NMR Restraints Grid

Result table
 (Save to zip file containing files for each block)

image mrblock_id pdb_id cing stage position program type
24974 2k5x cing 1-original 1 STAR chemical shift


 ##############################
 #  assigned chemical shifts  #
 ##############################



 ###################################
 #  Assigned chemical shift lists  #
 ###################################

###################################################################
#       Chemical Shift Ambiguity Index Value Definitions          #
#                                                                 #
#   Index Value            Definition                             #
#                                                                 #
#      1             Unique (geminal atoms and geminal methyl     #
#                         groups with identical chemical shifts   #
#                         are assumed to be assigned to           #
#                         stereospecific atoms)                   #
#      2             Ambiguity of geminal atoms or geminal methyl #
#                         proton groups                           #
#      3             Aromatic atoms on opposite sides of          #
#                         symmetrical rings (e.g. Tyr HE1 and HE2 #
#                         protons)                                #
#      4             Intraresidue ambiguities (e.g. Lys HG and    #
#                         HD protons or Trp HZ2 and HZ3 protons)  #
#      5             Interresidue ambiguities (Lys 12 vs. Lys 27) #
#      9             Ambiguous, specific ambiguity not defined    #
#                                                                 #
###################################################################

save_assigned_chemical_shifts_one
   _Saveframe_category               assigned_chemical_shifts


   loop_
      _Sample_label

      $sample 

   stop_

   _Sample_conditions_label         $sample_conditions
   _Chem_shift_reference_set_label  $chemical_shift_reference
   _Mol_system_component_name        IM9

   loop_
      _Atom_shift_assign_ID
      _Residue_seq_code
      _Residue_label
      _Atom_name
      _Atom_type
      _Chem_shift_value
      _Chem_shift_value_error
      _Chem_shift_ambiguity_code

        1  1 MET HA   H   4.08 . 1 
        2  1 MET CA   C  53.57 . 1 
        3  1 MET HB2  H   2.19 . 1 
        4  1 MET HB3  H   2.19 . 1 
        5  1 MET CB   C  32.47 . 1 
        6  1 MET HG2  H   2.56 . 1 
        7  1 MET HG3  H   2.56 . 1 
        8  1 MET CG   C  29.09 . 1 
        9  1 MET HE   H   1.47 . 1 
       10  1 MET CE   C  16.64 . 1 
       11  2 GLU HA   H   4.42 . 1 
       12  2 GLU CA   C  54.29 . 1 
       13  2 GLU HB2  H   2.03 . 1 
       14  2 GLU HB3  H   1.96 . 1 
       15  2 GLU CB   C  28.67 . 1 
       16  2 GLU HG2  H   2.34 . 1 
       17  2 GLU HG3  H   2.22 . 1 
       18  3 LEU H    H   8.45 . 1 
       19  3 LEU N    N 125.11 . 1 
       20  3 LEU HA   H   4.45 . 1 
       21  3 LEU CA   C  52.94 . 1 
       22  3 LEU HB2  H   1.6  . 1 
       23  3 LEU HB3  H   0.93 . 1 
       24  3 LEU CB   C  39.7  . 1 
       25  3 LEU HG   H   1.55 . 1 
       26  3 LEU CG   C  24.87 . 1 
       27  3 LEU HD1  H   0.67 . 1 
       28  3 LEU HD2  H   0.58 . 1 
       29  3 LEU CD1  C  23.11 . 1 
       30  3 LEU CD2  C  20.5  . 1 
       31  4 LYS H    H   7.8  . 1 
       32  4 LYS N    N 122.34 . 1 
       33  4 LYS HA   H   4.36 . 1 
       34  4 LYS CA   C  53.6  . 1 
       35  4 LYS HB2  H   1.99 . 1 
       36  4 LYS HB3  H   1.33 . 1 
       37  4 LYS CB   C  31.8  . 1 
       38  4 LYS HG2  H   1.55 . 1 
       39  4 LYS HG3  H   1.55 . 1 
       40  4 LYS CG   C  23.29 . 1 
       41  4 LYS HD2  H   1.24 . 1 
       42  4 LYS HD3  H   0.67 . 1 
       43  4 LYS CD   C  27.32 . 1 
       44  4 LYS HE2  H   2.77 . 1 
       45  4 LYS HE3  H   2.77 . 1 
       46  4 LYS CE   C  40.36 . 1 
       47  5 HIS H    H   8.75 . 1 
       48  5 HIS N    N 116.32 . 1 
       49  5 HIS HA   H   4.71 . 1 
       50  5 HIS CA   C  55.82 . 1 
       51  5 HIS HB2  H   3.38 . 1 
       52  5 HIS HB3  H   3.21 . 1 
       53  5 HIS CB   C  29.17 . 1 
       54  6 SER H    H   7.97 . 1 
       55  6 SER N    N 114.01 . 1 
       56  6 SER HA   H   4.76 . 1 
       57  6 SER CA   C  55.98 . 1 
       58  6 SER HB2  H   3.94 . 1 
       59  6 SER HB3  H   3.71 . 1 
       60  6 SER CB   C  63.89 . 1 
       61  7 ILE H    H   9.37 . 1 
       62  7 ILE N    N 127.2  . 1 
       63  7 ILE HA   H   4.12 . 1 
       64  7 ILE CA   C  64.05 . 1 
       65  7 ILE HB   H   1.69 . 1 
       66  7 ILE CB   C  35.32 . 1 
       67  7 ILE HG12 H   0.91 . 1 
       68  7 ILE HG13 H   0.89 . 1 
       69  7 ILE CG1  C  29.04 . 1 
       70  7 ILE HG2  H   0.54 . 1 
       71  7 ILE CG2  C  13.74 . 1 
       72  7 ILE HD1  H  -0.1  . 1 
       73  7 ILE CD1  C  11.79 . 1 
       74  8 SER H    H   7.55 . 1 
       75  8 SER N    N 113.32 . 1 
       76  8 SER HA   H   4.82 . 1 
       77  8 SER CA   C  57.08 . 1 
       78  8 SER HB2  H   4.03 . 1 
       79  8 SER HB3  H   3.92 . 1 
       80  8 SER CB   C  61.83 . 1 
       81  9 ASP H    H   7.94 . 1 
       82  9 ASP N    N 118.98 . 1 
       83  9 ASP HA   H   4.85 . 1 
       84  9 ASP CA   C  53.27 . 1 
       85  9 ASP HB2  H   2.9  . 1 
       86  9 ASP HB3  H   2.78 . 1 
       87  9 ASP CB   C  41.34 . 1 
       88 10 TYR H    H   8.31 . 1 
       89 10 TYR N    N 120.72 . 1 
       90 10 TYR HA   H   4.95 . 1 
       91 10 TYR CA   C  57.14 . 1 
       92 10 TYR HB2  H   3.57 . 1 
       93 10 TYR HB3  H   3.57 . 1 
       94 10 TYR CB   C  38.71 . 1 
       95 10 TYR HD1  H   7.45 . 1 
       96 10 TYR HD2  H   7.45 . 1 
       97 10 TYR HE1  H   7.03 . 1 
       98 10 TYR HE2  H   7.03 . 1 
       99 11 THR H    H   8.95 . 1 
      100 11 THR N    N 112.74 . 1 
      101 11 THR HA   H   5.06 . 1 
      102 11 THR CA   C  59.36 . 1 
      103 11 THR HB   H   4.75 . 1 
      104 11 THR CB   C  69    . 1 
      105 11 THR HG2  H   1.32 . 1 
      106 11 THR CG2  C  20.38 . 1 
      107 12 GLU H    H   9.34 . 1 
      108 12 GLU N    N 124.88 . 1 
      109 12 GLU HA   H   2.47 . 1 
      110 12 GLU CA   C  58.78 . 1 
      111 12 GLU HB2  H   2.16 . 1 
      112 12 GLU HB3  H   1.98 . 1 
      113 12 GLU CB   C  27.77 . 1 
      114 12 GLU HG2  H   2.06 . 1 
      115 12 GLU HG3  H   1.84 . 1 
      116 12 GLU CG   C  34.38 . 1 
      117 13 ALA H    H   8.41 . 1 
      118 13 ALA N    N 119.43 . 1 
      119 13 ALA HA   H   4.11 . 1 
      120 13 ALA CA   C  53.6  . 1 
      121 13 ALA HB   H   1.47 . 1 
      122 13 ALA CB   C  16.71 . 1 
      123 14 GLU H    H   8.04 . 1 
      124 14 GLU N    N 119.91 . 1 
      125 14 GLU HA   H   4.16 . 1 
      126 14 GLU CA   C  57.3  . 1 
      127 14 GLU HB2  H   2.77 . 1 
      128 14 GLU HB3  H   2.39 . 1 
      129 14 GLU CB   C  29.98 . 1 
      130 14 GLU HG2  H   2.58 . 1 
      131 14 GLU HG3  H   2.43 . 1 
      132 14 GLU CG   C  35.61 . 1 
      133 15 PHE H    H   8.82 . 1 
      134 15 PHE N    N 124.42 . 1 
      135 15 PHE HA   H   3.92 . 1 
      136 15 PHE CA   C  60.84 . 1 
      137 15 PHE HB2  H   2.91 . 1 
      138 15 PHE HB3  H   2.7  . 1 
      139 15 PHE CB   C  39.12 . 1 
      140 15 PHE HD1  H   6.73 . 1 
      141 15 PHE HD2  H   6.73 . 1 
      142 15 PHE HE1  H   6.86 . 1 
      143 15 PHE HE2  H   6.86 . 1 
      144 16 LEU H    H   9.08 . 1 
      145 16 LEU N    N 120.37 . 1 
      146 16 LEU HA   H   3.97 . 1 
      147 16 LEU CA   C  56.73 . 1 
      148 16 LEU HB2  H   2.97 . 1 
      149 16 LEU HB3  H   1.68 . 1 
      150 16 LEU CB   C  39.45 . 1 
      151 16 LEU HG   H   1.52 . 1 
      152 16 LEU CG   C  25.7  . 1 
      153 16 LEU HD1  H   0.98 . 1 
      154 16 LEU HD2  H   0.86 . 1 
      155 16 LEU CD1  C  23.76 . 1 
      156 16 LEU CD2  C  21.98 . 1 
      157 17 GLN H    H   7.97 . 1 
      158 17 GLN N    N 123.05 . 1 
      159 17 GLN HA   H   4.08 . 1 
      160 17 GLN CA   C  57.79 . 1 
      161 17 GLN HB2  H   2.33 . 1 
      162 17 GLN HB3  H   2.33 . 1 
      163 17 GLN CB   C  26.12 . 1 
      164 17 GLN HG2  H   2.5  . 1 
      165 17 GLN HG3  H   2.5  . 1 
      166 17 GLN CG   C  32.06 . 1 
      167 18 LEU H    H   7.57 . 1 
      168 18 LEU N    N 123.96 . 1 
      169 18 LEU HA   H   4.1  . 1 
      170 18 LEU CA   C  57.38 . 1 
      171 18 LEU HB2  H   1.87 . 1 
      172 18 LEU HB3  H   1.61 . 1 
      173 18 LEU CB   C  39.28 . 1 
      174 18 LEU HG   H   1.44 . 1 
      175 18 LEU CG   C  26.17 . 1 
      176 18 LEU HD1  H   0.74 . 1 
      177 18 LEU HD2  H   1.09 . 1 
      178 18 LEU CD1  C  24.31 . 1 
      179 18 LEU CD2  C  23.18 . 1 
      180 19 VAL H    H   8.31 . 1 
      181 19 VAL N    N 118.41 . 1 
      182 19 VAL HA   H   3.2  . 1 
      183 19 VAL CA   C  65.49 . 1 
      184 19 VAL HB   H   1.95 . 1 
      185 19 VAL CB   C  30.56 . 1 
      186 19 VAL HG1  H   0.91 . 1 
      187 19 VAL CG1  C  24.86 . 1 
      188 19 VAL HG2  H   0.76 . 1 
      189 19 VAL CG2  C  23.11 . 1 
      190 20 THR H    H   8.74 . 1 
      191 20 THR N    N 119.21 . 1 
      192 20 THR HA   H   3.91 . 1 
      193 20 THR CA   C  66.02 . 1 
      194 20 THR HB   H   4.17 . 1 
      195 20 THR CB   C  67.34 . 1 
      196 20 THR HG2  H   1.19 . 1 
      197 20 THR CG2  C  19.81 . 1 
      198 21 THR H    H   8.13 . 1 
      199 21 THR N    N 120.02 . 1 
      200 21 THR HA   H   3.94 . 1 
      201 21 THR CA   C  67.01 . 1 
      202 21 THR HB   H   4.55 . 1 
      203 21 THR CB   C  67.58 . 1 
      204 22 ILE H    H   7.77 . 1 
      205 22 ILE N    N 120.72 . 1 
      206 22 ILE HA   H   3.42 . 1 
      207 22 ILE CA   C  64.29 . 1 
      208 22 ILE HB   H   1.81 . 1 
      209 22 ILE CB   C  36.73 . 1 
      210 22 ILE HG12 H   1.85 . 1 
      211 22 ILE CG1  C  27.85 . 1 
      212 22 ILE HG2  H   0.7  . 1 
      213 22 ILE CG2  C  17.12 . 1 
      214 22 ILE HD1  H   0.58 . 1 
      215 22 ILE CD1  C  12.56 . 1 
      216 23 CYS H    H   8.97 . 1 
      217 23 CYS N    N 120.83 . 1 
      218 23 CYS HA   H   3.78 . 1 
      219 23 CYS CA   C  62.81 . 1 
      220 23 CYS HB2  H   3.04 . 1 
      221 23 CYS HB3  H   2.62 . 1 
      222 23 CYS CB   C  25.79 . 1 
      223 24 ASN H    H   7.75 . 1 
      224 24 ASN N    N 113.2  . 1 
      225 24 ASN HA   H   4.72 . 1 
      226 24 ASN CA   C  51.05 . 1 
      227 24 ASN HB2  H   3    . 1 
      228 24 ASN HB3  H   2.72 . 1 
      229 24 ASN CB   C  37.23 . 1 
      230 25 ALA H    H   8.59 . 1 
      231 25 ALA N    N 125.58 . 1 
      232 25 ALA HA   H   4.02 . 1 
      233 25 ALA CA   C  51.08 . 1 
      234 25 ALA HB   H   1.54 . 1 
      235 25 ALA CB   C  14.39 . 1 
      236 26 ASP H    H   8.59 . 1 
      237 26 ASP N    N 120.68 . 1 
      238 26 ASP HA   H   4.94 . 1 
      239 26 ASP CA   C  51.8  . 1 
      240 26 ASP HB2  H   3.07 . 1 
      241 26 ASP HB3  H   2.4  . 1 
      242 26 ASP CB   C  38.38 . 1 
      243 27 THR H    H   9.22 . 1 
      244 27 THR N    N 108.81 . 1 
      245 27 THR HA   H   4.78 . 1 
      246 27 THR CA   C  57.9  . 1 
      247 27 THR HB   H   4.59 . 1 
      248 27 THR CB   C  70.23 . 1 
      249 27 THR HG2  H   0.99 . 1 
      250 27 THR CG2  C  20.92 . 1 
      251 28 SER H    H   9.22 . 1 
      252 28 SER N    N 117.02 . 1 
      253 28 SER HA   H   4.59 . 1 
      254 28 SER CA   C  58.08 . 1 
      255 28 SER HB2  H   4.16 . 1 
      256 28 SER HB3  H   4.07 . 1 
      257 28 SER CB   C  62.17 . 1 
      258 29 SER H    H   7.37 . 1 
      259 29 SER N    N 112.85 . 1 
      260 29 SER HA   H   4.66 . 1 
      261 29 SER CA   C  55.66 . 1 
      262 29 SER HB2  H   4.27 . 1 
      263 29 SER HB3  H   4.11 . 1 
      264 29 SER CB   C  65.03 . 1 
      265 30 GLU H    H   8.86 . 1 
      266 30 GLU N    N 127.31 . 1 
      267 30 GLU CA   C  57.48 . 1 
      268 30 GLU CB   C  29.59 . 1 
      269 31 GLU H    H   8.84 . 1 
      270 31 GLU N    N 119.21 . 1 
      271 31 GLU HA   H   3.93 . 1 
      272 31 GLU CA   C  58.37 . 1 
      273 31 GLU HB2  H   2.11 . 1 
      274 31 GLU HB3  H   2.13 . 1 
      275 31 GLU CB   C  27.52 . 1 
      276 31 GLU HG2  H   2.05 . 1 
      277 31 GLU HG3  H   1.82 . 1 
      278 31 GLU CG   C  34.55 . 1 
      279 32 GLU H    H   7.95 . 1 
      280 32 GLU N    N 119.79 . 1 
      281 32 GLU HA   H   4.04 . 1 
      282 32 GLU CA   C  57.61 . 1 
      283 32 GLU HB2  H   2.21 . 1 
      284 32 GLU HB3  H   2.13 . 1 
      285 32 GLU CB   C  29.03 . 1 
      286 32 GLU HG2  H   2.26 . 1 
      287 32 GLU HG3  H   2.26 . 1 
      288 32 GLU CG   C  34.96 . 1 
      289 33 LEU H    H   7.37 . 1 
      290 33 LEU N    N 121.76 . 1 
      291 33 LEU HA   H   4.26 . 1 
      292 33 LEU CA   C  56.91 . 1 
      293 33 LEU HB2  H   1.87 . 1 
      294 33 LEU HB3  H   1.61 . 1 
      295 33 LEU CB   C  39.05 . 1 
      296 33 LEU HG   H   1.44 . 1 
      297 33 LEU CG   C  26.31 . 1 
      298 33 LEU HD1  H   0.74 . 1 
      299 33 LEU HD2  H   1.22 . 1 
      300 33 LEU CD1  C  24.22 . 1 
      301 33 LEU CD2  C  23.25 . 1 
      302 34 VAL H    H   8.8  . 1 
      303 34 VAL N    N 120.02 . 1 
      304 34 VAL HA   H   3.74 . 1 
      305 34 VAL CA   C  66.46 . 1 
      306 34 VAL HB   H   2.28 . 1 
      307 34 VAL CB   C  30.16 . 1 
      308 34 VAL HG1  H   1.07 . 1 
      309 34 VAL CG1  C  23.82 . 1 
      310 34 VAL HG2  H   1.1  . 1 
      311 34 VAL CG2  C  20.38 . 1 
      312 35 LYS H    H   8.34 . 1 
      313 35 LYS N    N 122.8  . 1 
      314 35 LYS HA   H   4.16 . 1 
      315 35 LYS CA   C  58.67 . 1 
      316 35 LYS HB2  H   2.1  . 1 
      317 35 LYS HB3  H   2.1  . 1 
      318 35 LYS CB   C  30.56 . 1 
      319 35 LYS HG2  H   1.43 . 1 
      320 35 LYS HG3  H   1.71 . 1 
      321 35 LYS CG   C  23.7  . 1 
      322 35 LYS HD2  H   1.78 . 1 
      323 35 LYS HD3  H   1.78 . 1 
      324 35 LYS CD   C  27.79 . 1 
      325 35 LYS HE2  H   2.98 . 1 
      326 35 LYS HE3  H   2.98 . 1 
      327 35 LYS CE   C  40.24 . 1 
      328 36 LEU H    H   8.37 . 1 
      329 36 LEU N    N 118.87 . 1 
      330 36 LEU HA   H   4.25 . 1 
      331 36 LEU CA   C  56.81 . 1 
      332 36 LEU HB2  H   2.19 . 1 
      333 36 LEU HB3  H   1.51 . 1 
      334 36 LEU CB   C  40.44 . 1 
      335 36 LEU HG   H   2.11 . 1 
      336 36 LEU CG   C  25    . 1 
      337 36 LEU HD1  H   0.9  . 1 
      338 36 LEU HD2  H   0.91 . 1 
      339 36 LEU CD1  C  24.45 . 1 
      340 36 LEU CD2  C  21.14 . 1 
      341 37 VAL H    H   8.89 . 1 
      342 37 VAL N    N 122.5  . 1 
      343 37 VAL HA   H   3.48 . 1 
      344 37 VAL CA   C  66.2  . 1 
      345 37 VAL HB   H   2.22 . 1 
      346 37 VAL CB   C  30.32 . 1 
      347 37 VAL HG1  H   0.94 . 1 
      348 37 VAL CG1  C  21.39 . 1 
      349 37 VAL HG2  H   0.87 . 1 
      350 37 VAL CG2  C  20.26 . 1 
      351 38 THR H    H   8.82 . 1 
      352 38 THR N    N 118.87 . 1 
      353 38 THR HA   H   4.11 . 1 
      354 38 THR CA   C  66.68 . 1 
      355 38 THR HB   H   4.27 . 1 
      356 38 THR CB   C  67.26 . 1 
      357 39 HIS H    H   8.42 . 1 
      358 39 HIS N    N 122.34 . 1 
      359 39 HIS HA   H   4.58 . 1 
      360 39 HIS CA   C  58.62 . 1 
      361 39 HIS HB2  H   3.73 . 1 
      362 39 HIS HB3  H   3.33 . 1 
      363 39 HIS CB   C  27.14 . 1 
      364 40 PHE H    H   9.07 . 1 
      365 40 PHE N    N 120.83 . 1 
      366 40 PHE HA   H   3.85 . 1 
      367 40 PHE CA   C  61.34 . 1 
      368 40 PHE HB2  H   3.82 . 1 
      369 40 PHE HB3  H   2.8  . 1 
      370 40 PHE CB   C  37.08 . 1 
      371 40 PHE HD1  H   6.88 . 1 
      372 40 PHE HD2  H   6.88 . 1 
      373 40 PHE HE1  H   7.12 . 1 
      374 40 PHE HE2  H   7.12 . 1 
      375 41 GLU H    H   8.85 . 1 
      376 41 GLU N    N 122.57 . 1 
      377 41 GLU HA   H   3.65 . 1 
      378 41 GLU CA   C  59.36 . 1 
      379 41 GLU HB2  H   2.72 . 1 
      380 41 GLU HB3  H   2.21 . 1 
      381 41 GLU CB   C  28.67 . 1 
      382 41 GLU HG2  H   3.03 . 1 
      383 41 GLU HG3  H   1.94 . 1 
      384 41 GLU CG   C  35.85 . 1 
      385 42 GLU H    H   8.45 . 1 
      386 42 GLU N    N 121.18 . 1 
      387 42 GLU HA   H   4.02 . 1 
      388 42 GLU CA   C  57.22 . 1 
      389 42 GLU HB2  H   2.28 . 1 
      390 42 GLU HB3  H   2.1  . 1 
      391 42 GLU CB   C  28.34 . 1 
      392 42 GLU HG2  H   2.86 . 1 
      393 42 GLU HG3  H   2.63 . 1 
      394 42 GLU CG   C  34.84 . 1 
      395 43 MET H    H   8.77 . 1 
      396 43 MET N    N 115.17 . 1 
      397 43 MET HA   H   4.52 . 1 
      398 43 MET CA   C  54.18 . 1 
      399 43 MET CB   C  34.68 . 1 
      400 43 MET CG   C  31.64 . 1 
      401 44 THR H    H   7.96 . 1 
      402 44 THR N    N 106.38 . 1 
      403 44 THR HA   H   3.55 . 1 
      404 44 THR CA   C  64.05 . 1 
      405 44 THR HB   H   3.72 . 1 
      406 44 THR CB   C  68.33 . 1 
      407 44 THR HG2  H   0.75 . 1 
      408 44 THR CG2  C  17.82 . 1 
      409 45 GLU H    H   7.45 . 1 
      410 45 GLU N    N 111.93 . 1 
      411 45 GLU HA   H   3.89 . 1 
      412 45 GLU CA   C  56.07 . 1 
      413 45 GLU HB2  H   2.53 . 1 
      414 45 GLU HB3  H   2.42 . 1 
      415 45 GLU CB   C  27.52 . 1 
      416 45 GLU HG2  H   2.22 . 1 
      417 45 GLU HG3  H   2.14 . 1 
      418 45 GLU CG   C  36.27 . 1 
      419 46 HIS H    H   7.4  . 1 
      420 46 HIS N    N 120.49 . 1 
      421 46 HIS HA   H   3.05 . 1 
      422 46 HIS CA   C  53.99 . 1 
      423 46 HIS HB2  H   2.7  . 1 
      424 46 HIS HB3  H   2.07 . 1 
      425 46 HIS CB   C  30.11 . 1 
      426 47 PRO HA   H   4.28 . 1 
      427 47 PRO CA   C  63.47 . 1 
      428 47 PRO HB2  H   2.34 . 1 
      429 47 PRO HB3  H   1.96 . 1 
      430 47 PRO CB   C  30.56 . 1 
      431 47 PRO HG2  H   1.93 . 1 
      432 47 PRO HG3  H   1.75 . 1 
      433 47 PRO CG   C  25.3  . 1 
      434 47 PRO HD2  H   3.06 . 1 
      435 47 PRO HD3  H   1.47 . 1 
      436 47 PRO CD   C  48.97 . 1 
      437 48 SER H    H  11.17 . 1 
      438 48 SER N    N 119.21 . 1 
      439 48 SER HA   H   4.54 . 1 
      440 48 SER CA   C  58.97 . 1 
      441 48 SER HB2  H   3.96 . 1 
      442 48 SER HB3  H   3.87 . 1 
      443 48 SER CB   C  61.83 . 1 
      444 49 GLY H    H   8.07 . 1 
      445 49 GLY N    N 106.84 . 1 
      446 49 GLY HA2  H   4.05 . 1 
      447 49 GLY HA3  H   3.86 . 1 
      448 49 GLY CA   C  45.69 . 1 
      449 50 SER H    H  10.07 . 1 
      450 50 SER N    N 122.8  . 1 
      451 50 SER HA   H   4.25 . 1 
      452 50 SER CA   C  61.25 . 1 
      453 50 SER HB2  H   4.06 . 1 
      454 50 SER HB3  H   4.43 . 1 
      455 50 SER CB   C  61.66 . 1 
      456 51 ASP H    H   8.83 . 1 
      457 51 ASP N    N 126.39 . 1 
      458 51 ASP HA   H   4.63 . 1 
      459 51 ASP CA   C  56.07 . 1 
      460 51 ASP HB2  H   3.28 . 1 
      461 51 ASP HB3  H   2.96 . 1 
      462 51 ASP CB   C  37.23 . 1 
      463 52 LEU H    H   7.59 . 1 
      464 52 LEU N    N 115.98 . 1 
      465 52 LEU HA   H   3.86 . 1 
      466 52 LEU CA   C  55.89 . 1 
      467 52 LEU HB2  H   1.67 . 1 
      468 52 LEU HB3  H   1.33 . 1 
      469 52 LEU CB   C  42    . 1 
      470 52 LEU HG   H   1.49 . 1 
      471 52 LEU CG   C  24.92 . 1 
      472 52 LEU HD1  H   0.4  . 1 
      473 52 LEU HD2  H   0.44 . 1 
      474 52 LEU CD1  C  23.41 . 1 
      475 52 LEU CD2  C  20.92 . 1 
      476 53 ILE H    H   6.71 . 1 
      477 53 ILE N    N 111    . 1 
      478 53 ILE HA   H   3.48 . 1 
      479 53 ILE CA   C  60.35 . 1 
      480 53 ILE HB   H   1.1  . 1 
      481 53 ILE CB   C  37.97 . 1 
      482 53 ILE HG12 H   0.83 . 1 
      483 53 ILE HG13 H   0.19 . 1 
      484 53 ILE CG1  C  26.49 . 1 
      485 53 ILE HG2  H  -0.28 . 1 
      486 53 ILE CG2  C  14.57 . 1 
      487 53 ILE HD1  H  -0.25 . 1 
      488 53 ILE CD1  C  11.49 . 1 
      489 54 TYR H    H   7.36 . 1 
      490 54 TYR N    N 115.98 . 1 
      491 54 TYR HA   H   4.36 . 1 
      492 54 TYR CA   C  59.44 . 1 
      493 54 TYR HB2  H   2.7  . 1 
      494 54 TYR HB3  H   2.73 . 1 
      495 54 TYR CB   C  40.6  . 1 
      496 54 TYR HD1  H   6.64 . 1 
      497 54 TYR HD2  H   6.8  . 1 
      498 54 TYR HE1  H   5.32 . 1 
      499 54 TYR HE2  H   6.2  . 1 
      500 54 TYR CD1  C 130.46 . 1 
      501 54 TYR CD2  C 131.93 . 1 
      502 54 TYR CE1  C 115.36 . 1 
      503 54 TYR CE2  C 116.2  . 1 
      504 55 TYR H    H   8.7  . 1 
      505 55 TYR N    N 116.32 . 1 
      506 55 TYR HA   H   4.84 . 1 
      507 55 TYR CA   C  54.91 . 1 
      508 55 TYR HB2  H   3.21 . 1 
      509 55 TYR HB3  H   2.49 . 1 
      510 55 TYR CB   C  38.01 . 1 
      511 55 TYR HD1  H   6.58 . 1 
      512 55 TYR HD2  H   7.23 . 1 
      513 56 PRO HA   H   4.41 . 1 
      514 56 PRO CA   C  61.04 . 1 
      515 56 PRO HB2  H   2.25 . 1 
      516 56 PRO HB3  H   2.04 . 1 
      517 56 PRO CB   C  30.98 . 1 
      518 56 PRO HG2  H   2.14 . 1 
      519 56 PRO HG3  H   1.88 . 1 
      520 56 PRO CG   C  25.24 . 1 
      521 56 PRO HD2  H   3.51 . 1 
      522 56 PRO HD3  H   3.02 . 1 
      523 56 PRO CD   C  48.83 . 1 
      524 57 LYS H    H   8.68 . 1 
      525 57 LYS N    N 122.57 . 1 
      526 57 LYS HA   H   4.37 . 1 
      527 57 LYS CA   C  53.69 . 1 
      528 57 LYS HB2  H   1.88 . 1 
      529 57 LYS HB3  H   1.88 . 1 
      530 57 LYS CB   C  31.14 . 1 
      531 57 LYS HG2  H   1.62 . 1 
      532 57 LYS HG3  H   1.62 . 1 
      533 57 LYS CG   C  23.11 . 1 
      534 57 LYS HD2  H   1.82 . 1 
      535 57 LYS HD3  H   1.82 . 1 
      536 57 LYS CD   C  27.2  . 1 
      537 57 LYS HE2  H   3.14 . 1 
      538 57 LYS HE3  H   3.14 . 1 
      539 57 LYS CE   C  40.29 . 1 
      540 58 GLU H    H   8.65 . 1 
      541 58 GLU N    N 123.49 . 1 
      542 58 GLU HA   H   4.09 . 1 
      543 58 GLU CA   C  57.3  . 1 
      544 58 GLU HB2  H   2.12 . 1 
      545 58 GLU HB3  H   2.02 . 1 
      546 58 GLU CB   C  27.6  . 1 
      547 58 GLU HG2  H   2.36 . 1 
      548 58 GLU HG3  H   2.36 . 1 
      549 58 GLU CG   C  34.49 . 1 
      550 59 GLY H    H   8.93 . 1 
      551 59 GLY N    N 115.4  . 1 
      552 59 GLY HA2  H   4.32 . 1 
      553 59 GLY HA3  H   3.75 . 1 
      554 59 GLY CA   C  43.64 . 1 
      555 60 ASP H    H   8.14 . 1 
      556 60 ASP N    N 122.57 . 1 
      557 60 ASP HA   H   4.77 . 1 
      558 60 ASP CA   C  52.69 . 1 
      559 60 ASP HB2  H   2.95 . 1 
      560 60 ASP HB3  H   2.69 . 1 
      561 60 ASP CB   C  38.96 . 1 
      562 61 ASP H    H   8.56 . 1 
      563 61 ASP N    N 121.76 . 1 
      564 61 ASP HA   H   4.61 . 1 
      565 61 ASP CA   C  51.79 . 1 
      566 61 ASP HB2  H   2.96 . 1 
      567 61 ASP HB3  H   2.74 . 1 
      568 61 ASP CB   C  39.53 . 1 
      569 62 ASP H    H   8.35 . 1 
      570 62 ASP N    N 125.81 . 1 
      571 62 ASP HA   H   4.45 . 1 
      572 62 ASP CA   C  51.3  . 1 
      573 62 ASP HB2  H   2.87 . 1 
      574 62 ASP HB3  H   2.3  . 1 
      575 62 ASP CB   C 138.16 . 1 
      576 63 SER H    H   8.21 . 1 
      577 63 SER N    N 116.32 . 1 
      578 63 SER HA   H   4.67 . 1 
      579 63 SER CA   C  55.94 . 1 
      580 63 SER HB2  H   4.2  . 1 
      581 63 SER HB3  H   4.15 . 1 
      582 63 SER CB   C  61.2  . 1 
      583 64 PRO HA   H   4.08 . 1 
      584 64 PRO CA   C  65.12 . 1 
      585 64 PRO HB2  H   2.1  . 1 
      586 64 PRO HB3  H   1.95 . 1 
      587 64 PRO CB   C  30.73 . 1 
      588 64 PRO CG   C  25.09 . 1 
      589 64 PRO HD2  H   3.86 . 1 
      590 64 PRO CD   C  48.93 . 1 
      591 65 SER H    H   8.3  . 1 
      592 65 SER N    N 110.07 . 1 
      593 65 SER HA   H   4.05 . 1 
      594 65 SER CA   C  60.15 . 1 
      595 65 SER HB2  H   3.93 . 1 
      596 65 SER HB3  H   3.86 . 1 
      597 65 SER CB   C  60.74 . 1 
      598 66 GLY H    H   8.02 . 1 
      599 66 GLY N    N 115.17 . 1 
      600 66 GLY HA2  H   3.77 . 1 
      601 66 GLY HA3  H   3.87 . 1 
      602 66 GLY CA   C  45.37 . 1 
      603 67 ILE H    H   8.81 . 1 
      604 67 ILE N    N 125.58 . 1 
      605 67 ILE HA   H   3.88 . 1 
      606 67 ILE CA   C  63.97 . 1 
      607 67 ILE HB   H   1.85 . 1 
      608 67 ILE CB   C  36.98 . 1 
      609 67 ILE HG12 H   1.77 . 1 
      610 67 ILE HG13 H   0.86 . 1 
      611 67 ILE CG1  C  27.2  . 1 
      612 67 ILE HG2  H   0.86 . 1 
      613 67 ILE CG2  C  16.49 . 1 
      614 67 ILE HD1  H   0.43 . 1 
      615 67 ILE CD1  C  14.34 . 1 
      616 68 VAL H    H   8.32 . 1 
      617 68 VAL N    N 119.68 . 1 
      618 68 VAL HA   H   3.64 . 1 
      619 68 VAL CA   C  67.09 . 1 
      620 68 VAL HB   H   2.39 . 1 
      621 68 VAL CB   C  29.74 . 1 
      622 68 VAL HG1  H   1.3  . 1 
      623 68 VAL CG1  C  23.64 . 1 
      624 68 VAL HG2  H   1.25 . 1 
      625 68 VAL CG2  C  20.8  . 1 
      626 69 ASN H    H   8.42 . 1 
      627 69 ASN N    N 119.1  . 1 
      628 69 ASN HA   H   4.62 . 1 
      629 69 ASN CA   C  55.57 . 1 
      630 69 ASN HB2  H   3.09 . 1 
      631 69 ASN HB3  H   3.05 . 1 
      632 69 ASN CB   C  36.82 . 1 
      633 70 THR H    H   8.8  . 1 
      634 70 THR N    N 120.6  . 1 
      635 70 THR HA   H   4.18 . 1 
      636 70 THR CA   C  65.75 . 1 
      637 70 THR HB   H   4.39 . 1 
      638 70 THR CB   C  67.09 . 1 
      639 70 THR HG2  H   1.4  . 1 
      640 70 THR CG2  C  16.11 . 1 
      641 71 VAL H    H   8.67 . 1 
      642 71 VAL N    N 122.45 . 1 
      643 71 VAL HA   H   3.59 . 1 
      644 71 VAL CA   C  66.97 . 1 
      645 71 VAL HB   H   2.54 . 1 
      646 71 VAL CB   C  30.4  . 1 
      647 71 VAL HG1  H   1.16 . 1 
      648 71 VAL CG1  C  21.98 . 1 
      649 71 VAL HG2  H   0.81 . 1 
      650 71 VAL CG2  C  19.2  . 1 
      651 72 LYS H    H   9.2  . 1 
      652 72 LYS N    N 121.18 . 1 
      653 72 LYS HA   H   3.95 . 1 
      654 72 LYS CA   C  58.37 . 1 
      655 72 LYS HB2  H   2.21 . 1 
      656 72 LYS CB   C  32.04 . 1 
      657 72 LYS HG2  H   1.82 . 1 
      658 72 LYS HG3  H   1.66 . 1 
      659 72 LYS CG   C  23.6  . 1 
      660 72 LYS HD2  H   1.95 . 1 
      661 72 LYS HD3  H   1.95 . 1 
      662 72 LYS CD   C  28.57 . 1 
      663 72 LYS HE2  H   3.17 . 1 
      664 72 LYS HE3  H   3.17 . 1 
      665 72 LYS CE   C  40.16 . 1 
      666 73 GLN H    H   8.7  . 1 
      667 73 GLN N    N 118.52 . 1 
      668 73 GLN HA   H   4.23 . 1 
      669 73 GLN CA   C  57.3  . 1 
      670 73 GLN HB2  H   2.35 . 1 
      671 73 GLN HB3  H   2.35 . 1 
      672 73 GLN CB   C  26.67 . 1 
      673 73 GLN HG2  H   2.75 . 1 
      674 73 GLN HG3  H   2.59 . 1 
      675 73 GLN CG   C  32.36 . 1 
      676 74 TRP H    H   8.64 . 1 
      677 74 TRP N    N 122.45 . 1 
      678 74 TRP HA   H   4.32 . 1 
      679 74 TRP CA   C  61.12 . 1 
      680 74 TRP HB2  H   3.66 . 1 
      681 74 TRP HB3  H   3.49 . 1 
      682 74 TRP CB   C  27.44 . 1 
      683 75 ARG H    H   9.1  . 1 
      684 75 ARG N    N 119.45 . 1 
      685 75 ARG HA   H   3.33 . 1 
      686 75 ARG CA   C  59.38 . 1 
      687 75 ARG HB2  H   2.36 . 1 
      688 75 ARG HB3  H   2.82 . 1 
      689 75 ARG CB   C  27.44 . 1 
      690 75 ARG CG   C  34.35 . 1 
      691 76 ALA H    H   7.72 . 1 
      692 76 ALA N    N 120.72 . 1 
      693 76 ALA HA   H   4.21 . 1 
      694 76 ALA CA   C  53.43 . 1 
      695 76 ALA HB   H   1.54 . 1 
      696 76 ALA CB   C  16.35 . 1 
      697 77 ALA H    H   8.09 . 1 
      698 77 ALA N    N 120.83 . 1 
      699 77 ALA HA   H   4.18 . 1 
      700 77 ALA CA   C  52.39 . 1 
      701 77 ALA HB   H   1.46 . 1 
      702 77 ALA CB   C  16.71 . 1 
      703 78 ASN H    H   7.12 . 1 
      704 78 ASN N    N 114.01 . 1 
      705 78 ASN HA   H   4.56 . 1 
      706 78 ASN CA   C  51.6  . 1 
      707 78 ASN HB2  H   2.38 . 1 
      708 78 ASN HB3  H   1.39 . 1 
      709 78 ASN CB   C  37.39 . 1 
      710 79 GLY H    H   7.65 . 1 
      711 79 GLY N    N 108.69 . 1 
      712 79 GLY HA2  H   3.9  . 1 
      713 79 GLY HA3  H   3.9  . 1 
      714 79 GLY CA   C  45.37 . 1 
      715 80 LYS H    H   8.11 . 1 
      716 80 LYS N    N 118.52 . 1 
      717 80 LYS HA   H   4.59 . 1 
      718 80 LYS CA   C  52.76 . 1 
      719 80 LYS HB2  H   2.18 . 1 
      720 80 LYS HB3  H   2.03 . 1 
      721 80 LYS CB   C  32.29 . 1 
      722 80 LYS HG2  H   1.34 . 1 
      723 80 LYS HG3  H   1.17 . 1 
      724 80 LYS CG   C  23.58 . 1 
      725 80 LYS HD2  H   1.7  . 1 
      726 80 LYS HD3  H   1.46 . 1 
      727 80 LYS CD   C  27.55 . 1 
      728 80 LYS HE2  H   3.22 . 1 
      729 80 LYS HE3  H   3.22 . 1 
      730 80 LYS CE   C  40.59 . 1 
      731 81 SER H    H   8.7  . 1 
      732 81 SER N    N 118.29 . 1 
      733 81 SER HA   H   4.15 . 1 
      734 81 SER CA   C  57.45 . 1 
      735 81 SER HB2  H   3.99 . 1 
      736 81 SER HB3  H   4.01 . 1 
      737 81 SER CB   C  62.41 . 1 
      738 82 GLY H    H   8.37 . 1 
      739 82 GLY N    N 109.62 . 1 
      740 82 GLY HA2  H   4.26 . 1 
      741 82 GLY HA3  H   3.61 . 1 
      742 82 GLY CA   C  41.13 . 1 
      743 83 PHE H    H   7.83 . 1 
      744 83 PHE N    N 116.44 . 1 
      745 83 PHE HA   H   4.73 . 1 
      746 83 PHE CA   C  57.07 . 1 
      747 83 PHE HB2  H   3.72 . 1 
      748 83 PHE HB3  H  12.72 . 1 
      749 83 PHE CB   C  38.29 . 1 
      750 83 PHE HD1  H   7.47 . 1 
      751 83 PHE HD2  H   7.47 . 1 
      752 83 PHE HE1  H   6.66 . 1 
      753 83 PHE HE2  H   6.66 . 1 
      754 84 LYS H    H   8.65 . 1 
      755 84 LYS N    N 124.19 . 1 
      756 84 LYS HA   H   4.25 . 1 
      757 84 LYS CA   C  55.53 . 1 
      758 84 LYS HB2  H   1.99 . 1 
      759 84 LYS HB3  H   1.53 . 1 
      760 84 LYS CB   C  31.13 . 1 
      761 84 LYS HG2  H   1.53 . 1 
      762 84 LYS HG3  H   1.5  . 1 
      763 84 LYS CG   C  22.87 . 1 
      764 84 LYS HD2  H   1.76 . 1 
      765 84 LYS HD3  H   1.76 . 1 
      766 84 LYS CD   C  28.15 . 1 
      767 84 LYS HE2  H   3.04 . 1 
      768 84 LYS HE3  H   3.04 . 1 
      769 84 LYS CE   C  40.42 . 1 
      770 85 GLN H    H   8.78 . 1 
      771 85 GLN N    N 126.04 . 1 
      772 85 GLN HA   H   4.37 . 1 
      773 85 GLN CA   C  54.83 . 1 
      774 85 GLN HB2  H   2.25 . 1 
      775 85 GLN HB3  H   2.14 . 1 
      776 85 GLN CB   C  28.38 . 1 
      777 85 GLN HG2  H   2.56 . 1 
      778 85 GLN HG3  H   2.56 . 1 
      779 85 GLN CG   C  32.36 . 1 
      780 86 GLY H    H   8.14 . 1 
      781 86 GLY N    N 117.25 . 1 
      782 86 GLY HA2  H   3.89 . 1 
      783 86 GLY HA3  H   3.89 . 1 
      784 86 GLY CA   C  44.45 . 1 

   stop_

save_
 ##############################
 #  assigned chemical shifts  #
 ##############################



 ###################################
 #  Assigned chemical shift lists  #
 ###################################

###################################################################
#       Chemical Shift Ambiguity Index Value Definitions          #
#                                                                 #
#   Index Value            Definition                             #
#                                                                 #
#      1             Unique (geminal atoms and geminal methyl     #
#                         groups with identical chemical shifts   #
#                         are assumed to be assigned to           #
#                         stereospecific atoms)                   #
#      2             Ambiguity of geminal atoms or geminal methyl #
#                         proton groups                           #
#      3             Aromatic atoms on opposite sides of          #
#                         symmetrical rings (e.g. Tyr HE1 and HE2 #
#                         protons)                                #
#      4             Intraresidue ambiguities (e.g. Lys HG and    #
#                         HD protons or Trp HZ2 and HZ3 protons)  #
#      5             Interresidue ambiguities (Lys 12 vs. Lys 27) #
#      9             Ambiguous, specific ambiguity not defined    #
#                                                                 #
###################################################################

save_assigned_chemical_shifts_for_major_conformer_of_E9_DNase
   _Saveframe_category               assigned_chemical_shifts

   _Details                         
;
Assignments refer to the major conformational species
of E9 DNase when bound to its inhibitor, Im9.
;

   loop_
      _Sample_label

      $sample_one 

   stop_

   _Sample_conditions_label         $sample_conditions_one
   _Chem_shift_reference_set_label  $chemical_shift_reference_set_one
   _Mol_system_component_name       'E9 DNase'

   loop_
      _Atom_shift_assign_ID
      _Residue_seq_code
      _Residue_label
      _Atom_name
      _Atom_type
      _Chem_shift_value
      _Chem_shift_value_error
      _Chem_shift_ambiguity_code

        1   2 GLU HA   H   4.37 . 1 
        2   2 GLU HB2  H   1.97 . 1 
        3   2 GLU C    C 175.96 . 1 
        4   2 GLU CA   C  55.06 . 1 
        5   2 GLU CB   C  29.36 . 1 
        6   3 SER H    H   8.65 . 1 
        7   3 SER HA   H   4.41 . 1 
        8   3 SER HB2  H   3.86 . 1 
        9   3 SER C    C 175.50 . 1 
       10   3 SER CA   C  56.95 . 1 
       11   3 SER CB   C  62.24 . 1 
       12   3 SER N    N 118.5  . 1 
       13   4 LYS H    H   8.66 . 1 
       14   4 LYS HA   H   4.13 . 1 
       15   4 LYS HB2  H   1.81 . 1 
       16   4 LYS HB3  H   1.68 . 1 
       17   4 LYS C    C 177.17 . 1 
       18   4 LYS CA   C  56.70 . 1 
       19   4 LYS CB   C  31.73 . 1 
       20   4 LYS N    N 124.1  . 1 
       21   5 ARG H    H   8.20 . 1 
       22   5 ARG HA   H   4.06 . 1 
       23   5 ARG HB2  H   1.72 . 1 
       24   5 ARG C    C 175.31 . 1 
       25   5 ARG CA   C  56.05 . 1 
       26   5 ARG CB   C  29.74 . 1 
       27   5 ARG N    N 118.8  . 1 
       28   6 ASN H    H   8.03 . 1 
       29   6 ASN HA   H   4.93 . 1 
       30   6 ASN HB2  H   3.06 . 1 
       31   6 ASN HB3  H   2.77 . 1 
       32   6 ASN HD21 H   7.01 . 1 
       33   6 ASN HD22 H   7.69 . 1 
       34   6 ASN C    C 173.65 . 1 
       35   6 ASN CA   C  51.24 . 1 
       36   6 ASN CB   C  37.90 . 1 
       37   6 ASN CG   C 176.98 . 1 
       38   6 ASN N    N 117.8  . 1 
       39   6 ASN ND2  N 113.4  . 1 
       40   7 LYS H    H   7.71 . 1 
       41   7 LYS CA   C  52.16 . 1 
       42   7 LYS N    N 121.4  . 1 
       43   8 PRO HA   H   4.93 . 1 
       44   8 PRO HB2  H   2.35 . 1 
       45   8 PRO HB3  H   1.87 . 1 
       46   8 PRO C    C 176.77 . 1 
       47   8 PRO CA   C  61.48 . 1 
       48   8 PRO CB   C  32.46 . 1 
       49   9 GLY H    H   8.30 . 1 
       50   9 GLY HA2  H   4.13 . 1 
       51   9 GLY HA3  H   3.79 . 1 
       52   9 GLY C    C 170.52 . 1 
       53   9 GLY CA   C  44.28 . 1 
       54   9 GLY N    N 109.0  . 1 
       55  10 LYS H    H   8.11 . 1 
       56  10 LYS HA   H   5.07 . 1 
       57  10 LYS HB2  H   1.49 . 1 
       58  10 LYS C    C 175.62 . 1 
       59  10 LYS CA   C  52.75 . 1 
       60  10 LYS CB   C  34.07 . 1 
       61  10 LYS N    N 119.4  . 1 
       62  11 ALA H    H   8.31 . 1 
       63  11 ALA HA   H   5.09 . 1 
       64  11 ALA HB   H   1.75 . 1 
       65  11 ALA C    C 177.73 . 1 
       66  11 ALA CA   C  50.92 . 1 
       67  11 ALA CB   C  17.81 . 1 
       68  11 ALA N    N 125.6  . 1 
       69  12 THR H    H   8.41 . 1 
       70  12 THR HA   H   4.69 . 1 
       71  12 THR HB   H   4.30 . 1 
       72  12 THR C    C 172.54 . 1 
       73  12 THR CA   C  58.61 . 1 
       74  12 THR CB   C  70.86 . 1 
       75  12 THR N    N 114.9  . 1 
       76  13 GLY H    H   8.62 . 1 
       77  13 GLY HA2  H   4.47 . 1 
       78  13 GLY HA3  H   3.84 . 1 
       79  13 GLY C    C 173.30 . 1 
       80  13 GLY CA   C  43.11 . 1 
       81  13 GLY N    N 108.6  . 1 
       82  14 LYS H    H   9.32 . 1 
       83  14 LYS HA   H   4.10 . 1 
       84  14 LYS HB2  H   1.89 . 1 
       85  14 LYS C    C 178.63 . 1 
       86  14 LYS CA   C  56.40 . 1 
       87  14 LYS CB   C  33.95 . 1 
       88  14 LYS N    N 119.6  . 1 
       89  15 GLY H    H   9.05 . 1 
       90  15 GLY HA2  H   3.84 . 1 
       91  15 GLY HA3  H   3.61 . 1 
       92  15 GLY C    C 173.54 . 1 
       93  15 GLY CA   C  43.54 . 1 
       94  15 GLY N    N 106.7  . 1 
       95  16 LYS H    H   8.14 . 1 
       96  16 LYS CA   C  51.37 . 1 
       97  16 LYS N    N 117.3  . 1 
       98  17 PRO HA   H   4.66 . 1 
       99  17 PRO HB2  H   2.25 . 2 
      100  17 PRO C    C 176.92 . 1 
      101  17 PRO CA   C  61.47 . 1 
      102  17 PRO CB   C  30.06 . 1 
      103  18 VAL H    H   8.59 . 1 
      104  18 VAL HA   H   4.70 . 1 
      105  18 VAL HB   H   2.46 . 1 
      106  18 VAL C    C 175.71 . 1 
      107  18 VAL CA   C  57.94 . 1 
      108  18 VAL N    N 118.2  . 1 
      109  19 GLY H    H   8.40 . 1 
      110  19 GLY HA2  H   4.52 . 1 
      111  19 GLY HA3  H   3.85 . 1 
      112  19 GLY C    C 174.21 . 1 
      113  19 GLY CA   C  42.32 . 1 
      114  19 GLY N    N 108.9  . 1 
      115  20 ASP H    H   8.32 . 1 
      116  20 ASP HA   H   4.46 . 1 
      117  20 ASP HB2  H   2.89 . 1 
      118  20 ASP HB3  H   2.77 . 1 
      119  20 ASP C    C 178.03 . 1 
      120  20 ASP CA   C  54.98 . 1 
      121  20 ASP CB   C  40.19 . 1 
      122  20 ASP N    N 116.0  . 1 
      123  21 LYS H    H   8.43 . 1 
      124  21 LYS HA   H   4.64 . 1 
      125  21 LYS HB2  H   1.66 . 1 
      126  21 LYS HB3  H   1.66 . 1 
      127  21 LYS C    C 178.38 . 1 
      128  21 LYS CA   C  54.61 . 1 
      129  21 LYS CB   C  29.69 . 1 
      130  21 LYS N    N 121.6  . 1 
      131  22 TRP H    H   7.71 . 1 
      132  22 TRP HA   H   4.35 . 1 
      133  22 TRP C    C 176.87 . 1 
      134  22 TRP CA   C  59.14 . 1 
      135  22 TRP N    N 121.8  . 1 
      136  23 LEU H    H   7.55 . 1 
      137  23 LEU HA   H   3.34 . 1 
      138  23 LEU C    C 180.50 . 1 
      139  23 LEU CA   C  55.25 . 1 
      140  23 LEU CB   C  37.88 . 1 
      141  23 LEU N    N 119.1  . 1 
      142  24 ASP H    H   8.29 . 1 
      143  24 ASP HA   H   4.29 . 1 
      144  24 ASP HB2  H   2.91 . 1 
      145  24 ASP HB3  H   2.63 . 1 
      146  24 ASP CA   C  56.16 . 1 
      147  24 ASP CB   C  38.75 . 1 
      148  24 ASP N    N 123.4  . 1 
      149  25 ASP H    H   7.56 . 1 
      150  25 ASP HA   H   4.37 . 1 
      151  25 ASP C    C 177.22 . 1 
      152  25 ASP CA   C  55.01 . 1 
      153  25 ASP CB   C  38.64 . 1 
      154  25 ASP N    N 119.8  . 1 
      155  26 ALA H    H   7.53 . 1 
      156  26 ALA HA   H   4.60 . 1 
      157  26 ALA HB   H   1.48 . 1 
      158  26 ALA C    C 176.97 . 1 
      159  26 ALA CA   C  52.73 . 1 
      160  26 ALA N    N 120.0  . 1 
      161  27 GLY H    H   7.38 . 1 
      162  27 GLY HA2  H   4.51 . 1 
      163  27 GLY HA3  H   3.62 . 1 
      164  27 GLY C    C 173.14 . 1 
      165  27 GLY CA   C  43.14 . 1 
      166  27 GLY N    N 101.9  . 1 
      167  28 LYS H    H   7.60 . 1 
      168  28 LYS HA   H   4.62 . 1 
      169  28 LYS HB2  H   1.76 . 1 
      170  28 LYS HB3  H   1.76 . 1 
      171  28 LYS C    C 173.66 . 1 
      172  28 LYS CA   C  53.15 . 1 
      173  28 LYS CB   C  35.24 . 1 
      174  28 LYS N    N 119.8  . 1 
      175  29 ASP H    H   8.91 . 1 
      176  29 ASP HA   H   4.16 . 1 
      177  29 ASP HB2  H   2.85 . 1 
      178  29 ASP HB3  H   2.85 . 1 
      179  29 ASP C    C 176.12 . 1 
      180  29 ASP CA   C  55.13 . 1 
      181  29 ASP CB   C  38.98 . 1 
      182  29 ASP N    N 119.3  . 1 
      183  30 SER H    H   8.30 . 1 
      184  30 SER HA   H   4.53 . 1 
      185  30 SER HB2  H   3.91 . 1 
      186  30 SER C    C 174.06 . 1 
      187  30 SER CA   C  56.80 . 1 
      188  30 SER CB   C  62.33 . 1 
      189  30 SER N    N 117.6  . 1 
      190  31 GLY H    H   8.39 . 1 
      191  31 GLY HA2  H   4.33 . 1 
      192  31 GLY HA3  H   4.33 . 1 
      193  31 GLY C    C 173.85 . 1 
      194  31 GLY CA   C  43.00 . 1 
      195  31 GLY N    N 108.3  . 1 
      196  32 ALA H    H   9.36 . 1 
      197  32 ALA CA   C  47.63 . 1 
      198  32 ALA N    N 123.9  . 1 
      199  33 PRO HA   H   4.63 . 1 
      200  33 PRO HB2  H   2.26 . 1 
      201  33 PRO HB3  H   1.90 . 1 
      202  34 ILE H    H   8.61 . 1 
      203  34 ILE N    N 118.6  . 1 
      204  35 PRO HA   H   4.64 . 1 
      205  35 PRO C    C 177.47 . 1 
      206  35 PRO CA   C  60.48 . 1 
      207  35 PRO CB   C  31.8  . 1 
      208  36 ASP H    H   8.58 . 1 
      209  36 ASP HA   H   4.39 . 1 
      210  36 ASP HB2  H   2.73 . 1 
      211  36 ASP HB3  H   2.11 . 1 
      212  36 ASP C    C 178.14 . 1 
      213  36 ASP CA   C  55.06 . 1 
      214  36 ASP CB   C  37.07 . 1 
      215  36 ASP N    N 130.0  . 1 
      216  37 ARG H    H   8.24 . 1 
      217  37 ARG HA   H   4.01 . 1 
      218  37 ARG C    C 178.63 . 1 
      219  37 ARG CA   C  57.62 . 1 
      220  37 ARG CB   C  30.43 . 1 
      221  37 ARG N    N 118.6  . 1 
      222  38 ILE H    H   6.94 . 1 
      223  38 ILE HA   H   3.64 . 1 
      224  38 ILE HB   H   1.93 . 1 
      225  38 ILE C    C 177.32 . 1 
      226  38 ILE CA   C  60.60 . 1 
      227  38 ILE CB   C  34.17 . 1 
      228  38 ILE N    N 116.3  . 1 
      229  39 ALA H    H   8.08 . 1 
      230  39 ALA HA   H   3.92 . 1 
      231  39 ALA HB   H   1.09 . 1 
      232  39 ALA C    C 179.24 . 1 
      233  39 ALA CA   C  53.82 . 1 
      234  39 ALA CB   C  15.12 . 1 
      235  39 ALA N    N 124.8  . 1 
      236  40 ASP H    H   8.30 . 1 
      237  40 ASP HA   H   4.25 . 1 
      238  40 ASP HB2  H   2.59 . 1 
      239  40 ASP HB3  H   2.59 . 1 
      240  40 ASP C    C 178.23 . 1 
      241  40 ASP CA   C  55.63 . 1 
      242  40 ASP CB   C  39.35 . 1 
      243  40 ASP N    N 115.0  . 1 
      244  41 LYS H    H   7.11 . 1 
      245  41 LYS HA   H   4.14 . 1 
      246  41 LYS HB2  H   1.91 . 9 
      247  41 LYS C    C 177.72 . 1 
      248  41 LYS CA   C  55.67 . 1 
      249  41 LYS CB   C  31.95 . 1 
      250  41 LYS N    N 117.2  . 1 
      251  42 LEU H    H   7.50 . 1 
      252  42 LEU HA   H   4.40 . 1 
      253  42 LEU HB2  H   1.61 . 1 
      254  42 LEU HB3  H   1.61 . 1 
      255  42 LEU C    C 176.02 . 1 
      256  42 LEU CA   C  53.70 . 1 
      257  42 LEU CB   C  41.72 . 1 
      258  42 LEU N    N 117.2  . 1 
      259  43 ARG H    H   7.93 . 1 
      260  43 ARG HA   H   3.48 . 1 
      261  43 ARG C    C 176.37 . 1 
      262  43 ARG CA   C  57.95 . 1 
      263  43 ARG CB   C  27.91 . 1 
      264  43 ARG N    N 119.7  . 1 
      265  44 ASP H    H   9.08 . 1 
      266  44 ASP HA   H   4.18 . 1 
      267  44 ASP HB2  H   3.12 . 1 
      268  44 ASP HB3  H   2.83 . 1 
      269  44 ASP C    C 174.75 . 1 
      270  44 ASP CA   C  55.90 . 1 
      271  44 ASP CB   C  38.36 . 1 
      272  44 ASP N    N 118.7  . 1 
      273  45 LYS H    H   8.08 . 1 
      274  45 LYS HA   H   4.17 . 1 
      275  45 LYS HB2  H   1.99 . 1 
      276  45 LYS HB3  H   1.36 . 1 
      277  45 LYS C    C 174.41 . 1 
      278  45 LYS CA   C  55.13 . 1 
      279  45 LYS CB   C  31.73 . 1 
      280  45 LYS N    N 121.0  . 1 
      281  46 GLU H    H   7.95 . 1 
      282  46 GLU HA   H   4.51 . 1 
      283  46 GLU HB2  H   1.75 . 1 
      284  46 GLU HB3  H   1.61 . 1 
      285  46 GLU C    C 175.21 . 1 
      286  46 GLU CA   C  53.66 . 1 
      287  46 GLU CB   C  30.43 . 1 
      288  46 GLU N    N 120.2  . 1 
      289  47 PHE H    H   8.59 . 1 
      290  47 PHE HA   H   4.68 . 1 
      291  47 PHE HB2  H   3.22 . 1 
      292  47 PHE HB3  H   2.26 . 1 
      293  47 PHE C    C 175.17 . 1 
      294  47 PHE CA   C  56.08 . 1 
      295  47 PHE CB   C  42.41 . 1 
      296  47 PHE N    N 122.5  . 1 
      297  48 LYS H    H   9.52 . 1 
      298  48 LYS HA   H   4.06 . 1 
      299  48 LYS HB2  H   1.91 . 1 
      300  48 LYS HB3  H   1.91 . 1 
      301  48 LYS C    C 174.96 . 1 
      302  48 LYS CA   C  56.44 . 1 
      303  48 LYS CB   C  32.02 . 1 
      304  48 LYS N    N 120.1  . 1 
      305  49 SER H    H   7.69 . 1 
      306  49 SER HA   H   4.55 . 1 
      307  49 SER HB2  H   4.05 . 1 
      308  49 SER C    C 175.56 . 1 
      309  49 SER CA   C  56.41 . 1 
      310  49 SER CB   C  64.45 . 1 
      311  49 SER N    N 108.9  . 1 
      312  50 PHE H    H   9.30 . 1 
      313  50 PHE HA   H   4.43 . 1 
      314  50 PHE HB2  H   3.06 . 1 
      315  50 PHE C    C 176.93 . 1 
      316  50 PHE CA   C  60.97 . 1 
      317  50 PHE CB   C  37.98 . 1 
      318  50 PHE N    N 122.5  . 1 
      319  51 ASP H    H   8.36 . 1 
      320  51 ASP HA   H   4.43 . 1 
      321  51 ASP HB2  H   2.69 . 1 
      322  51 ASP C    C 178.18 . 1 
      323  51 ASP CA   C  56.43 . 1 
      324  51 ASP CB   C  39.58 . 1 
      325  51 ASP N    N 118.3  . 1 
      326  52 ASP H    H   7.85 . 1 
      327  52 ASP HA   H   4.53 . 1 
      328  52 ASP HB2  H   3.11 . 1 
      329  52 ASP C    C 178.28 . 1 
      330  52 ASP CA   C  56.16 . 1 
      331  52 ASP CB   C  40.88 . 1 
      332  52 ASP N    N 121.0  . 1 
      333  53 PHE H    H   7.52 . 1 
      334  53 PHE HA   H   3.28 . 1 
      335  53 PHE C    C 174.36 . 1 
      336  53 PHE CA   C  59.58 . 1 
      337  53 PHE CB   C  37.52 . 1 
      338  53 PHE N    N 122.9  . 1 
      339  54 ARG H    H   8.27 . 1 
      340  54 ARG HA   H   3.03 . 1 
      341  54 ARG HB2  H   1.97 . 1 
      342  54 ARG HB3  H   1.53 . 1 
      343  54 ARG C    C 175.97 . 1 
      344  54 ARG CA   C  58.15 . 1 
      345  54 ARG CB   C  29.07 . 1 
      346  54 ARG N    N 120.2  . 1 
      347  55 LYS H    H   7.35 . 1 
      348  55 LYS HA   H   4.61 . 1 
      349  55 LYS HB2  H   1.99 . 1 
      350  55 LYS C    C 177.83 . 1 
      351  55 LYS CA   C  57.34 . 1 
      352  55 LYS CB   C  32.57 . 1 
      353  55 LYS N    N 116.4  . 1 
      354  56 ALA H    H   7.16 . 1 
      355  56 ALA HA   H   4.14 . 1 
      356  56 ALA HB   H   1.48 . 1 
      357  56 ALA C    C 179.79 . 1 
      358  56 ALA CA   C  53.39 . 1 
      359  56 ALA CB   C  17.62 . 1 
      360  56 ALA N    N 120.5  . 1 
      361  57 VAL H    H   7.64 . 1 
      362  57 VAL HA   H   2.80 . 1 
      363  57 VAL HB   H   1.37 . 1 
      364  57 VAL C    C 177.48 . 1 
      365  57 VAL CA   C  65.32 . 1 
      366  57 VAL CB   C  29.44 . 1 
      367  57 VAL N    N 118.5  . 1 
      368  58 TRP H    H   7.40 . 1 
      369  58 TRP HA   H   4.73 . 1 
      370  58 TRP C    C 178.44 . 1 
      371  58 TRP CA   C  58.30 . 1 
      372  58 TRP CB   C  27.84 . 1 
      373  58 TRP N    N 118.3  . 1 
      374  59 GLU H    H   8.70 . 1 
      375  59 GLU HA   H   4.13 . 1 
      376  59 GLU C    C 181.10 . 1 
      377  59 GLU CA   C  58.38 . 1 
      378  59 GLU CB   C  28.46 . 1 
      379  59 GLU N    N 119.4  . 1 
      380  60 GLU H    H   8.32 . 1 
      381  60 GLU HA   H   4.05 . 1 
      382  60 GLU HB2  H   2.03 . 1 
      383  60 GLU C    C 180.49 . 1 
      384  60 GLU CA   C  57.48 . 1 
      385  60 GLU N    N 119.2  . 1 
      386  61 VAL H    H   8.63 . 1 
      387  61 VAL HA   H   3.42 . 1 
      388  61 VAL C    C 177.98 . 1 
      389  61 VAL CA   C  66.15 . 1 
      390  61 VAL CB   C  30.70 . 1 
      391  61 VAL N    N 124.1  . 1 
      392  62 SER H    H   8.18 . 1 
      393  62 SER HB2  H   3.94 . 1 
      394  62 SER HB3  H   3.94 . 1 
      395  62 SER C    C 174.56 . 1 
      396  62 SER CA   C  60.01 . 1 
      397  62 SER CB   C  62.46 . 1 
      398  62 SER N    N 113.8  . 1 
      399  63 LYS H    H   6.99 . 1 
      400  63 LYS HA   H   4.20 . 1 
      401  63 LYS HB2  H   2.06 . 1 
      402  63 LYS HB3  H   1.66 . 1 
      403  63 LYS C    C 175.01 . 1 
      404  63 LYS CA   C  55.09 . 1 
      405  63 LYS CB   C  32.91 . 1 
      406  63 LYS N    N 119.4  . 1 
      407  64 ASP H    H   7.68 . 1 
      408  64 ASP CA   C  49.57 . 1 
      409  64 ASP N    N 123.6  . 1 
      410  65 PRO HA   H   4.22 . 1 
      411  65 PRO HB2  H   2.33 . 1 
      412  65 PRO HB3  H   2.01 . 1 
      413  65 PRO C    C 178.18 . 1 
      414  65 PRO CA   C  63.59 . 1 
      415  65 PRO CB   C  31.31 . 1 
      416  66 GLU H    H   7.82 . 1 
      417  66 GLU HA   H   4.29 . 1 
      418  66 GLU HB2  H   1.94 . 1 
      419  66 GLU HB3  H   1.94 . 1 
      420  66 GLU C    C 178.39 . 1 
      421  66 GLU CA   C  57.17 . 1 
      422  66 GLU CB   C  28.86 . 1 
      423  66 GLU N    N 115.9  . 1 
      424  67 LEU H    H   8.38 . 1 
      425  67 LEU HA   H   4.35 . 1 
      426  67 LEU HB2  H   1.44 . 1 
      427  67 LEU HB3  H   1.44 . 1 
      428  67 LEU C    C 179.29 . 1 
      429  67 LEU CA   C  55.12 . 1 
      430  67 LEU CB   C  41.31 . 1 
      431  67 LEU N    N 116.8  . 1 
      432  68 SER H    H   8.00 . 1 
      433  68 SER HA   H   4.50 . 1 
      434  68 SER HB2  H   4.05 . 1 
      435  68 SER HB3  H   4.05 . 1 
      436  68 SER C    C 175.20 . 1 
      437  68 SER CA   C  56.87 . 1 
      438  68 SER CB   C  63.13 . 1 
      439  68 SER N    N 110.4  . 1 
      440  69 LYS H    H   7.20 . 1 
      441  69 LYS HA   H   4.03 . 1 
      442  69 LYS HB2  H   2.33 . 1 
      443  69 LYS HB3  H   1.93 . 1 
      444  69 LYS C    C 176.93 . 1 
      445  69 LYS CA   C  58.50 . 1 
      446  69 LYS CB   C  32.23 . 1 
      447  69 LYS N    N 123.7  . 1 
      448  70 ASN H    H   8.75 . 1 
      449  70 ASN HA   H   4.90 . 1 
      450  70 ASN HB2  H   3.04 . 1 
      451  70 ASN HB3  H   2.59 . 1 
      452  70 ASN C    C 175.32 . 1 
      453  70 ASN CA   C  52.19 . 1 
      454  70 ASN CB   C  38.03 . 1 
      455  70 ASN N    N 113.8  . 1 
      456  71 LEU H    H   7.49 . 1 
      457  71 LEU HA   H   4.44 . 1 
      458  71 LEU C    C 175.06 . 1 
      459  71 LEU CA   C  52.31 . 1 
      460  71 LEU CB   C  41.83 . 1 
      461  71 LEU N    N 120.8  . 1 
      462  72 ASN H    H   9.02 . 1 
      463  72 ASN CA   C  50.17 . 1 
      464  72 ASN N    N 125.9  . 1 
      465  73 PRO HA   H   4.07 . 1 
      466  73 PRO HB2  H   2.32 . 9 
      467  73 PRO C    C 178.78 . 1 
      468  73 PRO CA   C  65.35 . 1 
      469  73 PRO CB   C  30.14 . 1 
      470  74 SER H    H   6.97 . 1 
      471  74 SER HA   H   4.90 . 1 
      472  74 SER HB2  H   3.49 . 1 
      473  74 SER C    C 177.33 . 1 
      474  74 SER CA   C  59.85 . 1 
      475  74 SER CB   C  61.90 . 1 
      476  74 SER N    N 113.0  . 1 
      477  75 ASN H    H   8.33 . 1 
      478  75 ASN HA   H   5.35 . 1 
      479  75 ASN HB2  H   3.31 . 1 
      480  75 ASN HB3  H   2.63 . 1 
      481  75 ASN C    C 178.94 . 1 
      482  75 ASN CA   C  51.99 . 1 
      483  75 ASN CB   C  37.78 . 1 
      484  75 ASN N    N 126.7  . 1 
      485  76 LYS H    H   9.14 . 1 
      486  76 LYS HA   H   4.00 . 1 
      487  76 LYS HB2  H   1.91 . 1 
      488  76 LYS HB3  H   1.91 . 1 
      489  76 LYS C    C 179.74 . 1 
      490  76 LYS CA   C  58.90 . 1 
      491  76 LYS CB   C  31.05 . 1 
      492  76 LYS N    N 120.8  . 1 
      493  77 SER H    H   8.39 . 1 
      494  77 SER C    C 175.92 . 1 
      495  77 SER CA   C  61.14 . 1 
      496  77 SER N    N 118.1  . 1 
      497  78 SER H    H   7.21 . 1 
      498  78 SER HA   H   4.23 . 1 
      499  78 SER HB2  H   3.92 . 1 
      500  78 SER C    C 177.38 . 1 
      501  78 SER CA   C  61.31 . 1 
      502  78 SER N    N 115.9  . 1 
      503  79 VAL H    H   7.86 . 1 
      504  79 VAL HA   H   4.87 . 1 
      505  79 VAL C    C 179.74 . 1 
      506  79 VAL CA   C  62.94 . 1 
      507  79 VAL CB   C  28.98 . 1 
      508  79 VAL N    N 112.6  . 1 
      509  80 SER H    H   8.08 . 1 
      510  80 SER HA   H   4.43 . 1 
      511  80 SER HB2  H   3.97 . 1 
      512  80 SER HB3  H   3.97 . 1 
      513  80 SER C    C 175.72 . 1 
      514  80 SER CA   C  60.09 . 1 
      515  80 SER CB   C  61.85 . 1 
      516  80 SER N    N 117.3  . 1 
      517  81 LYS H    H   7.15 . 1 
      518  81 LYS HA   H   4.26 . 1 
      519  81 LYS HB2  H   1.91 . 1 
      520  81 LYS HB3  H   1.66 . 1 
      521  81 LYS C    C 176.11 . 1 
      522  81 LYS CA   C  53.98 . 1 
      523  81 LYS CB   C  29.99 . 1 
      524  81 LYS N    N 119.7  . 1 
      525  82 GLY H    H   8.25 . 1 
      526  82 GLY HA2  H   4.24 . 1 
      527  82 GLY HA3  H   3.74 . 1 
      528  82 GLY C    C 173.09 . 1 
      529  82 GLY CA   C  44.54 . 1 
      530  82 GLY N    N 107.8  . 1 
      531  83 TYR H    H   7.35 . 1 
      532  83 TYR HA   H   4.86 . 1 
      533  83 TYR C    C 172.85 . 1 
      534  83 TYR CA   C  50.84 . 1 
      535  83 TYR CB   C  34.44 . 1 
      536  83 TYR N    N 120.5  . 1 
      537  84 SER H    H   7.81 . 1 
      538  84 SER CA   C  54.14 . 1 
      539  84 SER N    N 114.4  . 1 
      540  85 PRO HA   H   4.34 . 1 
      541  85 PRO C    C 176.37 . 1 
      542  85 PRO CA   C  60.05 . 1 
      543  86 PHE H    H   9.18 . 1 
      544  86 PHE HA   H   4.15 . 1 
      545  86 PHE C    C 178.28 . 1 
      546  86 PHE CA   C  57.35 . 1 
      547  86 PHE CB   C  39.20 . 1 
      548  86 PHE N    N 120.0  . 1 
      549  87 THR H    H   8.48 . 1 
      550  87 THR CA   C  58.61 . 1 
      551  87 THR N    N 114.7  . 1 
      552  88 PRO HA   H   4.00 . 1 
      553  88 PRO C    C 178.28 . 1 
      554  88 PRO CA   C  61.71 . 1 
      555  89 LYS H    H  10.99 . 1 
      556  89 LYS HA   H   3.62 . 1 
      557  89 LYS HB2  H   1.80 . 1 
      558  89 LYS C    C 178.18 . 1 
      559  89 LYS CA   C  58.58 . 1 
      560  89 LYS CB   C  30.44 . 1 
      561  89 LYS N    N 133.1  . 1 
      562  90 ASN H    H   8.83 . 1 
      563  90 ASN HA   H   4.35 . 1 
      564  90 ASN HB2  H   3.05 . 1 
      565  90 ASN HB3  H   2.74 . 1 
      566  90 ASN C    C 175.97 . 1 
      567  90 ASN CA   C  53.07 . 1 
      568  90 ASN CB   C  35.71 . 1 
      569  90 ASN N    N 115.3  . 1 
      570  91 GLN H    H   7.84 . 1 
      571  91 GLN HA   H   4.24 . 1 
      572  91 GLN C    C 173.96 . 1 
      573  91 GLN CA   C  53.05 . 1 
      574  91 GLN CB   C  28.06 . 1 
      575  91 GLN N    N 117.5  . 1 
      576  92 GLN H    H   7.32 . 1 
      577  92 GLN HA   H   4.12 . 1 
      578  92 GLN HB2  H   1.97 . 1 
      579  92 GLN C    C 176.32 . 1 
      580  92 GLN CA   C  53.87 . 1 
      581  92 GLN N    N 119.1  . 1 
      582  93 VAL H    H   8.17 . 1 
      583  93 VAL HA   H   4.18 . 1 
      584  93 VAL HB   H   1.74 . 1 
      585  93 VAL C    C 176.07 . 1 
      586  93 VAL CA   C  60.49 . 1 
      587  93 VAL CB   C  33.71 . 1 
      588  93 VAL N    N 119.3  . 1 
      589  94 GLY H    H   9.10 . 1 
      590  94 GLY HA2  H   3.79 . 1 
      591  94 GLY HA3  H   3.67 . 1 
      592  94 GLY C    C 174.66 . 1 
      593  94 GLY CA   C  45.89 . 1 
      594  94 GLY N    N 119.3  . 1 
      595  95 GLY H    H   8.65 . 1 
      596  95 GLY HA2  H   4.05 . 1 
      597  95 GLY HA3  H   3.68 . 1 
      598  95 GLY C    C 174.26 . 1 
      599  95 GLY CA   C  44.55 . 1 
      600  95 GLY N    N 114.1  . 1 
      601  96 ARG H    H   8.16 . 1 
      602  96 ARG HA   H   4.43 . 1 
      603  96 ARG HB2  H   2.08 . 1 
      604  96 ARG C    C 174.70 . 1 
      605  96 ARG CA   C  54.50 . 1 
      606  96 ARG CB   C  31.36 . 9 
      607  96 ARG N    N 123.3  . 1 
      608  97 LYS H    H   8.57 . 1 
      609  97 LYS HA   H   4.28 . 1 
      610  97 LYS HB2  H   1.37 . 1 
      611  97 LYS C    C 173.60 . 1 
      612  97 LYS CA   C  54.54 . 1 
      613  97 LYS CB   C  34.94 . 1 
      614  97 LYS N    N 121.2  . 1 
      615  98 VAL H    H   6.78 . 1 
      616  98 VAL HA   H   4.63 . 1 
      617  98 VAL HB   H   1.55 . 1 
      618  98 VAL C    C 176.20 . 1 
      619  98 VAL CA   C  56.56 . 1 
      620  98 VAL N    N 107.3  . 1 
      621  99 TYR H    H   7.64 . 1 
      622  99 TYR C    C 175.00 . 1 
      623  99 TYR CA   C  60.17 . 1 
      624  99 TYR N    N 117.8  . 1 
      625 100 GLU H    H   8.85 . 1 
      626 100 GLU HA   H   4.49 . 1 
      627 100 GLU C    C 174.51 . 1 
      628 100 GLU CA   C  52.99 . 1 
      629 100 GLU CB   C  32.20 . 1 
      630 100 GLU N    N 119.9  . 1 
      631 101 LEU H    H   8.40 . 1 
      632 101 LEU HA   H   5.22 . 1 
      633 101 LEU HB2  H   1.70 . 1 
      634 101 LEU C    C 175.46 . 1 
      635 101 LEU CA   C  52.49 . 1 
      636 101 LEU CB   C  42.02 . 1 
      637 101 LEU N    N 120.7  . 1 
      638 102 HIS H    H   9.02 . 1 
      639 102 HIS HA   H   5.01 . 1 
      640 102 HIS C    C 173.05 . 1 
      641 102 HIS CA   C  52.51 . 1 
      642 102 HIS N    N 119.3  . 1 
      643 103 HIS H    H  10.00 . 1 
      644 103 HIS HA   H   5.16 . 1 
      645 103 HIS HB2  H   2.93 . 1 
      646 103 HIS HB3  H   2.93 . 1 
      647 103 HIS C    C 175.06 . 1 
      648 103 HIS CA   C  55.53 . 1 
      649 103 HIS CB   C  28.22 . 1 
      650 103 HIS N    N 120.3  . 1 
      651 104 ASP H    H   8.21 . 1 
      652 104 ASP HA   H   4.37 . 1 
      653 104 ASP HB2  H   2.81 . 1 
      654 104 ASP HB3  H   2.39 . 1 
      655 104 ASP C    C 175.67 . 1 
      656 104 ASP CA   C  55.45 . 1 
      657 104 ASP CB   C  40.74 . 1 
      658 104 ASP N    N 125.5  . 1 
      659 105 LYS H    H   9.49 . 1 
      660 105 LYS CA   C  51.64 . 1 
      661 105 LYS N    N 122.1  . 1 
      662 106 PRO HA   H   4.31 . 1 
      663 106 PRO HB2  H   2.38 . 1 
      664 106 PRO HB3  H   1.72 . 1 
      665 106 PRO C    C 178.54 . 1 
      666 106 PRO CA   C  61.40 . 1 
      667 106 PRO CB   C  31.42 . 1 
      668 107 ILE H    H   8.72 . 1 
      669 107 ILE HA   H   3.97 . 1 
      670 107 ILE HB   H   1.62 . 1 
      671 107 ILE C    C 179.29 . 1 
      672 107 ILE CA   C  61.32 . 1 
      673 107 ILE CB   C  36.15 . 1 
      674 107 ILE N    N 125.6  . 1 
      675 108 SER H    H   8.53 . 1 
      676 108 SER HA   H   4.19 . 1 
      677 108 SER HB2  H   3.91 . 1 
      678 108 SER HB3  H   3.91 . 1 
      679 108 SER C    C 174.97 . 1 
      680 108 SER CA   C  58.61 . 1 
      681 108 SER CB   C  61.63 . 1 
      682 108 SER N    N 115.7  . 1 
      683 109 GLN H    H   7.47 . 1 
      684 109 GLN HA   H   4.53 . 1 
      685 109 GLN HB2  H   2.41 . 1 
      686 109 GLN HB3  H   1.62 . 1 
      687 109 GLN C    C 175.32 . 1 
      688 109 GLN CA   C  53.35 . 1 
      689 109 GLN CB   C  28.22 . 1 
      690 109 GLN N    N 119.8  . 1 
      691 110 GLY H    H   7.84 . 1 
      692 110 GLY HA2  H   4.26 . 1 
      693 110 GLY HA3  H   3.65 . 1 
      694 110 GLY C    C 175.22 . 1 
      695 110 GLY CA   C  43.69 . 1 
      696 110 GLY N    N 107.3  . 1 
      697 111 GLY H    H   8.09 . 1 
      698 111 GLY HA2  H   3.75 . 1 
      699 111 GLY HA3  H   3.41 . 1 
      700 111 GLY C    C 172.50 . 1 
      701 111 GLY CA   C  43.21 . 1 
      702 111 GLY N    N 109.7  . 1 
      703 112 GLU H    H   8.70 . 1 
      704 112 GLU HA   H   4.38 . 1 
      705 112 GLU HB2  H   2.03 . 1 
      706 112 GLU C    C 178.03 . 1 
      707 112 GLU CA   C  54.46 . 1 
      708 112 GLU CB   C  29.97 . 1 
      709 112 GLU N    N 122.2  . 1 
      710 113 VAL H    H   8.40 . 1 
      711 113 VAL HA   H   2.89 . 1 
      712 113 VAL HB   H   1.46 . 1 
      713 113 VAL C    C 177.27 . 1 
      714 113 VAL CA   C  63.68 . 1 
      715 113 VAL CB   C  31.42 . 1 
      716 113 VAL N    N 121.6  . 1 
      717 114 TYR H    H   8.55 . 1 
      718 114 TYR HA   H   4.11 . 1 
      719 114 TYR HB2  H   2.86 . 1 
      720 114 TYR C    C 173.34 . 1 
      721 114 TYR CA   C  54.98 . 1 
      722 114 TYR CB   C  36.30 . 1 
      723 114 TYR N    N 116.1  . 1 
      724 115 ASP H    H   6.12 . 1 
      725 115 ASP HA   H   4.77 . 1 
      726 115 ASP HB2  H   2.59 . 1 
      727 115 ASP C    C 177.57 . 1 
      728 115 ASP CA   C  50.72 . 1 
      729 115 ASP N    N 116.4  . 1 
      730 116 MET H    H   9.92 . 1 
      731 116 MET HA   H   3.83 . 1 
      732 116 MET C    C 176.78 . 1 
      733 116 MET CA   C  57.75 . 1 
      734 116 MET CB   C  32.38 . 1 
      735 116 MET N    N 126.4  . 1 
      736 117 ASP H    H   8.70 . 1 
      737 117 ASP HA   H   4.92 . 1 
      738 117 ASP HB2  H   2.89 . 1 
      739 117 ASP C    C 175.51 . 1 
      740 117 ASP CA   C  55.13 . 1 
      741 117 ASP CB   C  38.75 . 1 
      742 117 ASP N    N 118.0  . 1 
      743 118 ASN H    H   8.29 . 1 
      744 118 ASN HA   H   5.19 . 1 
      745 118 ASN HB2  H   3.07 . 1 
      746 118 ASN HB3  H   2.65 . 1 
      747 118 ASN C    C 173.75 . 1 
      748 118 ASN CA   C  50.53 . 1 
      749 118 ASN CB   C  40.41 . 1 
      750 118 ASN N    N 119.1  . 1 
      751 119 ILE H    H   6.70 . 1 
      752 119 ILE HA   H   4.76 . 1 
      753 119 ILE HB   H   1.50 . 1 
      754 119 ILE C    C 173.85 . 1 
      755 119 ILE CA   C  58.11 . 1 
      756 119 ILE CB   C  39.48 . 1 
      757 119 ILE N    N 119.6  . 1 
      758 120 ARG H    H   8.92 . 1 
      759 120 ARG HA   H   5.09 . 1 
      760 120 ARG C    C 174.80 . 1 
      761 120 ARG CA   C  50.97 . 1 
      762 120 ARG N    N 125.3  . 1 
      763 121 VAL H    H   9.97 . 1 
      764 121 VAL HA   H   5.16 . 1 
      765 121 VAL HB   H   2.07 . 1 
      766 121 VAL C    C 176.82 . 1 
      767 121 VAL CA   C  59.41 . 1 
      768 121 VAL CB   C  31.36 . 1 
      769 121 VAL N    N 123.7  . 1 
      770 122 THR H    H   9.68 . 1 
      771 122 THR HA   H   6.05 . 1 
      772 122 THR HB   H   4.46 . 1 
      773 122 THR C    C 175.67 . 1 
      774 122 THR CA   C  58.38 . 1 
      775 122 THR CB   C  66.04 . 1 
      776 122 THR N    N 116.5  . 1 
      777 123 THR H    H   7.52 . 1 
      778 123 THR CA   C  58.39 . 1 
      779 123 THR N    N 111.2  . 1 
      780 124 PRO HA   H   4.17 . 1 
      781 124 PRO C    C 177.13 . 1 
      782 124 PRO CA   C  64.55 . 1 
      783 124 PRO CB   C  31.76 . 1 
      784 125 LYS H    H   7.59 . 1 
      785 125 LYS HA   H   3.61 . 1 
      786 125 LYS C    C 177.13 . 1 
      787 125 LYS CA   C  57.73 . 1 
      788 125 LYS CB   C  31.91 . 1 
      789 125 LYS N    N 114.0  . 1 
      790 126 ARG H    H   7.69 . 1 
      791 126 ARG HA   H   4.23 . 1 
      792 126 ARG C    C 177.18 . 1 
      793 126 ARG CA   C  55.49 . 1 
      794 126 ARG CB   C  28.93 . 1 
      795 126 ARG N    N 116.7  . 1 
      796 127 HIS H    H   8.02 . 1 
      797 127 HIS HA   H   3.91 . 1 
      798 127 HIS HB2  H   3.03 . 9 
      799 127 HIS C    C 177.62 . 1 
      800 127 HIS CA   C  60.64 . 1 
      801 127 HIS CB   C  29.29 . 1 
      802 127 HIS N    N 118.5  . 1 
      803 128 ILE H    H   8.03 . 1 
      804 128 ILE HA   H   3.72 . 1 
      805 128 ILE HB   H   1.94 . 1 
      806 128 ILE C    C 178.38 . 1 
      807 128 ILE CA   C  62.81 . 1 
      808 128 ILE CB   C  36.88 . 1 
      809 128 ILE N    N 118.8  . 1 
      810 129 ASP H    H   8.15 . 1 
      811 129 ASP HA   H   4.44 . 1 
      812 129 ASP HB2  H   2.75 . 1 
      813 129 ASP C    C 179.08 . 1 
      814 129 ASP CA   C  55.87 . 1 
      815 129 ASP CB   C  39.44 . 1 
      816 129 ASP N    N 121.8  . 1 
      817 130 ILE H    H   8.35 . 1 
      818 130 ILE HA   H   3.67 . 1 
      819 130 ILE HB   H   1.57 . 1 
      820 130 ILE C    C 177.64 . 1 
      821 130 ILE CA   C  63.07 . 1 
      822 130 ILE CB   C  37.34 . 1 
      823 130 ILE N    N 119.9  . 1 
      824 131 HIS H    H   7.45 . 1 
      825 131 HIS HA   H   4.33 . 1 
      826 131 HIS HB2  H   3.23 . 1 
      827 131 HIS HB3  H   2.70 . 1 
      828 131 HIS C    C 174.50 . 1 
      829 131 HIS CA   C  55.83 . 1 
      830 131 HIS CB   C  27.85 . 1 
      831 131 HIS N    N 117.2  . 1 
      832 132 ARG H    H   7.74 . 1 
      833 132 ARG HA   H   4.27 . 1 
      834 132 ARG HB2  H   1.84 . 1 
      835 132 ARG C    C 176.57 . 1 
      836 132 ARG CA   C  55.65 . 1 
      837 132 ARG CB   C  29.41 . 1 
      838 132 ARG N    N 120.9  . 1 
      839 133 GLY H    H   8.24 . 1 
      840 133 GLY HA2  H   3.91 . 1 
      841 133 GLY C    C 173.15 . 1 
      842 133 GLY CA   C  44.17 . 1 
      843 133 GLY N    N 110.2  . 1 
      844 134 LYS H    H   7.76 . 1 
      845 134 LYS CA   C  55.73 . 1 
      846 134 LYS N    N 126.0  . 1 

   stop_

save_


save_assigned_chemical_shifts_for_minor_conformer_of_E9_DNase
   _Saveframe_category               assigned_chemical_shifts

   _Details                         
;
Assignments refer to the minor conformational species
of E9 DNase when bound to its inhibitor, Im9.
;

   loop_
      _Sample_label

      $sample_one 

   stop_

   _Sample_conditions_label         $sample_conditions_one
   _Chem_shift_reference_set_label  $chemical_shift_reference_set_one
   _Mol_system_component_name       'E9 DNase'

   loop_
      _Atom_shift_assign_ID
      _Residue_seq_code
      _Residue_label
      _Atom_name
      _Atom_type
      _Chem_shift_value
      _Chem_shift_value_error
      _Chem_shift_ambiguity_code

        1  14 LYS C   C 178.68 . 1 
        2  14 LYS CA  C  56.40 . 1 
        3  14 LYS CB  C  34.06 . 1 
        4  15 GLY H   H   9.17 . 1 
        5  15 GLY HA2 H   3.84 . 1 
        6  15 GLY HA3 H   3.61 . 1 
        7  15 GLY CA  C  43.42 . 1 
        8  15 GLY N   N 106.7  . 1 
        9  17 PRO HA  H   4.67 . 1 
       10  17 PRO HB2 H   2.31 . 1 
       11  17 PRO C   C 177.27 . 1 
       12  17 PRO CA  C  61.47 . 1 
       13  17 PRO CB  C  29.83 . 1 
       14  18 VAL H   H   8.68 . 1 
       15  18 VAL HA  H   4.68 . 1 
       16  18 VAL HB  H   2.26 . 1 
       17  18 VAL C   C 175.56 . 1 
       18  18 VAL CA  C  58.06 . 1 
       19  18 VAL CB  C  34.09 . 1 
       20  18 VAL N   N 118.2  . 1 
       21  19 GLY H   H   8.39 . 1 
       22  19 GLY HA2 H   4.48 . 1 
       23  19 GLY HA3 H   3.81 . 1 
       24  19 GLY C   C 174.30 . 1 
       25  19 GLY CA  C  42.90 . 1 
       26  19 GLY N   N 110.5  . 1 
       27  20 ASP H   H   8.38 . 1 
       28  20 ASP HA  H   4.41 . 1 
       29  20 ASP HB2 H   2.73 . 1 
       30  20 ASP C   C 177.03 . 1 
       31  20 ASP CA  C  54.33 . 1 
       32  20 ASP CB  C  39.84 . 1 
       33  20 ASP N   N 119.1  . 1 
       34  21 LYS H   H   8.33 . 1 
       35  21 LYS HA  H   4.62 . 1 
       36  21 LYS HB2 H   1.70 . 1 
       37  21 LYS C   C 175.67 . 1 
       38  21 LYS CA  C  53.78 . 1 
       39  21 LYS CB  C  30.12 . 1 
       40  21 LYS N   N 119.9  . 1 
       41  22 TRP H   H   7.55 . 1 
       42  22 TRP HA  H   4.41 . 1 
       43  22 TRP C   C 176.32 . 1 
       44  22 TRP CA  C  59.34 . 1 
       45  22 TRP N   N 122.1  . 1 
       46  23 LEU H   H   8.41 . 1 
       47  23 LEU HA  H   3.23 . 1 
       48  23 LEU C   C 180.34 . 1 
       49  23 LEU CA  C  55.26 . 1 
       50  23 LEU CB  C  38.34 . 1 
       51  23 LEU N   N 113.2  . 1 
       52  24 ASP H   H   8.05 . 1 
       53  24 ASP HA  H   4.35 . 1 
       54  24 ASP HB2 H   2.90 . 1 
       55  24 ASP HB3 H   2.63 . 1 
       56  24 ASP CA  C  56.32 . 1 
       57  24 ASP CB  C  39.18 . 1 
       58  24 ASP N   N 123.6  . 1 
       59  25 ASP H   H   7.92 . 1 
       60  25 ASP HA  H   4.37 . 1 
       61  25 ASP C   C 177.37 . 1 
       62  25 ASP CA  C  55.17 . 1 
       63  25 ASP CB  C  38.34 . 1 
       64  25 ASP N   N 120.1  . 1 
       65  26 ALA H   H   7.43 . 1 
       66  26 ALA HA  H   4.47 . 1 
       67  26 ALA HB  H   1.37 . 1 
       68  26 ALA C   C 176.93 . 1 
       69  26 ALA CA  C  52.55 . 1 
       70  26 ALA N   N 120.2  . 1 
       71  27 GLY H   H   7.44 . 1 
       72  27 GLY HA2 H   4.47 . 1 
       73  27 GLY HA3 H   3.62 . 1 
       74  27 GLY C   C 173.17 . 1 
       75  27 GLY CA  C  43.14 . 1 
       76  27 GLY N   N 102.1  . 1 
       77  28 LYS H   H   7.54 . 1 
       78  28 LYS HA  H   4.62 . 1 
       79  28 LYS HB2 H   1.76 . 1 
       80  28 LYS C   C 173.66 . 1 
       81  28 LYS CA  C  53.15 . 1 
       82  28 LYS CB  C  35.24 . 1 
       83  28 LYS N   N 119.8  . 1 
       84  29 ASP H   H   8.91 . 1 
       85  29 ASP HA  H   4.08 . 1 
       86  29 ASP HB2 H   2.82 . 1 
       87  29 ASP HB3 H   2.82 . 1 
       88  29 ASP C   C 176.06 . 1 
       89  29 ASP CA  C  55.13 . 1 
       90  29 ASP CB  C  38.98 . 1 
       91  29 ASP N   N 119.3  . 1 
       92  30 SER H   H   8.22 . 1 
       93  30 SER CA  C  56.80 . 1 
       94  30 SER N   N 117.4  . 1 
       95  31 GLY H   H   8.39 . 1 
       96  31 GLY HA2 H   4.33 . 1 
       97  31 GLY HA3 H   4.33 . 1 
       98  31 GLY C   C 173.29 . 1 
       99  31 GLY CA  C  43.00 . 1 
      100  31 GLY N   N 108.3  . 1 
      101  32 ALA H   H   9.37 . 1 
      102  32 ALA CA  C  47.59 . 1 
      103  32 ALA N   N 124.1  . 1 
      104  36 ASP H   H   8.74 . 1 
      105  36 ASP HA  H   4.39 . 1 
      106  36 ASP HB2 H   2.73 . 1 
      107  36 ASP HB3 H   2.11 . 1 
      108  36 ASP C   C 178.28 . 1 
      109  36 ASP CA  C  55.06 . 1 
      110  36 ASP CB  C  36.91 . 1 
      111  36 ASP N   N 131.3  . 1 
      112  37 ARG H   H   8.57 . 1 
      113  37 ARG HA  H   4.04 . 1 
      114  37 ARG C   C 178.44 . 1 
      115  37 ARG CA  C  57.18 . 1 
      116  37 ARG CB  C  30.35 . 1 
      117  37 ARG N   N 118.6  . 1 
      118  38 ILE H   H   6.91 . 1 
      119  38 ILE HA  H   3.68 . 1 
      120  38 ILE C   C 177.23 . 1 
      121  38 ILE CA  C  60.75 . 1 
      122  38 ILE N   N 116.9  . 1 
      123  39 ALA H   H   8.24 . 1 
      124  39 ALA HA  H   3.92 . 1 
      125  39 ALA HB  H   1.09 . 1 
      126  39 ALA C   C 179.30 . 1 
      127  39 ALA CA  C  53.82 . 1 
      128  39 ALA N   N 124.8  . 1 
      129  40 ASP H   H   8.33 . 1 
      130  40 ASP CA  C  55.71 . 1 
      131  40 ASP N   N 115.4  . 1 
      132  42 LEU H   H   7.41 . 1 
      133  42 LEU CA  C  53.82 . 1 
      134  42 LEU N   N 117.2  . 1 
      135  59 GLU H   H   8.70 . 1 
      136  59 GLU HA  H   4.13 . 1 
      137  59 GLU HB2 H   2.15 . 1 
      138  59 GLU HB3 H   1.92 . 1 
      139  59 GLU C   C 181.10 . 1 
      140  59 GLU CA  C  58.71 . 1 
      141  59 GLU CB  C  28.46 . 1 
      142  59 GLU N   N 119.4  . 1 
      143  60 GLU H   H   8.24 . 1 
      144  60 GLU C   C 180.49 . 1 
      145  60 GLU CA  C  57.53 . 1 
      146  60 GLU N   N 119.4  . 1 
      147  61 VAL H   H   8.61 . 1 
      148  61 VAL N   N 124.1  . 1 
      149  64 ASP H   H   7.70 . 1 
      150  64 ASP CA  C  49.57 . 1 
      151  64 ASP N   N 123.6  . 1 
      152  68 SER HA  H   4.23 . 1 
      153  68 SER C   C 175.80 . 1 
      154  68 SER CB  C  63.13 . 1 
      155  69 LYS H   H   7.12 . 1 
      156  69 LYS HA  H   4.09 . 1 
      157  69 LYS HB2 H   2.12 . 1 
      158  69 LYS HB3 H   1.92 . 1 
      159  69 LYS C   C 176.78 . 1 
      160  69 LYS CA  C  58.03 . 1 
      161  69 LYS CB  C  31.07 . 1 
      162  69 LYS N   N 122.1  . 1 
      163  70 ASN H   H   8.27 . 1 
      164  70 ASN HA  H   4.86 . 1 
      165  70 ASN HB2 H   3.13 . 1 
      166  70 ASN HB3 H   2.75 . 1 
      167  70 ASN C   C 175.06 . 1 
      168  70 ASN CA  C  52.28 . 1 
      169  70 ASN CB  C  38.01 . 1 
      170  70 ASN N   N 114.6  . 1 
      171  71 LEU H   H   7.65 . 1 
      172  71 LEU CA  C  52.27 . 1 
      173  71 LEU N   N 120.9  . 1 
      174 121 VAL H   H   9.86 . 1 
      175 121 VAL HA  H   5.16 . 1 
      176 121 VAL HB  H   2.07 . 1 
      177 121 VAL CA  C  59.06 . 1 
      178 121 VAL N   N 123.4  . 1 
      179 122 THR H   H   9.63 . 1 
      180 122 THR HA  H   6.05 . 1 
      181 122 THR HB  H   4.46 . 1 
      182 122 THR N   N 116.5  . 1 
      183 133 GLY H   H   7.99 . 1 
      184 133 GLY HA2 H   4.00 . 1 
      185 133 GLY C   C 173.15 . 1 
      186 133 GLY CA  C  44.43 . 1 
      187 133 GLY N   N 109.1  . 1 
      188 134 LYS H   H   7.85 . 1 
      189 134 LYS CA  C  55.17 . 1 
      190 134 LYS N   N 126.0  . 1 

   stop_

save_



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