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HEADER PROTEINASE INHIBITOR(TRYPSIN) 14-NOV-94 1AMC 1AMC 2
COMPND ALZHEIMER'S DISEASE AMYLOID BETA-PEPTIDE (RESIDUES 1 - 28) 1AMC 3
COMPND 2 (E.C. NUMBER NOT ASSIGNED) (NMR, 5 STRUCTURES) 1AMC 4
SOURCE HUMAN (HOMO SAPIENS) 1AMC 5
EXPDTA NMR 1AMC 6
AUTHOR J.TALAFOUS,K.J.MARCINOWSKI,G.KLOPMAN,M.G.ZAGORSKI 1AMC 7
REVDAT 1 26-JAN-95 1AMC 0 1AMC 8
JRNL AUTH J.TALAFOUS,K.J.MARCINOWSKI,G.KLOPMAN,M.G.ZAGORSKI 1AMC 9
JRNL TITL SOLUTION STRUCTURE OF RESIDUES 1 - 28 OF THE 1AMC 10
JRNL TITL 2 AMYLOID BETA-PEPTIDE 1AMC 11
JRNL REF BIOCHEMISTRY V. 33 7788 1994 1AMC 12
JRNL REFN ASTM BICHAW US ISSN 0006-2960 0033 1AMC 13
REMARK 1 1AMC 14
REMARK 1 REFERENCE 1 1AMC 15
REMARK 1 AUTH M.G.ZAGORSKI,C.J.BARROW 1AMC 16
REMARK 1 TITL NMR STUDIES OF AMYLOID BETA-PEPTIDES: PROTON 1AMC 17
REMARK 1 TITL 2 ASSIGNMENTS SECONDARY STRUCTURE, AND MECHANISM OF 1AMC 18
REMARK 1 TITL 3 AN ALPHA-HELIX TO BETA-SHEET CONVERSION FOR A 1AMC 19
REMARK 1 TITL 4 HOMOLOGOUS, 28-RESIDUE N-TERMINAL FRAGMENT 1AMC 20
REMARK 1 REF BIOCHEMISTRY V. 31 5621 1992 1AMC 21
REMARK 1 REFN ASTM BICHAW US ISSN 0006-2960 0033 1AMC 22
REMARK 1 REFERENCE 2 1AMC 23
REMARK 1 AUTH C.J.BARROW,M.G.ZAGORSKI 1AMC 24
REMARK 1 TITL SOLUTION STRUCTURES OF BETA-PEPTIDE AND ITS 1AMC 25
REMARK 1 TITL 2 CONSTITUENT FRAGMENTS: RELATION TO AMYLOID 1AMC 26
REMARK 1 TITL 3 DEPOSITION 1AMC 27
REMARK 1 REF SCIENCE V. 253 179 1991 1AMC 28
REMARK 1 REFN ASTM SCIEAS US ISSN 0036-8075 0038 1AMC 29
REMARK 2 1AMC 30
REMARK 2 RESOLUTION. NOT APPLICABLE. SEE REMARK 4. 1AMC 31
REMARK 3 1AMC 32
REMARK 3 REFINEMENT. 1AMC 33
REMARK 3 PROGRAM 1 X-PLOR 3.0 1AMC 34
REMARK 3 PROGRAM 1 BRUNGER 1AMC 35
REMARK 3 PROGRAM 2 GENERATE,DGSA,ACCEPT,AVERAGE, 1AMC 36
REMARK 3 PROGRAM 2 AND REFINE PROTOCOLS 1AMC 37
REMARK 3 AUTHORS 2 NILGES,GRONENBORN,BRUNGER, 1AMC 38
REMARK 3 AUTHORS 2 CLORE,KUSZEWSKI 1AMC 39
REMARK 3 1AMC 40
REMARK 3 NUMBER OF PROTEIN ATOMS: 438 1AMC 41
REMARK 3 1AMC 42
REMARK 3 1.) 100 STRUCTURES WERE GENERATED BY THE DGSA PROTOCOL 1AMC 43
REMARK 3 WITH THE FOLLOWING MODIFICATIONS: INITIAL TEMP=3000K, 1AMC 44
REMARK 3 HEATING STEPS=5000K COOLING STEPS=5000K, 2000 STEPS POWELL 1AMC 45
REMARK 3 MINIMIZATION, TIME STEP=0.003 PS, AND DIELECTRIC 1AMC 46
REMARK 3 CONSTANT=30. 1AMC 47
REMARK 3 2.) 95 OF THE 100 STRUCTURES WERE ACCEPTED BY THE ACCEPT 1AMC 48
REMARK 3 PROTOCOL. 1AMC 49
REMARK 3 3.) THE 95 STRUCTURES WERE AVERAGED AND MINIMIZED WITH THE 1AMC 50
REMARK 3 REFINE PROTOCOL WITH THE FOLLOWING MODIFICATIONS: COOLING 1AMC 51
REMARK 3 STEPS=5000 AND POWELL MINIMIZATION STEPS=10000 1AMC 52
REMARK 3 1AMC 53
REMARK 3 COORDINATES BELOW WERE PRODUCED BY MINIMIZING THE AVERAGE 1AMC 54
REMARK 3 OF ALL ACCEPTABLE STRUCTURES WHICH WERE GENERATED BY A 1AMC 55
REMARK 3 HYBRID DISTANCE GEOMETRY AND SIMULATED ANNEALING PROTOCOL. 1AMC 56
REMARK 3 1AMC 57
REMARK 3 STATISTICS INDICATING AGREEMENT OF MINIMIZED AVERAGE 1AMC 58
REMARK 3 STRUCTURE WITH EXPERIMENTAL RESTRAINTS AND IDEAL GEOMETRY 1AMC 59
REMARK 3 FOLLOW. 1AMC 60
REMARK 3 1AMC 61
REMARK 3 RESTRAINT TYPE NUMBER RMSD 1AMC 62
REMARK 3 DISTANCE (NO VIOLATIONS GREATER THAN 3.0 ANGSTROMS) 1AMC 63
REMARK 3 ALL 297 0.050 1AMC 64
REMARK 3 INTERRESIDUE 204 0.047 1AMC 65
REMARK 3 INTRARESIDUE 47 0.088 1AMC 66
REMARK 3 HYDROGEN BOND 46 0.015 1AMC 67
REMARK 3 TORSION ANGLES (NO VIOLATIONS GREATER THAN 5.0 DEGREES) 1AMC 68
REMARK 3 27 PHI, 2 CHI 29 0.004 1AMC 69
REMARK 3 1AMC 70
REMARK 3 IDEALIZED GEOMETRY 1AMC 71
REMARK 3 1AMC 72
REMARK 3 TYPE RMSD 1AMC 73
REMARK 3 BONDS 0.004 ANGSTROMS 1AMC 74
REMARK 3 ANGLES 0.387 DEGREES 1AMC 75
REMARK 3 IMPROPERS 0.007 DEGREES 1AMC 76
REMARK 3 1AMC 77
REMARK 3 X-PLOR POTENTIAL ENERGY TERMS 1AMC 78
REMARK 3 1AMC 79
REMARK 3 TERM TYPE ENERGY (KCAL/MOL) 1AMC 80
REMARK 3 OVERALL 70.0 1AMC 81
REMARK 3 NOE 36.8 1AMC 82
REMARK 3 CDIH 3.1 1AMC 83
REMARK 3 BONDS 5.9 1AMC 84
REMARK 3 ANGLES 18.0 1AMC 85
REMARK 3 IMPROPER 4.4 1AMC 86
REMARK 3 VDW (REPEL) 4.8 1AMC 87
REMARK 4 1AMC 88
REMARK 4 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION 1AMC 89
REMARK 4 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT 1AMC 90
REMARK 4 *CRYST1* AND *SCALE* RECORDS BE INCLUDED, BUT THE VALUES ON 1AMC 91
REMARK 4 THESE RECORDS ARE MEANINGLESS. 1AMC 92
REMARK 5 1AMC 93
REMARK 5 THESE COORDINATES WERE GENERATED FROM SOLUTION NMR DATA 1AMC 94
REMARK 5 COLLECTED IN H20:TRIFLUOROETHANOL-D3(4:6) AND 0.5 1AMC 95
REMARK 5 MILLIMOLAR NA2EDTA AND 0.05 MILLIMOLAR SODIUM AZIDE. PH 1AMC 96
REMARK 5 WAS SET AT 3.0. NMR DATA WAS COLLECTED AT 25 DEGREES 1AMC 97
REMARK 5 CELSIUS. 1AMC 98
REMARK 6 1AMC 99
REMARK 6 THE PROTEIN WAS GENERATED BY SOLID PHASE SYNTHESIS. 1AMC 100
REMARK 7 1AMC 101
REMARK 7 COLUMNS 61 - 66 OF *ATOM* RECORDS CONTAIN THE RMSD OF THE 1AMC 102
REMARK 7 ATOM IN THE FAMILY OF THE 95 ACCEPTED STRUCTURES. IN 1AMC 103
REMARK 7 ENTRIES GENERATED USING CRYSTALLOGRAPHIC TECHNIQUES, THESE 1AMC 104
REMARK 7 COLUMNS CONTAIN THE B VALUE. 1AMC 105
REMARK 8 1AMC 106
REMARK 8 THE ENTIRE STRUCTURE IS ESSENTIALLY ALPHA-HELICAL. 1AMC 107
REMARK 9 1AMC 108
REMARK 9 RESIDUE 4 - 25 HAVE THE MOST EXPERIMENTAL RESTRAINTS (NOE 1AMC 109
REMARK 9 CROSS PEAKS) AND ARE THE MOST DEFINED. 1AMC 110
REMARK 10 1AMC 111
REMARK 10 ORIGINAL DEPOSITION REVISED PRIOR TO RELEASE 1AMC 112
REMARK 10 TRACKING NUMBER: T5569, DATE REVISED: 04-DEC-94 1AMC 113
REMARK 11 1AMC 114
REMARK 11 CROSS REFERENCE TO SEQUENCE DATABASE 1AMC 115
REMARK 11 SWISS-PROT ENTRY NAME PDB ENTRY CHAIN NAME 1AMC 116
REMARK 11 A4_HUMAN 1AMC 117
SEQRES 1 28 ASP ALA GLU PHE ARG HIS ASP SER GLY TYR GLU VAL HIS 1AMC 118
SEQRES 2 28 HIS GLN LYS LEU VAL PHE PHE ALA GLU ASP VAL GLY SER 1AMC 119
SEQRES 3 28 ASN LYS 1AMC 120
HELIX 1 H1 PHE 4 GLY 25 1 MOST DEFINED HELICAL REGION 1AMC 121
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1 1AMC 122
ORIGX1 1.000000 0.000000 0.000000 0.00000 1AMC 123
ORIGX2 0.000000 1.000000 0.000000 0.00000 1AMC 124
ORIGX3 0.000000 0.000000 1.000000 0.00000 1AMC 125
SCALE1 1.000000 0.000000 0.000000 0.00000 1AMC 126
SCALE2 0.000000 1.000000 0.000000 0.00000 1AMC 127
SCALE3 0.000000 0.000000 1.000000 0.00000 1AMC 128
MODEL 1 1AMC 129
ATOM 1 N ASP 1 20.022 -5.487 -0.492 1.00 0.00 1AMC 130
ATOM 2 CA ASP 1 18.832 -4.846 -1.120 1.00 0.00 1AMC 131
ATOM 3 C ASP 1 17.590 -5.142 -0.280 1.00 0.00 1AMC 132
ATOM 4 O ASP 1 16.473 -4.916 -0.703 1.00 0.00 1AMC 133
ATOM 5 CB ASP 1 18.639 -5.405 -2.532 1.00 0.00 1AMC 134
ATOM 6 CG ASP 1 19.661 -4.773 -3.477 1.00 0.00 1AMC 135
ATOM 7 OD1 ASP 1 19.938 -3.595 -3.316 1.00 0.00 1AMC 136
ATOM 8 OD2 ASP 1 20.151 -5.477 -4.345 1.00 0.00 1AMC 137
ATOM 9 1H ASP 1 19.793 -6.469 -0.237 1.00 0.00 1AMC 138
ATOM 10 2H ASP 1 20.815 -5.480 -1.164 1.00 0.00 1AMC 139
ATOM 11 3H ASP 1 20.288 -4.958 0.365 1.00 0.00 1AMC 140
ATOM 12 HA ASP 1 18.985 -3.778 -1.174 1.00 0.00 1AMC 141
ATOM 13 1HB ASP 1 18.775 -6.477 -2.516 1.00 0.00 1AMC 142
ATOM 14 2HB ASP 1 17.642 -5.174 -2.877 1.00 0.00 1AMC 143
ATOM 15 N ALA 2 17.772 -5.647 0.910 1.00 0.00 1AMC 144
ATOM 16 CA ALA 2 16.603 -5.957 1.777 1.00 0.00 1AMC 145
ATOM 17 C ALA 2 15.763 -4.693 1.971 1.00 0.00 1AMC 146
ATOM 18 O ALA 2 14.716 -4.535 1.376 1.00 0.00 1AMC 147
ATOM 19 CB ALA 2 17.099 -6.454 3.135 1.00 0.00 1AMC 148
ATOM 20 H ALA 2 18.680 -5.822 1.234 1.00 0.00 1AMC 149
ATOM 21 HA ALA 2 16.000 -6.722 1.310 1.00 0.00 1AMC 150
ATOM 22 1HB ALA 2 17.967 -5.883 3.431 1.00 0.00 1AMC 151
ATOM 23 2HB ALA 2 16.320 -6.330 3.870 1.00 0.00 1AMC 152
ATOM 24 3HB ALA 2 17.364 -7.498 3.060 1.00 0.00 1AMC 153
ATOM 25 N GLU 3 16.215 -3.790 2.798 1.00 0.00 1AMC 154
ATOM 26 CA GLU 3 15.443 -2.538 3.029 1.00 0.00 1AMC 155
ATOM 27 C GLU 3 15.005 -1.944 1.690 1.00 0.00 1AMC 156
ATOM 28 O GLU 3 14.020 -1.239 1.605 1.00 0.00 1AMC 157
ATOM 29 CB GLU 3 16.308 -1.540 3.768 1.00 0.00 1AMC 158
ATOM 30 CG GLU 3 17.557 -1.219 2.946 1.00 0.00 1AMC 159
ATOM 31 CD GLU 3 18.418 -0.204 3.699 1.00 0.00 1AMC 160
ATOM 32 OE1 GLU 3 17.914 0.388 4.640 1.00 0.00 1AMC 161
ATOM 33 OE2 GLU 3 19.567 -0.037 3.325 1.00 0.00 1AMC 162
ATOM 34 H GLU 3 17.063 -3.937 3.268 1.00 0.00 1AMC 163
ATOM 35 HA GLU 3 14.581 -2.749 3.632 1.00 0.00 1AMC 164
ATOM 36 1HB GLU 3 15.736 -0.643 3.936 1.00 0.00 1AMC 165
ATOM 37 2HB GLU 3 16.593 -1.965 4.711 1.00 0.00 1AMC 166
ATOM 38 1HG GLU 3 18.123 -2.124 2.783 1.00 0.00 1AMC 167
ATOM 39 2HG GLU 3 17.265 -0.802 1.993 1.00 0.00 1AMC 168
ATOM 40 N PHE 4 15.733 -2.221 0.646 1.00 0.00 1AMC 169
ATOM 41 CA PHE 4 15.364 -1.673 -0.688 1.00 0.00 1AMC 170
ATOM 42 C PHE 4 13.967 -2.158 -1.084 1.00 0.00 1AMC 171
ATOM 43 O PHE 4 13.007 -1.411 -1.060 1.00 0.00 1AMC 172
ATOM 44 CB PHE 4 16.375 -2.136 -1.727 1.00 0.00 1AMC 173
ATOM 45 CG PHE 4 16.979 -0.921 -2.378 1.00 0.00 1AMC 174
ATOM 46 CD1 PHE 4 17.811 -0.074 -1.636 1.00 0.00 1AMC 175
ATOM 47 CD2 PHE 4 16.704 -0.639 -3.719 1.00 0.00 1AMC 176
ATOM 48 CE1 PHE 4 18.373 1.059 -2.241 1.00 0.00 1AMC 177
ATOM 49 CE2 PHE 4 17.264 0.494 -4.325 1.00 0.00 1AMC 178
ATOM 50 CZ PHE 4 18.100 1.342 -3.586 1.00 0.00 1AMC 179
ATOM 51 H PHE 4 16.526 -2.790 0.740 1.00 0.00 1AMC 180
ATOM 52 HA PHE 4 15.374 -0.593 -0.653 1.00 0.00 1AMC 181
ATOM 53 1HB PHE 4 17.150 -2.717 -1.246 1.00 0.00 1AMC 182
ATOM 54 2HB PHE 4 15.880 -2.738 -2.474 1.00 0.00 1AMC 183
ATOM 55 HD1 PHE 4 18.017 -0.292 -0.596 1.00 0.00 1AMC 184
ATOM 56 HD2 PHE 4 16.054 -1.292 -4.283 1.00 0.00 1AMC 185
ATOM 57 HE1 PHE 4 19.015 1.713 -1.671 1.00 0.00 1AMC 186
ATOM 58 HE2 PHE 4 17.052 0.712 -5.362 1.00 0.00 1AMC 187
ATOM 59 HZ PHE 4 18.532 2.214 -4.053 1.00 0.00 1AMC 188
ATOM 60 N ARG 5 13.844 -3.406 -1.449 1.00 0.00 1AMC 189
ATOM 61 CA ARG 5 12.508 -3.935 -1.849 1.00 0.00 1AMC 190
ATOM 62 C ARG 5 11.575 -3.950 -0.641 1.00 0.00 1AMC 191
ATOM 63 O ARG 5 10.385 -4.172 -0.761 1.00 0.00 1AMC 192
ATOM 64 CB ARG 5 12.655 -5.355 -2.402 1.00 0.00 1AMC 193
ATOM 65 CG ARG 5 13.817 -5.418 -3.381 1.00 0.00 1AMC 194
ATOM 66 CD ARG 5 13.908 -6.839 -3.896 1.00 0.00 1AMC 195
ATOM 67 NE ARG 5 15.042 -6.959 -4.856 1.00 0.00 1AMC 196
ATOM 68 CZ ARG 5 15.493 -8.138 -5.196 1.00 0.00 1AMC 197
ATOM 69 NH1 ARG 5 14.949 -9.216 -4.700 1.00 0.00 1AMC 198
ATOM 70 NH2 ARG 5 16.488 -8.237 -6.033 1.00 0.00 1AMC 199
ATOM 71 H ARG 5 14.628 -3.993 -1.462 1.00 0.00 1AMC 200
ATOM 72 HA ARG 5 12.091 -3.297 -2.601 1.00 0.00 1AMC 201
ATOM 73 1HB ARG 5 12.840 -6.046 -1.595 1.00 0.00 1AMC 202
ATOM 74 2HB ARG 5 11.750 -5.642 -2.913 1.00 0.00 1AMC 203
ATOM 75 1HG ARG 5 13.639 -4.740 -4.203 1.00 0.00 1AMC 204
ATOM 76 2HG ARG 5 14.736 -5.158 -2.880 1.00 0.00 1AMC 205
ATOM 77 1HD ARG 5 14.065 -7.503 -3.059 1.00 0.00 1AMC 206
ATOM 78 2HD ARG 5 12.982 -7.092 -4.389 1.00 0.00 1AMC 207
ATOM 79 HE ARG 5 15.452 -6.152 -5.231 1.00 0.00 1AMC 208
ATOM 80 1HH1 ARG 5 14.185 -9.145 -4.058 1.00 0.00 1AMC 209
ATOM 81 2HH1 ARG 5 15.296 -10.116 -4.963 1.00 0.00 1AMC 210
ATOM 82 1HH2 ARG 5 16.905 -7.412 -6.415 1.00 0.00 1AMC 211
ATOM 83 2HH2 ARG 5 16.834 -9.138 -6.294 1.00 0.00 1AMC 212
ATOM 84 N HIS 6 12.104 -3.704 0.516 1.00 0.00 1AMC 213
ATOM 85 CA HIS 6 11.255 -3.690 1.739 1.00 0.00 1AMC 214
ATOM 86 C HIS 6 10.414 -2.417 1.739 1.00 0.00 1AMC 215
ATOM 87 O HIS 6 9.220 -2.455 1.522 1.00 0.00 1AMC 216
ATOM 88 CB HIS 6 12.142 -3.719 2.986 1.00 0.00 1AMC 217
ATOM 89 CG HIS 6 11.317 -4.125 4.177 1.00 0.00 1AMC 218
ATOM 90 ND1 HIS 6 11.543 -5.310 4.862 1.00 0.00 1AMC 219
ATOM 91 CD2 HIS 6 10.266 -3.517 4.818 1.00 0.00 1AMC 220
ATOM 92 CE1 HIS 6 10.648 -5.376 5.863 1.00 0.00 1AMC 221
ATOM 93 NE2 HIS 6 9.845 -4.308 5.882 1.00 0.00 1AMC 222
ATOM 94 H HIS 6 13.059 -3.518 0.579 1.00 0.00 1AMC 223
ATOM 95 HA HIS 6 10.603 -4.552 1.736 1.00 0.00 1AMC 224
ATOM 96 1HB HIS 6 12.942 -4.431 2.841 1.00 0.00 1AMC 225
ATOM 97 2HB HIS 6 12.559 -2.738 3.154 1.00 0.00 1AMC 226
ATOM 98 HD1 HIS 6 12.230 -5.977 4.653 1.00 0.00 1AMC 227
ATOM 99 HD2 HIS 6 9.832 -2.567 4.539 1.00 0.00 1AMC 228
ATOM 100 HE1 HIS 6 10.585 -6.193 6.567 1.00 0.00 1AMC 229
ATOM 101 N ASP 7 11.026 -1.289 1.972 1.00 0.00 1AMC 230
ATOM 102 CA ASP 7 10.259 -0.014 1.976 1.00 0.00 1AMC 231
ATOM 103 C ASP 7 9.500 0.122 0.656 1.00 0.00 1AMC 232
ATOM 104 O ASP 7 8.375 0.573 0.624 1.00 0.00 1AMC 233
ATOM 105 CB ASP 7 11.220 1.162 2.137 1.00 0.00 1AMC 234
ATOM 106 CG ASP 7 10.452 2.476 1.983 1.00 0.00 1AMC 235
ATOM 107 OD1 ASP 7 9.519 2.687 2.741 1.00 0.00 1AMC 236
ATOM 108 OD2 ASP 7 10.808 3.249 1.109 1.00 0.00 1AMC 237
ATOM 109 H ASP 7 11.991 -1.280 2.138 1.00 0.00 1AMC 238
ATOM 110 HA ASP 7 9.557 -0.019 2.797 1.00 0.00 1AMC 239
ATOM 111 1HB ASP 7 11.673 1.122 3.118 1.00 0.00 1AMC 240
ATOM 112 2HB ASP 7 11.988 1.105 1.382 1.00 0.00 1AMC 241
ATOM 113 N SER 8 10.100 -0.271 -0.435 1.00 0.00 1AMC 242
ATOM 114 CA SER 8 9.393 -0.166 -1.743 1.00 0.00 1AMC 243
ATOM 115 C SER 8 8.032 -0.855 -1.622 1.00 0.00 1AMC 244
ATOM 116 O SER 8 6.992 -0.225 -1.698 1.00 0.00 1AMC 245
ATOM 117 CB SER 8 10.221 -0.850 -2.831 1.00 0.00 1AMC 246
ATOM 118 OG SER 8 11.236 0.039 -3.277 1.00 0.00 1AMC 247
ATOM 119 H SER 8 11.010 -0.640 -0.395 1.00 0.00 1AMC 248
ATOM 120 HA SER 8 9.251 0.876 -1.995 1.00 0.00 1AMC 249
ATOM 121 1HB SER 8 10.679 -1.739 -2.432 1.00 0.00 1AMC 250
ATOM 122 2HB SER 8 9.575 -1.119 -3.657 1.00 0.00 1AMC 251
ATOM 123 HG SER 8 11.928 -0.482 -3.690 1.00 0.00 1AMC 252
ATOM 124 N GLY 9 8.032 -2.145 -1.418 1.00 0.00 1AMC 253
ATOM 125 CA GLY 9 6.742 -2.874 -1.276 1.00 0.00 1AMC 254
ATOM 126 C GLY 9 6.088 -2.483 0.051 1.00 0.00 1AMC 255
ATOM 127 O GLY 9 4.978 -2.875 0.345 1.00 0.00 1AMC 256
ATOM 128 H GLY 9 8.882 -2.632 -1.348 1.00 0.00 1AMC 257
ATOM 129 1HA GLY 9 6.087 -2.612 -2.095 1.00 0.00 1AMC 258
ATOM 130 2HA GLY 9 6.925 -3.937 -1.285 1.00 0.00 1AMC 259
ATOM 131 N TYR 10 6.773 -1.715 0.856 1.00 0.00 1AMC 260
ATOM 132 CA TYR 10 6.206 -1.296 2.157 1.00 0.00 1AMC 261
ATOM 133 C TYR 10 5.120 -0.244 1.932 1.00 0.00 1AMC 262
ATOM 134 O TYR 10 3.997 -0.378 2.388 1.00 0.00 1AMC 263
ATOM 135 CB TYR 10 7.321 -0.689 3.002 1.00 0.00 1AMC 264
ATOM 136 CG TYR 10 6.877 -0.647 4.433 1.00 0.00 1AMC 265
ATOM 137 CD1 TYR 10 6.478 -1.826 5.067 1.00 0.00 1AMC 266
ATOM 138 CD2 TYR 10 6.862 0.567 5.123 1.00 0.00 1AMC 267
ATOM 139 CE1 TYR 10 6.060 -1.794 6.402 1.00 0.00 1AMC 268
ATOM 140 CE2 TYR 10 6.445 0.605 6.460 1.00 0.00 1AMC 269
ATOM 141 CZ TYR 10 6.045 -0.577 7.101 1.00 0.00 1AMC 270
ATOM 142 OH TYR 10 5.633 -0.542 8.418 1.00 0.00 1AMC 271
ATOM 143 H TYR 10 7.664 -1.412 0.607 1.00 0.00 1AMC 272
ATOM 144 HA TYR 10 5.790 -2.150 2.669 1.00 0.00 1AMC 273
ATOM 145 1HB TYR 10 8.210 -1.297 2.919 1.00 0.00 1AMC 274
ATOM 146 2HB TYR 10 7.534 0.313 2.660 1.00 0.00 1AMC 275
ATOM 147 HD1 TYR 10 6.490 -2.761 4.521 1.00 0.00 1AMC 276
ATOM 148 HD2 TYR 10 7.172 1.475 4.621 1.00 0.00 1AMC 277
ATOM 149 HE1 TYR 10 5.751 -2.705 6.893 1.00 0.00 1AMC 278
ATOM 150 HE2 TYR 10 6.434 1.542 6.994 1.00 0.00 1AMC 279
ATOM 151 HH TYR 10 5.058 0.218 8.529 1.00 0.00 1AMC 280
ATOM 152 N GLU 11 5.440 0.800 1.219 1.00 0.00 1AMC 281
ATOM 153 CA GLU 11 4.433 1.850 0.961 1.00 0.00 1AMC 282
ATOM 154 C GLU 11 3.461 1.324 -0.081 1.00 0.00 1AMC 283
ATOM 155 O GLU 11 2.266 1.481 0.027 1.00 0.00 1AMC 284
ATOM 156 CB GLU 11 5.123 3.111 0.436 1.00 0.00 1AMC 285
ATOM 157 CG GLU 11 5.569 3.977 1.616 1.00 0.00 1AMC 286
ATOM 158 CD GLU 11 6.985 4.497 1.361 1.00 0.00 1AMC 287
ATOM 159 OE1 GLU 11 7.899 3.689 1.349 1.00 0.00 1AMC 288
ATOM 160 OE2 GLU 11 7.130 5.695 1.181 1.00 0.00 1AMC 289
ATOM 161 H GLU 11 6.339 0.884 0.845 1.00 0.00 1AMC 290
ATOM 162 HA GLU 11 3.907 2.075 1.874 1.00 0.00 1AMC 291
ATOM 163 1HB GLU 11 5.984 2.829 -0.151 1.00 0.00 1AMC 292
[snip]
ATOM 2150 O SER 26 -18.805 2.088 1.391 1.00 0.00 1AMC2287
ATOM 2151 CB SER 26 -16.141 2.252 -0.669 1.00 0.00 1AMC2288
ATOM 2152 OG SER 26 -17.304 2.638 -1.389 1.00 0.00 1AMC2289
ATOM 2153 H SER 26 -14.573 1.166 1.097 1.00 0.00 1AMC2290
ATOM 2154 HA SER 26 -16.518 3.156 1.242 1.00 0.00 1AMC2291
ATOM 2155 1HB SER 26 -15.369 2.986 -0.823 1.00 0.00 1AMC2292
ATOM 2156 2HB SER 26 -15.794 1.288 -1.016 1.00 0.00 1AMC2293
ATOM 2157 HG SER 26 -17.945 1.927 -1.323 1.00 0.00 1AMC2294
ATOM 2158 N ASN 27 -17.903 0.209 0.693 1.00 0.00 1AMC2295
ATOM 2159 CA ASN 27 -19.191 -0.527 0.839 1.00 0.00 1AMC2296
ATOM 2160 C ASN 27 -19.100 -1.475 2.037 1.00 0.00 1AMC2297
ATOM 2161 O ASN 27 -19.388 -2.650 1.934 1.00 0.00 1AMC2298
ATOM 2162 CB ASN 27 -19.458 -1.338 -0.431 1.00 0.00 1AMC2299
ATOM 2163 CG ASN 27 -18.445 -2.465 -0.540 1.00 0.00 1AMC2300
ATOM 2164 OD1 ASN 27 -17.565 -2.595 0.288 1.00 0.00 1AMC2301
ATOM 2165 ND2 ASN 27 -18.535 -3.290 -1.537 1.00 0.00 1AMC2302
ATOM 2166 H ASN 27 -17.105 -0.263 0.374 1.00 0.00 1AMC2303
ATOM 2167 HA ASN 27 -19.994 0.178 0.993 1.00 0.00 1AMC2304
ATOM 2168 1HB ASN 27 -20.451 -1.759 -0.391 1.00 0.00 1AMC2305
ATOM 2169 2HB ASN 27 -19.369 -0.701 -1.297 1.00 0.00 1AMC2306
ATOM 2170 1HD2 ASN 27 -17.897 -4.015 -1.622 1.00 0.00 1AMC2307
ATOM 2171 2HD2 ASN 27 -19.246 -3.181 -2.202 1.00 0.00 1AMC2308
ATOM 2172 N LYS 28 -18.699 -0.974 3.173 1.00 0.00 1AMC2309
ATOM 2173 CA LYS 28 -18.587 -1.847 4.376 1.00 0.00 1AMC2310
ATOM 2174 C LYS 28 -19.814 -1.647 5.267 1.00 0.00 1AMC2311
ATOM 2175 O LYS 28 -19.820 -2.184 6.362 1.00 0.00 1AMC2312
ATOM 2176 CB LYS 28 -17.324 -1.478 5.158 1.00 0.00 1AMC2313
ATOM 2177 CG LYS 28 -16.390 -2.689 5.227 1.00 0.00 1AMC2314
ATOM 2178 CD LYS 28 -15.659 -2.694 6.572 1.00 0.00 1AMC2315
ATOM 2179 CE LYS 28 -16.662 -2.950 7.698 1.00 0.00 1AMC2316
ATOM 2180 NZ LYS 28 -16.683 -1.780 8.620 1.00 0.00 1AMC2317
ATOM 2181 OXT LYS 28 -20.728 -0.960 4.838 1.00 0.00 1AMC2318
ATOM 2182 H LYS 28 -18.470 -0.023 3.235 1.00 0.00 1AMC2319
ATOM 2183 HA LYS 28 -18.530 -2.879 4.067 1.00 0.00 1AMC2320
ATOM 2184 1HB LYS 28 -16.819 -0.661 4.661 1.00 0.00 1AMC2321
ATOM 2185 2HB LYS 28 -17.595 -1.178 6.159 1.00 0.00 1AMC2322
ATOM 2186 1HG LYS 28 -16.969 -3.595 5.128 1.00 0.00 1AMC2323
ATOM 2187 2HG LYS 28 -15.666 -2.632 4.427 1.00 0.00 1AMC2324
ATOM 2188 1HD LYS 28 -14.910 -3.473 6.571 1.00 0.00 1AMC2325
ATOM 2189 2HD LYS 28 -15.183 -1.737 6.728 1.00 0.00 1AMC2326
ATOM 2190 1HE LYS 28 -17.646 -3.096 7.278 1.00 0.00 1AMC2327
ATOM 2191 2HE LYS 28 -16.371 -3.835 8.245 1.00 0.00 1AMC2328
ATOM 2192 1HZ LYS 28 -15.716 -1.423 8.750 1.00 0.00 1AMC2329
ATOM 2193 2HZ LYS 28 -17.280 -1.030 8.214 1.00 0.00 1AMC2330
ATOM 2194 3HZ LYS 28 -17.070 -2.070 9.541 1.00 0.00 1AMC2331
TER 2195 LYS 28 1AMC2332
ENDMDL 1AMC2333
MASTER 104 0 0 1 0 0 0 6 2190 5 0 3 1AMC2334
END 1AMC2335
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