PDB Full entry for 1BPH HEADER HORMONE 30-OCT-92 1BPH 1BPH 2 COMPND INSULIN (CUBIC) IN 0.1M SODIUM SALT SOLUTION AT PH9 1BPH 3 SOURCE BOVINE (BOS $TAURUS) PANCREAS 1BPH 4 AUTHOR O.GURSKY,J.BADGER,Y.LI,D.L.D.CASPAR 1BPH 5 REVDAT 2 31-OCT-93 1BPHA 1 REMARK HET FORMUL 1BPHA 1 REVDAT 1 15-JAN-93 1BPH 0 1BPH 6 JRNL AUTH O.GURSKY,J.BADGER,Y.LI,D.L.D.CASPAR 1BPH 7 JRNL TITL CONFORMATIONAL CHANGES IN CUBIC INSULIN CRYSTALS 1BPH 8 JRNL TITL 2 IN THE PH RANGE 7-11 1BPH 9 JRNL REF BIOPHYS.J. V. 63 1210 1992 1BPH 10 JRNL REFN ASTM BIOJAU US ISSN 0006-3495 030 1BPH 11 REMARK 1 1BPH 12 REMARK 1 REFERENCE 1 1BPH 13 REMARK 1 AUTH O.GURSKY,Y.LI,J.BADGER,D.L.D.CASPAR 1BPH 14 REMARK 1 TITL MONOVALENT CATION BINDING IN CUBIC INSULIN 1BPH 15 REMARK 1 TITL 2 CRYSTALS 1BPH 16 REMARK 1 REF BIOPHYS.J. V. 61 604 1992 1BPH 17 REMARK 1 REFN ASTM BIOJAU US ISSN 0006-3495 030 1BPH 18 REMARK 1 REFERENCE 2 1BPH 19 REMARK 1 AUTH J.BADGER 1BPH 20 REMARK 1 TITL FLEXIBILITY IN CRYSTALLINE INSULINS 1BPH 21 REMARK 1 REF BIOPHYS.J. V. 61 816 1992 1BPH 22 REMARK 1 REFN ASTM BIOJAU US ISSN 0006-3495 030 1BPH 23 REMARK 1 REFERENCE 3 1BPHA 2 REMARK 1 AUTH J.BADGER,M.R.HARRIS,C.D.REYNOLDS,A.C.EVANS, 1BPH 25 REMARK 1 AUTH 2 E.J.DODSON,G.G.DODSON,A.C.T.NORTH 1BPH 26 REMARK 1 TITL STRUCTURE OF THE PIG INSULIN DIMER IN THE CUBIC 1BPH 27 REMARK 1 TITL 2 CRYSTAL 1BPH 28 REMARK 1 REF ACTA CRYSTALLOGR.,SECT.B V. 47 127 1991 1BPH 29 REMARK 1 REFN ASTM ASBSDK DK ISSN 0108-7681 622 1BPH 30 REMARK 1 REFERENCE 4 1BPHA 3 REMARK 1 AUTH J.BADGER,D.L.D.CASPAR 1BPH 32 REMARK 1 TITL WATER STRUCTURE IN CUBIC INSULIN CRYSTALS 1BPH 33 REMARK 1 REF PROC.NAT.ACAD.SCI.USA V. 88 622 1991 1BPH 34 REMARK 1 REFN ASTM PNASA6 US ISSN 0027-8424 040 1BPH 35 REMARK 1 REFERENCE 5 1BPHA 4 REMARK 1 AUTH E.J.DODSON,G.G.DODSON,A.LEWITOVA,M.SABESAN 1BPH 37 REMARK 1 TITL ZINC-FREE CUBIC PIG INSULIN: CRYSTALLIZATION AND 1BPH 38 REMARK 1 TITL 2 STRUCTURE DETERMINATION 1BPH 39 REMARK 1 REF J.MOL.BIOL. V. 125 387 1978 1BPH 40 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 070 1BPH 41 REMARK 2 1BPH 42 REMARK 2 RESOLUTION. 2.0 ANGSTROMS. 1BPH 43 REMARK 3 1BPH 44 REMARK 3 REFINEMENT. 1BPH 45 REMARK 3 PROGRAM PROLSQ 1BPH 46 REMARK 3 AUTHORS HENDRICKSON AND KONNERT 1BPH 47 REMARK 3 R VALUE 0.160 1BPH 48 REMARK 3 RMSD BOND DISTANCES 0.014 ANGSTROMS 1BPH 49 REMARK 3 RMSD BOND ANGLE DISTANCES 0.043 ANGSTROMS 1BPH 50 REMARK 4 1BPH 51 REMARK 4 THIS CRYSTAL FORM CONTAINS ONE INSULIN MOLECULE PER 1BPH 52 REMARK 4 ASYMMETRIC UNIT. THE SOLVENT VOLUME IS 64 PERCENT OF THE 1BPH 53 REMARK 4 CRYSTAL VOLUME. THERE ARE MANY ALTERED SIDE CHAIN TORSION 1BPH 54 REMARK 4 ANGLES AND MAIN CHAIN DISPLACEMENTS IN THE CUBIC CRYSTAL 1BPH 55 REMARK 4 STRUCTURE COMPARED TO OTHER INSULIN CRYSTAL FORMS. ABOUT 1BPH 56 REMARK 4 30 PER CENT OF THE AMINO ACID RESIDUES CAN ADOPT MULTIPLE 1BPH 57 REMARK 4 CONFORMATIONS WHICH WERE RELIABLY IDENTIFIED BY COMPARISON 1BPH 58 REMARK 4 OF THE DATA SETS COLLECTED FROM THE CRYSTALS IN THE PH 1BPH 59 REMARK 4 RANGE 7 - 11. THE WEIGHTS OF MANY OF SUCH MULTIPLE PROTEIN 1BPH 60 REMARK 4 AND SOLVENT CONFORMATIONS DEPEND ON SOLVENT IONIC 1BPH 61 REMARK 4 CONDITIONS (PH AND SALT CONCENTRATION). 1BPH 62 REMARK 5 1BPH 63 REMARK 5 THERE ARE FOUR RELATED ENTRIES: 1BPH 64 REMARK 5 1APH 0.1M SODIUM SALT SOLUTION AT PH 7 1BPH 65 REMARK 5 1BPH 0.1M SODIUM SALT SOLUTION AT PH 9 1BPH 66 REMARK 5 1CPH 0.1M SODIUM SALT SOLUTION AT PH 10 1BPH 67 REMARK 5 1DPH 1.0M SODIUM SALT SOLUTION AT PH 11 1BPH 68 REMARK 6 1BPH 69 REMARK 6 IN 1BPH AND 1CPH, THE SIDE CHAIN OF GLU A 4 CAN ADOPT TWO 1BPH 70 REMARK 6 ALTERNATIVE POSITIONS WHICH OVERLAP. THEIR RELATIVE WEIGHT 1BPH 71 REMARK 6 AND THE ATOMIC POSITIONS OF THE SECOND CONFORMER ARE NOT 1BPH 72 REMARK 6 ACCURATELY DETERMINED. 1BPH 73 REMARK 7 1BPH 74 REMARK 7 IN 1APH, 1BPH, AND 1DPH, THE SIDE CHAIN OF GLU B 21 IS 1BPH 75 REMARK 7 DISORDERED. IT HAS BEEN MODELED AS SUPERPOSITION OF TWO 1BPH 76 REMARK 7 CONFORMATIONS BUT ATOMIC POSITIONS FOR THESE CONFORMATIONS 1BPH 77 REMARK 7 ARE PROBABLY NOT VERY ACCURATE. 1BPH 78 REMARK 8 1BPH 79 REMARK 8 THE SIDE CHAIN OF LYS B 29 IS POORLY DEFINED IN THE 1BPH 80 REMARK 8 ELECTRON DENSITY MAPS. IN 1APH AND 1CPH, IT IS INCLUDED 1BPH 81 REMARK 8 WITH PARTIAL OCCUPANCY. IN 1BPH AND 1DPH, ITS COORDINATES 1BPH 82 REMARK 8 HAVE BEEN OMITTED FROM THE ENTRY. 1BPH 83 REMARK 9 1BPH 84 REMARK 9 THE MAIN AND SIDE CHAIN OF ALA B 30 (C-TERMINAL RESIDUE OF 1BPH 85 REMARK 9 CHAIN B) CAN ADOPT TWO SEPARATE CONFORMATIONS AND IS 1BPH 86 REMARK 9 DISORDERED IN EACH OF THESE CONFORMATIONS, WHICH LIMITED 1BPH 87 REMARK 9 THE ACCURACY OF DETERMINATION OF ATOMIC POSITIONS FOR THE 1BPH 88 REMARK 9 CONFORMERS OF ALA B 30. IN 1APH AND 1CPH, SINGLE 1BPH 89 REMARK 9 ALTERNATIVE CONFORMERS ARE PREDOMINANT BUT, DUE TO 1BPH 90 REMARK 9 DISORDER, THEY ARE ASSIGNED PARTIAL OCCUPANCIES. IN 1BPH 1BPH 91 REMARK 9 AND 1DPH, BOTH ALTERNATIVE CONFORMERS ARE INCLUDED IN THE 1BPH 92 REMARK 9 ENTRY. 1BPH 93 REMARK 10 1BPH 94 REMARK 10 1BPH, 1CPH, AND 1DPH CONTAIN A SODIUM ION. ANOTHER SODIUM 1BPH 95 REMARK 10 SITE OVERLAPS THE CONFORMATION OF HIS B 10 SIDE CHAIN THAT 1BPH 96 REMARK 10 IS PREDOMINANT IN 1APH. 1BPH 97 REMARK 11 1BPH 98 REMARK 11 THE 1,2-DICHLOROETHANE IS BOUND IS CIS CONFORMATION IN A 1BPH 99 REMARK 11 SYMMETRIC POSITION ACROSS THE CRYSTALLOGRAPHIC TWO-FOLD 1BPH 100 REMARK 11 AXIS BETWEEN THE TWO INSULIN DIMER-FORMING MOLECULES. 1BPH 101 REMARK 12 1BPH 102 REMARK 12 THERE IS A SHEET COMPRISING TWO ANTIPARALLEL STRANDS 1BPH 103 REMARK 12 PHE B 24 - TYR B 26 FROM TWO DIMER-FORMING INSULIN 1BPH 104 REMARK 12 MOLECULES. 1BPH 105 REMARK 13 1BPHA 5 REMARK 13 CORRECTION. RENUMBER REFERENCES SEQUENTIALLY. INSERT 1BPHA 6 REMARK 13 MISSING HET AND FORMUL RECORDS FOR NA. 31-OCT-93. 1BPHA 7 SEQRES 1 A 21 GLY ILE VAL GLU GLN CYS CYS ALA SER VAL CYS SER LEU 1BPH 106 SEQRES 2 A 21 TYR GLN LEU GLU ASN TYR CYS ASN 1BPH 107 SEQRES 1 B 30 PHE VAL ASN GLN HIS LEU CYS GLY SER HIS LEU VAL GLU 1BPH 108 SEQRES 2 B 30 ALA LEU TYR LEU VAL CYS GLY GLU ARG GLY PHE PHE TYR 1BPH 109 SEQRES 3 B 30 THR PRO LYS ALA 1BPH 110 HET DCE 200 4 1,2-DICHLOROETHANE(ETHYLENE DICHLORIDE) 1BPH 111 HET NA 88 1 SODIUM ION 1BPHA 8 FORMUL 3 DCE C2 H4 CL2 1BPH 112 FORMUL 4 NA NA1 1BPHA 9 FORMUL 5 HOH *55(H2 O1) 1BPHA 10 HELIX 1 A1 GLY A 1 VAL A 10 1 1BPH 114 HELIX 2 A2 SER A 12 GLU A 17 5 NOT IDEAL 1BPH 115 HELIX 3 B1 SER B 9 GLY B 20 1 1BPH 116 TURN 1 1B1 CYS B 19 ARG B 22 1BPH 117 TURN 2 1B2 GLY B 20 GLY B 23 1BPH 118 SSBOND 1 CYS A 6 CYS A 11 1BPH 119 SSBOND 2 CYS A 7 CYS B 7 1BPH 120 SSBOND 3 CYS A 20 CYS B 19 1BPH 121 CRYST1 78.900 78.900 78.900 90.00 90.00 90.00 I 21 3 24 1BPH 122 ORIGX1 1.000000 0.000000 0.000000 0.00000 1BPH 123 ORIGX2 0.000000 1.000000 0.000000 0.00000 1BPH 124 ORIGX3 0.000000 0.000000 1.000000 0.00000 1BPH 125 SCALE1 0.012674 0.000000 0.000000 0.00000 1BPH 126 SCALE2 0.000000 0.012674 0.000000 0.00000 1BPH 127 SCALE3 0.000000 0.000000 0.012674 0.00000 1BPH 128 ATOM 1 N GLY A 1 13.994 47.196 31.798 1.00 35.87 1BPH 129 ATOM 2 CA GLY A 1 14.277 46.226 30.708 1.00 38.67 1BPH 130 ATOM 3 C GLY A 1 15.574 45.507 31.085 1.00 31.18 1BPH 131 ATOM 4 O GLY A 1 16.078 45.660 32.217 1.00 22.60 1BPH 132 ATOM 5 N ILE A 2 16.088 44.766 30.126 1.00 28.39 1BPH 133 ATOM 6 CA ILE A 2 17.342 44.034 30.404 1.00 23.76 1BPH 134 ATOM 7 C ILE A 2 18.526 44.939 30.686 1.00 25.29 1BPH 135 ATOM 8 O ILE A 2 19.425 44.457 31.392 1.00 18.74 1BPH 136 ATOM 9 CB ILE A 2 17.571 43.072 29.158 1.00 27.36 1BPH 137 ATOM 10 CG1 ILE A 2 18.638 42.049 29.605 1.00 18.03 1BPH 138 ATOM 11 CG2 ILE A 2 17.859 43.936 27.903 1.00 25.54 1BPH 139 ATOM 12 CD1 ILE A 2 18.914 40.930 28.590 1.00 17.07 1BPH 140 ATOM 13 N VAL A 3 18.619 46.195 30.192 1.00 24.42 1BPH 141 ATOM 14 CA VAL A 3 19.774 47.080 30.436 1.00 30.26 1BPH 142 ATOM 15 C VAL A 3 19.952 47.453 31.895 1.00 19.08 1BPH 143 ATOM 16 O VAL A 3 21.018 47.421 32.561 1.00 28.15 1BPH 144 ATOM 17 CB VAL A 3 19.719 48.274 29.462 1.00 33.87 1BPH 145 ATOM 18 CG1 VAL A 3 20.847 49.225 29.754 1.00 30.40 1BPH 146 ATOM 19 CG2 VAL A 3 19.868 47.724 28.044 1.00 24.51 1BPH 147 ATOM 20 N GLU A 4 18.785 47.805 32.424 1.00 26.59 1BPH 148 ATOM 21 CA GLU A 4 18.622 48.172 33.836 1.00 33.10 1BPH 149 ATOM 22 C GLU A 4 18.969 46.987 34.752 1.00 22.38 1BPH 150 ATOM 23 O GLU A 4 19.636 47.147 35.769 1.00 29.96 1BPH 151 ATOM 24 CB AGLU A 4 17.142 48.344 34.231 0.35 22.89 1BPH 152 ATOM 25 CB BGLU A 4 17.162 48.608 34.081 0.65 37.01 1BPH 153 ATOM 26 CG AGLU A 4 16.803 49.669 34.917 0.35 33.05 1BPH 154 ATOM 27 CG BGLU A 4 16.697 49.754 33.207 0.65 48.14 1BPH 155 ATOM 28 CD AGLU A 4 16.821 50.817 33.941 0.35 40.87 1BPH 156 ATOM 29 CD BGLU A 4 16.519 49.715 31.729 0.65 41.33 1BPH 157 ATOM 30 OE1AGLU A 4 16.938 50.442 32.747 0.35 41.84 1BPH 158 ATOM 31 OE1BGLU A 4 16.123 48.772 31.061 0.65 41.92 1BPH 159 ATOM 32 OE2AGLU A 4 16.720 51.979 34.305 0.35 54.29 1BPH 160 ATOM 33 OE2BGLU A 4 16.817 50.811 31.170 0.65 56.54 1BPH 161 ATOM 34 N GLN A 5 18.441 45.830 34.333 1.00 20.82 1BPH 162 ATOM 35 CA GLN A 5 18.635 44.641 35.151 1.00 19.86 1BPH 163 ATOM 36 C GLN A 5 19.994 43.960 35.023 1.00 16.78 1BPH 164 ATOM 37 O GLN A 5 20.404 43.353 36.022 1.00 20.67 1BPH 165 ATOM 38 CB GLN A 5 17.478 43.610 34.976 1.00 18.46 1BPH 166 ATOM 39 CG GLN A 5 16.150 44.045 35.586 1.00 37.02 1BPH 167 ATOM 40 CD GLN A 5 16.141 44.774 36.915 1.00 49.99 1BPH 168 ATOM 41 OE1 GLN A 5 16.708 44.380 37.938 1.00 39.65 1BPH 169 ATOM 42 NE2 GLN A 5 15.509 45.970 37.000 1.00 39.64 1BPH 170 ATOM 43 N CYS A 6 20.601 44.044 33.852 1.00 19.89 1BPH 171 ATOM 44 CA CYS A 6 21.830 43.306 33.613 1.00 14.11 1BPH 172 ATOM 45 C CYS A 6 23.046 44.140 33.333 1.00 16.37 1BPH 173 ATOM 46 O CYS A 6 24.131 43.578 33.553 1.00 19.27 1BPH 174 ATOM 47 CB CYS A 6 21.540 42.343 32.426 1.00 12.56 1BPH 175 ATOM 48 SG CYS A 6 20.620 40.860 33.004 1.00 18.49 1BPH 176 ATOM 49 N CYS A 7 22.800 45.361 32.956 1.00 18.24 1BPH 177 ATOM 50 CA CYS A 7 23.972 46.225 32.671 1.00 18.70 1BPH 178 ATOM 51 C CYS A 7 24.119 47.181 33.861 1.00 29.28 1BPH 179 ATOM 52 O CYS A 7 25.178 47.219 34.496 1.00 20.97 1BPH 180 ATOM 53 CB CYS A 7 23.719 46.956 31.352 1.00 22.67 1BPH 181 ATOM 54 SG CYS A 7 24.924 48.305 30.971 1.00 25.81 1BPH 182 ATOM 55 N ALA A 8 23.058 47.915 34.156 1.00 16.88 1BPH 183 ATOM 56 CA ALA A 8 23.070 48.889 35.257 1.00 24.50 1BPH 184 ATOM 57 C ALA A 8 23.185 48.109 36.572 1.00 34.44 1BPH 185 ATOM 58 O ALA A 8 23.745 48.650 37.551 1.00 30.42 1BPH 186 ATOM 59 CB ALA A 8 21.895 49.858 35.177 1.00 18.63 1BPH 187 ATOM 60 N SER A 9 22.664 46.884 36.657 1.00 25.11 1BPH 188 ATOM 61 CA SER A 9 22.851 46.121 37.910 1.00 22.63 1BPH 189 ATOM 62 C SER A 9 23.385 44.771 37.460 1.00 29.30 1BPH 190 ATOM 63 O SER A 9 23.598 44.542 36.265 1.00 15.34 1BPH 191 ATOM 64 CB SER A 9 21.649 46.119 38.816 1.00 22.94 1BPH 192 ATOM 65 OG SER A 9 20.526 45.975 38.010 1.00 34.86 1BPH 193 ATOM 66 N VAL A 10 23.661 43.919 38.409 1.00 17.74 1BPH 194 ATOM 67 CA VAL A 10 24.193 42.573 38.101 1.00 20.85 1BPH 195 ATOM 68 C VAL A 10 23.045 41.689 37.593 1.00 17.87 1BPH 196 ATOM 69 O VAL A 10 21.941 41.599 38.137 1.00 18.28 1BPH 197 ATOM 70 CB VAL A 10 24.831 42.008 39.371 1.00 24.84 1BPH 198 ATOM 71 CG1 VAL A 10 25.318 40.584 39.225 1.00 19.36 1BPH 199 ATOM 72 CG2 VAL A 10 25.949 42.906 39.870 1.00 24.23 1BPH 200 ATOM 73 N CYS A 11 23.409 41.073 36.475 1.00 17.34 1BPH 201 ATOM 74 CA CYS A 11 22.505 40.156 35.785 1.00 12.14 1BPH 202 ATOM 75 C CYS A 11 22.391 38.858 36.587 1.00 13.83 1BPH 203 ATOM 76 O CYS A 11 23.093 38.527 37.518 1.00 17.27 1BPH 204 ATOM 77 CB CYS A 11 23.231 39.975 34.427 1.00 14.85 1BPH 205 ATOM 78 SG CYS A 11 22.037 39.465 33.101 1.00 18.76 1BPH 206 ATOM 79 N SER A 12 21.467 38.013 36.149 1.00 21.32 1BPH 207 ATOM 80 CA SER A 12 21.230 36.670 36.695 1.00 23.01 1BPH 208 ATOM 81 C SER A 12 20.829 35.760 35.522 1.00 26.32 1BPH 209 ATOM 82 O SER A 12 20.358 36.259 34.464 1.00 12.20 1BPH 210 ATOM 83 CB SER A 12 20.217 36.757 37.839 1.00 17.58 1BPH 211 ATOM 84 OG SER A 12 18.887 36.877 37.368 1.00 19.66 1BPH 212 ATOM 85 N LEU A 13 20.929 34.442 35.626 1.00 12.68 1BPH 213 ATOM 86 CA LEU A 13 20.507 33.477 34.628 1.00 14.94 1BPH 214 ATOM 87 C LEU A 13 18.999 33.601 34.423 1.00 19.36 1BPH 215 ATOM 88 O LEU A 13 18.325 33.607 33.364 1.00 16.76 1BPH 216 ATOM 89 CB LEU A 13 21.047 32.094 35.028 1.00 15.38 1BPH 217 ATOM 90 CG LEU A 13 20.643 30.910 34.154 1.00 18.77 1BPH 218 ATOM 91 CD1 LEU A 13 21.120 31.186 32.746 1.00 15.37 1BPH 219 ATOM 92 CD2 LEU A 13 21.204 29.577 34.634 1.00 16.24 1BPH 220 ATOM 93 N TYR A 14 18.322 33.783 35.540 1.00 16.62 1BPH 221 ATOM 94 CA TYR A 14 16.870 33.937 35.558 1.00 15.35 1BPH 222 ATOM 95 C TYR A 14 16.458 35.067 34.636 1.00 20.63 1BPH 223 ATOM 96 O TYR A 14 15.536 34.933 33.817 1.00 25.35 1BPH 224 ATOM 97 CB TYR A 14 16.372 34.081 37.019 1.00 25.01 1BPH 225 ATOM 98 CG TYR A 14 14.870 34.312 37.062 1.00 31.63 1BPH 226 ATOM 99 CD1 TYR A 14 14.371 35.585 36.750 1.00 24.28 1BPH 227 ATOM 100 CD2 TYR A 14 13.960 33.303 37.382 1.00 35.42 1BPH 228 ATOM 101 CE1 TYR A 14 13.014 35.862 36.749 1.00 23.66 1BPH 229 ATOM 102 CE2 TYR A 14 12.599 33.580 37.383 1.00 34.93 1BPH 230 ATOM 103 CZ TYR A 14 12.121 34.844 37.073 1.00 39.52 1BPH 231 ATOM 104 OH TYR A 14 10.777 35.174 37.078 1.00 68.21 1BPH 232 ATOM 105 N GLN A 15 17.065 36.223 34.801 1.00 19.89 1BPH 233 ATOM 106 CA GLN A 15 16.730 37.391 33.994 1.00 20.93 1BPH 234 ATOM 107 C GLN A 15 17.065 37.151 32.532 1.00 19.19 1BPH 235 ATOM 108 O GLN A 15 16.218 37.525 31.709 1.00 25.94 1BPH 236 ATOM 109 CB AGLN A 15 17.543 38.619 34.420 0.50 23.60 1BPH 237 ATOM 110 CB BGLN A 15 17.555 38.614 34.440 0.50 23.00 1BPH 238 ATOM 111 CG AGLN A 15 16.739 39.886 34.618 0.50 33.72 1BPH 239 ATOM 112 CG BGLN A 15 17.209 38.979 35.881 0.50 31.07 1BPH 240 ATOM 113 CD AGLN A 15 16.388 39.952 36.106 0.50 39.35 1BPH 241 ATOM 114 CD BGLN A 15 15.809 39.573 35.895 0.50 41.33 1BPH 242 ATOM 115 OE1AGLN A 15 15.218 39.680 36.411 0.50 35.08 1BPH 243 ATOM 116 OE1BGLN A 15 14.884 39.088 36.560 0.50 34.81 1BPH 244 ATOM 117 NE2AGLN A 15 17.446 40.258 36.864 0.50 27.66 1BPH 245 ATOM 118 NE2BGLN A 15 15.698 40.650 35.103 0.50 31.57 1BPH 246 ATOM 119 N LEU A 16 18.288 36.621 32.288 1.00 14.13 1BPH 247 ATOM 120 CA LEU A 16 18.624 36.401 30.881 1.00 14.29 1BPH 248 ATOM 121 C LEU A 16 17.652 35.441 30.216 1.00 18.55 1BPH 249 ATOM 122 O LEU A 16 17.286 35.647 29.050 1.00 16.30 1BPH 250 ATOM 123 CB LEU A 16 20.042 35.820 30.697 1.00 21.68 1BPH 251 ATOM 124 CG LEU A 16 21.271 36.691 30.744 1.00 25.01 1BPH 252 ATOM 125 CD1 LEU A 16 22.479 35.759 30.515 1.00 25.05 1BPH 253 ATOM 126 CD2 LEU A 16 21.217 37.844 29.749 1.00 18.88 1BPH 254 ATOM 127 N GLU A 17 17.257 34.367 30.913 1.00 17.57 1BPH 255 ATOM 128 CA GLU A 17 16.353 33.393 30.338 1.00 13.26 1BPH 256 ATOM 129 C GLU A 17 14.968 33.889 30.001 1.00 22.70 1BPH 257 ATOM 130 O GLU A 17 14.234 33.275 29.212 1.00 25.00 1BPH 258 ATOM 131 CB GLU A 17 16.183 32.146 31.209 1.00 17.01 1BPH 259 ATOM 132 CG GLU A 17 17.252 31.160 30.695 1.00 14.38 1BPH 260 ATOM 133 CD GLU A 17 16.968 29.843 31.385 1.00 24.91 1BPH 261 ATOM 134 OE1 GLU A 17 16.230 29.713 32.350 1.00 25.72 1BPH 262 ATOM 135 OE2 GLU A 17 17.675 28.984 30.830 1.00 22.42 1BPH 263 ATOM 136 N ASN A 18 14.618 35.021 30.563 1.00 22.30 1BPH 264 ATOM 137 CA ASN A 18 13.371 35.753 30.369 1.00 29.65 1BPH 265 ATOM 138 C ASN A 18 13.330 36.318 28.943 1.00 23.17 1BPH 266 ATOM 139 O ASN A 18 12.197 36.611 28.486 1.00 30.58 1BPH 267 ATOM 140 CB ASN A 18 13.153 36.870 31.413 1.00 36.00 1BPH 268 ATOM 141 CG ASN A 18 12.471 36.382 32.685 1.00 40.48 1BPH 269 ATOM 142 OD1 ASN A 18 11.899 35.275 32.723 1.00 33.48 1BPH 270 ATOM 143 ND2 ASN A 18 12.521 37.159 33.766 1.00 51.14 1BPH 271 ATOM 144 N TYR A 19 14.489 36.480 28.344 1.00 18.69 1BPH 272 ATOM 145 CA TYR A 19 14.612 37.028 26.974 1.00 19.02 1BPH 273 ATOM 146 C TYR A 19 14.875 36.010 25.898 1.00 17.88 1BPH 274 ATOM 147 O TYR A 19 15.089 36.370 24.716 1.00 34.62 1BPH 275 ATOM 148 CB TYR A 19 15.582 38.242 26.956 1.00 11.17 1BPH 276 ATOM 149 CG TYR A 19 15.202 39.302 27.972 1.00 22.53 1BPH 277 ATOM 150 CD1 TYR A 19 14.256 40.274 27.592 1.00 29.17 1BPH 278 ATOM 151 CD2 TYR A 19 15.718 39.328 29.269 1.00 25.46 1BPH 279 ATOM 152 CE1 TYR A 19 13.851 41.279 28.473 1.00 33.99 1BPH 280 ATOM 153 CE2 TYR A 19 15.309 40.322 30.152 1.00 31.02 1BPH 281 ATOM 154 CZ TYR A 19 14.378 41.296 29.759 1.00 34.79 1BPH 282 ATOM 155 OH TYR A 19 13.945 42.300 30.596 1.00 47.62 1BPH 283 ATOM 156 N CYS A 20 14.882 34.724 26.229 1.00 22.03 1BPH 284 ATOM 157 CA CYS A 20 15.071 33.633 25.251 1.00 13.67 1BPH 285 ATOM 158 C CYS A 20 13.703 33.483 24.597 1.00 25.89 1BPH 286 ATOM 159 O CYS A 20 12.739 33.787 25.363 1.00 23.95 1BPH 287 ATOM 160 CB CYS A 20 15.466 32.310 25.854 1.00 17.26 1BPH 288 ATOM 161 SG CYS A 20 17.051 32.374 26.639 1.00 18.75 1BPH 289 ATOM 162 N ASN A 21 13.709 33.073 23.332 1.00 27.33 1BPH 290 ATOM 163 CA ASN A 21 12.374 32.921 22.688 1.00 49.49 1BPH 291 ATOM 164 C ASN A 21 11.765 31.551 23.055 1.00 53.32 1BPH 292 ATOM 165 O ASN A 21 12.375 30.767 23.810 1.00 44.50 1BPH 293 ATOM 166 CB ASN A 21 12.289 33.173 21.186 1.00 35.48 1BPH 294 ATOM 167 CG ASN A 21 12.437 34.625 20.776 1.00 44.81 1BPH 295 ATOM 168 OD1 ASN A 21 13.159 34.867 19.780 1.00 53.99 1BPH 296 ATOM 169 ND2 ASN A 21 11.812 35.564 21.495 1.00 46.56 1BPH 297 ATOM 170 OXT ASN A 21 10.648 31.342 22.535 1.00 80.48 1BPH 298 TER 171 ASN A 21 1BPH 299 ATOM 172 N PHE B 1 28.961 32.694 34.302 1.00 38.09 1BPH 300 ATOM 173 CA PHE B 1 29.545 33.933 33.691 1.00 44.75 1BPH 301 ATOM 174 C PHE B 1 28.483 35.030 33.562 1.00 18.46 1BPH 302 ATOM 175 O PHE B 1 28.656 36.170 33.083 1.00 29.15 1BPH 303 ATOM 176 CB PHE B 1 30.190 33.486 32.346 1.00 36.50 1BPH 304 ATOM 177 CG PHE B 1 29.191 32.986 31.322 1.00 29.77 1BPH 305 ATOM 178 CD1 PHE B 1 28.691 31.688 31.351 1.00 22.29 1BPH 306 ATOM 179 CD2 PHE B 1 28.736 33.844 30.327 1.00 30.11 1BPH 307 ATOM 180 CE1 PHE B 1 27.758 31.234 30.415 1.00 30.11 1BPH 308 ATOM 181 CE2 PHE B 1 27.822 33.423 29.377 1.00 29.49 1BPH 309 ATOM 182 CZ PHE B 1 27.329 32.125 29.428 1.00 27.29 1BPH 310 ATOM 183 N VAL B 2 27.235 34.671 33.935 1.00 25.09 1BPH 311 ATOM 184 CA VAL B 2 26.085 35.571 33.793 1.00 23.88 1BPH 312 ATOM 185 C VAL B 2 25.902 36.506 34.969 1.00 24.42 1BPH 313 ATOM 186 O VAL B 2 25.269 37.560 34.801 1.00 19.63 1BPH 314 ATOM 187 CB VAL B 2 24.846 34.751 33.391 1.00 28.89 1BPH 315 ATOM 188 CG1 VAL B 2 25.094 33.931 32.115 1.00 27.49 1BPH 316 ATOM 189 CG2 VAL B 2 24.362 33.851 34.497 1.00 31.38 1BPH 317 ATOM 190 N ASN B 3 26.523 36.166 36.098 1.00 23.96 1BPH 318 ATOM 191 CA ASN B 3 26.319 37.001 37.308 1.00 26.03 1BPH 319 ATOM 192 C ASN B 3 27.296 38.147 37.504 1.00 23.25 1BPH 320 ATOM 193 O ASN B 3 28.095 38.255 38.450 1.00 31.89 1BPH 321 ATOM 194 CB ASN B 3 26.126 36.055 38.509 1.00 20.70 1BPH 322 ATOM 195 CG ASN B 3 25.048 34.990 38.438 1.00 21.82 1BPH 323 ATOM 196 OD1 ASN B 3 25.464 33.818 38.212 1.00 34.83 1BPH 324 ATOM 197 ND2 ASN B 3 23.735 35.160 38.603 1.00 21.66 1BPH 325 ATOM 198 N GLN B 4 27.150 39.080 36.576 1.00 19.70 1BPH 326 ATOM 199 CA GLN B 4 27.884 40.341 36.453 1.00 23.53 1BPH 327 ATOM 200 C GLN B 4 27.092 41.384 35.655 1.00 17.64 1BPH 328 ATOM 201 O GLN B 4 25.952 41.165 35.167 1.00 21.32 1BPH 329 ATOM 202 CB AGLN B 4 29.230 40.191 35.711 0.50 25.72 1BPH 330 ATOM 203 CB BGLN B 4 29.290 40.111 35.846 0.50 19.78 1BPH 331 ATOM 204 CG AGLN B 4 29.094 39.381 34.422 0.50 29.56 1BPH 332 ATOM 205 CG BGLN B 4 29.281 39.276 34.564 0.50 26.90 1BPH 333 ATOM 206 CD AGLN B 4 30.425 39.286 33.708 0.50 45.07 1BPH 334 ATOM 207 CD BGLN B 4 30.715 38.911 34.223 0.50 45.48 1BPH 335 ATOM 208 OE1AGLN B 4 31.085 40.292 33.432 0.50 29.76 1BPH 336 ATOM 209 OE1BGLN B 4 31.608 39.122 35.038 0.50 48.68 1BPH 337 ATOM 210 NE2AGLN B 4 30.823 38.045 33.409 0.50 48.65 1BPH 338 ATOM 211 NE2BGLN B 4 30.934 38.382 33.020 0.50 51.98 1BPH 339 ATOM 212 N HIS B 5 27.794 42.523 35.577 1.00 17.74 1BPH 340 ATOM 213 CA HIS B 5 27.245 43.647 34.804 1.00 20.53 1BPH 341 ATOM 214 C HIS B 5 27.629 43.308 33.357 1.00 27.58 1BPH 342 ATOM 215 O HIS B 5 28.829 43.196 33.087 1.00 32.38 1BPH 343 ATOM 216 CB HIS B 5 27.871 45.015 35.095 1.00 25.02 1BPH 344 ATOM 217 CG HIS B 5 27.648 45.348 36.552 1.00 30.13 1BPH 345 ATOM 218 ND1 HIS B 5 26.575 46.106 36.975 1.00 32.60 1BPH 346 ATOM 219 CD2 HIS B 5 28.379 44.998 37.644 1.00 26.30 1BPH 347 ATOM 220 CE1 HIS B 5 26.635 46.222 38.293 1.00 23.86 1BPH 348 ATOM 221 NE2 HIS B 5 27.700 45.560 38.701 1.00 34.89 1BPH 349 ATOM 222 N LEU B 6 26.631 43.149 32.533 1.00 24.85 1BPH 350 ATOM 223 CA LEU B 6 26.735 42.784 31.109 1.00 23.97 1BPH 351 ATOM 224 C LEU B 6 26.114 43.926 30.322 1.00 18.31 1BPH 352 ATOM 225 O LEU B 6 24.915 44.128 30.431 1.00 21.19 1BPH 353 ATOM 226 CB LEU B 6 26.005 41.442 30.891 1.00 16.72 1BPH 354 ATOM 227 CG LEU B 6 26.621 40.268 31.612 1.00 15.45 1BPH 355 ATOM 228 CD1 LEU B 6 25.816 39.046 31.244 1.00 19.17 1BPH 356 ATOM 229 CD2 LEU B 6 28.043 40.002 31.126 1.00 19.27 1BPH 357 ATOM 230 N CYS B 7 26.920 44.674 29.556 1.00 17.86 1BPH 358 ATOM 231 CA CYS B 7 26.462 45.814 28.768 1.00 19.62 1BPH 359 ATOM 232 C CYS B 7 26.858 45.662 27.288 1.00 22.38 1BPH 360 ATOM 233 O CYS B 7 27.898 45.036 27.074 1.00 22.92 1BPH 361 ATOM 234 CB CYS B 7 27.109 47.123 29.287 1.00 17.85 1BPH 362 ATOM 235 SG CYS B 7 26.732 47.463 31.070 1.00 25.70 1BPH 363 ATOM 236 N GLY B 8 26.025 46.230 26.437 1.00 24.29 1BPH 364 ATOM 237 CA GLY B 8 26.287 46.249 25.009 1.00 24.38 1BPH 365 ATOM 238 C GLY B 8 26.513 44.910 24.356 1.00 25.51 1BPH 366 ATOM 239 O GLY B 8 25.719 43.989 24.621 1.00 20.58 1BPH 367 ATOM 240 N SER B 9 27.559 44.734 23.567 1.00 17.06 1BPH 368 ATOM 241 CA SER B 9 27.780 43.457 22.821 1.00 20.76 1BPH 369 ATOM 242 C SER B 9 27.960 42.271 23.756 1.00 13.26 1BPH 370 ATOM 243 O SER B 9 27.726 41.050 23.546 1.00 21.64 1BPH 371 ATOM 244 CB SER B 9 28.926 43.722 21.836 1.00 9.93 1BPH 372 ATOM 245 OG SER B 9 30.124 43.870 22.628 1.00 21.17 1BPH 373 ATOM 246 N HIS B 10 28.457 42.657 24.911 1.00 16.62 1BPH 374 ATOM 247 CA HIS B 10 28.734 41.832 26.083 1.00 25.79 1BPH 375 ATOM 248 C HIS B 10 27.460 41.128 26.575 1.00 20.90 1BPH 376 ATOM 249 O HIS B 10 27.418 39.921 26.909 1.00 17.92 1BPH 377 ATOM 250 CB AHIS B 10 29.335 42.777 27.162 0.55 27.94 1BPH 378 ATOM 251 CB BHIS B 10 29.433 42.195 27.451 0.45 13.37 1BPH 379 ATOM 252 CG AHIS B 10 30.525 43.567 26.692 0.55 32.44 1BPH 380 ATOM 253 CG BHIS B 10 30.246 41.172 28.185 0.45 17.51 1BPH 381 ATOM 254 ND1AHIS B 10 31.593 43.770 27.539 0.55 17.49 1BPH 382 ATOM 255 ND1BHIS B 10 30.703 41.322 29.476 0.45 32.32 1BPH 383 ATOM 256 CD2AHIS B 10 30.835 44.205 25.517 0.55 19.87 1BPH 384 ATOM 257 CD2BHIS B 10 30.675 39.942 27.769 0.45 19.36 1BPH 385 ATOM 258 CE1AHIS B 10 32.517 44.483 26.899 0.55 21.40 1BPH 386 ATOM 259 CE1BHIS B 10 31.378 40.228 29.817 0.45 26.29 1BPH 387 ATOM 260 NE2AHIS B 10 32.069 44.777 25.695 0.55 23.22 1BPH 388 ATOM 261 NE2BHIS B 10 31.377 39.382 28.809 0.45 27.71 1BPH 389 ATOM 262 N LEU B 11 26.380 41.850 26.686 1.00 16.42 1BPH 390 ATOM 263 CA LEU B 11 25.074 41.416 27.079 1.00 15.37 1BPH 391 ATOM 264 C LEU B 11 24.463 40.535 25.985 1.00 22.39 1BPH 392 ATOM 265 O LEU B 11 23.865 39.466 26.274 1.00 18.48 1BPH 393 ATOM 266 CB LEU B 11 24.123 42.578 27.404 1.00 15.75 1BPH 394 ATOM 267 CG LEU B 11 22.712 42.161 27.865 1.00 19.09 1BPH 395 ATOM 268 CD1 LEU B 11 22.828 41.159 29.003 1.00 13.73 1BPH 396 ATOM 269 CD2 LEU B 11 22.006 43.433 28.285 1.00 22.91 1BPH 397 ATOM 270 N VAL B 12 24.627 40.983 24.752 1.00 22.66 1BPH 398 ATOM 271 CA VAL B 12 24.089 40.267 23.569 1.00 16.84 1BPH 399 ATOM 272 C VAL B 12 24.764 38.918 23.429 1.00 18.98 1BPH 400 ATOM 273 O VAL B 12 24.123 37.948 23.079 1.00 15.29 1BPH 401 ATOM 274 CB VAL B 12 24.186 41.080 22.252 1.00 21.43 1BPH 402 ATOM 275 CG1 VAL B 12 23.924 40.228 21.031 1.00 16.49 1BPH 403 ATOM 276 CG2 VAL B 12 23.250 42.289 22.279 1.00 15.00 1BPH 404 ATOM 277 N GLU B 13 26.059 38.848 23.646 1.00 16.90 1BPH 405 ATOM 278 CA GLU B 13 26.842 37.606 23.590 1.00 20.70 1BPH 406 ATOM 279 C GLU B 13 26.359 36.650 24.674 1.00 15.13 1BPH 407 ATOM 280 O GLU B 13 26.298 35.442 24.385 1.00 20.98 1BPH 408 ATOM 281 CB GLU B 13 28.279 38.024 23.829 1.00 15.61 1BPH 409 ATOM 282 CG GLU B 13 29.322 36.949 23.949 1.00 35.67 1BPH 410 ATOM 283 CD GLU B 13 30.683 37.640 23.806 1.00 42.31 1BPH 411 ATOM 284 OE1 GLU B 13 31.063 38.092 22.736 1.00 38.69 1BPH 412 ATOM 285 OE2 GLU B 13 31.150 37.644 24.962 1.00 45.93 1BPH 413 ATOM 286 N ALA B 14 26.033 37.139 25.878 1.00 13.46 1BPH 414 ATOM 287 CA ALA B 14 25.493 36.342 26.975 1.00 15.84 1BPH 415 ATOM 288 C ALA B 14 24.127 35.815 26.540 1.00 15.81 1BPH 416 ATOM 289 O ALA B 14 23.949 34.566 26.746 1.00 13.74 1BPH 417 ATOM 290 CB ALA B 14 25.481 37.089 28.314 1.00 13.53 1BPH 418 ATOM 291 N LEU B 15 23.228 36.592 25.926 1.00 15.58 1BPH 419 ATOM 292 CA LEU B 15 21.919 36.071 25.461 1.00 10.19 1BPH 420 ATOM 293 C LEU B 15 22.047 34.973 24.433 1.00 13.55 1BPH 421 ATOM 294 O LEU B 15 21.409 33.900 24.370 1.00 16.74 1BPH 422 ATOM 295 CB LEU B 15 21.155 37.262 24.912 1.00 17.54 1BPH 423 ATOM 296 CG LEU B 15 20.459 38.063 26.004 1.00 21.93 1BPH 424 ATOM 297 CD1 LEU B 15 20.024 39.374 25.342 1.00 22.50 1BPH 425 ATOM 298 CD2 LEU B 15 19.220 37.352 26.497 1.00 19.03 1BPH 426 ATOM 299 N TYR B 16 22.989 35.262 23.523 1.00 16.09 1BPH 427 ATOM 300 CA TYR B 16 23.333 34.339 22.435 1.00 13.16 1BPH 428 ATOM 301 C TYR B 16 23.766 32.983 22.946 1.00 12.93 1BPH 429 ATOM 302 O TYR B 16 23.294 31.923 22.469 1.00 16.48 1BPH 430 ATOM 303 CB TYR B 16 24.429 35.044 21.617 1.00 11.68 1BPH 431 ATOM 304 CG TYR B 16 24.933 34.090 20.552 1.00 14.65 1BPH 432 ATOM 305 CD1 TYR B 16 24.123 33.790 19.469 1.00 20.50 1BPH 433 ATOM 306 CD2 TYR B 16 26.205 33.529 20.621 1.00 15.14 1BPH 434 ATOM 307 CE1 TYR B 16 24.601 32.932 18.460 1.00 17.59 1BPH 435 ATOM 308 CE2 TYR B 16 26.730 32.669 19.650 1.00 12.82 1BPH 436 ATOM 309 CZ TYR B 16 25.887 32.420 18.568 1.00 22.15 1BPH 437 ATOM 310 OH TYR B 16 26.360 31.579 17.601 1.00 17.89 1BPH 438 ATOM 311 N LEU B 17 24.675 32.973 23.893 1.00 17.43 1BPH 439 ATOM 312 CA LEU B 17 25.242 31.773 24.507 1.00 15.03 1BPH 440 ATOM 313 C LEU B 17 24.259 31.012 25.366 1.00 20.12 1BPH 441 ATOM 314 O LEU B 17 24.151 29.775 25.246 1.00 15.32 1BPH 442 ATOM 315 CB LEU B 17 26.521 32.145 25.269 1.00 19.15 1BPH 443 ATOM 316 CG LEU B 17 27.759 32.528 24.462 1.00 28.76 1BPH 444 ATOM 317 CD1 LEU B 17 28.871 33.013 25.404 1.00 30.86 1BPH 445 ATOM 318 CD2 LEU B 17 28.147 31.338 23.587 1.00 18.48 1BPH 446 ATOM 319 N VAL B 18 23.490 31.650 26.195 1.00 15.94 1BPH 447 ATOM 320 CA VAL B 18 22.523 31.051 27.093 1.00 19.10 1BPH 448 ATOM 321 C VAL B 18 21.275 30.611 26.350 1.00 18.03 1BPH 449 ATOM 322 O VAL B 18 20.721 29.579 26.708 1.00 19.66 1BPH 450 ATOM 323 CB VAL B 18 22.197 32.054 28.238 1.00 18.92 1BPH 451 ATOM 324 CG1 VAL B 18 20.864 31.770 28.926 1.00 16.58 1BPH 452 ATOM 325 CG2 VAL B 18 23.354 32.196 29.202 1.00 19.69 1BPH 453 ATOM 326 N CYS B 19 20.862 31.405 25.370 1.00 14.58 1BPH 454 ATOM 327 CA CYS B 19 19.590 31.054 24.687 1.00 20.78 1BPH 455 ATOM 328 C CYS B 19 19.740 29.962 23.651 1.00 22.90 1BPH 456 ATOM 329 O CYS B 19 18.750 29.224 23.431 1.00 25.13 1BPH 457 ATOM 330 CB CYS B 19 18.870 32.312 24.167 1.00 14.23 1BPH 458 ATOM 331 SG CYS B 19 18.325 33.435 25.477 1.00 18.44 1BPH 459 ATOM 332 N GLY B 20 20.916 29.873 23.059 1.00 20.42 1BPH 460 ATOM 333 CA GLY B 20 21.184 28.845 22.045 1.00 28.47 1BPH 461 ATOM 334 C GLY B 20 20.204 28.975 20.883 1.00 27.38 1BPH 462 ATOM 335 O GLY B 20 19.860 30.077 20.446 1.00 25.32 1BPH 463 ATOM 336 N GLU B 21 19.683 27.825 20.492 1.00 23.51 1BPH 464 ATOM 337 CA GLU B 21 18.767 27.688 19.356 1.00 22.79 1BPH 465 ATOM 338 C GLU B 21 17.364 28.226 19.490 1.00 23.55 1BPH 466 ATOM 339 O GLU B 21 16.572 28.430 18.542 1.00 43.32 1BPH 467 ATOM 340 CB AGLU B 21 18.859 26.215 18.941 0.50 32.24 1BPH 468 ATOM 341 CB BGLU B 21 18.816 26.311 18.721 0.50 44.15 1BPH 469 ATOM 342 CG AGLU B 21 18.378 25.260 20.035 0.50 53.18 1BPH 470 ATOM 343 CG BGLU B 21 17.857 25.168 19.045 0.50 71.75 1BPH 471 ATOM 344 CD AGLU B 21 18.252 23.818 19.621 0.50 76.93 1BPH 472 ATOM 345 CD BGLU B 21 18.136 23.817 18.446 0.50 77.06 1BPH 473 ATOM 346 OE1AGLU B 21 19.209 23.104 19.342 0.50 80.08 1BPH 474 ATOM 347 OE1BGLU B 21 17.630 23.667 17.305 0.50 71.56 1BPH 475 ATOM 348 OE2AGLU B 21 17.052 23.450 19.601 0.50 75.98 1BPH 476 ATOM 349 OE2BGLU B 21 18.777 22.935 19.017 0.50 80.80 1BPH 477 ATOM 350 N ARG B 22 17.077 28.594 20.739 1.00 22.10 1BPH 478 ATOM 351 CA ARG B 22 15.791 29.231 20.994 1.00 18.98 1BPH 479 ATOM 352 C ARG B 22 15.879 30.641 20.378 1.00 18.56 1BPH 480 ATOM 353 O ARG B 22 14.904 31.088 19.746 1.00 42.38 1BPH 481 ATOM 354 CB AARG B 22 15.492 29.399 22.492 0.50 9.24 1BPH 482 ATOM 355 CB BARG B 22 15.582 29.686 22.588 0.50 20.08 1BPH 483 ATOM 356 CG AARG B 22 14.972 28.127 23.158 0.50 17.98 1BPH 484 ATOM 357 CG BARG B 22 15.281 28.313 23.184 0.50 37.23 1BPH 485 ATOM 358 CD AARG B 22 15.075 28.268 24.641 0.50 34.73 1BPH 486 ATOM 359 CD BARG B 22 16.299 27.936 24.208 0.50 39.44 1BPH 487 ATOM 360 NE AARG B 22 14.014 29.044 25.246 0.50 25.13 1BPH 488 ATOM 361 NE BARG B 22 15.871 28.298 25.586 0.50 18.60 1BPH 489 ATOM 362 CZ AARG B 22 13.996 29.348 26.552 0.50 32.64 1BPH 490 ATOM 363 CZ BARG B 22 16.859 28.110 26.487 0.50 27.52 1BPH 491 ATOM 364 NH1AARG B 22 14.997 28.924 27.329 0.50 22.11 1BPH 492 ATOM 365 NH1BARG B 22 17.844 27.323 26.036 0.50 35.85 1BPH 493 ATOM 366 NH2AARG B 22 12.979 30.074 27.020 0.50 23.08 1BPH 494 ATOM 367 NH2BARG B 22 16.875 28.645 27.689 0.50 15.95 1BPH 495 ATOM 368 N GLY B 23 17.009 31.302 20.575 1.00 21.37 1BPH 496 ATOM 369 CA GLY B 23 17.081 32.725 20.040 1.00 24.76 1BPH 497 ATOM 370 C GLY B 23 16.625 33.576 21.237 1.00 20.74 1BPH 498 ATOM 371 O GLY B 23 16.251 33.080 22.331 1.00 23.79 1BPH 499 ATOM 372 N PHE B 24 16.609 34.871 21.058 1.00 16.16 1BPH 500 ATOM 373 CA PHE B 24 16.259 35.828 22.135 1.00 20.18 1BPH 501 ATOM 374 C PHE B 24 15.747 37.093 21.444 1.00 22.61 1BPH 502 ATOM 375 O PHE B 24 15.751 37.262 20.216 1.00 19.52 1BPH 503 ATOM 376 CB PHE B 24 17.536 36.122 22.994 1.00 16.16 1BPH 504 ATOM 377 CG PHE B 24 18.734 36.613 22.192 1.00 23.39 1BPH 505 ATOM 378 CD1 PHE B 24 19.597 35.730 21.525 1.00 17.05 1BPH 506 ATOM 379 CD2 PHE B 24 18.978 37.990 22.047 1.00 15.66 1BPH 507 ATOM 380 CE1 PHE B 24 20.679 36.170 20.758 1.00 17.28 1BPH 508 ATOM 381 CE2 PHE B 24 20.030 38.490 21.281 1.00 17.82 1BPH 509 ATOM 382 CZ PHE B 24 20.877 37.562 20.642 1.00 18.98 1BPH 510 ATOM 383 N PHE B 25 15.333 38.026 22.260 1.00 15.44 1BPH 511 ATOM 384 CA PHE B 25 14.902 39.348 21.755 1.00 18.96 1BPH 512 ATOM 385 C PHE B 25 15.733 40.274 22.636 1.00 20.74 1BPH 513 ATOM 386 O PHE B 25 15.943 40.031 23.845 1.00 23.56 1BPH 514 ATOM 387 CB PHE B 25 13.410 39.424 21.662 1.00 28.65 1BPH 515 ATOM 388 CG PHE B 25 12.700 39.257 22.947 1.00 44.71 1BPH 516 ATOM 389 CD1 PHE B 25 12.560 40.338 23.828 1.00 56.33 1BPH 517 ATOM 390 CD2 PHE B 25 12.177 37.996 23.288 1.00 60.90 1BPH 518 ATOM 391 CE1 PHE B 25 11.875 40.179 25.064 1.00 44.39 1BPH 519 ATOM 392 CE2 PHE B 25 11.506 37.808 24.495 1.00 57.24 1BPH 520 ATOM 393 CZ PHE B 25 11.363 38.902 25.373 1.00 58.50 1BPH 521 ATOM 394 N TYR B 26 16.306 41.294 22.026 1.00 26.92 1BPH 522 ATOM 395 CA TYR B 26 17.153 42.278 22.725 1.00 19.55 1BPH 523 ATOM 396 C TYR B 26 16.499 43.636 22.535 1.00 30.21 1BPH 524 ATOM 397 O TYR B 26 16.600 44.187 21.417 1.00 24.71 1BPH 525 ATOM 398 CB TYR B 26 18.562 42.278 22.106 1.00 11.61 1BPH 526 ATOM 399 CG TYR B 26 19.452 43.398 22.631 1.00 21.36 1BPH 527 ATOM 400 CD1 TYR B 26 19.755 43.387 24.008 1.00 20.58 1BPH 528 ATOM 401 CD2 TYR B 26 19.916 44.465 21.863 1.00 15.42 1BPH 529 ATOM 402 CE1 TYR B 26 20.583 44.345 24.584 1.00 22.78 1BPH 530 ATOM 403 CE2 TYR B 26 20.723 45.448 22.460 1.00 18.05 1BPH 531 ATOM 404 CZ TYR B 26 21.073 45.393 23.806 1.00 28.02 1BPH 532 ATOM 405 OH TYR B 26 21.890 46.316 24.421 1.00 31.47 1BPH 533 ATOM 406 N THR B 27 15.848 44.126 23.579 1.00 27.14 1BPH 534 ATOM 407 CA THR B 27 15.158 45.457 23.477 1.00 42.36 1BPH 535 ATOM 408 C THR B 27 15.780 46.346 24.533 1.00 34.16 1BPH 536 ATOM 409 O THR B 27 15.374 46.325 25.714 1.00 38.15 1BPH 537 ATOM 410 CB THR B 27 13.612 45.233 23.635 1.00 49.00 1BPH 538 ATOM 411 OG1 THR B 27 13.389 44.741 24.999 1.00 70.15 1BPH 539 ATOM 412 CG2 THR B 27 13.021 44.176 22.692 1.00 54.18 1BPH 540 ATOM 413 N PRO B 28 16.809 47.082 24.129 1.00 39.30 1BPH 541 ATOM 414 CA PRO B 28 17.550 47.958 25.065 1.00 50.32 1BPH 542 ATOM 415 C PRO B 28 16.747 49.100 25.692 1.00 51.41 1BPH 543 ATOM 416 O PRO B 28 16.922 49.526 26.848 1.00 52.87 1BPH 544 ATOM 417 CB PRO B 28 18.744 48.435 24.231 1.00 33.07 1BPH 545 ATOM 418 CG PRO B 28 18.261 48.353 22.779 1.00 28.91 1BPH 546 ATOM 419 CD PRO B 28 17.355 47.133 22.751 1.00 30.72 1BPH 547 ATOM 420 N LYS B 29 15.830 49.593 24.905 1.00 58.03 1BPH 548 ATOM 421 CA ALYS B 29 14.935 50.708 25.214 0.50 56.38 1BPH 549 ATOM 422 CA BLYS B 29 15.106 50.841 24.970 0.50 57.81 1BPH 550 ATOM 423 C ALYS B 29 13.602 50.396 25.876 0.50 73.09 1BPH 551 ATOM 424 C BLYS B 29 13.915 50.201 25.692 0.50 66.40 1BPH 552 ATOM 425 O ALYS B 29 13.044 51.332 26.517 0.50 80.92 1BPH 553 ATOM 426 O BLYS B 29 12.908 49.842 25.053 0.50 53.34 1BPH 554 ATOM 427 CB ALYS B 29 14.689 51.541 23.932 0.50 58.98 1BPH 555 ATOM 428 CB BLYS B 29 14.658 51.386 23.598 0.50 45.66 1BPH 556 ATOM 429 N AALA B 30 13.056 49.194 25.782 0.50 74.55 1BPH 557 ATOM 430 N BALA B 30 14.075 50.102 27.005 0.50 71.75 1BPH 558 ATOM 431 CA AALA B 30 11.762 48.878 26.416 0.50 75.29 1BPH 559 ATOM 432 CA BALA B 30 13.075 49.536 27.915 0.50 73.80 1BPH 560 ATOM 433 C AALA B 30 11.853 47.818 27.515 0.50 68.10 1BPH 561 ATOM 434 C BALA B 30 12.867 50.426 29.144 0.50 73.94 1BPH 562 ATOM 435 O AALA B 30 10.774 47.235 27.799 0.50 65.90 1BPH 563 ATOM 436 O BALA B 30 12.394 49.828 30.144 0.50 69.68 1BPH 564 ATOM 437 CB AALA B 30 10.728 48.457 25.375 0.50 76.93 1BPH 565 ATOM 438 CB BALA B 30 13.512 48.144 28.366 0.50 73.70 1BPH 566 ATOM 439 OXTAALA B 30 12.952 47.610 28.048 0.50 63.45 1BPH 567 ATOM 440 OXTBALA B 30 13.182 51.623 29.061 0.50 76.41 1BPH 568 TER 441 ALA B 30 1BPH 569 HETATM 442 CL1 DCE 200 26.950 41.213 19.536 0.50 34.85 1BPH 570 HETATM 443 C1 DCE 200 28.222 40.003 20.178 0.50 24.42 1BPH 571 HETATM 444 C2 DCE 200 28.307 38.776 19.363 0.50 24.99 1BPH 572 HETATM 445 CL2 DCE 200 26.941 37.681 19.833 0.50 33.75 1BPH 573 HETATM 446 NA NA 88 20.339 43.145 38.263 0.50 13.22 1BPH 574 HETATM 447 O HOH 1 26.102 28.408 28.110 0.33 28.57 1BPH 575 HETATM 448 O HOH 2 26.719 28.525 28.242 0.66 30.29 1BPH 576 HETATM 449 O HOH 3 19.213 33.037 38.295 1.00 42.10 1BPH 577 HETATM 450 O HOH 4 21.104 32.216 20.645 1.00 26.61 1BPH 578 HETATM 451 O HOH 5 21.954 33.637 38.117 1.00 22.77 1BPH 579 HETATM 452 O HOH 6 25.355 29.575 16.012 1.00 37.71 1BPH 580 HETATM 453 O HOH 7 29.416 48.036 26.266 1.00 52.28 1BPH 581 HETATM 454 O HOH 8 23.316 47.073 26.907 1.00 35.56 1BPH 582 HETATM 455 O HOH 9 12.001 26.642 23.852 1.00 84.10 1BPH 583 HETATM 456 O HOH 10 29.629 38.631 27.887 0.50 36.47 1BPH 584 HETATM 457 O HOH 11 24.783 28.010 23.225 1.00 48.85 1BPH 585 HETATM 458 O HOH 12 10.060 28.856 28.439 1.00 57.62 1BPH 586 HETATM 459 O HOH 13 24.661 29.722 20.716 1.00 34.18 1BPH 587 HETATM 460 O HOH 14 19.309 51.671 37.680 1.00 71.85 1BPH 588 HETATM 461 O HOH 15 29.883 44.140 30.180 1.00 31.20 1BPH 589 HETATM 462 O HOH 16 19.460 51.625 32.662 1.00 56.77 1BPH 590 HETATM 463 O HOH 17 13.529 46.905 34.521 1.00 56.86 1BPH 591 HETATM 464 O HOH 18 27.754 49.256 34.634 1.00 59.80 1BPH 592 HETATM 465 O HOH 19 28.651 33.964 37.187 1.00 40.95 1BPH 593 HETATM 466 O HOH 20 25.911 50.450 38.269 1.00 73.37 1BPH 594 HETATM 467 O HOH 21 22.874 37.394 40.001 1.00 32.18 1BPH 595 HETATM 468 O HOH 22 14.461 44.482 27.832 1.00 33.04 1BPH 596 HETATM 469 O HOH 23 15.852 42.384 25.719 1.00 31.84 1BPH 597 HETATM 470 O HOH 24 16.330 47.795 28.775 1.00 26.21 1BPH 598 HETATM 471 O HOH 25 19.660 39.683 39.396 0.50 34.39 1BPH 599 HETATM 472 O HOH 26 30.929 40.726 21.439 1.00 51.07 1BPH 600 HETATM 473 O HOH 27 19.070 48.888 38.055 1.00 45.21 1BPH 601 HETATM 474 O HOH 28 20.424 43.275 40.602 0.50 17.83 1BPH 602 HETATM 475 O HOH 29 16.006 48.573 38.268 1.00 49.72 1BPH 603 HETATM 476 O HOH 30 30.639 36.135 26.950 0.50 32.80 1BPH 604 HETATM 477 O HOH 31 31.046 34.811 27.077 0.50 33.10 1BPH 605 HETATM 478 O HOH 32 30.194 36.915 29.974 1.00 56.34 1BPH 606 HETATM 479 O HOH 33 18.140 42.467 38.272 0.50 14.58 1BPH 607 HETATM 480 O HOH 34 22.081 48.485 22.596 1.00 55.97 1BPH 608 HETATM 481 O HOH 35 9.533 41.911 22.840 1.00 64.24 1BPH 609 HETATM 482 O HOH 36 11.567 44.462 28.369 1.00 52.66 1BPH 610 HETATM 483 O HOH 37 15.276 42.423 33.112 1.00 45.79 1BPH 611 HETATM 484 O HOH 38 28.678 39.163 40.782 1.00 62.27 1BPH 612 HETATM 485 O HOH 39 13.721 39.677 33.357 1.00 67.60 1BPH 613 HETATM 486 O HOH 40 13.370 41.327 35.143 1.00 66.32 1BPH 614 HETATM 487 O HOH 41 22.167 27.022 26.193 0.50 30.18 1BPH 615 HETATM 488 O HOH 42 20.620 26.388 25.258 0.50 29.67 1BPH 616 HETATM 489 O HOH 43 8.372 44.680 24.941 1.00 83.29 1BPH 617 HETATM 490 O HOH 44 23.122 28.165 19.140 1.00 72.74 1BPH 618 HETATM 491 O HOH 45 33.640 44.617 30.079 1.00 80.98 1BPH 619 HETATM 492 O HOH 46 23.340 51.881 29.149 1.00 78.00 1BPH 620 HETATM 493 O HOH 47 30.981 47.108 34.555 1.00 81.53 1BPH 621 HETATM 494 O HOH 48 34.483 40.238 32.020 1.00 81.32 1BPH 622 HETATM 495 O HOH 49 8.026 34.511 20.502 1.00 80.27 1BPH 623 HETATM 496 O HOH 50 10.258 41.722 20.218 1.00 69.65 1BPH 624 HETATM 497 O HOH 51 17.829 25.379 14.678 1.00 78.16 1BPH 625 HETATM 498 O HOH 52 19.217 52.503 35.050 1.00 68.12 1BPH 626 HETATM 499 O HOH 53 15.376 24.434 25.540 1.00 82.81 1BPH 627 HETATM 500 O HOH 54 21.768 55.234 32.076 1.00 85.97 1BPH 628 HETATM 501 O HOH 55 22.667 52.737 33.359 1.00 81.22 1BPH 629 CONECT 48 47 78 1BPH 630 CONECT 54 53 235 1BPH 631 CONECT 78 48 77 1BPH 632 CONECT 161 160 331 1BPH 633 CONECT 235 54 234 1BPH 634 CONECT 331 161 330 1BPH 635 CONECT 442 443 1BPH 636 CONECT 443 442 444 1BPH 637 CONECT 444 443 445 1BPH 638 CONECT 445 444 1BPH 639 MASTER 97 0 2 3 0 2 0 6 499 2 10 5 1BPHA 11 END 1BPH 641