*HEADER    PROTEIN BINDING/ENDOCYTOSIS             18-DEC-09   2KRI              
*TITLE     STRUCTURE OF A COMPLEX BETWEEN DOMAIN V OF BETA2-                     
*TITLE    2 GLYCOPROTEIN I AND THE FOURTH LIGAND-BINDING MODULE FROM             
*TITLE    3 LDLR DETERMINED WITH HADDOCK                                         
*COMPND    MOL_ID: 1;                                                            
*COMPND   2 MOLECULE: BETA-2-GLYCOPROTEIN 1;                                     
*COMPND   3 CHAIN: A;                                                            
*COMPND   4 FRAGMENT: SUSHI-LIKE DOMAIN;                                         
*COMPND   5 SYNONYM: BETA-2-GLYCOPROTEIN I, BETA(2)GPI, B2GPI,                   
*COMPND   6 APOLIPOPROTEIN H, APO-H, ACTIVATED PROTEIN C-BINDING                 
*COMPND   7 PROTEIN, APC INHIBITOR, ANTICARDIOLIPIN COFACTOR;                    
*COMPND   8 ENGINEERED: YES;                                                     
*COMPND   9 MOL_ID: 2;                                                           
*COMPND  10 MOLECULE: LOW-DENSITY LIPOPROTEIN RECEPTOR;                          
*COMPND  11 CHAIN: B;                                                            
*COMPND  12 FRAGMENT: LDL-RECEPTOR CLASS A 4 DOMAIN;                             
*COMPND  13 SYNONYM: LDL RECEPTOR;                                               
*COMPND  14 ENGINEERED: YES                                                      
*SOURCE    MOL_ID: 1;                                                            
*SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
*SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
*SOURCE   4 ORGANISM_TAXID: 9606;                                                
*SOURCE   5 GENE: APOH, B2G1;                                                    
*SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
*SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
*SOURCE   8 EXPRESSION_SYSTEM_VECTOR: PET 15;                                    
*SOURCE   9 MOL_ID: 2;                                                           
*SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
*SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
*SOURCE  12 ORGANISM_TAXID: 9606;                                                
*SOURCE  13 GENE: LDLR;                                                          
*SOURCE  14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
*SOURCE  15 EXPRESSION_SYSTEM_TAXID: 562;                                        
*SOURCE  16 EXPRESSION_SYSTEM_VECTOR: PMM                                        
*KEYWDS    ANTIPHOSPHOLIPID SYNDROME, THROMBOSIS, LDLR, RECEPTOR,                
*KEYWDS   2 DISULFIDE BOND, GLYCOPROTEIN, HEPARIN-BINDING, SUSHI,                
*KEYWDS   3 PROTEIN BINDING-ENDOCYTOSIS COMPLEX                                  
*EXPDTA    SOLUTION NMR                                                          
*NUMMDL    1                                                                     
*AUTHOR    N.BEGLOVA                                                             
*REVDAT   1   31-MAR-10 2KRI    0                                                


!
! HADDOCK AIR restraints for 1st molecule
!
!
assign ( resid 251  and segid A)
       (
        ( resid 143  and segid B)
     or
        ( resid 144  and segid B)
     or
        ( resid 149  and segid B)
     or
        ( resid 142  and segid B)
     or
        ( resid 148  and segid B)
     or
        ( resid 150  and segid B)
     or
        ( resid 151  and segid B)
       )  2.0 2.0 0.0
!
assign ( resid 286  and segid A)
       (
        ( resid 143  and segid B)
     or
        ( resid 144  and segid B)
     or
        ( resid 149  and segid B)
     or
        ( resid 142  and segid B)
     or
        ( resid 148  and segid B)
     or
        ( resid 150  and segid B)
     or
        ( resid 151  and segid B)
       )  2.0 2.0 0.0
!
assign ( resid 287  and segid A)
       (
        ( resid 143  and segid B)
     or
        ( resid 144  and segid B)
     or
        ( resid 149  and segid B)
     or
        ( resid 142  and segid B)
     or
        ( resid 148  and segid B)
     or
        ( resid 150  and segid B)
     or
        ( resid 151  and segid B)
       )  2.0 2.0 0.0
!
assign ( resid 305  and segid A)
       (
        ( resid 143  and segid B)
     or
        ( resid 144  and segid B)
     or
        ( resid 149  and segid B)
     or
        ( resid 142  and segid B)
     or
        ( resid 148  and segid B)
     or
        ( resid 150  and segid B)
     or
        ( resid 151  and segid B)
       )  2.0 2.0 0.0
!
assign ( resid 308  and segid A)
       (
        ( resid 143  and segid B)
     or
        ( resid 144  and segid B)
     or
        ( resid 149  and segid B)
     or
        ( resid 142  and segid B)
     or
        ( resid 148  and segid B)
     or
        ( resid 150  and segid B)
     or
        ( resid 151  and segid B)
       )  2.0 2.0 0.0
!
assign ( resid 309  and segid A)
       (
        ( resid 143  and segid B)
     or
        ( resid 144  and segid B)
     or
        ( resid 149  and segid B)
     or
        ( resid 142  and segid B)
     or
        ( resid 148  and segid B)
     or
        ( resid 150  and segid B)
     or
        ( resid 151  and segid B)
       )  2.0 2.0 0.0
!
assign ( resid 316  and segid A)
       (
        ( resid 143  and segid B)
     or
        ( resid 144  and segid B)
     or
        ( resid 149  and segid B)
     or
        ( resid 142  and segid B)
     or
        ( resid 148  and segid B)
     or
        ( resid 150  and segid B)
     or
        ( resid 151  and segid B)
       )  2.0 2.0 0.0
!
assign ( resid 322  and segid A)
       (
        ( resid 143  and segid B)
     or
        ( resid 144  and segid B)
     or
        ( resid 149  and segid B)
     or
        ( resid 142  and segid B)
     or
        ( resid 148  and segid B)
     or
        ( resid 150  and segid B)
     or
        ( resid 151  and segid B)
       )  2.0 2.0 0.0
!
assign ( resid 324  and segid A)
       (
        ( resid 143  and segid B)
     or
        ( resid 144  and segid B)
     or
        ( resid 149  and segid B)
     or
        ( resid 142  and segid B)
     or
        ( resid 148  and segid B)
     or
        ( resid 150  and segid B)
     or
        ( resid 151  and segid B)
       )  2.0 2.0 0.0
!
assign ( resid 326  and segid A)
       (
        ( resid 143  and segid B)
     or
        ( resid 144  and segid B)
     or
        ( resid 149  and segid B)
     or
        ( resid 142  and segid B)
     or
        ( resid 148  and segid B)
     or
        ( resid 150  and segid B)
     or
        ( resid 151  and segid B)
       )  2.0 2.0 0.0
!
! HADDOCK AIR restraints for 2nd molecule
!
!
assign ( resid 143  and segid B)
       (
        ( resid 251  and segid A)
     or
        ( resid 286  and segid A)
     or
        ( resid 287  and segid A)
     or
        ( resid 305  and segid A)
     or
        ( resid 308  and segid A)
     or
        ( resid 309  and segid A)
     or
        ( resid 316  and segid A)
     or
        ( resid 322  and segid A)
     or
        ( resid 324  and segid A)
     or
        ( resid 326  and segid A)
     or
        ( resid 248  and segid A)
     or
        ( resid 250  and segid A)
     or
        ( resid 284  and segid A)
     or
        ( resid 293  and segid A)
     or
        ( resid 302  and segid A)
     or
        ( resid 311  and segid A)
     or
        ( resid 312  and segid A)
     or
        ( resid 313  and segid A)
     or
        ( resid 315  and segid A)
     or
        ( resid 325  and segid A)
       )  2.0 2.0 0.0
!
assign ( resid 144  and segid B)
       (
        ( resid 251  and segid A)
     or
        ( resid 286  and segid A)
     or
        ( resid 287  and segid A)
     or
        ( resid 305  and segid A)
     or
        ( resid 308  and segid A)
     or
        ( resid 309  and segid A)
     or
        ( resid 316  and segid A)
     or
        ( resid 322  and segid A)
     or
        ( resid 324  and segid A)
     or
        ( resid 326  and segid A)
     or
        ( resid 248  and segid A)
     or
        ( resid 250  and segid A)
     or
        ( resid 284  and segid A)
     or
        ( resid 293  and segid A)
     or
        ( resid 302  and segid A)
     or
        ( resid 311  and segid A)
     or
        ( resid 312  and segid A)
     or
        ( resid 313  and segid A)
     or
        ( resid 315  and segid A)
     or
        ( resid 325  and segid A)
       )  2.0 2.0 0.0
!
assign ( resid 149  and segid B)
       (
        ( resid 251  and segid A)
     or
        ( resid 286  and segid A)
     or
        ( resid 287  and segid A)
     or
        ( resid 305  and segid A)
     or
        ( resid 308  and segid A)
     or
        ( resid 309  and segid A)
     or
        ( resid 316  and segid A)
     or
        ( resid 322  and segid A)
     or
        ( resid 324  and segid A)
     or
        ( resid 326  and segid A)
     or
        ( resid 248  and segid A)
     or
        ( resid 250  and segid A)
     or
        ( resid 284  and segid A)
     or
        ( resid 293  and segid A)
     or
        ( resid 302  and segid A)
     or
        ( resid 311  and segid A)
     or
        ( resid 312  and segid A)
     or
        ( resid 313  and segid A)
     or
        ( resid 315  and segid A)
     or
        ( resid 325  and segid A)
       )  2.0 2.0 0.0
!
! HADDOCK AIR restraints for 3rd molecule
!
!
! HADDOCK AIR restraints for 4th molecule
!
!
! HADDOCK AIR restraints for 5th molecule
!
!
! HADDOCK AIR restraints for 6th molecule
!


  Entry H atom name         Submitted Coord H atom name
    1    H    CYS 245           H        CYS 245 -17.908  -9.331   0.319
    2    H    LYS 246           H        LYS 246 -13.959 -10.980   0.430
    3    HZ1  LYS 246           HZ1      LYS 246 -11.139 -16.226   2.423
    4    HZ2  LYS 246           HZ2      LYS 246  -9.676 -15.387   2.276
    5    HZ3  LYS 246           HZ3      LYS 246 -10.810 -15.336   1.023
    6    H    LEU 247           H        LEU 247 -11.928  -9.136   4.093
    7    H    VAL 249           H        VAL 249  -7.794  -5.668   2.372
    8    H    LYS 250           H        LYS 250  -4.017  -5.238   4.804
    9    HZ1  LYS 250           HZ1      LYS 250  -1.233  -9.557   9.074
   10    HZ2  LYS 250           HZ2      LYS 250  -1.775  -8.509  10.287
   11    HZ3  LYS 250           HZ3      LYS 250  -1.216  -7.887   8.816
   12    H    LYS 251           H        LYS 251  -4.124  -3.272   6.370
   13    HZ1  LYS 251           HZ1      LYS 251  -2.932   0.769  12.167
   14    HZ2  LYS 251           HZ2      LYS 251  -1.566  -0.223  12.166
   15    HZ3  LYS 251           HZ3      LYS 251  -3.107  -0.913  12.071
   16    H    ALA 252           H        ALA 252  -6.751  -0.333   6.541
   17    H    THR 253           H        THR 253  -5.674   3.409   4.628
   18    HG1  THR 253           HG1      THR 253  -5.650   5.176   6.096
   19    H    VAL 254           H        VAL 254 -10.037   4.097   3.659
   20    H    VAL 255           H        VAL 255 -10.728   4.711  -0.691
   21    H    TYR 256           H        TYR 256 -14.361   6.125   0.769
   22    HH   TYR 256           HH       TYR 256 -20.904   0.464  -0.548
   23    H    GLN 257           H        GLN 257 -16.843   5.820  -2.506
   24   HE21  GLN 257          HE21      GLN 257 -21.341   6.659   0.220
   25   HE22  GLN 257          HE22      GLN 257 -22.901   5.935   0.061
   26    H    GLY 258           H        GLY 258 -15.881   8.142  -1.846
   27    H    GLU 259           H        GLU 259 -16.532   8.666   0.630
   28    H    ARG 260           H        ARG 260 -13.647   9.996   3.940
   29    HE   ARG 260           HE       ARG 260  -8.585  10.295   5.282
   30   HH11  ARG 260          HH11      ARG 260  -6.211  11.100   2.829
   31   HH12  ARG 260          HH12      ARG 260  -4.852  10.741   3.852
   32   HH21  ARG 260          HH21      ARG 260  -6.799   9.864   6.634
   33   HH22  ARG 260          HH22      ARG 260  -5.190  10.048   6.013
   34    H    VAL 261           H        VAL 261 -12.666   6.470   4.128
   35    H    LYS 262           H        LYS 262 -11.484   4.364   7.885
   36    HZ1  LYS 262           HZ1      LYS 262  -9.440   4.059  12.613
   37    HZ2  LYS 262           HZ2      LYS 262 -10.258   4.228  11.141
   38    HZ3  LYS 262           HZ3      LYS 262  -9.515   5.570  11.861
   39    H    ILE 263           H        ILE 263 -10.237   0.984   5.111
   40    H    GLN 264           H        GLN 264 -10.621  -0.753   7.046
   41   HE21  GLN 264          HE21      GLN 264  -8.241  -4.195   6.253
   42   HE22  GLN 264          HE22      GLN 264  -7.715  -2.786   5.404
   43    H    GLU 265           H        GLU 265 -12.784   0.002   8.225
   44    H    LYS 266           H        LYS 266 -14.541   0.888   7.384
   45    HZ1  LYS 266           HZ1      LYS 266 -19.105   5.503   6.517
   46    HZ2  LYS 266           HZ2      LYS 266 -20.557   4.933   5.860
   47    HZ3  LYS 266           HZ3      LYS 266 -19.711   6.184   5.085
   48    H    PHE 267           H        PHE 267 -15.208  -1.336   6.335
   49    H    LYS 268           H        LYS 268 -16.617  -2.886   8.099
   50    HZ1  LYS 268           HZ1      LYS 268 -18.322  -1.715  14.081
   51    HZ2  LYS 268           HZ2      LYS 268 -18.728  -3.314  14.457
   52    HZ3  LYS 268           HZ3      LYS 268 -19.943  -2.203  14.075
   53    H    ASN 269           H        ASN 269 -18.001  -5.032   7.575
   54   HD21  ASN 269          HD21      ASN 269 -22.146  -6.040   9.319
   55   HD22  ASN 269          HD22      ASN 269 -22.396  -7.505  10.204
   56    H    GLY 270           H        GLY 270 -16.984  -6.291   5.996
   57    H    MET 271           H        MET 271 -16.656  -7.163   1.812
   58    H    LEU 272           H        LEU 272 -19.776  -4.376  -0.001
   59    H    HIS 273           H        HIS 273 -22.204  -7.119  -2.734
   60    HD1  HIS 273           HD1      HIS 273 -24.217  -6.826  -6.863
   61    HE2  HIS 273           HE2      HIS 273 -21.994  -8.612  -9.660
   62    H    GLY 274           H        GLY 274 -19.577  -5.373  -5.761
   63    H    ASP 275           H        ASP 275 -19.677  -3.630  -4.209
   64    H    LYS 276           H        LYS 276 -18.425   0.690  -4.508
   65    HZ1  LYS 276           HZ1      LYS 276 -17.124   2.848 -12.060
   66    HZ2  LYS 276           HZ2      LYS 276 -17.272   4.028 -10.857
   67    HZ3  LYS 276           HZ3      LYS 276 -18.473   2.855 -11.041
   68    H    VAL 277           H        VAL 277 -13.954   0.534  -4.886
   69    H    SER 278           H        SER 278 -12.211   3.870  -3.150
   70    HG   SER 278           HG       SER 278 -11.861   4.357  -5.881
   71    H    PHE 279           H        PHE 279  -7.982   2.701  -4.200
   72    H    PHE 280           H        PHE 280  -5.464   3.955  -0.629
   73    H    CYS 281           H        CYS 281  -2.652   6.244  -3.333
   74    H    LYS 282           H        LYS 282   1.489   4.758  -2.780
   75    HZ1  LYS 282           HZ1      LYS 282   7.682   6.148  -0.254
   76    HZ2  LYS 282           HZ2      LYS 282   7.445   4.504   0.058
   77    HZ3  LYS 282           HZ3      LYS 282   7.424   5.624   1.339
   78    H    ASN 283           H        ASN 283   2.914   8.768  -3.929
   79   HD21  ASN 283          HD21      ASN 283   2.813  10.465  -8.251
   80   HD22  ASN 283          HD22      ASN 283   4.145  10.402  -9.354
   81    H    LYS 284           H        LYS 284   6.322   6.837  -5.884
   82    HZ1  LYS 284           HZ1      LYS 284   9.408   3.402  -9.457
   83    HZ2  LYS 284           HZ2      LYS 284   9.231   4.976  -8.857
   84    HZ3  LYS 284           HZ3      LYS 284   7.978   3.849  -8.673
   85    H    GLU 285           H        GLU 285   7.476   8.823  -6.971
   86    H    LYS 286           H        LYS 286   6.795  11.036  -7.058
   87    HZ1  LYS 286           HZ1      LYS 286   5.400  15.532 -11.525
   88    HZ2  LYS 286           HZ2      LYS 286   5.720  14.450 -12.781
   89    HZ3  LYS 286           HZ3      LYS 286   6.660  14.417 -11.379
   90    H    LYS 287           H        LYS 287   6.977  11.350  -4.763
   91    HZ1  LYS 287           HZ1      LYS 287  10.383  15.722  -0.028
   92    HZ2  LYS 287           HZ2      LYS 287  11.266  14.553   0.811
   93    HZ3  LYS 287           HZ3      LYS 287   9.857  15.204   1.492
   94    H    CYS 288           H        CYS 288   4.411  11.627  -4.073
   95    H    SER 289           H        SER 289   0.255  12.384  -2.740
   96    HG   SER 289           HG       SER 289  -1.466  11.551  -0.219
   97    H    TYR 290           H        TYR 290  -1.259   8.492  -4.289
   98    HH   TYR 290           HH       TYR 290   1.634   4.742  -8.729
   99    H    THR 291           H        THR 291  -4.892   8.537  -6.794
  100    HG1  THR 291           HG1      THR 291  -6.350   9.227  -5.879
  101    H    GLU 292           H        GLU 292  -5.761   4.416  -5.633
  102    H    ASP 293           H        ASP 293  -8.275   3.294  -9.029
  103    H    ALA 294           H        ALA 294 -11.524   1.059  -6.677
  104    H    GLN 295           H        GLN 295 -12.492  -3.096  -7.504
  105   HE21  GLN 295          HE21      GLN 295 -18.972  -1.042  -7.945
  106   HE22  GLN 295          HE22      GLN 295 -19.221  -0.808  -9.643
  107    H    CYS 296           H        CYS 296 -16.088  -3.819  -5.293
  108    H    ILE 297           H        ILE 297 -15.279  -7.670  -7.106
  109    H    ASP 298           H        ASP 298 -18.789  -8.801  -6.700
  110    H    GLY 299           H        GLY 299 -17.537 -10.483  -4.444
  111    H    THR 300           H        THR 300 -15.200 -11.605  -6.424
  112    HG1  THR 300           HG1      THR 300 -13.937 -12.963  -8.522
  113    H    ILE 301           H        ILE 301 -11.208  -9.638  -5.475
  114    H    GLU 302           H        GLU 302 -10.600  -5.934  -7.514
  115    H    VAL 303           H        VAL 303  -6.431  -6.595  -6.194
  116    H    LYS 305           H        LYS 305  -2.424  -1.238  -8.132
  117    HZ1  LYS 305           HZ1      LYS 305  -2.364  -0.513 -11.439
  118    HZ2  LYS 305           HZ2      LYS 305  -3.392  -1.213 -10.292
  119    HZ3  LYS 305           HZ3      LYS 305  -3.979  -0.819 -11.825
  120    H    CYS 306           H        CYS 306  -1.192   0.139  -6.771
  121    H    PHE 307           H        PHE 307  -0.799  -0.267  -4.693
  122    H    LYS 308           H        LYS 308   1.077   1.191  -1.037
  123    HZ1  LYS 308           HZ1      LYS 308   7.754   1.634   0.467
  124    HZ2  LYS 308           HZ2      LYS 308   7.883   0.377   1.607
  125    HZ3  LYS 308           HZ3      LYS 308   7.297   1.898   2.078
  126    H    GLU 309           H        GLU 309   1.347  -2.529   0.964
  127    H    HIS 310           H        HIS 310   0.570  -0.958   5.239
  128    HD1  HIS 310           HD1      HIS 310   1.305   2.616   4.692
  129    HE2  HIS 310           HE2      HIS 310   5.152   3.136   3.719
  130    H    SER 311           H        SER 311   3.803  -2.733   6.988
  131    HG   SER 311           HG       SER 311   3.849  -6.295   9.577
  132    H    SER 312           H        SER 312   1.500  -3.806  10.803
  133    HG   SER 312           HG       SER 312  -1.096  -3.297  12.311
  134    H    LEU 313           H        LEU 313   3.896  -4.071  11.757
  135    H    ALA 314           H        ALA 314   5.206  -1.980  12.477
  136    H    PHE 315           H        PHE 315   5.804  -0.316  10.567
  137    H    TRP 316           H        TRP 316   7.745   1.730  10.504
  138    HE1  TRP 316           HE1      TRP 316  10.439  -0.365   8.278
  139    H    LYS 317           H        LYS 317   6.714   4.312   9.266
  140    HZ1  LYS 317           HZ1      LYS 317   9.798  -0.055   5.526
  141    HZ2  LYS 317           HZ2      LYS 317   8.743  -0.274   4.214
  142    HZ3  LYS 317           HZ3      LYS 317   8.612  -1.260   5.587
  143    H    THR 318           H        THR 318   6.958   7.208   6.024
  144    HG1  THR 318           HG1      THR 318   6.500   9.200   6.608
  145    H    ASP 319           H        ASP 319   2.419   7.178   6.546
  146    H    ALA 320           H        ALA 320   0.578   4.579   3.224
  147    H    SER 321           H        SER 321  -1.641   5.962   3.564
  148    HG   SER 321           HG       SER 321  -3.054   5.098   4.515
  149    H    ASP 322           H        ASP 322  -0.664   8.225   4.081
  150    H    VAL 323           H        VAL 323   0.059   9.750   2.797
  151    H    LYS 324           H        LYS 324   1.582  13.874   1.421
  152    HZ1  LYS 324           HZ1      LYS 324   2.993  17.766  -3.551
  153    HZ2  LYS 324           HZ2      LYS 324   4.649  17.436  -3.488
  154    HZ3  LYS 324           HZ3      LYS 324   4.001  18.675  -2.541
  155    H    CYS 326           H        CYS 326  -1.514  13.257  -4.801
  156    H1   THR 126           H1       THR 126   9.883 -17.468  -0.145
  157    H2   THR 126           H2       THR 126  11.210 -16.888  -1.012
  158    H3   THR 126           H3       THR 126   9.732 -17.142  -1.793
  159    HG1  THR 126           HG1      THR 126  10.248 -16.138   2.469
  160    H    CYS 127           H        CYS 127  11.232 -15.901  -2.650
  161    H    GLY 128           H        GLY 128   9.877 -13.009  -5.045
  162    H    ALA 130           H        ALA 130   8.150 -11.237  -8.351
  163    H    SER 131           H        SER 131  10.228 -10.079  -7.153
  164    HG   SER 131           HG       SER 131   8.545 -10.727  -4.871
  165    H    PHE 132           H        PHE 132  11.639  -7.708  -3.687
  166    H    GLN 133           H        GLN 133  15.898  -8.440  -4.438
  167   HE21  GLN 133          HE21      GLN 133  18.135 -13.485  -1.115
  168   HE22  GLN 133          HE22      GLN 133  19.293 -14.092  -2.246
  169    H    CYS 134           H        CYS 134  16.326  -8.180  -0.105
  170    H    ASN 135           H        ASN 135  19.855  -5.540   1.173
  171   HD21  ASN 135          HD21      ASN 135  24.708  -6.686   1.667
  172   HD22  ASN 135          HD22      ASN 135  25.291  -6.110   0.144
  173    H    SER 136           H        SER 136  19.515  -7.139   3.053
  174    HG   SER 136           HG       SER 136  17.054  -7.479   4.962
  175    H    SER 137           H        SER 137  19.762  -9.583   2.241
  176    HG   SER 137           HG       SER 137  21.415 -12.313   3.960
  177    H    THR 138           H        THR 138  17.308  -9.910   3.172
  178    HG1  THR 138           HG1      THR 138  15.640  -9.015   5.687
  179    H    CYS 139           H        CYS 139  13.086 -11.112   1.825
  180    H    ILE 140           H        ILE 140  12.283  -7.856  -0.889
  181    H    GLN 142           H        GLN 142   8.234  -6.326  -5.542
  182   HE21  GLN 142          HE21      GLN 142  11.840  -4.667 -10.444
  183   HE22  GLN 142          HE22      GLN 142  10.701  -4.864 -11.729
  184    H    LEU 143           H        LEU 143   7.163  -3.870  -5.413
  185    H    TRP 144           H        TRP 144   8.667  -2.638  -3.654
  186    HE1  TRP 144           HE1      TRP 144   4.293  -2.524  -1.072
  187    H    ALA 145           H        ALA 145  10.491  -1.514  -4.300
  188    H    CYS 146           H        CYS 146  13.779   0.984  -2.746
  189    H    ASP 147           H        ASP 147  11.932   3.171  -2.006
  190    H    ASN 148           H        ASN 148  12.172   5.223  -1.460
  191   HD21  ASN 148          HD21      ASN 148  10.924   8.747  -2.999
  192   HD22  ASN 148          HD22      ASN 148  12.325   9.758  -2.975
  193    H    ASP 149           H        ASP 149  11.545   4.393   0.826
  194    H    ASP 151           H        ASP 151  12.881   0.036   3.177
  195    H    CYS 152           H        CYS 152  13.903  -1.981   3.239
  196    H    GLU 153           H        GLU 153  15.400  -5.279   6.127
  197    H    ASP 154           H        ASP 154  17.918  -4.110   6.123
  198    H    GLY 155           H        GLY 155  17.210  -1.961   5.561
  199    H    SER 156           H        SER 156  18.437  -2.185   3.178
  200    HG   SER 156           HG       SER 156  19.208  -3.954   2.664
  201    H    ASP 157           H        ASP 157  16.726  -1.408   1.389
  202    H    GLU 158           H        GLU 158  16.957   0.956   0.858
  203    H    TRP 159           H        TRP 159  18.547   1.598  -0.832
  204    HE1  TRP 159           HE1      TRP 159  25.089   3.963   0.243
  205    H    GLN 161           H        GLN 161  23.070   3.667  -2.807
  206   HE21  GLN 161          HE21      GLN 161  26.266   6.202  -3.444
  207   HE22  GLN 161          HE22      GLN 161  26.976   6.272  -5.018
  208    H    ARG 162           H        ARG 162  21.647   1.948  -4.222
  209    HE   ARG 162           HE       ARG 162  20.739  -3.370  -4.439
  210   HH11  ARG 162          HH11      ARG 162  21.877  -5.072  -1.603
  211   HH12  ARG 162          HH12      ARG 162  20.834  -6.439  -1.851
  212   HH21  ARG 162          HH21      ARG 162  19.349  -5.142  -4.754
  213   HH22  ARG 162          HH22      ARG 162  19.357  -6.461  -3.622
  214    H    CYS 163           H        CYS 163  20.738   2.249  -6.184