HEADER SERINE PROTEASE INHIBITOR 09-APR-92 1AAL REMARK This file edited to provide a pol-ALA chain (from chain A) REMARK for MR searches. The terminal 2 residues have been deleted. REMARK COMPND BOVINE PANCREATIC TRYPSIN INHIBITOR (BPTI, BASIC) MUTANT COMPND 2 WITH CYS 30 REPLACED BY VAL AND CYS 51 REPLACED BY ALA COMPND 3 (C30V,C51A) SOURCE BOVINE (BOS TAURUS) RECOMBINANT FORM EXPRESSED IN SOURCE 2 (ESCHERICHIA COLI) AUTHOR C.EIGENBROT,M.RANDAL,A.A.KOSSIAKOFF REVDAT 1 31-OCT-93 1AAL 0 JRNL AUTH C.EIGENBROT,M.RANDAL,A.A.KOSSIAKOFF JRNL TITL STRUCTURAL EFFECTS INDUCED BY MUTAGENESIS JRNL TITL 2 AFFECTED BY CRYSTAL PACKING FACTORS: THE JRNL TITL 3 STRUCTURE OF A 30-51 DISULFIDE MUTANT OF BASIC JRNL TITL 4 PANCREATIC TRYPSIN INHIBITOR JRNL REF PROTEINS.STRUCT.,FUNCT., V. 14 75 1992 JRNL REF 2 GENET. JRNL REFN ASTM PSFGEY US ISSN 0887-3585 867 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH C.EIGENBROT,M.RANDAL,A.A.KOSSIAKOFF REMARK 1 TITL STRUCTURAL EFFECTS INDUCED BY REMOVAL OF A REMARK 1 TITL 2 DISULFIDE BRIDGE: THE X-RAY STRUCTURE OF THE REMARK 1 TITL 3 /C30A(SLASH)C51A$ MUTANT OF BASIC PANCREATIC REMARK 1 TITL 4 TRYPSIN INHIBITOR AT 1.6 ANGSTROMS REMARK 1 REF PROTEIN ENG. V. 3 591 1990 REMARK 1 REFN ASTM PRENE9 UK ISSN 0269-2139 859 REMARK 2 REMARK 2 RESOLUTION. 1.6 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM PROLSQ REMARK 3 AUTHORS KONNERT,HENDRICKSON REMARK 3 R VALUE 0.179 REMARK 3 RMSD BOND DISTANCES 0.020 ANGSTROMS REMARK 3 RMSD BOND ANGLES 3.50 DEGREES REMARK 3 REMARK 3 NUMBER OF REFLECTIONS 15473 REMARK 3 RESOLUTION RANGE 8.0 - 1.6 ANGSTROMS REMARK 3 DATA CUTOFF 1.0 SIGMA(I) REMARK 3 REMARK 3 NUMBER OF PROTEIN ATOMS 906 REMARK 3 NUMBER OF PROTEIN ATOM SITES 945 REMARK 3 NUMBER OF SOLVENT ATOMS 121 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES (THE VALUES OF REMARK 3 SIGMA, IN PARENTHESES, ARE THE INPUT ESTIMATED REMARK 3 STANDARD DEVIATIONS THAT DETERMINE THE RELATIVE REMARK 3 WEIGHTS OF THE CORRESPONDING RESTRAINTS) REMARK 3 DISTANCE RESTRAINTS (ANGSTROMS) REMARK 3 BOND DISTANCE 0.020(0.020) REMARK 3 ANGLE DISTANCE 0.056(0.050) REMARK 3 PLANAR 1-4 DISTANCE 0.063(0.060) REMARK 3 PLANE RESTRAINT (ANGSTROMS) 0.016(0.020) REMARK 3 CHIRAL-CENTER RESTRAINT (ANGSTROMS**3) 0.154(0.125) REMARK 3 NON-BONDED CONTACT RESTRAINTS (ANGSTROMS) REMARK 3 SINGLE TORSION CONTACT 0.193(0.500) REMARK 3 MULTIPLE TORSION CONTACT 0.263(0.500) REMARK 3 POSSIBLE HYDROGEN BOND 0.218(0.500) REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINT (DEGREES) REMARK 3 PLANAR 3.4 ( 5.0) REMARK 3 STAGGERED 19.8 (60.0) REMARK 3 ORTHONORMAL 20.6 (45.0) REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS (ANGSTROMS**2) REMARK 3 MAIN-CHAIN BOND 2.0 (2.0) REMARK 3 MAIN-CHAIN ANGLE 2.9 (3.0) REMARK 3 SIDE-CHAIN BOND 3.0 (2.5) REMARK 3 SIDE-CHAIN ANGLE 4.9 (4.0) REMARK 4 REMARK 4 THERE ARE TWO MOLECULES IN THE ASYMMETRIC UNIT. REMARK 5 REMARK 5 THE TRANSFORMATION PRESENTED ON *MTRIX* RECORDS BELOW WILL REMARK 5 GENERATE APPROXIMATE COORDINATES FOR CHAIN B WHEN APPLIED REMARK 5 TO CHAIN A. REMARK 6 REMARK 6 ALA 58 OF CHAIN B COULD NOT BE LOCATED IN ELECTRON DENSITY REMARK 6 MAP AND IS ABSENT FROM THE MODEL. REMARK 7 REMARK 7 THERE IS A UNIQUE SALT-BRIDGE BETWEEN THE N AND C TERMINALS REMARK 7 OF MOLECULES WITH RESIDUE NUMBERS 1 - 58, WHICH HAS BEEN REMARK 7 SEEN IN SOLUTION (NMR) BUT NEVER CRYSTALLOGRAPHICALLY. SEQRES 1 A 58 ARG PRO ASP PHE CYS LEU GLU PRO PRO TYR THR GLY PRO SEQRES 2 A 58 CYS LYS ALA ARG ILE ILE ARG TYR PHE TYR ASN ALA LYS SEQRES 3 A 58 ALA GLY LEU VAL GLN THR PHE VAL TYR GLY GLY CYS ARG SEQRES 4 A 58 ALA LYS ARG ASN ASN PHE LYS SER ALA GLU ASP ALA MET SEQRES 5 A 58 ARG THR CYS GLY GLY ALA SEQRES 1 B 58 ARG PRO ASP PHE CYS LEU GLU PRO PRO TYR THR GLY PRO SEQRES 2 B 58 CYS LYS ALA ARG ILE ILE ARG TYR PHE TYR ASN ALA LYS SEQRES 3 B 58 ALA GLY LEU VAL GLN THR PHE VAL TYR GLY GLY CYS ARG SEQRES 4 B 58 ALA LYS ARG ASN ASN PHE LYS SER ALA GLU ASP ALA MET SEQRES 5 B 58 ARG THR CYS GLY GLY ALA FTNOTE 1 FTNOTE 1 THE FOLLOWING RESIDUES MODELLED WITH 2 SIDE CHAIN FTNOTE 1 CONFORMATIONS: GLU A 7, ARG A 17, ARG A 39, GLU A 49, FTNOTE 1 ASP B 3, ARG B 17, ARG B 39, ARG B 42, GLU B 49. HET IPS 59 5 INORGANIC PHOSPHATE GROUP FORMUL 3 IPS H1 O4 P1 -- FORMUL 4 HOH *126(H2 O1) HELIX 1 H1A PRO A 2 GLU A 7 5 HELIX 2 H2A SER A 47 GLY A 56 1 HELIX 3 H1B PRO B 2 GLU B 7 5 HELIX 4 H2B SER B 47 GLY B 56 1 SHEET 1 S1A 3 LEU A 29 TYR A 35 0 SHEET 2 S1A 3 ILE A 18 ASN A 24 -1 SHEET 3 S1A 3 PHE A 45 PHE A 45 -1 SHEET 1 S1B 3 LEU B 29 TYR B 35 0 SHEET 2 S1B 3 ILE B 18 ASN B 24 -1 SHEET 3 S1B 3 PHE B 45 PHE B 45 -1 TURN 1 T1A ALA A 25 GLY A 28 TURN 2 T1B ALA B 25 GLY B 28 SSBOND 1 CYS A 5 CYS A 55 SSBOND 2 CYS A 14 CYS A 38 SSBOND 3 CYS B 5 CYS B 55 SSBOND 4 CYS B 14 CYS B 38 CRYST1 56.280 89.580 48.360 90.00 90.00 90.00 C 2 2 21 16 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.017768 0.000000 0.000000 0.00000 SCALE2 0.000000 0.011163 0.000000 0.00000 SCALE3 0.000000 0.000000 0.020678 0.00000 MTRIX1 1 0.785512 -0.594349 -0.172394 46.50912 1 MTRIX2 1 -0.528944 -0.789422 0.311497 117.36581 1 MTRIX3 1 -0.321229 -0.153498 -0.934479 50.15519 1 ATOM 1 N ARG A 1 8.464 75.360 22.114 1.00 20.86 ATOM 2 CA ARG A 1 9.901 75.110 21.966 1.00 20.62 ATOM 3 C ARG A 1 10.653 76.351 22.437 1.00 20.68 ATOM 4 O ARG A 1 10.316 77.426 21.901 1.00 19.35 ATOM 5 CB ARG A 1 10.351 74.966 20.514 1.00 20.98 ATOM 12 N PRO A 2 11.568 76.300 23.381 1.00 18.72 ATOM 13 CA PRO A 2 12.233 77.498 23.858 1.00 16.53 ATOM 14 C PRO A 2 12.944 78.190 22.718 1.00 17.41 ATOM 15 O PRO A 2 13.602 77.599 21.818 1.00 16.76 ATOM 16 CB PRO A 2 13.164 77.006 24.955 1.00 18.80 ATOM 19 N ASP A 3 12.798 79.563 22.778 1.00 15.46 ATOM 20 CA ASP A 3 13.458 80.313 21.676 1.00 15.18 ATOM 21 C ASP A 3 14.983 80.179 21.625 1.00 12.85 ATOM 22 O ASP A 3 15.428 80.335 20.506 1.00 14.03 ATOM 23 CB ASP A 3 13.014 81.780 21.740 1.00 20.17 ATOM 27 N PHE A 4 15.591 79.914 22.750 1.00 12.65 ATOM 28 CA PHE A 4 17.064 79.762 22.721 1.00 14.12 ATOM 29 C PHE A 4 17.464 78.561 21.853 1.00 14.15 ATOM 30 O PHE A 4 18.641 78.513 21.495 1.00 16.14 ATOM 31 CB PHE A 4 17.658 79.637 24.098 1.00 16.08 ATOM 38 N CYS A 5 16.558 77.663 21.514 1.00 14.20 ATOM 39 CA CYS A 5 16.873 76.543 20.624 1.00 15.10 ATOM 40 C CYS A 5 17.168 77.016 19.223 1.00 16.55 ATOM 41 O CYS A 5 17.668 76.243 18.370 1.00 16.02 ATOM 42 CB CYS A 5 15.668 75.588 20.594 1.00 14.93 ATOM 44 N LEU A 6 16.807 78.266 18.842 1.00 14.50 ATOM 45 CA LEU A 6 17.024 78.804 17.486 1.00 14.47 ATOM 46 C LEU A 6 18.342 79.515 17.370 1.00 17.54 ATOM 47 O LEU A 6 18.693 79.935 16.260 1.00 21.11 ATOM 48 CB LEU A 6 15.825 79.742 17.254 1.00 17.01 ATOM 52 N GLU A 7 19.052 79.671 18.466 1.00 17.05 1 ATOM 53 CA GLU A 7 20.338 80.349 18.378 1.00 19.83 1 ATOM 54 C GLU A 7 21.462 79.480 17.848 1.00 20.57 1 ATOM 55 O GLU A 7 21.535 78.294 18.126 1.00 19.51 1 ATOM 56 CB GLU A 7 20.688 80.789 19.805 1.00 23.48 1 ATOM 65 N PRO A 8 22.428 80.050 17.152 1.00 19.92 ATOM 66 CA PRO A 8 23.622 79.375 16.710 1.00 19.60 ATOM 67 C PRO A 8 24.410 79.079 18.001 1.00 18.54 ATOM 68 O PRO A 8 24.276 79.687 19.093 1.00 19.74 ATOM 69 CB PRO A 8 24.384 80.310 15.771 1.00 21.10 ATOM 72 N PRO A 9 25.305 78.097 17.830 1.00 16.87 ATOM 73 CA PRO A 9 26.128 77.683 18.961 1.00 18.20 ATOM 74 C PRO A 9 27.205 78.718 19.290 1.00 17.67 ATOM 75 O PRO A 9 27.668 79.382 18.346 1.00 21.22 ATOM 76 CB PRO A 9 26.761 76.393 18.506 1.00 19.07 ATOM 79 N TYR A 10 27.507 78.815 20.522 1.00 17.34 ATOM 80 CA TYR A 10 28.495 79.823 20.925 1.00 19.86 ATOM 81 C TYR A 10 29.719 79.268 21.669 1.00 19.51 ATOM 82 O TYR A 10 29.554 78.813 22.808 1.00 18.61 ATOM 83 CB TYR A 10 27.668 80.689 21.875 1.00 19.76 ATOM 91 N THR A 11 30.837 79.416 20.973 1.00 21.67 ATOM 92 CA THR A 11 32.089 78.929 21.595 1.00 23.95 ATOM 93 C THR A 11 32.500 79.693 22.843 1.00 23.06 ATOM 94 O THR A 11 32.901 79.093 23.841 1.00 22.59 ATOM 95 CB THR A 11 33.293 78.966 20.602 1.00 25.20 ATOM 98 N GLY A 12 32.342 81.014 22.740 1.00 23.25 ATOM 99 CA GLY A 12 32.698 81.808 23.947 1.00 23.81 ATOM 100 C GLY A 12 34.221 82.103 23.795 1.00 27.38 ATOM 101 O GLY A 12 34.961 81.746 22.844 1.00 25.38 ATOM 102 N PRO A 13 34.637 82.803 24.853 1.00 28.43 ATOM 103 CA PRO A 13 36.021 83.275 24.902 1.00 30.78 ATOM 104 C PRO A 13 37.136 82.370 25.417 1.00 32.26 ATOM 105 O PRO A 13 38.318 82.623 24.995 1.00 35.12 ATOM 106 CB PRO A 13 35.815 84.536 25.777 1.00 31.51 ATOM 109 N CYS A 14 36.749 81.404 26.245 1.00 30.56 ATOM 110 CA CYS A 14 37.802 80.518 26.792 1.00 27.94 ATOM 111 C CYS A 14 38.382 79.624 25.720 1.00 28.18 ATOM 112 O CYS A 14 37.896 79.456 24.596 1.00 28.93 ATOM 113 CB CYS A 14 37.286 79.904 28.027 1.00 26.07 ATOM 115 N LYS A 15 39.556 79.101 26.144 1.00 29.18 ATOM 116 CA LYS A 15 40.348 78.297 25.201 1.00 30.82 ATOM 117 C LYS A 15 40.365 76.777 25.401 1.00 27.60 ATOM 118 O LYS A 15 41.183 76.182 24.666 1.00 27.90 ATOM 119 CB LYS A 15 41.787 78.852 25.119 1.00 37.07 ATOM 124 N ALA A 16 39.506 76.299 26.277 1.00 26.67 ATOM 125 CA ALA A 16 39.415 74.830 26.422 1.00 24.01 ATOM 126 C ALA A 16 38.766 74.379 25.114 1.00 25.47 ATOM 127 O ALA A 16 38.199 75.096 24.286 1.00 25.56 ATOM 128 CB ALA A 16 38.680 74.433 27.676 1.00 22.63 ATOM 129 N ARG A 17 38.872 73.072 24.839 1.00 26.40 1 ATOM 130 CA ARG A 17 38.286 72.346 23.676 1.00 26.70 1 ATOM 131 C ARG A 17 37.277 71.362 24.291 1.00 25.14 1 ATOM 132 O ARG A 17 37.734 70.304 24.769 1.00 26.15 1 ATOM 133 CB ARG A 17 39.367 71.638 22.897 1.00 28.92 1 ATOM 146 N ILE A 18 36.011 71.602 24.428 1.00 20.62 ATOM 147 CA ILE A 18 35.075 70.717 25.083 1.00 19.88 ATOM 148 C ILE A 18 34.032 70.422 24.048 1.00 21.36 ATOM 149 O ILE A 18 33.574 71.409 23.439 1.00 20.65 ATOM 150 CB ILE A 18 34.403 71.393 26.288 1.00 21.27 ATOM 154 N ILE A 19 33.650 69.216 23.794 1.00 17.49 ATOM 155 CA ILE A 19 32.665 68.970 22.737 1.00 16.60 ATOM 156 C ILE A 19 31.330 69.087 23.383 1.00 16.30 ATOM 157 O ILE A 19 31.132 68.475 24.439 1.00 18.10 ATOM 158 CB ILE A 19 32.936 67.574 22.025 1.00 19.06 ATOM 162 N ARG A 20 30.415 69.878 22.862 1.00 15.41 ATOM 163 CA ARG A 20 29.090 70.007 23.465 1.00 14.64 ATOM 164 C ARG A 20 28.141 69.817 22.320 1.00 12.20 ATOM 165 O ARG A 20 28.553 69.762 21.170 1.00 15.24 ATOM 166 CB ARG A 20 28.888 71.356 24.131 1.00 15.17 ATOM 173 N TYR A 21 26.872 69.710 22.675 1.00 14.41 ATOM 174 CA TYR A 21 25.857 69.523 21.637 1.00 13.84 ATOM 175 C TYR A 21 24.918 70.740 21.536 1.00 13.04 ATOM 176 O TYR A 21 24.721 71.350 22.603 1.00 14.99 ATOM 177 CB TYR A 21 24.968 68.310 22.060 1.00 16.71 ATOM 185 N PHE A 22 24.382 70.989 20.383 1.00 13.92 ATOM 186 CA PHE A 22 23.387 72.081 20.313 1.00 13.83 ATOM 187 C PHE A 22 22.307 71.545 19.386 1.00 13.66 ATOM 188 O PHE A 22 22.598 70.640 18.559 1.00 13.97 ATOM 189 CB PHE A 22 24.027 73.396 19.779 1.00 12.00 ATOM 196 N TYR A 23 21.144 72.188 19.414 1.00 13.24 ATOM 197 CA TYR A 23 20.069 71.820 18.476 1.00 14.21 ATOM 198 C TYR A 23 20.198 72.741 17.253 1.00 15.97 ATOM 199 O TYR A 23 20.187 73.969 17.418 1.00 14.40 ATOM 200 CB TYR A 23 18.721 71.966 19.217 1.00 16.67 ATOM 208 N ASN A 24 20.320 72.238 16.037 1.00 15.19 ATOM 209 CA ASN A 24 20.435 72.938 14.788 1.00 15.44 ATOM 210 C ASN A 24 19.026 73.037 14.246 1.00 19.79 ATOM 211 O ASN A 24 18.580 72.107 13.593 1.00 18.98 ATOM 212 CB ASN A 24 21.349 72.226 13.822 1.00 15.75 ATOM 216 N ALA A 25 18.306 74.117 14.503 1.00 21.58 ATOM 217 CA ALA A 25 16.900 74.144 14.033 1.00 25.17 ATOM 218 C ALA A 25 16.808 74.193 12.528 1.00 26.29 ATOM 219 O ALA A 25 15.699 73.783 12.192 1.00 29.48 ATOM 220 CB ALA A 25 16.101 75.262 14.663 1.00 28.60 ATOM 221 N LYS A 26 17.827 74.611 11.840 1.00 28.23 ATOM 222 CA LYS A 26 17.777 74.661 10.384 1.00 32.32 ATOM 223 C LYS A 26 17.830 73.187 9.950 1.00 34.61 ATOM 224 O LYS A 26 16.858 72.811 9.262 1.00 38.23 ATOM 225 CB LYS A 26 18.897 75.324 9.625 1.00 36.79 ATOM 230 N ALA A 27 18.871 72.449 10.322 1.00 32.61 ATOM 231 CA ALA A 27 18.995 71.017 9.961 1.00 30.00 ATOM 232 C ALA A 27 17.935 70.171 10.651 1.00 28.33 ATOM 233 O ALA A 27 17.709 69.052 10.130 1.00 30.06 ATOM 234 CB ALA A 27 20.404 70.465 10.229 1.00 27.42 ATOM 235 N GLY A 28 17.297 70.521 11.728 1.00 24.12 ATOM 236 CA GLY A 28 16.275 69.825 12.496 1.00 21.10 ATOM 237 C GLY A 28 16.963 68.646 13.209 1.00 22.53 ATOM 238 O GLY A 28 16.400 67.573 13.509 1.00 23.79 ATOM 239 N LEU A 29 18.230 68.777 13.563 1.00 19.59 ATOM 240 CA LEU A 29 19.002 67.751 14.254 1.00 18.84 ATOM 241 C LEU A 29 19.922 68.313 15.318 1.00 15.81 ATOM 242 O LEU A 29 20.301 69.478 15.136 1.00 15.45 ATOM 243 CB LEU A 29 19.948 67.189 13.161 1.00 21.36 ATOM 247 N VAL A 30 20.303 67.488 16.218 1.00 12.91 ATOM 248 CA VAL A 30 21.282 67.821 17.250 1.00 12.53 ATOM 249 C VAL A 30 22.622 67.647 16.574 1.00 13.08 ATOM 250 O VAL A 30 22.828 66.699 15.784 1.00 15.25 ATOM 251 CB VAL A 30 21.106 66.968 18.537 1.00 12.28 ATOM 254 N GLN A 31 23.575 68.536 16.809 1.00 13.05 ATOM 255 CA GLN A 31 24.933 68.504 16.265 1.00 11.90 ATOM 256 C GLN A 31 25.892 68.868 17.365 1.00 11.12 ATOM 257 O GLN A 31 25.561 69.250 18.468 1.00 12.54 ATOM 258 CB GLN A 31 25.115 69.374 15.063 1.00 16.78 ATOM 263 N THR A 32 27.164 68.685 17.052 1.00 14.10 ATOM 264 CA THR A 32 28.192 68.963 18.041 1.00 15.15 ATOM 265 C THR A 32 28.909 70.257 17.655 1.00 17.02 ATOM 266 O THR A 32 28.890 70.586 16.454 1.00 18.46 ATOM 267 CB THR A 32 29.361 67.896 18.177 1.00 19.89 ATOM 270 N PHE A 33 29.504 70.862 18.684 1.00 18.34 ATOM 271 CA PHE A 33 30.317 72.093 18.407 1.00 18.09 ATOM 272 C PHE A 33 31.385 72.116 19.508 1.00 18.53 ATOM 273 O PHE A 33 31.317 71.397 20.502 1.00 17.29 ATOM 274 CB PHE A 33 29.561 73.435 18.286 1.00 15.77 ATOM 281 N VAL A 34 32.400 72.952 19.335 1.00 20.53 ATOM 282 CA VAL A 34 33.494 73.073 20.325 1.00 19.96 ATOM 283 C VAL A 34 33.195 74.224 21.268 1.00 20.24 ATOM 284 O VAL A 34 33.055 75.341 20.694 1.00 21.38 ATOM 285 CB VAL A 34 34.804 73.282 19.524 1.00 22.06 ATOM 288 N TYR A 35 33.041 74.063 22.539 1.00 16.45 ATOM 289 CA TYR A 35 32.763 75.038 23.546 1.00 18.12 ATOM 290 C TYR A 35 34.116 75.380 24.185 1.00 22.13 ATOM 291 O TYR A 35 34.883 74.456 24.477 1.00 21.16 ATOM 292 CB TYR A 35 31.857 74.494 24.571 1.00 19.31 ATOM 300 N GLY A 36 34.444 76.656 24.350 1.00 21.39 ATOM 301 CA GLY A 36 35.769 76.974 24.925 1.00 19.17 ATOM 302 C GLY A 36 35.647 76.842 26.416 1.00 18.93 ATOM 303 O GLY A 36 36.726 76.994 27.058 1.00 22.05 ATOM 304 N GLY A 37 34.608 76.637 27.172 1.00 18.70 ATOM 305 CA GLY A 37 34.696 76.522 28.601 1.00 20.28 ATOM 306 C GLY A 37 34.026 77.479 29.548 1.00 22.86 ATOM 307 O GLY A 37 33.761 77.143 30.692 1.00 24.44 ATOM 308 N CYS A 38 33.730 78.687 29.036 1.00 26.41 ATOM 309 CA CYS A 38 33.077 79.794 29.783 1.00 25.34 ATOM 310 C CYS A 38 32.094 80.539 28.837 1.00 23.57 ATOM 311 O CYS A 38 32.135 80.630 27.596 1.00 22.72 ATOM 312 CB CYS A 38 34.107 80.778 30.462 1.00 23.34 ATOM 314 N ARG A 39 31.194 81.151 29.572 1.00 26.14 1 ATOM 315 CA ARG A 39 30.131 82.044 29.045 1.00 28.06 1 ATOM 316 C ARG A 39 29.132 81.338 28.117 1.00 24.19 1 ATOM 317 O ARG A 39 28.808 81.802 27.010 1.00 23.46 1 ATOM 318 CB ARG A 39 30.729 83.200 28.255 1.00 34.31 1 ATOM 331 N ALA A 40 28.672 80.211 28.625 1.00 23.30 ATOM 332 CA ALA A 40 27.743 79.469 27.742 1.00 22.57 ATOM 333 C ALA A 40 26.377 80.099 27.530 1.00 19.30 ATOM 334 O ALA A 40 25.822 80.624 28.470 1.00 23.11 ATOM 335 CB ALA A 40 27.509 78.095 28.401 1.00 21.71 ATOM 336 N LYS A 41 25.885 79.907 26.365 1.00 17.56 ATOM 337 CA LYS A 41 24.530 80.326 26.003 1.00 17.45 ATOM 338 C LYS A 41 23.650 79.121 26.336 1.00 18.56 ATOM 339 O LYS A 41 24.231 78.051 26.727 1.00 19.03 ATOM 340 CB LYS A 41 24.578 80.789 24.577 1.00 24.45 ATOM 345 N ARG A 42 22.351 79.209 26.186 1.00 14.52 ATOM 346 CA ARG A 42 21.452 78.133 26.544 1.00 17.46 ATOM 347 C ARG A 42 21.469 76.930 25.550 1.00 16.38 ATOM 348 O ARG A 42 21.132 75.837 26.070 1.00 16.65 ATOM 349 CB ARG A 42 20.052 78.714 26.862 1.00 14.61 ATOM 356 N ASN A 43 21.776 77.153 24.305 1.00 14.89 ATOM 357 CA ASN A 43 21.784 76.042 23.322 1.00 12.94 ATOM 358 C ASN A 43 23.176 75.334 23.459 1.00 9.93 ATOM 359 O ASN A 43 23.943 75.491 22.505 1.00 11.46 ATOM 360 CB ASN A 43 21.523 76.587 21.958 1.00 11.74 ATOM 364 N ASN A 44 23.299 74.731 24.627 1.00 10.79 ATOM 365 CA ASN A 44 24.641 74.100 24.886 1.00 14.46 ATOM 366 C ASN A 44 24.349 72.992 25.899 1.00 14.03 ATOM 367 O ASN A 44 23.922 73.219 27.044 1.00 13.49 ATOM 368 CB ASN A 44 25.644 75.196 25.277 1.00 15.33 ATOM 372 N PHE A 45 24.551 71.731 25.389 1.00 14.13 ATOM 373 CA PHE A 45 24.196 70.572 26.243 1.00 12.64 ATOM 374 C PHE A 45 25.392 69.593 26.355 1.00 12.67 ATOM 375 O PHE A 45 26.240 69.551 25.481 1.00 14.52 ATOM 376 CB PHE A 45 22.939 69.946 25.703 1.00 11.88 ATOM 383 N LYS A 46 25.270 68.927 27.502 1.00 14.58 ATOM 384 CA LYS A 46 26.372 67.947 27.785 1.00 18.14 ATOM 385 C LYS A 46 26.117 66.631 27.072 1.00 17.52 ATOM 386 O LYS A 46 27.097 65.872 26.934 1.00 20.52 ATOM 387 CB LYS A 46 26.543 67.842 29.317 1.00 22.85 ATOM 392 N SER A 47 24.913 66.358 26.621 1.00 16.64 ATOM 393 CA SER A 47 24.694 65.134 25.846 1.00 16.40 ATOM 394 C SER A 47 23.658 65.464 24.792 1.00 17.33 ATOM 395 O SER A 47 22.853 66.392 24.958 1.00 15.41 ATOM 396 CB SER A 47 24.130 64.126 26.812 1.00 16.80 ATOM 398 N ALA A 48 23.593 64.652 23.745 1.00 15.79 ATOM 399 CA ALA A 48 22.588 64.826 22.702 1.00 12.66 ATOM 400 C ALA A 48 21.206 64.586 23.246 1.00 13.16 ATOM 401 O ALA A 48 20.249 65.264 22.795 1.00 13.52 ATOM 402 CB ALA A 48 22.990 63.891 21.546 1.00 13.23 ATOM 403 N GLU A 49 20.972 63.722 24.230 1.00 13.58 1 ATOM 404 CA GLU A 49 19.632 63.455 24.727 1.00 16.44 1 ATOM 405 C GLU A 49 19.035 64.696 25.419 1.00 16.10 1 ATOM 406 O GLU A 49 17.828 64.886 25.279 1.00 16.64 1 ATOM 407 CB GLU A 49 19.800 62.282 25.673 1.00 21.10 1 ATOM 416 N ASP A 50 19.943 65.379 26.081 1.00 16.26 ATOM 417 CA ASP A 50 19.549 66.649 26.799 1.00 16.65 ATOM 418 C ASP A 50 19.100 67.686 25.766 1.00 14.86 ATOM 419 O ASP A 50 17.997 68.215 25.952 1.00 16.75 ATOM 420 CB ASP A 50 20.703 67.163 27.625 1.00 18.58 ATOM 424 N ALA A 51 19.903 67.869 24.740 1.00 13.53 ATOM 425 CA ALA A 51 19.550 68.827 23.656 1.00 11.98 ATOM 426 C ALA A 51 18.223 68.465 23.055 1.00 14.45 ATOM 427 O ALA A 51 17.368 69.312 22.792 1.00 16.50 ATOM 428 CB ALA A 51 20.661 68.922 22.609 1.00 10.64 ATOM 429 N MET A 52 17.968 67.196 22.643 1.00 14.11 ATOM 430 CA MET A 52 16.709 66.703 22.010 1.00 14.81 ATOM 431 C MET A 52 15.542 66.826 22.973 1.00 15.11 ATOM 432 O MET A 52 14.422 67.245 22.519 1.00 15.62 ATOM 433 CB MET A 52 16.863 65.225 21.599 1.00 15.64 ATOM 437 N ARG A 53 15.779 66.441 24.238 1.00 15.80 ATOM 438 CA ARG A 53 14.651 66.604 25.183 1.00 17.59 ATOM 439 C ARG A 53 14.154 68.086 25.314 1.00 19.02 ATOM 440 O ARG A 53 12.987 68.506 25.395 1.00 18.19 ATOM 441 CB ARG A 53 15.238 66.229 26.555 1.00 20.80 ATOM 448 N THR A 54 15.163 68.945 25.380 1.00 17.36 ATOM 449 CA THR A 54 14.880 70.392 25.555 1.00 18.29 ATOM 450 C THR A 54 14.423 71.056 24.286 1.00 16.48 ATOM 451 O THR A 54 13.429 71.794 24.441 1.00 19.53 ATOM 452 CB THR A 54 16.167 71.112 26.042 1.00 16.06 ATOM 455 N CYS A 55 15.014 70.877 23.152 1.00 14.64 ATOM 456 CA CYS A 55 14.712 71.541 21.906 1.00 16.99 ATOM 457 C CYS A 55 13.938 70.851 20.832 1.00 21.80 ATOM 458 O CYS A 55 13.596 71.532 19.848 1.00 22.67 ATOM 459 CB CYS A 55 16.017 72.048 21.302 1.00 12.21 ATOM 461 N GLY A 56 13.738 69.551 21.071 1.00 26.22 ATOM 462 CA GLY A 56 12.975 68.801 20.044 1.00 29.74 ATOM 463 C GLY A 56 11.504 68.978 20.460 1.00 34.19 ATOM 464 O GLY A 56 10.831 68.637 19.493 1.00 38.86 END