HEADER HYDROLASE(ACID PROTEINASE) 21-SEP-92 1HEF 1HEF 2 COMPND HIV-1 PROTEASE COMPLEXED WITH SKF 108738 (HEF) 1HEF 3 SOURCE HUMAN IMMUNODEFICIENCY VIRUS TYPE 1 RECOMBINANT FORM WITH 1HEF 4 SOURCE 2 SEQUENCE IDENTICAL TO STRAIN IIIB (BH10 ISOLATE) 1HEF 5 AUTHOR K.MURTHY,E.L.WINBORNE,M.D.MINNICH,J.S.CULP,C.DEBOUCK 1HEF 6 REVDAT 1 31-MAY-94 1HEF 0 1HEF 7 JRNL AUTH H.M.KRISHNA MURTHY,E.L.WINBORNE,M.D.MINNICH, 1HEF 8 JRNL AUTH 2 J.S.CULP,C.DEBOUCK 1HEF 9 JRNL TITL THE CRYSTAL STRUCTURES AT 2.2 ANGSTROMS 1HEF 10 JRNL TITL 2 RESOLUTION OF HYDROXYETHYLENE - BASED INHIBITORS 1HEF 11 JRNL TITL 3 BOUND TO HUMAN IMMUNODEFICIENCY VIRUS TYPE 1 1HEF 12 JRNL TITL 4 PROTEASE SHOW THAT THE INHIBITORS ARE PRESENT IN 1HEF 13 JRNL TITL 5 TWO DISTINCT ORIENTATIONS 1HEF 14 JRNL REF J.BIOL.CHEM. V. 267 22770 1992 1HEF 15 JRNL REFN ASTM JBCHA3 US ISSN 0021-9258 0071 1HEF 16 REMARK 1 1HEF 17 REMARK 2 1HEF 18 REMARK 2 RESOLUTION. 2.2 ANGSTROMS. 1HEF 19 REMARK 3 1HEF 20 REMARK 3 REFINEMENT. 1HEF 21 REMARK 3 PROGRAM PROLSQ 1HEF 22 REMARK 3 AUTHORS KONNERT,HENDRICKSON 1HEF 23 REMARK 3 R VALUE 0.159 1HEF 24 REMARK 3 1HEF 25 REMARK 3 NUMBER OF REFLECTIONS 3649 1HEF 26 REMARK 3 RESOLUTION RANGE 5.0 - 2.20 ANGSTROMS 1HEF 27 REMARK 3 DATA CUTOFF 2.0 SIGMA(I) 1HEF 28 REMARK 3 1HEF 29 REMARK 3 NUMBER OF PROTEIN ATOMS 801 1HEF 30 REMARK 3 NUMBER OF SOLVENT ATOMS 23 1HEF 31 REMARK 3 1HEF 32 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES (THE VALUES OF 1HEF 33 REMARK 3 SIGMA, IN PARENTHESES, ARE THE INPUT ESTIMATED 1HEF 34 REMARK 3 STANDARD DEVIATIONS THAT DETERMINE THE RELATIVE 1HEF 35 REMARK 3 WEIGHTS OF THE CORRESPONDING RESTRAINTS) 1HEF 36 REMARK 3 DISTANCE RESTRAINTS (ANGSTROMS) 1HEF 37 REMARK 3 BOND DISTANCE 0.020(0.025) 1HEF 38 REMARK 3 ANGLE DISTANCE 0.044(0.050) 1HEF 39 REMARK 3 PLANAR 1-4 DISTANCE 0.055(0.060) 1HEF 40 REMARK 3 CHIRAL-CENTER RESTRAINT (ANGSTROMS**3) 0.219(0.200) 1HEF 41 REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINT (DEGREES) 1HEF 42 REMARK 3 PLANAR (OMEGA) 1.7(2.0) 1HEF 43 REMARK 3 STAGGERED 23.7(15.0) 1HEF 44 REMARK 3 ORTHONORMAL 30.0(25.0) 1HEF 45 REMARK 4 1HEF 46 REMARK 4 HIV-1 PROTEASE IS A SYMMETRIC DIMER, WHILE THE INHIBITOR 1HEF 47 REMARK 4 (HEF) IS AN ASYMMETRIC MOLECULE. FURTHERMORE, THE 1HEF 48 REMARK 4 INHIBITOR IS SMALL ENOUGH TO BE ENTIRELY CONTAINED WITHIN 1HEF 49 REMARK 4 THE ACTIVE SITE OF THE ENZYME AND, THEREFORE, DOES NOT 1HEF 50 REMARK 4 CONTRIBUTE TO INTER-DIMER CONTACTS. THUS, OF THE TWO 1HEF 51 REMARK 4 POSSIBLE ORIENTATIONS OF THE INHIBITOR, NEITHER IS 1HEF 52 REMARK 4 THERMODYNAMICALLY PREFERRED. IN THE CRYSTAL STRUCTURE, 1HEF 53 REMARK 4 THEREFORE, BOTH ARE REPRESENTED EQUALLY. THE ASYMMETRIC 1HEF 54 REMARK 4 UNIT OF THE CRYSTAL THUS CONSISTS OF ONE PROTEASE MONOMER, 1HEF 55 REMARK 4 AND ONE COPY OF EACH OF TWO POSSIBLE ORIENTATIONS OF THE 1HEF 56 REMARK 4 INHIBITOR. EACH COPY OF THE INHIBITOR REPRESENTS HALF THE 1HEF 57 REMARK 4 TOTAL OCCUPANCY FOR THE INHIBITOR. THE TWO COPIES OF THE 1HEF 58 REMARK 4 INHIBITOR ARE RELATED BY A TWO-FOLD AXIS OF THE SPACE 1HEF 59 REMARK 4 GROUP AS ARE THE TWO MONOMERS OF THE PROTEASE DIMER. 1HEF 60 REMARK 4 HENCE A CALCULATION OF CLOSE CONTACTS WILL GENERATE A 1HEF 61 REMARK 4 LENGTHY LIST OF SPURIOUS, UNACCEPTABLY SHORT DISTANCES 1HEF 62 REMARK 4 BETWEEN ATOMS OF INHIBITOR MOLECULES RELATED BY TWO-FOLD 1HEF 63 REMARK 4 SYMMETRY AXES OF SPACE GROUP P6(1) 2 2. 1HEF 64 REMARK 5 1HEF 65 REMARK 5 SEQUENCE ADVISORY NOTICE: 1HEF 66 REMARK 5 DIFFERENCE BETWEEN SWISS-PROT AND PDB SEQUENCE. 1HEF 67 REMARK 5 1HEF 68 REMARK 5 SWISS-PROT ENTRY NAME: POL_HV1B1 1HEF 69 REMARK 5 1HEF 70 REMARK 5 SWISS-PROT RESIDUE PDB SEQRES 1HEF 71 REMARK 5 NAME NUMBER NAME CHAIN SEQ/INSERT CODE 1HEF 72 REMARK 5 MET 36 ASN 36 1HEF 73 REMARK 5 1HEF 74 REMARK 5 THIS VARIANT OF THE HIV 1 PROTEASE HAS ASN 36 AS CONFIRMED 1HEF 75 REMARK 5 BY INSPECTION OF THE ELECTRON DENSITY. SEE REFERENCES 14, 1HEF 76 REMARK 5 15, AND 16 OF REFERENCE 1 ABOVE, J.BIOL.CHEM. V.267:22770, 1HEF 77 REMARK 5 (1992). 1HEF 78 SEQRES 1 E 99 PRO GLN ILE THR LEU TRP GLN ARG PRO LEU VAL THR ILE 1HEF 79 SEQRES 2 E 99 LYS ILE GLY GLY GLN LEU LYS GLU ALA LEU LEU ASP THR 1HEF 80 SEQRES 3 E 99 GLY ALA ASP ASP THR VAL LEU GLU GLU ASN SER LEU PRO 1HEF 81 SEQRES 4 E 99 GLY ARG TRP LYS PRO LYS MET ILE GLY GLY ILE GLY GLY 1HEF 82 SEQRES 5 E 99 PHE ILE LYS VAL ARG GLN TYR ASP GLN ILE LEU ILE GLU 1HEF 83 SEQRES 6 E 99 ILE CYS GLY HIS LYS ALA ILE GLY THR VAL LEU VAL GLY 1HEF 84 SEQRES 7 E 99 PRO THR PRO VAL ASN ILE ILE GLY ARG ASN LEU LEU THR 1HEF 85 SEQRES 8 E 99 GLN ILE GLY CYS THR LEU ASN PHE 1HEF 86 SEQRES 1 I 8 ALA ALA PHE OHE PHE VAL VAL OME 1HEF 87 FTNOTE 1 1HEF 88 FTNOTE 1 RESIDUES PHE I 203, OHE I 203A, AND PHE I 204 REPRESENT 1HEF 89 FTNOTE 1 PHE-PSI(CHOH-CH2)-PHE. THUS ATOMS C AND N OF PHE I 203 1HEF 90 FTNOTE 1 AND ATOM N OF PHE I 204 ARE NOT PRESENT AND ARE REPLACED 1HEF 91 FTNOTE 1 BY THE ATOMS OF THE HET GROUP OHE. 1HEF 92 HET OHE I 203A 3 HYDROXYETHYLENE GROUP 1HEF 93 HET OME I 206A 2 METHOXY 1HEF 94 FORMUL 2 OHE C2 H4 O 1HEF 95 FORMUL 2 OME C1 H3 O1 1HEF 96 FORMUL 3 HOH *23(H2 O1) 1HEF 97 HELIX 1 1 GLY E 86 GLY E 94 1 ONLY HELIX IN STRUCTURE 1HEF 98 SHEET 1 SHE 8 LYS E 43 GLY E 49 0 1HEF 99 SHEET 2 SHE 8 GLY E 52 ILE E 66 -1 1HEF 100 SHEET 3 SHE 8 HIS E 69 GLY E 78 -1 1HEF 101 SHEET 4 SHE 8 THR E 31 GLU E 34 1 1HEF 102 SHEET 5 SHE 8 ASN E 83 ILE E 85 -1 1HEF 103 SHEET 6 SHE 8 GLN E 18 ASP E 25 1 1HEF 104 SHEET 7 SHE 8 PRO E 9 ILE E 15 -1 1HEF 105 SHEET 8 SHE 8 GLU E 65 ILE E 66 -1 1HEF 106 TURN 1 SU1 GLY E 16 GLN E 18 TURN ON THE SURFACE 1HEF 107 TURN 2 FLP ILE E 50 GLY E 52 PART OF THE "FLAP" 1HEF 108 TURN 3 SU2 ILE E 66 HIS E 69 TURN ON THE SURFACE 1HEF 109 SITE 1 CAT 3 ASP E 25 THR E 26 GLY E 27 1HEF 110 CRYST1 63.070 63.070 83.520 90.00 90.00 120.00 P 61 2 2 12 1HEF 111 ORIGX1 1.000000 0.000000 0.000000 0.00000 1HEF 112 ORIGX2 0.000000 1.000000 0.000000 0.00000 1HEF 113 ORIGX3 0.000000 0.000000 1.000000 0.00000 1HEF 114 SCALE1 0.015855 0.009154 0.000000 0.00000 1HEF 115 SCALE2 0.000000 0.018308 0.000000 0.00000 1HEF 116 SCALE3 0.000000 0.000000 0.011973 0.00000 1HEF 117 ATOM 1 N PRO E 1 -12.527 39.108 31.290 1.00 28.56 1HEF 118 ATOM 2 CA PRO E 1 -12.729 39.255 29.855 1.00 27.86 1HEF 119 ATOM 3 C PRO E 1 -13.549 38.149 29.220 1.00 28.26 1HEF 120 ATOM 4 O PRO E 1 -14.105 37.235 29.862 1.00 27.78 1HEF 121 ATOM 5 CB PRO E 1 -11.273 39.247 29.356 1.00 27.83 1HEF 122 ATOM 6 CG PRO E 1 -10.663 38.117 30.193 1.00 27.27 1HEF 123 ATOM 7 CD PRO E 1 -11.358 38.244 31.546 1.00 27.66 1HEF 124 ATOM 8 N GLN E 2 -13.602 38.301 27.907 1.00 28.88 1HEF 125 ATOM 9 CA GLN E 2 -14.289 37.466 26.903 1.00 29.18 1HEF 126 ATOM 10 C GLN E 2 -13.303 36.711 26.010 1.00 29.05 1HEF 127 ATOM 11 O GLN E 2 -12.594 37.416 25.236 1.00 29.88 1HEF 128 ATOM 12 CB GLN E 2 -14.916 38.483 25.958 1.00 30.97 1HEF 129 ATOM 13 CG GLN E 2 -16.323 38.335 25.560 1.00 38.47 1HEF 130 ATOM 14 CD GLN E 2 -16.752 39.616 24.844 1.00 52.58 1HEF 131 ATOM 15 OE1 GLN E 2 -16.071 40.114 23.966 1.00 49.00 1HEF 132 ATOM 16 NE2 GLN E 2 -17.874 40.155 25.298 1.00 51.31 1HEF 133 ATOM 17 N ILE E 3 -13.260 35.397 26.000 1.00 27.33 1HEF 134 ATOM 18 CA ILE E 3 -12.314 34.674 25.133 1.00 25.70 1HEF 135 ATOM 19 C ILE E 3 -13.002 33.974 23.949 1.00 24.59 1HEF 136 ATOM 20 O ILE E 3 -13.868 33.149 24.205 1.00 23.36 1HEF 137 ATOM 21 CB ILE E 3 -11.639 33.576 26.041 1.00 25.86 1HEF 138 ATOM 22 CG1 ILE E 3 -11.610 34.166 27.509 1.00 25.87 1HEF 139 ATOM 23 CG2 ILE E 3 -10.263 33.114 25.623 1.00 21.14 1HEF 140 ATOM 24 CD1 ILE E 3 -10.526 33.486 28.376 1.00 25.81 1HEF 141 ATOM 25 N THR E 4 -12.605 34.301 22.721 1.00 24.63 1HEF 142 ATOM 26 CA THR E 4 -13.187 33.637 21.519 1.00 23.88 1HEF 143 ATOM 27 C THR E 4 -12.271 32.416 21.378 1.00 22.84 1HEF 144 ATOM 28 O THR E 4 -11.179 32.433 21.972 1.00 19.08 1HEF 145 ATOM 29 CB THR E 4 -13.322 34.463 20.200 1.00 26.22 1HEF 146 ATOM 30 OG1 THR E 4 -11.996 34.991 19.953 1.00 21.23 1HEF 147 ATOM 31 CG2 THR E 4 -14.429 35.490 20.188 1.00 21.11 1HEF 148 ATOM 32 N LEU E 5 -12.755 31.422 20.654 1.00 23.26 1HEF 149 ATOM 33 CA LEU E 5 -12.013 30.170 20.578 1.00 21.19 1HEF 150 ATOM 34 C LEU E 5 -11.185 29.871 19.376 1.00 20.56 1HEF 151 ATOM 35 O LEU E 5 -10.855 28.685 19.208 1.00 17.39 1HEF 152 ATOM 36 CB LEU E 5 -13.021 29.081 21.076 1.00 19.87 1HEF 153 ATOM 37 CG LEU E 5 -13.625 29.337 22.473 1.00 19.64 1HEF 154 ATOM 38 CD1 LEU E 5 -14.827 28.427 22.717 1.00 18.22 1HEF 155 ATOM 39 CD2 LEU E 5 -12.527 28.984 23.536 1.00 19.30 1HEF 156 ATOM 40 N TRP E 6 -10.840 30.992 18.645 1.00 21.43 1HEF 157 ATOM 41 CA TRP E 6 -9.992 30.786 17.465 1.00 21.46 1HEF 158 ATOM 42 C TRP E 6 -8.666 30.228 17.891 1.00 21.36 1HEF 159 ATOM 43 O TRP E 6 -8.100 29.427 17.189 1.00 22.65 1HEF 160 ATOM 44 CB TRP E 6 -9.902 31.996 16.553 1.00 22.89 1HEF 161 ATOM 45 CG TRP E 6 -11.284 32.429 16.176 1.00 12.53 1HEF 162 ATOM 46 CD1 TRP E 6 -12.068 33.276 16.909 1.00 11.30 1HEF 163 ATOM 47 CD2 TRP E 6 -12.080 31.951 15.101 1.00 5.96 1HEF 164 ATOM 48 NE1 TRP E 6 -13.301 33.427 16.310 1.00 14.04 1HEF 165 ATOM 49 CE2 TRP E 6 -13.320 32.600 15.192 1.00 17.38 1HEF 166 ATOM 50 CE3 TRP E 6 -11.815 31.076 14.050 1.00 19.58 1HEF 167 ATOM 51 CZ2 TRP E 6 -14.341 32.443 14.272 1.00 14.02 1HEF 168 ATOM 52 CZ3 TRP E 6 -12.832 30.914 13.106 1.00 20.61 1HEF 169 ATOM 53 CH2 TRP E 6 -14.073 31.550 13.233 1.00 9.30 1HEF 170 ATOM 54 N GLN E 7 -8.145 30.594 19.046 1.00 22.88 1HEF 171 ATOM 55 CA GLN E 7 -6.830 30.028 19.518 1.00 21.30 1HEF 172 ATOM 56 C GLN E 7 -7.093 29.352 20.840 1.00 19.35 1HEF 173 ATOM 57 O GLN E 7 -8.184 29.571 21.386 1.00 18.64 1HEF 174 ATOM 58 CB GLN E 7 -5.727 31.064 19.457 1.00 35.50 1HEF 175 ATOM 59 CG GLN E 7 -4.657 30.689 18.406 1.00 36.26 1HEF 176 ATOM 60 CD GLN E 7 -3.585 31.754 18.327 1.00 44.51 1HEF 177 ATOM 61 OE1 GLN E 7 -3.821 32.977 18.456 1.00 43.89 1HEF 178 ATOM 62 NE2 GLN E 7 -2.367 31.267 18.125 1.00 36.81 1HEF 179 ATOM 63 N ARG E 8 -6.188 28.530 21.361 1.00 20.48 1HEF 180 ATOM 64 CA ARG E 8 -6.496 27.882 22.694 1.00 19.76 1HEF 181 ATOM 65 C ARG E 8 -6.647 28.925 23.784 1.00 17.86 1HEF 182 ATOM 66 O ARG E 8 -5.843 29.858 23.802 1.00 18.82 1HEF 183 ATOM 67 CB ARG E 8 -5.323 26.969 23.093 1.00 14.73 1HEF 184 ATOM 68 CG ARG E 8 -5.334 25.591 22.521 1.00 16.97 1HEF 185 ATOM 69 CD ARG E 8 -4.271 24.733 23.130 1.00 21.45 1HEF 186 ATOM 70 NE ARG E 8 -3.984 23.585 22.363 1.00 15.30 1HEF 187 ATOM 71 CZ ARG E 8 -3.022 22.688 22.463 1.00 22.41 1HEF 188 ATOM 72 NH1 ARG E 8 -2.141 22.785 23.444 1.00 21.78 1HEF 189 ATOM 73 NH2 ARG E 8 -2.954 21.687 21.579 1.00 17.41 1HEF 190 ATOM 74 N PRO E 9 -7.604 28.794 24.696 1.00 18.28 1HEF 191 ATOM 75 CA PRO E 9 -7.756 29.799 25.824 1.00 17.76 1HEF 192 ATOM 76 C PRO E 9 -6.735 29.516 26.926 1.00 19.34 1HEF 193 ATOM 77 O PRO E 9 -6.881 28.706 27.865 1.00 18.91 1HEF 194 ATOM 78 CB PRO E 9 -9.174 29.565 26.236 1.00 17.75 1HEF 195 ATOM 79 CG PRO E 9 -9.430 28.098 25.985 1.00 18.18 1HEF 196 ATOM 80 CD PRO E 9 -8.616 27.769 24.760 1.00 17.86 1HEF 197 ATOM 81 N LEU E 10 -5.614 30.205 26.801 1.00 19.75 1HEF 198 ATOM 82 CA LEU E 10 -4.437 30.116 27.663 1.00 20.30 1HEF 199 ATOM 83 C LEU E 10 -4.427 31.311 28.615 1.00 19.61 1HEF 200 ATOM 84 O LEU E 10 -4.774 32.382 28.092 1.00 21.13 1HEF 201 ATOM 85 CB LEU E 10 -3.166 30.228 26.789 1.00 19.63 1HEF 202 ATOM 86 CG LEU E 10 -2.728 28.858 26.256 1.00 21.19 1HEF 203 ATOM 87 CD1 LEU E 10 -1.256 28.922 25.891 1.00 18.02 1HEF 204 ATOM 88 CD2 LEU E 10 -3.019 27.930 27.437 1.00 12.86 1HEF 205 ATOM 89 N VAL E 11 -4.071 31.015 29.848 1.00 17.80 1HEF 206 ATOM 90 CA VAL E 11 -4.121 32.228 30.750 1.00 19.02 1HEF 207 ATOM 91 C VAL E 11 -3.052 32.020 31.773 1.00 20.91 1HEF 208 ATOM 92 O VAL E 11 -2.470 30.930 32.033 1.00 22.25 1HEF 209 ATOM 93 CB VAL E 11 -5.610 32.357 31.033 1.00 19.26 1HEF 210 ATOM 94 CG1 VAL E 11 -5.952 31.838 32.424 1.00 10.31 1HEF 211 ATOM 95 CG2 VAL E 11 -6.243 33.675 30.712 1.00 17.08 1HEF 212 ATOM 96 N THR E 12 -2.687 33.131 32.366 1.00 21.33 1HEF 213 ATOM 97 CA THR E 12 -1.637 33.176 33.382 1.00 19.97 1HEF 214 ATOM 98 C THR E 12 -2.216 32.804 34.732 1.00 19.25 1HEF 215 ATOM 99 O THR E 12 -3.289 33.331 35.069 1.00 19.92 1HEF 216 ATOM 100 CB THR E 12 -0.951 34.592 33.500 1.00 23.52 1HEF 217 ATOM 101 OG1 THR E 12 -0.574 34.947 32.163 1.00 23.46 1HEF 218 ATOM 102 CG2 THR E 12 0.306 34.553 34.424 1.00 15.43 1HEF 219 ATOM 103 N ILE E 13 -1.507 31.917 35.345 1.00 18.58 1HEF 220 ATOM 104 CA ILE E 13 -1.831 31.461 36.657 1.00 20.66 1HEF 221 ATOM 105 C ILE E 13 -0.537 31.666 37.510 1.00 20.93 1HEF 222 ATOM 106 O ILE E 13 0.595 31.607 37.064 1.00 21.31 1HEF 223 ATOM 107 CB ILE E 13 -2.436 30.039 36.853 1.00 12.96 1HEF 224 ATOM 108 CG1 ILE E 13 -1.298 29.028 36.963 1.00 20.17 1HEF 225 ATOM 109 CG2 ILE E 13 -3.547 29.730 35.848 1.00 26.02 1HEF 226 ATOM 110 CD1 ILE E 13 -1.576 27.546 36.622 1.00 19.60 1HEF 227 ATOM 111 N LYS E 14 -0.808 31.905 38.732 1.00 20.72 1HEF 228 ATOM 112 CA LYS E 14 0.205 32.070 39.760 1.00 20.84 1HEF 229 ATOM 113 C LYS E 14 -0.207 31.059 40.861 1.00 22.19 1HEF 230 ATOM 114 O LYS E 14 -1.310 31.194 41.416 1.00 23.04 1HEF 231 ATOM 115 CB LYS E 14 0.392 33.468 40.346 1.00 23.92 1HEF 232 ATOM 116 CG LYS E 14 1.448 33.368 41.477 1.00 32.50 1HEF 233 ATOM 117 CD LYS E 14 2.160 34.624 41.889 1.00 23.62 1HEF 234 ATOM 118 CE LYS E 14 3.041 34.400 43.085 1.00 18.25 1HEF 235 ATOM 119 NZ LYS E 14 3.804 35.652 43.498 1.00 26.90 1HEF 236 ATOM 120 N ILE E 15 0.635 30.054 41.058 1.00 22.22 1HEF 237 ATOM 121 CA ILE E 15 0.451 29.033 42.056 1.00 24.15 1HEF 238 ATOM 122 C ILE E 15 1.758 28.844 42.875 1.00 26.32 1HEF 239 ATOM 123 O ILE E 15 2.870 28.649 42.362 1.00 27.97 1HEF 240 ATOM 124 CB ILE E 15 0.016 27.591 41.669 1.00 24.08 1HEF 241 ATOM 125 CG1 ILE E 15 0.087 27.404 40.123 1.00 18.29 1HEF 242 ATOM 126 CG2 ILE E 15 -1.250 27.048 42.327 1.00 22.18 1HEF 243 ATOM 127 CD1 ILE E 15 1.635 27.462 39.797 1.00 34.10 1HEF 244 ATOM 128 N GLY E 16 1.595 28.904 44.153 1.00 27.45 1HEF 245 ATOM 129 CA GLY E 16 2.759 28.712 45.052 1.00 28.50 1HEF 246 ATOM 130 C GLY E 16 4.035 29.396 44.609 1.00 28.28 1HEF 247 ATOM 131 O GLY E 16 5.049 28.712 44.441 1.00 28.83 1HEF 248 ATOM 132 N GLY E 17 3.979 30.703 44.464 1.00 26.49 1HEF 249 ATOM 133 CA GLY E 17 5.101 31.560 44.097 1.00 25.41 1HEF 250 ATOM 134 C GLY E 17 5.642 31.377 42.722 1.00 25.82 1HEF 251 ATOM 135 O GLY E 17 6.704 31.969 42.393 1.00 25.73 1HEF 252 ATOM 136 N GLN E 18 4.956 30.560 41.905 1.00 26.00 1HEF 253 ATOM 137 CA GLN E 18 5.373 30.295 40.506 1.00 23.71 1HEF 254 ATOM 138 C GLN E 18 4.282 30.807 39.514 1.00 23.27 1HEF 255 ATOM 139 O GLN E 18 3.062 30.838 39.792 1.00 23.90 1HEF 256 ATOM 140 CB GLN E 18 5.665 28.846 40.330 1.00 21.94 1HEF 257 ATOM 141 CG GLN E 18 6.889 28.239 40.983 1.00 24.02 1HEF 258 ATOM 142 CD GLN E 18 7.025 26.784 40.640 1.00 24.73 1HEF 259 ATOM 143 OE1 GLN E 18 7.486 26.361 39.553 1.00 36.18 1HEF 260 ATOM 144 NE2 GLN E 18 6.593 25.929 41.531 1.00 24.65 1HEF 261 ATOM 145 N LEU E 19 4.779 31.211 38.331 1.00 20.42 1HEF 262 ATOM 146 CA LEU E 19 3.944 31.735 37.261 1.00 20.66 1HEF 263 ATOM 147 C LEU E 19 3.821 30.674 36.170 1.00 20.93 1HEF 264 ATOM 148 O LEU E 19 4.844 30.092 35.723 1.00 21.29 1HEF 265 ATOM 149 CB LEU E 19 4.440 33.037 36.653 1.00 19.70 1HEF 266 ATOM 150 CG LEU E 19 4.370 34.387 37.267 1.00 24.07 1HEF 267 ATOM 151 CD1 LEU E 19 3.506 34.491 38.554 1.00 11.63 1HEF 268 ATOM 152 CD2 LEU E 19 5.777 34.849 37.579 1.00 17.05 1HEF 269 ATOM 153 N LYS E 20 2.586 30.430 35.799 1.00 20.58 1HEF 270 ATOM 154 CA LYS E 20 2.416 29.401 34.728 1.00 20.17 1HEF 271 ATOM 155 C LYS E 20 1.279 29.827 33.823 1.00 20.60 1HEF 272 ATOM 156 O LYS E 20 0.499 30.707 34.193 1.00 21.27 1HEF 273 ATOM 157 CB LYS E 20 2.075 28.005 35.229 1.00 20.42 1HEF 274 ATOM 158 CG LYS E 20 3.291 27.288 35.899 1.00 25.09 1HEF 275 ATOM 159 CD LYS E 20 2.818 26.537 37.104 1.00 30.16 1HEF 276 ATOM 160 CE LYS E 20 3.744 25.427 37.592 1.00 24.51 1HEF 277 ATOM 161 NZ LYS E 20 5.061 25.572 36.954 1.00 25.67 1HEF 278 ATOM 162 N GLU E 21 1.256 29.097 32.721 1.00 20.77 1HEF 279 ATOM 163 CA GLU E 21 0.176 29.255 31.721 1.00 20.18 1HEF 280 ATOM 164 C GLU E 21 -0.660 27.947 31.861 1.00 18.12 1HEF 281 ATOM 165 O GLU E 21 -0.172 26.834 32.032 1.00 17.43 1HEF 282 ATOM 166 CB GLU E 21 0.577 29.376 30.281 1.00 23.66 1HEF 283 ATOM 167 CG GLU E 21 0.742 30.752 29.709 1.00 41.74 1HEF 284 ATOM 168 CD GLU E 21 1.218 30.991 28.325 1.00 51.59 1HEF 285 ATOM 169 OE1 GLU E 21 2.205 30.303 28.028 1.00 59.87 1HEF 286 ATOM 170 OE2 GLU E 21 0.680 31.821 27.590 1.00 50.30 1HEF 287 ATOM 171 N ALA E 22 -1.953 28.169 31.804 1.00 16.93 1HEF 288 ATOM 172 CA ALA E 22 -2.897 27.064 31.872 1.00 17.11 1HEF 289 ATOM 173 C ALA E 22 -3.994 27.284 30.832 1.00 17.06 1HEF 290 ATOM 174 O ALA E 22 -4.348 28.377 30.441 1.00 15.68 1HEF 291 ATOM 175 CB ALA E 22 -3.382 26.890 33.291 1.00 9.35 1HEF 292 ATOM 176 N LEU E 23 -4.581 26.236 30.379 1.00 18.70 1HEF 293 ATOM 177 CA LEU E 23 -5.718 26.181 29.396 1.00 17.31 1HEF 294 ATOM 178 C LEU E 23 -7.018 26.175 30.185 1.00 16.48 1HEF 295 ATOM 179 O LEU E 23 -7.101 25.340 31.166 1.00 14.81 1HEF 296 ATOM 180 CB LEU E 23 -5.424 24.797 28.764 1.00 22.89 1HEF 297 ATOM 181 CG LEU E 23 -5.951 24.326 27.445 1.00 28.16 1HEF 298 ATOM 182 CD1 LEU E 23 -7.079 23.323 27.519 1.00 29.53 1HEF 299 ATOM 183 CD2 LEU E 23 -6.367 25.484 26.573 1.00 19.93 1HEF 300 ATOM 184 N LEU E 24 -7.996 26.995 29.831 1.00 16.99 1HEF 301 ATOM 185 CA LEU E 24 -9.313 26.991 30.546 1.00 18.67 1HEF 302 ATOM 186 C LEU E 24 -10.059 25.834 29.889 1.00 18.61 1HEF 303 ATOM 187 O LEU E 24 -10.376 25.947 28.672 1.00 19.36 1HEF 304 ATOM 188 CB LEU E 24 -10.010 28.314 30.361 1.00 16.67 1HEF 305 ATOM 189 CG LEU E 24 -9.881 29.462 31.344 1.00 29.01 1HEF 306 ATOM 190 CD1 LEU E 24 -8.602 29.460 32.152 1.00 12.71 1HEF 307 ATOM 191 CD2 LEU E 24 -9.967 30.734 30.515 1.00 4.95 1HEF 308 ATOM 192 N ASP E 25 -10.313 24.773 30.585 1.00 17.59 1HEF 309 ATOM 193 CA ASP E 25 -10.963 23.582 30.077 1.00 16.57 1HEF 310 ATOM 194 C ASP E 25 -12.348 23.254 30.632 1.00 18.06 1HEF 311 ATOM 195 O ASP E 25 -12.577 22.745 31.716 1.00 19.72 1HEF 312 ATOM 196 CB ASP E 25 -9.978 22.426 30.148 1.00 16.88 1HEF 313 ATOM 197 CG ASP E 25 -10.406 21.144 29.475 1.00 15.25 1HEF 314 ATOM 198 OD1 ASP E 25 -11.323 21.129 28.674 1.00 13.01 1HEF 315 ATOM 199 OD2 ASP E 25 -9.933 20.021 29.674 1.00 12.67 1HEF 316 ATOM 200 N THR E 26 -13.370 23.552 29.846 1.00 17.09 1HEF 317 ATOM 201 CA THR E 26 -14.756 23.284 30.219 1.00 15.29 1HEF 318 ATOM 202 C THR E 26 -14.972 21.786 30.155 1.00 14.23 1HEF 319 ATOM 203 O THR E 26 -15.887 21.316 30.825 1.00 15.81 1HEF 320 ATOM 204 CB THR E 26 -15.800 24.114 29.398 1.00 20.37 1HEF 321 ATOM 205 OG1 THR E 26 -15.672 23.683 28.029 1.00 22.53 1HEF 322 ATOM 206 CG2 THR E 26 -15.693 25.609 29.629 1.00 14.81 1HEF 323 ATOM 207 N GLY E 27 -14.157 21.083 29.415 1.00 12.10 1HEF 324 ATOM 208 CA GLY E 27 -14.273 19.612 29.298 1.00 12.37 1HEF 325 ATOM 209 C GLY E 27 -13.645 18.882 30.487 1.00 12.39 1HEF 326 ATOM 210 O GLY E 27 -13.532 17.650 30.507 1.00 11.56 1HEF 327 ATOM 211 N ALA E 28 -13.148 19.593 31.498 1.00 14.36 1HEF 328 ATOM 212 CA ALA E 28 -12.490 18.938 32.659 1.00 14.82 1HEF 329 ATOM 213 C ALA E 28 -13.255 19.207 33.975 1.00 14.61 1HEF 330 ATOM 214 O ALA E 28 -13.599 20.370 34.308 1.00 16.90 1HEF 331 ATOM 215 CB ALA E 28 -11.083 19.492 32.805 1.00 14.18 1HEF 332 ATOM 216 N ASP E 29 -13.539 18.190 34.676 1.00 14.33 1HEF 333 ATOM 217 CA ASP E 29 -14.241 18.283 35.972 1.00 14.24 1HEF 334 ATOM 218 C ASP E 29 -13.202 18.853 36.953 1.00 14.72 1HEF 335 ATOM 219 O ASP E 29 -13.631 19.621 37.799 1.00 14.73 1HEF 336 ATOM 220 CB ASP E 29 -14.679 16.922 36.488 1.00 9.78 1HEF 337 ATOM 221 CG ASP E 29 -15.323 16.093 35.405 1.00 11.90 1HEF 338 ATOM 222 OD1 ASP E 29 -16.050 16.755 34.655 1.00 17.43 1HEF 339 ATOM 223 OD2 ASP E 29 -15.177 14.872 35.432 1.00 23.86 1HEF 340 ATOM 224 N ASP E 30 -11.961 18.452 36.732 1.00 15.25 1HEF 341 ATOM 225 CA ASP E 30 -10.878 18.951 37.632 1.00 17.99 1HEF 342 ATOM 226 C ASP E 30 -9.719 19.607 36.856 1.00 20.26 1HEF 343 ATOM 227 O ASP E 30 -9.449 19.455 35.660 1.00 18.76 1HEF 344 ATOM 228 CB ASP E 30 -10.242 17.762 38.396 1.00 17.06 1HEF 345 ATOM 229 CG ASP E 30 -11.139 16.781 39.050 1.00 27.91 1HEF 346 ATOM 230 OD1 ASP E 30 -11.906 17.106 39.969 1.00 35.60 1HEF 347 ATOM 231 OD2 ASP E 30 -11.090 15.619 38.597 1.00 39.82 1HEF 348 ATOM 232 N THR E 31 -8.950 20.278 37.718 1.00 21.67 1HEF 349 ATOM 233 CA THR E 31 -7.727 21.036 37.511 1.00 22.00 1HEF 350 ATOM 234 C THR E 31 -6.533 20.115 37.854 1.00 22.93 1HEF 351 ATOM 235 O THR E 31 -6.343 19.621 38.988 1.00 22.72 1HEF 352 ATOM 236 CB THR E 31 -7.732 22.286 38.519 1.00 18.71 1HEF 353 ATOM 237 OG1 THR E 31 -9.011 22.933 38.308 1.00 20.80 1HEF 354 ATOM 238 CG2 THR E 31 -6.528 23.224 38.378 1.00 13.63 1HEF 355 ATOM 239 N VAL E 32 -5.732 19.922 36.868 1.00 23.37 1HEF 356 ATOM 240 CA VAL E 32 -4.544 19.099 36.834 1.00 25.19 1HEF 357 ATOM 241 C VAL E 32 -3.380 19.916 36.246 1.00 27.49 1HEF 358 ATOM 242 O VAL E 32 -3.376 20.481 35.137 1.00 26.83 1HEF 359 ATOM 243 CB VAL E 32 -4.853 17.728 36.207 1.00 24.93 1HEF 360 ATOM 244 CG1 VAL E 32 -5.601 17.707 34.940 1.00 32.75 1HEF 361 ATOM 245 CG2 VAL E 32 -3.576 16.870 36.084 1.00 20.85 1HEF 362 ATOM 246 N LEU E 33 -2.382 20.036 37.089 1.00 29.05 1HEF 363 ATOM 247 CA LEU E 33 -1.201 20.810 36.680 1.00 31.70 1HEF 364 ATOM 248 C LEU E 33 -0.049 19.796 36.563 1.00 33.14 1HEF 365 ATOM 249 O LEU E 33 -0.058 18.770 37.261 1.00 32.43 1HEF 366 ATOM 250 CB LEU E 33 -0.998 21.884 37.746 1.00 30.27 1HEF 367 ATOM 251 CG LEU E 33 -2.039 22.894 38.142 1.00 33.56 1HEF 368 ATOM 252 CD1 LEU E 33 -1.348 24.033 38.970 1.00 32.45 1HEF 369 ATOM 253 CD2 LEU E 33 -2.715 23.498 36.926 1.00 20.19 1HEF 370 ATOM 254 N GLU E 34 0.872 20.189 35.700 1.00 35.54 1HEF 371 ATOM 255 CA GLU E 34 2.073 19.296 35.525 1.00 37.72 1HEF 372 ATOM 256 C GLU E 34 2.917 19.367 36.784 1.00 38.76 1HEF 373 ATOM 257 O GLU E 34 2.856 20.316 37.606 1.00 39.48 1HEF 374 ATOM 258 CB GLU E 34 2.906 19.722 34.329 1.00 36.45 1HEF 375 ATOM 259 CG GLU E 34 2.467 20.861 33.522 1.00 43.38 1HEF 376 ATOM 260 CD GLU E 34 3.071 21.645 32.467 1.00 47.23 1HEF 377 ATOM 261 OE1 GLU E 34 3.049 21.362 31.281 1.00 50.48 1HEF 378 ATOM 262 OE2 GLU E 34 3.649 22.737 32.835 1.00 32.31 1HEF 379 ATOM 263 N GLU E 35 3.724 18.358 36.985 1.00 40.01 1HEF 380 ATOM 264 CA GLU E 35 4.621 18.286 38.160 1.00 40.77 1HEF 381 ATOM 265 C GLU E 35 5.242 19.643 38.435 1.00 40.72 1HEF 382 ATOM 266 O GLU E 35 5.967 20.196 37.588 1.00 41.25 1HEF 383 ATOM 267 CB GLU E 35 5.736 17.278 37.935 1.00 42.10 1HEF 384 ATOM 268 CG GLU E 35 5.593 15.834 38.406 1.00 36.03 1HEF 385 ATOM 269 CD GLU E 35 5.025 15.645 39.769 1.00 38.58 1HEF 386 ATOM 270 OE1 GLU E 35 5.647 16.264 40.650 1.00 35.13 1HEF 387 ATOM 271 OE2 GLU E 35 4.038 14.979 40.039 1.00 49.90 1HEF 388 ATOM 272 N ASN E 36 4.955 20.204 39.568 1.00 41.41 1HEF 389 ATOM 273 CA ASN E 36 5.518 21.547 39.948 1.00 42.05 1HEF 390 ATOM 274 C ASN E 36 5.861 21.298 41.426 1.00 42.46 1HEF 391 ATOM 275 O ASN E 36 5.331 20.273 41.918 1.00 41.70 1HEF 392 ATOM 276 CB ASN E 36 4.658 22.742 39.608 1.00 39.83 1HEF 393 ATOM 277 CG ASN E 36 3.335 22.955 40.252 1.00 38.05 1HEF 394 ATOM 278 OD1 ASN E 36 2.706 22.100 40.903 1.00 35.77 1HEF 395 ATOM 279 ND2 ASN E 36 2.609 24.054 40.267 1.00 25.08 1HEF 396 ATOM 280 N SER E 37 6.676 22.160 42.001 1.00 43.58 1HEF 397 ATOM 281 CA SER E 37 7.041 21.973 43.425 1.00 45.01 1HEF 398 ATOM 282 C SER E 37 6.025 22.709 44.297 1.00 45.47 1HEF 399 ATOM 283 O SER E 37 6.048 23.942 44.436 1.00 45.54 1HEF 400 ATOM 284 CB SER E 37 8.449 22.443 43.721 1.00 48.92 1HEF 401 ATOM 285 OG SER E 37 8.470 23.296 44.844 1.00 57.54 1HEF 402 ATOM 286 N LEU E 38 5.165 21.899 44.853 1.00 46.18 1HEF 403 ATOM 287 CA LEU E 38 4.086 22.385 45.743 1.00 47.66 1HEF 404 ATOM 288 C LEU E 38 4.265 21.756 47.136 1.00 49.12 1HEF 405 ATOM 289 O LEU E 38 4.501 20.554 47.262 1.00 49.29 1HEF 406 ATOM 290 CB LEU E 38 2.793 22.056 45.042 1.00 41.21 1HEF 407 ATOM 291 CG LEU E 38 1.517 22.797 45.307 1.00 38.80 1HEF 408 ATOM 292 CD1 LEU E 38 1.574 24.239 44.811 1.00 38.02 1HEF 409 ATOM 293 CD2 LEU E 38 0.388 22.068 44.547 1.00 32.23 1HEF 410 ATOM 294 N PRO E 39 4.144 22.618 48.147 1.00 49.73 1HEF 411 ATOM 295 CA PRO E 39 4.289 22.195 49.542 1.00 49.93 1HEF 412 ATOM 296 C PRO E 39 2.962 21.748 50.125 1.00 49.51 1HEF 413 ATOM 297 O PRO E 39 1.899 22.257 49.733 1.00 49.82 1HEF 414 ATOM 298 CB PRO E 39 4.803 23.491 50.204 1.00 50.21 1HEF 415 ATOM 299 CG PRO E 39 3.996 24.550 49.490 1.00 50.08 1HEF 416 ATOM 300 CD PRO E 39 3.868 24.059 48.055 1.00 50.04 1HEF 417 ATOM 301 N GLY E 40 3.037 20.829 51.063 1.00 48.64 1HEF 418 ATOM 302 CA GLY E 40 1.877 20.275 51.760 1.00 47.49 1HEF 419 ATOM 303 C GLY E 40 1.799 18.768 51.587 1.00 46.29 1HEF 420 ATOM 304 O GLY E 40 2.692 18.159 50.971 1.00 45.86 1HEF 421 ATOM 305 N ARG E 41 0.736 18.220 52.162 1.00 46.12 1HEF 422 ATOM 306 CA ARG E 41 0.522 16.750 52.050 1.00 46.28 1HEF 423 ATOM 307 C ARG E 41 -0.363 16.552 50.825 1.00 46.69 1HEF 424 ATOM 308 O ARG E 41 -1.081 17.500 50.457 1.00 47.49 1HEF 425 ATOM 309 CB ARG E 41 -0.080 16.138 53.282 1.00 40.35 1HEF 426 ATOM 310 CG ARG E 41 -0.667 17.016 54.334 1.00 52.50 1HEF 427 ATOM 311 CD ARG E 41 -2.146 17.099 54.338 1.00 57.18 1HEF 428 ATOM 312 NE ARG E 41 -2.684 17.414 55.676 1.00 55.09 1HEF 429 ATOM 313 CZ ARG E 41 -3.911 17.944 55.803 1.00 63.41 1HEF 430 ATOM 314 NH1 ARG E 41 -4.572 18.301 54.703 1.00 63.08 1HEF 431 ATOM 315 NH2 ARG E 41 -4.475 18.174 56.979 1.00 63.78 1HEF 432 ATOM 316 N TRP E 42 -0.326 15.399 50.205 1.00 47.06 1HEF 433 ATOM 317 CA TRP E 42 -1.137 15.059 49.024 1.00 47.59 1HEF 434 ATOM 318 C TRP E 42 -1.402 13.553 49.117 1.00 47.98 1HEF 435 ATOM 319 O TRP E 42 -0.652 12.794 49.749 1.00 48.51 1HEF 436 ATOM 320 CB TRP E 42 -0.398 15.347 47.711 1.00 39.85 1HEF 437 ATOM 321 CG TRP E 42 0.917 14.626 47.759 1.00 53.59 1HEF 438 ATOM 322 CD1 TRP E 42 2.084 15.073 48.305 1.00 53.51 1HEF 439 ATOM 323 CD2 TRP E 42 1.170 13.299 47.286 1.00 52.70 1HEF 440 ATOM 324 NE1 TRP E 42 3.052 14.124 48.180 1.00 50.03 1HEF 441 ATOM 325 CE2 TRP E 42 2.531 13.025 47.558 1.00 51.66 1HEF 442 ATOM 326 CE3 TRP E 42 0.387 12.339 46.652 1.00 54.56 1HEF 443 ATOM 327 CZ2 TRP E 42 3.131 11.826 47.206 1.00 47.76 1HEF 444 ATOM 328 CZ3 TRP E 42 0.985 11.137 46.313 1.00 48.44 1HEF 445 ATOM 329 CH2 TRP E 42 2.317 10.891 46.577 1.00 53.62 1HEF 446 ATOM 330 N LYS E 43 -2.466 13.168 48.455 1.00 47.42 1HEF 447 ATOM 331 CA LYS E 43 -2.885 11.735 48.424 1.00 45.53 1HEF 448 ATOM 332 C LYS E 43 -2.814 11.277 46.972 1.00 44.63 1HEF 449 ATOM 333 O LYS E 43 -2.805 12.105 46.046 1.00 44.98 1HEF 450 ATOM 334 CB LYS E 43 -4.294 11.631 48.928 1.00 33.73 1HEF 451 ATOM 335 CG LYS E 43 -4.627 12.805 49.884 1.00 27.20 1HEF 452 ATOM 336 CD LYS E 43 -6.152 13.052 49.876 1.00 20.27 1HEF 453 ATOM 337 CE LYS E 43 -6.482 13.767 51.193 1.00 30.66 1HEF 454 ATOM 338 NZ LYS E 43 -7.839 14.371 51.010 1.00 39.24 1HEF 455 ATOM 339 N PRO E 44 -2.723 9.981 46.825 1.00 44.20 1HEF 456 ATOM 340 CA PRO E 44 -2.652 9.365 45.473 1.00 42.83 1HEF 457 ATOM 341 C PRO E 44 -4.066 9.384 44.920 1.00 41.92 1HEF 458 ATOM 342 O PRO E 44 -5.075 9.205 45.667 1.00 42.08 1HEF 459 ATOM 343 CB PRO E 44 -2.087 8.001 45.771 1.00 42.01 1HEF 460 ATOM 344 CG PRO E 44 -2.602 7.634 47.121 1.00 42.10 1HEF 461 ATOM 345 CD PRO E 44 -2.714 8.948 47.885 1.00 43.62 1HEF 462 ATOM 346 N LYS E 45 -4.149 9.601 43.626 1.00 40.37 1HEF 463 ATOM 347 CA LYS E 45 -5.481 9.625 43.000 1.00 38.42 1HEF 464 ATOM 348 C LYS E 45 -5.321 9.383 41.508 1.00 37.86 1HEF 465 ATOM 349 O LYS E 45 -4.206 9.516 41.006 1.00 38.40 1HEF 466 ATOM 350 CB LYS E 45 -6.226 10.888 43.293 1.00 36.01 1HEF 467 ATOM 351 CG LYS E 45 -7.622 10.898 42.703 1.00 36.18 1HEF 468 ATOM 352 CD LYS E 45 -8.386 12.150 43.120 1.00 36.97 1HEF 469 ATOM 353 CE LYS E 45 -9.258 12.580 41.923 1.00 39.23 1HEF 470 ATOM 354 NZ LYS E 45 -10.041 13.754 42.335 1.00 42.73 1HEF 471 ATOM 355 N MET E 46 -6.423 9.024 40.882 1.00 36.97 1HEF 472 ATOM 356 CA MET E 46 -6.405 8.732 39.428 1.00 35.62 1HEF 473 ATOM 357 C MET E 46 -7.564 9.429 38.738 1.00 34.12 1HEF 474 ATOM 358 O MET E 46 -8.711 9.438 39.222 1.00 34.12 1HEF 475 ATOM 359 CB MET E 46 -6.529 7.195 39.245 1.00 46.24 1HEF 476 ATOM 360 CG MET E 46 -5.947 6.511 40.455 1.00 45.56 1HEF 477 ATOM 361 SD MET E 46 -6.052 4.707 40.353 1.00 50.58 1HEF 478 ATOM 362 CE MET E 46 -5.822 4.396 38.580 1.00 57.04 1HEF 479 ATOM 363 N ILE E 47 -7.249 10.023 37.630 1.00 32.92 1HEF 480 ATOM 364 CA ILE E 47 -8.088 10.753 36.703 1.00 31.71 1HEF 481 ATOM 365 C ILE E 47 -8.048 10.113 35.314 1.00 30.56 1HEF 482 ATOM 366 O ILE E 47 -6.994 9.611 34.896 1.00 30.58 1HEF 483 ATOM 367 CB ILE E 47 -7.595 12.250 36.624 1.00 26.63 1HEF 484 ATOM 368 CG1 ILE E 47 -6.169 12.247 36.008 1.00 29.59 1HEF 485 ATOM 369 CG2 ILE E 47 -7.688 12.987 37.968 1.00 36.09 1HEF 486 ATOM 370 CD1 ILE E 47 -5.641 13.525 35.300 1.00 17.90 1HEF 487 ATOM 371 N GLY E 48 -9.160 10.104 34.610 1.00 29.99 1HEF 488 ATOM 372 CA GLY E 48 -9.183 9.525 33.235 1.00 31.25 1HEF 489 ATOM 373 C GLY E 48 -9.382 10.723 32.278 1.00 30.66 1HEF 490 ATOM 374 O GLY E 48 -9.888 11.755 32.712 1.00 30.75 1HEF 491 ATOM 375 N GLY E 49 -9.012 10.513 31.042 1.00 30.43 1HEF 492 ATOM 376 CA GLY E 49 -9.092 11.526 29.951 1.00 30.53 1HEF 493 ATOM 377 C GLY E 49 -9.237 10.735 28.666 1.00 30.69 1HEF 494 ATOM 378 O GLY E 49 -9.653 9.570 28.798 1.00 30.44 1HEF 495 ATOM 379 N ILE E 50 -8.942 11.295 27.496 1.00 32.00 1HEF 496 ATOM 380 CA ILE E 50 -9.122 10.464 26.315 1.00 33.65 1HEF 497 ATOM 381 C ILE E 50 -8.122 9.356 26.218 1.00 35.93 1HEF 498 ATOM 382 O ILE E 50 -8.749 8.407 25.716 1.00 36.56 1HEF 499 ATOM 383 CB ILE E 50 -9.459 11.055 24.930 1.00 36.63 1HEF 500 ATOM 384 CG1 ILE E 50 -8.263 11.850 24.374 1.00 39.80 1HEF 501 ATOM 385 CG2 ILE E 50 -10.822 11.753 24.782 1.00 32.21 1HEF 502 ATOM 386 CD1 ILE E 50 -7.370 10.939 23.458 1.00 46.74 1HEF 503 ATOM 387 N GLY E 51 -6.927 9.078 26.474 1.00 36.82 1HEF 504 ATOM 388 CA GLY E 51 -6.251 7.792 26.226 1.00 37.39 1HEF 505 ATOM 389 C GLY E 51 -6.212 6.885 27.433 1.00 38.11 1HEF 506 ATOM 390 O GLY E 51 -5.833 5.684 27.302 1.00 38.74 1HEF 507 ATOM 391 N GLY E 52 -6.592 7.379 28.602 1.00 37.55 1HEF 508 ATOM 392 CA GLY E 52 -6.545 6.478 29.776 1.00 37.66 1HEF 509 ATOM 393 C GLY E 52 -6.655 7.220 31.090 1.00 36.99 1HEF 510 ATOM 394 O GLY E 52 -7.246 8.300 31.176 1.00 37.44 1HEF 511 ATOM 395 N PHE E 53 -6.039 6.617 32.068 1.00 35.59 1HEF 512 ATOM 396 CA PHE E 53 -5.949 7.018 33.464 1.00 35.21 1HEF 513 ATOM 397 C PHE E 53 -4.496 7.276 33.830 1.00 36.11 1HEF 514 ATOM 398 O PHE E 53 -3.607 6.515 33.421 1.00 36.23 1HEF 515 ATOM 399 CB PHE E 53 -6.546 5.873 34.369 1.00 36.30 1HEF 516 ATOM 400 CG PHE E 53 -7.572 5.125 33.522 1.00 41.19 1HEF 517 ATOM 401 CD1 PHE E 53 -7.093 4.302 32.478 1.00 34.50 1HEF 518 ATOM 402 CD2 PHE E 53 -8.928 5.292 33.671 1.00 43.72 1HEF 519 ATOM 403 CE1 PHE E 53 -7.969 3.634 31.611 1.00 36.83 1HEF 520 ATOM 404 CE2 PHE E 53 -9.814 4.636 32.841 1.00 42.11 1HEF 521 ATOM 405 CZ PHE E 53 -9.340 3.796 31.801 1.00 38.53 1HEF 522 ATOM 406 N ILE E 54 -4.293 8.364 34.542 1.00 36.39 1HEF 523 ATOM 407 CA ILE E 54 -2.942 8.719 35.022 1.00 36.22 1HEF 524 ATOM 408 C ILE E 54 -3.166 8.856 36.566 1.00 35.50 1HEF 525 ATOM 409 O ILE E 54 -4.313 9.185 37.002 1.00 34.82 1HEF 526 ATOM 410 CB ILE E 54 -2.362 9.994 34.381 1.00 38.42 1HEF 527 ATOM 411 CG1 ILE E 54 -3.179 11.230 34.892 1.00 36.53 1HEF 528 ATOM 412 CG2 ILE E 54 -2.275 9.985 32.843 1.00 42.19 1HEF 529 ATOM 413 CD1 ILE E 54 -2.399 12.568 34.771 1.00 33.56 1HEF 530 ATOM 414 N LYS E 55 -2.103 8.593 37.285 1.00 34.09 1HEF 531 ATOM 415 CA LYS E 55 -2.206 8.717 38.766 1.00 34.48 1HEF 532 ATOM 416 C LYS E 55 -1.713 10.122 39.047 1.00 34.49 1HEF 533 ATOM 417 O LYS E 55 -0.738 10.573 38.412 1.00 34.70 1HEF 534 ATOM 418 CB LYS E 55 -1.469 7.641 39.522 1.00 39.65 1HEF 535 ATOM 419 CG LYS E 55 -1.608 6.241 38.850 1.00 25.29 1HEF 536 ATOM 420 CD LYS E 55 -0.417 6.045 37.889 1.00 31.49 1HEF 537 ATOM 421 CE LYS E 55 -0.471 4.761 37.112 1.00 37.93 1HEF 538 ATOM 422 NZ LYS E 55 -0.100 3.609 38.008 1.00 38.80 1HEF 539 ATOM 423 N VAL E 56 -2.378 10.792 39.945 1.00 34.59 1HEF 540 ATOM 424 CA VAL E 56 -1.980 12.189 40.295 1.00 34.54 1HEF 541 ATOM 425 C VAL E 56 -1.949 12.265 41.825 1.00 34.48 1HEF 542 ATOM 426 O VAL E 56 -2.257 11.232 42.446 1.00 35.68 1HEF 543 ATOM 427 CB VAL E 56 -3.084 13.135 39.765 1.00 30.07 1HEF 544 ATOM 428 CG1 VAL E 56 -3.121 13.180 38.247 1.00 32.09 1HEF 545 ATOM 429 CG2 VAL E 56 -4.443 12.732 40.343 1.00 32.82 1HEF 546 ATOM 430 N ARG E 57 -1.586 13.463 42.273 1.00 32.06 1HEF 547 ATOM 431 CA ARG E 57 -1.557 13.710 43.725 1.00 31.98 1HEF 548 ATOM 432 C ARG E 57 -2.545 14.879 43.987 1.00 30.77 1HEF 549 ATOM 433 O ARG E 57 -2.431 15.864 43.282 1.00 31.17 1HEF 550 ATOM 434 CB ARG E 57 -0.235 14.165 44.290 1.00 37.49 1HEF 551 ATOM 435 CG ARG E 57 1.058 13.554 43.932 1.00 36.81 1HEF 552 ATOM 436 CD ARG E 57 2.228 14.490 44.183 1.00 43.84 1HEF 553 ATOM 437 NE ARG E 57 3.167 14.110 43.141 1.00 60.67 1HEF 554 ATOM 438 CZ ARG E 57 4.431 13.809 43.144 1.00 63.43 1HEF 555 ATOM 439 NH1 ARG E 57 5.116 13.869 44.275 1.00 64.07 1HEF 556 ATOM 440 NH2 ARG E 57 5.207 13.431 42.128 1.00 62.06 1HEF 557 ATOM 441 N GLN E 58 -3.447 14.715 44.920 1.00 29.91 1HEF 558 ATOM 442 CA GLN E 58 -4.402 15.735 45.258 1.00 29.52 1HEF 559 ATOM 443 C GLN E 58 -3.864 16.488 46.505 1.00 30.72 1HEF 560 ATOM 444 O GLN E 58 -3.408 15.988 47.514 1.00 31.04 1HEF 561 ATOM 445 CB GLN E 58 -5.850 15.546 45.435 1.00 39.99 1HEF 562 ATOM 446 CG GLN E 58 -6.690 14.374 45.206 1.00 41.62 1HEF 563 ATOM 447 CD GLN E 58 -8.008 14.425 45.975 1.00 47.59 1HEF 564 ATOM 448 OE1 GLN E 58 -8.314 15.372 46.714 1.00 47.23 1HEF 565 ATOM 449 NE2 GLN E 58 -8.790 13.354 45.772 1.00 50.74 1HEF 566 ATOM 450 N TYR E 59 -4.029 17.768 46.288 1.00 31.30 1HEF 567 ATOM 451 CA TYR E 59 -3.701 18.892 47.159 1.00 30.15 1HEF 568 ATOM 452 C TYR E 59 -5.045 19.655 47.214 1.00 31.00 1HEF 569 ATOM 453 O TYR E 59 -5.682 19.977 46.177 1.00 30.73 1HEF 570 ATOM 454 CB TYR E 59 -2.576 19.664 46.568 1.00 26.43 1HEF 571 ATOM 455 CG TYR E 59 -1.177 19.186 46.562 1.00 24.50 1HEF 572 ATOM 456 CD1 TYR E 59 -0.688 18.307 45.594 1.00 27.70 1HEF 573 ATOM 457 CD2 TYR E 59 -0.265 19.655 47.543 1.00 32.59 1HEF 574 ATOM 458 CE1 TYR E 59 0.632 17.881 45.579 1.00 29.54 1HEF 575 ATOM 459 CE2 TYR E 59 1.052 19.232 47.533 1.00 32.85 1HEF 576 ATOM 460 CZ TYR E 59 1.505 18.367 46.575 1.00 33.69 1HEF 577 ATOM 461 OH TYR E 59 2.811 17.963 46.597 1.00 39.97 1HEF 578 ATOM 462 N ASP E 60 -5.426 19.880 48.451 1.00 30.83 1HEF 579 ATOM 463 CA ASP E 60 -6.672 20.581 48.805 1.00 30.75 1HEF 580 ATOM 464 C ASP E 60 -6.246 21.910 49.430 1.00 31.74 1HEF 581 ATOM 465 O ASP E 60 -5.092 22.036 49.902 1.00 32.45 1HEF 582 ATOM 466 CB ASP E 60 -7.459 19.795 49.857 1.00 39.89 1HEF 583 ATOM 467 CG ASP E 60 -7.845 18.418 49.447 1.00 46.98 1HEF 584 ATOM 468 OD1 ASP E 60 -7.370 17.880 48.428 1.00 52.08 1HEF 585 ATOM 469 OD2 ASP E 60 -8.658 17.805 50.147 1.00 55.08 1HEF 586 ATOM 470 N GLN E 61 -7.198 22.812 49.378 1.00 32.52 1HEF 587 ATOM 471 CA GLN E 61 -7.005 24.151 49.953 1.00 32.85 1HEF 588 ATOM 472 C GLN E 61 -5.884 24.881 49.262 1.00 31.86 1HEF 589 ATOM 473 O GLN E 61 -5.151 25.665 49.933 1.00 32.16 1HEF 590 ATOM 474 CB GLN E 61 -6.610 23.946 51.441 1.00 38.55 1HEF 591 ATOM 475 CG GLN E 61 -7.687 23.200 52.229 1.00 44.59 1HEF 592 ATOM 476 CD GLN E 61 -8.441 24.244 53.037 1.00 47.70 1HEF 593 ATOM 477 OE1 GLN E 61 -8.422 24.310 54.275 1.00 32.02 1HEF 594 ATOM 478 NE2 GLN E 61 -9.092 25.108 52.252 1.00 46.93 1HEF 595 ATOM 479 N ILE E 62 -5.733 24.617 47.975 1.00 30.51 1HEF 596 ATOM 480 CA ILE E 62 -4.658 25.309 47.236 1.00 28.73 1HEF 597 ATOM 481 C ILE E 62 -5.183 26.631 46.646 1.00 27.63 1HEF 598 ATOM 482 O ILE E 62 -6.195 26.692 45.988 1.00 25.91 1HEF 599 ATOM 483 CB ILE E 62 -3.936 24.418 46.190 1.00 26.41 1HEF 600 ATOM 484 CG1 ILE E 62 -3.182 23.226 46.807 1.00 29.72 1HEF 601 ATOM 485 CG2 ILE E 62 -2.989 25.213 45.225 1.00 24.85 1HEF 602 ATOM 486 CD1 ILE E 62 -2.441 23.448 48.147 1.00 34.96 1HEF 603 ATOM 487 N LEU E 63 -4.433 27.699 46.865 1.00 27.75 1HEF 604 ATOM 488 CA LEU E 63 -4.658 29.023 46.407 1.00 29.32 1HEF 605 ATOM 489 C LEU E 63 -4.045 29.120 44.998 1.00 30.19 1HEF 606 ATOM 490 O LEU E 63 -2.927 28.649 44.823 1.00 30.37 1HEF 607 ATOM 491 CB LEU E 63 -3.992 30.053 47.350 1.00 31.76 1HEF 608 ATOM 492 CG LEU E 63 -3.899 31.483 46.916 1.00 26.07 1HEF 609 ATOM 493 CD1 LEU E 63 -5.179 32.282 46.882 1.00 21.67 1HEF 610 ATOM 494 CD2 LEU E 63 -3.011 32.211 47.980 1.00 20.23 1HEF 611 ATOM 495 N ILE E 64 -4.778 29.729 44.103 1.00 30.04 1HEF 612 ATOM 496 CA ILE E 64 -4.379 29.971 42.726 1.00 29.00 1HEF 613 ATOM 497 C ILE E 64 -4.941 31.323 42.272 1.00 28.77 1HEF 614 ATOM 498 O ILE E 64 -6.019 31.765 42.635 1.00 28.63 1HEF 615 ATOM 499 CB ILE E 64 -4.815 28.851 41.740 1.00 35.14 1HEF 616 ATOM 500 CG1 ILE E 64 -4.267 27.457 42.138 1.00 32.62 1HEF 617 ATOM 501 CG2 ILE E 64 -4.378 29.050 40.246 1.00 31.68 1HEF 618 ATOM 502 CD1 ILE E 64 -4.611 26.466 40.960 1.00 42.67 1HEF 619 ATOM 503 N GLU E 65 -4.148 31.956 41.439 1.00 29.57 1HEF 620 ATOM 504 CA GLU E 65 -4.529 33.240 40.856 1.00 30.16 1HEF 621 ATOM 505 C GLU E 65 -4.635 32.995 39.328 1.00 29.76 1HEF 622 ATOM 506 O GLU E 65 -3.595 32.875 38.679 1.00 29.55 1HEF 623 ATOM 507 CB GLU E 65 -3.622 34.389 41.107 1.00 26.59 1HEF 624 ATOM 508 CG GLU E 65 -3.544 34.910 42.537 1.00 31.98 1HEF 625 ATOM 509 CD GLU E 65 -3.448 36.421 42.529 1.00 39.76 1HEF 626 ATOM 510 OE1 GLU E 65 -4.120 37.149 41.824 1.00 47.01 1HEF 627 ATOM 511 OE2 GLU E 65 -2.574 36.724 43.358 1.00 47.11 1HEF 628 ATOM 512 N ILE E 66 -5.878 32.910 38.919 1.00 29.67 1HEF 629 ATOM 513 CA ILE E 66 -6.180 32.686 37.495 1.00 29.72 1HEF 630 ATOM 514 C ILE E 66 -6.490 34.067 36.882 1.00 31.37 1HEF 631 ATOM 515 O ILE E 66 -7.519 34.700 37.187 1.00 31.63 1HEF 632 ATOM 516 CB ILE E 66 -7.301 31.660 37.369 1.00 25.01 1HEF 633 ATOM 517 CG1 ILE E 66 -6.903 30.360 38.174 1.00 19.23 1HEF 634 ATOM 518 CG2 ILE E 66 -7.823 31.273 35.958 1.00 18.28 1HEF 635 ATOM 519 CD1 ILE E 66 -8.242 29.703 38.663 1.00 16.82 1HEF 636 ATOM 520 N CYS E 67 -5.596 34.496 36.032 1.00 32.38 1HEF 637 ATOM 521 CA CYS E 67 -5.773 35.788 35.360 1.00 34.53 1HEF 638 ATOM 522 C CYS E 67 -6.167 36.810 36.418 1.00 34.78 1HEF 639 ATOM 523 O CYS E 67 -7.176 37.491 36.290 1.00 34.56 1HEF 640 ATOM 524 CB CYS E 67 -6.819 35.651 34.227 1.00 46.22 1HEF 641 ATOM 525 SG CYS E 67 -6.437 36.799 32.848 1.00 53.74 1HEF 642 ATOM 526 N GLY E 68 -5.352 36.919 37.437 1.00 35.71 1HEF 643 ATOM 527 CA GLY E 68 -5.559 37.836 38.540 1.00 37.47 1HEF 644 ATOM 528 C GLY E 68 -6.663 37.417 39.483 1.00 38.67 1HEF 645 ATOM 529 O GLY E 68 -6.715 38.033 40.595 1.00 40.44 1HEF 646 ATOM 530 N HIS E 69 -7.550 36.500 39.167 1.00 37.25 1HEF 647 ATOM 531 CA HIS E 69 -8.644 36.063 40.037 1.00 34.92 1HEF 648 ATOM 532 C HIS E 69 -8.167 34.930 40.955 1.00 33.57 1HEF 649 ATOM 533 O HIS E 69 -7.656 33.907 40.470 1.00 33.54 1HEF 650 ATOM 534 CB HIS E 69 -9.901 35.551 39.296 1.00 35.20 1HEF 651 ATOM 535 CG HIS E 69 -10.444 36.575 38.363 1.00 37.36 1HEF 652 ATOM 536 ND1 HIS E 69 -9.707 37.655 37.918 1.00 43.00 1HEF 653 ATOM 537 CD2 HIS E 69 -11.659 36.667 37.780 1.00 32.19 1HEF 654 ATOM 538 CE1 HIS E 69 -10.464 38.365 37.081 1.00 39.68 1HEF 655 ATOM 539 NE2 HIS E 69 -11.656 37.787 36.995 1.00 46.16 1HEF 656 ATOM 540 N LYS E 70 -8.343 35.175 42.226 1.00 31.12 1HEF 657 ATOM 541 CA LYS E 70 -7.951 34.256 43.280 1.00 28.90 1HEF 658 ATOM 542 C LYS E 70 -9.132 33.297 43.483 1.00 26.31 1HEF 659 ATOM 543 O LYS E 70 -10.256 33.745 43.261 1.00 26.13 1HEF 660 ATOM 544 CB LYS E 70 -7.548 34.821 44.604 1.00 33.89 1HEF 661 ATOM 545 CG LYS E 70 -6.341 35.768 44.590 1.00 37.87 1HEF 662 ATOM 546 CD LYS E 70 -6.350 36.532 45.921 1.00 44.91 1HEF 663 ATOM 547 CE LYS E 70 -6.322 38.038 45.664 1.00 54.20 1HEF 664 ATOM 548 NZ LYS E 70 -6.627 38.794 46.916 1.00 50.86 1HEF 665 ATOM 549 N ALA E 71 -8.746 32.125 43.862 1.00 24.42 1HEF 666 ATOM 550 CA ALA E 71 -9.666 31.025 44.123 1.00 23.61 1HEF 667 ATOM 551 C ALA E 71 -8.883 30.032 44.960 1.00 22.46 1HEF 668 ATOM 552 O ALA E 71 -7.628 30.113 44.864 1.00 22.14 1HEF 669 ATOM 553 CB ALA E 71 -10.095 30.411 42.775 1.00 26.87 1HEF 670 ATOM 554 N ILE E 72 -9.554 29.189 45.690 1.00 23.14 1HEF 671 ATOM 555 CA ILE E 72 -8.996 28.121 46.521 1.00 23.67 1HEF 672 ATOM 556 C ILE E 72 -9.740 26.836 46.147 1.00 23.01 1HEF 673 ATOM 557 O ILE E 72 -10.990 26.828 45.974 1.00 22.39 1HEF 674 ATOM 558 CB ILE E 72 -9.047 28.405 48.076 1.00 25.34 1HEF 675 ATOM 559 CG1 ILE E 72 -8.356 29.742 48.249 1.00 27.94 1HEF 676 ATOM 560 CG2 ILE E 72 -8.410 27.229 48.893 1.00 17.75 1HEF 677 ATOM 561 CD1 ILE E 72 -7.715 30.293 49.474 1.00 20.52 1HEF 678 ATOM 562 N GLY E 73 -8.933 25.779 46.073 1.00 21.77 1HEF 679 ATOM 563 CA GLY E 73 -9.603 24.501 45.717 1.00 20.83 1HEF 680 ATOM 564 C GLY E 73 -8.575 23.429 45.559 1.00 20.33 1HEF 681 ATOM 565 O GLY E 73 -7.427 23.568 45.941 1.00 20.70 1HEF 682 ATOM 566 N THR E 74 -9.115 22.382 45.014 1.00 22.50 1HEF 683 ATOM 567 CA THR E 74 -8.424 21.138 44.690 1.00 23.64 1HEF 684 ATOM 568 C THR E 74 -7.714 21.331 43.356 1.00 24.27 1HEF 685 ATOM 569 O THR E 74 -8.290 21.856 42.386 1.00 23.74 1HEF 686 ATOM 570 CB THR E 74 -9.349 19.877 44.803 1.00 24.69 1HEF 687 ATOM 571 OG1 THR E 74 -9.939 20.047 46.120 1.00 30.82 1HEF 688 ATOM 572 CG2 THR E 74 -8.628 18.488 44.733 1.00 18.03 1HEF 689 ATOM 573 N VAL E 75 -6.475 20.940 43.361 1.00 24.65 1HEF 690 ATOM 574 CA VAL E 75 -5.453 20.920 42.366 1.00 26.05 1HEF 691 ATOM 575 C VAL E 75 -4.756 19.527 42.329 1.00 26.42 1HEF 692 ATOM 576 O VAL E 75 -4.253 19.022 43.302 1.00 25.96 1HEF 693 ATOM 577 CB VAL E 75 -4.361 21.983 42.607 1.00 22.69 1HEF 694 ATOM 578 CG1 VAL E 75 -3.336 21.980 41.481 1.00 20.19 1HEF 695 ATOM 579 CG2 VAL E 75 -4.887 23.376 42.905 1.00 19.35 1HEF 696 ATOM 580 N LEU E 76 -4.750 18.939 41.145 1.00 27.41 1HEF 697 ATOM 581 CA LEU E 76 -4.133 17.632 40.919 1.00 27.22 1HEF 698 ATOM 582 C LEU E 76 -2.812 17.809 40.197 1.00 29.47 1HEF 699 ATOM 583 O LEU E 76 -2.730 18.518 39.169 1.00 30.90 1HEF 700 ATOM 584 CB LEU E 76 -5.200 16.798 40.228 1.00 20.34 1HEF 701 ATOM 585 CG LEU E 76 -6.467 16.500 40.944 1.00 18.95 1HEF 702 ATOM 586 CD1 LEU E 76 -7.448 15.651 40.101 1.00 29.20 1HEF 703 ATOM 587 CD2 LEU E 76 -6.213 15.857 42.287 1.00 17.86 1HEF 704 ATOM 588 N VAL E 77 -1.754 17.186 40.730 1.00 29.60 1HEF 705 ATOM 589 CA VAL E 77 -0.423 17.307 40.078 1.00 31.21 1HEF 706 ATOM 590 C VAL E 77 -0.064 15.932 39.530 1.00 32.79 1HEF 707 ATOM 591 O VAL E 77 -0.253 14.908 40.195 1.00 32.25 1HEF 708 ATOM 592 CB VAL E 77 0.583 17.963 41.049 1.00 25.11 1HEF 709 ATOM 593 CG1 VAL E 77 1.910 18.244 40.354 1.00 23.92 1HEF 710 ATOM 594 CG2 VAL E 77 0.044 19.192 41.755 1.00 18.98 1HEF 711 ATOM 595 N GLY E 78 0.448 15.920 38.307 1.00 34.33 1HEF 712 ATOM 596 CA GLY E 78 0.815 14.694 37.583 1.00 33.75 1HEF 713 ATOM 597 C GLY E 78 1.344 14.952 36.188 1.00 34.17 1HEF 714 ATOM 598 O GLY E 78 1.682 16.073 35.767 1.00 33.93 1HEF 715 ATOM 599 N PRO E 79 1.439 13.847 35.438 1.00 34.69 1HEF 716 ATOM 600 CA PRO E 79 1.976 13.868 34.067 1.00 34.85 1HEF 717 ATOM 601 C PRO E 79 0.985 14.242 33.011 1.00 35.08 1HEF 718 ATOM 602 O PRO E 79 0.477 13.399 32.238 1.00 36.15 1HEF 719 ATOM 603 CB PRO E 79 2.484 12.416 33.891 1.00 34.13 1HEF 720 ATOM 604 CG PRO E 79 1.342 11.679 34.573 1.00 34.36 1HEF 721 ATOM 605 CD PRO E 79 1.064 12.478 35.833 1.00 34.21 1HEF 722 ATOM 606 N THR E 80 0.684 15.523 32.972 1.00 34.81 1HEF 723 ATOM 607 CA THR E 80 -0.275 16.026 31.964 1.00 33.36 1HEF 724 ATOM 608 C THR E 80 0.563 16.790 30.969 1.00 32.97 1HEF 725 ATOM 609 O THR E 80 1.560 17.401 31.377 1.00 32.82 1HEF 726 ATOM 610 CB THR E 80 -1.380 16.856 32.709 1.00 35.69 1HEF 727 ATOM 611 OG1 THR E 80 -2.100 17.623 31.697 1.00 22.25 1HEF 728 ATOM 612 CG2 THR E 80 -0.803 17.694 33.863 1.00 22.35 1HEF 729 ATOM 613 N PRO E 81 0.165 16.745 29.712 1.00 32.90 1HEF 730 ATOM 614 CA PRO E 81 0.889 17.478 28.648 1.00 32.55 1HEF 731 ATOM 615 C PRO E 81 0.697 18.984 28.830 1.00 32.82 1HEF 732 ATOM 616 O PRO E 81 1.521 19.781 28.365 1.00 33.63 1HEF 733 ATOM 617 CB PRO E 81 0.330 16.926 27.351 1.00 31.94 1HEF 734 ATOM 618 CG PRO E 81 -0.751 15.959 27.692 1.00 32.18 1HEF 735 ATOM 619 CD PRO E 81 -1.018 16.017 29.197 1.00 32.67 1HEF 736 ATOM 620 N VAL E 82 -0.375 19.421 29.494 1.00 31.07 1HEF 737 ATOM 621 CA VAL E 82 -0.689 20.820 29.752 1.00 29.00 1HEF 738 ATOM 622 C VAL E 82 -1.280 21.039 31.144 1.00 27.23 1HEF 739 ATOM 623 O VAL E 82 -1.858 20.146 31.764 1.00 28.33 1HEF 740 ATOM 624 CB VAL E 82 -1.730 21.438 28.779 1.00 32.94 1HEF 741 ATOM 625 CG1 VAL E 82 -1.167 22.012 27.543 1.00 31.13 1HEF 742 ATOM 626 CG2 VAL E 82 -2.898 20.513 28.494 1.00 27.17 1HEF 743 ATOM 627 N ASN E 83 -1.161 22.256 31.575 1.00 25.93 1HEF 744 ATOM 628 CA ASN E 83 -1.703 22.737 32.882 1.00 23.49 1HEF 745 ATOM 629 C ASN E 83 -3.178 22.995 32.518 1.00 21.13 1HEF 746 ATOM 630 O ASN E 83 -3.384 23.760 31.552 1.00 20.60 1HEF 747 ATOM 631 CB ASN E 83 -1.015 23.985 33.398 1.00 20.23 1HEF 748 ATOM 632 CG ASN E 83 0.398 23.847 33.834 1.00 19.32 1HEF 749 ATOM 633 OD1 ASN E 83 0.736 22.918 34.592 1.00 16.95 1HEF 750 ATOM 634 ND2 ASN E 83 1.278 24.753 33.375 1.00 22.53 1HEF 751 ATOM 635 N ILE E 84 -4.078 22.324 33.189 1.00 19.94 1HEF 752 ATOM 636 CA ILE E 84 -5.509 22.458 32.924 1.00 19.16 1HEF 753 ATOM 637 C ILE E 84 -6.284 23.091 34.063 1.00 19.40 1HEF 754 ATOM 638 O ILE E 84 -6.146 22.659 35.233 1.00 18.80 1HEF 755 ATOM 639 CB ILE E 84 -6.101 20.960 32.729 1.00 20.98 1HEF 756 ATOM 640 CG1 ILE E 84 -5.545 20.322 31.450 1.00 18.02 1HEF 757 ATOM 641 CG2 ILE E 84 -7.616 20.873 32.767 1.00 21.59 1HEF 758 ATOM 642 CD1 ILE E 84 -5.626 18.782 31.409 1.00 18.38 1HEF 759 ATOM 643 N ILE E 85 -7.092 24.101 33.763 1.00 19.42 1HEF 760 ATOM 644 CA ILE E 85 -7.940 24.738 34.756 1.00 20.04 1HEF 761 ATOM 645 C ILE E 85 -9.316 24.138 34.453 1.00 18.92 1HEF 762 ATOM 646 O ILE E 85 -9.867 24.433 33.371 1.00 19.29 1HEF 763 ATOM 647 CB ILE E 85 -8.028 26.284 34.881 1.00 12.91 1HEF 764 ATOM 648 CG1 ILE E 85 -6.747 27.026 35.072 1.00 21.89 1HEF 765 ATOM 649 CG2 ILE E 85 -9.086 26.670 36.066 1.00 16.90 1HEF 766 ATOM 650 CD1 ILE E 85 -5.856 26.652 36.318 1.00 16.45 1HEF 767 ATOM 651 N GLY E 86 -9.843 23.349 35.320 1.00 18.40 1HEF 768 ATOM 652 CA GLY E 86 -11.107 22.692 35.249 1.00 17.54 1HEF 769 ATOM 653 C GLY E 86 -12.267 23.294 35.967 1.00 18.90 1HEF 770 ATOM 654 O GLY E 86 -12.344 24.345 36.650 1.00 18.57 1HEF 771 ATOM 655 N ARG E 87 -13.385 22.543 35.832 1.00 21.37 1HEF 772 ATOM 656 CA ARG E 87 -14.640 23.065 36.435 1.00 22.34 1HEF 773 ATOM 657 C ARG E 87 -14.655 23.491 37.864 1.00 23.54 1HEF 774 ATOM 658 O ARG E 87 -15.385 24.466 38.207 1.00 24.83 1HEF 775 ATOM 659 CB ARG E 87 -15.766 22.165 35.991 1.00 24.43 1HEF 776 ATOM 660 CG ARG E 87 -16.269 22.564 34.554 1.00 20.31 1HEF 777 ATOM 661 CD ARG E 87 -17.539 21.752 34.358 1.00 15.54 1HEF 778 ATOM 662 NE ARG E 87 -17.286 20.316 34.720 1.00 12.14 1HEF 779 ATOM 663 CZ ARG E 87 -18.047 19.856 35.741 1.00 17.26 1HEF 780 ATOM 664 NH1 ARG E 87 -18.837 20.790 36.299 1.00 23.36 1HEF 781 ATOM 665 NH2 ARG E 87 -17.982 18.611 36.124 1.00 20.55 1HEF 782 ATOM 666 N ASN E 88 -13.913 22.842 38.745 1.00 24.19 1HEF 783 ATOM 667 CA ASN E 88 -13.876 23.150 40.184 1.00 24.67 1HEF 784 ATOM 668 C ASN E 88 -13.421 24.567 40.414 1.00 25.17 1HEF 785 ATOM 669 O ASN E 88 -13.891 25.283 41.327 1.00 25.05 1HEF 786 ATOM 670 CB ASN E 88 -13.072 22.039 40.899 1.00 26.76 1HEF 787 ATOM 671 CG ASN E 88 -11.590 22.325 40.694 1.00 20.05 1HEF 788 ATOM 672 OD1 ASN E 88 -11.246 22.590 39.550 1.00 29.74 1HEF 789 ATOM 673 ND2 ASN E 88 -10.781 22.297 41.718 1.00 25.41 1HEF 790 ATOM 674 N LEU E 89 -12.511 25.016 39.557 1.00 24.27 1HEF 791 ATOM 675 CA LEU E 89 -11.970 26.338 39.589 1.00 23.78 1HEF 792 ATOM 676 C LEU E 89 -12.778 27.332 38.757 1.00 23.00 1HEF 793 ATOM 677 O LEU E 89 -13.115 28.405 39.315 1.00 22.89 1HEF 794 ATOM 678 CB LEU E 89 -10.442 26.257 39.434 1.00 29.74 1HEF 795 ATOM 679 CG LEU E 89 -9.712 25.396 40.450 1.00 36.31 1HEF 796 ATOM 680 CD1 LEU E 89 -8.212 25.405 40.201 1.00 40.71 1HEF 797 ATOM 681 CD2 LEU E 89 -9.989 25.886 41.860 1.00 32.04 1HEF 798 ATOM 682 N LEU E 90 -13.165 27.068 37.528 1.00 22.79 1HEF 799 ATOM 683 CA LEU E 90 -13.919 27.962 36.635 1.00 21.84 1HEF 800 ATOM 684 C LEU E 90 -15.158 28.587 37.262 1.00 21.81 1HEF 801 ATOM 685 O LEU E 90 -15.566 29.737 37.036 1.00 21.26 1HEF 802 ATOM 686 CB LEU E 90 -14.208 27.256 35.269 1.00 18.64 1HEF 803 ATOM 687 CG LEU E 90 -12.911 26.845 34.521 1.00 19.69 1HEF 804 ATOM 688 CD1 LEU E 90 -13.163 25.823 33.459 1.00 12.18 1HEF 805 ATOM 689 CD2 LEU E 90 -12.146 28.103 34.046 1.00 12.21 1HEF 806 ATOM 690 N THR E 91 -15.776 27.751 38.108 1.00 23.19 1HEF 807 ATOM 691 CA THR E 91 -16.978 28.213 38.809 1.00 24.55 1HEF 808 ATOM 692 C THR E 91 -16.527 29.303 39.777 1.00 26.46 1HEF 809 ATOM 693 O THR E 91 -17.202 30.336 39.833 1.00 27.12 1HEF 810 ATOM 694 CB THR E 91 -17.834 27.085 39.498 1.00 28.12 1HEF 811 ATOM 695 OG1 THR E 91 -16.901 26.380 40.385 1.00 25.75 1HEF 812 ATOM 696 CG2 THR E 91 -18.461 26.077 38.526 1.00 25.26 1HEF 813 ATOM 697 N GLN E 92 -15.406 29.063 40.491 1.00 26.40 1HEF 814 ATOM 698 CA GLN E 92 -14.988 30.116 41.436 1.00 26.22 1HEF 815 ATOM 699 C GLN E 92 -14.795 31.480 40.860 1.00 26.95 1HEF 816 ATOM 700 O GLN E 92 -15.121 32.495 41.526 1.00 27.81 1HEF 817 ATOM 701 CB GLN E 92 -13.756 29.651 42.250 1.00 29.34 1HEF 818 ATOM 702 CG GLN E 92 -14.191 28.513 43.179 1.00 30.64 1HEF 819 ATOM 703 CD GLN E 92 -13.049 28.109 44.092 1.00 36.45 1HEF 820 ATOM 704 OE1 GLN E 92 -12.599 26.974 44.071 1.00 43.82 1HEF 821 ATOM 705 NE2 GLN E 92 -12.649 29.141 44.850 1.00 35.15 1HEF 822 ATOM 706 N ILE E 93 -14.289 31.576 39.626 1.00 27.03 1HEF 823 ATOM 707 CA ILE E 93 -14.040 32.832 38.942 1.00 25.04 1HEF 824 ATOM 708 C ILE E 93 -15.156 33.363 38.051 1.00 24.93 1HEF 825 ATOM 709 O ILE E 93 -14.987 34.366 37.274 1.00 24.50 1HEF 826 ATOM 710 CB ILE E 93 -12.621 32.756 38.339 1.00 30.42 1HEF 827 ATOM 711 CG1 ILE E 93 -12.594 32.124 36.900 1.00 23.45 1HEF 828 ATOM 712 CG2 ILE E 93 -11.608 32.014 39.234 1.00 26.96 1HEF 829 ATOM 713 CD1 ILE E 93 -11.126 32.303 36.354 1.00 28.91 1HEF 830 ATOM 714 N GLY E 94 -16.322 32.771 38.173 1.00 23.99 1HEF 831 ATOM 715 CA GLY E 94 -17.532 33.123 37.491 1.00 24.20 1HEF 832 ATOM 716 C GLY E 94 -17.502 33.028 35.972 1.00 24.98 1HEF 833 ATOM 717 O GLY E 94 -18.111 33.829 35.267 1.00 25.67 1HEF 834 ATOM 718 N CYS E 95 -16.784 32.081 35.464 1.00 24.78 1HEF 835 ATOM 719 CA CYS E 95 -16.589 31.782 34.082 1.00 25.73 1HEF 836 ATOM 720 C CYS E 95 -17.754 31.036 33.437 1.00 26.60 1HEF 837 ATOM 721 O CYS E 95 -18.252 29.984 33.918 1.00 27.65 1HEF 838 ATOM 722 CB CYS E 95 -15.269 31.008 33.987 1.00 35.36 1HEF 839 ATOM 723 SG CYS E 95 -14.803 30.569 32.318 1.00 26.18 1HEF 840 ATOM 724 N THR E 96 -18.224 31.633 32.332 1.00 24.79 1HEF 841 ATOM 725 CA THR E 96 -19.323 30.948 31.598 1.00 24.48 1HEF 842 ATOM 726 C THR E 96 -19.020 30.852 30.082 1.00 24.55 1HEF 843 ATOM 727 O THR E 96 -18.131 31.522 29.510 1.00 23.32 1HEF 844 ATOM 728 CB THR E 96 -20.736 31.553 31.866 1.00 20.23 1HEF 845 ATOM 729 OG1 THR E 96 -20.659 32.922 31.383 1.00 24.70 1HEF 846 ATOM 730 CG2 THR E 96 -21.226 31.492 33.322 1.00 24.48 1HEF 847 ATOM 731 N LEU E 97 -19.778 30.013 29.457 1.00 24.73 1HEF 848 ATOM 732 CA LEU E 97 -19.751 29.720 27.994 1.00 25.80 1HEF 849 ATOM 733 C LEU E 97 -20.982 30.461 27.429 1.00 26.51 1HEF 850 ATOM 734 O LEU E 97 -22.048 30.420 28.085 1.00 28.60 1HEF 851 ATOM 735 CB LEU E 97 -19.764 28.250 27.894 1.00 23.66 1HEF 852 ATOM 736 CG LEU E 97 -19.102 27.355 26.917 1.00 26.12 1HEF 853 ATOM 737 CD1 LEU E 97 -17.727 27.800 26.436 1.00 27.80 1HEF 854 ATOM 738 CD2 LEU E 97 -19.016 25.993 27.658 1.00 15.90 1HEF 855 ATOM 739 N ASN E 98 -20.805 31.177 26.346 1.00 24.92 1HEF 856 ATOM 740 CA ASN E 98 -21.930 31.913 25.745 1.00 24.67 1HEF 857 ATOM 741 C ASN E 98 -21.871 31.649 24.221 1.00 24.58 1HEF 858 ATOM 742 O ASN E 98 -20.813 31.571 23.648 1.00 23.60 1HEF 859 ATOM 743 CB ASN E 98 -22.011 33.400 26.097 1.00 30.40 1HEF 860 ATOM 744 CG ASN E 98 -21.618 33.587 27.558 1.00 38.83 1HEF 861 ATOM 745 OD1 ASN E 98 -22.378 34.078 28.381 1.00 44.47 1HEF 862 ATOM 746 ND2 ASN E 98 -20.378 33.166 27.859 1.00 40.72 1HEF 863 ATOM 747 N PHE E 99 -23.068 31.552 23.705 1.00 26.45 1HEF 864 ATOM 748 CA PHE E 99 -23.317 31.310 22.282 1.00 27.45 1HEF 865 ATOM 749 C PHE E 99 -24.807 31.495 21.973 1.00 28.33 1HEF 866 ATOM 750 O PHE E 99 -25.350 30.581 21.256 1.00 30.24 1HEF 867 ATOM 751 CB PHE E 99 -22.828 29.958 21.868 1.00 22.95 1HEF 868 ATOM 752 CG PHE E 99 -23.593 28.726 22.229 1.00 37.05 1HEF 869 ATOM 753 CD1 PHE E 99 -23.359 28.050 23.421 1.00 35.73 1HEF 870 ATOM 754 CD2 PHE E 99 -24.524 28.199 21.312 1.00 39.69 1HEF 871 ATOM 755 CE1 PHE E 99 -24.037 26.895 23.722 1.00 37.86 1HEF 872 ATOM 756 CE2 PHE E 99 -25.245 27.041 21.617 1.00 37.71 1HEF 873 ATOM 757 CZ PHE E 99 -24.987 26.373 22.814 1.00 36.38 1HEF 874 ATOM 758 OXT PHE E 99 -25.379 32.464 22.390 1.00 35.50 1HEF 875 TER 759 PHE E 99 1HEF 876 ATOM 760 N ALA I 201 -13.642 13.616 34.983 0.50 17.94 1HEF 877 ATOM 761 CA ALA I 201 -12.296 13.889 34.557 0.50 17.97 1HEF 878 ATOM 762 C ALA I 201 -12.252 14.587 33.162 0.50 18.00 1HEF 879 ATOM 763 O ALA I 201 -13.275 14.436 32.477 0.50 18.00 1HEF 880 ATOM 764 CB ALA I 201 -11.399 12.672 34.540 0.50 17.99 1HEF 881 ATOM 765 N ALA I 202 -11.135 15.208 32.924 0.50 17.99 1HEF 882 ATOM 766 CA ALA I 202 -10.334 16.011 32.125 0.50 18.01 1HEF 883 ATOM 767 C ALA I 202 -10.043 15.353 30.741 0.50 18.01 1HEF 884 ATOM 768 O ALA I 202 -9.333 14.372 30.682 0.50 17.98 1HEF 885 ATOM 769 CB ALA I 202 -9.060 16.473 32.821 0.50 18.01 1HEF 886 ATOM 770 N PHE I 203 -10.590 16.009 29.745 0.50 18.01 1 1HEF 887 ATOM 771 CA PHE I 203 -10.831 16.107 28.357 0.50 18.01 1 1HEF 888 ATOM 772 CB PHE I 203 -12.372 15.977 28.102 0.50 18.02 1 1HEF 889 ATOM 773 CG PHE I 203 -12.955 14.659 28.617 0.50 18.02 1 1HEF 890 ATOM 774 CD1 PHE I 203 -12.287 13.433 28.347 0.50 17.98 1 1HEF 891 ATOM 775 CD2 PHE I 203 -14.128 14.695 29.382 0.50 18.02 1 1HEF 892 ATOM 776 CE1 PHE I 203 -12.824 12.232 28.847 0.50 17.99 1 1HEF 893 ATOM 777 CE2 PHE I 203 -14.662 13.473 29.870 0.50 18.01 1 1HEF 894 ATOM 778 CZ PHE I 203 -14.022 12.273 29.587 0.50 18.01 1 1HEF 895 HETATM 779 CH OHE I 203A -10.418 17.473 27.749 0.50 17.98 1 1HEF 896 HETATM 780 OH OHE I 203A -11.292 18.460 28.280 0.50 17.93 1 1HEF 897 HETATM 781 CH2 OHE I 203A -8.969 17.783 28.062 0.50 18.00 1 1HEF 898 ATOM 782 CA PHE I 204 -7.946 18.053 26.991 0.50 18.00 1 1HEF 899 ATOM 783 C PHE I 204 -7.761 17.071 25.855 0.50 17.98 1 1HEF 900 ATOM 784 O PHE I 204 -7.155 16.007 26.038 0.50 17.94 1 1HEF 901 ATOM 785 CB PHE I 204 -6.557 18.028 27.750 0.50 18.00 1 1HEF 902 ATOM 786 CG PHE I 204 -5.447 18.185 26.867 0.50 18.02 1 1HEF 903 ATOM 787 CD1 PHE I 204 -5.322 19.340 26.052 0.50 18.01 1 1HEF 904 ATOM 788 CD2 PHE I 204 -4.487 17.160 26.773 0.50 18.00 1 1HEF 905 ATOM 789 CE1 PHE I 204 -4.226 19.460 25.177 0.50 17.98 1 1HEF 906 ATOM 790 CE2 PHE I 204 -3.394 17.283 25.892 0.50 18.04 1 1HEF 907 ATOM 791 CZ PHE I 204 -3.259 18.453 25.103 0.50 17.98 1 1HEF 908 ATOM 792 N VAL I 205 -8.207 17.368 24.622 0.50 18.02 1HEF 909 ATOM 793 CA VAL I 205 -7.953 16.432 23.516 0.50 17.97 1HEF 910 ATOM 794 C VAL I 205 -7.129 17.271 22.495 0.50 17.99 1HEF 911 ATOM 795 O VAL I 205 -7.559 18.371 22.126 0.50 17.94 1HEF 912 ATOM 796 CB VAL I 205 -9.120 15.786 22.824 0.50 18.00 1HEF 913 ATOM 797 CG1 VAL I 205 -8.811 14.388 22.245 0.50 18.00 1HEF 914 ATOM 798 CG2 VAL I 205 -10.452 15.751 23.536 0.50 18.01 1HEF 915 ATOM 799 N VAL I 206 -6.050 16.641 22.122 0.50 17.98 1HEF 916 ATOM 800 CA VAL I 206 -4.965 16.837 21.252 0.50 17.98 1HEF 917 ATOM 801 C VAL I 206 -3.978 17.899 21.761 0.50 18.02 1HEF 918 ATOM 802 O VAL I 206 -4.110 18.174 22.955 0.50 18.07 1HEF 919 ATOM 803 CB VAL I 206 -5.375 17.234 19.823 0.50 18.00 1HEF 920 ATOM 804 CG1 VAL I 206 -5.601 18.734 19.733 0.50 17.97 1HEF 921 ATOM 805 CG2 VAL I 206 -4.319 16.655 18.858 0.50 18.00 1HEF 922 HETATM 806 CM OME I 206A -3.539 19.444 19.981 0.50 17.98 1HEF 923 HETATM 807 O OME I 206A -3.053 18.528 20.939 0.50 18.02 1HEF 924 TER 808 OME I 206A 1HEF 925 HETATM 809 O HOH 1 -8.127 13.908 27.801 1.00 21.42 1HEF 926 HETATM 810 O HOH 2 -9.358 21.310 48.079 1.00 64.37 1HEF 927 HETATM 811 O HOH 3 -8.753 25.667 26.067 1.00 62.69 1HEF 928 HETATM 812 O HOH 4 -4.465 38.463 35.849 1.00 54.66 1HEF 929 HETATM 813 O HOH 5 -17.746 34.500 19.086 1.00 52.81 1HEF 930 HETATM 814 O HOH 6 -0.272 29.435 17.271 1.00 71.83 1HEF 931 HETATM 815 O HOH 7 1.423 32.335 44.573 1.00 34.16 1HEF 932 HETATM 816 O HOH 8 -1.139 5.711 34.976 1.00 61.07 1HEF 933 HETATM 817 O HOH 9 -4.314 16.823 32.375 1.00 71.31 1HEF 934 HETATM 818 O HOH 10 -10.230 24.584 37.209 1.00 75.15 1HEF 935 HETATM 819 O HOH 11 -11.998 34.992 41.677 1.00 47.64 1HEF 936 HETATM 820 O HOH 12 -2.920 20.252 55.733 1.00 58.53 1HEF 937 HETATM 821 O HOH 13 -9.142 22.735 56.949 1.00 57.29 1HEF 938 HETATM 822 O HOH 14 -15.335 33.472 16.996 1.00 62.41 1HEF 939 HETATM 823 O HOH 15 0.458 9.825 43.743 1.00 60.86 1HEF 940 HETATM 824 O HOH 16 0.050 20.751 24.741 1.00 68.70 1HEF 941 HETATM 825 O HOH 17 -4.524 34.896 17.834 1.00 47.64 1HEF 942 HETATM 826 O HOH 18 4.521 30.604 29.201 1.00 67.22 1HEF 943 HETATM 827 O HOH 19 -2.957 19.358 53.669 1.00 71.16 1HEF 944 HETATM 828 O HOH 20 -7.374 37.181 29.765 1.00 59.40 1HEF 945 HETATM 829 O HOH 21 -12.371 26.128 48.397 1.00 45.00 1HEF 946 HETATM 830 O HOH 22 -15.701 36.428 36.390 1.00 64.84 1HEF 947 HETATM 831 O HOH 23 8.364 23.364 40.421 1.00 36.77 1HEF 948 CONECT 771 770 772 779 1HEF 949 CONECT 779 771 780 781 1HEF 950 CONECT 780 779 1HEF 951 CONECT 781 779 782 1HEF 952 CONECT 782 781 783 785 1HEF 953 CONECT 801 800 802 807 1HEF 954 CONECT 806 807 1HEF 955 CONECT 807 801 806 1HEF 956 MASTER 62 5 2 1 8 3 1 6 829 2 8 9 1HEF 957 END 1HEF 958