******************************** This file contains the results of the mutational analysis. The first column shows the user-specified residues to be mutated while the second column shows the target mutation. The last column shows the magnitude of change in scores of the protein complexes upon mutagenesis Positive values indicate the mutation is destabilising whereas Negative values indicate the mutation is stabilising ******************************** Residue number Residue chain Residue type Mutant Type Score Diff 1 A VAL ALA 75.513 41 A THR ALA 42.100 6 A ASP ALA 35.608 541 C ARG ALA 25.333 670 D GLN ALA 20.251 141 A ARG ALA 20.196 242 B ASP ALA 19.715 270 B GLN ALA 19.185 522 C HIS ALA 18.890 494 C ASP ALA 18.515 642 D ASP ALA 17.822 183 B ARG ALA 17.206 431 C ARG ALA 17.005 94 A ASP ALA 16.808 122 A HIS ALA 16.423 503 C HIS ALA 16.278 492 C ARG ALA 16.075 580 D TRP ALA 16.017 103 A HIS ALA 15.771 441 C THR ALA 15.626 583 D ARG ALA 15.406 31 A ARG ALA 15.248 259 B HIS ALA 14.991 180 B TRP ALA 14.988 107 A VAL ALA 14.477 263 B LYS ALA 14.181 92 A ARG ALA 14.137 658 D ALA ALA 14.034 258 B ALA ALA 13.648 178 B TYR ALA 13.353 435 C SER ALA 13.208 578 D TYR ALA 12.982 35 A SER ALA 12.961 42 A TYR ALA 12.754 38 A THR ALA 12.722 442 C TYR ALA 12.715 519 C PRO ALA 12.611 659 D HIS ALA 12.608 119 A PRO ALA 12.402 23 A GLU ALA 11.862 644 D GLU ALA 11.740 507 C VAL ALA 11.739 110 A ALA ALA 11.203 274 B GLN ALA 11.032 27 A GLU ALA 11.006 173 B ARG ALA 10.865 655 D CYS ALA 10.856 674 D GLN ALA 10.850 517 C PHE ALA 10.721 34 A LEU ALA 10.677 510 C ALA ALA 10.564 255 B CYS ALA 10.440 573 D ARG ALA 10.258 267 B PRO ALA 9.786 665 D PHE ALA 9.738 577 D VAL ALA 9.619 244 B GLU ALA 9.441 265 B PHE ALA 9.402 438 C THR ALA 9.316 667 D PRO ALA 9.151 523 C ALA ALA 9.150 654 D VAL ALA 8.792 111 A ALA ALA 8.385 40 A LYS ALA 8.307 177 B VAL ALA 7.979 436 C PHE ALA 7.966 117 A PHE ALA 7.895 511 C ALA ALA 7.691 526 C ASP ALA 7.358 651 D ASN ALA 7.261 251 B ASN ALA 7.132 176 B VAL ALA 6.872 645 D ASN ALA 6.818 96 A VAL ALA 6.700 497 C ASN ALA 6.579 126 A ASP ALA 6.499 518 C THR ALA 6.202 95 A PRO ALA 6.030 254 B VAL ALA 6.021 271 B ALA ALA 5.999 434 C LEU ALA 5.971 594 D PRO ALA 5.920 545 D HIS ALA 5.726 97 A ASN ALA 5.690 640 D HIS ALA 5.681 268 B PRO ALA 5.677 30 A GLU ALA 5.362 194 B PRO ALA 5.306 118 A THR ALA 5.301 123 A ALA ALA 5.267 540 C TYR ALA 5.261 495 C PRO ALA 5.241 688 D TYR ALA 5.094 288 B TYR ALA 4.985 20 A HIS ALA 4.910 245 B ASN ALA 4.870 506 C LEU ALA 4.852 36 A PHE ALA 4.789 576 D VAL ALA 4.630 140 A TYR ALA 4.548 671 D ALA ALA 4.527 668 D PRO ALA 4.492 256 B VAL ALA 4.278 247 B ARG ALA 4.258 248 B LEU ALA 4.139 643 D PRO ALA 4.086 184 B PHE ALA 4.000 243 B PRO ALA 3.936 496 C VAL ALA 3.927 106 A LEU ALA 3.864 579 D PRO ALA 3.734 427 C GLU ALA 3.699 520 C ALA ALA 3.698 179 B PRO ALA 3.573 595 D ASP ALA 3.471 430 C GLU ALA 3.441 437 C PRO ALA 3.401 266 B THR ALA 3.323 647 D ARG ALA 3.300 186 B GLU ALA 3.223 569 D GLU ALA 3.194 120 A ALA ALA 2.993 499 C LYS ALA 2.952 493 C VAL ALA 2.872 240 B HIS ALA 2.701 656 D VAL ALA 2.659 252 B VAL ALA 2.626 286 B HIS ALA 2.610 584 D PHE ALA 2.505 648 D LEU ALA 2.497 93 A VAL ALA 2.411 289 B HIS ALA 2.340 37 A PRO ALA 2.152 636 D CYS ALA 2.129 504 C CYS ALA 2.114 527 C LYS ALA 1.983 444 C PRO ALA 1.939 44 A PRO ALA 1.893 689 D HIS ALA 1.847 108 A THR ALA 1.824 586 D GLU ALA 1.807 666 D THR ALA 1.780 127 A LYS ALA 1.685 534 C THR ALA 1.588 401 C VAL ALA 1.533 134 A THR ALA 1.509 598 D MET ALA 1.422 198 B MET ALA 1.422 50 A HIS ALA 1.388 236 B CYS ALA 1.335 195 B ASP ALA 1.305 663 D LYS ALA 1.264 450 C HIS ALA 1.228 440 C LYS ALA 1.219 100 A LEU ALA 1.088 39 A THR ALA 1.041 45 A HIS ALA 0.982 112 A HIS ALA 0.968 500 C LEU ALA 0.934 145 B HIS ALA 0.921 508 C THR ALA 0.843 490 C LYS ALA 0.820 686 D HIS ALA 0.806 582 D GLN ALA 0.626 182 B GLN ALA 0.626 24 A TYR ALA 0.618 512 C HIS ALA 0.523 275 B LYS ALA 0.507 89 A HIS ALA 0.495 406 C ASP ALA 0.441 181 B THR ALA 0.432 675 D LYS ALA 0.399 90 A LYS ALA 0.296 116 A GLU ALA 0.247 652 D VAL ALA 0.215 169 B GLU ALA 0.191 677 D VAL ALA 0.185 673 D TYR ALA 0.175 516 C GLU ALA 0.163 273 B TYR ALA 0.144 104 A CYS ALA 0.137 646 D PHE ALA 0.114 641 D VAL ALA 0.111 114 A PRO ALA 0.098 591 D LEU ALA 0.097 191 B LEU ALA 0.097 439 C THR ALA 0.097 514 C PRO ALA 0.096 246 B PHE ALA 0.088 99 A LYS ALA 0.087 445 C HIS ALA 0.084 432 C MET ALA 0.083 115 A ALA ALA 0.082 88 A ALA ALA 0.082 130 A ALA ALA 0.082 515 C ALA ALA 0.080 488 C ALA ALA 0.080 530 C ALA ALA 0.079 278 B ALA ALA 0.076 685 D ALA ALA 0.075 285 B ALA ALA 0.075 678 D ALA ALA 0.075 257 B LEU ALA 0.072 409 C ASN ALA 0.070 113 A LEU ALA 0.053 235 B HIS ALA 0.052 513 C LEU ALA 0.050 597 D VAL ALA 0.031 637 D ASP ALA 0.029 91 A LEU ALA 0.011 491 C LEU ALA 0.009 581 D THR ALA -0.001 225 B LYS ALA -0.002 661 D PHE ALA -0.007 261 B PHE ALA -0.007 197 B VAL ALA -0.013 32 A MET ALA -0.062 150 B GLU ALA -0.069 537 C THR ALA -0.086 121 A VAL ALA -0.088 521 C VAL ALA -0.090 269 B VAL ALA -0.094 138 A SER ALA -0.097 669 D VAL ALA -0.141 538 C SER ALA -0.153 277 B VAL ALA -0.189 139 A LYS ALA -0.253 539 C LYS ALA -0.301 241 B VAL ALA -0.579