOM 864 N N . GLY A 2348 105 . 0.278 -14.584 27.535 1.00 17.32 ? ? ? ? ? . 105 GLY A N 2348 ATOM 865 C CA . GLY A 2348 105 . 0.314 -13.721 28.702 1.00 17.53 ? ? ? ? ? . 105 GLY A CA 2348 ATOM 866 C C . GLY A 2348 105 . 0.695 -12.289 28.385 1.00 18.09 ? ? ? ? ? . 105 GLY A C 2348 ATOM 867 O O . GLY A 2348 105 . 1.374 -11.625 29.192 1.00 18.88 ? ? ? ? ? . 105 GLY A O 2348 ATOM 868 N N . VAL A 2348 106 . 0.237 -11.800 27.229 1.00 16.90 ? ? ? ? ? . 106 VAL A N 2348 ATOM 869 C CA . VAL A 2348 106 . 0.450 -10.401 26.824 1.00 17.15 ? ? ? ? ? . 106 VAL A CA 2348 ATOM 870 C C . VAL A 2348 106 . -0.420 -9.510 27.720 1.00 17.09 ? ? ? ? ? . 106 VAL A C 2348 ATOM 871 O O . VAL A 2348 106 . -1.656 -9.601 27.679 1.00 17.42 ? ? ? ? ? . 106 VAL A O 2348 ATOM 872 C CB . VAL A 2348 106 . 0.113 -10.177 25.338 1.00 16.91 ? ? ? ? ? . 106 VAL A CB 2348 ATOM 873 C CG1 . VAL A 2348 106 . 0.239 -8.706 24.946 1.00 17.76 ? ? ? ? ? . 106 VAL A CG1 2348 ATOM 874 C CG2 . VAL A 2348 106 . 1.032 -11.025 24.467 1.00 16.80 ? ? ? ? ? . 106 VAL A CG2 2348 ATOM 875 N N A GLU A 2348 107 . 0.231 -8.684 28.544 0.48 16.42 ? ? ? ? ? . 107 GLU A N 2348 ATOM 876 N N B GLU A 2348 107 . 0.226 -8.667 28.525 0.52 16.18 ? ? ? ? ? . 107 GLU A N 2348 ATOM 877 C CA A GLU A 2348 107 . -0.457 -7.789 29.486 0.48 17.61 ? ? ? ? ? . 107 GLU A CA 2348 ATOM 878 C CA B GLU A 2348 107 . -0.482 -7.782 29.455 0.52 17.47 ? ? ? ? ? . 107 GLU A CA 2348 ATOM 879 C C A GLU A 2348 107 . -0.440 -6.314 29.071 0.48 16.30 ? ? ? ? ? . 107 GLU A C 2348 ATOM 880 C C B GLU A 2348 107 . -0.383 -6.294 29.118 0.52 16.22 ? ? ? ? ? . 107 GLU A C 2348 ATOM 881 O O A GLU A 2348 107 . -1.159 -5.512 29.658 0.48 15.00 ? ? ? ? ? . 107 GLU A O 2348 ATOM 882 O O B GLU A 2348 107 . -0.983 -5.467 29.799 0.52 14.91 ? ? ? ? ? . 107 GLU A O 2348 ATOM 883 C CB A GLU A 2348 107 . 0.136 -7.934 30.885 0.48 18.90 ? ? ? ? ? . 107 GLU A CB 2348 ATOM 884 C CB B GLU A 2348 107 . -0.026 -8.061 30.878 0.52 18.53 ? ? ? ? ? . 107 GLU A CB 2348 ATOM 885 C CG A GLU A 2348 107 . -0.152 -9.282 31.527 0.48 20.28 ? ? ? ? ? . 107 GLU A CG 2348 ATOM 886 C CG B GLU A 2348 107 . -0.457 -9.445 31.335 0.52 19.46 ? ? ? ? ? . 107 GLU A CG 2348 ATOM 887 C CD A GLU A 2348 107 . -1.634 -9.612 31.585 0.48 20.99 ? ? ? ? ? . 107 GLU A CD 2348 ATOM 888 C CD B GLU A 2348 107 . -0.230 -9.688 32.809 0.52 20.69 ? ? ? ? ? . 107 GLU A CD 2348 ATOM 889 O OE1 A GLU A 2348 107 . -1.964 -10.810 31.716 0.48 22.80 ? ? ? ? ? . 107 GLU A OE1 2348 ATOM 890 O OE2 A GLU A 2348 107 . -2.475 -8.685 31.501 0.48 20.81 ? ? ? ? ? 1- 107 GLU A OE2 2348 ATOM 891 O OE1 B GLU A 2348 107 . 0.552 -8.941 33.435 0.52 21.77 ? ? ? ? ? . 107 GLU A OE1 2348 ATOM 892 O OE2 B GLU A 2348 107 . -0.834 -10.641 33.338 0.52 20.72 ? ? ? ? ? 1- 107 GLU A OE2 2348 ATOM 893 N N . SER A 2348 108 . 0.380 -5.969 28.081 1.00 15.68 ? ? ? ? ? . 108 SER A N 2348 ATOM 894 C CA . SER A 2348 108 . 0.383 -4.638 27.500 1.00 17.08 ? ? ? ? ? . 108 SER A CA 2348 ATOM 895 C C . SER A 2348 108 . 0.985 -4.755 26.112 1.00 16.89 ? ? ? ? ? . 108 SER A C 2348 ATOM 896 O O . SER A 2348 108 . 1.450 -5.829 25.729 1.00 17.73 ? ? ? ? ? . 108 SER A O 2348 ATOM 897 C CB . SER A 2348 108 . 1.213 -3.668 28.353 1.00 18.24 ? ? ? ? ? . 108 SER A CB 2348 ATOM 898 O OG . SER A 2348 108 . 2.566 -4.088 28.395 1.00 19.50 ? ? ? ? ? . 108 SER A OG 2348 ATOM 899 N N . ILE A 2348 109 . 0.943 -3.654 25.361 1.00 16.59 ? ? ? ? ? . 109 ILE A N 2348 ATOM 900 C CA . ILE A 2348 109 . 1.631 -3.552 24.077 1.00 16.95 ? ? ? ? ? . 109 ILE A CA 2348 ATOM 901 C C . ILE A 2348 109 . 2.424 -2.244 24.042 1.00 17.07 ? ? ? ? ? . 109 ILE A C 2348 ATOM 902 O O . ILE A 2348 109 . 2.119 -1.314 24.806 1.00 15.40 ? ? ? ? ? . 109 ILE A O 2348 ATOM 903 C CB . ILE A 2348 109 . 0.661 -3.621 22.878 1.00 16.61 ? ? ? ? ? . 109 ILE A CB 2348 ATOM 904 C CG1 . ILE A 2348 109 . -0.342 -2.464 22.916 1.00 16.67 ? ? ? ? ? . 109 ILE A CG1 2348 ATOM 905 C CG2 . ILE A 2348 109 . -0.070 -4.947 22.864 1.00 17.96 ? ? ? ? ? . 109 ILE A CG2 2348 ATOM 906 C CD1 . ILE A 2348 109 . -1.334 -2.459 21.764 1.00 17.14 ? ? ? ? ? . 109 ILE A CD1 2348 ATOM 907 N N . PRO A 2348 110 . 3.455 -2.163 23.184 1.00 17.10 ? ? ? ? ? . 110 PRO A N 2348 ATOM 908 C CA . PRO A 2348 110 . 3.969 -3.163 22.255 1.00 16.27 ? ? ? ? ? . 110 PRO A CA 2348 ATOM 909 C C . PRO A 2348 110 . 4.615 -4.367 22.957 1.00 16.00 ? ? ? ? ? . 110 PRO A C 2348 ATOM 910 O O . PRO A 2348 110 . 5.305 -4.213 23.960 1.00 15.22 ? ? ? ? ? . 110 PRO A O 2348 ATOM 911 C CB . PRO A 2348 110 . 5.004 -2.363 21.462 1.00 16.63 ? ? ? ? ? . 110 PRO A CB 2348 ATOM 912 C CG . PRO A 2348 110 . 5.544 -1.416 22.461 1.00 14.86 ? ? ? ? ? . 110 PRO A CG 2348 ATOM 913 C CD . PRO A 2348 110 . 4.334 -0.974 23.215 1.00 16.56 ? ? ? ? ? . 110 PRO A CD 2348 ATOM 914 N N . THR A 2348 111 . 4.358 -5.563 22.450 1.00 16.65 ? ? ? ? ? . 111 THR A N 2348 ATOM 915 C CA . THR A 2348 111 . 5.020 -6.757 22.952 1.00 16.87 ? ? ? ? ? . 111 THR A CA 2348 ATOM 916 C C . THR A 2348 111 . 5.390 -7.633 21.753 1.00 16.48 ? ? ? ? ? . 111 THR A C 2348 ATOM 917 O O . THR A 2348 111 . 4.610 -7.759 20.799 1.00 16.90 ? ? ? ? ? . 111 THR A O 2348 ATOM 918 C CB . THR A 2348 111 . 4.107 -7.527 23.939 1.00 17.53 ? ? ? ? ? . 111 THR A CB 2348 ATOM 919 C CG2 . THR A 2348 111 . 4.684 -8.888 24.316 1.00 18.56 ? ? ? ? ? . 111 THR A CG2 2348 ATOM 920 O OG1 . THR A 2348 111 . 3.924 -6.761 25.132 1.00 18.31 ? ? ? ? ? . 111 THR A OG1 2348 ATOM 921 N N . LEU A 2348 112 . 6.592 -8.200 21.806 1.00 15.48 ? ? ? ? ? . 112 LEU A N 2348 ATOM 922 C CA . LEU A 2348 112 . 7.032 -9.243 20.872 1.00 16.77 ? ? ? ? ? . 112 LEU A CA 2348 ATOM 923 C C . LEU A 2348 112 . 7.096 -10.595 21.590 1.00 17.72 ? ? ? ? ? . 112 LEU A C 2348 ATOM 924 O O . LEU A 2348 112 . 7.684 -10.706 22.669 1.00 18.56 ? ? ? ? ? . 112 LEU A O 2348 ATOM 925 C CB . LEU A 2348 112 . 8.420 -8.917 20.311 1.00 16.88 ? ? ? ? ? . 112 LEU A CB 2348 ATOM 926 C CG . LEU A 2348 112 . 8.521 -7.687 19.408 1.00 17.77 ? ? ? ? ? . 112 LEU A CG 2348 ATOM 927 C CD1 . LEU A 2348 112 . 9.973 -7.390 19.033 1.00 16.92 ? ? ? ? ? . 112 LEU A CD1 2348 ATOM 928 C CD2 . LEU A 2348 112 . 7.689 -7.898 18.153 1.00 19.55 ? ? ? ? ? . 112 LEU A CD2 2348 ATOM 929 N N . ILE A 2348 113 . 6.496 -11.617 20.990 1.00 15.87 ? ? ? ? ? . 113 ILE A N 2348 ATOM 930 C CA . ILE A 2348 113 . 6.651 -12.997 21.460 1.00 15.67 ? ? ? ? ? . 113 ILE A CA 2348 ATOM 931 C C . ILE A 2348 113 . 7.452 -13.761 20.404 1.00 16.43 ? ? ? ? ? . 113 ILE A C 2348 ATOM 932 O O . ILE A 2348 113 . 7.100 -13.752 19.241 1.00 17.53 ? ? ? ? ? . 113 ILE A O 2348 ATOM 933 C CB . ILE A 2348 113 . 5.284 -13.665 21.671 1.00 16.79 ? ? ? ? ? . 113 ILE A CB 2348 ATOM 934 C CG1 . ILE A 2348 113 . 4.438 -12.866 22.669 1.00 16.77 ? ? ? ? ? . 113 ILE A CG1 2348 ATOM 935 C CG2 . ILE A 2348 113 . 5.450 -15.106 22.132 1.00 16.45 ? ? ? ? ? . 113 ILE A CG2 2348 ATOM 936 C CD1 . ILE A 2348 113 . 5.059 -12.691 24.033 1.00 17.44 ? ? ? ? ? . 113 ILE A CD1 2348 ATOM 937 N N . THR A 2348 114 . 8.548 -14.395 20.806 1.00 15.64 ? ? ? ? ? . 114 THR A N 2348 ATOM 938 C CA . THR A 2348 114 . 9.432 -15.065 19.851 1.00 15.54 ? ? ? ? ? . 114 THR A CA 2348 ATOM 939 C C . THR A 2348 114 . 9.105 -16.535 19.804 1.00 16.03 ? ? ? ? ? . 114 THR A C 2348 ATOM 940 O O . THR A 2348 114 . 9.069 -17.201 20.843 1.00 15.89 ? ? ? ? ? . 114 THR A O 2348 ATOM 941 C CB . THR A 2348 114 . 10.899 -14.877 20.248 1.00 16.17 ? ? ? ? ? . 114 THR A CB 2348 ATOM 942 C CG2 . THR A 2348 114 . 11.843 -15.242 19.082 1.00 17.31 ? ? ? ? ? . 114 THR A CG2 2348 ATOM 943 O OG1 . THR A 2348 114 . 11.091 -13.522 20.641 1.00 16.08 ? ? ? ? ? . 114 THR A OG1 2348 ATOM 944 N N A ILE A 2348 115 . 8.888 -17.070 18.605 0.55 16.54 ? ? ? ? ? . 115 ILE A N 2348 ATOM 945 N N B ILE A 2348 115 . 8.876 -17.020 18.585 0.45 15.81 ? ? ? ? ? . 115 ILE A N 2348 ATOM 946 C CA A ILE A 2348 115 . 8.499 -18.473 18.450 0.55 16.27 ? ? ? ? ? . 115 ILE A CA 2348 ATOM 947 C CA B ILE A 2348 115 . 8.382 -18.358 18.324 0.45 15.23 ? ? ? ? ? . 115 ILE A CA 2348 ATOM 948 C C A ILE A 2348 115 . 9.340 -19.134 17.352 0.55 15.48 ? ? ? ? ? . 115 ILE A C 2348 ATOM 949 C C B ILE A 2348 115 . 9.324 -19.049 17.348 0.45 14.86 ? ? ? ? ? . 115 ILE A C 2348 ATOM 950 O O A ILE A 2348 115 . 9.682 -18.500 16.351 0.55 15.76 ? ? ? ? ? . 115 ILE A O 2348 ATOM 951 O O B ILE A 2348 115 . 9.872 -18.421 16.445 0.45 14.85 ? ? ? ? ? . 115 ILE A O 2348 ATOM 952 C CB A ILE A 2348 115 . 6.978 -18.584 18.143 0.55 16.88 ? ? ? ? ? . 115 ILE A CB 2348 ATOM 953 C CB B ILE A 2348 115 . 6.970 -18.282 17.698 0.45 14.58 ? ? ? ? ? . 115 ILE A CB 2348 ATOM 954 C CG1 A ILE A 2348 115 . 6.158 -18.040 19.325 0.55 17.01 ? ? ? ? ? . 115 ILE A CG1 2348 ATOM 955 C CG2 A ILE A 2348 115 . 6.558 -20.022 17.847 0.55 17.77 ? ? ? ? ? . 115 ILE A CG2 2348 ATOM 956 C CG1 B ILE A 2348 115 . 6.030 -17.511 18.630 0.45 13.86 ? ? ? ? ? . 115 ILE A CG1 2348 ATOM 957 C CG2 B ILE A 2348 115 . 6.416 -19.669 17.440 0.45 15.79 ? ? ? ? ? . 115 ILE A CG2 2348 ATOM 958 C CD1 A ILE A 2348 115 . 4.718 -17.741 18.993 0.55 18.59 ? ? ? ? ? . 115 ILE A CD1 2348 ATOM 959 C CD1 B ILE A 2348 115 . 5.831 -18.198 19.961 0.45 13.69 ? ? ? ? ? . 115 ILE A CD1 2348 ATOM 960 N N A ASN A 2348 116 . 9.696 -20.393 17.578 0.55 14.26 ? ? ? ? ? . 116 ASN A N 2348 ATOM 961 N N B ASN A 2348 116 . 9.528 -20.339 17.550 0.45 14.15 ? ? ? ? ? . 116 ASN A N 2348 ATOM 962 C CA A ASN A 2348 116 . 10.195 -21.272 16.531 0.55 14.49 ? ? ? ? ? . 116 ASN A CA 2348 ATOM 963 C CA B ASN A 2348 116 . 10.161 -21.166 16.547 0.45 14.57 ? ? ? ? ? . 116 ASN A CA 2348 ATOM 964 C C A ASN A 2348 116 . 8.994 -21.667 15.677 0.55 14.67 ? ? ? ? ? . 116 ASN A C 2348 ATOM 965 C C B ASN A 2348 116 . 9.036 -21.700 15.669 0.45 14.67 ? ? ? ? ? . 116 ASN A C 2348 ATOM 966 O O A ASN A 2348 116 . 8.060 -22.285 16.182 0.55 14.82 ? ? ? ? ? . 116 ASN A O 2348 ATOM 967 O O B ASN A 2348 116 . 8.204 -22.467 16.147 0.45 14.81 ? ? ? ? ? . 116 ASN A O 2348 ATOM 968 C CB A ASN A 2348 116 . 10.852 -22.511 17.146 0.55 14.78 ? ? ? ? ? . 116 ASN A CB 2348 ATOM 969 C CB B ASN A 2348 116 . 10.920 -22.308 17.211 0.45 15.08 ? ? ? ? ? . 116 ASN A CB 2348 ATOM 970 C CG A ASN A 2348 116 . 11.479 -23.433 16.108 0.55 14.39 ? ? ? ? ? . 116 ASN A CG 2348 ATOM 971 C CG B ASN A 2348 116 . 11.701 -23.154 16.220 0.45 15.35 ? ? ? ? ? . 116 ASN A CG 2348 ATOM 972 N ND2 A ASN A 2348 116 . 12.807 -23.467 16.077 0.55 15.51 ? ? ? ? ? . 116 ASN A ND2 2348 ATOM 973 O OD1 A ASN A 2348 116 . 10.785 -24.115 15.358 0.55 13.66 ? ? ? ? ? . 116 ASN A OD1 2348 ATOM 974 N ND2 B ASN A 2348 116 . 11.743 -24.447 16.470 0.45 15.08 ? ? ? ? ? . 116 ASN A ND2 2348 ATOM 975 O OD1 B ASN A 2348 116 . 12.279 -22.646 15.258 0.45 15.65 ? ? ? ? ? . 116 ASN A OD1 2348 ATOM 976 N N . ALA A 2348 117 . 9.000 -21.278 14.401 1.00 14.43 ? ? ? ? ? . 117 ALA A N 2348 ATOM 977 C CA . ALA A 2348 117 . 7.853 -21.558 13.494 1.00 15.56 ? ? ? ? ? . 117 ALA A CA 2348 ATOM 978 C C . ALA A 2348 117 . 7.501 -23.034 13.368 1.00 16.26 ? ? ? ? ? . 117 ALA A C 2348 ATOM 979 O O . ALA A 2348 117 . 6.317 -23.404 13.362 1.00 19.27 ? ? ? ? ? . 117 ALA A O 2348 ATOM 980 C CB . ALA A 2348 117 . 8.106 -20.984 12.098 1.00 15.32 ? ? ? ? ? . 117 ALA A CB 2348 ATOM 981 N N . ASP A 2348 118 . 8.530 -23.869 13.280 1.00 13.71 ? ? ? ? ? . 118 ASP A N 2348 ATOM 982 C CA . ASP A 2348 118 . 8.340 -25.280 12.997 1.00 13.63 ? ? ? ? ? . 118 ASP A CA 2348 ATOM 983 C C . ASP A 2348 118 . 7.697 -26.025 14.164 1.00 13.30 ? ? ? ? ? . 118 ASP A C 2348 ATOM 984 O O . ASP A 2348 118 . 6.772 -26.787 13.955 1.00 12.97 ? ? ? ? ? . 118 ASP A O 2348 ATOM 985 C CB . ASP A 2348 118 . 9.665 -25.950 12.628 1.00 13.67 ? ? ? ? ? . 118 ASP A CB 2348 ATOM 986 C CG . ASP A 2348 118 . 10.195 -25.494 11.295 1.00 14.35 ? ? ? ? ? . 118 ASP A CG 2348 ATOM 987 O OD1 . ASP A 2348 118 . 9.479 -24.785 10.536 1.00 13.29 ? ? ? ? ? . 118 ASP A OD1 2348 ATOM 988 O OD2 . ASP A 2348 118 . 11.353 -25.828 11.017 1.00 16.07 ? ? ? ? ? 1- 118 ASP A OD2 2348 ATOM 989 N N . THR A 2348 119 . 8.191 -25.774 15.372 1.00 13.59 ? ? ? ? ? . 119 THR A N 2348 ATOM 990 C CA . THR A 2348 119 . 7.739 -26.479 16.573 1.00 13.80 ? ? ? ? ? . 119 THR A CA 2348 ATOM 991 C C . THR A 2348 119 . 6.693 -25.695 17.356 1.00 13.84 ? ? ? ? ? . 119 THR A C 2348 ATOM 992 O O . THR A 2348 119 . 6.050 -26.256 18.241 1.00 15.00 ? ? ? ? ? . 119 THR A O 2348 ATOM 993 C CB . THR A 2348 119 . 8.912 -26.737 17.531 1.00 14.43 ? ? ? ? ? . 119 THR A CB 2348 ATOM 994 C CG2 . THR A 2348 119 . 10.039 -27.489 16.838 1.00 16.16 ? ? ? ? ? . 119 THR A CG2 2348 ATOM 995 O OG1 . THR A 2348 119 . 9.392 -25.493 18.029 1.00 14.78 ? ? ? ? ? . 119 THR A OG1 2348 ATOM 996 N N . GLY A 2348 120 . 6.550 -24.410 17.051 1.00 13.31 ? ? ? ? ? . 120 GLY A N 2348 ATOM 997 C CA . GLY A 2348 120 . 5.745 -23.482 17.845 1.00 15.55 ? ? ? ? ? . 120 GLY A CA 2348 ATOM 998 C C . GLY A 2348 120 . 6.291 -23.172 19.227 1.00 15.73 ? ? ? ? ? . 120 GLY A C 2348 ATOM 999 O O . GLY A 2348 120 . 5.607 -22.535 20.029 1.00 18.55 ? ? ? ? ? . 120 GLY A O 2348 ATOM 1000 N N . ALA A 2348 121 . 7.522 -23.581 19.519 1.00 15.46 ? ? ? ? ? . 121 ALA A N 2348 ATOM 1001 C CA . ALA A 2348 121 . 8.064 -23.394 20.865 1.00 15.87 ? ? ? ? ? . 121 ALA A CA 2348 ATOM 1002 C C . ALA A 2348 121 . 8.213 -21.904 21.136 1.00 15.57 ? ? ? ? ? . 121 ALA A C 2348 ATOM 1003 O O . ALA A 2348 121 . 8.585 -21.138 20.241 1.00 13.38 ? ? ? ? ? . 121 ALA A O 2348 ATOM 1004 C CB . ALA A 2348 121 . 9.389 -24.104 21.016 1.00 16.46 ? ? ? ? ? . 121 ALA A CB 2348 ATOM 1005 N N . ILE A 2348 122 . 7.880 -21.483 22.353 1.00 15.28 ? ? ? ? ? . 122 ILE A N 2348 ATOM 1006 C CA . ILE A 2348 122 . 8.156 -20.104 22.776 1.00 14.91 ? ? ? ? ? . 122 ILE A CA 2348 ATOM 1007 C C . ILE A 2348 122 . 9.641 -20.062 23.119 1.00 15.51 ? ? ? ? ? . 122 ILE A C 2348 ATOM 1008 O O . ILE A 2348 122 . 10.119 -20.875 23.900 1.00 16.67 ? ? ? ? ? . 122 ILE A O 2348 ATOM 1009 C CB . ILE A 2348 122 . 7.290 -19.669 23.961 1.00 15.79 ? ? ? ? ? . 122 ILE A CB 2348 ATOM 1010 C CG1 . ILE A 2348 122 . 5.823 -19.696 23.552 1.00 17.18 ? ? ? ? ? . 122 ILE A CG1 2348 ATOM 1011 C CG2 . ILE A 2348 122 . 7.689 -18.266 24.434 1.00 17.48 ? ? ? ? ? . 122 ILE A CG2 2348 ATOM 1012 C CD1 . ILE A 2348 122 . 4.864 -19.526 24.708 1.00 17.88 ? ? ? ? ? . 122 ILE A CD1 2348 ATOM 1013 N N A ILE A 2348 123 . 10.392 -19.155 22.503 0.47 13.95 ? ? ? ? ? . 123 ILE A N 2348 ATOM 1014 N N B ILE A 2348 123 . 10.323 -19.113 22.485 0.53 15.23 ? ? ? ? ? . 123 ILE A N 2348 ATOM 1015 C CA A ILE A 2348 123 . 11.809 -18.977 22.850 0.47 14.95 ? ? ? ? ? . 123 ILE A CA 2348 ATOM 1016 C CA B ILE A 2348 123 . 11.762 -18.894 22.572 0.53 17.28 ? ? ? ? ? . 123 ILE A CA 2348 ATOM 1017 C C A ILE A 2348 123 . 12.170 -17.581 23.356 0.47 15.02 ? ? ? ? ? . 123 ILE A C 2348 ATOM 1018 C C B ILE A 2348 123 . 12.096 -17.681 23.473 0.53 16.15 ? ? ? ? ? . 123 ILE A C 2348 ATOM 1019 O O A ILE A 2348 123 . 13.349 -17.281 23.543 0.47 15.33 ? ? ? ? ? . 123 ILE A O 2348 ATOM 1020 O O B ILE A 2348 123 . 13.152 -17.646 24.107 0.53 15.98 ? ? ? ? ? . 123 ILE A O 2348 ATOM 1021 C CB A ILE A 2348 123 . 12.723 -19.369 21.683 0.47 14.78 ? ? ? ? ? . 123 ILE A CB 2348 ATOM 1022 C CB B ILE A 2348 123 . 12.330 -18.807 21.116 0.53 19.50 ? ? ? ? ? . 123 ILE A CB 2348 ATOM 1023 C CG1 A ILE A 2348 123 . 12.353 -18.591 20.417 0.47 14.37 ? ? ? ? ? . 123 ILE A CG1 2348 ATOM 1024 C CG2 A ILE A 2348 123 . 12.618 -20.868 21.444 0.47 15.29 ? ? ? ? ? . 123 ILE A CG2 2348 ATOM 1025 C CG1 B ILE A 2348 123 . 13.033 -20.116 20.737 0.53 21.28 ? ? ? ? ? . 123 ILE A CG1 2348 ATOM 1026 C CG2 B ILE A 2348 123 . 13.317 -17.675 20.906 0.53 20.71 ? ? ? ? ? . 123 ILE A CG2 2348 ATOM 1027 C CD1 A ILE A 2348 123 . 13.153 -19.012 19.200 0.47 14.19 ? ? ? ? ? . 123 ILE A CD1 2348 ATOM 1028 C CD1 B ILE A 2348 123 . 12.135 -21.339 20.747 0.53 22.34 ? ? ? ? ? . 123 ILE A CD1 2348 ATOM 1029 N N . GLY A 2348 124 . 11.173 -16.729 23.568 1.00 15.77 ? ? ? ? ? . 124 GLY A N 2348 ATOM 1030 C CA . GLY A 2348 124 . 11.373 -15.508 24.323 1.00 15.97 ? ? ? ? ? . 124 GLY A CA 2348 ATOM 1031 C C . GLY A 2348 124 . 10.096 -14.707 24.394 1.00 15.46 ? ? ? ? ? . 124 GLY A C 2348 ATOM 1032 O O . GLY A 2348 124 . 9.193 -14.882 23.581 1.00 15.31 ? ? ? ? ? . 124 GLY A O 2348 ATOM 1033 N N . THR A 2348 125 . 10.008 -13.856 25.405 1.00 14.42 ? ? ? ? ? . 125 THR A N 2348 ATOM 1034 C CA . THR A 2348 125 . 8.920 -12.890 25.529 1.00 14.27 ? ? ? ? ? . 125 THR A CA 2348 ATOM 1035 C C . THR A 2348 125 . 9.371 -11.431 25.677 1.00 14.34 ? ? ? ? ? . 125 THR A C 2348 ATOM 1036 O O . THR A 2348 125 . 8.520 -10.535 25.770 1.00 13.54 ? ? ? ? ? . 125 THR A O 2348 ATOM 1037 C CB . THR A 2348 125 . 8.063 -13.230 26.766 1.00 15.10 ? ? ? ? ? . 125 THR A CB 2348 ATOM 1038 C CG2 . THR A 2348 125 . 7.560 -14.673 26.687 1.00 15.56 ? ? ? ? ? . 125 THR A CG2 2348 ATOM 1039 O OG1 . THR A 2348 125 . 8.859 -13.073 27.951 1.00 15.70 ? ? ? ? ? . 125 THR A OG1 2348 ATOM 1040 N N A GLN A 2348 126 . 10.689 -11.200 25.676 0.65 15.74 ? ? ? ? ? . 126 GLN A N 2348 ATOM 1041 N N B GLN A 2348 126 . 10.683 -11.184 25.692 0.35 15.08 ? ? ? ? ? . 126 GLN A N 2348 ATOM 1042 C CA A GLN A 2348 126 . 11.267 -9.893 25.996 0.65 16.74 ? ? ? ? ? . 126 GLN A CA 2348 ATOM 1043 C CA B GLN A 2348 126 . 11.214 -9.851 25.975 0.35 15.65 ? ? ? ? ? . 126 GLN A CA 2348 ATOM 1044 C C A GLN A 2348 126 . 11.938 -9.209 24.799 0.65 16.96 ? ? ? ? ? . 126 GLN A C 2348 ATOM 1045 C C B GLN A 2348 126 . 11.948 -9.214 24.801 0.35 16.17 ? ? ? ? ? . 126 GLN A C 2348 ATOM 1046 O O A GLN A 2348 126 . 12.672 -8.231 24.982 0.65 18.20 ? ? ? ? ? . 126 GLN A O 2348 ATOM 1047 O O B GLN A 2348 126 . 12.738 -8.285 25.009 0.35 17.02 ? ? ? ? ? . 126 GLN A O 2348 ATOM 1048 C CB A GLN A 2348 126 . 12.281 -10.056 27.137 0.65 17.82 ? ? ? ? ? . 126 GLN A CB 2348 ATOM 1049 C CB B GLN A 2348 126 . 12.138 -9.924 27.186 0.35 15.92 ? ? ? ? ? . 126 GLN A CB 2348 ATOM 1050 C CG A GLN A 2348 126 . 11.700 -10.649 28.418 0.65 19.05 ? ? ? ? ? . 126 GLN A CG 2348 ATOM 1051 C CG B GLN A 2348 126 . 11.370 -10.101 28.485 0.35 16.11 ? ? ? ? ? . 126 GLN A CG 2348 ATOM 1052 C CD A GLN A 2348 126 . 10.613 -9.780 29.040 0.65 21.28 ? ? ? ? ? . 126 GLN A CD 2348 ATOM 1053 C CD B GLN A 2348 126 . 12.269 -10.217 29.694 0.35 16.65 ? ? ? ? ? . 126 GLN A CD 2348 ATOM 1054 N NE2 A GLN A 2348 126 . 9.365 -10.244 28.979 0.65 21.64 ? ? ? ? ? . 126 GLN A NE2 2348 ATOM 1055 O OE1 A GLN A 2348 126 . 10.896 -8.711 29.578 0.65 24.99 ? ? ? ? ? . 126 GLN A OE1 2348 ATOM 1056 N NE2 B GLN A 2348 126 . 12.111 -9.296 30.636 0.35 16.48 ? ? ? ? ? . 126 GLN A NE2 2348 ATOM 1057 O OE1 B GLN A 2348 126 . 13.085 -11.133 29.790 0.35 16.80 ? ? ? ? ? . 126 GLN A OE1 2348 ATOM 1058 N N . ALA A 2348 127 . 11.681 -9.681 23.580 1.00 16.07 ? ? ? ? ? . 127 ALA A N 2348 ATOM 1059 C CA . ALA A 2348 127 . 12.365 -9.138 22.395 1.00 15.77 ? ? ? ? ? . 127 ALA A CA 2348 ATOM 1060 C C . ALA A 2348 127 . 12.118 -7.629 22.136 1.00 16.92 ? ? ? ? ? . 127 ALA A C 2348 ATOM 1061 O O . ALA A 2348 127 . 12.988 -6.961 21.574 1.00 16.61 ? ? ? ? ? . 127 ALA A O 2348 ATOM 1062 C CB . ALA A 2348 127 . 12.088 -9.962 21.152 1.00 15.60 ? ? ? ? ? . 127 ALA A CB 2348 ATOM 1063 N N A ARG A 2348 128 . 10.956 -7.112 22.537 0.56 17.01 ? ? ? ? ? . 128 ARG A N 2348 ATOM 1064 N N B ARG A 2348 128 . 10.970 -7.103 22.563 0.44 16.65 ? ? ? ? ? . 128 ARG A N 2348 ATOM 1065 C CA A ARG A 2348 128 . 10.675 -5.662 22.452 0.56 17.35 ? ? ? ? ? . 128 ARG A CA 2348 ATOM 1066 C CA B ARG A 2348 128 . 10.711 -5.658 22.477 0.44 16.75 ? ? ? ? ? . 128 ARG A CA 2348 ATOM 1067 C C A ARG A 2348 128 . 11.742 -4.852 23.213 0.56 17.98 ? ? ? ? ? . 128 ARG A C 2348 ATOM 1068 C C B ARG A 2348 128 . 11.832 -4.909 23.210 0.44 17.06 ? ? ? ? ? . 128 ARG A C 2348 ATOM 1069 O O A ARG A 2348 128 . 12.117 -3.754 22.795 0.56 19.74 ? ? ? ? ? . 128 ARG A O 2348 ATOM 1070 O O B ARG A 2348 128 . 12.397 -3.949 22.691 0.44 18.15 ? ? ? ? ? . 128 ARG A O 2348 ATOM 1071 C CB A ARG A 2348 128 . 9.263 -5.347 22.979 0.56 17.73 ? ? ? ? ? . 128 ARG A CB 2348 ATOM 1072 C CB B ARG A 2348 128 . 9.339 -5.312 23.066 0.44 16.87 ? ? ? ? ? . 128 ARG A CB 2348 ATOM 1073 C CG A ARG A 2348 128 . 8.870 -3.865 23.016 0.56 18.71 ? ? ? ? ? . 128 ARG A CG 2348 ATOM 1074 C CG B ARG A 2348 128 . 8.901 -3.861 22.874 0.44 17.49 ? ? ? ? ? . 128 ARG A CG 2348 ATOM 1075 C CD A ARG A 2348 128 . 9.128 -3.215 24.373 0.56 20.16 ? ? ? ? ? . 128 ARG A CD 2348 ATOM 1076 C CD B ARG A 2348 128 . 9.642 -2.916 23.804 0.44 18.39 ? ? ? ? ? . 128 ARG A CD 2348 ATOM 1077 N NE A ARG A 2348 128 . 8.614 -1.848 24.461 0.56 21.19 ? ? ? ? ? . 128 ARG A NE 2348 ATOM 1078 N NE B ARG A 2348 128 . 9.174 -1.532 23.713 0.44 18.67 ? ? ? ? ? . 128 ARG A NE 2348 ATOM 1079 C CZ A ARG A 2348 128 . 9.152 -0.774 23.876 0.56 22.12 ? ? ? ? ? . 128 ARG A CZ 2348 ATOM 1080 C CZ B ARG A 2348 128 . 8.307 -0.973 24.557 0.44 18.88 ? ? ? ? ? . 128 ARG A CZ 2348 ATOM 1081 N NH1 A ARG A 2348 128 . 10.245 -0.862 23.118 0.56 21.19 ? ? ? ? ? 1+ 128 ARG A NH1 2348 ATOM 1082 N NH2 A ARG A 2348 128 . 8.582 0.419 24.051 0.56 22.67 ? ? ? ? ? . 128 ARG A NH2 2348 ATOM 1083 N NH1 B ARG A 2348 128 . 7.788 -1.677 25.551 0.44 18.59 ? ? ? ? ? 1+ 128 ARG A NH1 2348 ATOM 1084 N NH2 B ARG A 2348 128 . 7.951 0.296 24.402 0.44 19.51 ? ? ? ? ? . 128 ARG A NH2 2348 ATOM 1085 N N A THR A 2348 129 . 12.197 -5.402 24.338 0.56 16.60 ? ? ? ? ? . 129 THR A N 2348 ATOM 1086 N N B THR A 2348 129 . 12.172 -5.391 24.401 0.44 16.19 ? ? ? ? ? . 129 THR A N 2348 ATOM 1087 C CA A THR A 2348 129 . 13.260 -4.819 25.151 0.56 15.90 ? ? ? ? ? . 129 THR A CA 2348 ATOM 1088 C CA B THR A 2348 129 . 13.262 -4.829 25.190 0.44 15.82 ? ? ? ? ? . 129 THR A CA 2348 ATOM 1089 C C A THR A 2348 129 . 14.648 -5.072 24.556 0.56 15.75 ? ? ? ? ? . 129 THR A C 2348 ATOM 1090 C C B THR A 2348 129 . 14.652 -5.082 24.590 0.44 15.77 ? ? ? ? ? . 129 THR A C 2348 ATOM 1091 O O A THR A 2348 129 . 15.501 -4.173 24.523 0.56 14.19 ? ? ? ? ? . 129 THR A O 2348 ATOM 1092 O O B THR A 2348 129 . 15.508 -4.188 24.583 0.44 14.57 ? ? ? ? ? . 129 THR A O 2348 ATOM 1093 C CB A THR A 2348 129 . 13.199 -5.413 26.563 0.56 16.22 ? ? ? ? ? . 129 THR A CB 2348 ATOM 1094 C CB B THR A 2348 129 . 13.239 -5.411 26.607 0.44 16.28 ? ? ? ? ? . 129 THR A CB 2348 ATOM 1095 C CG2 A THR A 2348 129 . 14.194 -4.750 27.499 0.56 16.27 ? ? ? ? ? . 129 THR A CG2 2348 ATOM 1096 O OG1 A THR A 2348 129 . 11.866 -5.240 27.067 0.56 15.54 ? ? ? ? ? . 129 THR A OG1 2348 ATOM 1097 C CG2 B THR A 2348 129 . 14.425 -4.927 27.397 0.44 16.31 ? ? ? ? ? . 129 THR A CG2 2348 ATOM 1098 O OG1 B THR A 2348 129 . 12.025 -5.011 27.257 0.44 16.08 ? ? ? ? ? . 129 THR A OG1 2348 ATOM 1099 N N . ARG A 2348 130 . 14.877 -6.301 24.106 1.00 15.66 ? ? ? ? ? . 130 ARG A N 2348 ATOM 1100 C CA . ARG A 2348 130 . 16.188 -6.692 23.577 1.00 16.35 ? ? ? ? ? . 130 ARG A CA 2348 ATOM 1101 C C . ARG A 2348 130 . 16.559 -5.897 22.320 1.00 15.65 ? ? ? ? ? . 130 ARG A C 2348 ATOM 1102 O O . ARG A 2348 130 . 17.720 -5.558 22.136 1.00 15.70 ? ? ? ? ? . 130 ARG A O 2348 ATOM 1103 C CB . ARG A 2348 130 . 16.246 -8.188 23.306 1.00 18.25 ? ? ? ? ? . 130 ARG A CB 2348 ATOM 1104 C CG . ARG A 2348 130 . 16.058 -9.052 24.544 1.00 20.23 ? ? ? ? ? . 130 ARG A CG 2348 ATOM 1105 C CD . ARG A 2348 130 . 17.267 -9.045 25.461 1.00 24.15 ? ? ? ? ? . 130 ARG A CD 2348 ATOM 1106 N NE . ARG A 2348 130 . 16.962 -9.671 26.747 1.00 26.08 ? ? ? ? ? . 130 ARG A NE 2348 ATOM 1107 C CZ . ARG A 2348 130 . 16.384 -9.059 27.784 1.00 29.65 ? ? ? ? ? . 130 ARG A CZ 2348 ATOM 1108 N NH1 . ARG A 2348 130 . 15.999 -7.782 27.725 1.00 30.49 ? ? ? ? ? 1+ 130 ARG A NH1 2348 ATOM 1109 N NH2 . ARG A 2348 130 . 16.171 -9.748 28.906 1.00 33.51 ? ? ? ? ? . 130 ARG A NH2 2348 ATOM 1110 N N . VAL A 2348 131 . 15.561 -5.570 21.501 1.00 15.55 ? ? ? ? ? . 131 VAL A N 2348 ATOM 1111 C CA . VAL A 2348 131 . 15.755 -4.735 20.300 1.00 16.06 ? ? ? ? ? . 131 VAL A CA 2348 ATOM 1112 C C . VAL A 2348 131 . 16.319 -3.355 20.678 1.00 15.16 ? ? ? ? ? . 131 VAL A C 2348 ATOM 1113 O O . VAL A 2348 131 . 17.149 -2.806 19.958 1.00 14.17 ? ? ? ? ? . 131 VAL A O 2348 ATOM 1114 C CB . VAL A 2348 131 . 14.431 -4.608 19.503 1.00 18.89 ? ? ? ? ? . 131 VAL A CB 2348 ATOM 1115 C CG1 . VAL A 2348 131 . 14.491 -3.492 18.465 1.00 19.08 ? ? ? ? ? . 131 VAL A CG1 2348 ATOM 1116 C CG2 . VAL A 2348 131 . 14.079 -5.950 18.859 1.00 21.65 ? ? ? ? ? . 131 VAL A CG2 2348 ATOM 1117 N N A ILE A 2348 132 . 15.856 -2.817 21.806 0.19 15.13 ? ? ? ? ? . 132 ILE A N 2348 ATOM 1118 N N B ILE A 2348 132 . 15.884 -2.809 21.816 0.81 15.27 ? ? ? ? ? . 132 ILE A N 2348 ATOM 1119 C CA A ILE A 2348 132 . 16.341 -1.547 22.332 0.19 15.00 ? ? ? ? ? . 132 ILE A CA 2348 ATOM 1120 C CA B ILE A 2348 132 . 16.395 -1.520 22.293 0.81 14.70 ? ? ? ? ? . 132 ILE A CA 2348 ATOM 1121 C C A ILE A 2348 132 . 17.808 -1.612 22.736 0.19 14.96 ? ? ? ? ? . 132 ILE A C 2348 ATOM 1122 C C B ILE A 2348 132 . 17.849 -1.630 22.707 0.81 14.54 ? ? ? ? ? . 132 ILE A C 2348 ATOM 1123 O O A ILE A 2348 132 . 18.613 -0.783 22.313 0.19 14.79 ? ? ? ? ? . 132 ILE A O 2348 ATOM 1124 O O B ILE A 2348 132 . 18.686 -0.831 22.296 0.81 13.48 ? ? ? ? ? . 132 ILE A O 2348 ATOM 1125 C CB A ILE A 2348 132 . 15.520 -1.130 23.564 0.19 14.92 ? ? ? ? ? . 132 ILE A CB 2348 ATOM 1126 C CB B ILE A 2348 132 . 15.575 -0.974 23.489 0.81 14.72 ? ? ? ? ? . 132 ILE A CB 2348 ATOM 1127 C CG1 A ILE A 2348 132 . 14.034 -1.319 23.280 0.19 15.02 ? ? ? ? ? . 132 ILE A CG1 2348 ATOM 1128 C CG2 A ILE A 2348 132 . 15.824 0.307 23.942 0.19 14.66 ? ? ? ? ? . 132 ILE A CG2 2348 ATOM 1129 C CG1 B ILE A 2348 132 . 14.149 -0.656 23.059 0.81 15.47 ? ? ? ? ? . 132 ILE A CG1 2348 ATOM 1130 C CG2 B ILE A 2348 132 . 16.235 0.255 24.089 0.81 13.99 ? ? ? ? ? . 132 ILE A CG2 2348 ATOM 1131 C CD1 A ILE A 2348 132 . 13.567 -0.581 22.051 0.19 15.23 ? ? ? ? ? . 132 ILE A CD1 2348 ATOM 1132 C CD1 B ILE A 2348 132 . 13.182 -0.605 24.230 0.81 16.62 ? ? ? ? ? . 132 ILE A CD1 2348 ATOM 1133 N N . GLU A 2348 133 . 18.144 -2.599 23.559 1.00 14.85 ? ? ? ? ? . 133 GLU A N 2348 ATOM 1134 C CA . GLU A 2348 133 . 19.500 -2.725 24.095 1.00 15.86 ? ? ? ? ? . 133 GLU A CA 2348 ATOM 1135 C C . GLU A 2348 133 . 20.510 -3.300 23.114 1.00 15.18 ? ? ? ? ? . 133 GLU A C 2348 ATOM 1136 O O . GLU A 2348 133 . 21.694 -3.025 23.243 1.00 14.71 ? ? ? ? ? . 133 GLU A O 2348 ATOM 1137 C CB . GLU A 2348 133 . 19.516 -3.523 25.385 1.00 18.34 ? ? ? ? ? . 133 GLU A CB 2348 ATOM 1138 C CG . GLU A 2348 133 . 19.099 -4.959 25.269 1.00 21.00 ? ? ? ? ? . 133 GLU A CG 2348 ATOM 1139 C CD . GLU A 2348 133 . 19.009 -5.600 26.628 1.00 24.62 ? ? ? ? ? . 133 GLU A CD 2348 ATOM 1140 O OE1 . GLU A 2348 133 . 17.888 -5.653 27.182 1.00 24.54 ? ? ? ? ? . 133 GLU A OE1 2348 ATOM 1141 O OE2 . GLU A 2348 133 . 20.070 -6.015 27.133 1.00 24.87 ? ? ? ? ? 1- 133 GLU A OE2 2348 ATOM 1142 N N . ASP A 2348 134 . 20.031 -4.102 22.163 1.00 15.80 ? ? ? ? ? . 134 ASP A N 2348 ATOM 1143 C CA . ASP A 2348 134 . 20.885 -4.847 21.228 1.00 16.53 ? ? ? ? ? . 134 ASP A CA 2348 ATOM 1144 C C . ASP A 2348 134 . 20.373 -4.627 19.798 1.00 16.35 ? ? ? ? ? . 134 ASP A C 2348 ATOM 1145 O O . ASP A 2348 134 . 19.922 -5.562 19.131 1.00 16.33 ? ? ? ? ? . 134 ASP A O 2348 ATOM 1146 C CB . ASP A 2348 134 . 20.881 -6.341 21.606 1.00 16.03 ? ? ? ? ? . 134 ASP A CB 2348 ATOM 1147 C CG . ASP A 2348 134 . 21.859 -7.184 20.769 1.00 16.81 ? ? ? ? ? . 134 ASP A CG 2348 ATOM 1148 O OD1 . ASP A 2348 134 . 22.869 -6.642 20.264 1.00 16.39 ? ? ? ? ? . 134 ASP A OD1 2348 ATOM 1149 O OD2 . ASP A 2348 134 . 21.614 -8.404 20.635 1.00 16.25 ? ? ? ? ? 1- 134 ASP A OD2 2348 ATOM 1150 N N . PRO A 2348 135 . 20.451 -3.379 19.309 1.00 15.65 ? ? ? ? ? . 135 PRO A N 2348 ATOM 1151 C CA . PRO A 2348 135 . 19.917 -3.103 17.962 1.00 16.45 ? ? ? ? ? . 135 PRO A CA 2348 ATOM 1152 C C . PRO A 2348 135 . 20.699 -3.798 16.828 1.00 17.49 ? ? ? ? ? . 135 PRO A C 2348 ATOM 1153 O O . PRO A 2348 135 . 20.164 -3.961 15.727 1.00 19.27 ? ? ? ? ? . 135 PRO A O 2348 ATOM 1154 C CB . PRO A 2348 135 . 20.036 -1.580 17.849 1.00 16.15 ? ? ? ? ? . 135 PRO A CB 2348 ATOM 1155 C CG . PRO A 2348 135 . 21.147 -1.228 18.767 1.00 15.72 ? ? ? ? ? . 135 PRO A CG 2348 ATOM 1156 C CD . PRO A 2348 135 . 21.003 -2.165 19.931 1.00 16.34 ? ? ? ? ? . 135 PRO A CD 2348 ATOM 1157 N N . ASP A 2348 136 . 21.943 -4.192 17.089 1.00 18.50 ? ? ? ? ? . 136 ASP A N 2348 ATOM 1158 C CA . ASP A 2348 136 . 22.709 -4.962 16.102 1.00 18.72 ? ? ? ? ? . 136 ASP A CA 2348 ATOM 1159 C C . ASP A 2348 136 . 22.475 -6.472 16.207 1.00 19.15 ? ? ? ? ? . 136 ASP A C 2348 ATOM 1160 O O . ASP A 2348 136 . 23.067 -7.249 15.446 1.00 18.36 ? ? ? ? ? . 136 ASP A O 2348 ATOM 1161 C CB . ASP A 2348 136 . 24.208 -4.659 16.203 1.00 19.68 ? ? ? ? ? . 136 ASP A CB 2348 ATOM 1162 C CG . ASP A 2348 136 . 24.951 -5.002 14.926 1.00 20.65 ? ? ? ? ? . 136 ASP A CG 2348 ATOM 1163 O OD1 . ASP A 2348 136 . 24.302 -4.958 13.849 1.00 19.34 ? ? ? ? ? . 136 ASP A OD1 2348 ATOM 1164 O OD2 . ASP A 2348 136 . 26.167 -5.316 14.990 1.00 18.99 ? ? ? ? ? 1- 136 ASP A OD2 2348 ATOM 1165 N N . GLY A 2348 137 . 21.644 -6.897 17.152 1.00 19.37 ? ? ? ? ? . 137 GLY A N 2348 ATOM 1166 C CA . GLY A 2348 137 . 21.276 -8.295 17.269 1.00 18.65 ? ? ? ? ? . 137 GLY A CA 2348 ATOM 1167 C C . GLY A 2348 137 . 22.434 -9.246 17.520 1.00 18.62 ? ? ? ? ? . 137 GLY A C 2348 ATOM 1168 O O . GLY A 2348 137 . 22.362 -10.405 17.126 1.00 17.20 ? ? ? ? ? . 137 GLY A O 2348 ATOM 1169 N N . ALA A 2348 138 . 23.489 -8.772 18.186 1.00 18.23 ? ? ? ? ? . 138 ALA A N 2348 ATOM 1170 C CA . ALA A 2348 138 . 24.618 -9.638 18.572 1.00 18.91 ? ? ? ? ? . 138 ALA A CA 2348 ATOM 1171 C C . ALA A 2348 138 . 24.172 -10.873 19.359 1.00 18.87 ? ? ? ? ? . 138 ALA A C 2348 ATOM 1172 O O . ALA A 2348 138 . 24.763 -11.937 19.209 1.00 18.45 ? ? ? ? ? . 138 ALA A O 2348 ATOM 1173 C CB . ALA A 2348 138 . 25.646 -8.865 19.388 1.00 19.07 ? ? ? ? ? . 138 ALA A CB 2348 ATOM 1174 N N . ASN A 2348 139 . 23.150 -10.721 20.207 1.00 17.91 ? ? ? ? ? . 139 ASN A N 2348 ATOM 1175 C CA . ASN A 2348 139 . 22.657 -11.826 21.042 1.00 18.78 ? ? ? ? ? . 139 ASN A CA 2348 ATOM 1176 C C . ASN A 2348 139 . 21.320 -12.415 20.575 1.00 18.34 ? ? ? ? ? . 139 ASN A C 2348 ATOM 1177 O O . ASN A 2348 139 . 20.716 -13.222 21.284 1.00 16.63 ? ? ? ? ? . 139 ASN A O 2348 ATOM 1178 C CB . ASN A 2348 139 . 22.558 -11.357 22.493 1.00 20.43 ? ? ? ? ? . 139 ASN A CB 2348 ATOM 1179 C CG . ASN A 2348 139 . 23.907 -11.007 23.077 1.00 22.54 ? ? ? ? ? . 139 ASN A CG 2348 ATOM 1180 N ND2 . ASN A 2348 139 . 24.033 -9.800 23.604 1.00 24.70 ? ? ? ? ? . 139 ASN A ND2 2348 ATOM 1181 O OD1 . ASN A 2348 139 . 24.826 -11.813 23.049 1.00 25.00 ? ? ? ? ? . 139 ASN A OD1 2348 ATOM 1182 N N . PHE A 2348 140 . 20.862 -12.019 19.387 1.00 19.01 ? ? ? ? ? . 140 PHE A N 2348 ATOM 1183 C CA . PHE A 2348 140 . 19.669 -12.603 18.768 1.00 20.41 ? ? ? ? ? . 140 PHE A CA 2348 ATOM 1184 C C . PHE A 2348 140 . 19.812 -14.133 18.747 1.00 20.42 ? ? ? ? ? . 140 PHE A C 2348 ATOM 1185 O O . PHE A 2348 140 . 20.913 -14.633 18.513 1.00 17.90 ? ? ? ? ? . 140 PHE A O 2348 ATOM 1186 C CB . PHE A 2348 140 . 19.522 -12.084 17.327 1.00 21.52 ? ? ? ? ? . 140 PHE A CB 2348 ATOM 1187 C CG . PHE A 2348 140 . 18.452 -12.782 16.532 1.00 22.24 ? ? ? ? ? . 140 PHE A CG 2348 ATOM 1188 C CD1 . PHE A 2348 140 . 18.719 -13.998 15.901 1.00 21.67 ? ? ? ? ? . 140 PHE A CD1 2348 ATOM 1189 C CD2 . PHE A 2348 140 . 17.181 -12.252 16.440 1.00 21.18 ? ? ? ? ? . 140 PHE A CD2 2348 ATOM 1190 C CE1 . PHE A 2348 140 . 17.745 -14.662 15.185 1.00 20.84 ? ? ? ? ? . 140 PHE A CE1 2348 ATOM 1191 C CE2 . PHE A 2348 140 . 16.205 -12.923 15.721 1.00 21.80 ? ? ? ? ? . 140 PHE A CE2 2348 ATOM 1192 C CZ . PHE A 2348 140 . 16.490 -14.121 15.089 1.00 20.62 ? ? ? ? ? . 140 PHE A CZ 2348 ATOM 1193 N N . PRO A 2348 141 . 18.713 -14.878 18.978 1.00 19.68 ? ? ? ? ? . 141 PRO A N 2348 ATOM 1194 C CA . PRO A 2348 141 . 17.322 -14.496 19.270 1.00 20.19 ? ? ? ? ? . 141 PRO A CA 2348 ATOM 1195 C C . PRO A 2348 141 . 17.031 -14.317 20.773 1.00 20.52 ? ? ? ? ? . 141 PRO A C 2348 ATOM 1196 O O . PRO A 2348 141 . 15.896 -14.485 21.219 1.00 20.28 ? ? ? ? ? . 141 PRO A O 2348 ATOM 1197 C CB . PRO A 2348 141 . 16.531 -15.649 18.667 1.00 20.58 ? ? ? ? ? . 141 PRO A CB 2348 ATOM 1198 C CG . PRO A 2348 141 . 17.408 -16.822 18.883 1.00 22.19 ? ? ? ? ? . 141 PRO A CG 2348 ATOM 1199 C CD . PRO A 2348 141 . 18.835 -16.342 18.841 1.00 21.97 ? ? ? ? ? . 141 PRO A CD 2348 ATOM 1200 N N . TRP A 2348 142 . 18.070 -13.962 21.521 1.00 19.76 ? ? ? ? ? . 142 TRP A N 2348 ATOM 1201 C CA . TRP A 2348 142 . 17.983 -13.534 22.901 1.00 21.33 ? ? ? ? ? . 142 TRP A CA 2348 ATOM 1202 C C . TRP A 2348 142 . 17.420 -14.620 23.822 1.00 25.77 ? ? ? ? ? . 142 TRP A C 2348 ATOM 1203 O O . TRP A 2348 142 . 16.345 -14.426 24.421 1.00 25.77 ? ? ? ? ? . 142 TRP A O 2348 ATOM 1204 C CB . TRP A 2348 142 . 17.210 -12.224 23.014 1.00 19.99 ? ? ? ? ? . 142 TRP A CB 2348 ATOM 1205 C CG . TRP A 2348 142 . 17.778 -11.119 22.165 1.00 18.70 ? ? ? ? ? . 142 TRP A CG 2348 ATOM 1206 C CD1 . TRP A 2348 142 . 18.994 -10.522 22.306 1.00 18.19 ? ? ? ? ? . 142 TRP A CD1 2348 ATOM 1207 C CD2 . TRP A 2348 142 . 17.132 -10.461 21.076 1.00 17.96 ? ? ? ? ? . 142 TRP A CD2 2348 ATOM 1208 C CE2 . TRP A 2348 142 . 18.022 -9.480 20.595 1.00 18.04 ? ? ? ? ? . 142 TRP A CE2 2348 ATOM 1209 C CE3 . TRP A 2348 142 . 15.890 -10.610 20.454 1.00 18.59 ? ? ? ? ? . 142 TRP A CE3 2348 ATOM 1210 N NE1 . TRP A 2348 142 . 19.156 -9.555 21.357 1.00 17.87 ? ? ? ? ? . 142 TRP A NE1 2348 ATOM 1211 C CZ2 . TRP A 2348 142 . 17.711 -8.645 19.516 1.00 17.55 ? ? ? ? ? . 142 TRP A CZ2 2348 ATOM 1212 C CZ3 . TRP A 2348 142 . 15.574 -9.787 19.397 1.00 19.05 ? ? ? ? ? . 142 TRP A CZ3 2348 ATOM 1213 C CH2 . TRP A 2348 142 . 16.486 -8.803 18.938 1.00 18.51 ? ? ? ? ? . 142 TRP A CH2 2348 ATOM 1214 N N A PRO A 2348 143 . 18.105 -15.758 23.889 0.43 25.91 ? ? ? ? ? . 143 PRO A N 2348 ATOM 1215 N N B PRO A 2348 143 . 18.145 -15.709 23.950 0.57 28.56 ? ? ? ? ? . 143 PRO A N 2348 ATOM 1216 C CA A PRO A 2348 143 . 17.728 -16.750 24.895 0.43 26.55 ? ? ? ? ? . 143 PRO A CA 2348 ATOM 1217 C CA B PRO A 2348 143 . 17.683 -16.682 24.925 0.57 30.66 ? ? ? ? ? . 143 PRO A CA 2348 ATOM 1218 C C A PRO A 2348 143 . 18.114 -16.109 26.241 0.43 27.90 ? ? ? ? ? . 143 PRO A C 2348 ATOM 1219 C C B PRO A 2348 143 . 18.148 -16.217 26.307 0.57 33.98 ? ? ? ? ? . 143 PRO A C 2348 ATOM 1220 O O A PRO A 2348 143 . 19.033 -15.280 26.295 0.43 29.57 ? ? ? ? ? . 143 PRO A O 2348 ATOM 1221 O O B PRO A 2348 143 . 17.516 -16.577 27.281 0.57 40.90 ? ? ? ? ? . 143 PRO A O 2348 ATOM 1222 C CB A PRO A 2348 143 . 18.662 -17.907 24.589 0.43 26.47 ? ? ? ? ? . 143 PRO A CB 2348 ATOM 1223 C CB B PRO A 2348 143 . 18.464 -17.930 24.540 0.57 31.72 ? ? ? ? ? . 143 PRO A CB 2348 ATOM 1224 C CG A PRO A 2348 143 . 19.869 -17.262 24.025 0.43 27.23 ? ? ? ? ? . 143 PRO A CG 2348 ATOM 1225 C CG B PRO A 2348 143 . 19.714 -17.418 23.925 0.57 32.06 ? ? ? ? ? . 143 PRO A CG 2348 ATOM 1226 C CD A PRO A 2348 143 . 19.399 -16.061 23.265 0.43 26.55 ? ? ? ? ? . 143 PRO A CD 2348 ATOM 1227 C CD B PRO A 2348 143 . 19.334 -16.157 23.214 0.57 30.24 ? ? ? ? ? . 143 PRO A CD 2348 ATOM 1228 N N A ASN A 2348 144 . 17.447 -16.445 27.332 0.43 29.72 ? ? ? ? ? . 144 ASN A N 2348 ATOM 1229 N N B ASN A 2348 144 . 19.154 -15.333 26.349 0.57 43.48 ? ? ? ? ? . 144 ASN A N 2348 ATOM 1230 C CA A ASN A 2348 144 . 17.845 -15.794 28.584 0.43 31.67 ? ? ? ? ? . 144 ASN A CA 2348 ATOM 1231 C CA B ASN A 2348 144 . 19.879 -14.941 27.567 0.57 41.21 ? ? ? ? ? . 144 ASN A CA 2348 ATOM 1232 C C A ASN A 2348 144 . 19.155 -16.376 29.126 0.43 34.18 ? ? ? ? ? . 144 ASN A C 2348 ATOM 1233 C C B ASN A 2348 144 . 19.928 -16.021 28.652 0.57 46.68 ? ? ? ? ? . 144 ASN A C 2348 ATOM 1234 O O A ASN A 2348 144 . 19.292 -16.688 30.295 0.43 37.95 ? ? ? ? ? . 144 ASN A O 2348 ATOM 1235 O O B ASN A 2348 144 . 20.998 -16.385 29.101 0.57 44.85 ? ? ? ? ? . 144 ASN A O 2348 ATOM 1236 C CB A ASN A 2348 144 . 16.725 -15.785 29.643 0.43 31.33 ? ? ? ? ? . 144 ASN A CB 2348 ATOM 1237 C CB B ASN A 2348 144 . 19.766 -13.486 28.103 0.57 37.67 ? ? ? ? ? . 144 ASN A CB 2348 ATOM 1238 C CG A ASN A 2348 144 . 16.683 -14.482 30.437 0.43 30.34 ? ? ? ? ? . 144 ASN A CG 2348 ATOM 1239 C CG B ASN A 2348 144 . 18.456 -12.779 27.779 0.57 32.86 ? ? ? ? ? . 144 ASN A CG 2348 ATOM 1240 N ND2 A ASN A 2348 144 . 15.880 -14.449 31.481 0.43 29.27 ? ? ? ? ? . 144 ASN A ND2 2348 ATOM 1241 O OD1 A ASN A 2348 144 . 17.350 -13.516 30.096 0.43 30.43 ? ? ? ? ? . 144 ASN A OD1 2348 ATOM 1242 N ND2 B ASN A 2348 144 . 18.201 -12.534 26.509 0.57 28.80 ? ? ? ? ? . 144 ASN A ND2 2348 ATOM 1243 O OD1 B ASN A 2348 144 . 17.731 -12.384 28.685 0.57 29.27 ? ? ? ? ? . 144 ASN A OD1 2348 ATOM 1244 O OXT A ASN A 2348 144 . 20.133 -16.520 28.420 0.43 34.42 ? ? ? ? ? 1- 144 ASN A OXT 2348 ATOM 1245 O OXT B ASN A 2348 144 . 18.927 -16.583 29.037 0.57 53.68 ? ? ? ? ? 1- 144 ASN A OXT 2348 ATOM 1247 N N A MET B 2348 1 . -11.706 5.017 56.656 0.43 22.18 ? ? ? ? ? . 1 MET B N 2348 ATOM 1248 N N B MET B 2348 1 . -10.263 6.625 55.038 0.57 23.08 ? ? ? ? ? . 1 MET B N 2348 ATOM 1249 C CA A MET B 2348 1 . -12.271 6.276 56.125 0.43 21.05 ? ? ? ? ? . 1 MET B CA 2348 ATOM 1250 C CA B MET B 2348 1 . -11.550 6.284 55.722 0.57 21.74 ? ? ? ? ? . 1 MET B CA 2348 ATOM 1251 C C A MET B 2348 1 . -12.880 6.055 54.737 0.43 18.63 ? ? ? ? ? . 1 MET B C 2348 ATOM 1252 C C B MET B 2348 1 . -12.611 6.015 54.645 0.57 18.84 ? ? ? ? ? . 1 MET B C 2348 ATOM 1253 O O A MET B 2348 1 . -13.635 6.891 54.262 0.43 17.39 ? ? ? ? ? . 1 MET B O 2348 ATOM 1254 O O B MET B 2348 1 . -13.609 6.729 54.541 0.57 17.32 ? ? ? ? ? . 1 MET B O 2348 ATOM 1255 C CB A MET B 2348 1 . -11.191 7.364 56.082 0.43 23.26 ? ? ? ? ? . 1 MET B CB 2348 ATOM 1256 C CB B MET B 2348 1 . -11.956 7.421 56.682 0.57 22.75 ? ? ? ? ? . 1 MET B CB 2348 ATOM 1257 C CG A MET B 2348 1 . -11.725 8.759 55.817 0.43 24.37 ? ? ? ? ? . 1 MET B CG 2348 ATOM 1258 C CG B MET B 2348 1 . -11.759 8.816 56.094 0.57 25.92 ? ? ? ? ? . 1 MET B CG 2348 ATOM 1259 S SD A MET B 2348 1 . -12.403 9.556 57.288 0.43 28.56 ? ? ? ? ? . 1 MET B SD 2348 ATOM 1260 S SD B MET B 2348 1 . -12.629 10.143 56.953 0.57 32.83 ? ? ? ? ? . 1 MET B SD 2348 ATOM 1261 C CE A MET B 2348 1 . -10.917 10.251 58.005 0.43 26.64 ? ? ? ? ? . 1 MET B CE 2348 ATOM 1262 C CE B MET B 2348 1 . -11.453 10.487 58.263 0.57 31.42 ? ? ? ? ? . 1 MET B CE 2348 ATOM 1263 N N A SER B 2348 2 . -12.566 4.937 54.084 0.43 16.60 ? ? ? ? ? . 2 SER B N 2348 ATOM 1264 N N B SER B 2348 2 . -12.362 4.985 53.835 0.57 16.28 ? ? ? ? ? . 2 SER B N 2348 ATOM 1265 C CA A SER B 2348 2 . -13.172 4.646 52.781 0.43 15.75 ? ? ? ? ? . 2 SER B CA 2348 ATOM 1266 C CA B SER B 2348 2 . -13.169 4.686 52.653 0.57 15.59 ? ? ? ? ? . 2 SER B CA 2348 ATOM 1267 C C A SER B 2348 2 . -13.107 3.179 52.350 0.43 15.40 ? ? ? ? ? . 2 SER B C 2348 ATOM 1268 C C B SER B 2348 2 . -13.096 3.213 52.265 0.57 15.32 ? ? ? ? ? . 2 SER B C 2348 ATOM 1269 O O A SER B 2348 2 . -12.045 2.561 52.401 0.43 14.21 ? ? ? ? ? . 2 SER B O 2348 ATOM 1270 O O B SER B 2348 2 . -12.017 2.623 52.257 0.57 13.61 ? ? ? ? ? . 2 SER B O 2348 ATOM 1271 C CB A SER B 2348 2 . -12.523 5.490 51.687 0.43 15.63 ? ? ? ? ? . 2 SER B CB 2348 ATOM 1272 C CB B SER B 2348 2 . -12.692 5.524 51.467 0.57 15.50 ? ? ? ? ? . 2 SER B CB 2348 ATOM 1273 O OG A SER B 2348 2 . -13.065 5.154 50.418 0.43 15.21 ? ? ? ? ? . 2 SER B OG 2348 ATOM 1274 O OG B SER B 2348 2 . -13.386 5.187 50.274 0.57 14.86 ? ? ? ? ? . 2 SER B OG 2348 ATOM 1275 N N . GLY B 2348 3 . -14.245 2.642 51.902 1.00 14.47 ? ? ? ? ? . 3 GLY B N 2348 ATOM 1276 C CA . GLY B 2348 3 . -14.298 1.314 51.277 1.00 14.80 ? ? ? ? ? . 3 GLY B CA 2348 ATOM 1277 C C . GLY B 2348 3 . -13.580 1.196 49.938 1.00 15.16 ? ? ? ? ? . 3 GLY B C 2348 ATOM 1278 O O . GLY B 2348 3 . -13.220 0.087 49.533 1.00 15.61 ? ? ? ? ? . 3 GLY B O 2348 ATOM 1279 N N . LEU B 2348 4 . -13.361 2.324 49.247 1.00 14.58 ? ? ? ? ? . 4 LEU B N 2348 ATOM 1280 C CA . LEU B 2348 4 . -12.556 2.342 48.006 1.00 15.55 ? ? ? ? ? . 4 LEU B CA 2348 ATOM 1281 C C . LEU B 2348 4 . -11.104 1.921 48.248 1.00 14.48 ? ? ? ? ? . 4 LEU B C 2348 ATOM 1282 O O . LEU B 2348 4 . -10.423 1.450 47.326 1.00 15.12 ? ? ? ? ? . 4 LEU B O 2348 ATOM 1283 C CB . LEU B 2348 4 . -12.567 3.735 47.363 1.00 15.28 ? ? ? ? ? . 4 LEU B CB 2348 ATOM 1284 C CG . LEU B 2348 4 . -13.938 4.254 46.926 1.00 16.58 ? ? ? ? ? . 4 LEU B CG 2348 ATOM 1285 C CD1 . LEU B 2348 4 . -13.856 5.731 46.587 1.00 17.96 ? ? ? ? ? . 4 LEU B CD1 2348 ATOM 1286 C CD2 . LEU B 2348 4 . -14.485 3.440 45.759 1.00 18.60 ? ? ? ? ? . 4 LEU B CD2 2348 ATOM 1287 N N . ALA B 2348 5 . -10.626 2.111 49.479 1.00 14.44 ? ? ? ? ? . 5 ALA B N 2348 ATOM 1288 C CA . ALA B 2348 5 . -9.297 1.636 49.884 1.00 14.79 ? ? ? ? ? . 5 ALA B CA 2348 ATOM 1289 C C . ALA B 2348 5 . -9.128 0.108 49.844 1.00 14.46 ? ? ? ? ? . 5 ALA B C 2348 ATOM 1290 O O . ALA B 2348 5 . -8.012 -0.380 49.926 1.00 14.88 ? ? ? ? ? . 5 ALA B O 2348 ATOM 1291 C CB . ALA B 2348 5 . -8.953 2.150 51.264 1.00 15.63 ? ? ? ? ? . 5 ALA B CB 2348 ATOM 1292 N N . LYS B 2348 6 . -10.227 -0.637 49.760 1.00 14.86 ? ? ? ? ? . 6 LYS B N 2348 ATOM 1293 C CA . LYS B 2348 6 . -10.178 -2.076 49.494 1.00 16.27 ? ? ? ? ? . 6 LYS B CA 2348 ATOM 1294 C C . LYS B 2348 6 . -9.396 -2.367 48.203 1.00 16.76 ? ? ? ? ? . 6 LYS B C 2348 ATOM 1295 O O . LYS B 2348 6 . -8.616 -3.325 48.141 1.00 16.83 ? ? ? ? ? . 6 LYS B O 2348 ATOM 1296 C CB . LYS B 2348 6 . -11.604 -2.645 49.393 1.00 16.82 ? ? ? ? ? . 6 LYS B CB 2348 ATOM 1297 C CG . LYS B 2348 6 . -11.681 -4.156 49.223 1.00 17.15 ? ? ? ? ? . 6 LYS B CG 2348 ATOM 1298 C CD . LYS B 2348 6 . -13.116 -4.635 49.318 1.00 17.25 ? ? ? ? ? . 6 LYS B CD 2348 ATOM 1299 C CE . LYS B 2348 6 . -13.189 -6.150 49.305 1.00 17.66 ? ? ? ? ? . 6 LYS B CE 2348 ATOM 1300 N NZ . LYS B 2348 6 . -14.571 -6.571 49.617 1.00 17.19 ? ? ? ? ? 1+ 6 LYS B NZ 2348 ATOM 1301 N N . TYR B 2348 7 . -9.617 -1.529 47.190 1.00 19.75 ? ? ? ? ? . 7 TYR B N 2348 ATOM 1302 C CA . TYR B 2348 7 . -9.014 -1.687 45.856 1.00 21.36 ? ? ? ? ? . 7 TYR B CA 2348 ATOM 1303 C C . TYR B 2348 7 . -7.965 -0.642 45.491 1.00 21.83 ? ? ? ? ? . 7 TYR B C 2348 ATOM 1304 O O . TYR B 2348 7 . -7.142 -0.868 44.582 1.00 23.46 ? ? ? ? ? . 7 TYR B O 2348 ATOM 1305 C CB . TYR B 2348 7 . -10.127 -1.690 44.823 1.00 23.09 ? ? ? ? ? . 7 TYR B CB 2348 ATOM 1306 C CG . TYR B 2348 7 . -11.029 -2.868 45.004 1.00 24.75 ? ? ? ? ? . 7 TYR B CG 2348 ATOM 1307 C CD1 . TYR B 2348 7 . -10.552 -4.151 44.794 1.00 24.42 ? ? ? ? ? . 7 TYR B CD1 2348 ATOM 1308 C CD2 . TYR B 2348 7 . -12.353 -2.714 45.400 1.00 27.18 ? ? ? ? ? . 7 TYR B CD2 2348 ATOM 1309 C CE1 . TYR B 2348 7 . -11.363 -5.257 44.967 1.00 27.58 ? ? ? ? ? . 7 TYR B CE1 2348 ATOM 1310 C CE2 . TYR B 2348 7 . -13.172 -3.816 45.574 1.00 27.12 ? ? ? ? ? . 7 TYR B CE2 2348 ATOM 1311 C CZ . TYR B 2348 7 . -12.674 -5.083 45.353 1.00 29.00 ? ? ? ? ? . 7 TYR B CZ 2348 ATOM 1312 O OH . TYR B 2348 7 . -13.474 -6.184 45.532 1.00 31.06 ? ? ? ? ? . 7 TYR B OH 2348 ATOM 1313 N N . LEU B 2348 8 . -7.988 0.490 46.190 1.00 20.58 ? ? ? ? ? . 8 LEU B N 2348 ATOM 1314 C CA . LEU B 2348 8 . -6.995 1.534 46.034 1.00 22.55 ? ? ? ? ? . 8 LEU B CA 2348 ATOM 1315 C C . LEU B 2348 8 . -6.258 1.733 47.379 1.00 24.85 ? ? ? ? ? . 8 LEU B C 2348 ATOM 1316 O O . LEU B 2348 8 . -6.306 2.818 47.947 1.00 23.30 ? ? ? ? ? . 8 LEU B O 2348 ATOM 1317 C CB . LEU B 2348 8 . -7.674 2.820 45.535 1.00 21.81 ? ? ? ? ? . 8 LEU B CB 2348 ATOM 1318 C CG . LEU B 2348 8 . -8.652 2.723 44.351 1.00 22.20 ? ? ? ? ? . 8 LEU B CG 2348 ATOM 1319 C CD1 . LEU B 2348 8 . -9.436 4.019 44.145 1.00 21.75 ? ? ? ? ? . 8 LEU B CD1 2348 ATOM 1320 C CD2 . LEU B 2348 8 . -7.923 2.341 43.078 1.00 23.03 ? ? ? ? ? . 8 LEU B CD2 2348 ATOM 1321 N N . PRO B 2348 9 . -5.585 0.670 47.908 1.00 30.34 ? ? ? ? ? . 9 PRO B N 2348 ATOM 1322 C CA . PRO B 2348 9 . -4.840 0.839 49.177 1.00 32.73 ? ? ? ? ? . 9 PRO B CA 2348 ATOM 1323 C C . PRO B 2348 9 . -3.645 1.806 49.120 1.00 36.29 ? ? ? ? ? . 9 PRO B C 2348 ATOM 1324 O O . PRO B 2348 9 . -3.262 2.365 50.164 1.00 40.31 ? ? ? ? ? . 9 PRO B O 2348 ATOM 1325 C CB . PRO B 2348 9 . -4.339 -0.580 49.490 1.00 31.95 ? ? ? ? ? . 9 PRO B CB 2348 ATOM 1326 C CG . PRO B 2348 9 . -4.271 -1.254 48.169 1.00 31.95 ? ? ? ? ? . 9 PRO B CG 2348 ATOM 1327 C CD . PRO B 2348 9 . -5.444 -0.710 47.397 1.00 29.49 ? ? ? ? ? . 9 PRO B CD 2348 ATOM 1328 N N A GLY B 2348 10 . -3.058 1.957 47.930 0.77 38.24 ? ? ? ? ? . 10 GLY B N 2348 ATOM 1329 N N B GLY B 2348 10 . -3.067 1.997 47.933 0.23 34.42 ? ? ? ? ? . 10 GLY B N 2348 ATOM 1330 C CA A GLY B 2348 10 . -1.979 2.917 47.683 0.77 39.23 ? ? ? ? ? . 10 GLY B CA 2348 ATOM 1331 C CA B GLY B 2348 10 . -1.975 2.950 47.737 0.23 32.92 ? ? ? ? ? . 10 GLY B CA 2348 ATOM 1332 C C A GLY B 2348 10 . -2.440 4.297 47.238 0.77 39.23 ? ? ? ? ? . 10 GLY B C 2348 ATOM 1333 C C B GLY B 2348 10 . -2.466 4.376 47.572 0.23 31.25 ? ? ? ? ? . 10 GLY B C 2348 ATOM 1334 O O A GLY B 2348 10 . -1.600 5.153 46.952 0.77 39.50 ? ? ? ? ? . 10 GLY B O 2348 ATOM 1335 O O B GLY B 2348 10 . -1.769 5.323 47.932 0.23 30.40 ? ? ? ? ? . 10 GLY B O 2348 ATOM 1336 N N A ALA B 2348 11 . -3.757 4.512 47.157 0.77 38.23 ? ? ? ? ? . 11 ALA B N 2348 ATOM 1337 N N B ALA B 2348 11 . -3.671 4.530 47.029 0.23 30.15 ? ? ? ? ? . 11 ALA B N 2348 ATOM 1338 C CA A ALA B 2348 11 . -4.326 5.822 46.813 0.77 40.95 ? ? ? ? ? . 11 ALA B CA 2348 ATOM 1339 C CA B ALA B 2348 11 . -4.203 5.852 46.697 0.23 29.99 ? ? ? ? ? . 11 ALA B CA 2348 ATOM 1340 C C A ALA B 2348 11 . -4.804 6.550 48.057 0.77 42.60 ? ? ? ? ? . 11 ALA B C 2348 ATOM 1341 C C B ALA B 2348 11 . -4.673 6.627 47.920 0.23 29.56 ? ? ? ? ? . 11 ALA B C 2348 ATOM 1342 O O A ALA B 2348 11 . -5.473 5.956 48.913 0.77 38.62 ? ? ? ? ? . 11 ALA B O 2348 ATOM 1343 O O B ALA B 2348 11 . -4.896 6.055 48.992 0.23 29.66 ? ? ? ? ? . 11 ALA B O 2348 ATOM 1344 C CB A ALA B 2348 11 . -5.484 5.674 45.843 0.77 39.60 ? ? ? ? ? . 11 ALA B CB 2348 ATOM 1345 C CB B ALA B 2348 11 . -5.346 5.725 45.701 0.23 29.66 ? ? ? ? ? . 11 ALA B CB 2348 ATOM 1346 N N A THR B 2348 12 . -4.465 7.837 48.124 0.77 39.49 ? ? ? ? ? . 12 THR B N 2348 ATOM 1347 N N B THR B 2348 12 . -4.834 7.935 47.739 0.23 27.19 ? ? ? ? ? . 12 THR B N 2348 ATOM 1348 C CA A THR B 2348 12 . -4.919 8.740 49.169 0.77 38.81 ? ? ? ? ? . 12 THR B CA 2348 ATOM 1349 C CA B THR B 2348 12 . -5.309 8.803 48.802 0.23 25.87 ? ? ? ? ? . 12 THR B CA 2348 ATOM 1350 C C A THR B 2348 12 . -5.822 9.788 48.516 0.77 36.92 ? ? ? ? ? . 12 THR B C 2348 ATOM 1351 C C B THR B 2348 12 . -6.085 9.992 48.240 0.23 24.45 ? ? ? ? ? . 12 THR B C 2348 ATOM 1352 O O A THR B 2348 12 . -7.019 9.833 48.805 0.77 38.96 ? ? ? ? ? . 12 THR B O 2348 ATOM 1353 O O B THR B 2348 12 . -7.280 10.134 48.496 0.23 24.79 ? ? ? ? ? . 12 THR B O 2348 ATOM 1354 C CB A THR B 2348 12 . -3.715 9.350 49.932 0.77 43.31 ? ? ? ? ? . 12 THR B CB 2348 ATOM 1355 C CB B THR B 2348 12 . -4.146 9.331 49.661 0.23 25.76 ? ? ? ? ? . 12 THR B CB 2348 ATOM 1356 C CG2 A THR B 2348 12 . -4.034 10.710 50.580 0.77 44.76 ? ? ? ? ? . 12 THR B CG2 2348 ATOM 1357 O OG1 A THR B 2348 12 . -3.305 8.441 50.966 0.77 48.33 ? ? ? ? ? . 12 THR B OG1 2348 ATOM 1358 C CG2 B THR B 2348 12 . -3.507 8.198 50.450 0.23 26.96 ? ? ? ? ? . 12 THR B CG2 2348 ATOM 1359 O OG1 B THR B 2348 12 . -3.157 9.935 48.817 0.23 25.88 ? ? ? ? ? . 12 THR B OG1 2348 ATOM 1360 N N A ASN B 2348 13 . -5.262 10.611 47.633 0.77 31.56 ? ? ? ? ? . 13 ASN B N 2348 ATOM 1361 N N B ASN B 2348 13 . -5.412 10.841 47.470 0.23 22.85 ? ? ? ? ? . 13 ASN B N 2348 ATOM 1362 C CA A ASN B 2348 13 . -6.027 11.685 46.991 0.77 30.90 ? ? ? ? ? . 13 ASN B CA 2348 ATOM 1363 C CA B ASN B 2348 13 . -6.025 12.088 47.015 0.23 22.03 ? ? ? ? ? . 13 ASN B CA 2348 ATOM 1364 C C A ASN B 2348 13 . -6.517 11.306 45.593 0.77 26.89 ? ? ? ? ? . 13 ASN B C 2348 ATOM 1365 C C B ASN B 2348 13 . -6.297 12.126 45.512 0.23 20.53 ? ? ? ? ? . 13 ASN B C 2348 ATOM 1366 O O A ASN B 2348 13 . -5.977 10.403 44.946 0.77 27.86 ? ? ? ? ? . 13 ASN B O 2348 ATOM 1367 O O B ASN B 2348 13 . -5.403 12.391 44.707 0.23 18.91 ? ? ? ? ? . 13 ASN B O 2348 ATOM 1368 C CB A ASN B 2348 13 . -5.201 12.975 46.924 0.77 32.33 ? ? ? ? ? . 13 ASN B CB 2348 ATOM 1369 C CB B ASN B 2348 13 . -5.158 13.276 47.425 0.23 22.65 ? ? ? ? ? . 13 ASN B CB 2348 ATOM 1370 C CG A ASN B 2348 13 . -5.018 13.624 48.287 0.77 33.72 ? ? ? ? ? . 13 ASN B CG 2348 ATOM 1371 C CG B ASN B 2348 13 . -5.104 13.456 48.927 0.23 22.73 ? ? ? ? ? . 13 ASN B CG 2348 ATOM 1372 N ND2 A ASN B 2348 13 . -3.789 14.040 48.583 0.77 32.95 ? ? ? ? ? . 13 ASN B ND2 2348 ATOM 1373 O OD1 A ASN B 2348 13 . -5.972 13.755 49.064 0.77 36.48 ? ? ? ? ? . 13 ASN B OD1 2348 ATOM 1374 N ND2 B ASN B 2348 13 . -3.898 13.564 49.467 0.23 22.84 ? ? ? ? ? . 13 ASN B ND2 2348 ATOM 1375 O OD1 B ASN B 2348 13 . -6.139 13.488 49.597 0.23 23.02 ? ? ? ? ? . 13 ASN B OD1 2348 ATOM 1376 N N A LEU B 2348 14 . -7.561 12.004 45.156 0.77 22.05 ? ? ? ? ? . 14 LEU B N 2348 ATOM 1377 N N B LEU B 2348 14 . -7.552 11.874 45.153 0.23 19.29 ? ? ? ? ? . 14 LEU B N 2348 ATOM 1378 C CA A LEU B 2348 14 . -8.025 11.956 43.783 0.77 19.30 ? ? ? ? ? . 14 LEU B CA 2348 ATOM 1379 C CA B LEU B 2348 14 . -7.976 11.910 43.764 0.23 18.51 ? ? ? ? ? . 14 LEU B CA 2348 ATOM 1380 C C A LEU B 2348 14 . -7.920 13.356 43.196 0.77 18.33 ? ? ? ? ? . 14 LEU B C 2348 ATOM 1381 C C B LEU B 2348 14 . -7.877 13.327 43.209 0.23 18.03 ? ? ? ? ? . 14 LEU B C 2348 ATOM 1382 O O A LEU B 2348 14 . -8.134 14.353 43.895 0.77 18.60 ? ? ? ? ? . 14 LEU B O 2348 ATOM 1383 O O B LEU B 2348 14 . -8.049 14.300 43.943 0.23 18.30 ? ? ? ? ? . 14 LEU B O 2348 ATOM 1384 C CB A LEU B 2348 14 . -9.469 11.484 43.723 0.77 19.92 ? ? ? ? ? . 14 LEU B CB 2348 ATOM 1385 C CB B LEU B 2348 14 . -9.417 11.422 43.639 0.23 18.83 ? ? ? ? ? . 14 LEU B CB 2348 ATOM 1386 C CG A LEU B 2348 14 . -9.749 10.069 44.232 0.77 19.69 ? ? ? ? ? . 14 LEU B CG 2348 ATOM 1387 C CG B LEU B 2348 14 . -9.712 10.028 44.194 0.23 18.81 ? ? ? ? ? . 14 LEU B CG 2348 ATOM 1388 C CD1 A LEU B 2348 14 . -11.252 9.842 44.242 0.77 21.45 ? ? ? ? ? . 14 LEU B CD1 2348 ATOM 1389 C CD2 A LEU B 2348 14 . -9.054 9.028 43.375 0.77 17.90 ? ? ? ? ? . 14 LEU B CD2 2348 ATOM 1390 C CD1 B LEU B 2348 14 . -11.209 9.763 44.163 0.23 19.36 ? ? ? ? ? . 14 LEU B CD1 2348 ATOM 1391 C CD2 B LEU B 2348 14 . -8.959 8.967 43.412 0.23 18.31 ? ? ? ? ? . 14 LEU B CD2 2348 ATOM 1392 N N . LEU B 2348 15 . -7.599 13.428 41.911 1.00 17.26 ? ? ? ? ? . 15 LEU B N 2348 ATOM 1393 C CA . LEU B 2348 15 . -7.617 14.696 41.206 1.00 17.59 ? ? ? ? ? . 15 LEU B CA 2348 ATOM 1394 C C . LEU B 2348 15 . -9.072 15.103 41.062 1.00 16.76 ? ? ? ? ? . 15 LEU B C 2348 ATOM 1395 O O . LEU B 2348 15 . -9.936 14.262 40.835 1.00 16.90 ? ? ? ? ? . 15 LEU B O 2348 ATOM 1396 C CB . LEU B 2348 15 . -7.025 14.573 39.813 1.00 19.34 ? ? ? ? ? . 15 LEU B CB 2348 ATOM 1397 C CG . LEU B 2348 15 . -5.610 14.033 39.700 1.00 21.37 ? ? ? ? ? . 15 LEU B CG 2348 ATOM 1398 C CD1 . LEU B 2348 15 . -5.159 14.206 38.257 1.00 21.66 ? ? ? ? ? . 15 LEU B CD1 2348 ATOM 1399 C CD2 . LEU B 2348 15 . -4.668 14.726 40.666 1.00 24.43 ? ? ? ? ? . 15 LEU B CD2 2348 ATOM 1400 N N . SER B 2348 16 . -9.331 16.391 41.209 1.00 17.94 ? ? ? ? ? . 16 SER B N 2348 ATOM 1401 C CA . SER B 2348 16 . -10.680 16.929 41.064 1.00 18.12 ? ? ? ? ? . 16 SER B CA 2348 ATOM 1402 C C . SER B 2348 16 . -10.613 18.305 40.430 1.00 16.87 ? ? ? ? ? . 16 SER B C 2348 ATOM 1403 O O . SER B 2348 16 . -9.533 18.879 40.272 1.00 17.19 ? ? ? ? ? . 16 SER B O 2348 ATOM 1404 C CB . SER B 2348 16 . -11.370 17.023 42.422 1.00 19.13 ? ? ? ? ? . 16 SER B CB 2348 ATOM 1405 O OG . SER B 2348 16 . -10.823 18.059 43.187 1.00 22.41 ? ? ? ? ? . 16 SER B OG 2348 ATOM 1406 N N . LYS B 2348 17 . -11.782 18.828 40.086 1.00 15.53 ? ? ? ? ? . 17 LYS B N 2348 ATOM 1407 C CA . LYS B 2348 17 . -11.903 20.175 39.539 1.00 16.49 ? ? ? ? ? . 17 LYS B CA 2348 ATOM 1408 C C . LYS B 2348 17 . -11.794 21.268 40.598 1.00 15.39 ? ? ? ? ? . 17 LYS B C 2348 ATOM 1409 O O . LYS B 2348 17 . -11.669 22.438 40.252 1.00 13.92 ? ? ? ? ? . 17 LYS B O 2348 ATOM 1410 C CB . LYS B 2348 17 . -13.215 20.305 38.757 1.00 18.01 ? ? ? ? ? . 17 LYS B CB 2348 ATOM 1411 C CG . LYS B 2348 17 . -13.335 19.299 37.622 1.00 19.88 ? ? ? ? ? . 17 LYS B CG 2348 ATOM 1412 C CD . LYS B 2348 17 . -12.060 19.234 36.794 1.00 21.42 ? ? ? ? ? . 17 LYS B CD 2348 ATOM 1413 C CE . LYS B 2348 17 . -12.221 18.350 35.596 1.00 22.48 ? ? ? ? ? . 17 LYS B CE 2348 ATOM 1414 N NZ . LYS B 2348 17 . -11.123 18.520 34.616 1.00 19.77 ? ? ? ? ? 1+ 17 LYS B NZ 2348 ATOM 1415 N N . SER B 2348 18 . -11.851 20.881 41.874 1.00 15.35 ? ? ? ? ? . 18 SER B N 2348 ATOM 1416 C CA . SER B 2348 18 . -11.747 21.801 43.005 1.00 16.54 ? ? ? ? ? . 18 SER B CA 2348 ATOM 1417 C C . SER B 2348 18 . -10.391 21.703 43.686 1.00 17.70 ? ? ? ? ? . 18 SER B C 2348 ATOM 1418 O O . SER B 2348 18 . -10.142 22.414 44.649 1.00 19.21 ? ? ? ? ? . 18 SER B O 2348 ATOM 1419 C CB . SER B 2348 18 . -12.863 21.496 44.015 1.00 17.01 ? ? ? ? ? . 18 SER B CB 2348 ATOM 1420 O OG . SER B 2348 18 . -12.878 20.104 44.333 1.00 19.03 ? ? ? ? ? . 18 SER B OG 2348 ATOM 1421 N N . GLY B 2348 19 . -9.511 20.850 43.167 1.00 20.26 ? ? ? ? ? . 19 GLY B N 2348 ATOM 1422 C CA . GLY B 2348 19 . -8.183 20.625 43.734 1.00 23.91 ? ? ? ? ? . 19 GLY B CA 2348 ATOM 1423 C C . GLY B 2348 19 . -7.970 19.137 43.899 1.00 29.48 ? ? ? ? ? . 19 GLY B C 2348 ATOM 1424 O O . GLY B 2348 19 . -7.881 18.400 42.908 1.00 35.30 ? ? ? ? ? . 19 GLY B O 2348 ATOM 1425 N N . GLU B 2348 20 . -7.904 18.693 45.150 1.00 33.35 ? ? ? ? ? . 20 GLU B N 2348 ATOM 1426 C CA . GLU B 2348 20 . -7.828 17.270 45.476 1.00 34.73 ? ? ? ? ? . 20 GLU B CA 2348 ATOM 1427 C C . GLU B 2348 20 . -9.006 16.904 46.383 1.00 32.98 ? ? ? ? ? . 20 GLU B C 2348 ATOM 1428 O O . GLU B 2348 20 . -9.526 17.757 47.117 1.00 31.53 ? ? ? ? ? . 20 GLU B O 2348 ATOM 1429 C CB . GLU B 2348 20 . -6.491 16.945 46.160 1.00 42.13 ? ? ? ? ? . 20 GLU B CB 2348 ATOM 1430 C CG . GLU B 2348 20 . -5.367 16.492 45.220 1.00 47.38 ? ? ? ? ? . 20 GLU B CG 2348 ATOM 1431 C CD . GLU B 2348 20 . -4.580 17.617 44.549 1.00 54.02 ? ? ? ? ? . 20 GLU B CD 2348 ATOM 1432 O OE1 . GLU B 2348 20 . -4.618 18.780 45.019 1.00 57.55 ? ? ? ? ? . 20 GLU B OE1 2348 ATOM 1433 O OE2 . GLU B 2348 20 . -3.893 17.325 43.539 1.00 54.84 ? ? ? ? ? 1- 20 GLU B OE2 2348 ATOM 1434 N N . VAL B 2348 21 . -9.449 15.651 46.305 1.00 27.54 ? ? ? ? ? . 21 VAL B N 2348 ATOM 1435 C CA . VAL B 2348 21 . -10.457 15.135 47.231 1.00 23.77 ? ? ? ? ? . 21 VAL B CA 2348 ATOM 1436 C C . VAL B 2348 21 . -9.976 13.792 47.753 1.00 21.10 ? ? ? ? ? . 21 VAL B C 2348 ATOM 1437 O O . VAL B 2348 21 . -9.420 12.984 47.009 1.00 22.82 ? ? ? ? ? . 21 VAL B O 2348 ATOM 1438 C CB . VAL B 2348 21 . -11.882 15.041 46.615 1.00 25.46 ? ? ? ? ? . 21 VAL B CB 2348 ATOM 1439 C CG1 . VAL B 2348 21 . -12.259 16.337 45.908 1.00 26.17 ? ? ? ? ? . 21 VAL B CG1 2348 ATOM 1440 C CG2 . VAL B 2348 21 . -12.032 13.874 45.654 1.00 27.50 ? ? ? ? ? . 21 VAL B CG2 2348 ATOM 1441 N N . SER B 2348 22 . -10.156 13.584 49.049 1.00 19.01 ? ? ? ? ? . 22 SER B N 2348 ATOM 1442 C CA . SER B 2348 22 . -9.832 12.319 49.690 1.00 17.12 ? ? ? ? ? . 22 SER B CA 2348 ATOM 1443 C C . SER B 2348 22 . -10.837 11.257 49.280 1.00 16.89 ? ? ? ? ? . 22 SER B C 2348 ATOM 1444 O O . SER B 2348 22 . -11.969 11.559 48.900 1.00 16.17 ? ? ? ? ? . 22 SER B O 2348 ATOM 1445 C CB . SER B 2348 22 . -9.882 12.477 51.201 1.00 17.47 ? ? ? ? ? . 22 SER B CB 2348 ATOM 1446 O OG . SER B 2348 22 . -11.186 12.875 51.610 1.00 18.10 ? ? ? ? ? . 22 SER B OG 2348 ATOM 1447 N N . LEU B 2348 23 . -10.439 10.000 49.383 1.00 16.00 ? ? ? ? ? . 23 LEU B N 2348 ATOM 1448 C CA . LEU B 2348 23 . -11.392 8.910 49.209 1.00 16.76 ? ? ? ? ? . 23 LEU B CA 2348 ATOM 1449 C C . LEU B 2348 23 . -12.551 9.038 50.208 1.00 14.79 ? ? ? ? ? . 23 LEU B C 2348 ATOM 1450 O O . LEU B 2348 23 . -13.717 8.880 49.845 1.00 15.73 ? ? ? ? ? . 23 LEU B O 2348 ATOM 1451 C CB . LEU B 2348 23 . -10.689 7.563 49.369 1.00 17.74 ? ? ? ? ? . 23 LEU B CB 2348 ATOM 1452 C CG . LEU B 2348 23 . -9.584 7.244 48.339 1.00 17.52 ? ? ? ? ? . 23 LEU B CG 2348 ATOM 1453 C CD1 . LEU B 2348 23 . -9.084 5.812 48.539 1.00 18.55 ? ? ? ? ? . 23 LEU B CD1 2348 ATOM 1454 C CD2 . LEU B 2348 23 . -10.077 7.420 46.929 1.00 19.15 ? ? ? ? ? . 23 LEU B CD2 2348 ATOM 1455 N N . GLY B 2348 24 . -12.223 9.375 51.449 1.00 14.46 ? ? ? ? ? . 24 GLY B N 2348 ATOM 1456 C CA . GLY B 2348 24 . -13.214 9.637 52.492 1.00 14.61 ? ? ? ? ? . 24 GLY B CA 2348 ATOM 1457 C C . GLY B 2348 24 . -14.315 10.639 52.178 1.00 14.98 ? ? ? ? ? . 24 GLY B C 2348 ATOM 1458 O O . GLY B 2348 24 . -15.447 10.508 52.685 1.00 13.90 ? ? ? ? ? . 24 GLY B O 2348 ATOM 1459 N N A SER B 2348 25 . -14.002 11.639 51.359 0.33 14.74 ? ? ? ? ? . 25 SER B N 2348 ATOM 1460 N N B SER B 2348 25 . -13.985 11.632 51.354 0.67 14.83 ? ? ? ? ? . 25 SER B N 2348 ATOM 1461 C CA A SER B 2348 25 . -14.990 12.634 50.953 0.33 15.11 ? ? ? ? ? . 25 SER B CA 2348 ATOM 1462 C CA B SER B 2348 25 . -14.956 12.633 50.907 0.67 15.70 ? ? ? ? ? . 25 SER B CA 2348 ATOM 1463 C C A SER B 2348 25 . -16.139 12.061 50.107 0.33 14.62 ? ? ? ? ? . 25 SER B C 2348 ATOM 1464 C C B SER B 2348 25 . -16.142 12.045 50.133 0.67 14.69 ? ? ? ? ? . 25 SER B C 2348 ATOM 1465 O O A SER B 2348 25 . -17.161 12.727 49.940 0.33 14.68 ? ? ? ? ? . 25 SER B O 2348 ATOM 1466 O O B SER B 2348 25 . -17.192 12.679 50.049 0.67 14.89 ? ? ? ? ? . 25 SER B O 2348 ATOM 1467 C CB A SER B 2348 25 . -14.312 13.771 50.192 0.33 15.75 ? ? ? ? ? . 25 SER B CB 2348 ATOM 1468 C CB B SER B 2348 25 . -14.277 13.710 50.050 0.67 17.08 ? ? ? ? ? . 25 SER B CB 2348 ATOM 1469 O OG A SER B 2348 25 . -13.934 13.355 48.898 0.33 15.76 ? ? ? ? ? . 25 SER B OG 2348 ATOM 1470 O OG B SER B 2348 25 . -13.378 14.486 50.832 0.67 17.83 ? ? ? ? ? . 25 SER B OG 2348 ATOM 1471 N N . LEU B 2348 26 . -15.971 10.843 49.583 1.00 14.64 ? ? ? ? ? . 26 LEU B N 2348 ATOM 1472 C CA . LEU B 2348 26 . -17.013 10.154 48.810 1.00 14.28 ? ? ? ? ? . 26 LEU B CA 2348 ATOM 1473 C C . LEU B 2348 26 . -17.907 9.246 49.653 1.00 13.59 ? ? ? ? ? . 26 LEU B C 2348 ATOM 1474 O O . LEU B 2348 26 . -18.662 8.454 49.099 1.00 13.08 ? ? ? ? ? . 26 LEU B O 2348 ATOM 1475 C CB . LEU B 2348 26 . -16.349 9.345 47.686 1.00 14.88 ? ? ? ? ? . 26 LEU B CB 2348 ATOM 1476 C CG . LEU B 2348 26 . -15.426 10.153 46.765 1.00 15.17 ? ? ? ? ? . 26 LEU B CG 2348 ATOM 1477 C CD1 . LEU B 2348 26 . -14.967 9.289 45.614 1.00 17.04 ? ? ? ? ? . 26 LEU B CD1 2348 ATOM 1478 C CD2 . LEU B 2348 26 . -16.139 11.406 46.266 1.00 16.62 ? ? ? ? ? . 26 LEU B CD2 2348 ATOM 1479 N N . VAL B 2348 27 . -17.834 9.368 50.978 1.00 14.28 ? ? ? ? ? . 27 VAL B N 2348 ATOM 1480 C CA . VAL B 2348 27 . -18.698 8.635 51.891 1.00 15.50 ? ? ? ? ? . 27 VAL B CA 2348 ATOM 1481 C C . VAL B 2348 27 . -20.162 8.724 51.441 1.00 15.84 ? ? ? ? ? . 27 VAL B C 2348 ATOM 1482 O O . VAL B 2348 27 . -20.649 9.800 51.054 1.00 14.49 ? ? ? ? ? . 27 VAL B O 2348 ATOM 1483 C CB . VAL B 2348 27 . -18.547 9.163 53.351 1.00 16.29 ? ? ? ? ? . 27 VAL B CB 2348 ATOM 1484 C CG1 . VAL B 2348 27 . -18.972 10.632 53.485 1.00 15.80 ? ? ? ? ? . 27 VAL B CG1 2348 ATOM 1485 C CG2 . VAL B 2348 27 . -19.296 8.283 54.345 1.00 16.28 ? ? ? ? ? . 27 VAL B CG2 2348 ATOM 1486 N N . GLY B 2348 28 . -20.824 7.572 51.443 1.00 15.56 ? ? ? ? ? . 28 GLY B N 2348 ATOM 1487 C CA . GLY B 2348 28 . -22.236 7.472 51.117 1.00 17.43 ? ? ? ? ? . 28 GLY B CA 2348 ATOM 1488 C C . GLY B 2348 28 . -22.560 7.471 49.633 1.00 17.56 ? ? ? ? ? . 28 GLY B C 2348 ATOM 1489 O O . GLY B 2348 28 . -23.721 7.312 49.289 1.00 16.53 ? ? ? ? ? . 28 GLY B O 2348 ATOM 1490 N N . LYS B 2348 29 . -21.558 7.614 48.749 1.00 18.00 ? ? ? ? ? . 29 LYS B N 2348 ATOM 1491 C CA A LYS B 2348 29 . -21.810 7.728 47.306 0.68 17.72 ? ? ? ? ? . 29 LYS B CA 2348 ATOM 1492 C CA B LYS B 2348 29 . -21.809 7.727 47.308 0.32 17.27 ? ? ? ? ? . 29 LYS B CA 2348 ATOM 1493 C C . LYS B 2348 29 . -21.633 6.400 46.590 1.00 17.35 ? ? ? ? ? . 29 LYS B C 2348 ATOM 1494 O O . LYS B 2348 29 . -21.001 5.464 47.114 1.00 16.43 ? ? ? ? ? . 29 LYS B O 2348 ATOM 1495 C CB A LYS B 2348 29 . -20.896 8.779 46.665 0.68 18.98 ? ? ? ? ? . 29 LYS B CB 2348 ATOM 1496 C CB B LYS B 2348 29 . -20.890 8.777 46.675 0.32 17.40 ? ? ? ? ? . 29 LYS B CB 2348 ATOM 1497 C CG A LYS B 2348 29 . -21.075 10.175 47.237 0.68 20.34 ? ? ? ? ? . 29 LYS B CG 2348 ATOM 1498 C CG B LYS B 2348 29 . -21.159 10.185 47.167 0.32 17.58 ? ? ? ? ? . 29 LYS B CG 2348 ATOM 1499 C CD A LYS B 2348 29 . -20.626 11.246 46.260 0.68 21.02 ? ? ? ? ? . 29 LYS B CD 2348 ATOM 1500 C CD B LYS B 2348 29 . -20.246 11.205 46.514 0.32 17.42 ? ? ? ? ? . 29 LYS B CD 2348 ATOM 1501 C CE A LYS B 2348 29 . -20.516 12.609 46.928 0.68 21.70 ? ? ? ? ? . 29 LYS B CE 2348 ATOM 1502 C CE B LYS B 2348 29 . -20.670 12.621 46.874 0.32 17.47 ? ? ? ? ? . 29 LYS B CE 2348 ATOM 1503 N NZ A LYS B 2348 29 . -21.730 13.052 47.665 0.68 19.96 ? ? ? ? ? 1+ 29 LYS B NZ 2348 ATOM 1504 N NZ B LYS B 2348 29 . -21.930 13.032 46.203 0.32 16.73 ? ? ? ? ? 1+ 29 LYS B NZ 2348 ATOM 1505 N N . THR B 2348 30 . -22.222 6.329 45.404 1.00 16.11 ? ? ? ? ? . 30 THR B N 2348 ATOM 1506 C CA . THR B 2348 30 . -21.922 5.287 44.433 1.00 16.62 ? ? ? ? ? . 30 THR B CA 2348 ATOM 1507 C C . THR B 2348 30 . -20.765 5.868 43.640 1.00 16.77 ? ? ? ? ? . 30 THR B C 2348 ATOM 1508 O O . THR B 2348 30 . -20.761 7.061 43.352 1.00 15.79 ? ? ? ? ? . 30 THR B O 2348 ATOM 1509 C CB . THR B 2348 30 . -23.134 4.990 43.527 1.00 16.40 ? ? ? ? ? . 30 THR B CB 2348 ATOM 1510 C CG2 . THR B 2348 30 . -22.788 3.993 42.435 1.00 17.05 ? ? ? ? ? . 30 THR B CG2 2348 ATOM 1511 O OG1 . THR B 2348 30 . -24.174 4.432 44.329 1.00 16.31 ? ? ? ? ? . 30 THR B OG1 2348 ATOM 1512 N N . VAL B 2348 31 . -19.755 5.048 43.335 1.00 16.50 ? ? ? ? ? . 31 VAL B N 2348 ATOM 1513 C CA . VAL B 2348 31 . -18.612 5.519 42.588 1.00 16.20 ? ? ? ? ? . 31 VAL B CA 2348 ATOM 1514 C C . VAL B 2348 31 . -18.434 4.641 41.355 1.00 16.54 ? ? ? ? ? . 31 VAL B C 2348 ATOM 1515 O O . VAL B 2348 31 . -18.420 3.411 41.466 1.00 17.66 ? ? ? ? ? . 31 VAL B O 2348 ATOM 1516 C CB . VAL B 2348 31 . -17.335 5.511 43.452 1.00 17.15 ? ? ? ? ? . 31 VAL B CB 2348 ATOM 1517 C CG1 . VAL B 2348 31 . -16.106 5.860 42.622 1.00 18.31 ? ? ? ? ? . 31 VAL B CG1 2348 ATOM 1518 C CG2 . VAL B 2348 31 . -17.513 6.471 44.623 1.00 18.02 ? ? ? ? ? . 31 VAL B CG2 2348 ATOM 1519 N N . PHE B 2348 32 . -18.278 5.289 40.205 1.00 15.33 ? ? ? ? ? . 32 PHE B N 2348 ATOM 1520 C CA . PHE B 2348 32 . -17.954 4.605 38.959 1.00 15.97 ? ? ? ? ? . 32 PHE B CA 2348 ATOM 1521 C C . PHE B 2348 32 . -16.463 4.743 38.690 1.00 17.33 ? ? ? ? ? . 32 PHE B C 2348 ATOM 1522 O O . PHE B 2348 32 . -15.955 5.860 38.580 1.00 17.87 ? ? ? ? ? . 32 PHE B O 2348 ATOM 1523 C CB . PHE B 2348 32 . -18.704 5.203 37.795 1.00 15.59 ? ? ? ? ? . 32 PHE B CB 2348 ATOM 1524 C CG . PHE B 2348 32 . -20.174 4.974 37.825 1.00 16.67 ? ? ? ? ? . 32 PHE B CG 2348 ATOM 1525 C CD1 . PHE B 2348 32 . -20.695 3.707 37.597 1.00 16.26 ? ? ? ? ? . 32 PHE B CD1 2348 ATOM 1526 C CD2 . PHE B 2348 32 . -21.052 6.023 38.060 1.00 18.11 ? ? ? ? ? . 32 PHE B CD2 2348 ATOM 1527 C CE1 . PHE B 2348 32 . -22.049 3.483 37.605 1.00 16.54 ? ? ? ? ? . 32 PHE B CE1 2348 ATOM 1528 C CE2 . PHE B 2348 32 . -22.423 5.801 38.050 1.00 19.09 ? ? ? ? ? . 32 PHE B CE2 2348 ATOM 1529 C CZ . PHE B 2348 32 . -22.914 4.524 37.828 1.00 17.79 ? ? ? ? ? . 32 PHE B CZ 2348 ATOM 1530 N N . LEU B 2348 33 . -15.776 3.614 38.563 1.00 18.19 ? ? ? ? ? . 33 LEU B N 2348 ATOM 1531 C CA . LEU B 2348 33 . -14.390 3.613 38.108 1.00 16.59 ? ? ? ? ? . 33 LEU B CA 2348 ATOM 1532 C C . LEU B 2348 33 . -14.442 3.462 36.600 1.00 16.50 ? ? ? ? ? . 33 LEU B C 2348 ATOM 1533 O O . LEU B 2348 33 . -14.938 2.453 36.105 1.00 15.95 ? ? ? ? ? . 33 LEU B O 2348 ATOM 1534 C CB . LEU B 2348 33 . -13.592 2.478 38.746 1.00 17.76 ? ? ? ? ? . 33 LEU B CB 2348 ATOM 1535 C CG . LEU B 2348 33 . -13.565 2.381 40.272 1.00 17.52 ? ? ? ? ? . 33 LEU B CG 2348 ATOM 1536 C CD1 . LEU B 2348 33 . -12.655 1.235 40.659 1.00 20.03 ? ? ? ? ? . 33 LEU B CD1 2348 ATOM 1537 C CD2 . LEU B 2348 33 . -13.101 3.681 40.919 1.00 18.78 ? ? ? ? ? . 33 LEU B CD2 2348 ATOM 1538 N N . TYR B 2348 34 . -13.955 4.487 35.892 1.00 15.29 ? ? ? ? ? . 34 TYR B N 2348 ATOM 1539 C CA . TYR B 2348 34 . -14.051 4.587 34.456 1.00 15.84 ? ? ? ? ? . 34 TYR B CA 2348 ATOM 1540 C C . TYR B 2348 34 . -12.697 4.264 33.844 1.00 16.40 ? ? ? ? ? . 34 TYR B C 2348 ATOM 1541 O O . TYR B 2348 34 . -11.798 5.117 33.844 1.00 16.02 ? ? ? ? ? . 34 TYR B O 2348 ATOM 1542 C CB . TYR B 2348 34 . -14.539 5.978 34.030 1.00 16.34 ? ? ? ? ? . 34 TYR B CB 2348 ATOM 1543 C CG . TYR B 2348 34 . -14.638 6.174 32.511 1.00 16.48 ? ? ? ? ? . 34 TYR B CG 2348 ATOM 1544 C CD1 . TYR B 2348 34 . -14.960 5.108 31.653 1.00 16.84 ? ? ? ? ? . 34 TYR B CD1 2348 ATOM 1545 C CD2 . TYR B 2348 34 . -14.424 7.419 31.932 1.00 17.38 ? ? ? ? ? . 34 TYR B CD2 2348 ATOM 1546 C CE1 . TYR B 2348 34 . -15.060 5.286 30.293 1.00 17.26 ? ? ? ? ? . 34 TYR B CE1 2348 ATOM 1547 C CE2 . TYR B 2348 34 . -14.528 7.603 30.558 1.00 17.55 ? ? ? ? ? . 34 TYR B CE2 2348 ATOM 1548 C CZ . TYR B 2348 34 . -14.850 6.534 29.747 1.00 17.57 ? ? ? ? ? . 34 TYR B CZ 2348 ATOM 1549 O OH . TYR B 2348 34 . -14.931 6.690 28.388 1.00 18.64 ? ? ? ? ? . 34 TYR B OH 2348 ATOM 1550 N N . PHE B 2348 35 . -12.559 3.025 33.358 1.00 16.94 ? ? ? ? ? . 35 PHE B N 2348 ATOM 1551 C CA . PHE B 2348 35 . -11.319 2.588 32.702 1.00 16.15 ? ? ? ? ? . 35 PHE B CA 2348 ATOM 1552 C C . PHE B 2348 35 . -11.357 3.088 31.269 1.00 15.95 ? ? ? ? ? . 35 PHE B C 2348 ATOM 1553 O O . PHE B 2348 35 . -12.252 2.733 30.502 1.00 15.83 ? ? ? ? ? . 35 PHE B O 2348 ATOM 1554 C CB . PHE B 2348 35 . -11.131 1.073 32.787 1.00 16.88 ? ? ? ? ? . 35 PHE B CB 2348 ATOM 1555 C CG . PHE B 2348 35 . -10.865 0.569 34.181 1.00 17.15 ? ? ? ? ? . 35 PHE B CG 2348 ATOM 1556 C CD1 . PHE B 2348 35 . -11.887 0.445 35.101 1.00 17.70 ? ? ? ? ? . 35 PHE B CD1 2348 ATOM 1557 C CD2 . PHE B 2348 35 . -9.573 0.220 34.578 1.00 18.87 ? ? ? ? ? . 35 PHE B CD2 2348 ATOM 1558 C CE1 . PHE B 2348 35 . -11.643 -0.049 36.378 1.00 18.55 ? ? ? ? ? . 35 PHE B CE1 2348 ATOM 1559 C CE2 . PHE B 2348 35 . -9.317 -0.256 35.858 1.00 18.03 ? ? ? ? ? . 35 PHE B CE2 2348 ATOM 1560 C CZ . PHE B 2348 35 . -10.352 -0.385 36.761 1.00 20.83 ? ? ? ? ? . 35 PHE B CZ 2348 ATOM 1561 N N . SER B 2348 36 . -10.401 3.940 30.922 1.00 16.18 ? ? ? ? ? . 36 SER B N 2348 ATOM 1562 C CA . SER B 2348 36 . -10.418 4.655 29.654 1.00 16.32 ? ? ? ? ? . 36 SER B CA 2348 ATOM 1563 C C . SER B 2348 36 . -8.995 5.030 29.241 1.00 14.78 ? ? ? ? ? . 36 SER B C 2348 ATOM 1564 O O . SER B 2348 36 . -8.040 4.734 29.954 1.00 14.88 ? ? ? ? ? . 36 SER B O 2348 ATOM 1565 C CB . SER B 2348 36 . -11.285 5.920 29.788 1.00 17.87 ? ? ? ? ? . 36 SER B CB 2348 ATOM 1566 O OG . SER B 2348 36 . -11.535 6.503 28.519 1.00 18.57 ? ? ? ? ? . 36 SER B OG 2348 ATOM 1567 N N . ALA B 2348 37 . -8.857 5.660 28.080 1.00 15.35 ? ? ? ? ? . 37 ALA B N 2348 ATOM 1568 C CA . ALA B 2348 37 . -7.567 6.159 27.613 1.00 15.61 ? ? ? ? ? . 37 ALA B CA 2348 ATOM 1569 C C . ALA B 2348 37 . -7.805 7.204 26.551 1.00 16.69 ? ? ? ? ? . 37 ALA B C 2348 ATOM 1570 O O . ALA B 2348 37 . -8.754 7.075 25.778 1.00 16.13 ? ? ? ? ? . 37 ALA B O 2348 ATOM 1571 C CB . ALA B 2348 37 . -6.728 5.014 27.031 1.00 15.54 ? ? ? ? ? . 37 ALA B CB 2348 ATOM 1572 N N . SER B 2348 38 . -6.913 8.197 26.489 1.00 15.71 ? ? ? ? ? . 38 SER B N 2348 ATOM 1573 C CA . SER B 2348 38 . -7.072 9.335 25.581 1.00 17.09 ? ? ? ? ? . 38 SER B CA 2348 ATOM 1574 C C . SER B 2348 38 . -7.153 8.953 24.102 1.00 19.07 ? ? ? ? ? . 38 SER B C 2348 ATOM 1575 O O . SER B 2348 38 . -7.854 9.606 23.326 1.00 20.98 ? ? ? ? ? . 38 SER B O 2348 ATOM 1576 C CB . SER B 2348 38 . -5.941 10.335 25.773 1.00 15.69 ? ? ? ? ? . 38 SER B CB 2348 ATOM 1577 O OG . SER B 2348 38 . -4.701 9.809 25.396 1.00 15.44 ? ? ? ? ? . 38 SER B OG 2348 ATOM 1578 N N . TRP B 2348 39 . -6.463 7.874 23.742 1.00 17.71 ? ? ? ? ? . 39 TRP B N 2348 ATOM 1579 C CA . TRP B 2348 39 . -6.253 7.475 22.352 1.00 17.15 ? ? ? ? ? . 39 TRP B CA 2348 ATOM 1580 C C . TRP B 2348 39 . -7.121 6.299 21.897 1.00 17.30 ? ? ? ? ? . 39 TRP B C 2348 ATOM 1581 O O . TRP B 2348 39 . -7.026 5.902 20.745 1.00 15.89 ? ? ? ? ? . 39 TRP B O 2348 ATOM 1582 C CB . TRP B 2348 39 . -4.757 7.203 22.076 1.00 17.52 ? ? ? ? ? . 39 TRP B CB 2348 ATOM 1583 C CG . TRP B 2348 39 . -4.007 6.714 23.240 1.00 17.35 ? ? ? ? ? . 39 TRP B CG 2348 ATOM 1584 C CD1 . TRP B 2348 39 . -3.045 7.391 23.940 1.00 17.10 ? ? ? ? ? . 39 TRP B CD1 2348 ATOM 1585 C CD2 . TRP B 2348 39 . -4.166 5.451 23.891 1.00 16.65 ? ? ? ? ? . 39 TRP B CD2 2348 ATOM 1586 C CE2 . TRP B 2348 39 . -3.278 5.437 24.986 1.00 16.51 ? ? ? ? ? . 39 TRP B CE2 2348 ATOM 1587 C CE3 . TRP B 2348 39 . -4.985 4.334 23.666 1.00 17.15 ? ? ? ? ? . 39 TRP B CE3 2348 ATOM 1588 N NE1 . TRP B 2348 39 . -2.611 6.633 24.990 1.00 18.33 ? ? ? ? ? . 39 TRP B NE1 2348 ATOM 1589 C CZ2 . TRP B 2348 39 . -3.158 4.343 25.842 1.00 16.73 ? ? ? ? ? . 39 TRP B CZ2 2348 ATOM 1590 C CZ3 . TRP B 2348 39 . -4.871 3.244 24.540 1.00 17.40 ? ? ? ? ? . 39 TRP B CZ3 2348 ATOM 1591 C CH2 . TRP B 2348 39 . -3.974 3.272 25.619 1.00 17.72 ? ? ? ? ? . 39 TRP B CH2 2348 ATOM 1592 N N A CYS B 2348 40 . -7.942 5.730 22.791 0.50 17.64 ? ? ? ? ? . 40 CYS B N 2348 ATOM 1593 N N B CYS B 2348 40 . -7.980 5.787 22.782 0.50 17.88 ? ? ? ? ? . 40 CYS B N 2348 ATOM 1594 C CA A CYS B 2348 40 . -8.768 4.570 22.439 0.50 16.86 ? ? ? ? ? . 40 CYS B CA 2348 ATOM 1595 C CA B CYS B 2348 40 . -8.812 4.625 22.494 0.50 17.28 ? ? ? ? ? . 40 CYS B CA 2348 ATOM 1596 C C A CYS B 2348 40 . -10.035 5.057 21.740 0.50 16.54 ? ? ? ? ? . 40 CYS B C 2348 ATOM 1597 C C B CYS B 2348 40 . -10.071 5.074 21.747 0.50 16.75 ? ? ? ? ? . 40 CYS B C 2348 ATOM 1598 O O A CYS B 2348 40 . -10.790 5.824 22.317 0.50 16.77 ? ? ? ? ? . 40 CYS B O 2348 ATOM 1599 O O B CYS B 2348 40 . -10.858 5.829 22.299 0.50 16.99 ? ? ? ? ? . 40 CYS B O 2348 ATOM 1600 C CB A CYS B 2348 40 . -9.121 3.740 23.677 0.50 17.14 ? ? ? ? ? . 40 CYS B CB 2348 ATOM 1601 C CB B CYS B 2348 40 . -9.167 3.943 23.820 0.50 18.03 ? ? ? ? ? . 40 CYS B CB 2348 ATOM 1602 S SG A CYS B 2348 40 . -10.007 2.211 23.268 0.50 17.57 ? ? ? ? ? . 40 CYS B SG 2348 ATOM 1603 S SG B CYS B 2348 40 . -10.605 2.859 23.744 0.50 19.19 ? ? ? ? ? . 40 CYS B SG 2348 ATOM 1604 N N . PRO B 2348 41 . -10.253 4.654 20.475 1.00 16.94 ? ? ? ? ? . 41 PRO B N 2348 ATOM 1605 C CA . PRO B 2348 41 . -11.436 5.180 19.741 1.00 18.45 ? ? ? ? ? . 41 PRO B CA 2348 ATOM 1606 C C . PRO B 2348 41 . -12.810 4.984 20.378 1.00 17.82 ? ? ? ? ? . 41 PRO B C 2348 ATOM 1607 O O . PRO B 2348 41 . -13.539 5.965 20.492 1.00 16.82 ? ? ? ? ? . 41 PRO B O 2348 ATOM 1608 C CB . PRO B 2348 41 . -11.343 4.521 18.355 1.00 16.98 ? ? ? ? ? . 41 PRO B CB 2348 ATOM 1609 C CG . PRO B 2348 41 . -9.900 4.161 18.206 1.00 16.89 ? ? ? ? ? . 41 PRO B CG 2348 ATOM 1610 C CD . PRO B 2348 41 . -9.375 3.873 19.578 1.00 17.21 ? ? ? ? ? . 41 PRO B CD 2348 ATOM 1611 N N . PRO B 2348 42 . -13.155 3.755 20.820 1.00 18.29 ? ? ? ? ? . 42 PRO B N 2348 ATOM 1612 C CA . PRO B 2348 42 . -14.458 3.621 21.485 1.00 18.49 ? ? ? ? ? . 42 PRO B CA 2348 ATOM 1613 C C . PRO B 2348 42 . -14.634 4.453 22.767 1.00 18.34 ? ? ? ? ? . 42 PRO B C 2348 ATOM 1614 O O . PRO B 2348 42 . -15.752 4.859 23.076 1.00 17.26 ? ? ? ? ? . 42 PRO B O 2348 ATOM 1615 C CB . PRO B 2348 42 . -14.575 2.107 21.771 1.00 18.19 ? ? ? ? ? . 42 PRO B CB 2348 ATOM 1616 C CG . PRO B 2348 42 . -13.212 1.574 21.649 1.00 19.06 ? ? ? ? ? . 42 PRO B CG 2348 ATOM 1617 C CD . PRO B 2348 42 . -12.479 2.450 20.676 1.00 18.40 ? ? ? ? ? . 42 PRO B CD 2348 ATOM 1618 N N . CYS B 2348 43 . -13.552 4.727 23.492 1.00 17.22 ? ? ? ? ? . 43 CYS B N 2348 ATOM 1619 C CA . CYS B 2348 43 . -13.627 5.660 24.616 1.00 18.95 ? ? ? ? ? . 43 CYS B CA 2348 ATOM 1620 C C . CYS B 2348 43 . -14.010 7.054 24.154 1.00 18.30 ? ? ? ? ? . 43 CYS B C 2348 ATOM 1621 O O . CYS B 2348 43 . -14.776 7.731 24.840 1.00 17.47 ? ? ? ? ? . 43 CYS B O 2348 ATOM 1622 C CB . CYS B 2348 43 . -12.315 5.731 25.400 1.00 17.93 ? ? ? ? ? . 43 CYS B CB 2348 ATOM 1623 S SG . CYS B 2348 43 . -11.945 4.205 26.268 1.00 18.83 ? ? ? ? ? . 43 CYS B SG 2348 ATOM 1624 N N . ARG B 2348 44 . -13.488 7.475 22.999 1.00 18.41 ? ? ? ? ? . 44 ARG B N 2348 ATOM 1625 C CA . ARG B 2348 44 . -13.821 8.784 22.446 1.00 20.27 ? ? ? ? ? . 44 ARG B CA 2348 ATOM 1626 C C . ARG B 2348 44 . -15.314 8.919 22.195 1.00 18.08 ? ? ? ? ? . 44 ARG B C 2348 ATOM 1627 O O . ARG B 2348 44 . -15.884 9.989 22.410 1.00 17.78 ? ? ? ? ? . 44 ARG B O 2348 ATOM 1628 C CB . ARG B 2348 44 . -13.015 9.091 21.174 1.00 24.38 ? ? ? ? ? . 44 ARG B CB 2348 ATOM 1629 C CG . ARG B 2348 44 . -11.547 9.283 21.467 1.00 31.65 ? ? ? ? ? . 44 ARG B CG 2348 ATOM 1630 C CD . ARG B 2348 44 . -10.774 9.731 20.250 1.00 40.06 ? ? ? ? ? . 44 ARG B CD 2348 ATOM 1631 N NE . ARG B 2348 44 . -9.418 10.139 20.614 1.00 46.56 ? ? ? ? ? . 44 ARG B NE 2348 ATOM 1632 C CZ . ARG B 2348 44 . -8.478 10.527 19.754 1.00 50.40 ? ? ? ? ? . 44 ARG B CZ 2348 ATOM 1633 N NH1 . ARG B 2348 44 . -8.722 10.569 18.443 1.00 54.07 ? ? ? ? ? 1+ 44 ARG B NH1 2348 ATOM 1634 N NH2 . ARG B 2348 44 . -7.276 10.876 20.209 1.00 53.44 ? ? ? ? ? . 44 ARG B NH2 2348 ATOM 1635 N N . GLY B 2348 45 . -15.947 7.823 21.783 1.00 17.67 ? ? ? ? ? . 45 GLY B N 2348 ATOM 1636 C CA . GLY B 2348 45 . -17.390 7.801 21.531 1.00 17.84 ? ? ? ? ? . 45 GLY B CA 2348 ATOM 1637 C C . GLY B 2348 45 . -18.247 7.720 22.782 1.00 17.44 ? ? ? ? ? . 45 GLY B C 2348 ATOM 1638 O O . GLY B 2348 45 . -19.403 8.161 22.779 1.00 19.73 ? ? ? ? ? . 45 GLY B O 2348 ATOM 1639 N N . PHE B 2348 46 . -17.694 7.155 23.848 1.00 16.57 ? ? ? ? ? . 46 PHE B N 2348 ATOM 1640 C CA . PHE B 2348 46 . -18.431 6.950 25.088 1.00 17.20 ? ? ? ? ? . 46 PHE B CA 2348 ATOM 1641 C C . PHE B 2348 46 . -18.295 8.104 26.090 1.00 16.63 ? ? ? ? ? . 46 PHE B C 2348 ATOM 1642 O O . PHE B 2348 46 . -19.269 8.470 26.755 1.00 18.09 ? ? ? ? ? . 46 PHE B O 2348 ATOM 1643 C CB . PHE B 2348 46 . -18.031 5.622 25.739 1.00 15.59 ? ? ? ? ? . 46 PHE B CB 2348 ATOM 1644 C CG . PHE B 2348 46 . -18.777 5.345 26.999 1.00 16.81 ? ? ? ? ? . 46 PHE B CG 2348 ATOM 1645 C CD1 . PHE B 2348 46 . -20.168 5.219 26.980 1.00 16.35 ? ? ? ? ? . 46 PHE B CD1 2348 ATOM 1646 C CD2 . PHE B 2348 46 . -18.108 5.247 28.225 1.00 16.40 ? ? ? ? ? . 46 PHE B CD2 2348 ATOM 1647 C CE1 . PHE B 2348 46 . -20.867 4.988 28.154 1.00 16.37 ? ? ? ? ? . 46 PHE B CE1 2348 ATOM 1648 C CE2 . PHE B 2348 46 . -18.811 5.004 29.398 1.00 16.33 ? ? ? ? ? . 46 PHE B CE2 2348 ATOM 1649 C CZ . PHE B 2348 46 . -20.198 4.887 29.358 1.00 15.99 ? ? ? ? ? . 46 PHE B CZ 2348 ATOM 1650 N N . THR B 2348 47 . -17.106 8.685 26.208 1.00 15.70 ? ? ? ? ? . 47 THR B N 2348 ATOM 1651 C CA . THR B 2348 47 . -16.868 9.714 27.226 1.00 16.94 ? ? ? ? ? . 47 THR B CA 2348 ATOM 1652 C C . THR B 2348 47 . -17.912 10.856 27.243 1.00 17.07 ? ? ? ? ? . 47 THR B C 2348 ATOM 1653 O O . THR B 2348 47 . -18.349 11.248 28.330 1.00 16.48 ? ? ? ? ? . 47 THR B O 2348 ATOM 1654 C CB . THR B 2348 47 . -15.430 10.247 27.148 1.00 19.26 ? ? ? ? ? . 47 THR B CB 2348 ATOM 1655 C CG2 . THR B 2348 47 . -15.210 11.385 28.149 1.00 19.34 ? ? ? ? ? . 47 THR B CG2 2348 ATOM 1656 O OG1 . THR B 2348 47 . -14.530 9.163 27.429 1.00 19.80 ? ? ? ? ? . 47 THR B OG1 2348 ATOM 1657 N N . PRO B 2348 48 . -18.331 11.370 26.060 1.00 16.50 ? ? ? ? ? . 48 PRO B N 2348 ATOM 1658 C CA . PRO B 2348 48 . -19.352 12.439 26.034 1.00 16.75 ? ? ? ? ? . 48 PRO B CA 2348 ATOM 1659 C C . PRO B 2348 48 . -20.719 11.979 26.525 1.00 16.05 ? ? ? ? ? . 48 PRO B C 2348 ATOM 1660 O O . PRO B 2348 48 . -21.466 12.765 27.119 1.00 15.03 ? ? ? ? ? . 48 PRO B O 2348 ATOM 1661 C CB . PRO B 2348 48 . -19.442 12.835 24.547 1.00 17.41 ? ? ? ? ? . 48 PRO B CB 2348 ATOM 1662 C CG . PRO B 2348 48 . -18.246 12.261 23.903 1.00 17.90 ? ? ? ? ? . 48 PRO B CG 2348 ATOM 1663 C CD . PRO B 2348 48 . -17.832 11.072 24.704 1.00 18.03 ? ? ? ? ? . 48 PRO B CD 2348 ATOM 1664 N N . VAL B 2348 49 . -21.026 10.710 26.278 1.00 17.45 ? ? ? ? ? . 49 VAL B N 2348 ATOM 1665 C CA . VAL B 2348 49 . -22.276 10.119 26.729 1.00 18.57 ? ? ? ? ? . 49 VAL B CA 2348 ATOM 1666 C C . VAL B 2348 49 . -22.243 10.048 28.251 1.00 18.24 ? ? ? ? ? . 49 VAL B C 2348 ATOM 1667 O O . VAL B 2348 49 . -23.231 10.387 28.905 1.00 17.34 ? ? ? ? ? . 49 VAL B O 2348 ATOM 1668 C CB . VAL B 2348 49 . -22.505 8.703 26.161 1.00 21.18 ? ? ? ? ? . 49 VAL B CB 2348 ATOM 1669 C CG1 . VAL B 2348 49 . -23.853 8.147 26.632 1.00 23.32 ? ? ? ? ? . 49 VAL B CG1 2348 ATOM 1670 C CG2 . VAL B 2348 49 . -22.452 8.736 24.642 1.00 22.14 ? ? ? ? ? . 49 VAL B CG2 2348 ATOM 1671 N N . LEU B 2348 50 . -21.105 9.619 28.801 1.00 16.45 ? ? ? ? ? . 50 LEU B N 2348 ATOM 1672 C CA . LEU B 2348 50 . -20.964 9.533 30.254 1.00 17.01 ? ? ? ? ? . 50 LEU B CA 2348 ATOM 1673 C C . LEU B 2348 50 . -20.941 10.909 30.894 1.00 16.78 ? ? ? ? ? . 50 LEU B C 2348 ATOM 1674 O O . LEU B 2348 50 . -21.522 11.097 31.961 1.00 16.95 ? ? ? ? ? . 50 LEU B O 2348 ATOM 1675 C CB . LEU B 2348 50 . -19.728 8.714 30.655 1.00 17.57 ? ? ? ? ? . 50 LEU B CB 2348 ATOM 1676 C CG . LEU B 2348 50 . -19.486 8.477 32.154 1.00 17.08 ? ? ? ? ? . 50 LEU B CG 2348 ATOM 1677 C CD1 . LEU B 2348 50 . -20.623 7.695 32.799 1.00 17.71 ? ? ? ? ? . 50 LEU B CD1 2348 ATOM 1678 C CD2 . LEU B 2348 50 . -18.162 7.773 32.395 1.00 18.09 ? ? ? ? ? . 50 LEU B CD2 2348 ATOM 1679 N N . ALA B 2348 51 . -20.295 11.876 30.246 1.00 16.81 ? ? ? ? ? . 51 ALA B N 2348 ATOM 1680 C CA . ALA B 2348 51 . -20.333 13.269 30.722 1.00 15.97 ? ? ? ? ? . 51 ALA B CA 2348 ATOM 1681 C C . ALA B 2348 51 . -21.736 13.853 30.774 1.00 15.65 ? ? ? ? ? . 51 ALA B C 2348 ATOM 1682 O O . ALA B 2348 51 . -22.077 14.546 31.726 1.00 16.02 ? ? ? ? ? . 51 ALA B O 2348 ATOM 1683 C CB . ALA B 2348 51 . -19.426 14.156 29.890 1.00 14.73 ? ? ? ? ? . 51 ALA B CB 2348 ATOM 1684 N N . GLU B 2348 52 . -22.551 13.592 29.758 1.00 15.19 ? ? ? ? ? . 52 GLU B N 2348 ATOM 1685 C CA . GLU B 2348 52 . -23.941 14.038 29.776 1.00 16.90 ? ? ? ? ? . 52 GLU B CA 2348 ATOM 1686 C C . GLU B 2348 52 . -24.716 13.377 30.923 1.00 16.11 ? ? ? ? ? . 52 GLU B C 2348 ATOM 1687 O O . GLU B 2348 52 . -25.475 14.047 31.617 1.00 15.24 ? ? ? ? ? . 52 GLU B O 2348 ATOM 1688 C CB . GLU B 2348 52 . -24.619 13.757 28.426 1.00 19.85 ? ? ? ? ? . 52 GLU B CB 2348 ATOM 1689 C CG . GLU B 2348 52 . -26.027 14.336 28.294 1.00 21.97 ? ? ? ? ? . 52 GLU B CG 2348 ATOM 1690 C CD . GLU B 2348 52 . -26.678 14.037 26.951 1.00 26.15 ? ? ? ? ? . 52 GLU B CD 2348 ATOM 1691 O OE1 . GLU B 2348 52 . -25.970 13.605 26.008 1.00 26.88 ? ? ? ? ? . 52 GLU B OE1 2348 ATOM 1692 O OE2 . GLU B 2348 52 . -27.911 14.232 26.850 1.00 26.62 ? ? ? ? ? 1- 52 GLU B OE2 2348 ATOM 1693 N N . PHE B 2348 53 . -24.530 12.071 31.114 1.00 15.37 ? ? ? ? ? . 53 PHE B N 2348 ATOM 1694 C CA . PHE B 2348 53 . -25.170 11.341 32.218 1.00 15.90 ? ? ? ? ? . 53 PHE B CA 2348 ATOM 1695 C C . PHE B 2348 53 . -24.736 11.927 33.577 1.00 15.68 ? ? ? ? ? . 53 PHE B C 2348 ATOM 1696 O O . PHE B 2348 53 . -25.548 12.161 34.459 1.00 14.25 ? ? ? ? ? . 53 PHE B O 2348 ATOM 1697 C CB . PHE B 2348 53 . -24.829 9.842 32.131 1.00 18.04 ? ? ? ? ? . 53 PHE B CB 2348 ATOM 1698 C CG . PHE B 2348 53 . -25.649 8.979 33.042 1.00 17.72 ? ? ? ? ? . 53 PHE B CG 2348 ATOM 1699 C CD1 . PHE B 2348 53 . -26.890 8.471 32.625 1.00 19.59 ? ? ? ? ? . 53 PHE B CD1 2348 ATOM 1700 C CD2 . PHE B 2348 53 . -25.192 8.667 34.325 1.00 18.36 ? ? ? ? ? . 53 PHE B CD2 2348 ATOM 1701 C CE1 . PHE B 2348 53 . -27.646 7.665 33.479 1.00 20.58 ? ? ? ? ? . 53 PHE B CE1 2348 ATOM 1702 C CE2 . PHE B 2348 53 . -25.952 7.882 35.182 1.00 18.63 ? ? ? ? ? . 53 PHE B CE2 2348 ATOM 1703 C CZ . PHE B 2348 53 . -27.186 7.397 34.765 1.00 19.12 ? ? ? ? ? . 53 PHE B CZ 2348 ATOM 1704 N N . TYR B 2348 54 . -23.443 12.174 33.711 1.00 16.22 ? ? ? ? ? . 54 TYR B N 2348 ATOM 1705 C CA . TYR B 2348 54 . -22.864 12.791 34.900 1.00 16.80 ? ? ? ? ? . 54 TYR B CA 2348 ATOM 1706 C C . TYR B 2348 54 . -23.456 14.164 35.194 1.00 17.12 ? ? ? ? ? . 54 TYR B C 2348 ATOM 1707 O O . TYR B 2348 54 . -23.868 14.429 36.330 1.00 14.13 ? ? ? ? ? . 54 TYR B O 2348 ATOM 1708 C CB . TYR B 2348 54 . -21.349 12.901 34.733 1.00 17.77 ? ? ? ? ? . 54 TYR B CB 2348 ATOM 1709 C CG . TYR B 2348 54 . -20.606 13.433 35.935 1.00 17.67 ? ? ? ? ? . 54 TYR B CG 2348 ATOM 1710 C CD1 . TYR B 2348 54 . -20.241 12.595 36.984 1.00 19.54 ? ? ? ? ? . 54 TYR B CD1 2348 ATOM 1711 C CD2 . TYR B 2348 54 . -20.236 14.774 36.011 1.00 17.99 ? ? ? ? ? . 54 TYR B CD2 2348 ATOM 1712 C CE1 . TYR B 2348 54 . -19.553 13.086 38.099 1.00 18.82 ? ? ? ? ? . 54 TYR B CE1 2348 ATOM 1713 C CE2 . TYR B 2348 54 . -19.542 15.265 37.108 1.00 18.99 ? ? ? ? ? . 54 TYR B CE2 2348 ATOM 1714 C CZ . TYR B 2348 54 . -19.210 14.418 38.151 1.00 18.31 ? ? ? ? ? . 54 TYR B CZ 2348 ATOM 1715 O OH . TYR B 2348 54 . -18.510 14.930 39.221 1.00 18.74 ? ? ? ? ? . 54 TYR B OH 2348 ATOM 1716 N N . GLU B 2348 55 . -23.489 15.046 34.191 1.00 17.50 ? ? ? ? ? . 55 GLU B N 2348 ATOM 1717 C CA . GLU B 2348 55 . -24.071 16.376 34.399 1.00 19.67 ? ? ? ? ? . 55 GLU B CA 2348 ATOM 1718 C C . GLU B 2348 55 . -25.528 16.272 34.838 1.00 17.98 ? ? ? ? ? . 55 GLU B C 2348 ATOM 1719 O O . GLU B 2348 55 . -25.945 16.968 35.744 1.00 16.25 ? ? ? ? ? . 55 GLU B O 2348 ATOM 1720 C CB . GLU B 2348 55 . -23.941 17.257 33.149 1.00 24.87 ? ? ? ? ? . 55 GLU B CB 2348 ATOM 1721 C CG . GLU B 2348 55 . -22.527 17.753 32.894 1.00 31.42 ? ? ? ? ? . 55 GLU B CG 2348 ATOM 1722 C CD . GLU B 2348 55 . -22.014 18.658 34.006 1.00 38.94 ? ? ? ? ? . 55 GLU B CD 2348 ATOM 1723 O OE1 . GLU B 2348 55 . -22.737 19.618 34.387 1.00 43.93 ? ? ? ? ? . 55 GLU B OE1 2348 ATOM 1724 O OE2 . GLU B 2348 55 . -20.895 18.399 34.497 1.00 41.82 ? ? ? ? ? 1- 55 GLU B OE2 2348 ATOM 1725 N N . LYS B 2348 56 . -26.280 15.360 34.222 1.00 18.56 ? ? ? ? ? . 56 LYS B N 2348 ATOM 1726 C CA . LYS B 2348 56 . -27.717 15.217 34.507 1.00 18.98 ? ? ? ? ? . 56 LYS B CA 2348 ATOM 1727 C C . LYS B 2348 56 . -28.025 14.710 35.903 1.00 17.58 ? ? ? ? ? . 56 LYS B C 2348 ATOM 1728 O O . LYS B 2348 56 . -28.974 15.184 36.534 1.00 16.83 ? ? ? ? ? . 56 LYS B O 2348 ATOM 1729 C CB . LYS B 2348 56 . -28.402 14.254 33.521 1.00 23.33 ? ? ? ? ? . 56 LYS B CB 2348 ATOM 1730 C CG . LYS B 2348 56 . -29.299 14.920 32.482 1.00 28.96 ? ? ? ? ? . 56 LYS B CG 2348 ATOM 1731 C CD . LYS B 2348 56 . -30.217 13.890 31.823 1.00 29.28 ? ? ? ? ? . 56 LYS B CD 2348 ATOM 1732 C CE . LYS B 2348 56 . -31.047 14.501 30.712 1.00 29.01 ? ? ? ? ? . 56 LYS B CE 2348 ATOM 1733 N NZ . LYS B 2348 56 . -31.705 13.489 29.836 1.00 28.78 ? ? ? ? ? 1+ 56 LYS B NZ 2348 ATOM 1734 N N . HIS B 2348 57 . -27.267 13.711 36.347 1.00 15.89 ? ? ? ? ? . 57 HIS B N 2348 ATOM 1735 C CA . HIS B 2348 57 . -27.678 12.856 37.452 1.00 17.69 ? ? ? ? ? . 57 HIS B CA 2348 ATOM 1736 C C . HIS B 2348 57 . -26.739 12.753 38.653 1.00 17.22 ? ? ? ? ? . 57 HIS B C 2348 ATOM 1737 O O . HIS B 2348 57 . -27.149 12.180 39.658 1.00 18.59 ? ? ? ? ? . 57 HIS B O 2348 ATOM 1738 C CB . HIS B 2348 57 . -27.888 11.412 36.953 1.00 17.02 ? ? ? ? ? . 57 HIS B CB 2348 ATOM 1739 C CG . HIS B 2348 57 . -28.825 11.286 35.801 1.00 17.81 ? ? ? ? ? . 57 HIS B CG 2348 ATOM 1740 C CD2 . HIS B 2348 57 . -28.639 10.754 34.565 1.00 18.89 ? ? ? ? ? . 57 HIS B CD2 2348 ATOM 1741 N ND1 . HIS B 2348 57 . -30.140 11.681 35.855 1.00 17.57 ? ? ? ? ? . 57 HIS B ND1 2348 ATOM 1742 C CE1 . HIS B 2348 57 . -30.718 11.440 34.689 1.00 17.83 ? ? ? ? ? . 57 HIS B CE1 2348 ATOM 1743 N NE2 . HIS B 2348 57 . -29.833 10.862 33.894 1.00 17.22 ? ? ? ? ? . 57 HIS B NE2 2348 ATOM 1744 N N . HIS B 2348 58 . -25.498 13.238 38.573 1.00 15.59 ? ? ? ? ? . 58 HIS B N 2348 ATOM 1745 C CA . HIS B 2348 58 . -24.536 12.887 39.623 1.00 16.06 ? ? ? ? ? . 58 HIS B CA 2348 ATOM 1746 C C . HIS B 2348 58 . -24.926 13.425 41.003 1.00 14.76 ? ? ? ? ? . 58 HIS B C 2348 ATOM 1747 O O . HIS B 2348 58 . -24.618 12.803 41.994 1.00 16.12 ? ? ? ? ? . 58 HIS B O 2348 ATOM 1748 C CB . HIS B 2348 58 . -23.088 13.220 39.230 1.00 16.88 ? ? ? ? ? . 58 HIS B CB 2348 ATOM 1749 C CG . HIS B 2348 58 . -22.647 14.619 39.541 1.00 17.89 ? ? ? ? ? . 58 HIS B CG 2348 ATOM 1750 C CD2 . HIS B 2348 58 . -21.806 15.090 40.492 1.00 19.39 ? ? ? ? ? . 58 HIS B CD2 2348 ATOM 1751 N ND1 . HIS B 2348 58 . -23.009 15.708 38.780 1.00 18.72 ? ? ? ? ? . 58 HIS B ND1 2348 ATOM 1752 C CE1 . HIS B 2348 58 . -22.454 16.798 39.280 1.00 19.42 ? ? ? ? ? . 58 HIS B CE1 2348 ATOM 1753 N NE2 . HIS B 2348 58 . -21.713 16.449 40.316 1.00 20.87 ? ? ? ? ? . 58 HIS B NE2 2348 ATOM 1754 N N . VAL B 2348 59 . -25.648 14.545 41.065 1.00 16.39 ? ? ? ? ? . 59 VAL B N 2348 ATOM 1755 C CA . VAL B 2348 59 . -26.130 15.053 42.350 1.00 16.87 ? ? ? ? ? . 59 VAL B CA 2348 ATOM 1756 C C . VAL B 2348 59 . -27.353 14.277 42.829 1.00 17.10 ? ? ? ? ? . 59 VAL B C 2348 ATOM 1757 O O . VAL B 2348 59 . -27.352 13.747 43.950 1.00 16.17 ? ? ? ? ? . 59 VAL B O 2348 ATOM 1758 C CB . VAL B 2348 59 . -26.425 16.570 42.292 1.00 18.85 ? ? ? ? ? . 59 VAL B CB 2348 ATOM 1759 C CG1 . VAL B 2348 59 . -27.056 17.055 43.595 1.00 19.93 ? ? ? ? ? . 59 VAL B CG1 2348 ATOM 1760 C CG2 . VAL B 2348 59 . -25.131 17.324 42.014 1.00 19.28 ? ? ? ? ? . 59 VAL B CG2 2348 ATOM 1761 N N . ALA B 2348 60 . -28.393 14.211 41.992 1.00 16.61 ? ? ? ? ? . 60 ALA B N 2348 ATOM 1762 C CA . ALA B 2348 60 . -29.643 13.560 42.375 1.00 16.62 ? ? ? ? ? . 60 ALA B CA 2348 ATOM 1763 C C . ALA B 2348 60 . -29.499 12.083 42.675 1.00 16.56 ? ? ? ? ? . 60 ALA B C 2348 ATOM 1764 O O . ALA B 2348 60 . -30.263 11.552 43.487 1.00 16.27 ? ? ? ? ? . 60 ALA B O 2348 ATOM 1765 C CB . ALA B 2348 60 . -30.707 13.767 41.307 1.00 18.55 ? ? ? ? ? . 60 ALA B CB 2348 ATOM 1766 N N . LYS B 2348 61 . -28.543 11.427 42.013 1.00 15.97 ? ? ? ? ? . 61 LYS B N 2348 ATOM 1767 C CA . LYS B 2348 61 . -28.281 10.007 42.207 1.00 16.67 ? ? ? ? ? . 61 LYS B CA 2348 ATOM 1768 C C . LYS B 2348 61 . -26.993 9.747 42.998 1.00 16.95 ? ? ? ? ? . 61 LYS B C 2348 ATOM 1769 O O . LYS B 2348 61 . -26.540 8.604 43.087 1.00 17.30 ? ? ? ? ? . 61 LYS B O 2348 ATOM 1770 C CB . LYS B 2348 61 . -28.262 9.295 40.847 1.00 17.50 ? ? ? ? ? . 61 LYS B CB 2348 ATOM 1771 C CG . LYS B 2348 61 . -29.620 9.367 40.155 1.00 17.98 ? ? ? ? ? . 61 LYS B CG 2348 ATOM 1772 C CD . LYS B 2348 61 . -29.665 8.512 38.910 1.00 18.06 ? ? ? ? ? . 61 LYS B CD 2348 ATOM 1773 C CE . LYS B 2348 61 . -30.940 8.764 38.114 1.00 18.72 ? ? ? ? ? . 61 LYS B CE 2348 ATOM 1774 N NZ . LYS B 2348 61 . -32.150 8.403 38.884 1.00 18.99 ? ? ? ? ? 1+ 61 LYS B NZ 2348 ATOM 1775 N N . ASN B 2348 62 . -26.411 10.816 43.549 1.00 16.07 ? ? ? ? ? . 62 ASN B N 2348 ATOM 1776 C CA . ASN B 2348 62 . -25.332 10.747 44.530 1.00 15.99 ? ? ? ? ? . 62 ASN B CA 2348 ATOM 1777 C C . ASN B 2348 62 . -24.176 9.821 44.109 1.00 15.20 ? ? ? ? ? . 62 ASN B C 2348 ATOM 1778 O O . ASN B 2348 62 . -23.870 8.839 44.786 1.00 14.78 ? ? ? ? ? . 62 ASN B O 2348 ATOM 1779 C CB . ASN B 2348 62 . -25.899 10.343 45.905 1.00 18.04 ? ? ? ? ? . 62 ASN B CB 2348 ATOM 1780 C CG . ASN B 2348 62 . -24.956 10.670 47.054 1.00 17.36 ? ? ? ? ? . 62 ASN B CG 2348 ATOM 1781 N ND2 . ASN B 2348 62 . -24.904 9.799 48.057 1.00 16.56 ? ? ? ? ? . 62 ASN B ND2 2348 ATOM 1782 O OD1 . ASN B 2348 62 . -24.296 11.703 47.042 1.00 21.05 ? ? ? ? ? . 62 ASN B OD1 2348 ATOM 1783 N N . PHE B 2348 63 . -23.568 10.132 42.966 1.00 14.72 ? ? ? ? ? . 63 PHE B N 2348 ATOM 1784 C CA . PHE B 2348 63 . -22.431 9.358 42.491 1.00 15.39 ? ? ? ? ? . 63 PHE B CA 2348 ATOM 1785 C C . PHE B 2348 63 . -21.308 10.231 42.009 1.00 15.90 ? ? ? ? ? . 63 PHE B C 2348 ATOM 1786 O O . PHE B 2348 63 . -21.496 11.409 41.735 1.00 16.12 ? ? ? ? ? . 63 PHE B O 2348 ATOM 1787 C CB . PHE B 2348 63 . -22.814 8.338 41.395 1.00 16.32 ? ? ? ? ? . 63 PHE B CB 2348 ATOM 1788 C CG . PHE B 2348 63 . -23.291 8.943 40.089 1.00 17.02 ? ? ? ? ? . 63 PHE B CG 2348 ATOM 1789 C CD1 . PHE B 2348 63 . -22.385 9.329 39.099 1.00 18.25 ? ? ? ? ? . 63 PHE B CD1 2348 ATOM 1790 C CD2 . PHE B 2348 63 . -24.659 9.059 39.814 1.00 17.83 ? ? ? ? ? . 63 PHE B CD2 2348 ATOM 1791 C CE1 . PHE B 2348 63 . -22.829 9.859 37.889 1.00 18.50 ? ? ? ? ? . 63 PHE B CE1 2348 ATOM 1792 C CE2 . PHE B 2348 63 . -25.104 9.590 38.605 1.00 17.77 ? ? ? ? ? . 63 PHE B CE2 2348 ATOM 1793 C CZ . PHE B 2348 63 . -24.191 9.996 37.644 1.00 18.65 ? ? ? ? ? . 63 PHE B CZ 2348 ATOM 1794 N N . GLU B 2348 64 . -20.136 9.618 41.915 1.00 16.66 ? ? ? ? ? . 64 GLU B N 2348 ATOM 1795 C CA . GLU B 2348 64 . -18.989 10.231 41.263 1.00 17.84 ? ? ? ? ? . 64 GLU B CA 2348 ATOM 1796 C C . GLU B 2348 64 . -18.421 9.274 40.226 1.00 17.11 ? ? ? ? ? . 64 GLU B C 2348 ATOM 1797 O O . GLU B 2348 64 . -18.650 8.068 40.282 1.00 18.90 ? ? ? ? ? . 64 GLU B O 2348 ATOM 1798 C CB . GLU B 2348 64 . -17.894 10.592 42.270 1.00 19.70 ? ? ? ? ? . 64 GLU B CB 2348 ATOM 1799 C CG . GLU B 2348 64 . -18.038 11.949 42.930 1.00 22.91 ? ? ? ? ? . 64 GLU B CG 2348 ATOM 1800 C CD . GLU B 2348 64 . -17.795 13.134 42.007 1.00 23.63 ? ? ? ? ? . 64 GLU B CD 2348 ATOM 1801 O OE1 . GLU B 2348 64 . -17.573 12.954 40.778 1.00 20.92 ? ? ? ? ? . 64 GLU B OE1 2348 ATOM 1802 O OE2 . GLU B 2348 64 . -17.832 14.269 42.539 1.00 26.83 ? ? ? ? ? 1- 64 GLU B OE2 2348 ATOM 1803 N N . VAL B 2348 65 . -17.685 9.852 39.284 1.00 16.75 ? ? ? ? ? . 65 VAL B N 2348 ATOM 1804 C CA . VAL B 2348 65 . -16.929 9.114 38.290 1.00 16.81 ? ? ? ? ? . 65 VAL B CA 2348 ATOM 1805 C C . VAL B 2348 65 . -15.455 9.398 38.559 1.00 16.59 ? ? ? ? ? . 65 VAL B C 2348 ATOM 1806 O O . VAL B 2348 65 . -15.063 10.553 38.710 1.00 17.30 ? ? ? ? ? . 65 VAL B O 2348 ATOM 1807 C CB . VAL B 2348 65 . -17.326 9.539 36.864 1.00 18.23 ? ? ? ? ? . 65 VAL B CB 2348 ATOM 1808 C CG1 . VAL B 2348 65 . -16.423 8.884 35.833 1.00 18.75 ? ? ? ? ? . 65 VAL B CG1 2348 ATOM 1809 C CG2 . VAL B 2348 65 . -18.799 9.198 36.599 1.00 18.08 ? ? ? ? ? . 65 VAL B CG2 2348 ATOM 1810 N N . VAL B 2348 66 . -14.658 8.334 38.648 1.00 16.92 ? ? ? ? ? . 66 VAL B N 2348 ATOM 1811 C CA . VAL B 2348 66 . -13.201 8.450 38.793 1.00 16.10 ? ? ? ? ? . 66 VAL B CA 2348 ATOM 1812 C C . VAL B 2348 66 . -12.561 7.811 37.574 1.00 16.81 ? ? ? ? ? . 66 VAL B C 2348 ATOM 1813 O O . VAL B 2348 66 . -12.656 6.601 37.384 1.00 14.43 ? ? ? ? ? . 66 VAL B O 2348 ATOM 1814 C CB . VAL B 2348 66 . -12.690 7.736 40.048 1.00 15.87 ? ? ? ? ? . 66 VAL B CB 2348 ATOM 1815 C CG1 . VAL B 2348 66 . -11.174 7.884 40.168 1.00 16.03 ? ? ? ? ? . 66 VAL B CG1 2348 ATOM 1816 C CG2 . VAL B 2348 66 . -13.411 8.247 41.289 1.00 17.08 ? ? ? ? ? . 66 VAL B CG2 2348 ATOM 1817 N N . LEU B 2348 67 . -11.904 8.632 36.753 1.00 16.88 ? ? ? ? ? . 67 LEU B N 2348 ATOM 1818 C CA . LEU B 2348 67 . -11.100 8.120 35.642 1.00 16.83 ? ? ? ? ? . 67 LEU B CA 2348 ATOM 1819 C C . LEU B 2348 67 . -9.926 7.249 36.120 1.00 15.67 ? ? ? ? ? . 67 LEU B C 2348 ATOM 1820 O O . LEU B 2348 67 . -9.163 7.640 36.994 1.00 15.86 ? ? ? ? ? . 67 LEU B O 2348 ATOM 1821 C CB . LEU B 2348 67 . -10.535 9.290 34.811 1.00 16.36 ? ? ? ? ? . 67 LEU B CB 2348 ATOM 1822 C CG . LEU B 2348 67 . -9.493 8.998 33.735 1.00 16.45 ? ? ? ? ? . 67 LEU B CG 2348 ATOM 1823 C CD1 . LEU B 2348 67 . -10.126 8.191 32.623 1.00 16.86 ? ? ? ? ? . 67 LEU B CD1 2348 ATOM 1824 C CD2 . LEU B 2348 67 . -8.919 10.311 33.205 1.00 16.53 ? ? ? ? ? . 67 LEU B CD2 2348 ATOM 1825 N N A ILE B 2348 68 . -9.823 6.056 35.548 0.67 17.20 ? ? ? ? ? . 68 ILE B N 2348 ATOM 1826 N N B ILE B 2348 68 . -9.793 6.074 35.515 0.33 16.39 ? ? ? ? ? . 68 ILE B N 2348 ATOM 1827 C CA A ILE B 2348 68 . -8.662 5.189 35.698 0.67 16.28 ? ? ? ? ? . 68 ILE B CA 2348 ATOM 1828 C CA B ILE B 2348 68 . -8.637 5.209 35.708 0.33 15.93 ? ? ? ? ? . 68 ILE B CA 2348 ATOM 1829 C C A ILE B 2348 68 . -8.110 5.096 34.288 0.67 16.36 ? ? ? ? ? . 68 ILE B C 2348 ATOM 1830 C C B ILE B 2348 68 . -8.022 5.007 34.337 0.33 16.33 ? ? ? ? ? . 68 ILE B C 2348 ATOM 1831 O O A ILE B 2348 68 . -8.657 4.376 33.452 0.67 13.87 ? ? ? ? ? . 68 ILE B O 2348 ATOM 1832 O O B ILE B 2348 68 . -8.400 4.098 33.598 0.33 15.33 ? ? ? ? ? . 68 ILE B O 2348 ATOM 1833 C CB A ILE B 2348 68 . -9.034 3.787 36.222 0.67 16.98 ? ? ? ? ? . 68 ILE B CB 2348 ATOM 1834 C CB B ILE B 2348 68 . -9.031 3.868 36.330 0.33 15.94 ? ? ? ? ? . 68 ILE B CB 2348 ATOM 1835 C CG1 A ILE B 2348 68 . -9.950 3.865 37.462 0.67 17.02 ? ? ? ? ? . 68 ILE B CG1 2348 ATOM 1836 C CG2 A ILE B 2348 68 . -7.776 2.987 36.527 0.67 18.01 ? ? ? ? ? . 68 ILE B CG2 2348 ATOM 1837 C CG1 B ILE B 2348 68 . -9.732 4.115 37.670 0.33 15.51 ? ? ? ? ? . 68 ILE B CG1 2348 ATOM 1838 C CG2 B ILE B 2348 68 . -7.803 2.996 36.521 0.33 16.40 ? ? ? ? ? . 68 ILE B CG2 2348 ATOM 1839 C CD1 A ILE B 2348 68 . -9.327 4.506 38.681 0.67 17.83 ? ? ? ? ? . 68 ILE B CD1 2348 ATOM 1840 C CD1 B ILE B 2348 68 . -9.736 2.920 38.593 0.33 15.36 ? ? ? ? ? . 68 ILE B CD1 2348 ATOM 1841 N N . SER B 2348 69 . -7.064 5.870 34.018 1.00 16.47 ? ? ? ? ? . 69 SER B N 2348 ATOM 1842 C CA . SER B 2348 69 . -6.527 5.995 32.667 1.00 16.62 ? ? ? ? ? . 69 SER B CA 2348 ATOM 1843 C C . SER B 2348 69 . -5.413 5.016 32.337 1.00 16.16 ? ? ? ? ? . 69 SER B C 2348 ATOM 1844 O O . SER B 2348 69 . -4.464 4.866 33.110 1.00 16.34 ? ? ? ? ? . 69 SER B O 2348 ATOM 1845 C CB . SER B 2348 69 . -5.983 7.406 32.474 1.00 18.73 ? ? ? ? ? . 69 SER B CB 2348 ATOM 1846 O OG . SER B 2348 69 . -5.408 7.522 31.182 1.00 19.30 ? ? ? ? ? . 69 SER B OG 2348 ATOM 1847 N N . TRP B 2348 70 . -5.493 4.412 31.150 1.00 16.99 ? ? ? ? ? . 70 TRP B N 2348 ATOM 1848 C CA . TRP B 2348 70 . -4.410 3.551 30.621 1.00 17.24 ? ? ? ? ? . 70 TRP B CA 2348 ATOM 1849 C C . TRP B 2348 70 . -3.265 4.371 29.990 1.00 16.18 ? ? ? ? ? . 70 TRP B C 2348 ATOM 1850 O O . TRP B 2348 70 . -2.248 3.798 29.603 1.00 14.77 ? ? ? ? ? . 70 TRP B O 2348 ATOM 1851 C CB . TRP B 2348 70 . -4.944 2.531 29.584 1.00 18.94 ? ? ? ? ? . 70 TRP B CB 2348 ATOM 1852 C CG . TRP B 2348 70 . -4.583 1.101 29.898 1.00 20.10 ? ? ? ? ? . 70 TRP B CG 2348 ATOM 1853 C CD1 . TRP B 2348 70 . -3.473 0.425 29.498 1.00 22.08 ? ? ? ? ? . 70 TRP B CD1 2348 ATOM 1854 C CD2 . TRP B 2348 70 . -5.346 0.183 30.687 1.00 21.73 ? ? ? ? ? . 70 TRP B CD2 2348 ATOM 1855 C CE2 . TRP B 2348 70 . -4.629 -1.029 30.731 1.00 23.54 ? ? ? ? ? . 70 TRP B CE2 2348 ATOM 1856 C CE3 . TRP B 2348 70 . -6.561 0.272 31.369 1.00 22.88 ? ? ? ? ? . 70 TRP B CE3 2348 ATOM 1857 N NE1 . TRP B 2348 70 . -3.492 -0.856 29.994 1.00 23.05 ? ? ? ? ? . 70 TRP B NE1 2348 ATOM 1858 C CZ2 . TRP B 2348 70 . -5.096 -2.154 31.412 1.00 24.12 ? ? ? ? ? . 70 TRP B CZ2 2348 ATOM 1859 C CZ3 . TRP B 2348 70 . -7.028 -0.849 32.056 1.00 25.08 ? ? ? ? ? . 70 TRP B CZ3 2348 ATOM 1860 C CH2 . TRP B 2348 70 . -6.287 -2.046 32.077 1.00 24.62 ? ? ? ? ? . 70 TRP B CH2 2348 ATOM 1861 N N . ASP B 2348 71 . -3.418 5.697 29.885 1.00 16.38 ? ? ? ? ? . 71 ASP B N 2348 ATOM 1862 C CA . ASP B 2348 71 . -2.354 6.535 29.343 1.00 15.76 ? ? ? ? ? . 71 ASP B CA 2348 ATOM 1863 C C . ASP B 2348 71 . -1.033 6.307 30.099 1.00 14.95 ? ? ? ? ? . 71 ASP B C 2348 ATOM 1864 O O . ASP B 2348 71 . -1.014 6.240 31.328 1.00 15.32 ? ? ? ? ? . 71 ASP B O 2348 ATOM 1865 C CB . ASP B 2348 71 . -2.711 8.034 29.397 1.00 16.06 ? ? ? ? ? . 71 ASP B CB 2348 ATOM 1866 C CG . ASP B 2348 71 . -3.700 8.447 28.335 1.00 17.20 ? ? ? ? ? . 71 ASP B CG 2348 ATOM 1867 O OD1 . ASP B 2348 71 . -4.912 8.326 28.574 1.00 21.58 ? ? ? ? ? . 71 ASP B OD1 2348 ATOM 1868 O OD2 . ASP B 2348 71 . -3.291 8.929 27.260 1.00 17.68 ? ? ? ? ? 1- 71 ASP B OD2 2348 ATOM 1869 N N A GLU B 2348 72 . 0.053 6.175 29.353 0.51 14.50 ? ? ? ? ? . 72 GLU B N 2348 ATOM 1870 N N B GLU B 2348 72 . 0.048 6.158 29.342 0.49 14.34 ? ? ? ? ? . 72 GLU B N 2348 ATOM 1871 C CA A GLU B 2348 72 . 1.384 6.076 29.938 0.51 15.09 ? ? ? ? ? . 72 GLU B CA 2348 ATOM 1872 C CA B GLU B 2348 72 . 1.392 6.048 29.893 0.49 14.83 ? ? ? ? ? . 72 GLU B CA 2348 ATOM 1873 C C A GLU B 2348 72 . 2.188 7.360 29.820 0.51 14.34 ? ? ? ? ? . 72 GLU B C 2348 ATOM 1874 C C B GLU B 2348 72 . 2.186 7.348 29.808 0.49 14.17 ? ? ? ? ? . 72 GLU B C 2348 ATOM 1875 O O A GLU B 2348 72 . 3.306 7.430 30.334 0.51 13.00 ? ? ? ? ? . 72 GLU B O 2348 ATOM 1876 O O B GLU B 2348 72 . 3.298 7.415 30.335 0.49 12.82 ? ? ? ? ? . 72 GLU B O 2348 ATOM 1877 C CB A GLU B 2348 72 . 2.134 4.920 29.293 0.51 16.83 ? ? ? ? ? . 72 GLU B CB 2348 ATOM 1878 C CB B GLU B 2348 72 . 2.140 4.927 29.174 0.49 16.27 ? ? ? ? ? . 72 GLU B CB 2348 ATOM 1879 C CG A GLU B 2348 72 . 1.517 3.586 29.664 0.51 17.87 ? ? ? ? ? . 72 GLU B CG 2348 ATOM 1880 C CG B GLU B 2348 72 . 1.469 3.580 29.387 0.49 17.30 ? ? ? ? ? . 72 GLU B CG 2348 ATOM 1881 C CD A GLU B 2348 72 . 2.172 2.446 28.936 0.51 19.88 ? ? ? ? ? . 72 GLU B CD 2348 ATOM 1882 C CD B GLU B 2348 72 . 2.111 2.458 28.599 0.49 18.87 ? ? ? ? ? . 72 GLU B CD 2348 ATOM 1883 O OE1 A GLU B 2348 72 . 1.971 2.368 27.706 0.51 20.25 ? ? ? ? ? . 72 GLU B OE1 2348 ATOM 1884 O OE2 A GLU B 2348 72 . 2.872 1.640 29.592 0.51 21.48 ? ? ? ? ? 1- 72 GLU B OE2 2348 ATOM 1885 O OE1 B GLU B 2348 72 . 3.225 2.644 28.064 0.49 19.35 ? ? ? ? ? . 72 GLU B OE1 2348 ATOM 1886 O OE2 B GLU B 2348 72 . 1.490 1.377 28.529 0.49 19.70 ? ? ? ? ? 1- 72 GLU B OE2 2348 ATOM 1887 N N . ASN B 2348 73 . 1.620 8.362 29.146 1.00 14.22 ? ? ? ? ? . 73 ASN B N 2348 ATOM 1888 C CA . ASN B 2348 73 . 2.251 9.653 28.963 1.00 14.56 ? ? ? ? ? . 73 ASN B CA 2348 ATOM 1889 C C . ASN B 2348 73 . 1.516 10.611 29.883 1.00 15.20 ? ? ? ? ? . 73 ASN B C 2348 ATOM 1890 O O . ASN B 2348 73 . 0.299 10.782 29.768 1.00 15.15 ? ? ? ? ? . 73 ASN B O 2348 ATOM 1891 C CB . ASN B 2348 73 . 2.150 10.099 27.501 1.00 14.97 ? ? ? ? ? . 73 ASN B CB 2348 ATOM 1892 C CG . ASN B 2348 73 . 2.796 11.461 27.255 1.00 15.06 ? ? ? ? ? . 73 ASN B CG 2348 ATOM 1893 N ND2 . ASN B 2348 73 . 3.898 11.497 26.492 1.00 15.07 ? ? ? ? ? . 73 ASN B ND2 2348 ATOM 1894 O OD1 . ASN B 2348 73 . 2.309 12.465 27.753 1.00 14.79 ? ? ? ? ? . 73 ASN B OD1 2348 ATOM 1895 N N . GLU B 2348 74 . 2.250 11.208 30.814 1.00 15.32 ? ? ? ? ? . 74 GLU B N 2348 ATOM 1896 C CA . GLU B 2348 74 . 1.641 12.062 31.821 1.00 16.81 ? ? ? ? ? . 74 GLU B CA 2348 ATOM 1897 C C . GLU B 2348 74 . 0.997 13.322 31.235 1.00 15.94 ? ? ? ? ? . 74 GLU B C 2348 ATOM 1898 O O . GLU B 2348 74 . -0.087 13.721 31.687 1.00 16.38 ? ? ? ? ? . 74 GLU B O 2348 ATOM 1899 C CB . GLU B 2348 74 . 2.655 12.452 32.883 1.00 18.51 ? ? ? ? ? . 74 GLU B CB 2348 ATOM 1900 C CG . GLU B 2348 74 . 2.018 13.159 34.065 1.00 19.35 ? ? ? ? ? . 74 GLU B CG 2348 ATOM 1901 C CD . GLU B 2348 74 . 2.949 13.330 35.236 1.00 22.88 ? ? ? ? ? . 74 GLU B CD 2348 ATOM 1902 O OE1 . GLU B 2348 74 . 4.143 12.951 35.150 1.00 24.64 ? ? ? ? ? . 74 GLU B OE1 2348 ATOM 1903 O OE2 . GLU B 2348 74 . 2.481 13.867 36.255 1.00 25.05 ? ? ? ? ? 1- 74 GLU B OE2 2348 ATOM 1904 N N A SER B 2348 75 . 1.651 13.941 30.251 0.50 15.90 ? ? ? ? ? . 75 SER B N 2348 ATOM 1905 N N B SER B 2348 75 . 1.656 13.941 30.256 0.50 15.68 ? ? ? ? ? . 75 SER B N 2348 ATOM 1906 C CA A SER B 2348 75 . 1.104 15.148 29.605 0.50 15.77 ? ? ? ? ? . 75 SER B CA 2348 ATOM 1907 C CA B SER B 2348 75 . 1.115 15.142 29.594 0.50 15.45 ? ? ? ? ? . 75 SER B CA 2348 ATOM 1908 C C A SER B 2348 75 . -0.230 14.839 28.908 0.50 14.77 ? ? ? ? ? . 75 SER B C 2348 ATOM 1909 C C B SER B 2348 75 . -0.228 14.835 28.914 0.50 14.59 ? ? ? ? ? . 75 SER B C 2348 ATOM 1910 O O A SER B 2348 75 . -1.188 15.609 29.019 0.50 13.57 ? ? ? ? ? . 75 SER B O 2348 ATOM 1911 O O B SER B 2348 75 . -1.187 15.601 29.041 0.50 13.40 ? ? ? ? ? . 75 SER B O 2348 ATOM 1912 C CB A SER B 2348 75 . 2.122 15.753 28.623 0.50 16.44 ? ? ? ? ? . 75 SER B CB 2348 ATOM 1913 C CB B SER B 2348 75 . 2.128 15.696 28.582 0.50 15.81 ? ? ? ? ? . 75 SER B CB 2348 ATOM 1914 O OG A SER B 2348 75 . 2.210 15.005 27.421 0.50 16.71 ? ? ? ? ? . 75 SER B OG 2348 ATOM 1915 O OG B SER B 2348 75 . 1.655 16.888 27.982 0.50 15.64 ? ? ? ? ? . 75 SER B OG 2348 ATOM 1916 N N . ASP B 2348 76 . -0.291 13.701 28.218 1.00 14.38 ? ? ? ? ? . 76 ASP B N 2348 ATOM 1917 C CA . ASP B 2348 76 . -1.538 13.224 27.581 1.00 14.89 ? ? ? ? ? . 76 ASP B CA 2348 ATOM 1918 C C . ASP B 2348 76 . -2.647 12.977 28.614 1.00 15.39 ? ? ? ? ? . 76 ASP B C 2348 ATOM 1919 O O . ASP B 2348 76 . -3.806 13.366 28.415 1.00 14.77 ? ? ? ? ? . 76 ASP B O 2348 ATOM 1920 C CB . ASP B 2348 76 . -1.311 11.899 26.823 1.00 16.41 ? ? ? ? ? . 76 ASP B CB 2348 ATOM 1921 C CG . ASP B 2348 76 . -0.498 12.050 25.540 1.00 17.78 ? ? ? ? ? . 76 ASP B CG 2348 ATOM 1922 O OD1 . ASP B 2348 76 . -0.205 13.182 25.087 1.00 18.98 ? ? ? ? ? . 76 ASP B OD1 2348 ATOM 1923 O OD2 . ASP B 2348 76 . -0.156 10.993 24.968 1.00 18.58 ? ? ? ? ? 1- 76 ASP B OD2 2348 ATOM 1924 N N . PHE B 2348 77 . -2.289 12.316 29.706 1.00 14.34 ? ? ? ? ? . 77 PHE B N 2348 ATOM 1925 C CA . PHE B 2348 77 . -3.213 12.106 30.819 1.00 15.15 ? ? ? ? ? . 77 PHE B CA 2348 ATOM 1926 C C . PHE B 2348 77 . -3.856 13.408 31.312 1.00 15.18 ? ? ? ? ? . 77 PHE B C 2348 ATOM 1927 O O . PHE B 2348 77 . -5.078 13.505 31.385 1.00 14.13 ? ? ? ? ? . 77 PHE B O 2348 ATOM 1928 C CB . PHE B 2348 77 . -2.497 11.412 31.980 1.00 15.59 ? ? ? ? ? . 77 PHE B CB 2348 ATOM 1929 C CG . PHE B 2348 77 . -3.292 11.375 33.246 1.00 15.99 ? ? ? ? ? . 77 PHE B CG 2348 ATOM 1930 C CD1 . PHE B 2348 77 . -4.276 10.423 33.429 1.00 18.33 ? ? ? ? ? . 77 PHE B CD1 2348 ATOM 1931 C CD2 . PHE B 2348 77 . -3.055 12.289 34.261 1.00 16.11 ? ? ? ? ? . 77 PHE B CD2 2348 ATOM 1932 C CE1 . PHE B 2348 77 . -5.023 10.386 34.604 1.00 18.64 ? ? ? ? ? . 77 PHE B CE1 2348 ATOM 1933 C CE2 . PHE B 2348 77 . -3.798 12.256 35.433 1.00 17.39 ? ? ? ? ? . 77 PHE B CE2 2348 ATOM 1934 C CZ . PHE B 2348 77 . -4.772 11.305 35.607 1.00 16.62 ? ? ? ? ? . 77 PHE B CZ 2348 ATOM 1935 N N . HIS B 2348 78 . -3.030 14.390 31.644 1.00 15.40 ? ? ? ? ? . 78 HIS B N 2348 ATOM 1936 C CA . HIS B 2348 78 . -3.555 15.661 32.155 1.00 17.09 ? ? ? ? ? . 78 HIS B CA 2348 ATOM 1937 C C . HIS B 2348 78 . -4.412 16.407 31.136 1.00 17.40 ? ? ? ? ? . 78 HIS B C 2348 ATOM 1938 O O . HIS B 2348 78 . -5.402 17.034 31.503 1.00 17.56 ? ? ? ? ? . 78 HIS B O 2348 ATOM 1939 C CB . HIS B 2348 78 . -2.430 16.539 32.692 1.00 17.58 ? ? ? ? ? . 78 HIS B CB 2348 ATOM 1940 C CG . HIS B 2348 78 . -1.902 16.063 34.007 1.00 20.23 ? ? ? ? ? . 78 HIS B CG 2348 ATOM 1941 C CD2 . HIS B 2348 78 . -2.519 15.881 35.199 1.00 22.72 ? ? ? ? ? . 78 HIS B CD2 2348 ATOM 1942 N ND1 . HIS B 2348 78 . -0.596 15.675 34.190 1.00 22.98 ? ? ? ? ? . 78 HIS B ND1 2348 ATOM 1943 C CE1 . HIS B 2348 78 . -0.427 15.287 35.441 1.00 22.39 ? ? ? ? ? . 78 HIS B CE1 2348 ATOM 1944 N NE2 . HIS B 2348 78 . -1.577 15.400 36.074 1.00 22.36 ? ? ? ? ? . 78 HIS B NE2 2348 ATOM 1945 N N . ASP B 2348 79 . -4.044 16.334 29.863 1.00 17.23 ? ? ? ? ? . 79 ASP B N 2348 ATOM 1946 C CA . ASP B 2348 79 . -4.809 17.007 28.812 1.00 18.76 ? ? ? ? ? . 79 ASP B CA 2348 ATOM 1947 C C . ASP B 2348 79 . -6.208 16.401 28.687 1.00 16.45 ? ? ? ? ? . 79 ASP B C 2348 ATOM 1948 O O . ASP B 2348 79 . -7.200 17.117 28.642 1.00 15.60 ? ? ? ? ? . 79 ASP B O 2348 ATOM 1949 C CB . ASP B 2348 79 . -4.066 16.918 27.481 1.00 20.61 ? ? ? ? ? . 79 ASP B CB 2348 ATOM 1950 C CG . ASP B 2348 79 . -4.800 17.602 26.350 1.00 24.25 ? ? ? ? ? . 79 ASP B CG 2348 ATOM 1951 O OD1 . ASP B 2348 79 . -4.755 18.849 26.268 1.00 26.86 ? ? ? ? ? . 79 ASP B OD1 2348 ATOM 1952 O OD2 . ASP B 2348 79 . -5.416 16.883 25.534 1.00 27.35 ? ? ? ? ? 1- 79 ASP B OD2 2348 ATOM 1953 N N A TYR B 2348 80 . -6.218 15.075 28.656 0.75 17.30 ? ? ? ? ? . 80 TYR B N 2348 ATOM 1954 N N B TYR B 2348 80 . -6.333 15.079 28.645 0.25 15.42 ? ? ? ? ? . 80 TYR B N 2348 ATOM 1955 C CA A TYR B 2348 80 . -7.403 14.258 28.526 0.75 17.12 ? ? ? ? ? . 80 TYR B CA 2348 ATOM 1956 C CA B TYR B 2348 80 . -7.669 14.505 28.437 0.25 14.69 ? ? ? ? ? . 80 TYR B CA 2348 ATOM 1957 C C A TYR B 2348 80 . -8.387 14.510 29.684 0.75 17.25 ? ? ? ? ? . 80 TYR B C 2348 ATOM 1958 C C B TYR B 2348 80 . -8.505 14.348 29.715 0.25 15.60 ? ? ? ? ? . 80 TYR B C 2348 ATOM 1959 O O A TYR B 2348 80 . -9.548 14.887 29.472 0.75 17.68 ? ? ? ? ? . 80 TYR B O 2348 ATOM 1960 O O B TYR B 2348 80 . -9.730 14.238 29.614 0.25 15.85 ? ? ? ? ? . 80 TYR B O 2348 ATOM 1961 C CB A TYR B 2348 80 . -6.947 12.779 28.473 0.75 19.75 ? ? ? ? ? . 80 TYR B CB 2348 ATOM 1962 C CB B TYR B 2348 80 . -7.620 13.232 27.594 0.25 13.59 ? ? ? ? ? . 80 TYR B CB 2348 ATOM 1963 C CG A TYR B 2348 80 . -8.040 11.764 28.299 0.75 19.82 ? ? ? ? ? . 80 TYR B CG 2348 ATOM 1964 C CG B TYR B 2348 80 . -7.652 11.923 28.323 0.25 12.64 ? ? ? ? ? . 80 TYR B CG 2348 ATOM 1965 C CD1 A TYR B 2348 80 . -9.071 11.977 27.394 0.75 22.62 ? ? ? ? ? . 80 TYR B CD1 2348 ATOM 1966 C CD2 A TYR B 2348 80 . -8.031 10.564 29.011 0.75 20.66 ? ? ? ? ? . 80 TYR B CD2 2348 ATOM 1967 C CD1 B TYR B 2348 80 . -6.607 11.540 29.141 0.25 12.20 ? ? ? ? ? . 80 TYR B CD1 2348 ATOM 1968 C CD2 B TYR B 2348 80 . -8.709 11.040 28.144 0.25 12.38 ? ? ? ? ? . 80 TYR B CD2 2348 ATOM 1969 C CE1 A TYR B 2348 80 . -10.072 11.043 27.217 0.75 21.39 ? ? ? ? ? . 80 TYR B CE1 2348 ATOM 1970 C CE2 A TYR B 2348 80 . -9.026 9.619 28.828 0.75 19.95 ? ? ? ? ? . 80 TYR B CE2 2348 ATOM 1971 C CE1 B TYR B 2348 80 . -6.623 10.325 29.788 0.25 12.04 ? ? ? ? ? . 80 TYR B CE1 2348 ATOM 1972 C CE2 B TYR B 2348 80 . -8.730 9.820 28.776 0.25 12.02 ? ? ? ? ? . 80 TYR B CE2 2348 ATOM 1973 C CZ A TYR B 2348 80 . -10.042 9.862 27.921 0.75 20.46 ? ? ? ? ? . 80 TYR B CZ 2348 ATOM 1974 C CZ B TYR B 2348 80 . -7.686 9.470 29.596 0.25 11.93 ? ? ? ? ? . 80 TYR B CZ 2348 ATOM 1975 O OH A TYR B 2348 80 . -11.080 8.979 27.733 0.75 19.80 ? ? ? ? ? . 80 TYR B OH 2348 ATOM 1976 O OH B TYR B 2348 80 . -7.698 8.260 30.223 0.25 11.61 ? ? ? ? ? . 80 TYR B OH 2348 ATOM 1977 N N . TYR B 2348 81 . -7.879 14.343 30.898 1.00 16.13 ? ? ? ? ? . 81 TYR B N 2348 ATOM 1978 C CA . TYR B 2348 81 . -8.640 14.508 32.140 1.00 16.72 ? ? ? ? ? . 81 TYR B CA 2348 ATOM 1979 C C . TYR B 2348 81 . -9.094 15.980 32.334 1.00 17.50 ? ? ? ? ? . 81 TYR B C 2348 ATOM 1980 O O . TYR B 2348 81 . -10.201 16.233 32.822 1.00 16.04 ? ? ? ? ? . 81 TYR B O 2348 ATOM 1981 C CB . TYR B 2348 81 . -7.863 13.991 33.382 1.00 17.47 ? ? ? ? ? . 81 TYR B CB 2348 ATOM 1982 C CG . TYR B 2348 81 . -8.551 14.403 34.640 1.00 17.17 ? ? ? ? ? . 81 TYR B CG 2348 ATOM 1983 C CD1 . TYR B 2348 81 . -9.853 13.975 34.896 1.00 17.53 ? ? ? ? ? . 81 TYR B CD1 2348 ATOM 1984 C CD2 . TYR B 2348 81 . -7.970 15.303 35.523 1.00 17.37 ? ? ? ? ? . 81 TYR B CD2 2348 ATOM 1985 C CE1 . TYR B 2348 81 . -10.531 14.408 36.021 1.00 17.74 ? ? ? ? ? . 81 TYR B CE1 2348 ATOM 1986 C CE2 . TYR B 2348 81 . -8.644 15.731 36.654 1.00 18.24 ? ? ? ? ? . 81 TYR B CE2 2348 ATOM 1987 C CZ . TYR B 2348 81 . -9.926 15.287 36.893 1.00 18.24 ? ? ? ? ? . 81 TYR B CZ 2348 ATOM 1988 O OH . TYR B 2348 81 . -10.599 15.711 38.016 1.00 18.62 ? ? ? ? ? . 81 TYR B OH 2348 ATOM 1989 N N . GLY B 2348 82 . -8.252 16.930 31.935 1.00 16.13 ? ? ? ? ? . 82 GLY B N 2348 ATOM 1990 C CA . GLY B 2348 82 . -8.599 18.338 31.970 1.00 16.93 ? ? ? ? ? . 82 GLY B CA 2348 ATOM 1991 C C . GLY B 2348 82 . -9.946 18.666 31.345 1.00 17.49 ? ? ? ? ? . 82 GLY B C 2348 ATOM 1992 O O . GLY B 2348 82 . -10.647 19.548 31.829 1.00 16.88 ? ? ? ? ? . 82 GLY B O 2348 ATOM 1993 N N . LYS B 2348 83 . -10.310 17.941 30.288 1.00 18.69 ? ? ? ? ? . 83 LYS B N 2348 ATOM 1994 C CA . LYS B 2348 83 . -11.560 18.194 29.551 1.00 20.72 ? ? ? ? ? . 83 LYS B CA 2348 ATOM 1995 C C . LYS B 2348 83 . -12.777 17.454 30.090 1.00 21.80 ? ? ? ? ? . 83 LYS B C 2348 ATOM 1996 O O . LYS B 2348 83 . -13.892 17.664 29.595 1.00 21.26 ? ? ? ? ? . 83 LYS B O 2348 ATOM 1997 C CB . LYS B 2348 83 . -11.357 17.854 28.073 1.00 21.83 ? ? ? ? ? . 83 LYS B CB 2348 ATOM 1998 C CG . LYS B 2348 83 . -10.329 18.748 27.429 1.00 22.78 ? ? ? ? ? . 83 LYS B CG 2348 ATOM 1999 C CD . LYS B 2348 83 . -10.121 18.447 25.961 1.00 24.60 ? ? ? ? ? . 83 LYS B CD 2348 ATOM 2000 C CE . LYS B 2348 83 . -8.850 19.122 25.477 1.00 28.02 ? ? ? ? ? . 83 LYS B CE 2348 ATOM 2001 N NZ . LYS B 2348 83 . -8.602 18.925 24.023 1.00 30.17 ? ? ? ? ? 1+ 83 LYS B NZ 2348 ATOM 2002 N N . MET B 2348 84 . -12.563 16.577 31.073 1.00 20.82 ? ? ? ? ? . 84 MET B N 2348 ATOM 2003 C CA . MET B 2348 84 . -13.635 15.814 31.708 1.00 21.27 ? ? ? ? ? . 84 MET B CA 2348 ATOM 2004 C C . MET B 2348 84 . -14.193 16.598 32.884 1.00 22.00 ? ? ? ? ? . 84 MET B C 2348 ATOM 2005 O O . MET B 2348 84 . -13.534 17.523 33.357 1.00 23.51 ? ? ? ? ? . 84 MET B O 2348 ATOM 2006 C CB . MET B 2348 84 . -13.118 14.469 32.193 1.00 19.77 ? ? ? ? ? . 84 MET B CB 2348 ATOM 2007 C CG . MET B 2348 84 . -12.706 13.549 31.072 1.00 19.50 ? ? ? ? ? . 84 MET B CG 2348 ATOM 2008 S SD . MET B 2348 84 . -11.882 12.101 31.749 1.00 19.88 ? ? ? ? ? . 84 MET B SD 2348 ATOM 2009 C CE . MET B 2348 84 . -11.718 11.109 30.270 1.00 20.94 ? ? ? ? ? . 84 MET B CE 2348 ATOM 2010 N N . PRO B 2348 85 . -15.411 16.248 33.352 1.00 20.76 ? ? ? ? ? . 85 PRO B N 2348 ATOM 2011 C CA . PRO B 2348 85 . -16.043 17.010 34.433 1.00 19.33 ? ? ? ? ? . 85 PRO B CA 2348 ATOM 2012 C C . PRO B 2348 85 . -15.858 16.459 35.847 1.00 18.20 ? ? ? ? ? . 85 PRO B C 2348 ATOM 2013 O O . PRO B 2348 85 . -16.214 17.136 36.814 1.00 18.87 ? ? ? ? ? . 85 PRO B O 2348 ATOM 2014 C CB . PRO B 2348 85 . -17.523 16.975 34.043 1.00 20.30 ? ? ? ? ? . 85 PRO B CB 2348 ATOM 2015 C CG . PRO B 2348 85 . -17.690 15.664 33.349 1.00 20.64 ? ? ? ? ? . 85 PRO B CG 2348 ATOM 2016 C CD . PRO B 2348 85 . -16.360 15.315 32.717 1.00 19.64 ? ? ? ? ? . 85 PRO B CD 2348 ATOM 2017 N N . TRP B 2348 86 . -15.245 15.279 35.975 1.00 16.54 ? ? ? ? ? . 86 TRP B N 2348 ATOM 2018 C CA . TRP B 2348 86 . -15.322 14.466 37.192 1.00 16.95 ? ? ? ? ? . 86 TRP B CA 2348 ATOM 2019 C C . TRP B 2348 86 . -13.931 14.316 37.872 1.00 16.70 ? ? ? ? ? . 86 TRP B C 2348 ATOM 2020 O O . TRP B 2348 86 . -13.138 15.253 37.827 1.00 18.08 ? ? ? ? ? . 86 TRP B O 2348 ATOM 2021 C CB . TRP B 2348 86 . -15.991 13.136 36.856 1.00 17.51 ? ? ? ? ? . 86 TRP B CB 2348 ATOM 2022 C CG . TRP B 2348 86 . -15.446 12.465 35.622 1.00 17.81 ? ? ? ? ? . 86 TRP B CG 2348 ATOM 2023 C CD1 . TRP B 2348 86 . -14.152 12.120 35.374 1.00 17.90 ? ? ? ? ? . 86 TRP B CD1 2348 ATOM 2024 C CD2 . TRP B 2348 86 . -16.185 12.099 34.457 1.00 17.07 ? ? ? ? ? . 86 TRP B CD2 2348 ATOM 2025 C CE2 . TRP B 2348 86 . -15.268 11.526 33.545 1.00 17.35 ? ? ? ? ? . 86 TRP B CE2 2348 ATOM 2026 C CE3 . TRP B 2348 86 . -17.535 12.187 34.096 1.00 17.36 ? ? ? ? ? . 86 TRP B CE3 2348 ATOM 2027 N NE1 . TRP B 2348 86 . -14.037 11.558 34.135 1.00 17.06 ? ? ? ? ? . 86 TRP B NE1 2348 ATOM 2028 C CZ2 . TRP B 2348 86 . -15.654 11.038 32.287 1.00 16.49 ? ? ? ? ? . 86 TRP B CZ2 2348 ATOM 2029 C CZ3 . TRP B 2348 86 . -17.925 11.708 32.854 1.00 17.25 ? ? ? ? ? . 86 TRP B CZ3 2348 ATOM 2030 C CH2 . TRP B 2348 86 . -16.984 11.145 31.953 1.00 17.92 ? ? ? ? ? . 86 TRP B CH2 2348 ATOM 2031 N N . LEU B 2348 87 . -13.625 13.161 38.465 1.00 16.41 ? ? ? ? ? . 87 LEU B N 2348 ATOM 2032 C CA . LEU B 2348 87 . -12.401 12.963 39.230 1.00 14.55 ? ? ? ? ? . 87 LEU B CA 2348 ATOM 2033 C C . LEU B 2348 87 . -11.466 12.019 38.498 1.00 16.57 ? ? ? ? ? . 87 LEU B C 2348 ATOM 2034 O O . LEU B 2348 87 . -11.854 11.400 37.515 1.00 17.83 ? ? ? ? ? . 87 LEU B O 2348 ATOM 2035 C CB . LEU B 2348 87 . -12.740 12.359 40.588 1.00 15.07 ? ? ? ? ? . 87 LEU B CB 2348 ATOM 2036 C CG . LEU B 2348 87 . -13.758 13.084 41.461 1.00 15.98 ? ? ? ? ? . 87 LEU B CG 2348 ATOM 2037 C CD1 . LEU B 2348 87 . -13.923 12.349 42.771 1.00 17.46 ? ? ? ? ? . 87 LEU B CD1 2348 ATOM 2038 C CD2 . LEU B 2348 87 . -13.319 14.486 41.736 1.00 17.54 ? ? ? ? ? . 87 LEU B CD2 2348 ATOM 2039 N N . ALA B 2348 88 . -10.230 11.911 38.973 1.00 16.57 ? ? ? ? ? . 88 ALA B N 2348 ATOM 2040 C CA . ALA B 2348 88 . -9.283 10.961 38.396 1.00 16.36 ? ? ? ? ? . 88 ALA B CA 2348 ATOM 2041 C C . ALA B 2348 88 . -8.323 10.412 39.434 1.00 15.96 ? ? ? ? ? . 88 ALA B C 2348 ATOM 2042 O O . ALA B 2348 88 . -7.891 11.115 40.346 1.00 15.90 ? ? ? ? ? . 88 ALA B O 2348 ATOM 2043 C CB . ALA B 2348 88 . -8.501 11.609 37.260 1.00 17.50 ? ? ? ? ? . 88 ALA B CB 2348 ATOM 2044 N N . LEU B 2348 89 . -7.990 9.136 39.275 1.00 17.02 ? ? ? ? ? . 89 LEU B N 2348 ATOM 2045 C CA . LEU B 2348 89 . -6.879 8.537 40.014 1.00 16.46 ? ? ? ? ? . 89 LEU B CA 2348 ATOM 2046 C C . LEU B 2348 89 . -5.615 9.205 39.475 1.00 16.33 ? ? ? ? ? . 89 LEU B C 2348 ATOM 2047 O O . LEU B 2348 89 . -5.440 9.269 38.238 1.00 16.60 ? ? ? ? ? . 89 LEU B O 2348 ATOM 2048 C CB . LEU B 2348 89 . -6.824 7.035 39.770 1.00 17.31 ? ? ? ? ? . 89 LEU B CB 2348 ATOM 2049 C CG . LEU B 2348 89 . -5.809 6.233 40.587 1.00 18.05 ? ? ? ? ? . 89 LEU B CG 2348 ATOM 2050 C CD1 . LEU B 2348 89 . -6.200 6.221 42.055 1.00 20.17 ? ? ? ? ? . 89 LEU B CD1 2348 ATOM 2051 C CD2 . LEU B 2348 89 . -5.715 4.824 40.026 1.00 18.99 ? ? ? ? ? . 89 LEU B CD2 2348 ATOM 2052 N N . PRO B 2348 90 . -4.742 9.705 40.367 1.00 16.37 ? ? ? ? ? . 90 PRO B N 2348 ATOM 2053 C CA . PRO B 2348 90 . -3.571 10.431 39.892 1.00 16.40 ? ? ? ? ? . 90 PRO B CA 2348 ATOM 2054 C C . PRO B 2348 90 . -2.658 9.608 38.990 1.00 16.81 ? ? ? ? ? . 90 PRO B C 2348 ATOM 2055 O O . PRO B 2348 90 . -2.636 8.362 39.054 1.00 15.83 ? ? ? ? ? . 90 PRO B O 2348 ATOM 2056 C CB . PRO B 2348 90 . -2.851 10.810 41.181 1.00 17.22 ? ? ? ? ? . 90 PRO B CB 2348 ATOM 2057 C CG . PRO B 2348 90 . -3.955 10.949 42.178 1.00 18.64 ? ? ? ? ? . 90 PRO B CG 2348 ATOM 2058 C CD . PRO B 2348 90 . -4.875 9.819 41.833 1.00 17.87 ? ? ? ? ? . 90 PRO B CD 2348 ATOM 2059 N N . PHE B 2348 91 . -1.912 10.306 38.150 1.00 16.95 ? ? ? ? ? . 91 PHE B N 2348 ATOM 2060 C CA . PHE B 2348 91 . -0.984 9.620 37.268 1.00 16.32 ? ? ? ? ? . 91 PHE B CA 2348 ATOM 2061 C C . PHE B 2348 91 . 0.043 8.771 38.029 1.00 16.14 ? ? ? ? ? . 91 PHE B C 2348 ATOM 2062 O O . PHE B 2348 91 . 0.493 7.737 37.501 1.00 15.16 ? ? ? ? ? . 91 PHE B O 2348 ATOM 2063 C CB . PHE B 2348 91 . -0.273 10.597 36.345 1.00 15.66 ? ? ? ? ? . 91 PHE B CB 2348 ATOM 2064 C CG . PHE B 2348 91 . 0.595 9.920 35.332 1.00 15.90 ? ? ? ? ? . 91 PHE B CG 2348 ATOM 2065 C CD1 . PHE B 2348 91 . 0.040 9.360 34.195 1.00 16.28 ? ? ? ? ? . 91 PHE B CD1 2348 ATOM 2066 C CD2 . PHE B 2348 91 . 1.970 9.805 35.545 1.00 14.93 ? ? ? ? ? . 91 PHE B CD2 2348 ATOM 2067 C CE1 . PHE B 2348 91 . 0.850 8.722 33.258 1.00 16.87 ? ? ? ? ? . 91 PHE B CE1 2348 ATOM 2068 C CE2 . PHE B 2348 91 . 2.779 9.154 34.629 1.00 15.84 ? ? ? ? ? . 91 PHE B CE2 2348 ATOM 2069 C CZ . PHE B 2348 91 . 2.225 8.610 33.484 1.00 15.95 ? ? ? ? ? . 91 PHE B CZ 2348 ATOM 2070 N N . ASP B 2348 92 . 0.414 9.169 39.251 1.00 17.39 ? ? ? ? ? . 92 ASP B N 2348 ATOM 2071 C CA . ASP B 2348 92 . 1.409 8.390 40.023 1.00 19.84 ? ? ? ? ? . 92 ASP B CA 2348 ATOM 2072 C C . ASP B 2348 92 . 0.920 7.009 40.500 1.00 18.70 ? ? ? ? ? . 92 ASP B C 2348 ATOM 2073 O O . ASP B 2348 92 . 1.689 6.251 41.095 1.00 17.34 ? ? ? ? ? . 92 ASP B O 2348 ATOM 2074 C CB . ASP B 2348 92 . 2.017 9.195 41.182 1.00 23.77 ? ? ? ? ? . 92 ASP B CB 2348 ATOM 2075 C CG . ASP B 2348 92 . 1.025 9.518 42.290 1.00 27.83 ? ? ? ? ? . 92 ASP B CG 2348 ATOM 2076 O OD1 . ASP B 2348 92 . -0.133 9.067 42.259 1.00 32.30 ? ? ? ? ? . 92 ASP B OD1 2348 ATOM 2077 O OD2 . ASP B 2348 92 . 1.423 10.254 43.209 1.00 34.80 ? ? ? ? ? 1- 92 ASP B OD2 2348 ATOM 2078 N N . GLN B 2348 93 . -0.349 6.696 40.239 1.00 16.99 ? ? ? ? ? . 93 GLN B N 2348 ATOM 2079 C CA . GLN B 2348 93 . -0.886 5.361 40.461 1.00 17.43 ? ? ? ? ? . 93 GLN B CA 2348 ATOM 2080 C C . GLN B 2348 93 . -0.942 4.506 39.196 1.00 16.35 ? ? ? ? ? . 93 GLN B C 2348 ATOM 2081 O O . GLN B 2348 93 . -1.478 3.408 39.235 1.00 16.83 ? ? ? ? ? . 93 GLN B O 2348 ATOM 2082 C CB . GLN B 2348 93 . -2.288 5.477 41.064 1.00 18.99 ? ? ? ? ? . 93 GLN B CB 2348 ATOM 2083 C CG . GLN B 2348 93 . -2.320 6.261 42.358 1.00 20.51 ? ? ? ? ? . 93 GLN B CG 2348 ATOM 2084 C CD . GLN B 2348 93 . -1.539 5.571 43.445 1.00 22.84 ? ? ? ? ? . 93 GLN B CD 2348 ATOM 2085 N NE2 . GLN B 2348 93 . -0.516 6.241 43.965 1.00 22.79 ? ? ? ? ? . 93 GLN B NE2 2348 ATOM 2086 O OE1 . GLN B 2348 93 . -1.836 4.424 43.797 1.00 23.59 ? ? ? ? ? . 93 GLN B OE1 2348 ATOM 2087 N N . ARG B 2348 94 . -0.395 4.997 38.082 1.00 17.24 ? ? ? ? ? . 94 ARG B N 2348 ATOM 2088 C CA . ARG B 2348 94 . -0.444 4.275 36.806 1.00 16.88 ? ? ? ? ? . 94 ARG B CA 2348 ATOM 2089 C C . ARG B 2348 94 . 0.105 2.829 36.885 1.00 16.61 ? ? ? ? ? . 94 ARG B C 2348 ATOM 2090 O O . ARG B 2348 94 . -0.405 1.942 36.208 1.00 17.97 ? ? ? ? ? . 94 ARG B O 2348 ATOM 2091 C CB . ARG B 2348 94 . 0.281 5.072 35.707 1.00 17.63 ? ? ? ? ? . 94 ARG B CB 2348 ATOM 2092 C CG . ARG B 2348 94 . 0.329 4.393 34.334 1.00 19.00 ? ? ? ? ? . 94 ARG B CG 2348 ATOM 2093 C CD . ARG B 2348 94 . -1.058 4.079 33.804 1.00 17.72 ? ? ? ? ? . 94 ARG B CD 2348 ATOM 2094 N NE . ARG B 2348 94 . -1.060 3.417 32.503 1.00 17.08 ? ? ? ? ? . 94 ARG B NE 2348 ATOM 2095 C CZ . ARG B 2348 94 . -0.901 2.110 32.284 1.00 17.71 ? ? ? ? ? . 94 ARG B CZ 2348 ATOM 2096 N NH1 . ARG B 2348 94 . -0.665 1.259 33.283 1.00 19.74 ? ? ? ? ? 1+ 94 ARG B NH1 2348 ATOM 2097 N NH2 . ARG B 2348 94 . -0.952 1.649 31.033 1.00 16.77 ? ? ? ? ? . 94 ARG B NH2 2348 ATOM 2098 N N . SER B 2348 95 . 1.110 2.589 37.724 1.00 16.31 ? ? ? ? ? . 95 SER B N 2348 ATOM 2099 C CA . SER B 2348 95 . 1.672 1.234 37.903 1.00 16.21 ? ? ? ? ? . 95 SER B CA 2348 ATOM 2100 C C . SER B 2348 95 . 0.683 0.205 38.487 1.00 17.13 ? ? ? ? ? . 95 SER B C 2348 ATOM 2101 O O . SER B 2348 95 . 0.927 -0.996 38.403 1.00 19.32 ? ? ? ? ? . 95 SER B O 2348 ATOM 2102 C CB . SER B 2348 95 . 2.920 1.280 38.787 1.00 15.66 ? ? ? ? ? . 95 SER B CB 2348 ATOM 2103 O OG . SER B 2348 95 . 2.575 1.563 40.126 1.00 14.53 ? ? ? ? ? . 95 SER B OG 2348 ATOM 2104 N N . THR B 2348 96 . -0.421 0.682 39.062 1.00 16.77 ? ? ? ? ? . 96 THR B N 2348 ATOM 2105 C CA . THR B 2348 96 . -1.479 -0.163 39.608 1.00 16.98 ? ? ? ? ? . 96 THR B CA 2348 ATOM 2106 C C . THR B 2348 96 . -2.621 -0.451 38.641 1.00 16.70 ? ? ? ? ? . 96 THR B C 2348 ATOM 2107 O O . THR B 2348 96 . -3.480 -1.274 38.956 1.00 16.12 ? ? ? ? ? . 96 THR B O 2348 ATOM 2108 C CB . THR B 2348 96 . -2.103 0.475 40.877 1.00 16.65 ? ? ? ? ? . 96 THR B CB 2348 ATOM 2109 C CG2 . THR B 2348 96 . -1.027 0.868 41.859 1.00 16.78 ? ? ? ? ? . 96 THR B CG2 2348 ATOM 2110 O OG1 . THR B 2348 96 . -2.918 1.611 40.536 1.00 17.39 ? ? ? ? ? . 96 THR B OG1 2348 ATOM 2111 N N . VAL B 2348 97 . -2.645 0.212 37.484 1.00 15.95 ? ? ? ? ? . 97 VAL B N 2348 ATOM 2112 C CA . VAL B 2348 97 . -3.832 0.207 36.622 1.00 15.76 ? ? ? ? ? . 97 VAL B CA 2348 ATOM 2113 C C . VAL B 2348 97 . -4.077 -1.175 36.010 1.00 15.32 ? ? ? ? ? . 97 VAL B C 2348 ATOM 2114 O O . VAL B 2348 97 . -5.210 -1.640 36.009 1.00 15.15 ? ? ? ? ? . 97 VAL B O 2348 ATOM 2115 C CB . VAL B 2348 97 . -3.749 1.265 35.510 1.00 15.29 ? ? ? ? ? . 97 VAL B CB 2348 ATOM 2116 C CG1 . VAL B 2348 97 . -4.886 1.099 34.503 1.00 16.21 ? ? ? ? ? . 97 VAL B CG1 2348 ATOM 2117 C CG2 . VAL B 2348 97 . -3.809 2.652 36.114 1.00 16.16 ? ? ? ? ? . 97 VAL B CG2 2348 ATOM 2118 N N . SER B 2348 98 . -3.022 -1.815 35.518 1.00 16.70 ? ? ? ? ? . 98 SER B N 2348 ATOM 2119 C CA . SER B 2348 98 . -3.121 -3.162 34.944 1.00 17.78 ? ? ? ? ? . 98 SER B CA 2348 ATOM 2120 C C . SER B 2348 98 . -3.711 -4.159 35.943 1.00 17.26 ? ? ? ? ? . 98 SER B C 2348 ATOM 2121 O O . SER B 2348 98 . -4.674 -4.865 35.619 1.00 17.51 ? ? ? ? ? . 98 SER B O 2348 ATOM 2122 C CB . SER B 2348 98 . -1.752 -3.661 34.430 1.00 18.21 ? ? ? ? ? . 98 SER B CB 2348 ATOM 2123 O OG . SER B 2348 98 . -1.807 -5.045 34.069 1.00 20.56 ? ? ? ? ? . 98 SER B OG 2348 ATOM 2124 N N . GLU B 2348 99 . -3.143 -4.226 37.148 1.00 17.06 ? ? ? ? ? . 99 GLU B N 2348 ATOM 2125 C CA . GLU B 2348 99 . -3.667 -5.155 38.154 1.00 17.20 ? ? ? ? ? . 99 GLU B CA 2348 ATOM 2126 C C . GLU B 2348 99 . -5.072 -4.783 38.623 1.00 17.25 ? ? ? ? ? . 99 GLU B C 2348 ATOM 2127 O O . GLU B 2348 99 . -5.868 -5.674 38.935 1.00 15.69 ? ? ? ? ? . 99 GLU B O 2348 ATOM 2128 C CB . GLU B 2348 99 . -2.720 -5.319 39.348 1.00 18.28 ? ? ? ? ? . 99 GLU B CB 2348 ATOM 2129 C CG . GLU B 2348 99 . -1.454 -6.112 39.035 1.00 19.77 ? ? ? ? ? . 99 GLU B CG 2348 ATOM 2130 C CD . GLU B 2348 99 . -1.704 -7.546 38.571 1.00 22.07 ? ? ? ? ? . 99 GLU B CD 2348 ATOM 2131 O OE1 . GLU B 2348 99 . -2.608 -8.234 39.099 1.00 21.98 ? ? ? ? ? . 99 GLU B OE1 2348 ATOM 2132 O OE2 . GLU B 2348 99 . -0.970 -7.999 37.671 1.00 22.99 ? ? ? ? ? 1- 99 GLU B OE2 2348 ATOM 2133 N N A LEU B 2348 100 . -5.370 -3.482 38.680 0.49 17.03 ? ? ? ? ? . 100 LEU B N 2348 ATOM 2134 N N B LEU B 2348 100 . -5.386 -3.488 38.661 0.51 16.95 ? ? ? ? ? . 100 LEU B N 2348 ATOM 2135 C CA A LEU B 2348 100 . -6.731 -3.011 38.953 0.49 18.24 ? ? ? ? ? . 100 LEU B CA 2348 ATOM 2136 C CA B LEU B 2348 100 . -6.748 -3.063 38.997 0.51 18.11 ? ? ? ? ? . 100 LEU B CA 2348 ATOM 2137 C C A LEU B 2348 100 . -7.730 -3.589 37.945 0.49 18.23 ? ? ? ? ? . 100 LEU B C 2348 ATOM 2138 C C B LEU B 2348 100 . -7.752 -3.577 37.944 0.51 18.21 ? ? ? ? ? . 100 LEU B C 2348 ATOM 2139 O O A LEU B 2348 100 . -8.764 -4.145 38.323 0.49 18.26 ? ? ? ? ? . 100 LEU B O 2348 ATOM 2140 O O B LEU B 2348 100 . -8.818 -4.088 38.298 0.51 18.44 ? ? ? ? ? . 100 LEU B O 2348 ATOM 2141 C CB A LEU B 2348 100 . -6.786 -1.489 38.904 0.49 18.06 ? ? ? ? ? . 100 LEU B CB 2348 ATOM 2142 C CB B LEU B 2348 100 . -6.832 -1.543 39.150 0.51 17.78 ? ? ? ? ? . 100 LEU B CB 2348 ATOM 2143 C CG A LEU B 2348 100 . -6.484 -0.751 40.200 0.49 18.12 ? ? ? ? ? . 100 LEU B CG 2348 ATOM 2144 C CG B LEU B 2348 100 . -8.092 -1.031 39.858 0.51 17.55 ? ? ? ? ? . 100 LEU B CG 2348 ATOM 2145 C CD1 A LEU B 2348 100 . -6.557 0.747 39.948 0.49 17.99 ? ? ? ? ? . 100 LEU B CD1 2348 ATOM 2146 C CD2 A LEU B 2348 100 . -7.443 -1.195 41.299 0.49 19.03 ? ? ? ? ? . 100 LEU B CD2 2348 ATOM 2147 C CD1 B LEU B 2348 100 . -8.094 -1.376 41.349 0.51 17.86 ? ? ? ? ? . 100 LEU B CD1 2348 ATOM 2148 C CD2 B LEU B 2348 100 . -8.232 0.466 39.661 0.51 18.12 ? ? ? ? ? . 100 LEU B CD2 2348 ATOM 2149 N N . GLY B 2348 101 . -7.400 -3.464 36.664 1.00 18.06 ? ? ? ? ? . 101 GLY B N 2348 ATOM 2150 C CA . GLY B 2348 101 . -8.206 -4.062 35.585 1.00 19.07 ? ? ? ? ? . 101 GLY B CA 2348 ATOM 2151 C C . GLY B 2348 101 . -8.386 -5.570 35.750 1.00 17.32 ? ? ? ? ? . 101 GLY B C 2348 ATOM 2152 O O . GLY B 2348 101 . -9.493 -6.087 35.597 1.00 18.58 ? ? ? ? ? . 101 GLY B O 2348 ATOM 2153 N N . LYS B 2348 102 . -7.307 -6.267 36.093 1.00 16.19 ? ? ? ? ? . 102 LYS B N 2348 ATOM 2154 C CA . LYS B 2348 102 . -7.359 -7.714 36.299 1.00 17.21 ? ? ? ? ? . 102 LYS B CA 2348 ATOM 2155 C C . LYS B 2348 102 . -8.251 -8.074 37.468 1.00 16.89 ? ? ? ? ? . 102 LYS B C 2348 ATOM 2156 O O . LYS B 2348 102 . -8.994 -9.048 37.402 1.00 15.61 ? ? ? ? ? . 102 LYS B O 2348 ATOM 2157 C CB . LYS B 2348 102 . -5.988 -8.296 36.592 1.00 19.27 ? ? ? ? ? . 102 LYS B CB 2348 ATOM 2158 C CG . LYS B 2348 102 . -5.054 -8.400 35.410 1.00 22.58 ? ? ? ? ? . 102 LYS B CG 2348 ATOM 2159 C CD . LYS B 2348 102 . -3.933 -9.364 35.782 1.00 25.96 ? ? ? ? ? . 102 LYS B CD 2348 ATOM 2160 C CE . LYS B 2348 102 . -2.604 -8.938 35.215 1.00 29.86 ? ? ? ? ? . 102 LYS B CE 2348 ATOM 2161 N NZ . LYS B 2348 102 . -1.511 -9.795 35.762 1.00 31.62 ? ? ? ? ? 1+ 102 LYS B NZ 2348 ATOM 2162 N N . THR B 2348 103 . -8.164 -7.288 38.538 1.00 16.61 ? ? ? ? ? . 103 THR B N 2348 ATOM 2163 C CA . THR B 2348 103 . -8.990 -7.508 39.735 1.00 17.16 ? ? ? ? ? . 103 THR B CA 2348 ATOM 2164 C C . THR B 2348 103 . -10.494 -7.450 39.412 1.00 16.65 ? ? ? ? ? . 103 THR B C 2348 ATOM 2165 O O . THR B 2348 103 . -11.278 -8.237 39.953 1.00 18.21 ? ? ? ? ? . 103 THR B O 2348 ATOM 2166 C CB . THR B 2348 103 . -8.658 -6.470 40.842 1.00 17.12 ? ? ? ? ? . 103 THR B CB 2348 ATOM 2167 C CG2 . THR B 2348 103 . -9.615 -6.587 42.020 1.00 17.45 ? ? ? ? ? . 103 THR B CG2 2348 ATOM 2168 O OG1 . THR B 2348 103 . -7.320 -6.677 41.310 1.00 16.38 ? ? ? ? ? . 103 THR B OG1 2348 ATOM 2169 N N . PHE B 2348 104 . -10.879 -6.530 38.536 1.00 15.70 ? ? ? ? ? . 104 PHE B N 2348 ATOM 2170 C CA . PHE B 2348 104 . -12.294 -6.337 38.179 1.00 17.76 ? ? ? ? ? . 104 PHE B CA 2348 ATOM 2171 C C . PHE B 2348 104 . -12.747 -7.074 36.907 1.00 18.79 ? ? ? ? ? . 104 PHE B C 2348 ATOM 2172 O O . PHE B 2348 104 . -13.915 -6.939 36.501 1.00 20.78 ? ? ? ? ? . 104 PHE B O 2348 ATOM 2173 C CB . PHE B 2348 104 . -12.604 -4.847 38.050 1.00 17.44 ? ? ? ? ? . 104 PHE B CB 2348 ATOM 2174 C CG . PHE B 2348 104 . -12.388 -4.055 39.319 1.00 19.30 ? ? ? ? ? . 104 PHE B CG 2348 ATOM 2175 C CD1 . PHE B 2348 104 . -12.955 -4.455 40.525 1.00 20.46 ? ? ? ? ? . 104 PHE B CD1 2348 ATOM 2176 C CD2 . PHE B 2348 104 . -11.632 -2.877 39.301 1.00 19.35 ? ? ? ? ? . 104 PHE B CD2 2348 ATOM 2177 C CE1 . PHE B 2348 104 . -12.761 -3.707 41.684 1.00 20.50 ? ? ? ? ? . 104 PHE B CE1 2348 ATOM 2178 C CE2 . PHE B 2348 104 . -11.446 -2.126 40.453 1.00 20.68 ? ? ? ? ? . 104 PHE B CE2 2348 ATOM 2179 C CZ . PHE B 2348 104 . -12.012 -2.547 41.646 1.00 20.25 ? ? ? ? ? . 104 PHE B CZ 2348 ATOM 2180 N N . GLY B 2348 105 . -11.847 -7.847 36.306 1.00 16.85 ? ? ? ? ? . 105 GLY B N 2348 ATOM 2181 C CA . GLY B 2348 105 . -12.113 -8.598 35.074 1.00 18.18 ? ? ? ? ? . 105 GLY B CA 2348 ATOM 2182 C C . GLY B 2348 105 . -12.337 -7.691 33.882 1.00 18.23 ? ? ? ? ? . 105 GLY B C 2348 ATOM 2183 O O . GLY B 2348 105 . -13.190 -7.968 33.053 1.00 19.24 ? ? ? ? ? . 105 GLY B O 2348 ATOM 2184 N N . VAL B 2348 106 . -11.565 -6.611 33.802 1.00 17.92 ? ? ? ? ? . 106 VAL B N 2348 ATOM 2185 C CA . VAL B 2348 106 . -11.660 -5.655 32.700 1.00 18.96 ? ? ? ? ? . 106 VAL B CA 2348 ATOM 2186 C C . VAL B 2348 106 . -10.959 -6.293 31.498 1.00 19.83 ? ? ? ? ? . 106 VAL B C 2348 ATOM 2187 O O . VAL B 2348 106 . -9.751 -6.549 31.544 1.00 21.37 ? ? ? ? ? . 106 VAL B O 2348 ATOM 2188 C CB . VAL B 2348 106 . -11.004 -4.288 33.060 1.00 17.64 ? ? ? ? ? . 106 VAL B CB 2348 ATOM 2189 C CG1 . VAL B 2348 106 . -10.986 -3.352 31.858 1.00 18.20 ? ? ? ? ? . 106 VAL B CG1 2348 ATOM 2190 C CG2 . VAL B 2348 106 . -11.722 -3.622 34.235 1.00 17.98 ? ? ? ? ? . 106 VAL B CG2 2348 ATOM 2191 N N . GLU B 2348 107 . -11.727 -6.593 30.452 1.00 18.84 ? ? ? ? ? . 107 GLU B N 2348 ATOM 2192 C CA . GLU B 2348 107 . -11.218 -7.272 29.245 1.00 21.13 ? ? ? ? ? . 107 GLU B CA 2348 ATOM 2193 C C . GLU B 2348 107 . -11.037 -6.331 28.051 1.00 18.68 ? ? ? ? ? . 107 GLU B C 2348 ATOM 2194 O O . GLU B 2348 107 . -10.450 -6.722 27.037 1.00 18.15 ? ? ? ? ? . 107 GLU B O 2348 ATOM 2195 C CB . GLU B 2348 107 . -12.152 -8.423 28.848 1.00 24.82 ? ? ? ? ? . 107 GLU B CB 2348 ATOM 2196 C CG . GLU B 2348 107 . -12.270 -9.529 29.884 1.00 28.31 ? ? ? ? ? . 107 GLU B CG 2348 ATOM 2197 C CD . GLU B 2348 107 . -10.950 -10.220 30.205 1.00 34.01 ? ? ? ? ? . 107 GLU B CD 2348 ATOM 2198 O OE1 . GLU B 2348 107 . -10.734 -10.534 31.395 1.00 44.29 ? ? ? ? ? . 107 GLU B OE1 2348 ATOM 2199 O OE2 . GLU B 2348 107 . -10.126 -10.442 29.289 1.00 32.07 ? ? ? ? ? 1- 107 GLU B OE2 2348 ATOM 2200 N N . SER B 2348 108 . -11.561 -5.118 28.175 1.00 17.73 ? ? ? ? ? . 108 SER B N 2348 ATOM 2201 C CA . SER B 2348 108 . -11.397 -4.071 27.175 1.00 17.33 ? ? ? ? ? . 108 SER B CA 2348 ATOM 2202 C C . SER B 2348 108 . -11.818 -2.738 27.778 1.00 15.74 ? ? ? ? ? . 108 SER B C 2348 ATOM 2203 O O . SER B 2348 108 . -12.361 -2.699 28.876 1.00 15.99 ? ? ? ? ? . 108 SER B O 2348 ATOM 2204 C CB . SER B 2348 108 . -12.256 -4.347 25.952 1.00 19.74 ? ? ? ? ? . 108 SER B CB 2348 ATOM 2205 O OG . SER B 2348 108 . -13.625 -4.264 26.285 1.00 22.41 ? ? ? ? ? . 108 SER B OG 2348 ATOM 2206 N N . ILE B 2348 109 . -11.559 -1.649 27.067 1.00 14.80 ? ? ? ? ? . 109 ILE B N 2348 ATOM 2207 C CA . ILE B 2348 109 . -12.072 -0.339 27.467 1.00 15.47 ? ? ? ? ? . 109 ILE B CA 2348 ATOM 2208 C C . ILE B 2348 109 . -12.845 0.251 26.296 1.00 16.17 ? ? ? ? ? . 109 ILE B C 2348 ATOM 2209 O O . ILE B 2348 109 . -12.602 -0.128 25.144 1.00 16.27 ? ? ? ? ? . 109 ILE B O 2348 ATOM 2210 C CB . ILE B 2348 109 . -10.972 0.632 27.987 1.00 16.02 ? ? ? ? ? . 109 ILE B CB 2348 ATOM 2211 C CG1 . ILE B 2348 109 . -9.961 0.967 26.903 1.00 15.75 ? ? ? ? ? . 109 ILE B CG1 2348 ATOM 2212 C CG2 . ILE B 2348 109 . -10.282 0.054 29.216 1.00 15.93 ? ? ? ? ? . 109 ILE B CG2 2348 ATOM 2213 C CD1 . ILE B 2348 109 . -8.993 2.067 27.266 1.00 16.37 ? ? ? ? ? . 109 ILE B CD1 2348 ATOM 2214 N N . PRO B 2348 110 . -13.792 1.170 26.568 1.00 16.95 ? ? ? ? ? . 110 PRO B N 2348 ATOM 2215 C CA . PRO B 2348 110 . -14.237 1.696 27.863 1.00 16.22 ? ? ? ? ? . 110 PRO B CA 2348 ATOM 2216 C C . PRO B 2348 110 . -14.920 0.644 28.734 1.00 17.60 ? ? ? ? ? . 110 PRO B C 2348 ATOM 2217 O O . PRO B 2348 110 . -15.617 -0.236 28.202 1.00 16.52 ? ? ? ? ? . 110 PRO B O 2348 ATOM 2218 C CB . PRO B 2348 110 . -15.259 2.765 27.461 1.00 18.10 ? ? ? ? ? . 110 PRO B CB 2348 ATOM 2219 C CG . PRO B 2348 110 . -15.822 2.275 26.186 1.00 18.28 ? ? ? ? ? . 110 PRO B CG 2348 ATOM 2220 C CD . PRO B 2348 110 . -14.652 1.644 25.470 1.00 17.16 ? ? ? ? ? . 110 PRO B CD 2348 ATOM 2221 N N . THR B 2348 111 . -14.694 0.716 30.045 1.00 16.11 ? ? ? ? ? . 111 THR B N 2348 ATOM 2222 C CA . THR B 2348 111 . -15.409 -0.126 31.022 1.00 17.84 ? ? ? ? ? . 111 THR B CA 2348 ATOM 2223 C C . THR B 2348 111 . -15.693 0.701 32.267 1.00 15.92 ? ? ? ? ? . 111 THR B C 2348 ATOM 2224 O O . THR B 2348 111 . -14.854 1.488 32.684 1.00 16.14 ? ? ? ? ? . 111 THR B O 2348 ATOM 2225 C CB . THR B 2348 111 . -14.610 -1.402 31.404 1.00 19.98 ? ? ? ? ? . 111 THR B CB 2348 ATOM 2226 C CG2 . THR B 2348 111 . -15.277 -2.166 32.547 1.00 23.70 ? ? ? ? ? . 111 THR B CG2 2348 ATOM 2227 O OG1 . THR B 2348 111 . -14.558 -2.285 30.281 1.00 20.70 ? ? ? ? ? . 111 THR B OG1 2348 ATOM 2228 N N . LEU B 2348 112 . -16.896 0.545 32.814 1.00 16.09 ? ? ? ? ? . 112 LEU B N 2348 ATOM 2229 C CA . LEU B 2348 112 . -17.268 1.097 34.111 1.00 16.65 ? ? ? ? ? . 112 LEU B CA 2348 ATOM 2230 C C . LEU B 2348 112 . -17.415 -0.020 35.152 1.00 16.97 ? ? ? ? ? . 112 LEU B C 2348 ATOM 2231 O O . LEU B 2348 112 . -18.046 -1.039 34.895 1.00 15.77 ? ? ? ? ? . 112 LEU B O 2348 ATOM 2232 C CB . LEU B 2348 112 . -18.584 1.885 34.009 1.00 17.47 ? ? ? ? ? . 112 LEU B CB 2348 ATOM 2233 C CG . LEU B 2348 112 . -18.569 3.198 33.214 1.00 18.01 ? ? ? ? ? . 112 LEU B CG 2348 ATOM 2234 C CD1 . LEU B 2348 112 . -19.969 3.779 33.085 1.00 18.77 ? ? ? ? ? . 112 LEU B CD1 2348 ATOM 2235 C CD2 . LEU B 2348 112 . -17.646 4.216 33.837 1.00 17.16 ? ? ? ? ? . 112 LEU B CD2 2348 ATOM 2236 N N . ILE B 2348 113 . -16.826 0.192 36.329 1.00 17.00 ? ? ? ? ? . 113 ILE B N 2348 ATOM 2237 C CA . ILE B 2348 113 . -17.007 -0.670 37.479 1.00 16.38 ? ? ? ? ? . 113 ILE B CA 2348 ATOM 2238 C C . ILE B 2348 113 . -17.716 0.177 38.540 1.00 16.37 ? ? ? ? ? . 113 ILE B C 2348 ATOM 2239 O O . ILE B 2348 113 . -17.248 1.255 38.896 1.00 16.22 ? ? ? ? ? . 113 ILE B O 2348 ATOM 2240 C CB . ILE B 2348 113 . -15.657 -1.185 38.022 1.00 17.79 ? ? ? ? ? . 113 ILE B CB 2348 ATOM 2241 C CG1 . ILE B 2348 113 . -14.838 -1.867 36.895 1.00 17.85 ? ? ? ? ? . 113 ILE B CG1 2348 ATOM 2242 C CG2 . ILE B 2348 113 . -15.877 -2.141 39.192 1.00 18.54 ? ? ? ? ? . 113 ILE B CG2 2348 ATOM 2243 C CD1 . ILE B 2348 113 . -15.488 -3.095 36.280 1.00 18.47 ? ? ? ? ? . 113 ILE B CD1 2348 ATOM 2244 N N . THR B 2348 114 . -18.842 -0.325 39.028 1.00 15.43 ? ? ? ? ? . 114 THR B N 2348 ATOM 2245 C CA . THR B 2348 114 . -19.682 0.402 39.975 1.00 16.48 ? ? ? ? ? . 114 THR B CA 2348 ATOM 2246 C C . THR B 2348 114 . -19.412 -0.113 41.381 1.00 16.42 ? ? ? ? ? . 114 THR B C 2348 ATOM 2247 O O . THR B 2348 114 . -19.584 -1.308 41.647 1.00 16.58 ? ? ? ? ? . 114 THR B O 2348 ATOM 2248 C CB . THR B 2348 114 . -21.168 0.225 39.621 1.00 15.92 ? ? ? ? ? . 114 THR B CB 2348 ATOM 2249 C CG2 . THR B 2348 114 . -22.027 1.243 40.350 1.00 16.26 ? ? ? ? ? . 114 THR B CG2 2348 ATOM 2250 O OG1 . THR B 2348 114 . -21.344 0.401 38.213 1.00 15.73 ? ? ? ? ? . 114 THR B OG1 2348 ATOM 2251 N N . ILE B 2348 115 . -18.990 0.787 42.273 1.00 16.90 ? ? ? ? ? . 115 ILE B N 2348 ATOM 2252 C CA . ILE B 2348 115 . -18.544 0.407 43.625 1.00 17.54 ? ? ? ? ? . 115 ILE B CA 2348 ATOM 2253 C C . ILE B 2348 115 . -19.263 1.239 44.688 1.00 16.17 ? ? ? ? ? . 115 ILE B C 2348 ATOM 2254 O O . ILE B 2348 115 . -19.466 2.428 44.522 1.00 15.85 ? ? ? ? ? . 115 ILE B O 2348 ATOM 2255 C CB . ILE B 2348 115 . -17.015 0.585 43.794 1.00 20.42 ? ? ? ? ? . 115 ILE B CB 2348 ATOM 2256 C CG1 . ILE B 2348 115 . -16.282 -0.201 42.713 1.00 23.68 ? ? ? ? ? . 115 ILE B CG1 2348 ATOM 2257 C CG2 . ILE B 2348 115 . -16.553 0.099 45.166 1.00 21.05 ? ? ? ? ? . 115 ILE B CG2 2348 ATOM 2258 C CD1 . ILE B 2348 115 . -14.778 -0.142 42.803 1.00 25.90 ? ? ? ? ? . 115 ILE B CD1 2348 ATOM 2259 N N . ASN B 2348 116 . -19.662 0.582 45.767 1.00 16.90 ? ? ? ? ? . 116 ASN B N 2348 ATOM 2260 C CA . ASN B 2348 116 . -20.147 1.263 46.971 1.00 16.70 ? ? ? ? ? . 116 ASN B CA 2348 ATOM 2261 C C . ASN B 2348 116 . -18.931 1.852 47.702 1.00 16.05 ? ? ? ? ? . 116 ASN B C 2348 ATOM 2262 O O . ASN B 2348 116 . -18.058 1.101 48.162 1.00 15.37 ? ? ? ? ? . 116 ASN B O 2348 ATOM 2263 C CB . ASN B 2348 116 . -20.874 0.266 47.859 1.00 17.51 ? ? ? ? ? . 116 ASN B CB 2348 ATOM 2264 C CG . ASN B 2348 116 . -21.445 0.897 49.111 1.00 20.14 ? ? ? ? ? . 116 ASN B CG 2348 ATOM 2265 N ND2 . ASN B 2348 116 . -22.754 0.873 49.224 1.00 25.82 ? ? ? ? ? . 116 ASN B ND2 2348 ATOM 2266 O OD1 . ASN B 2348 116 . -20.714 1.380 49.974 1.00 18.71 ? ? ? ? ? . 116 ASN B OD1 2348 ATOM 2267 N N . ALA B 2348 117 . -18.896 3.176 47.829 1.00 16.79 ? ? ? ? ? . 117 ALA B N 2348 ATOM 2268 C CA . ALA B 2348 117 . -17.761 3.890 48.455 1.00 17.20 ? ? ? ? ? . 117 ALA B CA 2348 ATOM 2269 C C . ALA B 2348 117 . -17.479 3.493 49.908 1.00 17.04 ? ? ? ? ? . 117 ALA B C 2348 ATOM 2270 O O . ALA B 2348 117 . -16.322 3.460 50.323 1.00 16.84 ? ? ? ? ? . 117 ALA B O 2348 ATOM 2271 C CB . ALA B 2348 117 . -17.982 5.391 48.369 1.00 17.96 ? ? ? ? ? . 117 ALA B CB 2348 ATOM 2272 N N . ASP B 2348 118 . -18.530 3.193 50.676 1.00 16.23 ? ? ? ? ? . 118 ASP B N 2348 ATOM 2273 C CA . ASP B 2348 118 . -18.388 2.829 52.092 1.00 16.61 ? ? ? ? ? . 118 ASP B CA 2348 ATOM 2274 C C . ASP B 2348 118 . -17.863 1.421 52.371 1.00 16.96 ? ? ? ? ? . 118 ASP B C 2348 ATOM 2275 O O . ASP B 2348 118 . -17.174 1.215 53.368 1.00 16.07 ? ? ? ? ? . 118 ASP B O 2348 ATOM 2276 C CB . ASP B 2348 118 . -19.737 2.982 52.822 1.00 18.01 ? ? ? ? ? . 118 ASP B CB 2348 ATOM 2277 C CG . ASP B 2348 118 . -20.237 4.389 52.815 1.00 19.29 ? ? ? ? ? . 118 ASP B CG 2348 ATOM 2278 O OD1 . ASP B 2348 118 . -19.439 5.311 52.540 1.00 17.79 ? ? ? ? ? . 118 ASP B OD1 2348 ATOM 2279 O OD2 . ASP B 2348 118 . -21.440 4.585 53.062 1.00 19.94 ? ? ? ? ? 1- 118 ASP B OD2 2348 ATOM 2280 N N . THR B 2348 119 . -18.225 0.452 51.526 1.00 16.79 ? ? ? ? ? . 119 THR B N 2348 ATOM 2281 C CA . THR B 2348 119 . -17.870 -0.963 51.759 1.00 16.25 ? ? ? ? ? . 119 THR B CA 2348 ATOM 2282 C C . THR B 2348 119 . -16.845 -1.529 50.766 1.00 15.04 ? ? ? ? ? . 119 THR B C 2348 ATOM 2283 O O . THR B 2348 119 . -16.168 -2.523 51.061 1.00 15.85 ? ? ? ? ? . 119 THR B O 2348 ATOM 2284 C CB . THR B 2348 119 . -19.130 -1.849 51.728 1.00 15.66 ? ? ? ? ? . 119 THR B CB 2348 ATOM 2285 C CG2 . THR B 2348 119 . -20.150 -1.347 52.749 1.00 16.06 ? ? ? ? ? . 119 THR B CG2 2348 ATOM 2286 O OG1 . THR B 2348 119 . -19.708 -1.815 50.418 1.00 16.00 ? ? ? ? ? . 119 THR B OG1 2348 ATOM 2287 N N . GLY B 2348 120 . -16.742 -0.913 49.600 1.00 14.05 ? ? ? ? ? . 120 GLY B N 2348 ATOM 2288 C CA . GLY B 2348 120 . -15.979 -1.465 48.502 1.00 15.89 ? ? ? ? ? . 120 GLY B CA 2348 ATOM 2289 C C . GLY B 2348 120 . -16.681 -2.581 47.748 1.00 16.20 ? ? ? ? ? . 120 GLY B C 2348 ATOM 2290 O O . GLY B 2348 120 . -16.062 -3.214 46.898 1.00 18.41 ? ? ? ? ? . 120 GLY B O 2348 ATOM 2291 N N . ALA B 2348 121 . -17.958 -2.821 48.022 1.00 17.23 ? ? ? ? ? . 121 ALA B N 2348 ATOM 2292 C CA . ALA B 2348 121 . -18.705 -3.859 47.317 1.00 17.65 ? ? ? ? ? . 121 ALA B CA 2348 ATOM 2293 C C . ALA B 2348 121 . -18.873 -3.430 45.858 1.00 18.18 ? ? ? ? ? . 121 ALA B C 2348 ATOM 2294 O O . ALA B 2348 121 . -19.147 -2.257 45.572 1.00 16.95 ? ? ? ? ? . 121 ALA B O 2348 ATOM 2295 C CB . ALA B 2348 121 . -20.064 -4.092 47.957 1.00 19.25 ? ? ? ? ? . 121 ALA B CB 2348 ATOM 2296 N N . ILE B 2348 122 . -18.699 -4.386 44.947 1.00 18.05 ? ? ? ? ? . 122 ILE B N 2348 ATOM 2297 C CA . ILE B 2348 122 . -18.941 -4.164 43.525 1.00 18.12 ? ? ? ? ? . 122 ILE B CA 2348 ATOM 2298 C C . ILE B 2348 122 . -20.440 -4.340 43.276 1.00 20.59 ? ? ? ? ? . 122 ILE B C 2348 ATOM 2299 O O . ILE B 2348 122 . -20.977 -5.455 43.410 1.00 19.10 ? ? ? ? ? . 122 ILE B O 2348 ATOM 2300 C CB . ILE B 2348 122 . -18.156 -5.143 42.628 1.00 20.60 ? ? ? ? ? . 122 ILE B CB 2348 ATOM 2301 C CG1 . ILE B 2348 122 . -16.683 -5.237 43.056 1.00 21.44 ? ? ? ? ? . 122 ILE B CG1 2348 ATOM 2302 C CG2 . ILE B 2348 122 . -18.285 -4.741 41.163 1.00 20.26 ? ? ? ? ? . 122 ILE B CG2 2348 ATOM 2303 C CD1 . ILE B 2348 122 . -15.966 -3.917 43.167 1.00 22.79 ? ? ? ? ? . 122 ILE B CD1 2348 ATOM 2304 N N . ILE B 2348 123 . -21.091 -3.220 42.955 1.00 19.17 ? ? ? ? ? . 123 ILE B N 2348 ATOM 2305 C CA . ILE B 2348 123 . -22.524 -3.148 42.665 1.00 19.40 ? ? ? ? ? . 123 ILE B CA 2348 ATOM 2306 C C . ILE B 2348 123 . -22.828 -3.699 41.282 1.00 20.40 ? ? ? ? ? . 123 ILE B C 2348 ATOM 2307 O O . ILE B 2348 123 . -23.866 -4.326 41.074 1.00 21.80 ? ? ? ? ? . 123 ILE B O 2348 ATOM 2308 C CB . ILE B 2348 123 . -23.019 -1.673 42.737 1.00 19.90 ? ? ? ? ? . 123 ILE B CB 2348 ATOM 2309 C CG1 . ILE B 2348 123 . -23.002 -1.193 44.187 1.00 20.39 ? ? ? ? ? . 123 ILE B CG1 2348 ATOM 2310 C CG2 . ILE B 2348 123 . -24.415 -1.498 42.128 1.00 20.67 ? ? ? ? ? . 123 ILE B CG2 2348 ATOM 2311 C CD1 . ILE B 2348 123 . -23.096 0.301 44.351 1.00 19.36 ? ? ? ? ? . 123 ILE B CD1 2348 ATOM 2312 N N . GLY B 2348 124 . -21.937 -3.423 40.337 1.00 18.81 ? ? ? ? ? . 124 GLY B N 2348 ATOM 2313 C CA . GLY B 2348 124 . -22.146 -3.798 38.949 1.00 18.93 ? ? ? ? ? . 124 GLY B CA 2348 ATOM 2314 C C . GLY B 2348 124 . -20.917 -3.561 38.098 1.00 18.59 ? ? ? ? ? . 124 GLY B C 2348 ATOM 2315 O O . GLY B 2348 124 . -19.977 -2.870 38.514 1.00 17.42 ? ? ? ? ? . 124 GLY B O 2348 ATOM 2316 N N . THR B 2348 125 . -20.915 -4.183 36.918 1.00 16.72 ? ? ? ? ? . 125 THR B N 2348 ATOM 2317 C CA . THR B 2348 125 . -19.809 -4.078 35.974 1.00 18.21 ? ? ? ? ? . 125 THR B CA 2348 ATOM 2318 C C . THR B 2348 125 . -20.260 -3.682 34.544 1.00 18.06 ? ? ? ? ? . 125 THR B C 2348 ATOM 2319 O O . THR B 2348 125 . -19.433 -3.643 33.641 1.00 17.16 ? ? ? ? ? . 125 THR B O 2348 ATOM 2320 C CB . THR B 2348 125 . -19.051 -5.431 35.924 1.00 17.85 ? ? ? ? ? . 125 THR B CB 2348 ATOM 2321 C CG2 . THR B 2348 125 . -18.663 -5.884 37.328 1.00 19.30 ? ? ? ? ? . 125 THR B CG2 2348 ATOM 2322 O OG1 . THR B 2348 125 . -19.902 -6.432 35.363 1.00 17.40 ? ? ? ? ? . 125 THR B OG1 2348 ATOM 2323 N N . GLN B 2348 126 . -21.554 -3.380 34.350 1.00 17.06 ? ? ? ? ? . 126 GLN B N 2348 ATOM 2324 C CA . GLN B 2348 126 . -22.139 -3.200 33.006 1.00 18.96 ? ? ? ? ? . 126 GLN B CA 2348 ATOM 2325 C C . GLN B 2348 126 . -22.612 -1.762 32.731 1.00 16.18 ? ? ? ? ? . 126 GLN B C 2348 ATOM 2326 O O . GLN B 2348 126 . -23.266 -1.519 31.717 1.00 16.00 ? ? ? ? ? . 126 GLN B O 2348 ATOM 2327 C CB . GLN B 2348 126 . -23.318 -4.179 32.800 1.00 21.53 ? ? ? ? ? . 126 GLN B CB 2348 ATOM 2328 C CG . GLN B 2348 126 . -22.997 -5.639 33.127 1.00 26.65 ? ? ? ? ? . 126 GLN B CG 2348 ATOM 2329 C CD . GLN B 2348 126 . -21.992 -6.255 32.163 1.00 33.54 ? ? ? ? ? . 126 GLN B CD 2348 ATOM 2330 N NE2 . GLN B 2348 126 . -20.900 -6.819 32.704 1.00 32.18 ? ? ? ? ? . 126 GLN B NE2 2348 ATOM 2331 O OE1 . GLN B 2348 126 . -22.197 -6.230 30.944 1.00 36.43 ? ? ? ? ? . 126 GLN B OE1 2348 ATOM 2332 N N . ALA B 2348 127 . -22.264 -0.808 33.593 1.00 16.05 ? ? ? ? ? . 127 ALA B N 2348 ATOM 2333 C CA . ALA B 2348 127 . -22.760 0.564 33.436 1.00 15.75 ? ? ? ? ? . 127 ALA B CA 2348 ATOM 2334 C C . ALA B 2348 127 . -22.341 1.243 32.141 1.00 15.23 ? ? ? ? ? . 127 ALA B C 2348 ATOM 2335 O O . ALA B 2348 127 . -23.034 2.142 31.687 1.00 15.93 ? ? ? ? ? . 127 ALA B O 2348 ATOM 2336 C CB . ALA B 2348 127 . -22.400 1.425 34.627 1.00 15.67 ? ? ? ? ? . 127 ALA B CB 2348 ATOM 2337 N N . ARG B 2348 128 . -21.240 0.798 31.530 1.00 14.93 ? ? ? ? ? . 128 ARG B N 2348 ATOM 2338 C CA . ARG B 2348 128 . -20.830 1.298 30.206 1.00 15.96 ? ? ? ? ? . 128 ARG B CA 2348 ATOM 2339 C C . ARG B 2348 128 . -21.925 1.121 29.144 1.00 15.06 ? ? ? ? ? . 128 ARG B C 2348 ATOM 2340 O O . ARG B 2348 128 . -22.027 1.926 28.218 1.00 15.65 ? ? ? ? ? . 128 ARG B O 2348 ATOM 2341 C CB . ARG B 2348 128 . -19.519 0.644 29.737 1.00 17.36 ? ? ? ? ? . 128 ARG B CB 2348 ATOM 2342 C CG . ARG B 2348 128 . -19.030 1.060 28.355 1.00 18.28 ? ? ? ? ? . 128 ARG B CG 2348 ATOM 2343 C CD . ARG B 2348 128 . -19.475 0.089 27.261 1.00 18.70 ? ? ? ? ? . 128 ARG B CD 2348 ATOM 2344 N NE . ARG B 2348 128 . -18.961 0.461 25.948 1.00 20.10 ? ? ? ? ? . 128 ARG B NE 2348 ATOM 2345 C CZ . ARG B 2348 128 . -19.426 1.445 25.180 1.00 19.13 ? ? ? ? ? . 128 ARG B CZ 2348 ATOM 2346 N NH1 . ARG B 2348 128 . -20.456 2.197 25.558 1.00 19.69 ? ? ? ? ? 1+ 128 ARG B NH1 2348 ATOM 2347 N NH2 . ARG B 2348 128 . -18.859 1.668 24.002 1.00 18.47 ? ? ? ? ? . 128 ARG B NH2 2348 ATOM 2348 N N . THR B 2348 129 . -22.702 0.051 29.241 1.00 15.09 ? ? ? ? ? . 129 THR B N 2348 ATOM 2349 C CA . THR B 2348 129 . -23.852 -0.119 28.355 1.00 14.80 ? ? ? ? ? . 129 THR B CA 2348 ATOM 2350 C C . THR B 2348 129 . -25.135 0.426 28.952 1.00 15.27 ? ? ? ? ? . 129 THR B C 2348 ATOM 2351 O O . THR B 2348 129 . -25.954 0.976 28.224 1.00 15.86 ? ? ? ? ? . 129 THR B O 2348 ATOM 2352 C CB . THR B 2348 129 . -24.066 -1.592 27.963 1.00 15.34 ? ? ? ? ? . 129 THR B CB 2348 ATOM 2353 C CG2 . THR B 2348 129 . -22.915 -2.076 27.139 1.00 15.87 ? ? ? ? ? . 129 THR B CG2 2348 ATOM 2354 O OG1 . THR B 2348 129 . -24.144 -2.393 29.141 1.00 16.33 ? ? ? ? ? . 129 THR B OG1 2348 ATOM 2355 N N . ARG B 2348 130 . -25.323 0.275 30.262 1.00 15.00 ? ? ? ? ? . 130 ARG B N 2348 ATOM 2356 C CA . ARG B 2348 130 . -26.568 0.715 30.893 1.00 17.13 ? ? ? ? ? . 130 ARG B CA 2348 ATOM 2357 C C . ARG B 2348 130 . -26.825 2.216 30.730 1.00 15.71 ? ? ? ? ? . 130 ARG B C 2348 ATOM 2358 O O . ARG B 2348 130 . -27.975 2.620 30.566 1.00 15.21 ? ? ? ? ? . 130 ARG B O 2348 ATOM 2359 C CB . ARG B 2348 130 . -26.612 0.354 32.379 1.00 17.49 ? ? ? ? ? . 130 ARG B CB 2348 ATOM 2360 C CG . ARG B 2348 130 . -26.602 -1.128 32.693 1.00 19.40 ? ? ? ? ? . 130 ARG B CG 2348 ATOM 2361 C CD . ARG B 2348 130 . -27.939 -1.798 32.398 1.00 23.34 ? ? ? ? ? . 130 ARG B CD 2348 ATOM 2362 N NE . ARG B 2348 130 . -27.856 -3.263 32.477 1.00 25.67 ? ? ? ? ? . 130 ARG B NE 2348 ATOM 2363 C CZ . ARG B 2348 130 . -27.249 -4.044 31.578 1.00 29.30 ? ? ? ? ? . 130 ARG B CZ 2348 ATOM 2364 N NH1 . ARG B 2348 130 . -26.635 -3.522 30.505 1.00 32.20 ? ? ? ? ? 1+ 130 ARG B NH1 2348 ATOM 2365 N NH2 . ARG B 2348 130 . -27.232 -5.363 31.757 1.00 30.69 ? ? ? ? ? . 130 ARG B NH2 2348 ATOM 2366 N N . VAL B 2348 131 . -25.762 3.019 30.763 1.00 17.22 ? ? ? ? ? . 131 VAL B N 2348 ATOM 2367 C CA . VAL B 2348 131 . -25.866 4.465 30.546 1.00 18.71 ? ? ? ? ? . 131 VAL B CA 2348 ATOM 2368 C C . VAL B 2348 131 . -26.491 4.773 29.164 1.00 18.50 ? ? ? ? ? . 131 VAL B C 2348 ATOM 2369 O O . VAL B 2348 131 . -27.324 5.668 29.033 1.00 18.95 ? ? ? ? ? . 131 VAL B O 2348 ATOM 2370 C CB . VAL B 2348 131 . -24.483 5.156 30.689 1.00 19.83 ? ? ? ? ? . 131 VAL B CB 2348 ATOM 2371 C CG1 . VAL B 2348 131 . -24.538 6.599 30.221 1.00 22.90 ? ? ? ? ? . 131 VAL B CG1 2348 ATOM 2372 C CG2 . VAL B 2348 131 . -23.979 5.076 32.124 1.00 19.15 ? ? ? ? ? . 131 VAL B CG2 2348 ATOM 2373 N N . ILE B 2348 132 . -26.120 3.994 28.158 1.00 16.67 ? ? ? ? ? . 132 ILE B N 2348 ATOM 2374 C CA . ILE B 2348 132 . -26.661 4.145 26.812 1.00 16.90 ? ? ? ? ? . 132 ILE B CA 2348 ATOM 2375 C C . ILE B 2348 132 . -28.113 3.643 26.739 1.00 16.29 ? ? ? ? ? . 132 ILE B C 2348 ATOM 2376 O O . ILE B 2348 132 . -28.967 4.263 26.096 1.00 16.44 ? ? ? ? ? . 132 ILE B O 2348 ATOM 2377 C CB . ILE B 2348 132 . -25.800 3.359 25.799 1.00 17.24 ? ? ? ? ? . 132 ILE B CB 2348 ATOM 2378 C CG1 . ILE B 2348 132 . -24.362 3.915 25.762 1.00 20.53 ? ? ? ? ? . 132 ILE B CG1 2348 ATOM 2379 C CG2 . ILE B 2348 132 . -26.477 3.315 24.433 1.00 17.11 ? ? ? ? ? . 132 ILE B CG2 2348 ATOM 2380 C CD1 . ILE B 2348 132 . -24.119 5.034 24.790 1.00 24.40 ? ? ? ? ? . 132 ILE B CD1 2348 ATOM 2381 N N A GLU B 2348 133 . -28.423 2.510 27.395 0.00 20.00 ? ? ? ? ? . 133 GLU B N 2348 ATOM 2382 N N B GLU B 2348 133 . -28.382 2.515 27.392 1.00 16.20 ? ? ? ? ? . 133 GLU B N 2348 ATOM 2383 C CA A GLU B 2348 133 . -29.761 1.917 27.397 0.00 20.00 ? ? ? ? ? . 133 GLU B CA 2348 ATOM 2384 C CA B GLU B 2348 133 . -29.721 1.911 27.407 1.00 16.09 ? ? ? ? ? . 133 GLU B CA 2348 ATOM 2385 C C A GLU B 2348 133 . -30.756 2.689 28.261 0.00 20.00 ? ? ? ? ? . 133 GLU B C 2348 ATOM 2386 C C B GLU B 2348 133 . -30.751 2.681 28.240 1.00 15.31 ? ? ? ? ? . 133 GLU B C 2348 ATOM 2387 O O A GLU B 2348 133 . -31.968 2.622 28.042 0.00 20.00 ? ? ? ? ? . 133 GLU B O 2348 ATOM 2388 O O B GLU B 2348 133 . -31.953 2.593 27.972 1.00 13.81 ? ? ? ? ? . 133 GLU B O 2348 ATOM 2389 C CB A GLU B 2348 133 . -29.692 0.475 27.901 0.00 20.00 ? ? ? ? ? . 133 GLU B CB 2348 ATOM 2390 C CB B GLU B 2348 133 . -29.641 0.482 27.956 1.00 17.60 ? ? ? ? ? . 133 GLU B CB 2348 ATOM 2391 C CG A GLU B 2348 133 . -28.792 -0.432 27.085 0.00 20.00 ? ? ? ? ? . 133 GLU B CG 2348 ATOM 2392 C CG B GLU B 2348 133 . -28.771 -0.446 27.118 1.00 18.12 ? ? ? ? ? . 133 GLU B CG 2348 ATOM 2393 C CD A GLU B 2348 133 . -28.619 -1.805 27.715 0.00 20.00 ? ? ? ? ? . 133 GLU B CD 2348 ATOM 2394 C CD B GLU B 2348 133 . -28.629 -1.834 27.719 1.00 23.40 ? ? ? ? ? . 133 GLU B CD 2348 ATOM 2395 O OE1 A GLU B 2348 133 . -29.026 -1.980 28.883 0.00 20.00 ? ? ? ? ? . 133 GLU B OE1 2348 ATOM 2396 O OE2 A GLU B 2348 133 . -28.080 -2.710 27.040 0.00 20.00 ? ? ? ? ? 1- 133 GLU B OE2 2348 ATOM 2397 O OE1 B GLU B 2348 133 . -29.036 -2.035 28.889 1.00 26.51 ? ? ? ? ? . 133 GLU B OE1 2348 ATOM 2398 O OE2 B GLU B 2348 133 . -28.127 -2.736 27.000 1.00 24.92 ? ? ? ? ? 1- 133 GLU B OE2 2348 ATOM 2399 N N . ASP B 2348 134 . -30.272 3.427 29.234 1.00 14.63 ? ? ? ? ? . 134 ASP B N 2348 ATOM 2400 C CA . ASP B 2348 134 . -31.098 4.039 30.257 1.00 14.66 ? ? ? ? ? . 134 ASP B CA 2348 ATOM 2401 C C . ASP B 2348 134 . -30.534 5.443 30.535 1.00 14.28 ? ? ? ? ? . 134 ASP B C 2348 ATOM 2402 O O . ASP B 2348 134 . -29.995 5.697 31.610 1.00 14.15 ? ? ? ? ? . 134 ASP B O 2348 ATOM 2403 C CB . ASP B 2348 134 . -31.029 3.145 31.494 1.00 14.80 ? ? ? ? ? . 134 ASP B CB 2348 ATOM 2404 C CG . ASP B 2348 134 . -31.928 3.600 32.640 1.00 15.67 ? ? ? ? ? . 134 ASP B CG 2348 ATOM 2405 O OD1 . ASP B 2348 134 . -32.885 4.373 32.428 1.00 15.40 ? ? ? ? ? . 134 ASP B OD1 2348 ATOM 2406 O OD2 . ASP B 2348 134 . -31.670 3.133 33.784 1.00 16.14 ? ? ? ? ? 1- 134 ASP B OD2 2348 ATOM 2407 N N . PRO B 2348 135 . -30.624 6.355 29.549 1.00 14.67 ? ? ? ? ? . 135 PRO B N 2348 ATOM 2408 C CA . PRO B 2348 135 . -29.977 7.677 29.718 1.00 14.78 ? ? ? ? ? . 135 PRO B CA 2348 ATOM 2409 C C . PRO B 2348 135 . -30.502 8.548 30.877 1.00 14.89 ? ? ? ? ? . 135 PRO B C 2348 ATOM 2410 O O . PRO B 2348 135 . -29.768 9.410 31.374 1.00 15.32 ? ? ? ? ? . 135 PRO B O 2348 ATOM 2411 C CB . PRO B 2348 135 . -30.218 8.381 28.373 1.00 15.25 ? ? ? ? ? . 135 PRO B CB 2348 ATOM 2412 C CG . PRO B 2348 135 . -30.790 7.356 27.446 1.00 16.44 ? ? ? ? ? . 135 PRO B CG 2348 ATOM 2413 C CD . PRO B 2348 135 . -31.390 6.272 28.292 1.00 15.89 ? ? ? ? ? . 135 PRO B CD 2348 ATOM 2414 N N . ASP B 2348 136 . -31.757 8.355 31.277 1.00 15.18 ? ? ? ? ? . 136 ASP B N 2348 ATOM 2415 C CA . ASP B 2348 136 . -32.283 9.049 32.464 1.00 15.63 ? ? ? ? ? . 136 ASP B CA 2348 ATOM 2416 C C . ASP B 2348 136 . -32.159 8.264 33.780 1.00 16.54 ? ? ? ? ? . 136 ASP B C 2348 ATOM 2417 O O . ASP B 2348 136 . -32.680 8.702 34.820 1.00 16.53 ? ? ? ? ? . 136 ASP B O 2348 ATOM 2418 C CB . ASP B 2348 136 . -33.708 9.558 32.208 1.00 16.92 ? ? ? ? ? . 136 ASP B CB 2348 ATOM 2419 C CG . ASP B 2348 136 . -33.724 10.785 31.317 1.00 17.19 ? ? ? ? ? . 136 ASP B CG 2348 ATOM 2420 O OD1 . ASP B 2348 136 . -32.848 11.663 31.491 1.00 19.61 ? ? ? ? ? . 136 ASP B OD1 2348 ATOM 2421 O OD2 . ASP B 2348 136 . -34.608 10.885 30.447 1.00 16.73 ? ? ? ? ? 1- 136 ASP B OD2 2348 ATOM 2422 N N . GLY B 2348 137 . -31.429 7.139 33.740 1.00 15.48 ? ? ? ? ? . 137 GLY B N 2348 ATOM 2423 C CA . GLY B 2348 137 . -31.066 6.372 34.932 1.00 15.18 ? ? ? ? ? . 137 GLY B CA 2348 ATOM 2424 C C . GLY B 2348 137 . -32.218 5.870 35.764 1.00 15.76 ? ? ? ? ? . 137 GLY B C 2348 ATOM 2425 O O . GLY B 2348 137 . -32.130 5.846 37.003 1.00 14.72 ? ? ? ? ? . 137 GLY B O 2348 ATOM 2426 N N . ALA B 2348 138 . -33.317 5.498 35.102 1.00 16.78 ? ? ? ? ? . 138 ALA B N 2348 ATOM 2427 C CA . ALA B 2348 138 . -34.455 4.902 35.790 1.00 16.69 ? ? ? ? ? . 138 ALA B CA 2348 ATOM 2428 C C . ALA B 2348 138 . -34.043 3.709 36.648 1.00 16.56 ? ? ? ? ? . 138 ALA B C 2348 ATOM 2429 O O . ALA B 2348 138 . -34.481 3.599 37.787 1.00 16.42 ? ? ? ? ? . 138 ALA B O 2348 ATOM 2430 C CB . ALA B 2348 138 . -35.529 4.493 34.796 1.00 17.21 ? ? ? ? ? . 138 ALA B CB 2348 ATOM 2431 N N . ASN B 2348 139 . -33.158 2.866 36.111 1.00 15.91 ? ? ? ? ? . 139 ASN B N 2348 ATOM 2432 C CA . ASN B 2348 139 . -32.708 1.642 36.777 1.00 16.24 ? ? ? ? ? . 139 ASN B CA 2348 ATOM 2433 C C . ASN B 2348 139 . -31.351 1.739 37.470 1.00 16.81 ? ? ? ? ? . 139 ASN B C 2348 ATOM 2434 O O . ASN B 2348 139 . -30.799 0.732 37.912 1.00 17.05 ? ? ? ? ? . 139 ASN B O 2348 ATOM 2435 C CB . ASN B 2348 139 . -32.759 0.500 35.767 1.00 18.11 ? ? ? ? ? . 139 ASN B CB 2348 ATOM 2436 C CG . ASN B 2348 139 . -34.194 0.133 35.404 1.00 19.83 ? ? ? ? ? . 139 ASN B CG 2348 ATOM 2437 N ND2 . ASN B 2348 139 . -34.481 0.024 34.124 1.00 20.88 ? ? ? ? ? . 139 ASN B ND2 2348 ATOM 2438 O OD1 . ASN B 2348 139 . -35.032 -0.029 36.280 1.00 23.51 ? ? ? ? ? . 139 ASN B OD1 2348 ATOM 2439 N N . PHE B 2348 140 . -30.828 2.958 37.598 1.00 16.22 ? ? ? ? ? . 140 PHE B N 2348 ATOM 2440 C CA . PHE B 2348 140 . -29.580 3.208 38.327 1.00 17.64 ? ? ? ? ? . 140 PHE B CA 2348 ATOM 2441 C C . PHE B 2348 140 . -29.668 2.659 39.767 1.00 18.96 ? ? ? ? ? . 140 PHE B C 2348 ATOM 2442 O O . PHE B 2348 140 . -30.713 2.807 40.414 1.00 15.66 ? ? ? ? ? . 140 PHE B O 2348 ATOM 2443 C CB . PHE B 2348 140 . -29.310 4.724 38.347 1.00 18.45 ? ? ? ? ? . 140 PHE B CB 2348 ATOM 2444 C CG . PHE B 2348 140 . -28.154 5.125 39.214 1.00 17.77 ? ? ? ? ? . 140 PHE B CG 2348 ATOM 2445 C CD1 . PHE B 2348 140 . -28.314 5.281 40.581 1.00 18.71 ? ? ? ? ? . 140 PHE B CD1 2348 ATOM 2446 C CD2 . PHE B 2348 140 . -26.902 5.336 38.662 1.00 19.83 ? ? ? ? ? . 140 PHE B CD2 2348 ATOM 2447 C CE1 . PHE B 2348 140 . -27.247 5.635 41.388 1.00 19.21 ? ? ? ? ? . 140 PHE B CE1 2348 ATOM 2448 C CE2 . PHE B 2348 140 . -25.839 5.721 39.469 1.00 18.92 ? ? ? ? ? . 140 PHE B CE2 2348 ATOM 2449 C CZ . PHE B 2348 140 . -26.017 5.858 40.828 1.00 18.52 ? ? ? ? ? . 140 PHE B CZ 2348 ATOM 2450 N N . PRO B 2348 141 . -28.576 2.041 40.288 1.00 20.41 ? ? ? ? ? . 141 PRO B N 2348 ATOM 2451 C CA . PRO B 2348 141 . -27.244 1.803 39.717 1.00 20.11 ? ? ? ? ? . 141 PRO B CA 2348 ATOM 2452 C C . PRO B 2348 141 . -27.077 0.490 38.928 1.00 21.32 ? ? ? ? ? . 141 PRO B C 2348 ATOM 2453 O O . PRO B 2348 141 . -25.948 0.030 38.762 1.00 24.20 ? ? ? ? ? . 141 PRO B O 2348 ATOM 2454 C CB . PRO B 2348 141 . -26.362 1.785 40.961 1.00 20.66 ? ? ? ? ? . 141 PRO B CB 2348 ATOM 2455 C CG . PRO B 2348 141 . -27.208 1.126 41.985 1.00 20.62 ? ? ? ? ? . 141 PRO B CG 2348 ATOM 2456 C CD . PRO B 2348 141 . -28.635 1.561 41.690 1.00 22.19 ? ? ? ? ? . 141 PRO B CD 2348 ATOM 2457 N N . TRP B 2348 142 . -28.183 -0.093 38.455 1.00 22.13 ? ? ? ? ? . 142 TRP B N 2348 ATOM 2458 C CA . TRP B 2348 142 . -28.196 -1.272 37.585 1.00 22.88 ? ? ? ? ? . 142 TRP B CA 2348 ATOM 2459 C C . TRP B 2348 142 . -27.597 -2.535 38.225 1.00 27.43 ? ? ? ? ? . 142 TRP B C 2348 ATOM 2460 O O . TRP B 2348 142 . -26.693 -3.159 37.664 1.00 28.69 ? ? ? ? ? . 142 TRP B O 2348 ATOM 2461 C CB . TRP B 2348 142 . -27.548 -0.969 36.234 1.00 20.48 ? ? ? ? ? . 142 TRP B CB 2348 ATOM 2462 C CG . TRP B 2348 142 . -28.048 0.278 35.596 1.00 19.57 ? ? ? ? ? . 142 TRP B CG 2348 ATOM 2463 C CD1 . TRP B 2348 142 . -29.266 0.468 35.016 1.00 19.51 ? ? ? ? ? . 142 TRP B CD1 2348 ATOM 2464 C CD2 . TRP B 2348 142 . -27.335 1.514 35.462 1.00 19.44 ? ? ? ? ? . 142 TRP B CD2 2348 ATOM 2465 C CE2 . TRP B 2348 142 . -28.188 2.417 34.783 1.00 18.08 ? ? ? ? ? . 142 TRP B CE2 2348 ATOM 2466 C CE3 . TRP B 2348 142 . -26.049 1.947 35.837 1.00 19.06 ? ? ? ? ? . 142 TRP B CE3 2348 ATOM 2467 N NE1 . TRP B 2348 142 . -29.356 1.750 34.516 1.00 19.65 ? ? ? ? ? . 142 TRP B NE1 2348 ATOM 2468 C CZ2 . TRP B 2348 142 . -27.801 3.720 34.473 1.00 17.32 ? ? ? ? ? . 142 TRP B CZ2 2348 ATOM 2469 C CZ3 . TRP B 2348 142 . -25.667 3.235 35.533 1.00 19.30 ? ? ? ? ? . 142 TRP B CZ3 2348 ATOM 2470 C CH2 . TRP B 2348 142 . -26.541 4.114 34.851 1.00 19.76 ? ? ? ? ? . 142 TRP B CH2 2348 ATOM 2471 N N . PRO B 2348 143 . -28.131 -2.929 39.393 1.00 31.65 ? ? ? ? ? . 143 PRO B N 2348 ATOM 2472 C CA . PRO B 2348 143 . -27.712 -4.186 40.002 1.00 36.16 ? ? ? ? ? . 143 PRO B CA 2348 ATOM 2473 C C . PRO B 2348 143 . -28.212 -5.407 39.215 1.00 39.42 ? ? ? ? ? . 143 PRO B C 2348 ATOM 2474 O O . PRO B 2348 143 . -29.291 -5.370 38.615 1.00 36.58 ? ? ? ? ? . 143 PRO B O 2348 ATOM 2475 C CB . PRO B 2348 143 . -28.372 -4.127 41.381 1.00 35.00 ? ? ? ? ? . 143 PRO B CB 2348 ATOM 2476 C CG . PRO B 2348 143 . -29.627 -3.370 41.132 1.00 33.72 ? ? ? ? ? . 143 PRO B CG 2348 ATOM 2477 C CD . PRO B 2348 143 . -29.212 -2.291 40.169 1.00 31.42 ? ? ? ? ? . 143 PRO B CD 2348 ATOM 2478 N N . ASN B 2348 144 . -27.436 -6.486 39.261 1.00 48.21 ? ? ? ? ? . 144 ASN B N 2348 ATOM 2479 C CA . ASN B 2348 144 . -27.747 -7.734 38.535 1.00 49.64 ? ? ? ? ? . 144 ASN B CA 2348 ATOM 2480 C C . ASN B 2348 144 . -29.042 -8.395 39.025 1.00 46.88 ? ? ? ? ? . 144 ASN B C 2348 ATOM 2481 O O . ASN B 2348 144 . -29.532 -8.104 40.119 1.00 43.00 ? ? ? ? ? . 144 ASN B O 2348 ATOM 2482 C CB . ASN B 2348 144 . -26.590 -8.735 38.669 1.00 49.51 ? ? ? ? ? . 144 ASN B CB 2348 ATOM 2483 C CG . ASN B 2348 144 . -25.262 -8.155 38.222 1.00 53.00 ? ? ? ? ? . 144 ASN B CG 2348 ATOM 2484 N ND2 . ASN B 2348 144 . -25.061 -8.087 36.913 1.00 55.30 ? ? ? ? ? . 144 ASN B ND2 2348 ATOM 2485 O OD1 . ASN B 2348 144 . -24.441 -7.737 39.047 1.00 49.90 ? ? ? ? ? . 144 ASN B OD1 2348 ATOM 2486 O OXT . ASN B 2348 144 . -29.634 -9.235 38.341 1.00 41.41 ? ? ? ? ? 1- 144 ASN B OXT 2348 # data_SASDE94_MODEL_2349 # _sas_model.id 2349 _sas_model.type_of_model atomic _sas_model.version . _sas_model.symmetry . _sas_model.comment . _sas_model.fitting_id 1705 _sas_model.radius . # loop_ _atom_site.group_PDB _atom_site.id _atom_site.type_symbol _atom_site.label_atom_id _atom_site.label_alt_id _atom_site.label_comp_id _atom_site.label_asym_id _atom_site.label_entity_id _atom_site.label_seq_id _atom_site.pdbx_PDB_ins_code _atom_site.Cartn_x _atom_site.Cartn_y _atom_site.Cartn_z _atom_site.occupancy _atom_site.B_iso_or_equiv _atom_site.Cartn_x_esd _atom_site.Cartn_y_esd _atom_site.Cartn_z_esd _atom_site.occupancy_esd _atom_site.B_iso_or_equiv_esd _atom_site.pdbx_formal_charge _atom_site.auth_seq_id _atom_site.auth_comp_id _atom_site.auth_asym_id _atom_site.auth_atom_id _atom_site.pdbx_PDB_model_num ATOM 1 N N . MET A 2349 1 . 1.498 -29.784 9.466 1.00 42.34 ? ? ? ? ? . 1 MET A N 2349 ATOM 2 C CA . MET A 2349 1 . 1.362 -28.330 9.713 1.00 38.79 ? ? ? ? ? . 1 MET A CA 2349 ATOM 3 C C . MET A 2349 1 . 2.451 -27.795 10.648 1.00 34.46 ? ? ? ? ? . 1 MET A C 2349 ATOM 4 O O . MET A 2349 1 . 3.019 -28.519 11.476 1.00 28.07 ? ? ? ? ? . 1 MET A O 2349 ATOM 5 C CB . MET A 2349 1 . -0.032 -28.003 10.280 1.00 43.44 ? ? ? ? ? . 1 MET A CB 2349 ATOM 6 C CG . MET A 2349 1 . -1.163 -28.074 9.261 1.00 48.34 ? ? ? ? ? . 1 MET A CG 2349 ATOM 7 S SD . MET A 2349 1 . -1.096 -26.763 8.019 1.00 56.59 ? ? ? ? ? . 1 MET A SD 2349 ATOM 8 C CE . MET A 2349 1 . -1.944 -27.553 6.650 1.00 53.77 ? ? ? ? ? . 1 MET A CE 2349 ATOM 9 N N . SER A 2349 2 . 2.702 -26.498 10.518 1.00 31.58 ? ? ? ? ? . 2 SER A N 2349 ATOM 10 C CA . SER A 2349 2 . 3.686 -25.813 11.340 1.00 29.58 ? ? ? ? ? . 2 SER A CA 2349 ATOM 11 C C . SER A 2349 2 . 3.179 -25.647 12.742 1.00 28.87 ? ? ? ? ? . 2 SER A C 2349 ATOM 12 O O . SER A 2349 2 . 1.976 -25.688 12.985 1.00 24.92 ? ? ? ? ? . 2 SER A O 2349 ATOM 13 C CB . SER A 2349 2 . 3.985 -24.427 10.800 1.00 31.81 ? ? ? ? ? . 2 SER A CB 2349 ATOM 14 O OG . SER A 2349 2 . 2.955 -23.494 11.097 1.00 29.45 ? ? ? ? ? . 2 SER A OG 2349 ATOM 15 N N . GLY A 2349 3 . 4.105 -25.396 13.653 1.00 26.92 ? ? ? ? ? . 3 GLY A N 2349 ATOM 16 C CA . GLY A 2349 3 . 3.752 -25.062 15.022 1.00 27.19 ? ? ? ? ? . 3 GLY A CA 2349 ATOM 17 C C . GLY A 2349 3 . 3.057 -23.717 15.142 1.00 26.26 ? ? ? ? ? . 3 GLY A C 2349 ATOM 18 O O . GLY A 2349 3 . 2.392 -23.466 16.134 1.00 31.06 ? ? ? ? ? . 3 GLY A O 2349 ATOM 19 N N . LEU A 2349 4 . 3.204 -22.842 14.148 1.00 27.31 ? ? ? ? ? . 4 LEU A N 2349 ATOM 20 C CA . LEU A 2349 4 . 2.393 -21.618 14.096 1.00 28.14 ? ? ? ? ? . 4 LEU A CA 2349 ATOM 21 C C . LEU A 2349 4 . 0.907 -21.935 13.926 1.00 26.94 ? ? ? ? ? . 4 LEU A C 2349 ATOM 22 O O . LEU A 2349 4 . 0.070 -21.235 14.495 1.00 25.83 ? ? ? ? ? . 4 LEU A O 2349 ATOM 23 C CB . LEU A 2349 4 . 2.859 -20.661 12.988 1.00 31.30 ? ? ? ? ? . 4 LEU A CB 2349 ATOM 24 C CG . LEU A 2349 4 . 4.018 -19.719 13.288 1.00 32.68 ? ? ? ? ? . 4 LEU A CG 2349 ATOM 25 C CD1 . LEU A 2349 4 . 4.270 -18.858 12.063 1.00 34.49 ? ? ? ? ? . 4 LEU A CD1 2349 ATOM 26 C CD2 . LEU A 2349 4 . 3.718 -18.844 14.497 1.00 34.30 ? ? ? ? ? . 4 LEU A CD2 2349 ATOM 27 N N . ALA A 2349 5 . 0.579 -22.994 13.176 1.00 26.99 ? ? ? ? ? . 5 ALA A N 2349 ATOM 28 C CA . ALA A 2349 5 . -0.817 -23.451 13.048 1.00 29.14 ? ? ? ? ? . 5 ALA A CA 2349 ATOM 29 C C . ALA A 2349 5 . -1.502 -23.807 14.377 1.00 31.57 ? ? ? ? ? . 5 ALA A C 2349 ATOM 30 O O . ALA A 2349 5 . -2.722 -23.642 14.499 1.00 38.23 ? ? ? ? ? . 5 ALA A O 2349 ATOM 31 C CB . ALA A 2349 5 . -0.923 -24.626 12.077 1.00 32.07 ? ? ? ? ? . 5 ALA A CB 2349 ATOM 32 N N . LYS A 2349 6 . -0.746 -24.274 15.372 1.00 28.88 ? ? ? ? ? . 6 LYS A N 2349 ATOM 33 C CA . LYS A 2349 6 . -1.337 -24.554 16.690 1.00 28.76 ? ? ? ? ? . 6 LYS A CA 2349 ATOM 34 C C . LYS A 2349 6 . -1.895 -23.293 17.343 1.00 24.63 ? ? ? ? ? . 6 LYS A C 2349 ATOM 35 O O . LYS A 2349 6 . -2.853 -23.372 18.095 1.00 25.15 ? ? ? ? ? . 6 LYS A O 2349 ATOM 36 C CB . LYS A 2349 6 . -0.356 -25.256 17.646 1.00 32.13 ? ? ? ? ? . 6 LYS A CB 2349 ATOM 37 C CG . LYS A 2349 6 . 0.511 -24.341 18.526 1.00 31.95 ? ? ? ? ? . 6 LYS A CG 2349 ATOM 38 C CD . LYS A 2349 6 . 1.607 -25.092 19.277 1.00 33.12 ? ? ? ? ? . 6 LYS A CD 2349 ATOM 39 C CE . LYS A 2349 6 . 2.655 -25.712 18.350 1.00 32.32 ? ? ? ? ? . 6 LYS A CE 2349 ATOM 40 N NZ . LYS A 2349 6 . 3.554 -26.649 19.060 1.00 28.93 ? ? ? ? ? 1+ 6 LYS A NZ 2349 ATOM 41 N N . TYR A 2349 7 . -1.273 -22.149 17.060 1.00 23.51 ? ? ? ? ? . 7 TYR A N 2349 ATOM 42 C CA . TYR A 2349 7 . -1.713 -20.858 17.597 1.00 24.18 ? ? ? ? ? . 7 TYR A CA 2349 ATOM 43 C C . TYR A 2349 7 . -2.735 -20.147 16.721 1.00 25.86 ? ? ? ? ? . 7 TYR A C 2349 ATOM 44 O O . TYR A 2349 7 . -3.549 -19.381 17.235 1.00 25.45 ? ? ? ? ? . 7 TYR A O 2349 ATOM 45 C CB . TYR A 2349 7 . -0.526 -19.931 17.799 1.00 22.86 ? ? ? ? ? . 7 TYR A CB 2349 ATOM 46 C CG . TYR A 2349 7 . 0.519 -20.473 18.741 1.00 20.79 ? ? ? ? ? . 7 TYR A CG 2349 ATOM 47 C CD1 . TYR A 2349 7 . 0.199 -20.788 20.060 1.00 19.65 ? ? ? ? ? . 7 TYR A CD1 2349 ATOM 48 C CD2 . TYR A 2349 7 . 1.841 -20.635 18.325 1.00 19.30 ? ? ? ? ? . 7 TYR A CD2 2349 ATOM 49 C CE1 . TYR A 2349 7 . 1.162 -21.270 20.934 1.00 19.28 ? ? ? ? ? . 7 TYR A CE1 2349 ATOM 50 C CE2 . TYR A 2349 7 . 2.805 -21.114 19.186 1.00 19.91 ? ? ? ? ? . 7 TYR A CE2 2349 ATOM 51 C CZ . TYR A 2349 7 . 2.462 -21.430 20.493 1.00 19.68 ? ? ? ? ? . 7 TYR A CZ 2349 ATOM 52 O OH . TYR A 2349 7 . 3.427 -21.901 21.354 1.00 19.23 ? ? ? ? ? . 7 TYR A OH 2349 ATOM 53 N N . LEU A 2349 8 . -2.711 -20.410 15.413 1.00 25.61 ? ? ? ? ? . 8 LEU A N 2349 ATOM 54 C CA . LEU A 2349 8 . -3.604 -19.742 14.468 1.00 27.57 ? ? ? ? ? . 8 LEU A CA 2349 ATOM 55 C C . LEU A 2349 8 . -4.522 -20.703 13.671 1.00 30.41 ? ? ? ? ? . 8 LEU A C 2349 ATOM 56 O O . LEU A 2349 8 . -4.503 -20.676 12.444 1.00 31.20 ? ? ? ? ? . 8 LEU A O 2349 ATOM 57 C CB . LEU A 2349 8 . -2.750 -18.882 13.517 1.00 26.23 ? ? ? ? ? . 8 LEU A CB 2349 ATOM 58 C CG . LEU A 2349 8 . -1.810 -17.852 14.164 1.00 24.95 ? ? ? ? ? . 8 LEU A CG 2349 ATOM 59 C CD1 . LEU A 2349 8 . -0.828 -17.290 13.142 1.00 26.14 ? ? ? ? ? . 8 LEU A CD1 2349 ATOM 60 C CD2 . LEU A 2349 8 . -2.602 -16.730 14.822 1.00 25.27 ? ? ? ? ? . 8 LEU A CD2 2349 ATOM 61 N N A PRO A 2349 9 . -5.300 -21.558 14.376 0.49 34.84 ? ? ? ? ? . 9 PRO A N 2349 ATOM 62 N N B PRO A 2349 9 . -5.359 -21.503 14.365 0.51 33.67 ? ? ? ? ? . 9 PRO A N 2349 ATOM 63 C CA A PRO A 2349 9 . -6.293 -22.381 13.700 0.49 37.05 ? ? ? ? ? . 9 PRO A CA 2349 ATOM 64 C CA B PRO A 2349 9 . -6.175 -22.534 13.697 0.51 35.34 ? ? ? ? ? . 9 PRO A CA 2349 ATOM 65 C C A PRO A 2349 9 . -7.506 -21.519 13.432 0.49 38.35 ? ? ? ? ? . 9 PRO A C 2349 ATOM 66 C C B PRO A 2349 9 . -7.186 -22.013 12.660 0.51 36.39 ? ? ? ? ? . 9 PRO A C 2349 ATOM 67 O O A PRO A 2349 9 . -8.118 -21.001 14.366 0.49 39.55 ? ? ? ? ? . 9 PRO A O 2349 ATOM 68 O O B PRO A 2349 9 . -7.420 -22.691 11.657 0.51 37.00 ? ? ? ? ? . 9 PRO A O 2349 ATOM 69 C CB A PRO A 2349 9 . -6.624 -23.442 14.742 0.49 36.54 ? ? ? ? ? . 9 PRO A CB 2349 ATOM 70 C CB B PRO A 2349 9 . -6.909 -23.210 14.865 0.51 34.76 ? ? ? ? ? . 9 PRO A CB 2349 ATOM 71 C CG A PRO A 2349 9 . -6.535 -22.693 16.022 0.49 36.43 ? ? ? ? ? . 9 PRO A CG 2349 ATOM 72 C CG B PRO A 2349 9 . -6.953 -22.172 15.932 0.51 34.10 ? ? ? ? ? . 9 PRO A CG 2349 ATOM 73 C CD A PRO A 2349 9 . -5.375 -21.751 15.840 0.49 36.25 ? ? ? ? ? . 9 PRO A CD 2349 ATOM 74 C CD B PRO A 2349 9 . -5.641 -21.459 15.815 0.51 34.53 ? ? ? ? ? . 9 PRO A CD 2349 ATOM 75 N N A GLY A 2349 10 . -7.850 -21.363 12.165 0.49 38.66 ? ? ? ? ? . 10 GLY A N 2349 ATOM 76 N N B GLY A 2349 10 . -7.776 -20.841 12.911 0.51 35.97 ? ? ? ? ? . 10 GLY A N 2349 ATOM 77 C CA A GLY A 2349 10 . -8.786 -20.329 11.768 0.49 37.94 ? ? ? ? ? . 10 GLY A CA 2349 ATOM 78 C CA B GLY A 2349 10 . -8.733 -20.217 11.981 0.51 36.27 ? ? ? ? ? . 10 GLY A CA 2349 ATOM 79 C C A GLY A 2349 10 . -8.121 -19.416 10.757 0.49 37.83 ? ? ? ? ? . 10 GLY A C 2349 ATOM 80 C C B GLY A 2349 10 . -8.107 -19.480 10.800 0.51 37.15 ? ? ? ? ? . 10 GLY A C 2349 ATOM 81 O O A GLY A 2349 10 . -8.796 -18.870 9.876 0.49 37.03 ? ? ? ? ? . 10 GLY A O 2349 ATOM 82 O O B GLY A 2349 10 . -8.798 -19.134 9.836 0.51 37.06 ? ? ? ? ? . 10 GLY A O 2349 ATOM 83 N N . ALA A 2349 11 . -6.803 -19.231 10.888 1.00 36.15 ? ? ? ? ? . 11 ALA A N 2349 ATOM 84 C CA . ALA A 2349 11 . -6.026 -18.586 9.835 1.00 35.46 ? ? ? ? ? . 11 ALA A CA 2349 ATOM 85 C C . ALA A 2349 11 . -5.687 -19.603 8.758 1.00 36.66 ? ? ? ? ? . 11 ALA A C 2349 ATOM 86 O O . ALA A 2349 11 . -5.713 -20.816 8.988 1.00 35.61 ? ? ? ? ? . 11 ALA A O 2349 ATOM 87 C CB . ALA A 2349 11 . -4.743 -17.992 10.401 1.00 34.28 ? ? ? ? ? . 11 ALA A CB 2349 ATOM 88 N N . THR A 2349 12 . -5.403 -19.089 7.571 1.00 35.16 ? ? ? ? ? . 12 THR A N 2349 ATOM 89 C CA . THR A 2349 12 . -4.620 -19.821 6.582 1.00 34.41 ? ? ? ? ? . 12 THR A CA 2349 ATOM 90 C C . THR A 2349 12 . -3.465 -18.927 6.157 1.00 30.55 ? ? ? ? ? . 12 THR A C 2349 ATOM 91 O O . THR A 2349 12 . -2.309 -19.284 6.369 1.00 33.15 ? ? ? ? ? . 12 THR A O 2349 ATOM 92 C CB . THR A 2349 12 . -5.447 -20.322 5.371 1.00 37.60 ? ? ? ? ? . 12 THR A CB 2349 ATOM 93 C CG2 . THR A 2349 12 . -5.624 -21.844 5.441 1.00 41.25 ? ? ? ? ? . 12 THR A CG2 2349 ATOM 94 O OG1 . THR A 2349 12 . -6.745 -19.707 5.356 1.00 40.05 ? ? ? ? ? . 12 THR A OG1 2349 ATOM 95 N N . ASN A 2349 13 . -3.761 -17.760 5.589 1.00 24.01 ? ? ? ? ? . 13 ASN A N 2349 ATOM 96 C CA . ASN A 2349 13 . -2.702 -16.909 5.058 1.00 21.19 ? ? ? ? ? . 13 ASN A CA 2349 ATOM 97 C C . ASN A 2349 13 . -2.485 -15.671 5.897 1.00 19.45 ? ? ? ? ? . 13 ASN A C 2349 ATOM 98 O O . ASN A 2349 13 . -3.378 -15.222 6.620 1.00 21.50 ? ? ? ? ? . 13 ASN A O 2349 ATOM 99 C CB . ASN A 2349 13 . -2.997 -16.518 3.609 1.00 23.60 ? ? ? ? ? . 13 ASN A CB 2349 ATOM 100 C CG . ASN A 2349 13 . -3.062 -17.718 2.683 1.00 25.11 ? ? ? ? ? . 13 ASN A CG 2349 ATOM 101 N ND2 . ASN A 2349 13 . -4.029 -17.717 1.771 1.00 24.16 ? ? ? ? ? . 13 ASN A ND2 2349 ATOM 102 O OD1 . ASN A 2349 13 . -2.256 -18.644 2.795 1.00 28.41 ? ? ? ? ? . 13 ASN A OD1 2349 ATOM 103 N N . LEU A 2349 14 . -1.277 -15.134 5.781 1.00 16.54 ? ? ? ? ? . 14 LEU A N 2349 ATOM 104 C CA . LEU A 2349 14 . -0.881 -13.881 6.390 1.00 15.38 ? ? ? ? ? . 14 LEU A CA 2349 ATOM 105 C C . LEU A 2349 14 . -0.723 -12.879 5.271 1.00 15.70 ? ? ? ? ? . 14 LEU A C 2349 ATOM 106 O O . LEU A 2349 14 . -0.384 -13.251 4.152 1.00 16.70 ? ? ? ? ? . 14 LEU A O 2349 ATOM 107 C CB . LEU A 2349 14 . 0.455 -14.057 7.118 1.00 15.56 ? ? ? ? ? . 14 LEU A CB 2349 ATOM 108 C CG . LEU A 2349 14 . 0.466 -15.081 8.254 1.00 15.33 ? ? ? ? ? . 14 LEU A CG 2349 ATOM 109 C CD1 . LEU A 2349 14 . 1.865 -15.199 8.824 1.00 16.03 ? ? ? ? ? . 14 LEU A CD1 2349 ATOM 110 C CD2 . LEU A 2349 14 . -0.512 -14.706 9.360 1.00 14.84 ? ? ? ? ? . 14 LEU A CD2 2349 ATOM 111 N N . LEU A 2349 15 . -0.963 -11.610 5.571 1.00 15.63 ? ? ? ? ? . 15 LEU A N 2349 ATOM 112 C CA . LEU A 2349 15 . -0.692 -10.536 4.620 1.00 16.16 ? ? ? ? ? . 15 LEU A CA 2349 ATOM 113 C C . LEU A 2349 15 . 0.817 -10.328 4.485 1.00 16.48 ? ? ? ? ? . 15 LEU A C 2349 ATOM 114 O O . LEU A 2349 15 . 1.537 -10.488 5.458 1.00 15.72 ? ? ? ? ? . 15 LEU A O 2349 ATOM 115 C CB . LEU A 2349 15 . -1.302 -9.224 5.088 1.00 15.78 ? ? ? ? ? . 15 LEU A CB 2349 ATOM 116 C CG . LEU A 2349 15 . -2.774 -9.203 5.473 1.00 16.53 ? ? ? ? ? . 15 LEU A CG 2349 ATOM 117 C CD1 . LEU A 2349 15 . -3.169 -7.778 5.854 1.00 17.40 ? ? ? ? ? . 15 LEU A CD1 2349 ATOM 118 C CD2 . LEU A 2349 15 . -3.657 -9.742 4.356 1.00 15.86 ? ? ? ? ? . 15 LEU A CD2 2349 ATOM 119 N N . SER A 2349 16 . 1.274 -9.967 3.289 1.00 16.81 ? ? ? ? ? . 16 SER A N 2349 ATOM 120 C CA . SER A 2349 16 . 2.659 -9.490 3.089 1.00 18.19 ? ? ? ? ? . 16 SER A CA 2349 ATOM 121 C C . SER A 2349 16 . 2.617 -8.199 2.266 1.00 19.91 ? ? ? ? ? . 16 SER A C 2349 ATOM 122 O O . SER A 2349 16 . 1.553 -7.749 1.839 1.00 18.64 ? ? ? ? ? . 16 SER A O 2349 ATOM 123 C CB . SER A 2349 16 . 3.525 -10.544 2.378 1.00 19.00 ? ? ? ? ? . 16 SER A CB 2349 ATOM 124 O OG . SER A 2349 16 . 3.353 -10.503 0.969 1.00 19.59 ? ? ? ? ? . 16 SER A OG 2349 ATOM 125 N N . LYS A 2349 17 . 3.780 -7.614 2.027 1.00 21.51 ? ? ? ? ? . 17 LYS A N 2349 ATOM 126 C CA . LYS A 2349 17 . 3.855 -6.435 1.165 1.00 24.73 ? ? ? ? ? . 17 LYS A CA 2349 ATOM 127 C C . LYS A 2349 17 . 3.444 -6.732 -0.283 1.00 25.66 ? ? ? ? ? . 17 LYS A C 2349 ATOM 128 O O . LYS A 2349 17 . 3.019 -5.819 -0.983 1.00 27.03 ? ? ? ? ? . 17 LYS A O 2349 ATOM 129 C CB . LYS A 2349 17 . 5.262 -5.832 1.197 1.00 25.50 ? ? ? ? ? . 17 LYS A CB 2349 ATOM 130 C CG . LYS A 2349 17 . 5.682 -5.273 2.551 1.00 25.81 ? ? ? ? ? . 17 LYS A CG 2349 ATOM 131 C CD . LYS A 2349 17 . 4.736 -4.187 3.056 1.00 28.95 ? ? ? ? ? . 17 LYS A CD 2349 ATOM 132 C CE . LYS A 2349 17 . 3.753 -4.693 4.113 1.00 28.57 ? ? ? ? ? . 17 LYS A CE 2349 ATOM 133 N NZ . LYS A 2349 17 . 2.971 -3.562 4.702 1.00 25.15 ? ? ? ? ? 1+ 17 LYS A NZ 2349 ATOM 134 N N . SER A 2349 18 . 3.555 -7.992 -0.712 1.00 25.74 ? ? ? ? ? . 18 SER A N 2349 ATOM 135 C CA . SER A 2349 18 . 3.177 -8.416 -2.070 1.00 30.18 ? ? ? ? ? . 18 SER A CA 2349 ATOM 136 C C . SER A 2349 18 . 2.143 -9.546 -2.074 1.00 32.37 ? ? ? ? ? . 18 SER A C 2349 ATOM 137 O O . SER A 2349 18 . 2.384 -10.619 -2.635 1.00 35.88 ? ? ? ? ? . 18 SER A O 2349 ATOM 138 C CB . SER A 2349 18 . 4.431 -8.893 -2.797 1.00 31.94 ? ? ? ? ? . 18 SER A CB 2349 ATOM 139 O OG . SER A 2349 18 . 4.959 -10.040 -2.149 1.00 33.68 ? ? ? ? ? . 18 SER A OG 2349 ATOM 140 N N . GLY A 2349 19 . 0.995 -9.323 -1.452 1.00 31.20 ? ? ? ? ? . 19 GLY A N 2349 ATOM 141 C CA . GLY A 2349 19 . -0.034 -10.370 -1.395 1.00 32.15 ? ? ? ? ? . 19 GLY A CA 2349 ATOM 142 C C . GLY A 2349 19 . 0.276 -11.471 -0.382 1.00 31.51 ? ? ? ? ? . 19 GLY A C 2349 ATOM 143 O O . GLY A 2349 19 . 1.310 -11.458 0.288 1.00 33.38 ? ? ? ? ? . 19 GLY A O 2349 ATOM 144 N N . GLU A 2349 20 . -0.629 -12.434 -0.282 1.00 26.41 ? ? ? ? ? . 20 GLU A N 2349 ATOM 145 C CA . GLU A 2349 20 . -0.691 -13.290 0.884 1.00 24.83 ? ? ? ? ? . 20 GLU A CA 2349 ATOM 146 C C . GLU A 2349 20 . 0.330 -14.411 0.824 1.00 21.95 ? ? ? ? ? . 20 GLU A C 2349 ATOM 147 O O . GLU A 2349 20 . 0.679 -14.879 -0.254 1.00 20.93 ? ? ? ? ? . 20 GLU A O 2349 ATOM 148 C CB . GLU A 2349 20 . -2.102 -13.854 1.040 1.00 28.97 ? ? ? ? ? . 20 GLU A CB 2349 ATOM 149 C CG . GLU A 2349 20 . -3.156 -12.772 1.249 1.00 29.83 ? ? ? ? ? . 20 GLU A CG 2349 ATOM 150 C CD . GLU A 2349 20 . -4.539 -13.321 1.561 1.00 31.70 ? ? ? ? ? . 20 GLU A CD 2349 ATOM 151 O OE1 . GLU A 2349 20 . -4.814 -14.491 1.202 1.00 33.49 ? ? ? ? ? . 20 GLU A OE1 2349 ATOM 152 O OE2 . GLU A 2349 20 . -5.349 -12.565 2.154 1.00 34.19 ? ? ? ? ? 1- 20 GLU A OE2 2349 ATOM 153 N N . VAL A 2349 21 . 0.799 -14.822 1.996 1.00 18.14 ? ? ? ? ? . 21 VAL A N 2349 ATOM 154 C CA . VAL A 2349 21 . 1.739 -15.940 2.130 1.00 18.05 ? ? ? ? ? . 21 VAL A CA 2349 ATOM 155 C C . VAL A 2349 21 . 1.210 -16.964 3.137 1.00 16.57 ? ? ? ? ? . 21 VAL A C 2349 ATOM 156 O O . VAL A 2349 21 . 0.519 -16.610 4.089 1.00 15.65 ? ? ? ? ? . 21 VAL A O 2349 ATOM 157 C CB . VAL A 2349 21 . 3.150 -15.466 2.542 1.00 18.57 ? ? ? ? ? . 21 VAL A CB 2349 ATOM 158 C CG1 . VAL A 2349 21 . 3.672 -14.437 1.540 1.00 19.84 ? ? ? ? ? . 21 VAL A CG1 2349 ATOM 159 C CG2 . VAL A 2349 21 . 3.176 -14.922 3.970 1.00 17.16 ? ? ? ? ? . 21 VAL A CG2 2349 ATOM 160 N N . SER A 2349 22 . 1.533 -18.230 2.906 1.00 15.34 ? ? ? ? ? . 22 SER A N 2349 ATOM 161 C CA . SER A 2349 22 . 1.073 -19.315 3.767 1.00 16.37 ? ? ? ? ? . 22 SER A CA 2349 ATOM 162 C C . SER A 2349 22 . 1.872 -19.345 5.061 1.00 16.62 ? ? ? ? ? . 22 SER A C 2349 ATOM 163 O O . SER A 2349 22 . 3.000 -18.826 5.142 1.00 15.98 ? ? ? ? ? . 22 SER A O 2349 ATOM 164 C CB . SER A 2349 22 . 1.237 -20.655 3.056 1.00 17.61 ? ? ? ? ? . 22 SER A CB 2349 ATOM 165 O OG . SER A 2349 22 . 2.618 -20.887 2.815 1.00 17.06 ? ? ? ? ? . 22 SER A OG 2349 ATOM 166 N N . LEU A 2349 23 . 1.305 -19.988 6.072 1.00 17.27 ? ? ? ? ? . 23 LEU A N 2349 ATOM 167 C CA . LEU A 2349 23 . 2.058 -20.286 7.290 1.00 17.54 ? ? ? ? ? . 23 LEU A CA 2349 ATOM 168 C C . LEU A 2349 23 . 3.271 -21.187 6.998 1.00 15.71 ? ? ? ? ? . 23 LEU A C 2349 ATOM 169 O O . LEU A 2349 23 . 4.357 -20.961 7.555 1.00 15.68 ? ? ? ? ? . 23 LEU A O 2349 ATOM 170 C CB . LEU A 2349 23 . 1.158 -20.925 8.354 1.00 19.09 ? ? ? ? ? . 23 LEU A CB 2349 ATOM 171 C CG . LEU A 2349 23 . 0.047 -20.044 8.926 1.00 19.85 ? ? ? ? ? . 23 LEU A CG 2349 ATOM 172 C CD1 . LEU A 2349 23 . -0.781 -20.855 9.912 1.00 20.80 ? ? ? ? ? . 23 LEU A CD1 2349 ATOM 173 C CD2 . LEU A 2349 23 . 0.588 -18.800 9.598 1.00 20.11 ? ? ? ? ? . 23 LEU A CD2 2349 ATOM 174 N N . GLY A 2349 24 . 3.092 -22.170 6.110 1.00 14.87 ? ? ? ? ? . 24 GLY A N 2349 ATOM 175 C CA . GLY A 2349 24 . 4.183 -23.039 5.652 1.00 14.51 ? ? ? ? ? . 24 GLY A CA 2349 ATOM 176 C C . GLY A 2349 24 . 5.381 -22.325 5.024 1.00 14.47 ? ? ? ? ? . 24 GLY A C 2349 ATOM 177 O O . GLY A 2349 24 . 6.505 -22.845 5.067 1.00 12.91 ? ? ? ? ? . 24 GLY A O 2349 ATOM 178 N N . SER A 2349 25 . 5.160 -21.133 4.454 1.00 14.24 ? ? ? ? ? . 25 SER A N 2349 ATOM 179 C CA . SER A 2349 25 . 6.248 -20.339 3.852 1.00 14.58 ? ? ? ? ? . 25 SER A CA 2349 ATOM 180 C C . SER A 2349 25 . 7.295 -19.881 4.877 1.00 15.23 ? ? ? ? ? . 25 SER A C 2349 ATOM 181 O O . SER A 2349 25 . 8.425 -19.538 4.510 1.00 15.85 ? ? ? ? ? . 25 SER A O 2349 ATOM 182 C CB . SER A 2349 25 . 5.691 -19.131 3.076 1.00 14.16 ? ? ? ? ? . 25 SER A CB 2349 ATOM 183 O OG . SER A 2349 25 . 5.236 -18.112 3.943 1.00 13.91 ? ? ? ? ? . 25 SER A OG 2349 ATOM 184 N N . LEU A 2349 26 . 6.900 -19.862 6.153 1.00 15.28 ? ? ? ? ? . 26 LEU A N 2349 ATOM 185 C CA . LEU A 2349 26 . 7.770 -19.517 7.262 1.00 15.71 ? ? ? ? ? . 26 LEU A CA 2349 ATOM 186 C C . LEU A 2349 26 . 8.551 -20.698 7.831 1.00 13.64 ? ? ? ? ? . 26 LEU A C 2349 ATOM 187 O O . LEU A 2349 26 . 9.162 -20.554 8.882 1.00 12.80 ? ? ? ? ? . 26 LEU A O 2349 ATOM 188 C CB . LEU A 2349 26 . 6.938 -18.882 8.384 1.00 17.44 ? ? ? ? ? . 26 LEU A CB 2349 ATOM 189 C CG . LEU A 2349 26 . 6.047 -17.702 7.946 1.00 20.26 ? ? ? ? ? . 26 LEU A CG 2349 ATOM 190 C CD1 . LEU A 2349 26 . 5.260 -17.143 9.118 1.00 22.13 ? ? ? ? ? . 26 LEU A CD1 2349 ATOM 191 C CD2 . LEU A 2349 26 . 6.881 -16.637 7.276 1.00 23.52 ? ? ? ? ? . 26 LEU A CD2 2349 ATOM 192 N N . VAL A 2349 27 . 8.555 -21.833 7.132 1.00 13.12 ? ? ? ? ? . 27 VAL A N 2349 ATOM 193 C CA . VAL A 2349 27 . 9.321 -23.014 7.537 1.00 13.59 ? ? ? ? ? . 27 VAL A CA 2349 ATOM 194 C C . VAL A 2349 27 . 10.754 -22.634 7.923 1.00 13.89 ? ? ? ? ? . 27 VAL A C 2349 ATOM 195 O O . VAL A 2349 27 . 11.416 -21.850 7.236 1.00 13.58 ? ? ? ? ? . 27 VAL A O 2349 ATOM 196 C CB . VAL A 2349 27 . 9.281 -24.133 6.469 1.00 12.77 ? ? ? ? ? . 27 VAL A CB 2349 ATOM 197 C CG1 . VAL A 2349 27 . 9.896 -23.694 5.145 1.00 12.72 ? ? ? ? ? . 27 VAL A CG1 2349 ATOM 198 C CG2 . VAL A 2349 27 . 9.933 -25.428 6.964 1.00 13.09 ? ? ? ? ? . 27 VAL A CG2 2349 ATOM 199 N N . GLY A 2349 28 . 11.165 -23.100 9.095 1.00 14.31 ? ? ? ? ? . 28 GLY A N 2349 ATOM 200 C CA . GLY A 2349 28 . 12.540 -22.930 9.573 1.00 14.56 ? ? ? ? ? . 28 GLY A CA 2349 ATOM 201 C C . GLY A 2349 28 . 12.871 -21.574 10.159 1.00 13.61 ? ? ? ? ? . 28 GLY A C 2349 ATOM 202 O O . GLY A 2349 28 . 14.008 -21.365 10.620 1.00 13.45 ? ? ? ? ? . 28 GLY A O 2349 ATOM 203 N N . LYS A 2349 29 . 11.900 -20.657 10.167 1.00 14.17 ? ? ? ? ? . 29 LYS A N 2349 ATOM 204 C CA . LYS A 2349 29 . 12.110 -19.302 10.657 1.00 14.57 ? ? ? ? ? . 29 LYS A CA 2349 ATOM 205 C C . LYS A 2349 29 . 11.932 -19.163 12.159 1.00 14.89 ? ? ? ? ? . 29 LYS A C 2349 ATOM 206 O O . LYS A 2349 29 . 11.235 -19.949 12.797 1.00 14.69 ? ? ? ? ? . 29 LYS A O 2349 ATOM 207 C CB . LYS A 2349 29 . 11.153 -18.306 9.975 1.00 15.81 ? ? ? ? ? . 29 LYS A CB 2349 ATOM 208 C CG . LYS A 2349 29 . 11.404 -18.134 8.484 1.00 16.45 ? ? ? ? ? . 29 LYS A CG 2349 ATOM 209 C CD . LYS A 2349 29 . 12.316 -16.947 8.202 1.00 17.42 ? ? ? ? ? . 29 LYS A CD 2349 ATOM 210 C CE . LYS A 2349 29 . 12.498 -16.708 6.715 1.00 17.30 ? ? ? ? ? . 29 LYS A CE 2349 ATOM 211 N NZ . LYS A 2349 29 . 13.044 -17.885 5.999 1.00 19.11 ? ? ? ? ? 1+ 29 LYS A NZ 2349 ATOM 212 N N . THR A 2349 30 . 12.603 -18.156 12.701 1.00 14.18 ? ? ? ? ? . 30 THR A N 2349 ATOM 213 C CA . THR A 2349 30 . 12.220 -17.550 13.977 1.00 14.27 ? ? ? ? ? . 30 THR A CA 2349 ATOM 214 C C . THR A 2349 30 . 11.144 -16.525 13.641 1.00 15.54 ? ? ? ? ? . 30 THR A C 2349 ATOM 215 O O . THR A 2349 30 . 11.293 -15.738 12.701 1.00 15.21 ? ? ? ? ? . 30 THR A O 2349 ATOM 216 C CB . THR A 2349 30 . 13.423 -16.869 14.660 1.00 15.36 ? ? ? ? ? . 30 THR A CB 2349 ATOM 217 C CG2 . THR A 2349 30 . 12.991 -16.093 15.905 1.00 17.24 ? ? ? ? ? . 30 THR A CG2 2349 ATOM 218 O OG1 . THR A 2349 30 . 14.393 -17.861 15.017 1.00 15.76 ? ? ? ? ? . 30 THR A OG1 2349 ATOM 219 N N . VAL A 2349 31 . 10.046 -16.537 14.380 1.00 14.34 ? ? ? ? ? . 31 VAL A N 2349 ATOM 220 C CA . VAL A 2349 31 . 8.934 -15.639 14.093 1.00 15.79 ? ? ? ? ? . 31 VAL A CA 2349 ATOM 221 C C . VAL A 2349 31 . 8.663 -14.816 15.342 1.00 16.49 ? ? ? ? ? . 31 VAL A C 2349 ATOM 222 O O . VAL A 2349 31 . 8.590 -15.357 16.455 1.00 15.72 ? ? ? ? ? . 31 VAL A O 2349 ATOM 223 C CB . VAL A 2349 31 . 7.675 -16.424 13.645 1.00 17.31 ? ? ? ? ? . 31 VAL A CB 2349 ATOM 224 C CG1 . VAL A 2349 31 . 6.467 -15.506 13.473 1.00 19.83 ? ? ? ? ? . 31 VAL A CG1 2349 ATOM 225 C CG2 . VAL A 2349 31 . 7.959 -17.190 12.356 1.00 16.54 ? ? ? ? ? . 31 VAL A CG2 2349 ATOM 226 N N . PHE A 2349 32 . 8.564 -13.502 15.158 1.00 16.30 ? ? ? ? ? . 32 PHE A N 2349 ATOM 227 C CA . PHE A 2349 32 . 8.143 -12.616 16.214 1.00 16.84 ? ? ? ? ? . 32 PHE A CA 2349 ATOM 228 C C . PHE A 2349 32 . 6.687 -12.259 15.980 1.00 16.42 ? ? ? ? ? . 32 PHE A C 2349 ATOM 229 O O . PHE A 2349 32 . 6.341 -11.721 14.924 1.00 18.32 ? ? ? ? ? . 32 PHE A O 2349 ATOM 230 C CB . PHE A 2349 32 . 8.955 -11.336 16.217 1.00 19.26 ? ? ? ? ? . 32 PHE A CB 2349 ATOM 231 C CG . PHE A 2349 32 . 10.415 -11.530 16.494 1.00 19.00 ? ? ? ? ? . 32 PHE A CG 2349 ATOM 232 C CD1 . PHE A 2349 32 . 10.870 -11.695 17.797 1.00 19.12 ? ? ? ? ? . 32 PHE A CD1 2349 ATOM 233 C CD2 . PHE A 2349 32 . 11.344 -11.506 15.462 1.00 20.74 ? ? ? ? ? . 32 PHE A CD2 2349 ATOM 234 C CE1 . PHE A 2349 32 . 12.222 -11.839 18.070 1.00 19.85 ? ? ? ? ? . 32 PHE A CE1 2349 ATOM 235 C CE2 . PHE A 2349 32 . 12.707 -11.659 15.734 1.00 21.50 ? ? ? ? ? . 32 PHE A CE2 2349 ATOM 236 C CZ . PHE A 2349 32 . 13.134 -11.818 17.049 1.00 20.68 ? ? ? ? ? . 32 PHE A CZ 2349 ATOM 237 N N . LEU A 2349 33 . 5.849 -12.554 16.959 1.00 14.24 ? ? ? ? ? . 33 LEU A N 2349 ATOM 238 C CA . LEU A 2349 33 . 4.475 -12.091 16.982 1.00 14.81 ? ? ? ? ? . 33 LEU A CA 2349 ATOM 239 C C . LEU A 2349 33 . 4.477 -10.717 17.622 1.00 15.85 ? ? ? ? ? . 33 LEU A C 2349 ATOM 240 O O . LEU A 2349 33 . 4.880 -10.578 18.777 1.00 15.41 ? ? ? ? ? . 33 LEU A O 2349 ATOM 241 C CB . LEU A 2349 33 . 3.592 -13.056 17.779 1.00 15.00 ? ? ? ? ? . 33 LEU A CB 2349 ATOM 242 C CG . LEU A 2349 33 . 3.603 -14.485 17.239 1.00 16.27 ? ? ? ? ? . 33 LEU A CG 2349 ATOM 243 C CD1 . LEU A 2349 33 . 2.632 -15.324 18.051 1.00 17.02 ? ? ? ? ? . 33 LEU A CD1 2349 ATOM 244 C CD2 . LEU A 2349 33 . 3.259 -14.541 15.757 1.00 17.70 ? ? ? ? ? . 33 LEU A CD2 2349 ATOM 245 N N . TYR A 2349 34 . 4.035 -9.718 16.859 1.00 16.06 ? ? ? ? ? . 34 TYR A N 2349 ATOM 246 C CA . TYR A 2349 34 . 4.112 -8.329 17.268 1.00 15.69 ? ? ? ? ? . 34 TYR A CA 2349 ATOM 247 C C . TYR A 2349 34 . 2.721 -7.828 17.608 1.00 15.39 ? ? ? ? ? . 34 TYR A C 2349 ATOM 248 O O . TYR A 2349 34 . 1.965 -7.440 16.735 1.00 14.35 ? ? ? ? ? . 34 TYR A O 2349 ATOM 249 C CB . TYR A 2349 34 . 4.773 -7.466 16.198 1.00 16.16 ? ? ? ? ? . 34 TYR A CB 2349 ATOM 250 C CG . TYR A 2349 34 . 4.825 -5.977 16.516 1.00 16.03 ? ? ? ? ? . 34 TYR A CG 2349 ATOM 251 C CD1 . TYR A 2349 34 . 4.977 -5.516 17.821 1.00 16.83 ? ? ? ? ? . 34 TYR A CD1 2349 ATOM 252 C CD2 . TYR A 2349 34 . 4.769 -5.031 15.488 1.00 17.63 ? ? ? ? ? . 34 TYR A CD2 2349 ATOM 253 C CE1 . TYR A 2349 34 . 5.030 -4.159 18.098 1.00 17.21 ? ? ? ? ? . 34 TYR A CE1 2349 ATOM 254 C CE2 . TYR A 2349 34 . 4.829 -3.670 15.759 1.00 17.31 ? ? ? ? ? . 34 TYR A CE2 2349 ATOM 255 C CZ . TYR A 2349 34 . 4.965 -3.243 17.069 1.00 16.44 ? ? ? ? ? . 34 TYR A CZ 2349 ATOM 256 O OH . TYR A 2349 34 . 5.016 -1.898 17.366 1.00 17.87 ? ? ? ? ? . 34 TYR A OH 2349 ATOM 257 N N . PHE A 2349 35 . 2.438 -7.854 18.898 1.00 15.23 ? ? ? ? ? . 35 PHE A N 2349 ATOM 258 C CA . PHE A 2349 35 . 1.192 -7.354 19.477 1.00 16.74 ? ? ? ? ? . 35 PHE A CA 2349 ATOM 259 C C . PHE A 2349 35 . 1.248 -5.831 19.553 1.00 16.39 ? ? ? ? ? . 35 PHE A C 2349 ATOM 260 O O . PHE A 2349 35 . 2.115 -5.268 20.223 1.00 17.11 ? ? ? ? ? . 35 PHE A O 2349 ATOM 261 C CB . PHE A 2349 35 . 0.966 -7.980 20.843 1.00 17.16 ? ? ? ? ? . 35 PHE A CB 2349 ATOM 262 C CG . PHE A 2349 35 . 0.735 -9.454 20.782 1.00 18.26 ? ? ? ? ? . 35 PHE A CG 2349 ATOM 263 C CD1 . PHE A 2349 35 . 1.802 -10.330 20.795 1.00 18.94 ? ? ? ? ? . 35 PHE A CD1 2349 ATOM 264 C CD2 . PHE A 2349 35 . -0.552 -9.974 20.684 1.00 19.43 ? ? ? ? ? . 35 PHE A CD2 2349 ATOM 265 C CE1 . PHE A 2349 35 . 1.605 -11.695 20.708 1.00 19.02 ? ? ? ? ? . 35 PHE A CE1 2349 ATOM 266 C CE2 . PHE A 2349 35 . -0.759 -11.344 20.614 1.00 19.14 ? ? ? ? ? . 35 PHE A CE2 2349 ATOM 267 C CZ . PHE A 2349 35 . 0.321 -12.205 20.626 1.00 19.19 ? ? ? ? ? . 35 PHE A CZ 2349 ATOM 268 N N . SER A 2349 36 . 0.344 -5.181 18.822 1.00 17.49 ? ? ? ? ? . 36 SER A N 2349 ATOM 269 C CA . SER A 2349 36 . 0.415 -3.732 18.583 1.00 18.12 ? ? ? ? ? . 36 SER A CA 2349 ATOM 270 C C . SER A 2349 36 . -0.954 -3.153 18.254 1.00 17.25 ? ? ? ? ? . 36 SER A C 2349 ATOM 271 O O . SER A 2349 36 . -1.942 -3.878 18.155 1.00 16.75 ? ? ? ? ? . 36 SER A O 2349 ATOM 272 C CB . SER A 2349 36 . 1.391 -3.425 17.436 1.00 19.11 ? ? ? ? ? . 36 SER A CB 2349 ATOM 273 O OG . SER A 2349 36 . 1.744 -2.041 17.380 1.00 20.12 ? ? ? ? ? . 36 SER A OG 2349 ATOM 274 N N . ALA A 2349 37 . -0.999 -1.835 18.129 1.00 16.02 ? ? ? ? ? . 37 ALA A N 2349 ATOM 275 C CA . ALA A 2349 37 . -2.210 -1.132 17.705 1.00 17.21 ? ? ? ? ? . 37 ALA A CA 2349 ATOM 276 C C . ALA A 2349 37 . -1.822 0.227 17.163 1.00 16.58 ? ? ? ? ? . 37 ALA A C 2349 ATOM 277 O O . ALA A 2349 37 . -0.894 0.865 17.681 1.00 16.07 ? ? ? ? ? . 37 ALA A O 2349 ATOM 278 C CB . ALA A 2349 37 . -3.176 -0.987 18.865 1.00 16.09 ? ? ? ? ? . 37 ALA A CB 2349 ATOM 279 N N . SER A 2349 38 . -2.538 0.673 16.134 1.00 16.09 ? ? ? ? ? . 38 SER A N 2349 ATOM 280 C CA . SER A 2349 38 . -2.180 1.894 15.393 1.00 15.94 ? ? ? ? ? . 38 SER A CA 2349 ATOM 281 C C . SER A 2349 38 . -2.215 3.154 16.234 1.00 16.06 ? ? ? ? ? . 38 SER A C 2349 ATOM 282 O O . SER A 2349 38 . -1.492 4.108 15.933 1.00 15.57 ? ? ? ? ? . 38 SER A O 2349 ATOM 283 C CB . SER A 2349 38 . -3.111 2.110 14.198 1.00 15.53 ? ? ? ? ? . 38 SER A CB 2349 ATOM 284 O OG . SER A 2349 38 . -4.417 2.483 14.611 1.00 13.61 ? ? ? ? ? . 38 SER A OG 2349 ATOM 285 N N . TRP A 2349 39 . -3.083 3.153 17.250 1.00 14.29 ? ? ? ? ? . 39 TRP A N 2349 ATOM 286 C CA . TRP A 2349 39 . -3.327 4.323 18.102 1.00 15.81 ? ? ? ? ? . 39 TRP A CA 2349 ATOM 287 C C . TRP A 2349 39 . -2.576 4.292 19.439 1.00 15.54 ? ? ? ? ? . 39 TRP A C 2349 ATOM 288 O O . TRP A 2349 39 . -2.677 5.230 20.197 1.00 14.28 ? ? ? ? ? . 39 TRP A O 2349 ATOM 289 C CB . TRP A 2349 39 . -4.835 4.560 18.336 1.00 16.03 ? ? ? ? ? . 39 TRP A CB 2349 ATOM 290 C CG . TRP A 2349 39 . -5.696 3.342 18.284 1.00 17.02 ? ? ? ? ? . 39 TRP A CG 2349 ATOM 291 C CD1 . TRP A 2349 39 . -6.597 3.017 17.301 1.00 16.62 ? ? ? ? ? . 39 TRP A CD1 2349 ATOM 292 C CD2 . TRP A 2349 39 . -5.734 2.265 19.233 1.00 17.48 ? ? ? ? ? . 39 TRP A CD2 2349 ATOM 293 C CE2 . TRP A 2349 39 . -6.689 1.329 18.758 1.00 16.65 ? ? ? ? ? . 39 TRP A CE2 2349 ATOM 294 C CE3 . TRP A 2349 39 . -5.061 2.002 20.438 1.00 17.08 ? ? ? ? ? . 39 TRP A CE3 2349 ATOM 295 N NE1 . TRP A 2349 39 . -7.186 1.815 17.579 1.00 16.89 ? ? ? ? ? . 39 TRP A NE1 2349 ATOM 296 C CZ2 . TRP A 2349 39 . -6.978 0.143 19.435 1.00 17.13 ? ? ? ? ? . 39 TRP A CZ2 2349 ATOM 297 C CZ3 . TRP A 2349 39 . -5.351 0.824 21.116 1.00 17.20 ? ? ? ? ? . 39 TRP A CZ3 2349 ATOM 298 C CH2 . TRP A 2349 39 . -6.305 -0.098 20.607 1.00 17.58 ? ? ? ? ? . 39 TRP A CH2 2349 ATOM 299 N N A CYS A 2349 40 . -1.820 3.233 19.710 0.50 15.53 ? ? ? ? ? . 40 CYS A N 2349 ATOM 300 N N B CYS A 2349 40 . -1.828 3.220 19.708 0.50 15.76 ? ? ? ? ? . 40 CYS A N 2349 ATOM 301 C CA A CYS A 2349 40 . -1.099 3.113 20.973 0.50 15.94 ? ? ? ? ? . 40 CYS A CA 2349 ATOM 302 C CA B CYS A 2349 40 . -1.048 3.086 20.945 0.50 16.31 ? ? ? ? ? . 40 CYS A CA 2349 ATOM 303 C C A CYS A 2349 40 . 0.252 3.841 20.875 0.50 15.63 ? ? ? ? ? . 40 CYS A C 2349 ATOM 304 C C B CYS A 2349 40 . 0.259 3.881 20.821 0.50 15.84 ? ? ? ? ? . 40 CYS A C 2349 ATOM 305 O O A CYS A 2349 40 . 1.104 3.413 20.104 0.50 15.01 ? ? ? ? ? . 40 CYS A O 2349 ATOM 306 O O B CYS A 2349 40 . 1.084 3.541 19.979 0.50 15.24 ? ? ? ? ? . 40 CYS A O 2349 ATOM 307 C CB A CYS A 2349 40 . -0.881 1.639 21.293 0.50 17.19 ? ? ? ? ? . 40 CYS A CB 2349 ATOM 308 C CB B CYS A 2349 40 . -0.732 1.603 21.194 0.50 17.85 ? ? ? ? ? . 40 CYS A CB 2349 ATOM 309 S SG A CYS A 2349 40 . -0.070 1.366 22.877 0.50 18.83 ? ? ? ? ? . 40 CYS A SG 2349 ATOM 310 S SG B CYS A 2349 40 . 0.692 1.280 22.270 0.50 20.15 ? ? ? ? ? . 40 CYS A SG 2349 ATOM 311 N N . PRO A 2349 41 . 0.452 4.940 21.641 1.00 15.67 ? ? ? ? ? . 41 PRO A N 2349 ATOM 312 C CA . PRO A 2349 41 . 1.703 5.735 21.475 1.00 16.29 ? ? ? ? ? . 41 PRO A CA 2349 ATOM 313 C C . PRO A 2349 41 . 3.027 4.964 21.556 1.00 17.16 ? ? ? ? ? . 41 PRO A C 2349 ATOM 314 O O . PRO A 2349 41 . 3.835 5.088 20.625 1.00 16.58 ? ? ? ? ? . 41 PRO A O 2349 ATOM 315 C CB . PRO A 2349 41 . 1.589 6.838 22.534 1.00 16.29 ? ? ? ? ? . 41 PRO A CB 2349 ATOM 316 C CG . PRO A 2349 41 . 0.113 6.972 22.756 1.00 17.02 ? ? ? ? ? . 41 PRO A CG 2349 ATOM 317 C CD . PRO A 2349 41 . -0.466 5.598 22.594 1.00 16.25 ? ? ? ? ? . 41 PRO A CD 2349 ATOM 318 N N . PRO A 2349 42 . 3.238 4.137 22.603 1.00 16.73 ? ? ? ? ? . 42 PRO A N 2349 ATOM 319 C CA . PRO A 2349 42 . 4.509 3.413 22.587 1.00 16.97 ? ? ? ? ? . 42 PRO A CA 2349 ATOM 320 C C . PRO A 2349 42 . 4.682 2.470 21.399 1.00 17.31 ? ? ? ? ? . 42 PRO A C 2349 ATOM 321 O O . PRO A 2349 42 . 5.815 2.236 21.007 1.00 18.01 ? ? ? ? ? . 42 PRO A O 2349 ATOM 322 C CB . PRO A 2349 42 . 4.524 2.635 23.913 1.00 18.24 ? ? ? ? ? . 42 PRO A CB 2349 ATOM 323 C CG . PRO A 2349 42 . 3.144 2.716 24.442 1.00 20.34 ? ? ? ? ? . 42 PRO A CG 2349 ATOM 324 C CD . PRO A 2349 42 . 2.500 3.930 23.859 1.00 17.99 ? ? ? ? ? . 42 PRO A CD 2349 ATOM 325 N N . CYS A 2349 43 . 3.583 1.953 20.830 1.00 17.08 ? ? ? ? ? . 43 CYS A N 2349 ATOM 326 C CA . CYS A 2349 43 . 3.654 1.131 19.615 1.00 17.71 ? ? ? ? ? . 43 CYS A CA 2349 ATOM 327 C C . CYS A 2349 43 . 4.071 1.965 18.412 1.00 18.28 ? ? ? ? ? . 43 CYS A C 2349 ATOM 328 O O . CYS A 2349 43 . 4.896 1.539 17.592 1.00 17.92 ? ? ? ? ? . 43 CYS A O 2349 ATOM 329 C CB . CYS A 2349 43 . 2.302 0.486 19.283 1.00 16.62 ? ? ? ? ? . 43 CYS A CB 2349 ATOM 330 S SG . CYS A 2349 43 . 1.804 -0.806 20.436 1.00 17.97 ? ? ? ? ? . 43 CYS A SG 2349 ATOM 331 N N . ARG A 2349 44 . 3.472 3.148 18.300 1.00 18.14 ? ? ? ? ? . 44 ARG A N 2349 ATOM 332 C CA . ARG A 2349 44 . 3.794 4.048 17.197 1.00 19.48 ? ? ? ? ? . 44 ARG A CA 2349 ATOM 333 C C . ARG A 2349 44 . 5.273 4.436 17.232 1.00 18.72 ? ? ? ? ? . 44 ARG A C 2349 ATOM 334 O O . ARG A 2349 44 . 5.871 4.609 16.184 1.00 18.31 ? ? ? ? ? . 44 ARG A O 2349 ATOM 335 C CB . ARG A 2349 44 . 2.889 5.272 17.211 1.00 19.31 ? ? ? ? ? . 44 ARG A CB 2349 ATOM 336 C CG . ARG A 2349 44 . 1.429 4.933 16.938 1.00 20.47 ? ? ? ? ? . 44 ARG A CG 2349 ATOM 337 C CD . ARG A 2349 44 . 0.501 5.909 17.620 1.00 25.71 ? ? ? ? ? . 44 ARG A CD 2349 ATOM 338 N NE . ARG A 2349 44 . 0.489 7.222 16.986 1.00 27.26 ? ? ? ? ? . 44 ARG A NE 2349 ATOM 339 C CZ . ARG A 2349 44 . -0.417 7.656 16.109 1.00 32.49 ? ? ? ? ? . 44 ARG A CZ 2349 ATOM 340 N NH1 . ARG A 2349 44 . -1.424 6.879 15.692 1.00 36.29 ? ? ? ? ? 1+ 44 ARG A NH1 2349 ATOM 341 N NH2 . ARG A 2349 44 . -0.309 8.895 15.634 1.00 31.30 ? ? ? ? ? . 44 ARG A NH2 2349 ATOM 342 N N . GLY A 2349 45 . 5.852 4.549 18.432 1.00 16.87 ? ? ? ? ? . 45 GLY A N 2349 ATOM 343 C CA . GLY A 2349 45 . 7.291 4.825 18.587 1.00 16.30 ? ? ? ? ? . 45 GLY A CA 2349 ATOM 344 C C . GLY A 2349 45 . 8.197 3.625 18.399 1.00 17.31 ? ? ? ? ? . 45 GLY A C 2349 ATOM 345 O O . GLY A 2349 45 . 9.343 3.761 17.968 1.00 16.80 ? ? ? ? ? . 45 GLY A O 2349 ATOM 346 N N . PHE A 2349 46 . 7.690 2.440 18.711 1.00 17.16 ? ? ? ? ? . 46 PHE A N 2349 ATOM 347 C CA . PHE A 2349 46 . 8.479 1.220 18.586 1.00 16.13 ? ? ? ? ? . 46 PHE A CA 2349 ATOM 348 C C . PHE A 2349 46 . 8.512 0.651 17.162 1.00 16.60 ? ? ? ? ? . 46 PHE A C 2349 ATOM 349 O O . PHE A 2349 46 . 9.535 0.198 16.710 1.00 16.70 ? ? ? ? ? . 46 PHE A O 2349 ATOM 350 C CB . PHE A 2349 46 . 7.967 0.150 19.541 1.00 15.86 ? ? ? ? ? . 46 PHE A CB 2349 ATOM 351 C CG . PHE A 2349 46 . 8.771 -1.108 19.489 1.00 16.05 ? ? ? ? ? . 46 PHE A CG 2349 ATOM 352 C CD1 . PHE A 2349 46 . 10.130 -1.082 19.799 1.00 17.33 ? ? ? ? ? . 46 PHE A CD1 2349 ATOM 353 C CD2 . PHE A 2349 46 . 8.199 -2.300 19.084 1.00 17.49 ? ? ? ? ? . 46 PHE A CD2 2349 ATOM 354 C CE1 . PHE A 2349 46 . 10.889 -2.235 19.714 1.00 18.28 ? ? ? ? ? . 46 PHE A CE1 2349 ATOM 355 C CE2 . PHE A 2349 46 . 8.954 -3.462 19.011 1.00 17.09 ? ? ? ? ? . 46 PHE A CE2 2349 ATOM 356 C CZ . PHE A 2349 46 . 10.300 -3.424 19.324 1.00 17.72 ? ? ? ? ? . 46 PHE A CZ 2349 ATOM 357 N N . THR A 2349 47 . 7.376 0.671 16.476 1.00 16.70 ? ? ? ? ? . 47 THR A N 2349 ATOM 358 C CA . THR A 2349 47 . 7.269 0.187 15.102 1.00 15.83 ? ? ? ? ? . 47 THR A CA 2349 ATOM 359 C C . THR A 2349 47 . 8.421 0.636 14.151 1.00 16.94 ? ? ? ? ? . 47 THR A C 2349 ATOM 360 O O . THR A 2349 47 . 9.011 -0.218 13.479 1.00 16.96 ? ? ? ? ? . 47 THR A O 2349 ATOM 361 C CB . THR A 2349 47 . 5.867 0.510 14.547 1.00 16.66 ? ? ? ? ? . 47 THR A CB 2349 ATOM 362 C CG2 . THR A 2349 47 . 5.752 0.297 13.034 1.00 16.80 ? ? ? ? ? . 47 THR A CG2 2349 ATOM 363 O OG1 . THR A 2349 47 . 4.915 -0.318 15.229 1.00 18.14 ? ? ? ? ? . 47 THR A OG1 2349 ATOM 364 N N . PRO A 2349 48 . 8.758 1.947 14.112 1.00 16.14 ? ? ? ? ? . 48 PRO A N 2349 ATOM 365 C CA . PRO A 2349 48 . 9.871 2.352 13.228 1.00 15.16 ? ? ? ? ? . 48 PRO A CA 2349 ATOM 366 C C . PRO A 2349 48 . 11.242 1.798 13.654 1.00 15.43 ? ? ? ? ? . 48 PRO A C 2349 ATOM 367 O O . PRO A 2349 48 . 12.110 1.557 12.800 1.00 15.62 ? ? ? ? ? . 48 PRO A O 2349 ATOM 368 C CB . PRO A 2349 48 . 9.825 3.888 13.265 1.00 15.95 ? ? ? ? ? . 48 PRO A CB 2349 ATOM 369 C CG . PRO A 2349 48 . 9.028 4.237 14.475 1.00 16.18 ? ? ? ? ? . 48 PRO A CG 2349 ATOM 370 C CD . PRO A 2349 48 . 8.057 3.109 14.670 1.00 16.84 ? ? ? ? ? . 48 PRO A CD 2349 ATOM 371 N N . VAL A 2349 49 . 11.421 1.568 14.952 1.00 15.24 ? ? ? ? ? . 49 VAL A N 2349 ATOM 372 C CA . VAL A 2349 49 . 12.653 0.979 15.497 1.00 15.00 ? ? ? ? ? . 49 VAL A CA 2349 ATOM 373 C C . VAL A 2349 49 . 12.738 -0.490 15.080 1.00 16.44 ? ? ? ? ? . 49 VAL A C 2349 ATOM 374 O O . VAL A 2349 49 . 13.785 -0.970 14.589 1.00 17.54 ? ? ? ? ? . 49 VAL A O 2349 ATOM 375 C CB . VAL A 2349 49 . 12.683 1.119 17.046 1.00 14.01 ? ? ? ? ? . 49 VAL A CB 2349 ATOM 376 C CG1 . VAL A 2349 49 . 13.850 0.377 17.659 1.00 13.62 ? ? ? ? ? . 49 VAL A CG1 2349 ATOM 377 C CG2 . VAL A 2349 49 . 12.703 2.591 17.436 1.00 13.12 ? ? ? ? ? . 49 VAL A CG2 2349 ATOM 378 N N . LEU A 2349 50 . 11.629 -1.205 15.264 1.00 16.04 ? ? ? ? ? . 50 LEU A N 2349 ATOM 379 C CA . LEU A 2349 50 . 11.549 -2.607 14.859 1.00 16.65 ? ? ? ? ? . 50 LEU A CA 2349 ATOM 380 C C . LEU A 2349 50 . 11.728 -2.754 13.346 1.00 16.14 ? ? ? ? ? . 50 LEU A C 2349 ATOM 381 O O . LEU A 2349 50 . 12.392 -3.689 12.896 1.00 17.52 ? ? ? ? ? . 50 LEU A O 2349 ATOM 382 C CB . LEU A 2349 50 . 10.228 -3.235 15.291 1.00 17.24 ? ? ? ? ? . 50 LEU A CB 2349 ATOM 383 C CG . LEU A 2349 50 . 10.134 -4.760 15.088 1.00 18.60 ? ? ? ? ? . 50 LEU A CG 2349 ATOM 384 C CD1 . LEU A 2349 50 . 11.292 -5.525 15.736 1.00 18.52 ? ? ? ? ? . 50 LEU A CD1 2349 ATOM 385 C CD2 . LEU A 2349 50 . 8.808 -5.265 15.625 1.00 20.67 ? ? ? ? ? . 50 LEU A CD2 2349 ATOM 386 N N . ALA A 2349 51 . 11.158 -1.827 12.578 1.00 15.16 ? ? ? ? ? . 51 ALA A N 2349 ATOM 387 C CA . ALA A 2349 51 . 11.350 -1.791 11.114 1.00 16.39 ? ? ? ? ? . 51 ALA A CA 2349 ATOM 388 C C . ALA A 2349 51 . 12.807 -1.689 10.702 1.00 16.39 ? ? ? ? ? . 51 ALA A C 2349 ATOM 389 O O . ALA A 2349 51 . 13.234 -2.388 9.789 1.00 16.12 ? ? ? ? ? . 51 ALA A O 2349 ATOM 390 C CB . ALA A 2349 51 . 10.558 -0.659 10.489 1.00 16.94 ? ? ? ? ? . 51 ALA A CB 2349 ATOM 391 N N . GLU A 2349 52 . 13.571 -0.833 11.380 1.00 15.83 ? ? ? ? ? . 52 GLU A N 2349 ATOM 392 C CA . GLU A 2349 52 . 15.018 -0.741 11.136 1.00 17.29 ? ? ? ? ? . 52 GLU A CA 2349 ATOM 393 C C . GLU A 2349 52 . 15.738 -2.056 11.452 1.00 16.77 ? ? ? ? ? . 52 GLU A C 2349 ATOM 394 O O . GLU A 2349 52 . 16.547 -2.538 10.644 1.00 17.83 ? ? ? ? ? . 52 GLU A O 2349 ATOM 395 C CB . GLU A 2349 52 . 15.655 0.398 11.929 1.00 19.04 ? ? ? ? ? . 52 GLU A CB 2349 ATOM 396 C CG . GLU A 2349 52 . 15.197 1.779 11.502 1.00 23.10 ? ? ? ? ? . 52 GLU A CG 2349 ATOM 397 C CD . GLU A 2349 52 . 15.652 2.158 10.111 1.00 27.07 ? ? ? ? ? . 52 GLU A CD 2349 ATOM 398 O OE1 . GLU A 2349 52 . 16.805 1.871 9.753 1.00 26.53 ? ? ? ? ? . 52 GLU A OE1 2349 ATOM 399 O OE2 . GLU A 2349 52 . 14.838 2.741 9.372 1.00 35.08 ? ? ? ? ? 1- 52 GLU A OE2 2349 ATOM 400 N N . PHE A 2349 53 . 15.440 -2.626 12.617 1.00 17.09 ? ? ? ? ? . 53 PHE A N 2349 ATOM 401 C CA . PHE A 2349 53 . 15.961 -3.927 13.008 1.00 17.72 ? ? ? ? ? . 53 PHE A CA 2349 ATOM 402 C C . PHE A 2349 53 . 15.659 -5.004 11.960 1.00 18.04 ? ? ? ? ? . 53 PHE A C 2349 ATOM 403 O O . PHE A 2349 53 . 16.544 -5.765 11.559 1.00 17.15 ? ? ? ? ? . 53 PHE A O 2349 ATOM 404 C CB . PHE A 2349 53 . 15.394 -4.344 14.367 1.00 17.66 ? ? ? ? ? . 53 PHE A CB 2349 ATOM 405 C CG . PHE A 2349 53 . 16.073 -5.523 14.955 1.00 17.72 ? ? ? ? ? . 53 PHE A CG 2349 ATOM 406 C CD1 . PHE A 2349 53 . 17.204 -5.365 15.759 1.00 19.84 ? ? ? ? ? . 53 PHE A CD1 2349 ATOM 407 C CD2 . PHE A 2349 53 . 15.613 -6.800 14.692 1.00 18.67 ? ? ? ? ? . 53 PHE A CD2 2349 ATOM 408 C CE1 . PHE A 2349 53 . 17.855 -6.470 16.294 1.00 18.69 ? ? ? ? ? . 53 PHE A CE1 2349 ATOM 409 C CE2 . PHE A 2349 53 . 16.250 -7.909 15.237 1.00 19.49 ? ? ? ? ? . 53 PHE A CE2 2349 ATOM 410 C CZ . PHE A 2349 53 . 17.381 -7.740 16.022 1.00 19.50 ? ? ? ? ? . 53 PHE A CZ 2349 ATOM 411 N N . TYR A 2349 54 . 14.402 -5.066 11.538 1.00 18.62 ? ? ? ? ? . 54 TYR A N 2349 ATOM 412 C CA . TYR A 2349 54 . 13.957 -5.985 10.484 1.00 16.78 ? ? ? ? ? . 54 TYR A CA 2349 ATOM 413 C C . TYR A 2349 54 . 14.740 -5.808 9.197 1.00 17.12 ? ? ? ? ? . 54 TYR A C 2349 ATOM 414 O O . TYR A 2349 54 . 15.274 -6.777 8.637 1.00 16.38 ? ? ? ? ? . 54 TYR A O 2349 ATOM 415 C CB . TYR A 2349 54 . 12.465 -5.744 10.204 1.00 17.54 ? ? ? ? ? . 54 TYR A CB 2349 ATOM 416 C CG . TYR A 2349 54 . 11.834 -6.704 9.220 1.00 17.88 ? ? ? ? ? . 54 TYR A CG 2349 ATOM 417 C CD1 . TYR A 2349 54 . 11.284 -7.902 9.655 1.00 17.99 ? ? ? ? ? . 54 TYR A CD1 2349 ATOM 418 C CD2 . TYR A 2349 54 . 11.783 -6.414 7.859 1.00 18.12 ? ? ? ? ? . 54 TYR A CD2 2349 ATOM 419 C CE1 . TYR A 2349 54 . 10.703 -8.787 8.776 1.00 17.40 ? ? ? ? ? . 54 TYR A CE1 2349 ATOM 420 C CE2 . TYR A 2349 54 . 11.201 -7.294 6.965 1.00 18.18 ? ? ? ? ? . 54 TYR A CE2 2349 ATOM 421 C CZ . TYR A 2349 54 . 10.656 -8.477 7.430 1.00 18.40 ? ? ? ? ? . 54 TYR A CZ 2349 ATOM 422 O OH . TYR A 2349 54 . 10.066 -9.352 6.548 1.00 18.64 ? ? ? ? ? . 54 TYR A OH 2349 ATOM 423 N N . GLU A 2349 55 . 14.825 -4.567 8.729 1.00 18.35 ? ? ? ? ? . 55 GLU A N 2349 ATOM 424 C CA . GLU A 2349 55 . 15.479 -4.298 7.450 1.00 19.54 ? ? ? ? ? . 55 GLU A CA 2349 ATOM 425 C C . GLU A 2349 55 . 16.941 -4.728 7.457 1.00 17.47 ? ? ? ? ? . 55 GLU A C 2349 ATOM 426 O O . GLU A 2349 55 . 17.426 -5.225 6.444 1.00 16.00 ? ? ? ? ? . 55 GLU A O 2349 ATOM 427 C CB . GLU A 2349 55 . 15.344 -2.832 7.037 1.00 23.35 ? ? ? ? ? . 55 GLU A CB 2349 ATOM 428 C CG . GLU A 2349 55 . 13.904 -2.394 6.757 1.00 27.78 ? ? ? ? ? . 55 GLU A CG 2349 ATOM 429 C CD . GLU A 2349 55 . 13.379 -2.755 5.374 1.00 33.34 ? ? ? ? ? . 55 GLU A CD 2349 ATOM 430 O OE1 . GLU A 2349 55 . 13.957 -3.640 4.695 1.00 38.81 ? ? ? ? ? . 55 GLU A OE1 2349 ATOM 431 O OE2 . GLU A 2349 55 . 12.365 -2.144 4.970 1.00 33.79 ? ? ? ? ? 1- 55 GLU A OE2 2349 ATOM 432 N N . LYS A 2349 56 . 17.630 -4.527 8.582 1.00 17.29 ? ? ? ? ? . 56 LYS A N 2349 ATOM 433 C CA . LYS A 2349 56 . 19.040 -4.884 8.705 1.00 17.51 ? ? ? ? ? . 56 LYS A CA 2349 ATOM 434 C C . LYS A 2349 56 . 19.255 -6.396 8.816 1.00 15.74 ? ? ? ? ? . 56 LYS A C 2349 ATOM 435 O O . LYS A 2349 56 . 20.181 -6.935 8.183 1.00 16.74 ? ? ? ? ? . 56 LYS A O 2349 ATOM 436 C CB . LYS A 2349 56 . 19.699 -4.158 9.902 1.00 20.10 ? ? ? ? ? . 56 LYS A CB 2349 ATOM 437 C CG . LYS A 2349 56 . 21.202 -4.417 10.024 1.00 22.06 ? ? ? ? ? . 56 LYS A CG 2349 ATOM 438 C CD . LYS A 2349 56 . 21.921 -3.570 11.086 1.00 24.35 ? ? ? ? ? . 56 LYS A CD 2349 ATOM 439 C CE . LYS A 2349 56 . 23.451 -3.707 10.942 1.00 26.58 ? ? ? ? ? . 56 LYS A CE 2349 ATOM 440 N NZ . LYS A 2349 56 . 24.320 -2.988 11.937 1.00 24.67 ? ? ? ? ? 1+ 56 LYS A NZ 2349 ATOM 441 N N . HIS A 2349 57 . 18.415 -7.076 9.599 1.00 14.57 ? ? ? ? ? . 57 HIS A N 2349 ATOM 442 C CA . HIS A 2349 57 . 18.718 -8.424 10.085 1.00 15.29 ? ? ? ? ? . 57 HIS A CA 2349 ATOM 443 C C . HIS A 2349 57 . 17.814 -9.569 9.624 1.00 15.31 ? ? ? ? ? . 57 HIS A C 2349 ATOM 444 O O . HIS A 2349 57 . 18.170 -10.726 9.880 1.00 16.33 ? ? ? ? ? . 57 HIS A O 2349 ATOM 445 C CB . HIS A 2349 57 . 18.690 -8.468 11.612 1.00 15.83 ? ? ? ? ? . 57 HIS A CB 2349 ATOM 446 C CG . HIS A 2349 57 . 19.586 -7.481 12.281 1.00 16.66 ? ? ? ? ? . 57 HIS A CG 2349 ATOM 447 C CD2 . HIS A 2349 57 . 19.312 -6.513 13.190 1.00 18.19 ? ? ? ? ? . 57 HIS A CD2 2349 ATOM 448 N ND1 . HIS A 2349 57 . 20.944 -7.457 12.094 1.00 16.54 ? ? ? ? ? . 57 HIS A ND1 2349 ATOM 449 C CE1 . HIS A 2349 57 . 21.471 -6.502 12.836 1.00 18.76 ? ? ? ? ? . 57 HIS A CE1 2349 ATOM 450 N NE2 . HIS A 2349 57 . 20.502 -5.918 13.519 1.00 17.63 ? ? ? ? ? . 57 HIS A NE2 2349 ATOM 451 N N . HIS A 2349 58 . 16.668 -9.294 8.996 1.00 15.07 ? ? ? ? ? . 58 HIS A N 2349 ATOM 452 C CA . HIS A 2349 58 . 15.663 -10.363 8.809 1.00 15.32 ? ? ? ? ? . 58 HIS A CA 2349 ATOM 453 C C . HIS A 2349 58 . 16.142 -11.508 7.916 1.00 15.60 ? ? ? ? ? . 58 HIS A C 2349 ATOM 454 O O . HIS A 2349 58 . 15.814 -12.666 8.172 1.00 16.71 ? ? ? ? ? . 58 HIS A O 2349 ATOM 455 C CB . HIS A 2349 58 . 14.270 -9.838 8.384 1.00 16.50 ? ? ? ? ? . 58 HIS A CB 2349 ATOM 456 C CG . HIS A 2349 58 . 14.110 -9.576 6.917 1.00 16.28 ? ? ? ? ? . 58 HIS A CG 2349 ATOM 457 C CD2 . HIS A 2349 58 . 13.530 -10.314 5.939 1.00 17.28 ? ? ? ? ? . 58 HIS A CD2 2349 ATOM 458 N ND1 . HIS A 2349 58 . 14.514 -8.401 6.318 1.00 18.08 ? ? ? ? ? . 58 HIS A ND1 2349 ATOM 459 C CE1 . HIS A 2349 58 . 14.236 -8.449 5.025 1.00 19.03 ? ? ? ? ? . 58 HIS A CE1 2349 ATOM 460 N NE2 . HIS A 2349 58 . 13.622 -9.592 4.773 1.00 19.90 ? ? ? ? ? . 58 HIS A NE2 2349 ATOM 461 N N . VAL A 2349 59 . 16.953 -11.183 6.909 1.00 14.27 ? ? ? ? ? . 59 VAL A N 2349 ATOM 462 C CA . VAL A 2349 59 . 17.521 -12.205 6.060 1.00 14.71 ? ? ? ? ? . 59 VAL A CA 2349 ATOM 463 C C . VAL A 2349 59 . 18.661 -12.908 6.783 1.00 14.94 ? ? ? ? ? . 59 VAL A C 2349 ATOM 464 O O . VAL A 2349 59 . 18.645 -14.134 6.937 1.00 14.29 ? ? ? ? ? . 59 VAL A O 2349 ATOM 465 C CB . VAL A 2349 59 . 17.994 -11.612 4.722 1.00 14.66 ? ? ? ? ? . 59 VAL A CB 2349 ATOM 466 C CG1 . VAL A 2349 59 . 18.666 -12.682 3.873 1.00 14.25 ? ? ? ? ? . 59 VAL A CG1 2349 ATOM 467 C CG2 . VAL A 2349 59 . 16.805 -10.993 3.980 1.00 14.94 ? ? ? ? ? . 59 VAL A CG2 2349 ATOM 468 N N . ALA A 2349 60 . 19.645 -12.144 7.246 1.00 15.73 ? ? ? ? ? . 60 ALA A N 2349 ATOM 469 C CA . ALA A 2349 60 . 20.864 -12.747 7.823 1.00 17.51 ? ? ? ? ? . 60 ALA A CA 2349 ATOM 470 C C . ALA A 2349 60 . 20.557 -13.591 9.054 1.00 16.03 ? ? ? ? ? . 60 ALA A C 2349 ATOM 471 O O . ALA A 2349 60 . 21.143 -14.653 9.242 1.00 15.29 ? ? ? ? ? . 60 ALA A O 2349 ATOM 472 C CB . ALA A 2349 60 . 21.898 -11.674 8.149 1.00 18.78 ? ? ? ? ? . 60 ALA A CB 2349 ATOM 473 N N . LYS A 2349 61 . 19.598 -13.149 9.864 1.00 14.83 ? ? ? ? ? . 61 LYS A N 2349 ATOM 474 C CA . LYS A 2349 61 . 19.226 -13.871 11.088 1.00 15.73 ? ? ? ? ? . 61 LYS A CA 2349 ATOM 475 C C . LYS A 2349 61 . 17.927 -14.693 10.936 1.00 17.18 ? ? ? ? ? . 61 LYS A C 2349 ATOM 476 O O . LYS A 2349 61 . 17.409 -15.236 11.923 1.00 18.10 ? ? ? ? ? . 61 LYS A O 2349 ATOM 477 C CB . LYS A 2349 61 . 19.132 -12.891 12.265 1.00 15.99 ? ? ? ? ? . 61 LYS A CB 2349 ATOM 478 C CG . LYS A 2349 61 . 20.452 -12.166 12.504 1.00 18.28 ? ? ? ? ? . 61 LYS A CG 2349 ATOM 479 C CD . LYS A 2349 61 . 20.439 -11.283 13.741 1.00 20.10 ? ? ? ? ? . 61 LYS A CD 2349 ATOM 480 C CE . LYS A 2349 61 . 21.754 -10.505 13.895 1.00 20.17 ? ? ? ? ? . 61 LYS A CE 2349 ATOM 481 N NZ . LYS A 2349 61 . 22.893 -11.355 14.328 1.00 19.55 ? ? ? ? ? 1+ 61 LYS A NZ 2349 ATOM 482 N N . ASN A 2349 62 . 17.428 -14.784 9.701 1.00 16.86 ? ? ? ? ? . 62 ASN A N 2349 ATOM 483 C CA . ASN A 2349 62 . 16.360 -15.705 9.305 1.00 16.87 ? ? ? ? ? . 62 ASN A CA 2349 ATOM 484 C C . ASN A 2349 62 . 15.135 -15.622 10.221 1.00 16.20 ? ? ? ? ? . 62 ASN A C 2349 ATOM 485 O O . ASN A 2349 62 . 14.743 -16.606 10.871 1.00 15.82 ? ? ? ? ? . 62 ASN A O 2349 ATOM 486 C CB . ASN A 2349 62 . 16.895 -17.137 9.242 1.00 17.98 ? ? ? ? ? . 62 ASN A CB 2349 ATOM 487 C CG . ASN A 2349 62 . 15.989 -18.059 8.453 1.00 17.03 ? ? ? ? ? . 62 ASN A CG 2349 ATOM 488 N ND2 . ASN A 2349 62 . 15.720 -19.247 8.994 1.00 15.43 ? ? ? ? ? . 62 ASN A ND2 2349 ATOM 489 O OD1 . ASN A 2349 62 . 15.544 -17.708 7.365 1.00 16.98 ? ? ? ? ? . 62 ASN A OD1 2349 ATOM 490 N N . PHE A 2349 63 . 14.555 -14.436 10.284 1.00 15.83 ? ? ? ? ? . 63 PHE A N 2349 ATOM 491 C CA . PHE A 2349 63 . 13.315 -14.245 11.005 1.00 15.98 ? ? ? ? ? . 63 PHE A CA 2349 ATOM 492 C C . PHE A 2349 63 . 12.272 -13.479 10.209 1.00 16.65 ? ? ? ? ? . 63 PHE A C 2349 ATOM 493 O O . PHE A 2349 63 . 12.540 -12.876 9.147 1.00 14.62 ? ? ? ? ? . 63 PHE A O 2349 ATOM 494 C CB . PHE A 2349 63 . 13.555 -13.608 12.392 1.00 15.93 ? ? ? ? ? . 63 PHE A CB 2349 ATOM 495 C CG . PHE A 2349 63 . 14.065 -12.191 12.351 1.00 16.47 ? ? ? ? ? . 63 PHE A CG 2349 ATOM 496 C CD1 . PHE A 2349 63 . 13.192 -11.131 12.154 1.00 17.02 ? ? ? ? ? . 63 PHE A CD1 2349 ATOM 497 C CD2 . PHE A 2349 63 . 15.419 -11.914 12.539 1.00 17.98 ? ? ? ? ? . 63 PHE A CD2 2349 ATOM 498 C CE1 . PHE A 2349 63 . 13.646 -9.823 12.123 1.00 16.99 ? ? ? ? ? . 63 PHE A CE1 2349 ATOM 499 C CE2 . PHE A 2349 63 . 15.874 -10.605 12.516 1.00 17.17 ? ? ? ? ? . 63 PHE A CE2 2349 ATOM 500 C CZ . PHE A 2349 63 . 14.992 -9.562 12.310 1.00 17.23 ? ? ? ? ? . 63 PHE A CZ 2349 ATOM 501 N N . GLU A 2349 64 . 11.065 -13.521 10.753 1.00 16.63 ? ? ? ? ? . 64 GLU A N 2349 ATOM 502 C CA . GLU A 2349 64 . 9.931 -12.790 10.211 1.00 16.06 ? ? ? ? ? . 64 GLU A CA 2349 ATOM 503 C C . GLU A 2349 64 . 9.161 -12.165 11.375 1.00 16.89 ? ? ? ? ? . 64 GLU A C 2349 ATOM 504 O O . GLU A 2349 64 . 9.251 -12.634 12.498 1.00 16.07 ? ? ? ? ? . 64 GLU A O 2349 ATOM 505 C CB . GLU A 2349 64 . 9.043 -13.756 9.433 1.00 17.67 ? ? ? ? ? . 64 GLU A CB 2349 ATOM 506 C CG . GLU A 2349 64 . 7.934 -13.109 8.651 1.00 20.12 ? ? ? ? ? . 64 GLU A CG 2349 ATOM 507 C CD . GLU A 2349 64 . 8.458 -12.085 7.676 1.00 20.42 ? ? ? ? ? . 64 GLU A CD 2349 ATOM 508 O OE1 . GLU A 2349 64 . 8.489 -10.901 8.045 1.00 19.99 ? ? ? ? ? . 64 GLU A OE1 2349 ATOM 509 O OE2 . GLU A 2349 64 . 8.839 -12.477 6.559 1.00 20.73 ? ? ? ? ? 1- 64 GLU A OE2 2349 ATOM 510 N N . VAL A 2349 65 . 8.413 -11.107 11.097 1.00 16.69 ? ? ? ? ? . 65 VAL A N 2349 ATOM 511 C CA . VAL A 2349 65 . 7.578 -10.458 12.100 1.00 15.86 ? ? ? ? ? . 65 VAL A CA 2349 ATOM 512 C C . VAL A 2349 65 . 6.140 -10.529 11.600 1.00 14.98 ? ? ? ? ? . 65 VAL A C 2349 ATOM 513 O O . VAL A 2349 65 . 5.879 -10.397 10.391 1.00 14.44 ? ? ? ? ? . 65 VAL A O 2349 ATOM 514 C CB . VAL A 2349 65 . 8.066 -9.013 12.345 1.00 17.34 ? ? ? ? ? . 65 VAL A CB 2349 ATOM 515 C CG1 . VAL A 2349 65 . 7.112 -8.225 13.239 1.00 18.32 ? ? ? ? ? . 65 VAL A CG1 2349 ATOM 516 C CG2 . VAL A 2349 65 . 9.464 -9.038 12.945 1.00 18.63 ? ? ? ? ? . 65 VAL A CG2 2349 ATOM 517 N N . VAL A 2349 66 . 5.212 -10.798 12.517 1.00 14.94 ? ? ? ? ? . 66 VAL A N 2349 ATOM 518 C CA . VAL A 2349 66 . 3.791 -10.901 12.186 1.00 15.77 ? ? ? ? ? . 66 VAL A CA 2349 ATOM 519 C C . VAL A 2349 66 . 3.013 -9.926 13.068 1.00 16.12 ? ? ? ? ? . 66 VAL A C 2349 ATOM 520 O O . VAL A 2349 66 . 2.954 -10.091 14.287 1.00 18.95 ? ? ? ? ? . 66 VAL A O 2349 ATOM 521 C CB . VAL A 2349 66 . 3.248 -12.327 12.365 1.00 15.17 ? ? ? ? ? . 66 VAL A CB 2349 ATOM 522 C CG1 . VAL A 2349 66 . 1.807 -12.407 11.883 1.00 14.64 ? ? ? ? ? . 66 VAL A CG1 2349 ATOM 523 C CG2 . VAL A 2349 66 . 4.127 -13.332 11.615 1.00 15.43 ? ? ? ? ? . 66 VAL A CG2 2349 ATOM 524 N N . LEU A 2349 67 . 2.413 -8.925 12.441 1.00 14.97 ? ? ? ? ? . 67 LEU A N 2349 ATOM 525 C CA . LEU A 2349 67 . 1.558 -7.976 13.155 1.00 15.42 ? ? ? ? ? . 67 LEU A CA 2349 ATOM 526 C C . LEU A 2349 67 . 0.311 -8.673 13.669 1.00 14.43 ? ? ? ? ? . 67 LEU A C 2349 ATOM 527 O O . LEU A 2349 67 . -0.406 -9.315 12.914 1.00 15.61 ? ? ? ? ? . 67 LEU A O 2349 ATOM 528 C CB . LEU A 2349 67 . 1.134 -6.830 12.239 1.00 16.16 ? ? ? ? ? . 67 LEU A CB 2349 ATOM 529 C CG . LEU A 2349 67 . 0.138 -5.813 12.822 1.00 16.89 ? ? ? ? ? . 67 LEU A CG 2349 ATOM 530 C CD1 . LEU A 2349 67 . 0.748 -5.117 14.038 1.00 18.06 ? ? ? ? ? . 67 LEU A CD1 2349 ATOM 531 C CD2 . LEU A 2349 67 . -0.302 -4.804 11.764 1.00 16.86 ? ? ? ? ? . 67 LEU A CD2 2349 ATOM 532 N N . ILE A 2349 68 . 0.069 -8.515 14.959 1.00 16.21 ? ? ? ? ? . 68 ILE A N 2349 ATOM 533 C CA . ILE A 2349 68 . -1.140 -8.969 15.618 1.00 16.24 ? ? ? ? ? . 68 ILE A CA 2349 ATOM 534 C C . ILE A 2349 68 . -1.759 -7.692 16.195 1.00 16.84 ? ? ? ? ? . 68 ILE A C 2349 ATOM 535 O O . ILE A 2349 68 . -1.309 -7.202 17.220 1.00 16.78 ? ? ? ? ? . 68 ILE A O 2349 ATOM 536 C CB . ILE A 2349 68 . -0.842 -9.969 16.752 1.00 15.81 ? ? ? ? ? . 68 ILE A CB 2349 ATOM 537 C CG1 . ILE A 2349 68 . 0.100 -11.106 16.287 1.00 15.85 ? ? ? ? ? . 68 ILE A CG1 2349 ATOM 538 C CG2 . ILE A 2349 68 . -2.143 -10.534 17.291 1.00 16.11 ? ? ? ? ? . 68 ILE A CG2 2349 ATOM 539 C CD1 . ILE A 2349 68 . -0.444 -11.963 15.172 1.00 15.85 ? ? ? ? ? . 68 ILE A CD1 2349 ATOM 540 N N . SER A 2349 69 . -2.769 -7.158 15.519 1.00 18.12 ? ? ? ? ? . 69 SER A N 2349 ATOM 541 C CA . SER A 2349 69 . -3.262 -5.825 15.839 1.00 18.34 ? ? ? ? ? . 69 SER A CA 2349 ATOM 542 C C . SER A 2349 69 . -4.568 -5.818 16.640 1.00 17.36 ? ? ? ? ? . 69 SER A C 2349 ATOM 543 O O . SER A 2349 69 . -5.517 -6.553 16.339 1.00 15.89 ? ? ? ? ? . 69 SER A O 2349 ATOM 544 C CB . SER A 2349 69 . -3.454 -5.013 14.563 1.00 20.93 ? ? ? ? ? . 69 SER A CB 2349 ATOM 545 O OG . SER A 2349 69 . -3.970 -3.726 14.871 1.00 22.79 ? ? ? ? ? . 69 SER A OG 2349 ATOM 546 N N . TRP A 2349 70 . -4.612 -4.932 17.630 1.00 17.71 ? ? ? ? ? . 70 TRP A N 2349 ATOM 547 C CA . TRP A 2349 70 . -5.849 -4.612 18.370 1.00 17.54 ? ? ? ? ? . 70 TRP A CA 2349 ATOM 548 C C . TRP A 2349 70 . -6.788 -3.654 17.619 1.00 16.23 ? ? ? ? ? . 70 TRP A C 2349 ATOM 549 O O . TRP A 2349 70 . -7.870 -3.325 18.129 1.00 15.84 ? ? ? ? ? . 70 TRP A O 2349 ATOM 550 C CB . TRP A 2349 70 . -5.522 -4.043 19.773 1.00 18.64 ? ? ? ? ? . 70 TRP A CB 2349 ATOM 551 C CG . TRP A 2349 70 . -5.764 -5.026 20.876 1.00 18.49 ? ? ? ? ? . 70 TRP A CG 2349 ATOM 552 C CD1 . TRP A 2349 70 . -6.897 -5.175 21.635 1.00 20.30 ? ? ? ? ? . 70 TRP A CD1 2349 ATOM 553 C CD2 . TRP A 2349 70 . -4.846 -6.010 21.326 1.00 19.25 ? ? ? ? ? . 70 TRP A CD2 2349 ATOM 554 C CE2 . TRP A 2349 70 . -5.481 -6.736 22.357 1.00 20.72 ? ? ? ? ? . 70 TRP A CE2 2349 ATOM 555 C CE3 . TRP A 2349 70 . -3.546 -6.347 20.958 1.00 20.16 ? ? ? ? ? . 70 TRP A CE3 2349 ATOM 556 N NE1 . TRP A 2349 70 . -6.733 -6.207 22.522 1.00 19.85 ? ? ? ? ? . 70 TRP A NE1 2349 ATOM 557 C CZ2 . TRP A 2349 70 . -4.852 -7.783 23.021 1.00 20.72 ? ? ? ? ? . 70 TRP A CZ2 2349 ATOM 558 C CZ3 . TRP A 2349 70 . -2.918 -7.378 21.619 1.00 21.27 ? ? ? ? ? . 70 TRP A CZ3 2349 ATOM 559 C CH2 . TRP A 2349 70 . -3.570 -8.090 22.638 1.00 22.10 ? ? ? ? ? . 70 TRP A CH2 2349 ATOM 560 N N . ASP A 2349 71 . -6.400 -3.183 16.430 1.00 14.95 ? ? ? ? ? . 71 ASP A N 2349 ATOM 561 C CA . ASP A 2349 71 . -7.261 -2.280 15.672 1.00 15.71 ? ? ? ? ? . 71 ASP A CA 2349 ATOM 562 C C . ASP A 2349 71 . -8.605 -2.930 15.328 1.00 14.08 ? ? ? ? ? . 71 ASP A C 2349 ATOM 563 O O . ASP A 2349 71 . -8.633 -4.074 14.887 1.00 13.83 ? ? ? ? ? . 71 ASP A O 2349 ATOM 564 C CB . ASP A 2349 71 . -6.575 -1.838 14.377 1.00 16.40 ? ? ? ? ? . 71 ASP A CB 2349 ATOM 565 C CG . ASP A 2349 71 . -5.488 -0.813 14.617 1.00 16.78 ? ? ? ? ? . 71 ASP A CG 2349 ATOM 566 O OD1 . ASP A 2349 71 . -5.861 0.357 14.863 1.00 16.06 ? ? ? ? ? . 71 ASP A OD1 2349 ATOM 567 O OD2 . ASP A 2349 71 . -4.277 -1.173 14.553 1.00 18.80 ? ? ? ? ? 1- 71 ASP A OD2 2349 ATOM 568 N N . GLU A 2349 72 . -9.689 -2.197 15.550 1.00 13.55 ? ? ? ? ? . 72 GLU A N 2349 ATOM 569 C CA A GLU A 2349 72 . -11.051 -2.601 15.169 0.66 14.70 ? ? ? ? ? . 72 GLU A CA 2349 ATOM 570 C CA B GLU A 2349 72 . -11.003 -2.662 15.116 0.34 14.17 ? ? ? ? ? . 72 GLU A CA 2349 ATOM 571 C C . GLU A 2349 72 . -11.544 -1.845 13.940 1.00 14.43 ? ? ? ? ? . 72 GLU A C 2349 ATOM 572 O O . GLU A 2349 72 . -12.612 -2.162 13.403 1.00 15.02 ? ? ? ? ? . 72 GLU A O 2349 ATOM 573 C CB A GLU A 2349 72 . -12.032 -2.365 16.325 0.66 15.58 ? ? ? ? ? . 72 GLU A CB 2349 ATOM 574 C CB B GLU A 2349 72 . -11.951 -2.732 16.315 0.34 14.14 ? ? ? ? ? . 72 GLU A CB 2349 ATOM 575 C CG A GLU A 2349 72 . -11.825 -3.284 17.523 0.66 17.74 ? ? ? ? ? . 72 GLU A CG 2349 ATOM 576 C CG B GLU A 2349 72 . -11.456 -3.763 17.335 0.34 14.63 ? ? ? ? ? . 72 GLU A CG 2349 ATOM 577 C CD A GLU A 2349 72 . -12.840 -3.071 18.643 0.66 18.62 ? ? ? ? ? . 72 GLU A CD 2349 ATOM 578 C CD B GLU A 2349 72 . -12.487 -4.156 18.381 0.34 15.00 ? ? ? ? ? . 72 GLU A CD 2349 ATOM 579 O OE1 A GLU A 2349 72 . -13.397 -1.946 18.785 0.66 20.42 ? ? ? ? ? . 72 GLU A OE1 2349 ATOM 580 O OE2 A GLU A 2349 72 . -13.078 -4.039 19.399 0.66 18.80 ? ? ? ? ? 1- 72 GLU A OE2 2349 ATOM 581 O OE1 B GLU A 2349 72 . -13.558 -3.519 18.446 0.34 15.59 ? ? ? ? ? . 72 GLU A OE1 2349 ATOM 582 O OE2 B GLU A 2349 72 . -12.220 -5.118 19.141 0.34 14.77 ? ? ? ? ? 1- 72 GLU A OE2 2349 ATOM 583 N N . ASN A 2349 73 . -10.789 -0.830 13.505 1.00 14.08 ? ? ? ? ? . 73 ASN A N 2349 ATOM 584 C CA . ASN A 2349 73 . -11.154 -0.041 12.336 1.00 14.22 ? ? ? ? ? . 73 ASN A CA 2349 ATOM 585 C C . ASN A 2349 73 . -10.271 -0.425 11.153 1.00 13.82 ? ? ? ? ? . 73 ASN A C 2349 ATOM 586 O O . ASN A 2349 73 . -9.048 -0.290 11.203 1.00 13.41 ? ? ? ? ? . 73 ASN A O 2349 ATOM 587 C CB . ASN A 2349 73 . -11.065 1.455 12.613 1.00 15.75 ? ? ? ? ? . 73 ASN A CB 2349 ATOM 588 C CG . ASN A 2349 73 . -11.382 2.282 11.378 1.00 16.44 ? ? ? ? ? . 73 ASN A CG 2349 ATOM 589 N ND2 . ASN A 2349 73 . -12.576 2.835 11.326 1.00 16.80 ? ? ? ? ? . 73 ASN A ND2 2349 ATOM 590 O OD1 . ASN A 2349 73 . -10.571 2.366 10.456 1.00 17.63 ? ? ? ? ? . 73 ASN A OD1 2349 ATOM 591 N N . GLU A 2349 74 . -10.908 -0.880 10.082 1.00 12.83 ? ? ? ? ? . 74 GLU A N 2349 ATOM 592 C CA . GLU A 2349 74 . -10.164 -1.428 8.942 1.00 13.34 ? ? ? ? ? . 74 GLU A CA 2349 ATOM 593 C C . GLU A 2349 74 . -9.264 -0.399 8.251 1.00 12.42 ? ? ? ? ? . 74 GLU A C 2349 ATOM 594 O O . GLU A 2349 74 . -8.163 -0.752 7.810 1.00 12.27 ? ? ? ? ? . 74 GLU A O 2349 ATOM 595 C CB . GLU A 2349 74 . -11.098 -2.104 7.937 1.00 13.28 ? ? ? ? ? . 74 GLU A CB 2349 ATOM 596 C CG . GLU A 2349 74 . -10.322 -2.877 6.864 1.00 14.42 ? ? ? ? ? . 74 GLU A CG 2349 ATOM 597 C CD . GLU A 2349 74 . -11.098 -3.992 6.185 1.00 15.31 ? ? ? ? ? . 74 GLU A CD 2349 ATOM 598 O OE1 . GLU A 2349 74 . -12.342 -4.043 6.291 1.00 16.61 ? ? ? ? ? . 74 GLU A OE1 2349 ATOM 599 O OE2 . GLU A 2349 74 . -10.428 -4.814 5.521 1.00 16.63 ? ? ? ? ? 1- 74 GLU A OE2 2349 ATOM 600 N N A SER A 2349 75 . -9.716 0.852 8.158 0.50 12.08 ? ? ? ? ? . 75 SER A N 2349 ATOM 601 N N B SER A 2349 75 . -9.720 0.852 8.162 0.50 12.17 ? ? ? ? ? . 75 SER A N 2349 ATOM 602 C CA A SER A 2349 75 . -8.889 1.908 7.555 0.50 12.63 ? ? ? ? ? . 75 SER A CA 2349 ATOM 603 C CA B SER A 2349 75 . -8.902 1.929 7.582 0.50 12.79 ? ? ? ? ? . 75 SER A CA 2349 ATOM 604 C C A SER A 2349 75 . -7.615 2.172 8.375 0.50 12.99 ? ? ? ? ? . 75 SER A C 2349 ATOM 605 C C B SER A 2349 75 . -7.614 2.148 8.378 0.50 13.06 ? ? ? ? ? . 75 SER A C 2349 ATOM 606 O O A SER A 2349 75 . -6.534 2.346 7.802 0.50 12.87 ? ? ? ? ? . 75 SER A O 2349 ATOM 607 O O B SER A 2349 75 . -6.530 2.275 7.797 0.50 12.91 ? ? ? ? ? . 75 SER A O 2349 ATOM 608 C CB A SER A 2349 75 . -9.691 3.193 7.344 0.50 12.19 ? ? ? ? ? . 75 SER A CB 2349 ATOM 609 C CB B SER A 2349 75 . -9.687 3.235 7.505 0.50 12.53 ? ? ? ? ? . 75 SER A CB 2349 ATOM 610 O OG A SER A 2349 75 . -9.929 3.865 8.562 0.50 12.51 ? ? ? ? ? . 75 SER A OG 2349 ATOM 611 O OG B SER A 2349 75 . -11.042 2.992 7.190 0.50 12.90 ? ? ? ? ? . 75 SER A OG 2349 ATOM 612 N N . ASP A 2349 76 . -7.737 2.174 9.705 1.00 13.63 ? ? ? ? ? . 76 ASP A N 2349 ATOM 613 C CA . ASP A 2349 76 . -6.574 2.273 10.604 1.00 14.12 ? ? ? ? ? . 76 ASP A CA 2349 ATOM 614 C C . ASP A 2349 76 . -5.635 1.088 10.406 1.00 14.27 ? ? ? ? ? . 76 ASP A C 2349 ATOM 615 O O . ASP A 2349 76 . -4.413 1.264 10.305 1.00 15.60 ? ? ? ? ? . 76 ASP A O 2349 ATOM 616 C CB . ASP A 2349 76 . -6.999 2.328 12.092 1.00 15.22 ? ? ? ? ? . 76 ASP A CB 2349 ATOM 617 C CG . ASP A 2349 76 . -7.739 3.609 12.471 1.00 17.74 ? ? ? ? ? . 76 ASP A CG 2349 ATOM 618 O OD1 . ASP A 2349 76 . -7.583 4.650 11.792 1.00 18.03 ? ? ? ? ? . 76 ASP A OD1 2349 ATOM 619 O OD2 . ASP A 2349 76 . -8.511 3.555 13.461 1.00 18.66 ? ? ? ? ? 1- 76 ASP A OD2 2349 ATOM 620 N N . PHE A 2349 77 . -6.198 -0.116 10.328 1.00 13.52 ? ? ? ? ? . 77 PHE A N 2349 ATOM 621 C CA . PHE A 2349 77 . -5.377 -1.318 10.207 1.00 14.12 ? ? ? ? ? . 77 PHE A CA 2349 ATOM 622 C C . PHE A 2349 77 . -4.500 -1.258 8.952 1.00 13.79 ? ? ? ? ? . 77 PHE A C 2349 ATOM 623 O O . PHE A 2349 77 . -3.297 -1.442 9.049 1.00 14.65 ? ? ? ? ? . 77 PHE A O 2349 ATOM 624 C CB . PHE A 2349 77 . -6.250 -2.570 10.169 1.00 14.39 ? ? ? ? ? . 77 PHE A CB 2349 ATOM 625 C CG . PHE A 2349 77 . -5.489 -3.825 9.863 1.00 14.28 ? ? ? ? ? . 77 PHE A CG 2349 ATOM 626 C CD1 . PHE A 2349 77 . -4.882 -4.561 10.885 1.00 14.15 ? ? ? ? ? . 77 PHE A CD1 2349 ATOM 627 C CD2 . PHE A 2349 77 . -5.389 -4.282 8.545 1.00 13.66 ? ? ? ? ? . 77 PHE A CD2 2349 ATOM 628 C CE1 . PHE A 2349 77 . -4.198 -5.736 10.592 1.00 14.66 ? ? ? ? ? . 77 PHE A CE1 2349 ATOM 629 C CE2 . PHE A 2349 77 . -4.715 -5.450 8.263 1.00 14.31 ? ? ? ? ? . 77 PHE A CE2 2349 ATOM 630 C CZ . PHE A 2349 77 . -4.106 -6.167 9.277 1.00 13.75 ? ? ? ? ? . 77 PHE A CZ 2349 ATOM 631 N N . HIS A 2349 78 . -5.105 -0.968 7.800 1.00 13.17 ? ? ? ? ? . 78 HIS A N 2349 ATOM 632 C CA . HIS A 2349 78 . -4.363 -1.017 6.526 1.00 15.15 ? ? ? ? ? . 78 HIS A CA 2349 ATOM 633 C C . HIS A 2349 78 . -3.291 0.066 6.463 1.00 16.44 ? ? ? ? ? . 78 HIS A C 2349 ATOM 634 O O . HIS A 2349 78 . -2.177 -0.197 6.034 1.00 18.01 ? ? ? ? ? . 78 HIS A O 2349 ATOM 635 C CB . HIS A 2349 78 . -5.293 -0.947 5.327 1.00 15.24 ? ? ? ? ? . 78 HIS A CB 2349 ATOM 636 C CG . HIS A 2349 78 . -6.138 -2.171 5.161 1.00 16.20 ? ? ? ? ? . 78 HIS A CG 2349 ATOM 637 C CD2 . HIS A 2349 78 . -7.474 -2.321 5.042 1.00 16.05 ? ? ? ? ? . 78 HIS A CD2 2349 ATOM 638 N ND1 . HIS A 2349 78 . -5.603 -3.438 5.092 1.00 16.80 ? ? ? ? ? . 78 HIS A ND1 2349 ATOM 639 C CE1 . HIS A 2349 78 . -6.577 -4.317 4.956 1.00 16.55 ? ? ? ? ? . 78 HIS A CE1 2349 ATOM 640 N NE2 . HIS A 2349 78 . -7.722 -3.664 4.911 1.00 16.79 ? ? ? ? ? . 78 HIS A NE2 2349 ATOM 641 N N . ASP A 2349 79 . -3.634 1.265 6.931 1.00 16.68 ? ? ? ? ? . 79 ASP A N 2349 ATOM 642 C CA . ASP A 2349 79 . -2.676 2.375 7.024 1.00 16.83 ? ? ? ? ? . 79 ASP A CA 2349 ATOM 643 C C . ASP A 2349 79 . -1.470 2.068 7.917 1.00 15.94 ? ? ? ? ? . 79 ASP A C 2349 ATOM 644 O O . ASP A 2349 79 . -0.336 2.356 7.523 1.00 17.28 ? ? ? ? ? . 79 ASP A O 2349 ATOM 645 C CB . ASP A 2349 79 . -3.376 3.617 7.558 1.00 17.23 ? ? ? ? ? . 79 ASP A CB 2349 ATOM 646 C CG . ASP A 2349 79 . -2.424 4.781 7.759 1.00 20.48 ? ? ? ? ? . 79 ASP A CG 2349 ATOM 647 O OD1 . ASP A 2349 79 . -2.084 5.421 6.759 1.00 20.77 ? ? ? ? ? . 79 ASP A OD1 2349 ATOM 648 O OD2 . ASP A 2349 79 . -2.011 5.037 8.914 1.00 25.19 ? ? ? ? ? 1- 79 ASP A OD2 2349 ATOM 649 N N . TYR A 2349 80 . -1.730 1.494 9.099 1.00 14.61 ? ? ? ? ? . 80 TYR A N 2349 ATOM 650 C CA . TYR A 2349 80 . -0.697 1.179 10.096 1.00 17.20 ? ? ? ? ? . 80 TYR A CA 2349 ATOM 651 C C . TYR A 2349 80 . 0.221 0.072 9.590 1.00 17.19 ? ? ? ? ? . 80 TYR A C 2349 ATOM 652 O O . TYR A 2349 80 . 1.447 0.196 9.633 1.00 16.67 ? ? ? ? ? . 80 TYR A O 2349 ATOM 653 C CB . TYR A 2349 80 . -1.340 0.758 11.427 1.00 18.55 ? ? ? ? ? . 80 TYR A CB 2349 ATOM 654 C CG . TYR A 2349 80 . -0.396 0.484 12.583 1.00 18.63 ? ? ? ? ? . 80 TYR A CG 2349 ATOM 655 C CD1 . TYR A 2349 80 . 0.683 1.323 12.833 1.00 23.04 ? ? ? ? ? . 80 TYR A CD1 2349 ATOM 656 C CD2 . TYR A 2349 80 . -0.627 -0.565 13.480 1.00 20.76 ? ? ? ? ? . 80 TYR A CD2 2349 ATOM 657 C CE1 . TYR A 2349 80 . 1.538 1.105 13.894 1.00 22.93 ? ? ? ? ? . 80 TYR A CE1 2349 ATOM 658 C CE2 . TYR A 2349 80 . 0.226 -0.795 14.558 1.00 21.46 ? ? ? ? ? . 80 TYR A CE2 2349 ATOM 659 C CZ . TYR A 2349 80 . 1.316 0.057 14.752 1.00 22.68 ? ? ? ? ? . 80 TYR A CZ 2349 ATOM 660 O OH . TYR A 2349 80 . 2.212 -0.095 15.781 1.00 22.57 ? ? ? ? ? . 80 TYR A OH 2349 ATOM 661 N N . TYR A 2349 81 . -0.381 -1.002 9.092 1.00 17.50 ? ? ? ? ? . 81 TYR A N 2349 ATOM 662 C CA . TYR A 2349 81 . 0.379 -2.102 8.498 1.00 16.24 ? ? ? ? ? . 81 TYR A CA 2349 ATOM 663 C C . TYR A 2349 81 . 1.140 -1.652 7.227 1.00 18.13 ? ? ? ? ? . 81 TYR A C 2349 ATOM 664 O O . TYR A 2349 81 . 2.207 -2.185 6.913 1.00 15.85 ? ? ? ? ? . 81 TYR A O 2349 ATOM 665 C CB . TYR A 2349 81 . -0.539 -3.302 8.214 1.00 16.74 ? ? ? ? ? . 81 TYR A CB 2349 ATOM 666 C CG . TYR A 2349 81 . 0.157 -4.417 7.487 1.00 15.44 ? ? ? ? ? . 81 TYR A CG 2349 ATOM 667 C CD1 . TYR A 2349 81 . 1.326 -4.962 7.996 1.00 15.29 ? ? ? ? ? . 81 TYR A CD1 2349 ATOM 668 C CD2 . TYR A 2349 81 . -0.327 -4.903 6.270 1.00 16.27 ? ? ? ? ? . 81 TYR A CD2 2349 ATOM 669 C CE1 . TYR A 2349 81 . 1.991 -5.974 7.330 1.00 16.12 ? ? ? ? ? . 81 TYR A CE1 2349 ATOM 670 C CE2 . TYR A 2349 81 . 0.337 -5.915 5.598 1.00 16.03 ? ? ? ? ? . 81 TYR A CE2 2349 ATOM 671 C CZ . TYR A 2349 81 . 1.494 -6.446 6.138 1.00 15.55 ? ? ? ? ? . 81 TYR A CZ 2349 ATOM 672 O OH . TYR A 2349 81 . 2.175 -7.436 5.481 1.00 15.91 ? ? ? ? ? . 81 TYR A OH 2349 ATOM 673 N N . GLY A 2349 82 . 0.590 -0.673 6.520 1.00 17.41 ? ? ? ? ? . 82 GLY A N 2349 ATOM 674 C CA . GLY A 2349 82 . 1.289 0.024 5.435 1.00 18.28 ? ? ? ? ? . 82 GLY A CA 2349 ATOM 675 C C . GLY A 2349 82 . 2.637 0.633 5.811 1.00 20.09 ? ? ? ? ? . 82 GLY A C 2349 ATOM 676 O O . GLY A 2349 82 . 3.493 0.785 4.952 1.00 24.29 ? ? ? ? ? . 82 GLY A O 2349 ATOM 677 N N . LYS A 2349 83 . 2.831 0.980 7.081 1.00 22.68 ? ? ? ? ? . 83 LYS A N 2349 ATOM 678 C CA . LYS A 2349 83 . 4.127 1.471 7.568 1.00 25.21 ? ? ? ? ? . 83 LYS A CA 2349 ATOM 679 C C . LYS A 2349 83 . 5.180 0.368 7.755 1.00 24.73 ? ? ? ? ? . 83 LYS A C 2349 ATOM 680 O O . LYS A 2349 83 . 6.347 0.694 7.939 1.00 27.09 ? ? ? ? ? . 83 LYS A O 2349 ATOM 681 C CB . LYS A 2349 83 . 3.966 2.226 8.900 1.00 27.32 ? ? ? ? ? . 83 LYS A CB 2349 ATOM 682 C CG . LYS A 2349 83 . 3.068 3.460 8.822 1.00 28.44 ? ? ? ? ? . 83 LYS A CG 2349 ATOM 683 C CD . LYS A 2349 83 . 2.696 3.960 10.213 1.00 29.59 ? ? ? ? ? . 83 LYS A CD 2349 ATOM 684 C CE . LYS A 2349 83 . 1.544 4.950 10.191 1.00 32.72 ? ? ? ? ? . 83 LYS A CE 2349 ATOM 685 N NZ . LYS A 2349 83 . 2.009 6.314 9.830 1.00 33.48 ? ? ? ? ? 1+ 83 LYS A NZ 2349 ATOM 686 N N . MET A 2349 84 . 4.781 -0.911 7.691 1.00 19.28 ? ? ? ? ? . 84 MET A N 2349 ATOM 687 C CA . MET A 2349 84 . 5.594 -2.020 8.159 1.00 17.95 ? ? ? ? ? . 84 MET A CA 2349 ATOM 688 C C . MET A 2349 84 . 6.094 -2.867 6.992 1.00 17.98 ? ? ? ? ? . 84 MET A C 2349 ATOM 689 O O . MET A 2349 84 . 5.361 -3.039 6.022 1.00 18.70 ? ? ? ? ? . 84 MET A O 2349 ATOM 690 C CB . MET A 2349 84 . 4.741 -2.887 9.073 1.00 18.33 ? ? ? ? ? . 84 MET A CB 2349 ATOM 691 C CG . MET A 2349 84 . 4.178 -2.120 10.259 1.00 17.16 ? ? ? ? ? . 84 MET A CG 2349 ATOM 692 S SD . MET A 2349 84 . 3.073 -3.159 11.216 1.00 18.23 ? ? ? ? ? . 84 MET A SD 2349 ATOM 693 C CE . MET A 2349 84 . 2.572 -2.030 12.508 1.00 19.33 ? ? ? ? ? . 84 MET A CE 2349 ATOM 694 N N . PRO A 2349 85 . 7.327 -3.413 7.084 1.00 15.09 ? ? ? ? ? . 85 PRO A N 2349 ATOM 695 C CA . PRO A 2349 85 . 7.898 -4.245 6.004 1.00 14.89 ? ? ? ? ? . 85 PRO A CA 2349 ATOM 696 C C . PRO A 2349 85 . 7.578 -5.746 6.060 1.00 14.31 ? ? ? ? ? . 85 PRO A C 2349 ATOM 697 O O . PRO A 2349 85 . 7.878 -6.490 5.111 1.00 16.07 ? ? ? ? ? . 85 PRO A O 2349 ATOM 698 C CB . PRO A 2349 85 . 9.418 -4.058 6.204 1.00 13.50 ? ? ? ? ? . 85 PRO A CB 2349 ATOM 699 C CG . PRO A 2349 85 . 9.557 -3.858 7.671 1.00 14.27 ? ? ? ? ? . 85 PRO A CG 2349 ATOM 700 C CD . PRO A 2349 85 . 8.354 -3.051 8.079 1.00 14.84 ? ? ? ? ? . 85 PRO A CD 2349 ATOM 701 N N . TRP A 2349 86 . 7.021 -6.177 7.179 1.00 14.39 ? ? ? ? ? . 86 TRP A N 2349 ATOM 702 C CA . TRP A 2349 86 . 6.848 -7.584 7.527 1.00 15.05 ? ? ? ? ? . 86 TRP A CA 2349 ATOM 703 C C . TRP A 2349 86 . 5.414 -8.087 7.212 1.00 14.93 ? ? ? ? ? . 86 TRP A C 2349 ATOM 704 O O . TRP A 2349 86 . 4.763 -7.552 6.308 1.00 15.89 ? ? ? ? ? . 86 TRP A O 2349 ATOM 705 C CB . TRP A 2349 86 . 7.249 -7.774 8.986 1.00 16.09 ? ? ? ? ? . 86 TRP A CB 2349 ATOM 706 C CG . TRP A 2349 86 . 6.594 -6.805 9.948 1.00 16.38 ? ? ? ? ? . 86 TRP A CG 2349 ATOM 707 C CD1 . TRP A 2349 86 . 5.277 -6.720 10.275 1.00 16.39 ? ? ? ? ? . 86 TRP A CD1 2349 ATOM 708 C CD2 . TRP A 2349 86 . 7.254 -5.759 10.661 1.00 16.60 ? ? ? ? ? . 86 TRP A CD2 2349 ATOM 709 C CE2 . TRP A 2349 86 . 6.275 -5.092 11.428 1.00 16.59 ? ? ? ? ? . 86 TRP A CE2 2349 ATOM 710 C CE3 . TRP A 2349 86 . 8.580 -5.340 10.752 1.00 17.11 ? ? ? ? ? . 86 TRP A CE3 2349 ATOM 711 N NE1 . TRP A 2349 86 . 5.074 -5.703 11.176 1.00 17.10 ? ? ? ? ? . 86 TRP A NE1 2349 ATOM 712 C CZ2 . TRP A 2349 86 . 6.576 -4.003 12.239 1.00 16.34 ? ? ? ? ? . 86 TRP A CZ2 2349 ATOM 713 C CZ3 . TRP A 2349 86 . 8.880 -4.259 11.571 1.00 16.26 ? ? ? ? ? . 86 TRP A CZ3 2349 ATOM 714 C CH2 . TRP A 2349 86 . 7.883 -3.601 12.300 1.00 16.70 ? ? ? ? ? . 86 TRP A CH2 2349 ATOM 715 N N . LEU A 2349 87 . 4.947 -9.122 7.918 1.00 14.24 ? ? ? ? ? . 87 LEU A N 2349 ATOM 716 C CA . LEU A 2349 87 . 3.666 -9.781 7.638 1.00 14.03 ? ? ? ? ? . 87 LEU A CA 2349 ATOM 717 C C . LEU A 2349 87 . 2.585 -9.335 8.606 1.00 13.87 ? ? ? ? ? . 87 LEU A C 2349 ATOM 718 O O . LEU A 2349 87 . 2.870 -8.625 9.570 1.00 15.16 ? ? ? ? ? . 87 LEU A O 2349 ATOM 719 C CB . LEU A 2349 87 . 3.834 -11.298 7.738 1.00 14.67 ? ? ? ? ? . 87 LEU A CB 2349 ATOM 720 C CG . LEU A 2349 87 . 4.941 -11.933 6.902 1.00 15.26 ? ? ? ? ? . 87 LEU A CG 2349 ATOM 721 C CD1 . LEU A 2349 87 . 4.898 -13.451 7.044 1.00 17.71 ? ? ? ? ? . 87 LEU A CD1 2349 ATOM 722 C CD2 . LEU A 2349 87 . 4.848 -11.552 5.423 1.00 15.24 ? ? ? ? ? . 87 LEU A CD2 2349 ATOM 723 N N . ALA A 2349 88 . 1.338 -9.735 8.355 1.00 14.07 ? ? ? ? ? . 88 ALA A N 2349 ATOM 724 C CA . ALA A 2349 88 . 0.243 -9.403 9.270 1.00 13.95 ? ? ? ? ? . 88 ALA A CA 2349 ATOM 725 C C . ALA A 2349 88 . -0.837 -10.476 9.311 1.00 14.05 ? ? ? ? ? . 88 ALA A C 2349 ATOM 726 O O . ALA A 2349 88 . -1.203 -11.084 8.292 1.00 13.51 ? ? ? ? ? . 88 ALA A O 2349 ATOM 727 C CB . ALA A 2349 88 . -0.376 -8.068 8.919 1.00 14.60 ? ? ? ? ? . 88 ALA A CB 2349 ATOM 728 N N . LEU A 2349 89 . -1.325 -10.720 10.521 1.00 14.21 ? ? ? ? ? . 89 LEU A N 2349 ATOM 729 C CA . LEU A 2349 89 . -2.521 -11.514 10.693 1.00 14.62 ? ? ? ? ? . 89 LEU A CA 2349 ATOM 730 C C . LEU A 2349 89 . -3.619 -10.667 10.045 1.00 15.33 ? ? ? ? ? . 89 LEU A C 2349 ATOM 731 O O . LEU A 2349 89 . -3.754 -9.482 10.397 1.00 16.78 ? ? ? ? ? . 89 LEU A O 2349 ATOM 732 C CB . LEU A 2349 89 . -2.799 -11.754 12.179 1.00 15.84 ? ? ? ? ? . 89 LEU A CB 2349 ATOM 733 C CG . LEU A 2349 89 . -4.017 -12.623 12.472 1.00 17.67 ? ? ? ? ? . 89 LEU A CG 2349 ATOM 734 C CD1 . LEU A 2349 89 . -3.789 -14.077 12.038 1.00 17.19 ? ? ? ? ? . 89 LEU A CD1 2349 ATOM 735 C CD2 . LEU A 2349 89 . -4.381 -12.542 13.948 1.00 18.01 ? ? ? ? ? . 89 LEU A CD2 2349 ATOM 736 N N . PRO A 2349 90 . -4.369 -11.236 9.079 1.00 15.61 ? ? ? ? ? . 90 PRO A N 2349 ATOM 737 C CA . PRO A 2349 90 . -5.337 -10.408 8.338 1.00 15.39 ? ? ? ? ? . 90 PRO A CA 2349 ATOM 738 C C . PRO A 2349 90 . -6.419 -9.804 9.235 1.00 16.09 ? ? ? ? ? . 90 PRO A C 2349 ATOM 739 O O . PRO A 2349 90 . -6.743 -10.365 10.289 1.00 17.53 ? ? ? ? ? . 90 PRO A O 2349 ATOM 740 C CB . PRO A 2349 90 . -5.942 -11.382 7.316 1.00 15.62 ? ? ? ? ? . 90 PRO A CB 2349 ATOM 741 C CG . PRO A 2349 90 . -5.047 -12.581 7.294 1.00 15.55 ? ? ? ? ? . 90 PRO A CG 2349 ATOM 742 C CD . PRO A 2349 90 . -4.440 -12.653 8.660 1.00 15.71 ? ? ? ? ? . 90 PRO A CD 2349 ATOM 743 N N . PHE A 2349 91 . -6.969 -8.674 8.808 1.00 15.01 ? ? ? ? ? . 91 PHE A N 2349 ATOM 744 C CA . PHE A 2349 91 . -8.012 -7.972 9.554 1.00 15.12 ? ? ? ? ? . 91 PHE A CA 2349 ATOM 745 C C . PHE A 2349 91 . -9.234 -8.855 9.838 1.00 14.96 ? ? ? ? ? . 91 PHE A C 2349 ATOM 746 O O . PHE A 2349 91 . -9.821 -8.765 10.919 1.00 14.30 ? ? ? ? ? . 91 PHE A O 2349 ATOM 747 C CB . PHE A 2349 91 . -8.419 -6.696 8.808 1.00 14.17 ? ? ? ? ? . 91 PHE A CB 2349 ATOM 748 C CG . PHE A 2349 91 . -9.368 -5.827 9.575 1.00 14.33 ? ? ? ? ? . 91 PHE A CG 2349 ATOM 749 C CD1 . PHE A 2349 91 . -8.907 -5.015 10.596 1.00 14.03 ? ? ? ? ? . 91 PHE A CD1 2349 ATOM 750 C CD2 . PHE A 2349 91 . -10.718 -5.837 9.293 1.00 14.08 ? ? ? ? ? . 91 PHE A CD2 2349 ATOM 751 C CE1 . PHE A 2349 91 . -9.778 -4.214 11.312 1.00 14.13 ? ? ? ? ? . 91 PHE A CE1 2349 ATOM 752 C CE2 . PHE A 2349 91 . -11.593 -5.031 10.000 1.00 14.14 ? ? ? ? ? . 91 PHE A CE2 2349 ATOM 753 C CZ . PHE A 2349 91 . -11.125 -4.227 11.017 1.00 13.32 ? ? ? ? ? . 91 PHE A CZ 2349 ATOM 754 N N . ASP A 2349 92 . -9.589 -9.745 8.906 1.00 15.56 ? ? ? ? ? . 92 ASP A N 2349 ATOM 755 C CA . ASP A 2349 92 . -10.703 -10.677 9.134 1.00 17.16 ? ? ? ? ? . 92 ASP A CA 2349 ATOM 756 C C . ASP A 2349 92 . -10.492 -11.723 10.253 1.00 16.55 ? ? ? ? ? . 92 ASP A C 2349 ATOM 757 O O . ASP A 2349 92 . -11.442 -12.405 10.630 1.00 15.77 ? ? ? ? ? . 92 ASP A O 2349 ATOM 758 C CB . ASP A 2349 92 . -11.183 -11.323 7.817 1.00 19.89 ? ? ? ? ? . 92 ASP A CB 2349 ATOM 759 C CG . ASP A 2349 92 . -10.238 -12.389 7.264 1.00 22.49 ? ? ? ? ? . 92 ASP A CG 2349 ATOM 760 O OD1 . ASP A 2349 92 . -9.083 -12.505 7.702 1.00 25.02 ? ? ? ? ? . 92 ASP A OD1 2349 ATOM 761 O OD2 . ASP A 2349 92 . -10.682 -13.123 6.358 1.00 28.11 ? ? ? ? ? 1- 92 ASP A OD2 2349 ATOM 762 N N . GLN A 2349 93 . -9.265 -11.838 10.772 1.00 18.68 ? ? ? ? ? . 93 GLN A N 2349 ATOM 763 C CA . GLN A 2349 93 . -8.950 -12.682 11.938 1.00 19.24 ? ? ? ? ? . 93 GLN A CA 2349 ATOM 764 C C . GLN A 2349 93 . -8.865 -11.918 13.267 1.00 19.92 ? ? ? ? ? . 93 GLN A C 2349 ATOM 765 O O . GLN A 2349 93 . -8.488 -12.498 14.294 1.00 19.87 ? ? ? ? ? . 93 GLN A O 2349 ATOM 766 C CB . GLN A 2349 93 . -7.613 -13.387 11.705 1.00 21.09 ? ? ? ? ? . 93 GLN A CB 2349 ATOM 767 C CG . GLN A 2349 93 . -7.585 -14.287 10.491 1.00 22.02 ? ? ? ? ? . 93 GLN A CG 2349 ATOM 768 C CD . GLN A 2349 93 . -8.625 -15.367 10.592 1.00 22.70 ? ? ? ? ? . 93 GLN A CD 2349 ATOM 769 N NE2 . GLN A 2349 93 . -9.587 -15.348 9.687 1.00 24.75 ? ? ? ? ? . 93 GLN A NE2 2349 ATOM 770 O OE1 . GLN A 2349 93 . -8.582 -16.194 11.502 1.00 26.33 ? ? ? ? ? . 93 GLN A OE1 2349 ATOM 771 N N . ARG A 2349 94 . -9.195 -10.629 13.268 1.00 18.83 ? ? ? ? ? . 94 ARG A N 2349 ATOM 772 C CA . ARG A 2349 94 . -9.008 -9.798 14.473 1.00 18.44 ? ? ? ? ? . 94 ARG A CA 2349 ATOM 773 C C . ARG A 2349 94 . -9.787 -10.249 15.731 1.00 20.01 ? ? ? ? ? . 94 ARG A C 2349 ATOM 774 O O . ARG A 2349 94 . -9.382 -9.946 16.856 1.00 21.06 ? ? ? ? ? . 94 ARG A O 2349 ATOM 775 C CB . ARG A 2349 94 . -9.362 -8.352 14.163 1.00 18.84 ? ? ? ? ? . 94 ARG A CB 2349 ATOM 776 C CG . ARG A 2349 94 . -10.833 -8.137 13.869 1.00 17.70 ? ? ? ? ? . 94 ARG A CG 2349 ATOM 777 C CD . ARG A 2349 94 . -11.074 -6.817 13.167 1.00 17.62 ? ? ? ? ? . 94 ARG A CD 2349 ATOM 778 N NE . ARG A 2349 94 . -12.479 -6.584 12.868 1.00 16.14 ? ? ? ? ? . 94 ARG A NE 2349 ATOM 779 C CZ . ARG A 2349 94 . -13.172 -7.168 11.890 1.00 15.93 ? ? ? ? ? . 94 ARG A CZ 2349 ATOM 780 N NH1 . ARG A 2349 94 . -12.618 -8.075 11.077 1.00 15.88 ? ? ? ? ? 1+ 94 ARG A NH1 2349 ATOM 781 N NH2 . ARG A 2349 94 . -14.447 -6.844 11.720 1.00 15.41 ? ? ? ? ? . 94 ARG A NH2 2349 ATOM 782 N N . SER A 2349 95 . -10.894 -10.966 15.554 1.00 18.52 ? ? ? ? ? . 95 SER A N 2349 ATOM 783 C CA . SER A 2349 95 . -11.631 -11.517 16.704 1.00 19.63 ? ? ? ? ? . 95 SER A CA 2349 ATOM 784 C C . SER A 2349 95 . -10.806 -12.529 17.529 1.00 20.04 ? ? ? ? ? . 95 SER A C 2349 ATOM 785 O O . SER A 2349 95 . -11.153 -12.802 18.675 1.00 23.68 ? ? ? ? ? . 95 SER A O 2349 ATOM 786 C CB . SER A 2349 95 . -12.957 -12.140 16.257 1.00 19.52 ? ? ? ? ? . 95 SER A CB 2349 ATOM 787 O OG . SER A 2349 95 . -12.750 -13.290 15.451 1.00 19.99 ? ? ? ? ? . 95 SER A OG 2349 ATOM 788 N N . THR A 2349 96 . -9.726 -13.065 16.955 1.00 18.79 ? ? ? ? ? . 96 THR A N 2349 ATOM 789 C CA . THR A 2349 96 . -8.848 -14.022 17.638 1.00 19.20 ? ? ? ? ? . 96 THR A CA 2349 ATOM 790 C C . THR A 2349 96 . -7.699 -13.365 18.408 1.00 18.18 ? ? ? ? ? . 96 THR A C 2349 ATOM 791 O O . THR A 2349 96 . -7.004 -14.049 19.141 1.00 18.92 ? ? ? ? ? . 96 THR A O 2349 ATOM 792 C CB . THR A 2349 96 . -8.234 -15.045 16.647 1.00 18.50 ? ? ? ? ? . 96 THR A CB 2349 ATOM 793 C CG2 . THR A 2349 96 . -9.306 -15.722 15.827 1.00 19.51 ? ? ? ? ? . 96 THR A CG2 2349 ATOM 794 O OG1 . THR A 2349 96 . -7.308 -14.396 15.773 1.00 17.89 ? ? ? ? ? . 96 THR A OG1 2349 ATOM 795 N N . VAL A 2349 97 . -7.509 -12.050 18.253 1.00 17.87 ? ? ? ? ? . 97 VAL A N 2349 ATOM 796 C CA . VAL A 2349 97 . -6.369 -11.333 18.837 1.00 17.37 ? ? ? ? ? . 97 VAL A CA 2349 ATOM 797 C C . VAL A 2349 97 . -6.320 -11.387 20.366 1.00 17.80 ? ? ? ? ? . 97 VAL A C 2349 ATOM 798 O O . VAL A 2349 97 . -5.255 -11.611 20.940 1.00 20.08 ? ? ? ? ? . 97 VAL A O 2349 ATOM 799 C CB . VAL A 2349 97 . -6.303 -9.861 18.321 1.00 17.84 ? ? ? ? ? . 97 VAL A CB 2349 ATOM 800 C CG1 . VAL A 2349 97 . -5.371 -8.987 19.152 1.00 19.58 ? ? ? ? ? . 97 VAL A CG1 2349 ATOM 801 C CG2 . VAL A 2349 97 . -5.879 -9.848 16.855 1.00 18.67 ? ? ? ? ? . 97 VAL A CG2 2349 ATOM 802 N N . SER A 2349 98 . -7.446 -11.187 21.024 1.00 18.78 ? ? ? ? ? . 98 SER A N 2349 ATOM 803 C CA . SER A 2349 98 . -7.464 -11.238 22.490 1.00 21.28 ? ? ? ? ? . 98 SER A CA 2349 ATOM 804 C C . SER A 2349 98 . -7.035 -12.609 23.030 1.00 18.77 ? ? ? ? ? . 98 SER A C 2349 ATOM 805 O O . SER A 2349 98 . -6.158 -12.685 23.897 1.00 18.08 ? ? ? ? ? . 98 SER A O 2349 ATOM 806 C CB . SER A 2349 98 . -8.832 -10.833 23.032 1.00 25.06 ? ? ? ? ? . 98 SER A CB 2349 ATOM 807 O OG . SER A 2349 98 . -9.007 -9.449 22.802 1.00 31.85 ? ? ? ? ? . 98 SER A OG 2349 ATOM 808 N N . GLU A 2349 99 . -7.616 -13.681 22.496 1.00 19.69 ? ? ? ? ? . 99 GLU A N 2349 ATOM 809 C CA . GLU A 2349 99 . -7.262 -15.038 22.954 1.00 21.24 ? ? ? ? ? . 99 GLU A CA 2349 ATOM 810 C C . GLU A 2349 99 . -5.793 -15.374 22.682 1.00 17.41 ? ? ? ? ? . 99 GLU A C 2349 ATOM 811 O O . GLU A 2349 99 . -5.151 -16.025 23.503 1.00 15.18 ? ? ? ? ? . 99 GLU A O 2349 ATOM 812 C CB . GLU A 2349 99 . -8.204 -16.125 22.399 1.00 26.09 ? ? ? ? ? . 99 GLU A CB 2349 ATOM 813 C CG . GLU A 2349 99 . -9.552 -16.237 23.134 1.00 32.76 ? ? ? ? ? . 99 GLU A CG 2349 ATOM 814 C CD . GLU A 2349 99 . -9.435 -16.520 24.639 1.00 38.23 ? ? ? ? ? . 99 GLU A CD 2349 ATOM 815 O OE1 . GLU A 2349 99 . -10.112 -15.830 25.435 1.00 38.21 ? ? ? ? ? . 99 GLU A OE1 2349 ATOM 816 O OE2 . GLU A 2349 99 . -8.659 -17.420 25.035 1.00 43.04 ? ? ? ? ? 1- 99 GLU A OE2 2349 ATOM 817 N N A LEU A 2349 100 . -5.267 -14.922 21.547 0.62 17.52 ? ? ? ? ? . 100 LEU A N 2349 ATOM 818 N N B LEU A 2349 100 . -5.274 -14.931 21.535 0.38 17.54 ? ? ? ? ? . 100 LEU A N 2349 ATOM 819 C CA A LEU A 2349 100 . -3.843 -15.073 21.262 0.62 17.97 ? ? ? ? ? . 100 LEU A CA 2349 ATOM 820 C CA B LEU A 2349 100 . -3.842 -15.024 21.233 0.38 17.83 ? ? ? ? ? . 100 LEU A CA 2349 ATOM 821 C C A LEU A 2349 100 . -2.991 -14.334 22.306 0.62 17.34 ? ? ? ? ? . 100 LEU A C 2349 ATOM 822 C C B LEU A 2349 100 . -2.996 -14.330 22.297 0.38 17.23 ? ? ? ? ? . 100 LEU A C 2349 ATOM 823 O O A LEU A 2349 100 . -2.009 -14.887 22.811 0.62 17.52 ? ? ? ? ? . 100 LEU A O 2349 ATOM 824 O O B LEU A 2349 100 . -2.015 -14.895 22.788 0.38 17.39 ? ? ? ? ? . 100 LEU A O 2349 ATOM 825 C CB A LEU A 2349 100 . -3.512 -14.591 19.845 0.62 17.99 ? ? ? ? ? . 100 LEU A CB 2349 ATOM 826 C CB B LEU A 2349 100 . -3.539 -14.408 19.866 0.38 17.92 ? ? ? ? ? . 100 LEU A CB 2349 ATOM 827 C CG A LEU A 2349 100 . -2.154 -15.017 19.286 0.62 18.53 ? ? ? ? ? . 100 LEU A CG 2349 ATOM 828 C CG B LEU A 2349 100 . -3.832 -15.294 18.660 0.38 18.30 ? ? ? ? ? . 100 LEU A CG 2349 ATOM 829 C CD1 A LEU A 2349 100 . -2.036 -16.528 19.154 0.62 18.85 ? ? ? ? ? . 100 LEU A CD1 2349 ATOM 830 C CD2 A LEU A 2349 100 . -1.922 -14.346 17.940 0.62 18.72 ? ? ? ? ? . 100 LEU A CD2 2349 ATOM 831 C CD1 B LEU A 2349 100 . -3.529 -14.555 17.366 0.38 18.21 ? ? ? ? ? . 100 LEU A CD1 2349 ATOM 832 C CD2 B LEU A 2349 100 . -3.032 -16.584 18.760 0.38 18.99 ? ? ? ? ? . 100 LEU A CD2 2349 ATOM 833 N N . GLY A 2349 101 . -3.394 -13.112 22.652 1.00 16.30 ? ? ? ? ? . 101 GLY A N 2349 ATOM 834 C CA . GLY A 2349 101 . -2.751 -12.353 23.730 1.00 17.07 ? ? ? ? ? . 101 GLY A CA 2349 ATOM 835 C C . GLY A 2349 101 . -2.761 -13.100 25.058 1.00 16.31 ? ? ? ? ? . 101 GLY A C 2349 ATOM 836 O O . GLY A 2349 101 . -1.743 -13.175 25.749 1.00 16.49 ? ? ? ? ? . 101 GLY A O 2349 ATOM 837 N N . LYS A 2349 102 . -3.894 -13.712 25.373 1.00 16.43 ? ? ? ? ? . 102 LYS A N 2349 ATOM 838 C CA . LYS A 2349 102 . -4.015 -14.519 26.581 1.00 18.92 ? ? ? ? ? . 102 LYS A CA 2349 ATOM 839 C C . LYS A 2349 102 . -3.185 -15.794 26.544 1.00 17.88 ? ? ? ? ? . 102 LYS A C 2349 ATOM 840 O O . LYS A 2349 102 . -2.693 -16.236 27.592 1.00 17.27 ? ? ? ? ? . 102 LYS A O 2349 ATOM 841 C CB . LYS A 2349 102 . -5.471 -14.864 26.852 1.00 20.65 ? ? ? ? ? . 102 LYS A CB 2349 ATOM 842 C CG . LYS A 2349 102 . -6.288 -13.651 27.240 1.00 23.12 ? ? ? ? ? . 102 LYS A CG 2349 ATOM 843 C CD . LYS A 2349 102 . -7.765 -13.982 27.284 1.00 26.40 ? ? ? ? ? . 102 LYS A CD 2349 ATOM 844 C CE . LYS A 2349 102 . -8.599 -12.716 27.350 1.00 30.33 ? ? ? ? ? . 102 LYS A CE 2349 ATOM 845 N NZ . LYS A 2349 102 . -10.031 -13.013 27.641 1.00 32.61 ? ? ? ? ? 1+ 102 LYS A NZ 2349 ATOM 846 N N . THR A 2349 103 . -3.048 -16.401 25.367 1.00 16.42 ? ? ? ? ? . 103 THR A N 2349 ATOM 847 C CA . THR A 2349 103 . -2.195 -17.586 25.218 1.00 17.78 ? ? ? ? ? . 103 THR A CA 2349 ATOM 848 C C . THR A 2349 103 . -0.744 -17.326 25.664 1.00 17.24 ? ? ? ? ? . 103 THR A C 2349 ATOM 849 O O . THR A 2349 103 . -0.141 -18.175 26.318 1.00 18.04 ? ? ? ? ? . 103 THR A O 2349 ATOM 850 C CB . THR A 2349 103 . -2.246 -18.126 23.775 1.00 18.81 ? ? ? ? ? . 103 THR A CB 2349 ATOM 851 C CG2 . THR A 2349 103 . -1.316 -19.326 23.587 1.00 20.17 ? ? ? ? ? . 103 THR A CG2 2349 ATOM 852 O OG1 . THR A 2349 103 . -3.593 -18.515 23.477 1.00 20.80 ? ? ? ? ? . 103 THR A OG1 2349 ATOM 853 N N . PHE A 2349 104 . -0.216 -16.152 25.328 1.00 19.05 ? ? ? ? ? . 104 PHE A N 2349 ATOM 854 C CA . PHE A 2349 104 . 1.181 -15.790 25.614 1.00 19.38 ? ? ? ? ? . 104 PHE A CA 2349 ATOM 855 C C . PHE A 2349 104 . 1.370 -14.884 26.835 1.00 20.42 ? ? ? ? ? . 104 PHE A C 2349 ATOM 856 O O . PHE A 2349 104 . 2.509 -14.490 27.138 1.00 21.98 ? ? ? ? ? . 104 PHE A O 2349 ATOM 857 C CB . PHE A 2349 104 . 1.800 -15.141 24.379 1.00 19.21 ? ? ? ? ? . 104 PHE A CB 2349 ATOM 858 C CG . PHE A 2349 104 . 1.787 -16.032 23.169 1.00 18.31 ? ? ? ? ? . 104 PHE A CG 2349 ATOM 859 C CD1 . PHE A 2349 104 . 2.515 -17.212 23.163 1.00 18.08 ? ? ? ? ? . 104 PHE A CD1 2349 ATOM 860 C CD2 . PHE A 2349 104 . 1.042 -15.701 22.042 1.00 18.77 ? ? ? ? ? . 104 PHE A CD2 2349 ATOM 861 C CE1 . PHE A 2349 104 . 2.515 -18.044 22.052 1.00 19.62 ? ? ? ? ? . 104 PHE A CE1 2349 ATOM 862 C CE2 . PHE A 2349 104 . 1.023 -16.536 20.933 1.00 19.73 ? ? ? ? ? . 104 PHE A CE2 2349 ATOM 863 C CZ . PHE A 2349 104 . 1.766 -17.706 20.933 1.00 19.63 ? ? ? ? ? . 104 PHE A CZ 2349 ATOM 864 N N . GLY A 2349 105 . 0.278 -14.584 27.535 1.00 17.32 ? ? ? ? ? . 105 GLY A N 2349 ATOM 865 C CA . GLY A 2349 105 . 0.314 -13.721 28.702 1.00 17.53 ? ? ? ? ? . 105 GLY A CA 2349 ATOM 866 C C . GLY A 2349 105 . 0.695 -12.289 28.385 1.00 18.09 ? ? ? ? ? . 105 GLY A C 2349 ATOM 867 O O . GLY A 2349 105 . 1.374 -11.625 29.192 1.00 18.88 ? ? ? ? ? . 105 GLY A O 2349 ATOM 868 N N . VAL A 2349 106 . 0.237 -11.800 27.229 1.00 16.90 ? ? ? ? ? . 106 VAL A N 2349 ATOM 869 C CA . VAL A 2349 106 . 0.450 -10.401 26.824 1.00 17.15 ? ? ? ? ? . 106 VAL A CA 2349 ATOM 870 C C . VAL A 2349 106 . -0.420 -9.510 27.720 1.00 17.09 ? ? ? ? ? . 106 VAL A C 2349 ATOM 871 O O . VAL A 2349 106 . -1.656 -9.601 27.679 1.00 17.42 ? ? ? ? ? . 106 VAL A O 2349 ATOM 872 C CB . VAL A 2349 106 . 0.113 -10.177 25.338 1.00 16.91 ? ? ? ? ? . 106 VAL A CB 2349 ATOM 873 C CG1 . VAL A 2349 106 . 0.239 -8.706 24.946 1.00 17.76 ? ? ? ? ? . 106 VAL A CG1 2349 ATOM 874 C CG2 . VAL A 2349 106 . 1.032 -11.025 24.467 1.00 16.80 ? ? ? ? ? . 106 VAL A CG2 2349 ATOM 875 N N A GLU A 2349 107 . 0.231 -8.684 28.544 0.48 16.42 ? ? ? ? ? . 107 GLU A N 2349 ATOM 876 N N B GLU A 2349 107 . 0.226 -8.667 28.525 0.52 16.18 ? ? ? ? ? . 107 GLU A N 2349 ATOM 877 C CA A GLU A 2349 107 . -0.457 -7.789 29.486 0.48 17.61 ? ? ? ? ? . 107 GLU A CA 2349 ATOM 878 C CA B GLU A 2349 107 . -0.482 -7.782 29.455 0.52 17.47 ? ? ? ? ? . 107 GLU A CA 2349 ATOM 879 C C A GLU A 2349 107 . -0.440 -6.314 29.071 0.48 16.30 ? ? ? ? ? . 107 GLU A C 2349 ATOM 880 C C B GLU A 2349 107 . -0.383 -6.294 29.118 0.52 16.22 ? ? ? ? ? . 107 GLU A C 2349 ATOM 881 O O A GLU A 2349 107 . -1.159 -5.512 29.658 0.48 15.00 ? ? ? ? ? . 107 GLU A O 2349 ATOM 882 O O B GLU A 2349 107 . -0.983 -5.467 29.799 0.52 14.91 ? ? ? ? ? . 107 GLU A O 2349 ATOM 883 C CB A GLU A 2349 107 . 0.136 -7.934 30.885 0.48 18.90 ? ? ? ? ? . 107 GLU A CB 2349 ATOM 884 C CB B GLU A 2349 107 . -0.026 -8.061 30.878 0.52 18.53 ? ? ? ? ? . 107 GLU A CB 2349 ATOM 885 C CG A GLU A 2349 107 . -0.152 -9.282 31.527 0.48 20.28 ? ? ? ? ? . 107 GLU A CG 2349 ATOM 886 C CG B GLU A 2349 107 . -0.457 -9.445 31.335 0.52 19.46 ? ? ? ? ? . 107 GLU A CG 2349 ATOM 887 C CD A GLU A 2349 107 . -1.634 -9.612 31.585 0.48 20.99 ? ? ? ? ? . 107 GLU A CD 2349 ATOM 888 C CD B GLU A 2349 107 . -0.230 -9.688 32.809 0.52 20.69 ? ? ? ? ? . 107 GLU A CD 2349 ATOM 889 O OE1 A GLU A 2349 107 . -1.964 -10.810 31.716 0.48 22.80 ? ? ? ? ? . 107 GLU A OE1 2349 ATOM 890 O OE2 A GLU A 2349 107 . -2.475 -8.685 31.501 0.48 20.81 ? ? ? ? ? 1- 107 GLU A OE2 2349 ATOM 891 O OE1 B GLU A 2349 107 . 0.552 -8.941 33.435 0.52 21.77 ? ? ? ? ? . 107 GLU A OE1 2349 ATOM 892 O OE2 B GLU A 2349 107 . -0.834 -10.641 33.338 0.52 20.72 ? ? ? ? ? 1- 107 GLU A OE2 2349 ATOM 893 N N . SER A 2349 108 . 0.380 -5.969 28.081 1.00 15.68 ? ? ? ? ? . 108 SER A N 2349 ATOM 894 C CA . SER A 2349 108 . 0.383 -4.638 27.500 1.00 17.08 ? ? ? ? ? . 108 SER A CA 2349 ATOM 895 C C . SER A 2349 108 . 0.985 -4.755 26.112 1.00 16.89 ? ? ? ? ? . 108 SER A C 2349 ATOM 896 O O . SER A 2349 108 . 1.450 -5.829 25.729 1.00 17.73 ? ? ? ? ? . 108 SER A O 2349 ATOM 897 C CB . SER A 2349 108 . 1.213 -3.668 28.353 1.00 18.24 ? ? ? ? ? . 108 SER A CB 2349 ATOM 898 O OG . SER A 2349 108 . 2.566 -4.088 28.395 1.00 19.50 ? ? ? ? ? . 108 SER A OG 2349 ATOM 899 N N . ILE A 2349 109 . 0.943 -3.654 25.361 1.00 16.59 ? ? ? ? ? . 109 ILE A N 2349 ATOM 900 C CA . ILE A 2349 109 . 1.631 -3.552 24.077 1.00 16.95 ? ? ? ? ? . 109 ILE A CA 2349 ATOM 901 C C . ILE A 2349 109 . 2.424 -2.244 24.042 1.00 17.07 ? ? ? ? ? . 109 ILE A C 2349 ATOM 902 O O . ILE A 2349 109 . 2.119 -1.314 24.806 1.00 15.40 ? ? ? ? ? . 109 ILE A O 2349 ATOM 903 C CB . ILE A 2349 109 . 0.661 -3.621 22.878 1.00 16.61 ? ? ? ? ? . 109 ILE A CB 2349 ATOM 904 C CG1 . ILE A 2349 109 . -0.342 -2.464 22.916 1.00 16.67 ? ? ? ? ? . 109 ILE A CG1 2349 ATOM 905 C CG2 . ILE A 2349 109 . -0.070 -4.947 22.864 1.00 17.96 ? ? ? ? ? . 109 ILE A CG2 2349 ATOM 906 C CD1 . ILE A 2349 109 . -1.334 -2.459 21.764 1.00 17.14 ? ? ? ? ? . 109 ILE A CD1 2349 ATOM 907 N N . PRO A 2349 110 . 3.455 -2.163 23.184 1.00 17.10 ? ? ? ? ? . 110 PRO A N 2349 ATOM 908 C CA . PRO A 2349 110 . 3.969 -3.163 22.255 1.00 16.27 ? ? ? ? ? . 110 PRO A CA 2349 ATOM 909 C C . PRO A 2349 110 . 4.615 -4.367 22.957 1.00 16.00 ? ? ? ? ? . 110 PRO A C 2349 ATOM 910 O O . PRO A 2349 110 . 5.305 -4.213 23.960 1.00 15.22 ? ? ? ? ? . 110 PRO A O 2349 ATOM 911 C CB . PRO A 2349 110 . 5.004 -2.363 21.462 1.00 16.63 ? ? ? ? ? . 110 PRO A CB 2349 ATOM 912 C CG . PRO A 2349 110 . 5.544 -1.416 22.461 1.00 14.86 ? ? ? ? ? . 110 PRO A CG 2349 ATOM 913 C CD . PRO A 2349 110 . 4.334 -0.974 23.215 1.00 16.56 ? ? ? ? ? . 110 PRO A CD 2349 ATOM 914 N N . THR A 2349 111 . 4.358 -5.563 22.450 1.00 16.65 ? ? ? ? ? . 111 THR A N 2349 ATOM 915 C CA . THR A 2349 111 . 5.020 -6.757 22.952 1.00 16.87 ? ? ? ? ? . 111 THR A CA 2349 ATOM 916 C C . THR A 2349 111 . 5.390 -7.633 21.753 1.00 16.48 ? ? ? ? ? . 111 THR A C 2349 ATOM 917 O O . THR A 2349 111 . 4.610 -7.759 20.799 1.00 16.90 ? ? ? ? ? . 111 THR A O 2349 ATOM 918 C CB . THR A 2349 111 . 4.107 -7.527 23.939 1.00 17.53 ? ? ? ? ? . 111 THR A CB 2349 ATOM 919 C CG2 . THR A 2349 111 . 4.684 -8.888 24.316 1.00 18.56 ? ? ? ? ? . 111 THR A CG2 2349 ATOM 920 O OG1 . THR A 2349 111 . 3.924 -6.761 25.132 1.00 18.31 ? ? ? ? ? . 111 THR A OG1 2349 ATOM 921 N N . LEU A 2349 112 . 6.592 -8.200 21.806 1.00 15.48 ? ? ? ? ? . 112 LEU A N 2349 ATOM 922 C CA . LEU A 2349 112 . 7.032 -9.243 20.872 1.00 16.77 ? ? ? ? ? . 112 LEU A CA 2349 ATOM 923 C C . LEU A 2349 112 . 7.096 -10.595 21.590 1.00 17.72 ? ? ? ? ? . 112 LEU A C 2349 ATOM 924 O O . LEU A 2349 112 . 7.684 -10.706 22.669 1.00 18.56 ? ? ? ? ? . 112 LEU A O 2349 ATOM 925 C CB . LEU A 2349 112 . 8.420 -8.917 20.311 1.00 16.88 ? ? ? ? ? . 112 LEU A CB 2349 ATOM 926 C CG . LEU A 2349 112 . 8.521 -7.687 19.408 1.00 17.77 ? ? ? ? ? . 112 LEU A CG 2349 ATOM 927 C CD1 . LEU A 2349 112 . 9.973 -7.390 19.033 1.00 16.92 ? ? ? ? ? . 112 LEU A CD1 2349 ATOM 928 C CD2 . LEU A 2349 112 . 7.689 -7.898 18.153 1.00 19.55 ? ? ? ? ? . 112 LEU A CD2 2349 ATOM 929 N N . ILE A 2349 113 . 6.496 -11.617 20.990 1.00 15.87 ? ? ? ? ? . 113 ILE A N 2349 ATOM 930 C CA . ILE A 2349 113 . 6.651 -12.997 21.460 1.00 15.67 ? ? ? ? ? . 113 ILE A CA 2349 ATOM 931 C C . ILE A 2349 113 . 7.452 -13.761 20.404 1.00 16.43 ? ? ? ? ? . 113 ILE A C 2349 ATOM 932 O O . ILE A 2349 113 . 7.100 -13.752 19.241 1.00 17.53 ? ? ? ? ? . 113 ILE A O 2349 ATOM 933 C CB . ILE A 2349 113 . 5.284 -13.665 21.671 1.00 16.79 ? ? ? ? ? . 113 ILE A CB 2349 ATOM 934 C CG1 . ILE A 2349 113 . 4.438 -12.866 22.669 1.00 16.77 ? ? ? ? ? . 113 ILE A CG1 2349 ATOM 935 C CG2 . ILE A 2349 113 . 5.450 -15.106 22.132 1.00 16.45 ? ? ? ? ? . 113 ILE A CG2 2349 ATOM 936 C CD1 . ILE A 2349 113 . 5.059 -12.691 24.033 1.00 17.44 ? ? ? ? ? . 113 ILE A CD1 2349 ATOM 937 N N . THR A 2349 114 . 8.548 -14.395 20.806 1.00 15.64 ? ? ? ? ? . 114 THR A N 2349 ATOM 938 C CA . THR A 2349 114 . 9.432 -15.065 19.851 1.00 15.54 ? ? ? ? ? . 114 THR A CA 2349 ATOM 939 C C . THR A 2349 114 . 9.105 -16.535 19.804 1.00 16.03 ? ? ? ? ? . 114 THR A C 2349 ATOM 940 O O . THR A 2349 114 . 9.069 -17.201 20.843 1.00 15.89 ? ? ? ? ? . 114 THR A O 2349 ATOM 941 C CB . THR A 2349 114 . 10.899 -14.877 20.248 1.00 16.17 ? ? ? ? ? . 114 THR A CB 2349 ATOM 942 C CG2 . THR A 2349 114 . 11.843 -15.242 19.082 1.00 17.31 ? ? ? ? ? . 114 THR A CG2 2349 ATOM 943 O OG1 . THR A 2349 114 . 11.091 -13.522 20.641 1.00 16.08 ? ? ? ? ? . 114 THR A OG1 2349 ATOM 944 N N A ILE A 2349 115 . 8.888 -17.070 18.605 0.55 16.54 ? ? ? ? ? . 115 ILE A N 2349 ATOM 945 N N B ILE A 2349 115 . 8.876 -17.020 18.585 0.45 15.81 ? ? ? ? ? . 115 ILE A N 2349 ATOM 946 C CA A ILE A 2349 115 . 8.499 -18.473 18.450 0.55 16.27 ? ? ? ? ? . 115 ILE A CA 2349 ATOM 947 C CA B ILE A 2349 115 . 8.382 -18.358 18.324 0.45 15.23 ? ? ? ? ? . 115 ILE A CA 2349 ATOM 948 C C A ILE A 2349 115 . 9.340 -19.134 17.352 0.55 15.48 ? ? ? ? ? . 115 ILE A C 2349 ATOM 949 C C B ILE A 2349 115 . 9.324 -19.049 17.348 0.45 14.86 ? ? ? ? ? . 115 ILE A C 2349 ATOM 950 O O A ILE A 2349 115 . 9.682 -18.500 16.351 0.55 15.76 ? ? ? ? ? . 115 ILE A O 2349 ATOM 951 O O B ILE A 2349 115 . 9.872 -18.421 16.445 0.45 14.85 ? ? ? ? ? . 115 ILE A O 2349 ATOM 952 C CB A ILE A 2349 115 . 6.978 -18.584 18.143 0.55 16.88 ? ? ? ? ? . 115 ILE A CB 2349 ATOM 953 C CB B ILE A 2349 115 . 6.970 -18.282 17.698 0.45 14.58 ? ? ? ? ? . 115 ILE A CB 2349 ATOM 954 C CG1 A ILE A 2349 115 . 6.158 -18.040 19.325 0.55 17.01 ? ? ? ? ? . 115 ILE A CG1 2349 ATOM 955 C CG2 A ILE A 2349 115 . 6.558 -20.022 17.847 0.55 17.77 ? ? ? ? ? . 115 ILE A CG2 2349 ATOM 956 C CG1 B ILE A 2349 115 . 6.030 -17.511 18.630 0.45 13.86 ? ? ? ? ? . 115 ILE A CG1 2349 ATOM 957 C CG2 B ILE A 2349 115 . 6.416 -19.669 17.440 0.45 15.79 ? ? ? ? ? . 115 ILE A CG2 2349 ATOM 958 C CD1 A ILE A 2349 115 . 4.718 -17.741 18.993 0.55 18.59 ? ? ? ? ? . 115 ILE A CD1 2349 ATOM 959 C CD1 B ILE A 2349 115 . 5.831 -18.198 19.961 0.45 13.69 ? ? ? ? ? . 115 ILE A CD1 2349 ATOM 960 N N A ASN A 2349 116 . 9.696 -20.393 17.578 0.55 14.26 ? ? ? ? ? . 116 ASN A N 2349 ATOM 961 N N B ASN A 2349 116 . 9.528 -20.339 17.550 0.45 14.15 ? ? ? ? ? . 116 ASN A N 2349 ATOM 962 C CA A ASN A 2349 116 . 10.195 -21.272 16.531 0.55 14.49 ? ? ? ? ? . 116 ASN A CA 2349 ATOM 963 C CA B ASN A 2349 116 . 10.161 -21.166 16.547 0.45 14.57 ? ? ? ? ? . 116 ASN A CA 2349 ATOM 964 C C A ASN A 2349 116 . 8.994 -21.667 15.677 0.55 14.67 ? ? ? ? ? . 116 ASN A C 2349 ATOM 965 C C B ASN A 2349 116 . 9.036 -21.700 15.669 0.45 14.67 ? ? ? ? ? . 116 ASN A C 2349 ATOM 966 O O A ASN A 2349 116 . 8.060 -22.285 16.182 0.55 14.82 ? ? ? ? ? . 116 ASN A O 2349 ATOM 967 O O B ASN A 2349 116 . 8.204 -22.467 16.147 0.45 14.81 ? ? ? ? ? . 116 ASN A O 2349 ATOM 968 C CB A ASN A 2349 116 . 10.852 -22.511 17.146 0.55 14.78 ? ? ? ? ? . 116 ASN A CB 2349 ATOM 969 C CB B ASN A 2349 116 . 10.920 -22.308 17.211 0.45 15.08 ? ? ? ? ? . 116 ASN A CB 2349 ATOM 970 C CG A ASN A 2349 116 . 11.479 -23.433 16.108 0.55 14.39 ? ? ? ? ? . 116 ASN A CG 2349 ATOM 971 C CG B ASN A 2349 116 . 11.701 -23.154 16.220 0.45 15.35 ? ? ? ? ? . 116 ASN A CG 2349 ATOM 972 N ND2 A ASN A 2349 116 . 12.807 -23.467 16.077 0.55 15.51 ? ? ? ? ? . 116 ASN A ND2 2349 ATOM 973 O OD1 A ASN A 2349 116 . 10.785 -24.115 15.358 0.55 13.66 ? ? ? ? ? . 116 ASN A OD1 2349 ATOM 974 N ND2 B ASN A 2349 116 . 11.743 -24.447 16.470 0.45 15.08 ? ? ? ? ? . 116 ASN A ND2 2349 ATOM 975 O OD1 B ASN A 2349 116 . 12.279 -22.646 15.258 0.45 15.65 ? ? ? ? ? . 116 ASN A OD1 2349 ATOM 976 N N . ALA A 2349 117 . 9.000 -21.278 14.401 1.00 14.43 ? ? ? ? ? . 117 ALA A N 2349 ATOM 977 C CA . ALA A 2349 117 . 7.853 -21.558 13.494 1.00 15.56 ? ? ? ? ? . 117 ALA A CA 2349 ATOM 978 C C . ALA A 2349 117 . 7.501 -23.034 13.368 1.00 16.26 ? ? ? ? ? . 117 ALA A C 2349 ATOM 979 O O . ALA A 2349 117 . 6.317 -23.404 13.362 1.00 19.27 ? ? ? ? ? . 117 ALA A O 2349 ATOM 980 C CB . ALA A 2349 117 . 8.106 -20.984 12.098 1.00 15.32 ? ? ? ? ? . 117 ALA A CB 2349 ATOM 981 N N . ASP A 2349 118 . 8.530 -23.869 13.280 1.00 13.71 ? ? ? ? ? . 118 ASP A N 2349 ATOM 982 C CA . ASP A 2349 118 . 8.340 -25.280 12.997 1.00 13.63 ? ? ? ? ? . 118 ASP A CA 2349 ATOM 983 C C . ASP A 2349 118 . 7.697 -26.025 14.164 1.00 13.30 ? ? ? ? ? . 118 ASP A C 2349 ATOM 984 O O . ASP A 2349 118 . 6.772 -26.787 13.955 1.00 12.97 ? ? ? ? ? . 118 ASP A O 2349 ATOM 985 C CB . ASP A 2349 118 . 9.665 -25.950 12.628 1.00 13.67 ? ? ? ? ? . 118 ASP A CB 2349 ATOM 986 C CG . ASP A 2349 118 . 10.195 -25.494 11.295 1.00 14.35 ? ? ? ? ? . 118 ASP A CG 2349 ATOM 987 O OD1 . ASP A 2349 118 . 9.479 -24.785 10.536 1.00 13.29 ? ? ? ? ? . 118 ASP A OD1 2349 ATOM 988 O OD2 . ASP A 2349 118 . 11.353 -25.828 11.017 1.00 16.07 ? ? ? ? ? 1- 118 ASP A OD2 2349 ATOM 989 N N . THR A 2349 119 . 8.191 -25.774 15.372 1.00 13.59 ? ? ? ? ? . 119 THR A N 2349 ATOM 990 C CA . THR A 2349 119 . 7.739 -26.479 16.573 1.00 13.80 ? ? ? ? ? . 119 THR A CA 2349 ATOM 991 C C . THR A 2349 119 . 6.693 -25.695 17.356 1.00 13.84 ? ? ? ? ? . 119 THR A C 2349 ATOM 992 O O . THR A 2349 119 . 6.050 -26.256 18.241 1.00 15.00 ? ? ? ? ? . 119 THR A O 2349 ATOM 993 C CB . THR A 2349 119 . 8.912 -26.737 17.531 1.00 14.43 ? ? ? ? ? . 119 THR A CB 2349 ATOM 994 C CG2 . THR A 2349 119 . 10.039 -27.489 16.838 1.00 16.16 ? ? ? ? ? . 119 THR A CG2 2349 ATOM 995 O OG1 . THR A 2349 119 . 9.392 -25.493 18.029 1.00 14.78 ? ? ? ? ? . 119 THR A OG1 2349 ATOM 996 N N . GLY A 2349 120 . 6.550 -24.410 17.051 1.00 13.31 ? ? ? ? ? . 120 GLY A N 2349 ATOM 997 C CA . GLY A 2349 120 . 5.745 -23.482 17.845 1.00 15.55 ? ? ? ? ? . 120 GLY A CA 2349 ATOM 998 C C . GLY A 2349 120 . 6.291 -23.172 19.227 1.00 15.73 ? ? ? ? ? . 120 GLY A C 2349 ATOM 999 O O . GLY A 2349 120 . 5.607 -22.535 20.029 1.00 18.55 ? ? ? ? ? . 120 GLY A O 2349 ATOM 1000 N N . ALA A 2349 121 . 7.522 -23.581 19.519 1.00 15.46 ? ? ? ? ? . 121 ALA A N 2349 ATOM 1001 C CA . ALA A 2349 121 . 8.064 -23.394 20.865 1.00 15.87 ? ? ? ? ? . 121 ALA A CA 2349 ATOM 1002 C C . ALA A 2349 121 . 8.213 -21.904 21.136 1.00 15.57 ? ? ? ? ? . 121 ALA A C 2349 ATOM 1003 O O . ALA A 2349 121 . 8.585 -21.138 20.241 1.00 13.38 ? ? ? ? ? . 121 ALA A O 2349 ATOM 1004 C CB . ALA A 2349 121 . 9.389 -24.104 21.016 1.00 16.46 ? ? ? ? ? . 121 ALA A CB 2349 ATOM 1005 N N . ILE A 2349 122 . 7.880 -21.483 22.353 1.00 15.28 ? ? ? ? ? . 122 ILE A N 2349 ATOM 1006 C CA . ILE A 2349 122 . 8.156 -20.104 22.776 1.00 14.91 ? ? ? ? ? . 122 ILE A CA 2349 ATOM 1007 C C . ILE A 2349 122 . 9.641 -20.062 23.119 1.00 15.51 ? ? ? ? ? . 122 ILE A C 2349 ATOM 1008 O O . ILE A 2349 122 . 10.119 -20.875 23.900 1.00 16.67 ? ? ? ? ? . 122 ILE A O 2349 ATOM 1009 C CB . ILE A 2349 122 . 7.290 -19.669 23.961 1.00 15.79 ? ? ? ? ? . 122 ILE A CB 2349 ATOM 1010 C CG1 . ILE A 2349 122 . 5.823 -19.696 23.552 1.00 17.18 ? ? ? ? ? . 122 ILE A CG1 2349 ATOM 1011 C CG2 . ILE A 2349 122 . 7.689 -18.266 24.434 1.00 17.48 ? ? ? ? ? . 122 ILE A CG2 2349 ATOM 1012 C CD1 . ILE A 2349 122 . 4.864 -19.526 24.708 1.00 17.88 ? ? ? ? ? . 122 ILE A CD1 2349 ATOM 1013 N N A ILE A 2349 123 . 10.392 -19.155 22.503 0.47 13.95 ? ? ? ? ? . 123 ILE A N 2349 ATOM 1014 N N B ILE A 2349 123 . 10.323 -19.113 22.485 0.53 15.23 ? ? ? ? ? . 123 ILE A N 2349 ATOM 1015 C CA A ILE A 2349 123 . 11.809 -18.977 22.850 0.47 14.95 ? ? ? ? ? . 123 ILE A CA 2349 ATOM 1016 C CA B ILE A 2349 123 . 11.762 -18.894 22.572 0.53 17.28 ? ? ? ? ? . 123 ILE A CA 2349 ATOM 1017 C C A ILE A 2349 123 . 12.170 -17.581 23.356 0.47 15.02 ? ? ? ? ? . 123 ILE A C 2349 ATOM 1018 C C B ILE A 2349 123 . 12.096 -17.681 23.473 0.53 16.15 ? ? ? ? ? . 123 ILE A C 2349 ATOM 1019 O O A ILE A 2349 123 . 13.349 -17.281 23.543 0.47 15.33 ? ? ? ? ? . 123 ILE A O 2349 ATOM 1020 O O B ILE A 2349 123 . 13.152 -17.646 24.107 0.53 15.98 ? ? ? ? ? . 123 ILE A O 2349 ATOM 1021 C CB A ILE A 2349 123 . 12.723 -19.369 21.683 0.47 14.78 ? ? ? ? ? . 123 ILE A CB 2349 ATOM 1022 C CB B ILE A 2349 123 . 12.330 -18.807 21.116 0.53 19.50 ? ? ? ? ? . 123 ILE A CB 2349 ATOM 1023 C CG1 A ILE A 2349 123 . 12.353 -18.591 20.417 0.47 14.37 ? ? ? ? ? . 123 ILE A CG1 2349 ATOM 1024 C CG2 A ILE A 2349 123 . 12.618 -20.868 21.444 0.47 15.29 ? ? ? ? ? . 123 ILE A CG2 2349 ATOM 1025 C CG1 B ILE A 2349 123 . 13.033 -20.116 20.737 0.53 21.28 ? ? ? ? ? . 123 ILE A CG1 2349 ATOM 1026 C CG2 B ILE A 2349 123 . 13.317 -17.675 20.906 0.53 20.71 ? ? ? ? ? . 123 ILE A CG2 2349 ATOM 1027 C CD1 A ILE A 2349 123 . 13.153 -19.012 19.200 0.47 14.19 ? ? ? ? ? . 123 ILE A CD1 2349 ATOM 1028 C CD1 B ILE A 2349 123 . 12.135 -21.339 20.747 0.53 22.34 ? ? ? ? ? . 123 ILE A CD1 2349 ATOM 1029 N N . GLY A 2349 124 . 11.173 -16.729 23.568 1.00 15.77 ? ? ? ? ? . 124 GLY A N 2349 ATOM 1030 C CA . GLY A 2349 124 . 11.373 -15.508 24.323 1.00 15.97 ? ? ? ? ? . 124 GLY A CA 2349 ATOM 1031 C C . GLY A 2349 124 . 10.096 -14.707 24.394 1.00 15.46 ? ? ? ? ? . 124 GLY A C 2349 ATOM 1032 O O . GLY A 2349 124 . 9.193 -14.882 23.581 1.00 15.31 ? ? ? ? ? . 124 GLY A O 2349 ATOM 1033 N N . THR A 2349 125 . 10.008 -13.856 25.405 1.00 14.42 ? ? ? ? ? . 125 THR A N 2349 ATOM 1034 C CA . THR A 2349 125 . 8.920 -12.890 25.529 1.00 14.27 ? ? ? ? ? . 125 THR A CA 2349 ATOM 1035 C C . THR A 2349 125 . 9.371 -11.431 25.677 1.00 14.34 ? ? ? ? ? . 125 THR A C 2349 ATOM 1036 O O . THR A 2349 125 . 8.520 -10.535 25.770 1.00 13.54 ? ? ? ? ? . 125 THR A O 2349 ATOM 1037 C CB . THR A 2349 125 . 8.063 -13.230 26.766 1.00 15.10 ? ? ? ? ? . 125 THR A CB 2349 ATOM 1038 C CG2 . THR A 2349 125 . 7.560 -14.673 26.687 1.00 15.56 ? ? ? ? ? . 125 THR A CG2 2349 ATOM 1039 O OG1 . THR A 2349 125 . 8.859 -13.073 27.951 1.00 15.70 ? ? ? ? ? . 125 THR A OG1 2349 ATOM 1040 N N A GLN A 2349 126 . 10.689 -11.200 25.676 0.65 15.74 ? ? ? ? ? . 126 GLN A N 2349 ATOM 1041 N N B GLN A 2349 126 . 10.683 -11.184 25.692 0.35 15.08 ? ? ? ? ? . 126 GLN A N 2349 ATOM 1042 C CA A GLN A 2349 126 . 11.267 -9.893 25.996 0.65 16.74 ? ? ? ? ? . 126 GLN A CA 2349 ATOM 1043 C CA B GLN A 2349 126 . 11.214 -9.851 25.975 0.35 15.65 ? ? ? ? ? . 126 GLN A CA 2349 ATOM 1044 C C A GLN A 2349 126 . 11.938 -9.209 24.799 0.65 16.96 ? ? ? ? ? . 126 GLN A C 2349 ATOM 1045 C C B GLN A 2349 126 . 11.948 -9.214 24.801 0.35 16.17 ? ? ? ? ? . 126 GLN A C 2349 ATOM 1046 O O A GLN A 2349 126 . 12.672 -8.231 24.982 0.65 18.20 ? ? ? ? ? . 126 GLN A O 2349 ATOM 1047 O O B GLN A 2349 126 . 12.738 -8.285 25.009 0.35 17.02 ? ? ? ? ? . 126 GLN A O 2349 ATOM 1048 C CB A GLN A 2349 126 . 12.281 -10.056 27.137 0.65 17.82 ? ? ? ? ? . 126 GLN A CB 2349 ATOM 1049 C CB B GLN A 2349 126 . 12.138 -9.924 27.186 0.35 15.92 ? ? ? ? ? . 126 GLN A CB 2349 ATOM 1050 C CG A GLN A 2349 126 . 11.700 -10.649 28.418 0.65 19.05 ? ? ? ? ? . 126 GLN A CG 2349 ATOM 1051 C CG B GLN A 2349 126 . 11.370 -10.101 28.485 0.35 16.11 ? ? ? ? ? . 126 GLN A CG 2349 ATOM 1052 C CD A GLN A 2349 126 . 10.613 -9.780 29.040 0.65 21.28 ? ? ? ? ? . 126 GLN A CD 2349 ATOM 1053 C CD B GLN A 2349 126 . 12.269 -10.217 29.694 0.35 16.65 ? ? ? ? ? . 126 GLN A CD 2349 ATOM 1054 N NE2 A GLN A 2349 126 . 9.365 -10.244 28.979 0.65 21.64 ? ? ? ? ? . 126 GLN A NE2 2349 ATOM 1055 O OE1 A GLN A 2349 126 . 10.896 -8.711 29.578 0.65 24.99 ? ? ? ? ? . 126 GLN A OE1 2349 ATOM 1056 N NE2 B GLN A 2349 126 . 12.111 -9.296 30.636 0.35 16.48 ? ? ? ? ? . 126 GLN A NE2 2349 ATOM 1057 O OE1 B GLN A 2349 126 . 13.085 -11.133 29.790 0.35 16.80 ? ? ? ? ? . 126 GLN A OE1 2349 ATOM 1058 N N . ALA A 2349 127 . 11.681 -9.681 23.580 1.00 16.07 ? ? ? ? ? . 127 ALA A N 2349 ATOM 1059 C CA . ALA A 2349 127 . 12.365 -9.138 22.395 1.00 15.77 ? ? ? ? ? . 127 ALA A CA 2349 ATOM 1060 C C . ALA A 2349 127 . 12.118 -7.629 22.136 1.00 16.92 ? ? ? ? ? . 127 ALA A C 2349 ATOM 1061 O O . ALA A 2349 127 . 12.988 -6.961 21.574 1.00 16.61 ? ? ? ? ? . 127 ALA A O 2349 ATOM 1062 C CB . ALA A 2349 127 . 12.088 -9.962 21.152 1.00 15.60 ? ? ? ? ? . 127 ALA A CB 2349 ATOM 1063 N N A ARG A 2349 128 . 10.956 -7.112 22.537 0.56 17.01 ? ? ? ? ? . 128 ARG A N 2349 ATOM 1064 N N B ARG A 2349 128 . 10.970 -7.103 22.563 0.44 16.65 ? ? ? ? ? . 128 ARG A N 2349 ATOM 1065 C CA A ARG A 2349 128 . 10.675 -5.662 22.452 0.56 17.35 ? ? ? ? ? . 128 ARG A CA 2349 ATOM 1066 C CA B ARG A 2349 128 . 10.711 -5.658 22.477 0.44 16.75 ? ? ? ? ? . 128 ARG A CA 2349 ATOM 1067 C C A ARG A 2349 128 . 11.742 -4.852 23.213 0.56 17.98 ? ? ? ? ? . 128 ARG A C 2349 ATOM 1068 C C B ARG A 2349 128 . 11.832 -4.909 23.210 0.44 17.06 ? ? ? ? ? . 128 ARG A C 2349 ATOM 1069 O O A ARG A 2349 128 . 12.117 -3.754 22.795 0.56 19.74 ? ? ? ? ? . 128 ARG A O 2349 ATOM 1070 O O B ARG A 2349 128 . 12.397 -3.949 22.691 0.44 18.15 ? ? ? ? ? . 128 ARG A O 2349 ATOM 1071 C CB A ARG A 2349 128 . 9.263 -5.347 22.979 0.56 17.73 ? ? ? ? ? . 128 ARG A CB 2349 ATOM 1072 C CB B ARG A 2349 128 . 9.339 -5.312 23.066 0.44 16.87 ? ? ? ? ? . 128 ARG A CB 2349 ATOM 1073 C CG A ARG A 2349 128 . 8.870 -3.865 23.016 0.56 18.71 ? ? ? ? ? . 128 ARG A CG 2349 ATOM 1074 C CG B ARG A 2349 128 . 8.901 -3.861 22.874 0.44 17.49 ? ? ? ? ? . 128 ARG A CG 2349 ATOM 1075 C CD A ARG A 2349 128 . 9.128 -3.215 24.373 0.56 20.16 ? ? ? ? ? . 128 ARG A CD 2349 ATOM 1076 C CD B ARG A 2349 128 . 9.642 -2.916 23.804 0.44 18.39 ? ? ? ? ? . 128 ARG A CD 2349 ATOM 1077 N NE A ARG A 2349 128 . 8.614 -1.848 24.461 0.56 21.19 ? ? ? ? ? . 128 ARG A NE 2349 ATOM 1078 N NE B ARG A 2349 128 . 9.174 -1.532 23.713 0.44 18.67 ? ? ? ? ? . 128 ARG A NE 2349 ATOM 1079 C CZ A ARG A 2349 128 . 9.152 -0.774 23.876 0.56 22.12 ? ? ? ? ? . 128 ARG A CZ 2349 ATOM 1080 C CZ B ARG A 2349 128 . 8.307 -0.973 24.557 0.44 18.88 ? ? ? ? ? . 128 ARG A CZ 2349 ATOM 1081 N NH1 A ARG A 2349 128 . 10.245 -0.862 23.118 0.56 21.19 ? ? ? ? ? 1+ 128 ARG A NH1 2349 ATOM 1082 N NH2 A ARG A 2349 128 . 8.582 0.419 24.051 0.56 22.67 ? ? ? ? ? . 128 ARG A NH2 2349 ATOM 1083 N NH1 B ARG A 2349 128 . 7.788 -1.677 25.551 0.44 18.59 ? ? ? ? ? 1+ 128 ARG A NH1 2349 ATOM 1084 N NH2 B ARG A 2349 128 . 7.951 0.296 24.402 0.44 19.51 ? ? ? ? ? . 128 ARG A NH2 2349 ATOM 1085 N N A THR A 2349 129 . 12.197 -5.402 24.338 0.56 16.60 ? ? ? ? ? . 129 THR A N 2349 ATOM 1086 N N B THR A 2349 129 . 12.172 -5.391 24.401 0.44 16.19 ? ? ? ? ? . 129 THR A N 2349 ATOM 1087 C CA A THR A 2349 129 . 13.260 -4.819 25.151 0.56 15.90 ? ? ? ? ? . 129 THR A CA 2349 ATOM 1088 C CA B THR A 2349 129 . 13.262 -4.829 25.190 0.44 15.82 ? ? ? ? ? . 129 THR A CA 2349 ATOM 1089 C C A THR A 2349 129 . 14.648 -5.072 24.556 0.56 15.75 ? ? ? ? ? . 129 THR A C 2349 ATOM 1090 C C B THR A 2349 129 . 14.652 -5.082 24.590 0.44 15.77 ? ? ? ? ? . 129 THR A C 2349 ATOM 1091 O O A THR A 2349 129 . 15.501 -4.173 24.523 0.56 14.19 ? ? ? ? ? . 129 THR A O 2349 ATOM 1092 O O B THR A 2349 129 . 15.508 -4.188 24.583 0.44 14.57 ? ? ? ? ? . 129 THR A O 2349 ATOM 1093 C CB A THR A 2349 129 . 13.199 -5.413 26.563 0.56 16.22 ? ? ? ? ? . 129 THR A CB 2349 ATOM 1094 C CB B THR A 2349 129 . 13.239 -5.411 26.607 0.44 16.28 ? ? ? ? ? . 129 THR A CB 2349 ATOM 1095 C CG2 A THR A 2349 129 . 14.194 -4.750 27.499 0.56 16.27 ? ? ? ? ? . 129 THR A CG2 2349 ATOM 1096 O OG1 A THR A 2349 129 . 11.866 -5.240 27.067 0.56 15.54 ? ? ? ? ? . 129 THR A OG1 2349 ATOM 1097 C CG2 B THR A 2349 129 . 14.425 -4.927 27.397 0.44 16.31 ? ? ? ? ? . 129 THR A CG2 2349 ATOM 1098 O OG1 B THR A 2349 129 . 12.025 -5.011 27.257 0.44 16.08 ? ? ? ? ? . 129 THR A OG1 2349 ATOM 1099 N N . ARG A 2349 130 . 14.877 -6.301 24.106 1.00 15.66 ? ? ? ? ? . 130 ARG A N 2349 ATOM 1100 C CA . ARG A 2349 130 . 16.188 -6.692 23.577 1.00 16.35 ? ? ? ? ? . 130 ARG A CA 2349 ATOM 1101 C C . ARG A 2349 130 . 16.559 -5.897 22.320 1.00 15.65 ? ? ? ? ? . 130 ARG A C 2349 ATOM 1102 O O . ARG A 2349 130 . 17.720 -5.558 22.136 1.00 15.70 ? ? ? ? ? . 130 ARG A O 2349 ATOM 1103 C CB . ARG A 2349 130 . 16.246 -8.188 23.306 1.00 18.25 ? ? ? ? ? . 130 ARG A CB 2349 ATOM 1104 C CG . ARG A 2349 130 . 16.058 -9.052 24.544 1.00 20.23 ? ? ? ? ? . 130 ARG A CG 2349 ATOM 1105 C CD . ARG A 2349 130 . 17.267 -9.045 25.461 1.00 24.15 ? ? ? ? ? . 130 ARG A CD 2349 ATOM 1106 N NE . ARG A 2349 130 . 16.962 -9.671 26.747 1.00 26.08 ? ? ? ? ? . 130 ARG A NE 2349 ATOM 1107 C CZ . ARG A 2349 130 . 16.384 -9.059 27.784 1.00 29.65 ? ? ? ? ? . 130 ARG A CZ 2349 ATOM 1108 N NH1 . ARG A 2349 130 . 15.999 -7.782 27.725 1.00 30.49 ? ? ? ? ? 1+ 130 ARG A NH1 2349 ATOM 1109 N NH2 . ARG A 2349 130 . 16.171 -9.748 28.906 1.00 33.51 ? ? ? ? ? . 130 ARG A NH2 2349 ATOM 1110 N N . VAL A 2349 131 . 15.561 -5.570 21.501 1.00 15.55 ? ? ? ? ? . 131 VAL A N 2349 ATOM 1111 C CA . VAL A 2349 131 . 15.755 -4.735 20.300 1.00 16.06 ? ? ? ? ? . 131 VAL A CA 2349 ATOM 1112 C C . VAL A 2349 131 . 16.319 -3.355 20.678 1.00 15.16 ? ? ? ? ? . 131 VAL A C 2349 ATOM 1113 O O . VAL A 2349 131 . 17.149 -2.806 19.958 1.00 14.17 ? ? ? ? ? . 131 VAL A O 2349 ATOM 1114 C CB . VAL A 2349 131 . 14.431 -4.608 19.503 1.00 18.89 ? ? ? ? ? . 131 VAL A CB 2349 ATOM 1115 C CG1 . VAL A 2349 131 . 14.491 -3.492 18.465 1.00 19.08 ? ? ? ? ? . 131 VAL A CG1 2349 ATOM 1116 C CG2 . VAL A 2349 131 . 14.079 -5.950 18.859 1.00 21.65 ? ? ? ? ? . 131 VAL A CG2 2349 ATOM 1117 N N A ILE A 2349 132 . 15.856 -2.817 21.806 0.19 15.13 ? ? ? ? ? . 132 ILE A N 2349 ATOM 1118 N N B ILE A 2349 132 . 15.884 -2.809 21.816 0.81 15.27 ? ? ? ? ? . 132 ILE A N 2349 ATOM 1119 C CA A ILE A 2349 132 . 16.341 -1.547 22.332 0.19 15.00 ? ? ? ? ? . 132 ILE A CA 2349 ATOM 1120 C CA B ILE A 2349 132 . 16.395 -1.520 22.293 0.81 14.70 ? ? ? ? ? . 132 ILE A CA 2349 ATOM 1121 C C A ILE A 2349 132 . 17.808 -1.612 22.736 0.19 14.96 ? ? ? ? ? . 132 ILE A C 2349 ATOM 1122 C C B ILE A 2349 132 . 17.849 -1.630 22.707 0.81 14.54 ? ? ? ? ? . 132 ILE A C 2349 ATOM 1123 O O A ILE A 2349 132 . 18.613 -0.783 22.313 0.19 14.79 ? ? ? ? ? . 132 ILE A O 2349 ATOM 1124 O O B ILE A 2349 132 . 18.686 -0.831 22.296 0.81 13.48 ? ? ? ? ? . 132 ILE A O 2349 ATOM 1125 C CB A ILE A 2349 132 . 15.520 -1.130 23.564 0.19 14.92 ? ? ? ? ? . 132 ILE A CB 2349 ATOM 1126 C CB B ILE A 2349 132 . 15.575 -0.974 23.489 0.81 14.72 ? ? ? ? ? . 132 ILE A CB 2349 ATOM 1127 C CG1 A ILE A 2349 132 . 14.034 -1.319 23.280 0.19 15.02 ? ? ? ? ? . 132 ILE A CG1 2349 ATOM 1128 C CG2 A ILE A 2349 132 . 15.824 0.307 23.942 0.19 14.66 ? ? ? ? ? . 132 ILE A CG2 2349 ATOM 1129 C CG1 B ILE A 2349 132 . 14.149 -0.656 23.059 0.81 15.47 ? ? ? ? ? . 132 ILE A CG1 2349 ATOM 1130 C CG2 B ILE A 2349 132 . 16.235 0.255 24.089 0.81 13.99 ? ? ? ? ? . 132 ILE A CG2 2349 ATOM 1131 C CD1 A ILE A 2349 132 . 13.567 -0.581 22.051 0.19 15.23 ? ? ? ? ? . 132 ILE A CD1 2349 ATOM 1132 C CD1 B ILE A 2349 132 . 13.182 -0.605 24.230 0.81 16.62 ? ? ? ? ? . 132 ILE A CD1 2349 ATOM 1133 N N . GLU A 2349 133 . 18.144 -2.599 23.559 1.00 14.85 ? ? ? ? ? . 133 GLU A N 2349 ATOM 1134 C CA . GLU A 2349 133 . 19.500 -2.725 24.095 1.00 15.86 ? ? ? ? ? . 133 GLU A CA 2349 ATOM 1135 C C . GLU A 2349 133 . 20.510 -3.300 23.114 1.00 15.18 ? ? ? ? ? . 133 GLU A C 2349 ATOM 1136 O O . GLU A 2349 133 . 21.694 -3.025 23.243 1.00 14.71 ? ? ? ? ? . 133 GLU A O 2349 ATOM 1137 C CB . GLU A 2349 133 . 19.516 -3.523 25.385 1.00 18.34 ? ? ? ? ? . 133 GLU A CB 2349 ATOM 1138 C CG . GLU A 2349 133 . 19.099 -4.959 25.269 1.00 21.00 ? ? ? ? ? . 133 GLU A CG 2349 ATOM 1139 C CD . GLU A 2349 133 . 19.009 -5.600 26.628 1.00 24.62 ? ? ? ? ? . 133 GLU A CD 2349 ATOM 1140 O OE1 . GLU A 2349 133 . 17.888 -5.653 27.182 1.00 24.54 ? ? ? ? ? . 133 GLU A OE1 2349 ATOM 1141 O OE2 . GLU A 2349 133 . 20.070 -6.015 27.133 1.00 24.87 ? ? ? ? ? 1- 133 GLU A OE2 2349 ATOM 1142 N N . ASP A 2349 134 . 20.031 -4.102 22.163 1.00 15.80 ? ? ? ? ? . 134 ASP A N 2349 ATOM 1143 C CA . ASP A 2349 134 . 20.885 -4.847 21.228 1.00 16.53 ? ? ? ? ? . 134 ASP A CA 2349 ATOM 1144 C C . ASP A 2349 134 . 20.373 -4.627 19.798 1.00 16.35 ? ? ? ? ? . 134 ASP A C 2349 ATOM 1145 O O . ASP A 2349 134 . 19.922 -5.562 19.131 1.00 16.33 ? ? ? ? ? . 134 ASP A O 2349 ATOM 1146 C CB . ASP A 2349 134 . 20.881 -6.341 21.606 1.00 16.03 ? ? ? ? ? . 134 ASP A CB 2349 ATOM 1147 C CG . ASP A 2349 134 . 21.859 -7.184 20.769 1.00 16.81 ? ? ? ? ? . 134 ASP A CG 2349 ATOM 1148 O OD1 . ASP A 2349 134 . 22.869 -6.642 20.264 1.00 16.39 ? ? ? ? ? . 134 ASP A OD1 2349 ATOM 1149 O OD2 . ASP A 2349 134 . 21.614 -8.404 20.635 1.00 16.25 ? ? ? ? ? 1- 134 ASP A OD2 2349 ATOM 1150 N N . PRO A 2349 135 . 20.451 -3.379 19.309 1.00 15.65 ? ? ? ? ? . 135 PRO A N 2349 ATOM 1151 C CA . PRO A 2349 135 . 19.917 -3.103 17.962 1.00 16.45 ? ? ? ? ? . 135 PRO A CA 2349 ATOM 1152 C C . PRO A 2349 135 . 20.699 -3.798 16.828 1.00 17.49 ? ? ? ? ? . 135 PRO A C 2349 ATOM 1153 O O . PRO A 2349 135 . 20.164 -3.961 15.727 1.00 19.27 ? ? ? ? ? . 135 PRO A O 2349 ATOM 1154 C CB . PRO A 2349 135 . 20.036 -1.580 17.849 1.00 16.15 ? ? ? ? ? . 135 PRO A CB 2349 ATOM 1155 C CG . PRO A 2349 135 . 21.147 -1.228 18.767 1.00 15.72 ? ? ? ? ? . 135 PRO A CG 2349 ATOM 1156 C CD . PRO A 2349 135 . 21.003 -2.165 19.931 1.00 16.34 ? ? ? ? ? . 135 PRO A CD 2349 ATOM 1157 N N . ASP A 2349 136 . 21.943 -4.192 17.089 1.00 18.50 ? ? ? ? ? . 136 ASP A N 2349 ATOM 1158 C CA . ASP A 2349 136 . 22.709 -4.962 16.102 1.00 18.72 ? ? ? ? ? . 136 ASP A CA 2349 ATOM 1159 C C . ASP A 2349 136 . 22.475 -6.472 16.207 1.00 19.15 ? ? ? ? ? . 136 ASP A C 2349 ATOM 1160 O O . ASP A 2349 136 . 23.067 -7.249 15.446 1.00 18.36 ? ? ? ? ? . 136 ASP A O 2349 ATOM 1161 C CB . ASP A 2349 136 . 24.208 -4.659 16.203 1.00 19.68 ? ? ? ? ? . 136 ASP A CB 2349 ATOM 1162 C CG . ASP A 2349 136 . 24.951 -5.002 14.926 1.00 20.65 ? ? ? ? ? . 136 ASP A CG 2349 ATOM 1163 O OD1 . ASP A 2349 136 . 24.302 -4.958 13.849 1.00 19.34 ? ? ? ? ? . 136 ASP A OD1 2349 ATOM 1164 O OD2 . ASP A 2349 136 . 26.167 -5.316 14.990 1.00 18.99 ? ? ? ? ? 1- 136 ASP A OD2 2349 ATOM 1165 N N . GLY A 2349 137 . 21.644 -6.897 17.152 1.00 19.37 ? ? ? ? ? . 137 GLY A N 2349 ATOM 1166 C CA . GLY A 2349 137 . 21.276 -8.295 17.269 1.00 18.65 ? ? ? ? ? . 137 GLY A CA 2349 ATOM 1167 C C . GLY A 2349 137 . 22.434 -9.246 17.520 1.00 18.62 ? ? ? ? ? . 137 GLY A C 2349 ATOM 1168 O O . GLY A 2349 137 . 22.362 -10.405 17.126 1.00 17.20 ? ? ? ? ? . 137 GLY A O 2349 ATOM 1169 N N . ALA A 2349 138 . 23.489 -8.772 18.186 1.00 18.23 ? ? ? ? ? . 138 ALA A N 2349 ATOM 1170 C CA . ALA A 2349 138 . 24.618 -9.638 18.572 1.00 18.91 ? ? ? ? ? . 138 ALA A CA 2349 ATOM 1171 C C . ALA A 2349 138 . 24.172 -10.873 19.359 1.00 18.87 ? ? ? ? ? . 138 ALA A C 2349 ATOM 1172 O O . ALA A 2349 138 . 24.763 -11.937 19.209 1.00 18.45 ? ? ? ? ? . 138 ALA A O 2349 ATOM 1173 C CB . ALA A 2349 138 . 25.646 -8.865 19.388 1.00 19.07 ? ? ? ? ? . 138 ALA A CB 2349 ATOM 1174 N N . ASN A 2349 139 . 23.150 -10.721 20.207 1.00 17.91 ? ? ? ? ? . 139 ASN A N 2349 ATOM 1175 C CA . ASN A 2349 139 . 22.657 -11.826 21.042 1.00 18.78 ? ? ? ? ? . 139 ASN A CA 2349 ATOM 1176 C C . ASN A 2349 139 . 21.320 -12.415 20.575 1.00 18.34 ? ? ? ? ? . 139 ASN A C 2349 ATOM 1177 O O . ASN A 2349 139 . 20.716 -13.222 21.284 1.00 16.63 ? ? ? ? ? . 139 ASN A O 2349 ATOM 1178 C CB . ASN A 2349 139 . 22.558 -11.357 22.493 1.00 20.43 ? ? ? ? ? . 139 ASN A CB 2349 ATOM 1179 C CG . ASN A 2349 139 . 23.907 -11.007 23.077 1.00 22.54 ? ? ? ? ? . 139 ASN A CG 2349 ATOM 1180 N ND2 . ASN A 2349 139 . 24.033 -9.800 23.604 1.00 24.70 ? ? ? ? ? . 139 ASN A ND2 2349 ATOM 1181 O OD1 . ASN A 2349 139 . 24.826 -11.813 23.049 1.00 25.00 ? ? ? ? ? . 139 ASN A OD1 2349 ATOM 1182 N N . PHE A 2349 140 . 20.862 -12.019 19.387 1.00 19.01 ? ? ? ? ? . 140 PHE A N 2349 ATOM 1183 C CA . PHE A 2349 140 . 19.669 -12.603 18.768 1.00 20.41 ? ? ? ? ? . 140 PHE A CA 2349 ATOM 1184 C C . PHE A 2349 140 . 19.812 -14.133 18.747 1.00 20.42 ? ? ? ? ? . 140 PHE A C 2349 ATOM 1185 O O . PHE A 2349 140 . 20.913 -14.633 18.513 1.00 17.90 ? ? ? ? ? . 140 PHE A O 2349 ATOM 1186 C CB . PHE A 2349 140 . 19.522 -12.084 17.327 1.00 21.52 ? ? ? ? ? . 140 PHE A CB 2349 ATOM 1187 C CG . PHE A 2349 140 . 18.452 -12.782 16.532 1.00 22.24 ? ? ? ? ? . 140 PHE A CG 2349 ATOM 1188 C CD1 . PHE A 2349 140 . 18.719 -13.998 15.901 1.00 21.67 ? ? ? ? ? . 140 PHE A CD1 2349 ATOM 1189 C CD2 . PHE A 2349 140 . 17.181 -12.252 16.440 1.00 21.18 ? ? ? ? ? . 140 PHE A CD2 2349 ATOM 1190 C CE1 . PHE A 2349 140 . 17.745 -14.662 15.185 1.00 20.84 ? ? ? ? ? . 140 PHE A CE1 2349 ATOM 1191 C CE2 . PHE A 2349 140 . 16.205 -12.923 15.721 1.00 21.80 ? ? ? ? ? . 140 PHE A CE2 2349 ATOM 1192 C CZ . PHE A 2349 140 . 16.490 -14.121 15.089 1.00 20.62 ? ? ? ? ? . 140 PHE A CZ 2349 ATOM 1193 N N . PRO A 2349 141 . 18.713 -14.878 18.978 1.00 19.68 ? ? ? ? ? . 141 PRO A N 2349 ATOM 1194 C CA . PRO A 2349 141 . 17.322 -14.496 19.270 1.00 20.19 ? ? ? ? ? . 141 PRO A CA 2349 ATOM 1195 C C . PRO A 2349 141 . 17.031 -14.317 20.773 1.00 20.52 ? ? ? ? ? . 141 PRO A C 2349 ATOM 1196 O O . PRO A 2349 141 . 15.896 -14.485 21.219 1.00 20.28 ? ? ? ? ? . 141 PRO A O 2349 ATOM 1197 C CB . PRO A 2349 141 . 16.531 -15.649 18.667 1.00 20.58 ? ? ? ? ? . 141 PRO A CB 2349 ATOM 1198 C CG . PRO A 2349 141 . 17.408 -16.822 18.883 1.00 22.19 ? ? ? ? ? . 141 PRO A CG 2349 ATOM 1199 C CD . PRO A 2349 141 . 18.835 -16.342 18.841 1.00 21.97 ? ? ? ? ? . 141 PRO A CD 2349 ATOM 1200 N N . TRP A 2349 142 . 18.070 -13.962 21.521 1.00 19.76 ? ? ? ? ? . 142 TRP A N 2349 ATOM 1201 C CA . TRP A 2349 142 . 17.983 -13.534 22.901 1.00 21.33 ? ? ? ? ? . 142 TRP A CA 2349 ATOM 1202 C C . TRP A 2349 142 . 17.420 -14.620 23.822 1.00 25.77 ? ? ? ? ? . 142 TRP A C 2349 ATOM 1203 O O . TRP A 2349 142 . 16.345 -14.426 24.421 1.00 25.77 ? ? ? ? ? . 142 TRP A O 2349 ATOM 1204 C CB . TRP A 2349 142 . 17.210 -12.224 23.014 1.00 19.99 ? ? ? ? ? . 142 TRP A CB 2349 ATOM 1205 C CG . TRP A 2349 142 . 17.778 -11.119 22.165 1.00 18.70 ? ? ? ? ? . 142 TRP A CG 2349 ATOM 1206 C CD1 . TRP A 2349 142 . 18.994 -10.522 22.306 1.00 18.19 ? ? ? ? ? . 142 TRP A CD1 2349 ATOM 1207 C CD2 . TRP A 2349 142 . 17.132 -10.461 21.076 1.00 17.96 ? ? ? ? ? . 142 TRP A CD2 2349 ATOM 1208 C CE2 . TRP A 2349 142 . 18.022 -9.480 20.595 1.00 18.04 ? ? ? ? ? . 142 TRP A CE2 2349 ATOM 1209 C CE3 . TRP A 2349 142 . 15.890 -10.610 20.454 1.00 18.59 ? ? ? ? ? . 142 TRP A CE3 2349 ATOM 1210 N NE1 . TRP A 2349 142 . 19.156 -9.555 21.357 1.00 17.87 ? ? ? ? ? . 142 TRP A NE1 2349 ATOM 1211 C CZ2 . TRP A 2349 142 . 17.711 -8.645 19.516 1.00 17.55 ? ? ? ? ? . 142 TRP A CZ2 2349 ATOM 1212 C CZ3 . TRP A 2349 142 . 15.574 -9.787 19.397 1.00 19.05 ? ? ? ? ? . 142 TRP A CZ3 2349 ATOM 1213 C CH2 . TRP A 2349 142 . 16.486 -8.803 18.938 1.00 18.51 ? ? ? ? ? . 142 TRP A CH2 2349 ATOM 1214 N N A PRO A 2349 143 . 18.105 -15.758 23.889 0.43 25.91 ? ? ? ? ? . 143 PRO A N 2349 ATOM 1215 N N B PRO A 2349 143 . 18.145 -15.709 23.950 0.57 28.56 ? ? ? ? ? . 143 PRO A N 2349 ATOM 1216 C CA A PRO A 2349 143 . 17.728 -16.750 24.895 0.43 26.55 ? ? ? ? ? . 143 PRO A CA 2349 ATOM 1217 C CA B PRO A 2349 143 . 17.683 -16.682 24.925 0.57 30.66 ? ? ? ? ? . 143 PRO A CA 2349 ATOM 1218 C C A PRO A 2349 143 . 18.114 -16.109 26.241 0.43 27.90 ? ? ? ? ? . 143 PRO A C 2349 ATOM 1219 C C B PRO A 2349 143 . 18.148 -16.217 26.307 0.57 33.98 ? ? ? ? ? . 143 PRO A C 2349 ATOM 1220 O O A PRO A 2349 143 . 19.033 -15.280 26.295 0.43 29.57 ? ? ? ? ? . 143 PRO A O 2349 ATOM 1221 O O B PRO A 2349 143 . 17.516 -16.577 27.281 0.57 40.90 ? ? ? ? ? . 143 PRO A O 2349 ATOM 1222 C CB A PRO A 2349 143 . 18.662 -17.907 24.589 0.43 26.47 ? ? ? ? ? . 143 PRO A CB 2349 ATOM 1223 C CB B PRO A 2349 143 . 18.464 -17.930 24.540 0.57 31.72 ? ? ? ? ? . 143 PRO A CB 2349 ATOM 1224 C CG A PRO A 2349 143 . 19.869 -17.262 24.025 0.43 27.23 ? ? ? ? ? . 143 PRO A CG 2349 ATOM 1225 C CG B PRO A 2349 143 . 19.714 -17.418 23.925 0.57 32.06 ? ? ? ? ? . 143 PRO A CG 2349 ATOM 1226 C CD A PRO A 2349 143 . 19.399 -16.061 23.265 0.43 26.55 ? ? ? ? ? . 143 PRO A CD 2349 ATOM 1227 C CD B PRO A 2349 143 . 19.334 -16.157 23.214 0.57 30.24 ? ? ? ? ? . 143 PRO A CD 2349 ATOM 1228 N N A ASN A 2349 144 . 17.447 -16.445 27.332 0.43 29.72 ? ? ? ? ? . 144 ASN A N 2349 ATOM 1229 N N B ASN A 2349 144 . 19.154 -15.333 26.349 0.57 43.48 ? ? ? ? ? . 144 ASN A N 2349 ATOM 1230 C CA A ASN A 2349 144 . 17.845 -15.794 28.584 0.43 31.67 ? ? ? ? ? . 144 ASN A CA 2349 ATOM 1231 C CA B ASN A 2349 144 . 19.879 -14.941 27.567 0.57 41.21 ? ? ? ? ? . 144 ASN A CA 2349 ATOM 1232 C C A ASN A 2349 144 . 19.155 -16.376 29.126 0.43 34.18 ? ? ? ? ? . 144 ASN A C 2349 ATOM 1233 C C B ASN A 2349 144 . 19.928 -16.021 28.652 0.57 46.68 ? ? ? ? ? . 144 ASN A C 2349 ATOM 1234 O O A ASN A 2349 144 . 19.292 -16.688 30.295 0.43 37.95 ? ? ? ? ? . 144 ASN A O 2349 ATOM 1235 O O B ASN A 2349 144 . 20.998 -16.385 29.101 0.57 44.85 ? ? ? ? ? . 144 ASN A O 2349 ATOM 1236 C CB A ASN A 2349 144 . 16.725 -15.785 29.643 0.43 31.33 ? ? ? ? ? . 144 ASN A CB 2349 ATOM 1237 C CB B ASN A 2349 144 . 19.766 -13.486 28.103 0.57 37.67 ? ? ? ? ? . 144 ASN A CB 2349 ATOM 1238 C CG A ASN A 2349 144 . 16.683 -14.482 30.437 0.43 30.34 ? ? ? ? ? . 144 ASN A CG 2349 ATOM 1239 C CG B ASN A 2349 144 . 18.456 -12.779 27.779 0.57 32.86 ? ? ? ? ? . 144 ASN A CG 2349 ATOM 1240 N ND2 A ASN A 2349 144 . 15.880 -14.449 31.481 0.43 29.27 ? ? ? ? ? . 144 ASN A ND2 2349 ATOM 1241 O OD1 A ASN A 2349 144 . 17.350 -13.516 30.096 0.43 30.43 ? ? ? ? ? . 144 ASN A OD1 2349 ATOM 1242 N ND2 B ASN A 2349 144 . 18.201 -12.534 26.509 0.57 28.80 ? ? ? ? ? . 144 ASN A ND2 2349 ATOM 1243 O OD1 B ASN A 2349 144 . 17.731 -12.384 28.685 0.57 29.27 ? ? ? ? ? . 144 ASN A OD1 2349 ATOM 1244 O OXT A ASN A 2349 144 . 20.133 -16.520 28.420 0.43 34.42 ? ? ? ? ? 1- 144 ASN A OXT 2349 ATOM 1245 O OXT B ASN A 2349 144 . 18.927 -16.583 29.037 0.57 53.68 ? ? ? ? ? 1- 144 ASN A OXT 2349 #