*HEADER    IMMUNE SYSTEM/HYDROLASE                 01-JUL-08   2K5X              
*TITLE     CHEMICAL SHIFT STRUCTURE OF COLICIN E9 DNASE DOMAIN WITH              
*TITLE    2 ITS COGNATE IMMUNITY PROTEIN IM9                                     
*COMPND    MOL_ID: 1;                                                            
*COMPND   2 MOLECULE: COLICIN-E9 IMMUNITY PROTEIN;                               
*COMPND   3 CHAIN: A;                                                            
*COMPND   4 SYNONYM: IMME9, MICROCIN-E9 IMMUNITY PROTEIN;                        
*COMPND   5 ENGINEERED: YES;                                                     
*COMPND   6 MOL_ID: 2;                                                           
*COMPND   7 MOLECULE: COLICIN-E9;                                                
*COMPND   8 CHAIN: B;                                                            
*COMPND   9 FRAGMENT: UNP RESIDUES 450-582;                                      
*COMPND  10 EC: 3.1.-.-;                                                         
*COMPND  11 ENGINEERED: YES                                                      
*SOURCE    MOL_ID: 1;                                                            
*SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
*SOURCE   3 ORGANISM_TAXID: 562;                                                 
*SOURCE   4 GENE: IMM, CEIE9;                                                    
*SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
*SOURCE   6 MOL_ID: 2;                                                           
*SOURCE   7 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
*SOURCE   8 ORGANISM_TAXID: 562;                                                 
*SOURCE   9 GENE: COL, CEI;                                                      
*SOURCE  10 EXPRESSION_SYSTEM: ESCHERICHIA COLI                                  
*KEYWDS    COLICIN E9, IMMUNITY PROTEIN IM9, BACTERIOCIN IMMUNITY,               
*KEYWDS   2 PLASMID, ANTIBIOTIC, ANTIMICROBIAL, BACTERIOCIN,                     
*KEYWDS   3 ENDONUCLEASE, HYDROLASE, METAL-BINDING, NUCLEASE, ZINC,              
*KEYWDS   4 IMMUNE SYSTEM/HYDROLASE COMPLEX                                      
*EXPDTA    SOLUTION NMR                                                          
*AUTHOR    R.W.MONTALVAO, A.CAVALLI, M.VENDRUSCOLO                               
*REVDAT   1   09-DEC-08 2K5X    0                                                


 ##############################
 #  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_

  Entry H atom name         Submitted Coord H atom name
    1    H1   MET   1           HT1      MET   1   1.131   8.670  67.148
    2    H2   MET   1           HT2      MET   1   1.813   9.841  66.030
    3    H3   MET   1           HT3      MET   1   1.514   8.217  65.564
    4    H    GLU   2           H        GLU   2  -2.299   8.106  64.695
    5    H    LEU   3           H        LEU   3  -0.348   5.258  65.689
    6    H    LYS   4           H        LYS   4  -0.122   1.333  63.749
    7    HZ1  LYS   4           HZ1      LYS   4  -5.503  -2.620  67.449
    8    HZ2  LYS   4           HZ2      LYS   4  -4.083  -3.418  67.417
    9    HZ3  LYS   4           HZ3      LYS   4  -4.019  -2.049  68.187
   10    H    HIS   5           H        HIS   5   1.411  -1.023  67.210
   11    HD1  HIS   5           HD1      HIS   5   5.043   1.427  68.483
   12    H    SER   6           H        SER   6   2.555  -2.814  65.889
   13    HG   SER   6           HG       SER   6   6.059  -3.400  66.705
   14    H    ILE   7           H        ILE   7   3.681  -6.276  63.527
   15    H    SER   8           H        SER   8   2.947  -7.541  66.041
   16    HG   SER   8           HG       SER   8   3.189 -10.277  67.267
   17    H    ASP   9           H        ASP   9   0.624  -5.781  67.018
   18    H    TYR  10           H        TYR  10  -1.552  -6.917  65.965
   19    HH   TYR  10           HH       TYR  10  -1.984  -1.778  60.473
   20    H    THR  11           H        THR  11  -5.845  -7.463  66.278
   21    HG1  THR  11           HG1      THR  11  -8.003  -7.914  66.963
   22    H    GLU  12           H        GLU  12  -5.849 -11.751  64.729
   23    H    ALA  13           H        ALA  13  -8.353 -11.042  63.195
   24    H    GLU  14           H        GLU  14  -8.367  -8.005  63.259
   25    H    PHE  15           H        PHE  15  -5.878  -7.669  61.736
   26    H    LEU  16           H        LEU  16  -6.424  -8.944  59.363
   27    H    GLN  17           H        GLN  17  -8.488  -7.096  58.643
   28   HE21  GLN  17          HE21      GLN  17  -9.593  -1.761  56.876
   29   HE22  GLN  17          HE22      GLN  17  -8.873  -0.751  58.188
   30    H    LEU  18           H        LEU  18  -6.837  -4.655  58.285
   31    H    VAL  19           H        VAL  19  -5.441  -5.931  55.811
   32    H    THR  20           H        THR  20  -7.677  -6.351  54.026
   33    HG1  THR  20           HG1      THR  20  -9.459  -7.469  54.380
   34    H    THR  21           H        THR  21  -8.348  -3.594  53.588
   35    HG1  THR  21           HG1      THR  21  -9.148  -2.394  54.817
   36    H    ILE  22           H        ILE  22  -6.424  -2.655  52.365
   37    H    CYS  23           H        CYS  23  -6.657  -4.324  50.093
   38    H    ASN  24           H        ASN  24  -8.630  -3.326  48.631
   39   HD21  ASN  24          HD21      ASN  24 -11.380  -4.317  49.513
   40   HD22  ASN  24          HD22      ASN  24 -12.540  -5.354  48.750
   41    H    ALA  25           H        ALA  25  -7.372  -1.360  47.639
   42    H    ASP  26           H        ASP  26  -8.541   0.570  49.354
   43    H    THR  27           H        THR  27  -9.289   4.003  48.627
   44    HG1  THR  27           HG1      THR  27  -5.959   4.174  50.494
   45    H    SER  28           H        SER  28  -8.135   7.755  49.929
   46    HG   SER  28           HG       SER  28  -9.216  10.971  47.045
   47    H    SER  29           H        SER  29  -6.106   8.656  48.690
   48    HG   SER  29           HG       SER  29  -5.477  11.554  46.304
   49    H    GLU  30           H        GLU  30  -3.667   8.175  45.203
   50    H    GLU  31           H        GLU  31  -1.483   9.034  47.160
   51    H    GLU  32           H        GLU  32  -2.240   7.861  49.279
   52    H    LEU  33           H        LEU  33  -2.474   5.407  49.281
   53    H    VAL  34           H        VAL  34   0.230   4.544  48.623
   54    H    LYS  35           H        LYS  35   0.937   4.772  51.462
   55    HZ1  LYS  35           HZ1      LYS  35   3.508  11.186  54.521
   56    HZ2  LYS  35           HZ2      LYS  35   1.989  10.926  53.867
   57    HZ3  LYS  35           HZ3      LYS  35   2.419  10.421  55.480
   58    H    LEU  36           H        LEU  36  -0.454   3.454  52.961
   59    H    VAL  37           H        VAL  37   0.784   1.033  52.014
   60    H    THR  38           H        THR  38   3.298   1.092  52.635
   61    HG1  THR  38           HG1      THR  38   4.938   2.301  52.055
   62    H    HIS  39           H        HIS  39   2.896   1.130  55.558
   63    HD1  HIS  39           HD1      HIS  39   2.985  -0.528  59.900
   64    H    PHE  40           H        PHE  40   1.908  -1.450  55.853
   65    H    GLU  41           H        GLU  41   4.242  -3.117  55.145
   66    H    GLU  42           H        GLU  42   6.376  -2.288  57.055
   67    H    MET  43           H        MET  43   5.214  -3.407  59.302
   68    H    THR  44           H        THR  44   4.929  -5.809  59.286
   69    HG1  THR  44           HG1      THR  44   4.671 -10.314  59.309
   70    H    GLU  45           H        GLU  45   7.330  -6.825  59.334
   71    H    HIS  46           H        HIS  46   7.605  -9.729  57.776
   72    HD1  HIS  46           HD1      HIS  46   8.040 -13.185  54.735
   73    H    SER  48           H        SER  48   9.978 -10.240  51.654
   74    HG   SER  48           HG       SER  48   7.736 -11.376  51.050
   75    H    GLY  49           H        GLY  49   7.558  -8.862  52.161
   76    H    SER  50           H        SER  50   6.150  -5.046  50.394
   77    HG   SER  50           HG       SER  50   6.665  -2.575  48.729
   78    H    ASP  51           H        ASP  51   6.219  -6.699  47.881
   79    H    LEU  52           H        LEU  52   4.513  -8.769  48.360
   80    H    ILE  53           H        ILE  53   2.054  -8.225  48.294
   81    H    TYR  54           H        TYR  54   1.897  -7.087  46.107
   82    HH   TYR  54           HH       TYR  54  -1.559  -1.588  47.309
   83    H    TYR  55           H        TYR  55   2.713  -8.739  44.015
   84    HH   TYR  55           HH       TYR  55   3.048  -3.739  39.169
   85    H    LYS  57           H        LYS  57   2.299 -14.790  44.359
   86    HZ1  LYS  57           HZ1      LYS  57   8.583 -14.696  47.840
   87    HZ2  LYS  57           HZ2      LYS  57   6.973 -14.766  48.254
   88    HZ3  LYS  57           HZ3      LYS  57   7.790 -16.249  47.982
   89    H    GLU  58           H        GLU  58   3.928 -17.931  41.823
   90    H    GLY  59           H        GLY  59  -0.063 -19.873  42.636
   91    H    ASP  60           H        ASP  60   0.741 -19.012  44.634
   92    H    ASP  61           H        ASP  61  -2.912 -18.647  47.559
   93    H    ASP  62           H        ASP  62  -4.117 -15.729  44.720
   94    H    SER  63           H        SER  63  -5.775 -14.100  47.857
   95    HG   SER  63           HG       SER  63  -8.262 -15.286  47.999
   96    H    SER  65           H        SER  65  -8.656 -12.518  51.871
   97    HG   SER  65           HG       SER  65  -9.677 -13.218  54.296
   98    H    GLY  66           H        GLY  66  -6.756 -14.333  51.288
   99    H    ILE  67           H        ILE  67  -4.558 -13.462  51.114
  100    H    VAL  68           H        VAL  68  -4.340 -12.912  53.862
  101    H    ASN  69           H        ASN  69  -4.085 -15.419  54.748
  102   HD21  ASN  69          HD21      ASN  69  -2.999 -20.067  55.325
  103   HD22  ASN  69          HD22      ASN  69  -4.161 -21.202  55.968
  104    H    THR  70           H        THR  70  -1.660 -15.912  54.039
  105    HG1  THR  70           HG1      THR  70  -1.211 -16.819  52.076
  106    H    VAL  71           H        VAL  71  -0.018 -14.517  55.148
  107    H    LYS  72           H        LYS  72  -0.701 -15.531  57.909
  108    HZ1  LYS  72           HZ1      LYS  72  -5.959 -20.454  60.189
  109    HZ2  LYS  72           HZ2      LYS  72  -5.855 -18.794  59.746
  110    HZ3  LYS  72           HZ3      LYS  72  -5.177 -19.830  58.698
  111    H    GLN  73           H        GLN  73   0.800 -18.238  57.543
  112   HE21  GLN  73          HE21      GLN  73  -0.305 -20.068  54.634
  113   HE22  GLN  73          HE22      GLN  73  -0.803 -21.580  53.899
  114    H    TRP  74           H        TRP  74   3.266 -17.785  56.886
  115    HE1  TRP  74           HE1      TRP  74   9.475 -15.575  55.345
  116    H    ARG  75           H        ARG  75   4.244 -16.056  59.485
  117    HE   ARG  75           HE       ARG  75   3.630 -12.970  63.494
  118   HH11  ARG  75          HH12      ARG  75   6.586 -11.752  62.239
  119   HH12  ARG  75          HH11      ARG  75   7.240 -10.972  63.632
  120   HH21  ARG  75          HH22      ARG  75   4.197 -11.630  65.351
  121   HH22  ARG  75          HH21      ARG  75   5.763 -11.067  65.651
  122    H    ALA  76           H        ALA  76   4.118 -18.430  61.212
  123    H    ALA  77           H        ALA  77   5.964 -20.019  60.282
  124    H    ASN  78           H        ASN  78   8.300 -19.217  60.223
  125   HD21  ASN  78          HD21      ASN  78   8.513 -17.925  58.469
  126   HD22  ASN  78          HD22      ASN  78   9.673 -18.588  57.299
  127    H    GLY  79           H        GLY  79   8.432 -19.041  62.905
  128    H    LYS  80           H        LYS  80   7.934 -17.055  63.917
  129    HZ1  LYS  80           HZ1      LYS  80  13.319 -12.140  62.723
  130    HZ2  LYS  80           HZ2      LYS  80  12.080 -11.258  63.363
  131    HZ3  LYS  80           HZ3      LYS  80  12.766 -12.489  64.245
  132    H    SER  81           H        SER  81   7.337 -13.146  66.290
  133    HG   SER  81           HG       SER  81   5.888 -10.236  67.924
  134    H    GLY  82           H        GLY  82   4.822 -13.627  65.591
  135    H    PHE  83           H        PHE  83   0.257 -13.849  65.827
  136    H    LYS  84           H        LYS  84  -2.233 -10.394  67.124
  137    HZ1  LYS  84           HZ1      LYS  84  -3.426  -5.714  73.468
  138    HZ2  LYS  84           HZ2      LYS  84  -2.372  -6.885  72.865
  139    HZ3  LYS  84           HZ3      LYS  84  -2.689  -5.452  71.997
  140    H    GLN  85           H        GLN  85  -2.568 -11.539  71.590
  141   HE21  GLN  85          HE21      GLN  85  -6.832 -15.073  75.044
  142   HE22  GLN  85          HE22      GLN  85  -5.656 -14.952  76.422
  143    H    GLY  86           H        GLY  86  -4.908 -14.379  69.262
  144    H1   MET   1           HT1      MET   1  10.339  30.434  40.329
  145    H2   MET   1           HT2      MET   1  10.740  29.040  39.450
  146    H3   MET   1           HT3      MET   1  10.419  28.869  41.086
  147    H    GLU   2           H        GLU   2   6.562  27.881  40.237
  148    H    SER   3           H        SER   3   8.222  24.016  38.810
  149    HG   SER   3           HG       SER   3  10.246  21.994  35.576
  150    H    LYS   4           H        LYS   4   7.619  24.017  34.309
  151    HZ1  LYS   4           HZ1      LYS   4   6.028  26.028  27.938
  152    HZ2  LYS   4           HZ2      LYS   4   7.636  26.076  28.518
  153    HZ3  LYS   4           HZ3      LYS   4   7.087  24.874  27.481
  154    H    ARG   5           H        ARG   5   5.934  21.667  34.849
  155    HE   ARG   5           HE       ARG   5   6.794  16.396  36.700
  156   HH11  ARG   5          HH12      ARG   5   7.137  17.511  33.436
  157   HH12  ARG   5          HH11      ARG   5   6.986  15.994  32.671
  158   HH21  ARG   5          HH22      ARG   5   7.098  14.154  35.715
  159   HH22  ARG   5          HH21      ARG   5   6.767  14.162  34.091
  160    H    ASN   6           H        ASN   6   3.590  22.210  36.321
  161   HD21  ASN   6          HD21      ASN   6   1.177  23.200  40.497
  162   HD22  ASN   6          HD22      ASN   6  -0.273  22.570  40.782
  163    H    LYS   7           H        LYS   7   0.408  21.914  35.047
  164    HZ1  LYS   7           HZ1      LYS   7   2.864  27.278  30.438
  165    HZ2  LYS   7           HZ2      LYS   7   2.551  28.706  31.431
  166    HZ3  LYS   7           HZ3      LYS   7   3.716  27.527  31.927
  167    H    GLY   9           H        GLY   9  -3.558  21.665  30.095
  168    H    LYS  10           H        LYS  10  -1.868  21.428  25.846
  169    HZ1  LYS  10           HZ1      LYS  10  -5.658  25.021  21.524
  170    HZ2  LYS  10           HZ2      LYS  10  -4.015  24.382  21.282
  171    HZ3  LYS  10           HZ3      LYS  10  -5.396  23.622  20.787
  172    H    ALA  11           H        ALA  11  -3.624  17.514  25.671
  173    H    THR  12           H        THR  12   0.292  15.969  23.813
  174    HG1  THR  12           HG1      THR  12   1.525  17.613  22.441
  175    H    GLY  13           H        GLY  13  -0.448  13.288  20.049
  176    H    LYS  14           H        LYS  14   2.344  10.198  19.637
  177    HZ1  LYS  14           HZ1      LYS  14   2.737   6.604  11.896
  178    HZ2  LYS  14           HZ2      LYS  14   2.987   8.203  12.413
  179    HZ3  LYS  14           HZ3      LYS  14   4.114   7.059  12.994
  180    H    GLY  15           H        GLY  15   3.110   7.894  19.330
  181    H    LYS  16           H        LYS  16   3.597   4.655  21.551
  182    HZ1  LYS  16           HZ1      LYS  16   8.824   2.181  17.152
  183    HZ2  LYS  16           HZ2      LYS  16   7.651   3.209  16.486
  184    HZ3  LYS  16           HZ3      LYS  16   9.239   3.809  16.880
  185    H    VAL  18           H        VAL  18   2.390  -0.590  21.619
  186    H    GLY  19           H        GLY  19   3.582  -4.065  23.939
  187    H    ASP  20           H        ASP  20   0.810  -7.249  24.830
  188    H    LYS  21           H        LYS  21   3.175  -7.660  26.615
  189    HZ1  LYS  21           HZ1      LYS  21   2.852 -13.126  31.008
  190    HZ2  LYS  21           HZ2      LYS  21   4.243 -12.402  31.667
  191    HZ3  LYS  21           HZ3      LYS  21   2.609 -11.725  31.941
  192    H    TRP  22           H        TRP  22   3.524  -5.126  27.810
  193    HE1  TRP  22           HE1      TRP  22  -0.044  -3.029  29.933
  194    H    LEU  23           H        LEU  23   3.849  -4.069  30.587
  195    H    ASP  24           H        ASP  24   6.255  -5.571  31.589
  196    H    ASP  25           H        ASP  25   8.253  -3.675  30.858
  197    H    ALA  26           H        ALA  26   9.135  -2.088  32.081
  198    H    GLY  27           H        GLY  27  11.927  -2.140  33.002
  199    H    LYS  28           H        LYS  28  13.300  -1.344  31.131
  200    HZ1  LYS  28           HZ1      LYS  28  12.495  -8.006  29.560
  201    HZ2  LYS  28           HZ2      LYS  28  12.308  -6.681  28.672
  202    HZ3  LYS  28           HZ3      LYS  28  13.704  -7.707  28.382
  203    H    ASP  29           H        ASP  29  17.438  -0.377  29.765
  204    H    SER  30           H        SER  30  14.876   2.646  28.128
  205    HG   SER  30           HG       SER  30  17.611   5.543  28.210
  206    H    GLY  31           H        GLY  31  13.681   2.182  29.544
  207    H    ALA  32           H        ALA  32   9.400   1.938  29.849
  208    H    ILE  34           H        ILE  34   5.288   6.076  26.044
  209    H    ASP  36           H        ASP  36   0.956   2.878  21.403
  210    H    ARG  37           H        ARG  37  -1.969   2.367  22.181
  211    HE   ARG  37           HE       ARG  37  -4.827  -1.661  23.198
  212   HH11  ARG  37          HH12      ARG  37  -2.343  -1.631  20.870
  213   HH12  ARG  37          HH11      ARG  37  -1.344  -2.830  21.736
  214   HH21  ARG  37          HH22      ARG  37  -3.579  -3.023  24.251
  215   HH22  ARG  37          HH21      ARG  37  -2.029  -3.654  23.762
  216    H    ILE  38           H        ILE  38  -2.536   3.767  24.137
  217    H    ALA  39           H        ALA  39  -1.968   6.144  23.725
  218    H    ASP  40           H        ASP  40  -3.930   6.438  21.313
  219    H    LYS  41           H        LYS  41  -6.172   7.224  23.020
  220    HZ1  LYS  41           HZ1      LYS  41  -8.478   2.926  21.931
  221    HZ2  LYS  41           HZ2      LYS  41  -8.239   4.588  21.323
  222    HZ3  LYS  41           HZ3      LYS  41  -7.751   4.115  22.820
  223    H    LEU  42           H        LEU  42  -5.559   9.989  23.334
  224    H    ARG  43           H        ARG  43  -6.420  11.749  22.209
  225    HE   ARG  43           HE       ARG  43  -3.140  12.414  17.633
  226   HH11  ARG  43          HH12      ARG  43  -5.529   9.841  17.022
  227   HH12  ARG  43          HH11      ARG  43  -4.340   8.623  17.171
  228   HH21  ARG  43          HH22      ARG  43  -1.672  10.634  18.016
  229   HH22  ARG  43          HH21      ARG  43  -2.215   9.026  17.928
  230    H    ASP  44           H        ASP  44  -4.513  15.173  22.245
  231    H    LYS  45           H        LYS  45  -6.467  15.470  24.034
  232    HZ1  LYS  45           HZ1      LYS  45 -11.062  11.154  25.976
  233    HZ2  LYS  45           HZ2      LYS  45  -9.595  11.513  25.329
  234    HZ3  LYS  45           HZ3      LYS  45  -9.841  11.916  26.950
  235    H    GLU  46           H        GLU  46  -8.721  18.548  26.536
  236    H    PHE  47           H        PHE  47  -5.164  19.459  29.028
  237    H    LYS  48           H        LYS  48  -5.731  18.698  33.257
  238    HZ1  LYS  48           HZ1      LYS  48  -9.883  18.122  37.661
  239    HZ2  LYS  48           HZ2      LYS  48  -9.598  19.691  38.244
  240    HZ3  LYS  48           HZ3      LYS  48 -10.790  19.336  37.034
  241    H    SER  49           H        SER  49  -3.683  18.545  34.316
  242    HG   SER  49           HG       SER  49  -3.003  18.131  38.249
  243    H    PHE  50           H        PHE  50   0.623  18.314  34.895
  244    H    ASP  51           H        ASP  51  -0.214  16.206  37.178
  245    H    ASP  52           H        ASP  52  -2.859  15.841  36.263
  246    H    PHE  53           H        PHE  53  -2.650  14.908  34.120
  247    H    ARG  54           H        ARG  54  -1.456  12.610  34.493
  248    HE   ARG  54           HE       ARG  54   0.147  10.962  38.945
  249   HH11  ARG  54          HH12      ARG  54  -0.732   7.717  38.314
  250   HH12  ARG  54          HH11      ARG  54  -2.314   7.650  38.897
  251   HH21  ARG  54          HH22      ARG  54  -1.836  11.114  40.121
  252   HH22  ARG  54          HH21      ARG  54  -2.981   9.838  40.113
  253    H    LYS  55           H        LYS  55  -3.268  10.951  36.099
  254    HZ1  LYS  55           HZ1      LYS  55  -9.248  14.023  38.492
  255    HZ2  LYS  55           HZ2      LYS  55  -7.602  14.282  38.876
  256    HZ3  LYS  55           HZ3      LYS  55  -8.042  14.030  37.202
  257    H    ALA  56           H        ALA  56  -5.566  10.603  33.689
  258    H    VAL  57           H        VAL  57  -3.733   9.026  31.738
  259    H    TRP  58           H        TRP  58  -2.951   6.591  33.498
  260    HE1  TRP  58           HE1      TRP  58   1.013   5.970  36.722
  261    H    GLU  59           H        GLU  59  -5.777   5.792  33.492
  262    H    GLU  60           H        GLU  60  -6.436   5.121  31.316
  263    H    VAL  61           H        VAL  61  -4.829   2.938  30.683
  264    H    SER  62           H        SER  62  -6.600   0.898  32.674
  265    HG   SER  62           HG       SER  62  -9.047   1.325  33.545
  266    H    LYS  63           H        LYS  63  -8.624   0.924  30.841
  267    HZ1  LYS  63           HZ1      LYS  63 -10.800   6.355  29.835
  268    HZ2  LYS  63           HZ2      LYS  63 -11.546   5.405  28.664
  269    HZ3  LYS  63           HZ3      LYS  63 -12.544   5.976  29.837
  270    H    ASP  64           H        ASP  64  -7.909  -0.437  28.931
  271    H    GLU  66           H        GLU  66  -6.050  -4.602  26.212
  272    H    LEU  67           H        LEU  67  -4.556  -3.852  27.753
  273    H    SER  68           H        SER  68  -4.885  -3.599  30.407
  274    HG   SER  68           HG       SER  68  -6.681  -3.126  31.500
  275    H    LYS  69           H        LYS  69  -3.808  -6.150  30.702
  276    HZ1  LYS  69           HZ1      LYS  69  -4.161 -10.089  25.387
  277    HZ2  LYS  69           HZ2      LYS  69  -3.259 -11.134  26.468
  278    HZ3  LYS  69           HZ3      LYS  69  -4.781 -11.424  25.819
  279    H    ASN  70           H        ASN  70  -1.733  -7.669  32.145
  280   HD21  ASN  70          HD21      ASN  70   0.886  -8.517  30.683
  281   HD22  ASN  70          HD22      ASN  70   0.993 -10.230  30.262
  282    H    LEU  71           H        LEU  71  -2.783  -7.500  34.651
  283    H    ASN  72           H        ASN  72  -2.299  -7.682  39.075
  284   HD21  ASN  72          HD21      ASN  72  -2.444  -9.907  43.060
  285   HD22  ASN  72          HD22      ASN  72  -2.054  -8.465  43.660
  286    H    SER  74           H        SER  74  -5.614  -7.040  43.068
  287    HG   SER  74           HG       SER  74  -4.439  -3.535  45.291
  288    H    ASN  75           H        ASN  75  -3.716  -5.314  41.706
  289   HD21  ASN  75          HD21      ASN  75  -0.797  -5.965  40.728
  290   HD22  ASN  75          HD22      ASN  75   0.649  -5.124  41.249
  291    H    LYS  76           H        LYS  76  -5.277  -4.832  39.801
  292    HZ1  LYS  76           HZ1      LYS  76  -5.782  -8.477  34.094
  293    HZ2  LYS  76           HZ2      LYS  76  -5.294  -7.001  34.576
  294    HZ3  LYS  76           HZ3      LYS  76  -5.181  -8.339  35.606
  295    H    SER  77           H        SER  77  -7.703  -3.490  41.039
  296    HG   SER  77           HG       SER  77  -9.104  -3.879  42.952
  297    H    SER  78           H        SER  78  -6.180  -1.151  41.542
  298    HG   SER  78           HG       SER  78  -4.400  -0.952  42.636
  299    H    VAL  79           H        VAL  79  -5.316  -0.083  38.947
  300    H    SER  80           H        SER  80  -7.855   0.378  37.777
  301    HG   SER  80           HG       SER  80  -9.560  -0.632  38.477
  302    H    LYS  81           H        LYS  81  -8.450   2.646  39.402
  303    HZ1  LYS  81           HZ1      LYS  81 -10.466   0.746  45.094
  304    HZ2  LYS  81           HZ2      LYS  81 -10.103   2.264  45.407
  305    HZ3  LYS  81           HZ3      LYS  81 -11.660   1.957  45.090
  306    H    GLY  82           H        GLY  82  -7.278   4.526  37.905
  307    H    TYR  83           H        TYR  83  -5.378   4.765  39.607
  308    HH   TYR  83           HH       TYR  83  -6.632   9.553  44.481
  309    H    SER  84           H        SER  84  -0.803   5.509  40.027
  310    HG   SER  84           HG       SER  84   2.519   5.797  38.706
  311    H    PHE  86           H        PHE  86   1.621  -1.915  40.780
  312    H    THR  87           H        THR  87   5.740  -1.743  42.522
  313    HG1  THR  87           HG1      THR  87   7.428  -0.460  41.877
  314    H    LYS  89           H        LYS  89   9.724  -7.775  43.581
  315    HZ1  LYS  89           HZ1      LYS  89   9.700  -4.652  50.662
  316    HZ2  LYS  89           HZ2      LYS  89   8.628  -4.160  49.387
  317    HZ3  LYS  89           HZ3      LYS  89   8.741  -5.757  49.871
  318    H    ASN  90           H        ASN  90  12.110  -7.017  42.444
  319   HD21  ASN  90          HD21      ASN  90  14.857  -7.951  38.872
  320   HD22  ASN  90          HD22      ASN  90  13.316  -8.281  38.408
  321    H    GLN  91           H        GLN  91  11.816  -4.110  42.712
  322   HE21  GLN  91          HE21      GLN  91  14.559  -3.708  39.569
  323   HE22  GLN  91          HE22      GLN  91  15.239  -2.646  38.408
  324    H    GLN  92           H        GLN  92  11.049  -2.783  43.870
  325   HE21  GLN  92          HE21      GLN  92   6.526  -3.809  44.742
  326   HE22  GLN  92          HE22      GLN  92   6.068  -3.832  46.445
  327    H    VAL  93           H        VAL  93  11.504   1.521  44.925
  328    H    GLY  94           H        GLY  94  12.677   0.282  48.056
  329    H    GLY  95           H        GLY  95  12.061   4.160  48.961
  330    H    ARG  96           H        ARG  96  10.901   4.355  47.106
  331    HE   ARG  96           HE       ARG  96  10.454   7.779  41.831
  332   HH11  ARG  96          HH12      ARG  96  13.330   8.857  43.247
  333   HH12  ARG  96          HH11      ARG  96  13.203  10.509  42.879
  334   HH21  ARG  96          HH22      ARG  96  10.006   9.965  41.370
  335   HH22  ARG  96          HH21      ARG  96  11.119  11.232  41.830
  336    H    LYS  97           H        LYS  97   7.097   3.754  45.758
  337    HZ1  LYS  97           HZ1      LYS  97   6.842   1.840  51.149
  338    HZ2  LYS  97           HZ2      LYS  97   8.447   1.582  50.456
  339    HZ3  LYS  97           HZ3      LYS  97   7.207   2.351  49.674
  340    H    VAL  98           H        VAL  98   5.726   3.562  43.931
  341    H    TYR  99           H        TYR  99   4.252   2.013  39.700
  342    HH   TYR  99           HH       TYR  99   6.589  -2.883  35.147
  343    H    GLU 100           H        GLU 100   7.051   4.715  37.006
  344    H    LEU 101           H        LEU 101   5.471   8.723  35.849
  345    H    HIS 102           H        HIS 102   8.203   8.482  32.525
  346    HD1  HIS 102           HD1      HIS 102  12.375  10.673  34.780
  347    H    HIS 103           H        HIS 103  11.678  11.161  31.685
  348    HD1  HIS 103           HD1      HIS 103   8.252  12.177  29.509
  349    H    ASP 104           H        ASP 104  11.595  11.771  27.370
  350    H    LYS 105           H        LYS 105  12.984  13.799  26.635
  351    HZ1  LYS 105           HZ1      LYS 105  15.425  19.950  24.282
  352    HZ2  LYS 105           HZ2      LYS 105  14.993  19.366  22.738
  353    HZ3  LYS 105           HZ3      LYS 105  13.862  19.265  23.906
  354    H    ILE 107           H        ILE 107  13.324  17.864  31.652
  355    H    SER 108           H        SER 108  14.497  20.620  32.147
  356    HG   SER 108           HG       SER 108  16.639  21.073  33.862
  357    H    GLN 109           H        GLN 109  15.720  20.783  29.395
  358   HE21  GLN 109          HE21      GLN 109  20.521  19.256  25.439
  359   HE22  GLN 109          HE22      GLN 109  21.816  19.393  26.556
  360    H    GLY 110           H        GLY 110  14.155  22.265  27.649
  361    H    GLY 111           H        GLY 111  12.523  20.483  27.733
  362    H    GLU 112           H        GLU 112   9.968  18.067  24.898
  363    H    VAL 113           H        VAL 113   7.102  18.986  27.931
  364    H    TYR 114           H        TYR 114   3.868  18.422  28.034
  365    HH   TYR 114           HH       TYR 114  -0.117  20.391  32.868
  366    H    ASP 115           H        ASP 115   4.349  15.412  26.214
  367    H    MET 116           H        MET 116   2.478  12.996  23.591
  368    H    ASP 117           H        ASP 117   4.520  11.442  22.374
  369    H    ASN 118           H        ASN 118   6.727  11.827  24.259
  370   HD21  ASN 118          HD21      ASN 118   8.655  15.068  26.569
  371   HD22  ASN 118          HD22      ASN 118  10.247  14.982  27.348
  372    H    ILE 119           H        ILE 119   6.755  10.005  25.974
  373    H    ARG 120           H        ARG 120   8.398   8.741  29.466
  374    HE   ARG 120           HE       ARG 120  11.101   4.524  27.408
  375   HH11  ARG 120          HH12      ARG 120  13.005   7.207  25.713
  376   HH12  ARG 120          HH11      ARG 120  14.191   6.197  25.513
  377   HH21  ARG 120          HH22      ARG 120  12.749   3.202  26.613
  378   HH22  ARG 120          HH21      ARG 120  14.187   3.900  25.964
  379    H    VAL 121           H        VAL 121   7.307   4.559  29.652
  380    H    THR 122           H        THR 122   7.812   4.725  34.081
  381    HG1  THR 122           HG1      THR 122   9.174   6.058  34.513
  382    H    THR 123           H        THR 123  10.722   1.671  35.430
  383    HG1  THR 123           HG1      THR 123  12.396  -0.220  36.504
  384    H    LYS 125           H        LYS 125  12.903   1.611  40.167
  385    HZ1  LYS 125           HZ1      LYS 125  20.554   0.026  39.425
  386    HZ2  LYS 125           HZ2      LYS 125  19.111   0.367  38.572
  387    HZ3  LYS 125           HZ3      LYS 125  19.687   1.522  39.662
  388    H    ARG 126           H        ARG 126  13.698   2.348  37.551
  389    HE   ARG 126           HE       ARG 126  16.576   3.261  32.094
  390   HH11  ARG 126          HH12      ARG 126  18.211   1.284  34.467
  391   HH12  ARG 126          HH11      ARG 126  19.681   1.330  33.603
  392   HH21  ARG 126          HH22      ARG 126  18.609   2.911  30.775
  393   HH22  ARG 126          HH21      ARG 126  19.764   1.742  31.350
  394    H    HIS 127           H        HIS 127  12.912   5.156  37.337
  395    HD1  HIS 127           HD1      HIS 127  11.767   9.577  40.080
  396    H    ILE 128           H        ILE 128  14.511   6.369  39.457
  397    H    ASP 129           H        ASP 129  17.200   5.419  38.492
  398    H    ILE 130           H        ILE 130  17.345   7.361  35.857
  399    H    HIS 131           H        HIS 131  17.141   9.613  36.752
  400    HD1  HIS 131           HD1      HIS 131  17.082  14.079  35.671
  401    H    ARG 132           H        ARG 132  19.669   9.651  38.012
  402    HE   ARG 132           HE       ARG 132  25.008   9.691  35.799
  403   HH11  ARG 132          HH12      ARG 132  21.584   8.515  35.659
  404   HH12  ARG 132          HH11      ARG 132  21.710   8.066  34.062
  405   HH21  ARG 132          HH22      ARG 132  24.989   9.218  33.721
  406   HH22  ARG 132          HH21      ARG 132  23.698   8.249  32.921
  407    H    GLY 133           H        GLY 133  19.502   9.038  40.707
  408    H    LYS 134           H        LYS 134  18.847  11.985  42.114
  409    HZ1  LYS 134           HZ1      LYS 134  19.429  16.818  46.321
  410    HZ2  LYS 134           HZ2      LYS 134  18.309  17.601  45.273
  411    HZ3  LYS 134           HZ3      LYS 134  17.783  16.240  45.997