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1bdm.pdb
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HEADER OXIDOREDUCTASE(NAD(A)-CHOH(D)) 16-FEB-93 1BDM 1BDM 2
COMPND MALATE DEHYDROGENASE (E.C.1.1.1.37) MUTANT WITH THR 189 1BDM 3
COMPND 2 REPLACED BY ILE (T189I) COMPLEXED WITH BETA-6-HYDROXY- 1BDM 4
COMPND 3 1,4,5,6-TETRAHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE 1BDM 5
COMPND 4 (REFERRED TO AS (6HTN)AD, OR NADHX) 1BDM 6
SOURCE (THERMUS FLAVUS, STRAIN F428) 1BDM 7
AUTHOR C.A.KELLY,J.J.BIRKTOFT 1BDM 8
REVDAT 1 20-DEC-94 1BDM 0 1BDM 9
JRNL AUTH C.A.KELLY,M.NISHIYAMA,T.BEPPU,J.J.BIRKTOFT 1BDM 10
JRNL TITL THE STRUCTURE AT 1.8 ANGSTROMS RESOLUTION OF A 1BDM 11
JRNL TITL 2 SINGLE SITE MUTANT (T189I) OF MALATE 1BDM 12
JRNL TITL 3 DEHYDROGENASE FROM THERMUS FLAVUS WITH INCREASED 1BDM 13
JRNL TITL 4 ENZYMATIC ACTIVITY 1BDM 14
JRNL REF TO BE PUBLISHED 1BDM 15
JRNL REFN 0353 1BDM 16
REMARK 1 1BDM 17
REMARK 1 REFERENCE 1 1BDM 18
REMARK 1 AUTH C.A.KELLY,M.NISHIYAMA,Y.ONISHI,T.BEPPU, 1BDM 19
REMARK 1 AUTH 2 J.J.BIRKTOFT 1BDM 20
REMARK 1 TITL DETERMINANTS OF PROTEIN THERMOSTABILITY OBSERVED 1BDM 21
REMARK 1 TITL 2 IN THE 1.9 ANGSTROMS CRYSTAL STRUCTURE OF MALATE 1BDM 22
REMARK 1 TITL 3 DEHYDROGENASE FROM THE THERMOPHILIC BACTERIUM 1BDM 23
REMARK 1 TITL 4 THERMUS FLAVUS 1BDM 24
REMARK 1 REF BIOCHEMISTRY V. 32 3913 1993 1BDM 25
REMARK 1 REFN ASTM BICHAW US ISSN 0006-2960 0033 1BDM 26
REMARK 1 REFERENCE 2 1BDM 27
REMARK 1 AUTH C.A.KELLY,S.SARFATY,M.NISHIYAMA,T.BEPPU, 1BDM 28
REMARK 1 AUTH 2 J.J.BIRKTOFT 1BDM 29
REMARK 1 TITL PRELIMINARY X-RAY DIFFRACTION ANALYSIS OF A 1BDM 30
REMARK 1 TITL 2 CRYSTALLIZABLE MUTANT OF MALATE DEHYDROGENASE 1BDM 31
REMARK 1 TITL 3 FROM THE THERMOPHILE THERMUS FLAVUS 1BDM 32
REMARK 1 REF J.MOL.BIOL. V. 221 383 1991 1BDM 33
REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 0070 1BDM 34
REMARK 1 REFERENCE 3 1BDM 35
REMARK 1 AUTH M.NISHIYAMA,K.SHIMADA,S.HORINOUCHI,T.BEPPU 1BDM 36
REMARK 1 TITL ROLE OF THREONINE 190 IN MODULATING THE CATALYTIC 1BDM 37
REMARK 1 TITL 2 FUNCTION OF MALATE DEHYDROGENASE FROM A 1BDM 38
REMARK 1 TITL 3 THERMOPHILE THERMUS FLAVUS 1BDM 39
REMARK 1 REF J.BIOL.CHEM. V. 266 14294 1991 1BDM 40
REMARK 1 REFN ASTM JBCHA3 US ISSN 0021-9258 0071 1BDM 41
REMARK 1 REFERENCE 4 1BDM 42
REMARK 1 AUTH J.J.BIRKTOFT,G.RHODES,L.J.BANASZAK 1BDM 43
REMARK 1 TITL REFINED CRYSTAL STRUCTURE OF CYTOPLASMIC MALATE 1BDM 44
REMARK 1 TITL 2 DEHYDROGENASE AT 2.5-ANGSTROMS RESOLUTION 1BDM 45
REMARK 1 REF BIOCHEMISTRY V. 28 6065 1989 1BDM 46
REMARK 1 REFN ASTM BICHAW US ISSN 0006-2960 0033 1BDM 47
REMARK 1 REFERENCE 5 1BDM 48
REMARK 1 AUTH M.NISHIYAMA,N.MATSUBARA,K.YAMAMOTO,S.IIJIMA, 1BDM 49
REMARK 1 AUTH 2 T.UOZUMI,T.BEPPU 1BDM 50
REMARK 1 TITL NUCLEOTIDE SEQUENCE OF THE MALATE DEHYDROGENASE 1BDM 51
REMARK 1 TITL 2 GENE OF THERMUS FLAVUS AND ITS MUTATION DIRECTING 1BDM 52
REMARK 1 TITL 3 AN INCREASE IN ENZYME ACTIVITY 1BDM 53
REMARK 1 REF J.BIOL.CHEM. V. 261 14178 1986 1BDM 54
REMARK 1 REFN ASTM JBCHA3 US ISSN 0021-9258 0071 1BDM 55
REMARK 1 REFERENCE 6 1BDM 56
REMARK 1 AUTH N.J.OPPENHEIMER 1BDM 57
REMARK 1 TITL CHEMISTRY AND SOLUTION CONFORMATION OF THE 1BDM 58
REMARK 1 TITL 2 PYRIDINE COENZYMES 1BDM 59
REMARK 1 EDIT J.EVERSE,B.ANDERSON,K.-S.YOU 1BDM 60
REMARK 1 REF THE PYRIDINE NUCLEOTIDE 51 1982 1BDM 61
REMARK 1 REF 2 COENZYMES 1BDM 62
REMARK 1 PUBL ACADEMIC PRESS, NEW YORK 1BDM 63
REMARK 1 REFN ISBN 0-12-244750-6 0768 1BDM 64
REMARK 1 REFERENCE 7 1BDM 65
REMARK 1 AUTH L.J.BANASZAK,R.A.BRADSHAW 1BDM 66
REMARK 1 TITL MALATE DEHYDROGENASE 1BDM 67
REMARK 1 EDIT P.D.BOYER 1BDM 68
REMARK 1 REF THE ENZYMES,THIRD EDITION V. 11A 369 1975 1BDM 69
REMARK 1 PUBL ACADEMIC PRESS,NEW YORK 1BDM 70
REMARK 1 REFN ISBN 0-12-122711-1 0436 1BDM 71
REMARK 2 1BDM 72
REMARK 2 RESOLUTION. 1.8 ANGSTROMS. 1BDM 73
REMARK 3 1BDM 74
REMARK 3 REFINEMENT. 1BDM 75
REMARK 3 PROGRAM X-PLOR 1BDM 76
REMARK 3 AUTHORS BRUNGER 1BDM 77
REMARK 3 R VALUE 0.169 1BDM 78
REMARK 3 RMSD BOND DISTANCES 0.014 ANGSTROMS 1BDM 79
REMARK 3 RMSD BOND ANGLES 2.77 DEGREES 1BDM 80
REMARK 4 1BDM 81
REMARK 4 THE SIDE CHAIN OF GLU 27 IN EACH SUBUNIT WAS BEST FIT TO 1BDM 82
REMARK 4 THE ELECTRON DENSITY BY ASSIGNING TWO CONFORMATIONS WHOSE 1BDM 83
REMARK 4 COORDINATES ARE INCLUDED IN THIS DATA SET. THE PEPTIDE 1BDM 84
REMARK 4 BACKBONE BETWEEN RESIDUES 90 AND 101, EXCLUSIVE, OF THE A 1BDM 85
REMARK 4 SUBUNIT COULD NOT BE TRACED DUE TO POOR ELECTRON DENSITY. 1BDM 86
REMARK 5 1BDM 87
REMARK 5 THE NUMBERING SYSTEM IS THE SAME AS THAT USED FOR THE 1BDM 88
REMARK 5 CYTOPLASMIC MALATE DEHYDROGENASE STRUCTURE. THE DELETION 1BDM 89
REMARK 5 REGIONS IN TMDH-T189I, 201 - 204, 213 AND 276, LEAD TO 1BDM 90
REMARK 5 DISCONTINUITIES IN THE TMDH NUMBERING; HOWEVER, THESE DO 1BDM 91
REMARK 5 NOT REPRESENT BREAKS IN THE PEPTIDE CHAIN. 1BDM 92
REMARK 6 1BDM 93
REMARK 6 THE ASYMMETRIC UNIT CONTAINS TWO SUBUNITS WHICH HAVE BEEN 1BDM 94
REMARK 6 ASSIGNED CHAIN IDENTIFIERS *A* AND *B*. THEY ARE RELATED 1BDM 95
REMARK 6 BY A NON-CRYSTALLOGRAPHIC SYMMETRY AXIS WITH A ROTATION 1BDM 96
REMARK 6 ANGLE OF 180.0 DEGREES. THE TRANSFORMATION PROVIDED ON 1BDM 97
REMARK 6 THE *MTRIX* RECORDS BELOW YIELDS OPTIMAL SUPERPOSITION OF 1BDM 98
REMARK 6 SUBUNIT A UPON SUBUNIT B BASED UPON ALL ALPHA CARBON ATOMS. 1BDM 99
REMARK 7 1BDM 100
REMARK 7 WHILE THE ENZYME WAS CRYSTALLIZED AT PH 7.5 IN THE PRESENCE 1BDM 101
REMARK 7 OF THE REDUCED COENZYME NADH, THE ELECTRON DENSITY MAP WAS 1BDM 102
REMARK 7 BEST FIT BY THE MODIFIED COENZYME REFERRED TO AS NADHX. 1BDM 103
REMARK 8 1BDM 104
REMARK 8 NAX IS BETA-6-HYDROXY-1,4,5,6,-TETRAHYDRONICOTINAMIDE 1BDM 105
REMARK 8 ADENINE DINUCLEOTIDE. 1BDM 106
REMARK 9 1BDM 107
REMARK 9 CROSS REFERENCE TO SEQUENCE DATABASE 1BDM 108
REMARK 9 SWISS-PROT ENTRY NAME PDB ENTRY CHAIN NAME 1BDM 109
REMARK 9 MDH_THEFL A 1BDM 110
REMARK 10 1BDM 111
REMARK 10 RESIDUES OF CHAIN A MISSING FROM THE ATOM LIST 1BDM 112
REMARK 10 SEQUENCE NUMBER IS THAT FROM SWISS-PROT ENTRY 1BDM 113
REMARK 10 ARG 92 1BDM 114
REMARK 10 LYS 93 1BDM 115
REMARK 10 ALA 94 1BDM 116
REMARK 10 GLY 95 1BDM 117
REMARK 10 MET 96 1BDM 118
REMARK 10 GLU 97 1BDM 119
REMARK 10 ARG 98 1BDM 120
REMARK 10 ARG 99 1BDM 121
REMARK 10 ASP 100 1BDM 122
REMARK 10 LEU 101 1BDM 123
REMARK 11 1BDM 124
REMARK 11 SEQUENCE ADVISORY NOTICE 1BDM 125
REMARK 11 DIFFERENCE BETWEEN SWISS-PROT AND PDB SEQUENCE. 1BDM 126
REMARK 11 1BDM 127
REMARK 11 SWISS-PROT ENTRY NAME: MDH_THEFL 1BDM 128
REMARK 11 1BDM 129
REMARK 11 SWISS-PROT RESIDUE PDB SEQRES 1BDM 130
REMARK 11 1BDM 131
REMARK 11 NAME NUMBER NAME CHAIN SEQ/INSERT CODE 1BDM 132
REMARK 11 LYS 75 ASP A 74 1BDM 133
REMARK 11 1BDM 134
REMARK 11 CROSS REFERENCE TO SEQUENCE DATABASE 1BDM 135
REMARK 11 SWISS-PROT ENTRY NAME PDB ENTRY CHAIN NAME 1BDM 136
REMARK 11 MDH_THEFL B 1BDM 137
REMARK 11 1BDM 138
REMARK 11 SEQUENCE ADVISORY NOTICE 1BDM 139
REMARK 11 DIFFERENCE BETWEEN SWISS-PROT AND PDB SEQUENCE. 1BDM 140
REMARK 11 1BDM 141
REMARK 11 SWISS-PROT ENTRY NAME: MDH_THEFL 1BDM 142
REMARK 11 1BDM 143
REMARK 11 SWISS-PROT RESIDUE PDB SEQRES 1BDM 144
REMARK 11 1BDM 145
REMARK 11 NAME NUMBER NAME CHAIN SEQ/INSERT CODE 1BDM 146
REMARK 11 LYS 75 ASP B 74 1BDM 147
REMARK 11 1BDM 148
REMARK 11 THE SEQUENCE PRESENTED IN THE ENTRY FITS THE OBSERVED 1BDM 149
REMARK 11 DENSITY BETTER THAN THE PUBLISHED SEQUENCE. 1BDM 150
SEQRES 1 A 327 MET LYS ALA PRO VAL ARG VAL ALA VAL THR GLY ALA ALA 1BDM 151
SEQRES 2 A 327 GLY GLN ILE GLY TYR SER LEU LEU PHE ARG ILE ALA ALA 1BDM 152
SEQRES 3 A 327 GLY GLU MET LEU GLY LYS ASP GLN PRO VAL ILE LEU GLN 1BDM 153
SEQRES 4 A 327 LEU LEU GLU ILE PRO GLN ALA MET LYS ALA LEU GLU GLY 1BDM 154
SEQRES 5 A 327 VAL VAL MET GLU LEU GLU ASP CYS ALA PHE PRO LEU LEU 1BDM 155
SEQRES 6 A 327 ALA GLY LEU GLU ALA THR ASP ASP PRO ASP VAL ALA PHE 1BDM 156
SEQRES 7 A 327 LYS ASP ALA ASP TYR ALA LEU LEU VAL GLY ALA ALA PRO 1BDM 157
SEQRES 8 A 327 ARG LYS ALA GLY MET GLU ARG ARG ASP LEU LEU GLN VAL 1BDM 158
SEQRES 9 A 327 ASN GLY LYS ILE PHE THR GLU GLN GLY ARG ALA LEU ALA 1BDM 159
SEQRES 10 A 327 GLU VAL ALA LYS LYS ASP VAL LYS VAL LEU VAL VAL GLY 1BDM 160
SEQRES 11 A 327 ASN PRO ALA ASN THR ASN ALA LEU ILE ALA TYR LYS ASN 1BDM 161
SEQRES 12 A 327 ALA PRO GLY LEU ASN PRO ARG ASN PHE THR ALA MET THR 1BDM 162
SEQRES 13 A 327 ARG LEU ASP HIS ASN ARG ALA LYS ALA GLN LEU ALA LYS 1BDM 163
SEQRES 14 A 327 LYS THR GLY THR GLY VAL ASP ARG ILE ARG ARG MET THR 1BDM 164
SEQRES 15 A 327 VAL TRP GLY ASN HIS SER SER ILE MET PHE PRO ASP LEU 1BDM 165
SEQRES 16 A 327 PHE HIS ALA GLU VAL ASP GLY ARG PRO ALA LEU GLU LEU 1BDM 166
SEQRES 17 A 327 VAL ASP MET GLU TRP TYR GLU LYS VAL PHE ILE PRO THR 1BDM 167
SEQRES 18 A 327 VAL ALA GLN ARG GLY ALA ALA ILE ILE GLN ALA ARG GLY 1BDM 168
SEQRES 19 A 327 ALA SER SER ALA ALA SER ALA ALA ASN ALA ALA ILE GLU 1BDM 169
SEQRES 20 A 327 HIS ILE ARG ASP TRP ALA LEU GLY THR PRO GLU GLY ASP 1BDM 170
SEQRES 21 A 327 TRP VAL SER MET ALA VAL PRO SER GLN GLY GLU TYR GLY 1BDM 171
SEQRES 22 A 327 ILE PRO GLU GLY ILE VAL TYR SER PHE PRO VAL THR ALA 1BDM 172
SEQRES 23 A 327 LYS ASP GLY ALA TYR ARG VAL VAL GLU GLY LEU GLU ILE 1BDM 173
SEQRES 24 A 327 ASN GLU PHE ALA ARG LYS ARG MET GLU ILE THR ALA GLN 1BDM 174
SEQRES 25 A 327 GLU LEU LEU ASP GLU MET GLU GLN VAL LYS ALA LEU GLY 1BDM 175
SEQRES 26 A 327 LEU ILE 1BDM 176
SEQRES 1 B 327 MET LYS ALA PRO VAL ARG VAL ALA VAL THR GLY ALA ALA 1BDM 177
SEQRES 2 B 327 GLY GLN ILE GLY TYR SER LEU LEU PHE ARG ILE ALA ALA 1BDM 178
SEQRES 3 B 327 GLY GLU MET LEU GLY LYS ASP GLN PRO VAL ILE LEU GLN 1BDM 179
SEQRES 4 B 327 LEU LEU GLU ILE PRO GLN ALA MET LYS ALA LEU GLU GLY 1BDM 180
SEQRES 5 B 327 VAL VAL MET GLU LEU GLU ASP CYS ALA PHE PRO LEU LEU 1BDM 181
SEQRES 6 B 327 ALA GLY LEU GLU ALA THR ASP ASP PRO ASP VAL ALA PHE 1BDM 182
SEQRES 7 B 327 LYS ASP ALA ASP TYR ALA LEU LEU VAL GLY ALA ALA PRO 1BDM 183
SEQRES 8 B 327 ARG LYS ALA GLY MET GLU ARG ARG ASP LEU LEU GLN VAL 1BDM 184
SEQRES 9 B 327 ASN GLY LYS ILE PHE THR GLU GLN GLY ARG ALA LEU ALA 1BDM 185
SEQRES 10 B 327 GLU VAL ALA LYS LYS ASP VAL LYS VAL LEU VAL VAL GLY 1BDM 186
SEQRES 11 B 327 ASN PRO ALA ASN THR ASN ALA LEU ILE ALA TYR LYS ASN 1BDM 187
SEQRES 12 B 327 ALA PRO GLY LEU ASN PRO ARG ASN PHE THR ALA MET THR 1BDM 188
SEQRES 13 B 327 ARG LEU ASP HIS ASN ARG ALA LYS ALA GLN LEU ALA LYS 1BDM 189
SEQRES 14 B 327 LYS THR GLY THR GLY VAL ASP ARG ILE ARG ARG MET THR 1BDM 190
SEQRES 15 B 327 VAL TRP GLY ASN HIS SER SER ILE MET PHE PRO ASP LEU 1BDM 191
SEQRES 16 B 327 PHE HIS ALA GLU VAL ASP GLY ARG PRO ALA LEU GLU LEU 1BDM 192
SEQRES 17 B 327 VAL ASP MET GLU TRP TYR GLU LYS VAL PHE ILE PRO THR 1BDM 193
SEQRES 18 B 327 VAL ALA GLN ARG GLY ALA ALA ILE ILE GLN ALA ARG GLY 1BDM 194
SEQRES 19 B 327 ALA SER SER ALA ALA SER ALA ALA ASN ALA ALA ILE GLU 1BDM 195
SEQRES 20 B 327 HIS ILE ARG ASP TRP ALA LEU GLY THR PRO GLU GLY ASP 1BDM 196
SEQRES 21 B 327 TRP VAL SER MET ALA VAL PRO SER GLN GLY GLU TYR GLY 1BDM 197
SEQRES 22 B 327 ILE PRO GLU GLY ILE VAL TYR SER PHE PRO VAL THR ALA 1BDM 198
SEQRES 23 B 327 LYS ASP GLY ALA TYR ARG VAL VAL GLU GLY LEU GLU ILE 1BDM 199
SEQRES 24 B 327 ASN GLU PHE ALA ARG LYS ARG MET GLU ILE THR ALA GLN 1BDM 200
SEQRES 25 B 327 GLU LEU LEU ASP GLU MET GLU GLN VAL LYS ALA LEU GLY 1BDM 201
SEQRES 26 B 327 LEU ILE 1BDM 202
FTNOTE 1 1BDM 203
FTNOTE 1 CIS PROLINE - PRO A 131 1BDM 204
FTNOTE 2 1BDM 205
FTNOTE 2 CIS PROLINE - PRO B 131 1BDM 206
HET NAX A 334 45 SEE REMARK 8 1BDM 207
HET NAX B 334 45 SEE REMARK 8 1BDM 208
FORMUL 3 NAX 2(C21 H29 N7 O15 P2) 1BDM 209
FORMUL 4 HOH *202(H2 O1) 1BDM 210
HELIX 1 BA GLN A 14 ALA A 24 1 1BDM 211
HELIX 2 CA PRO A 43 GLU A 57 1 1BDM 212
HELIX 3 CPA PRO A 73 ALA A 76 1 1BDM 213
HELIX 4 DEA LEU A 101 VAL A 118 1 1BDM 214
HELIX 5 1FA ALA A 132 LYS A 141 1 1BDM 215
HELIX 6 2FA ARG A 156 THR A 170 1 1BDM 216
HELIX 7 GPA ALA A 208 VAL A 212 1 1BDM 217
HELIX 8 1GA MET A 215 ALA A 227 1 1BDM 218
HELIX 9 2GA ARG A 229 ARG A 237 1 1BDM 219
HELIX 10 3GA ALA A 242 ALA A 257 1 1BDM 220
HELIX 11 HA GLU A 306 ALA A 328 1 1BDM 221
HELIX 12 BB GLN B 14 ALA B 24 1 1BDM 222
HELIX 13 CB PRO B 43 GLU B 57 1 1BDM 223
HELIX 14 CPB PRO B 73 ALA B 76 1 1BDM 224
HELIX 15 DEB ARG B 97 VAL B 118 1 1BDM 225
HELIX 16 1FB ALA B 132 LYS B 141 1 1BDM 226
HELIX 17 2FB ARG B 156 THR B 170 1 1BDM 227
HELIX 18 GPB ALA B 208 VAL B 212 1 1BDM 228
HELIX 19 1GB MET B 215 ALA B 227 1 1BDM 229
HELIX 20 2GB ARG B 229 ARG B 237 1 1BDM 230
HELIX 21 3GB ALA B 242 LEU B 258 1 1BDM 231
HELIX 22 HB GLU B 306 ALA B 328 1 1BDM 232
SHEET 1 S1A 6 LEU A 64 THR A 70 0 1BDM 233
SHEET 2 S1A 6 VAL A 35 LEU A 40 1 1BDM 234
SHEET 3 S1A 6 VAL A 4 THR A 9 1 1BDM 235
SHEET 4 S1A 6 TYR A 82 LEU A 85 1 1BDM 236
SHEET 5 S1A 6 LYS A 124 VAL A 127 1 1BDM 237
SHEET 6 S1A 6 PHE A 151 ALA A 153 1 1BDM 238
SHEET 1 S2A 3 ILE A 177 TRP A 183 0 1BDM 239
SHEET 2 S2A 3 PHE A 191 VAL A 199 -1 1BDM 240
SHEET 3 S2A 3 ARG A 206 PRO A 207 -1 1BDM 241
SHEET 1 S3A 3 VAL A 266 PRO A 271 0 1BDM 242
SHEET 2 S3A 3 VAL A 284 LYS A 292 -1 1BDM 243
SHEET 3 S3A 3 ALA A 295 VAL A 298 -1 1BDM 244
SHEET 1 S1B 6 LEU B 64 THR B 70 0 1BDM 245
SHEET 2 S1B 6 VAL B 35 LEU B 40 1 1BDM 246
SHEET 3 S1B 6 VAL B 4 THR B 9 1 1BDM 247
SHEET 4 S1B 6 TYR B 82 LEU B 85 1 1BDM 248
SHEET 5 S1B 6 LYS B 124 VAL B 127 1 1BDM 249
SHEET 6 S1B 6 PHE B 151 ALA B 153 1 1BDM 250
SHEET 1 S2B 3 ILE B 177 TRP B 183 0 1BDM 251
SHEET 2 S2B 3 PHE B 191 VAL B 199 -1 1BDM 252
SHEET 3 S2B 3 ARG B 206 PRO B 207 -1 1BDM 253
SHEET 1 S3B 3 VAL B 266 PRO B 271 0 1BDM 254
SHEET 2 S3B 3 VAL B 284 LYS B 292 -1 1BDM 255
SHEET 3 S3B 3 ALA B 295 VAL B 298 -1 1BDM 256
TURN 1 T1 GLY A 10 GLY A 13 1BDM 257
TURN 2 T2 GLY A 30 GLN A 33 1BDM 258
TURN 3 T3 PHE A 61 LEU A 64 1BDM 259
TURN 4 T4 PHE A 77 ALA A 80 1BDM 260
TURN 5 T6 LYS A 120 VAL A 123 1BDM 261
TURN 6 T7 ALA A 143 LEU A 146 1BDM 262
TURN 7 T8 ASN A 147 ASN A 150 1BDM 263
TURN 8 T9 PRO A 148 PHE A 151 1BDM 264
TURN 9 T10 GLY A 173 ARG A 176 1BDM 265
TURN 10 T11 VAL A 174 ILE A 177 1BDM 266
TURN 11 T12 SER A 187 MET A 190 1BDM 267
TURN 12 T13 VAL A 199 ARG A 206 EIGHT RESIDUE TURN 1BDM 268
TURN 13 T14 PRO A 261 ASP A 264 1BDM 269
TURN 14 T15 GLY A 274 GLY A 278 FIVE RESIDUE TURN 1BDM 270
TURN 15 T16 GLU A 275 ILE A 279 FIVE RESIDUE TURN 1BDM 271
TURN 16 T17 PRO A 280 ILE A 283 1BDM 272
TURN 17 T18 LYS A 292 ALA A 295 1BDM 273
TURN 18 T19 LYS A 327 GLY A 330 1BDM 274
TURN 19 T20 GLY B 10 GLY B 13 1BDM 275
TURN 20 T21 GLY B 30 GLN B 33 1BDM 276
TURN 21 T22 PHE B 61 LEU B 64 1BDM 277
TURN 22 T23 PHE B 77 ALA B 80 1BDM 278
TURN 23 T24 LYS B 92 MET B 95 1BDM 279
TURN 24 T25 LYS B 120 VAL B 123 1BDM 280
TURN 25 T26 ALA B 143 LEU B 146 1BDM 281
TURN 26 T27 ASN B 147 ASN B 150 1BDM 282
TURN 27 T28 PRO B 148 PHE B 151 1BDM 283
TURN 28 T29 GLY B 173 ARG B 176 1BDM 284
TURN 29 T30 VAL B 174 ILE B 177 1BDM 285
TURN 30 T31 SER B 187 MET B 190 1BDM 286
TURN 31 T32 VAL B 199 ARG B 206 EIGHT RESIDUE TURN 1BDM 287
TURN 32 T33 PRO B 261 ASP B 264 1BDM 288
TURN 33 T34 GLY B 274 GLY B 278 FIVE RESIDUE TURN 1BDM 289
TURN 34 T35 GLU B 275 ILE B 279 FIVE RESIDUE TURN 1BDM 290
TURN 35 T36 LYS B 292 ALA B 295 1BDM 291
TURN 36 T37 LYS B 327 GLY B 330 1BDM 292
CRYST1 71.750 88.640 118.970 90.00 90.00 90.00 P 21 21 21 4 1BDM 293
ORIGX1 1.000000 0.000000 0.000000 0.00000 1BDM 294
ORIGX2 0.000000 1.000000 0.000000 0.00000 1BDM 295
ORIGX3 0.000000 0.000000 1.000000 0.00000 1BDM 296
SCALE1 0.013937 0.000000 0.000000 0.00000 1BDM 297
SCALE2 0.000000 0.011282 0.000000 0.00000 1BDM 298
SCALE3 0.000000 0.000000 0.008405 0.00000 1BDM 299
MTRIX1 1 -0.609800 0.001100 -0.792600 81.32230 1 1BDM 300
MTRIX2 1 0.006700 -1.000000 -0.006600 51.70460 1 1BDM 301
MTRIX3 1 -0.792600 -0.009400 0.609700 40.40520 1 1BDM 302
ATOM 1 N MET A 0 16.028 13.076 55.757 1.00 63.21 1BDM 303
ATOM 2 CA MET A 0 16.260 13.742 54.492 1.00 53.09 1BDM 304
ATOM 3 C MET A 0 15.055 13.528 53.639 1.00 51.55 1BDM 305
ATOM 4 O MET A 0 14.377 12.489 53.648 1.00 57.82 1BDM 306
ATOM 5 CB MET A 0 17.312 12.991 53.701 1.00 45.37 1BDM 307
ATOM 6 CG MET A 0 18.632 13.033 54.409 1.00 47.41 1BDM 308
ATOM 7 SD MET A 0 19.388 14.642 54.127 1.00 69.60 1BDM 309
ATOM 8 CE MET A 0 20.286 14.763 55.709 1.00 57.50 1BDM 310
ATOM 9 N LYS A 1 14.882 14.454 52.761 1.00 47.21 1BDM 311
ATOM 10 CA LYS A 1 13.815 14.166 51.863 1.00 43.54 1BDM 312
ATOM 11 C LYS A 1 14.099 12.989 50.921 1.00 39.13 1BDM 313
ATOM 12 O LYS A 1 15.158 12.331 50.941 1.00 45.91 1BDM 314
ATOM 13 CB LYS A 1 13.533 15.458 51.171 1.00 42.39 1BDM 315
ATOM 14 CG LYS A 1 13.750 16.601 52.162 1.00 35.55 1BDM 316
ATOM 15 CD LYS A 1 13.037 17.748 51.513 1.00 51.75 1BDM 317
ATOM 16 CE LYS A 1 12.853 19.026 52.283 1.00 67.06 1BDM 318
ATOM 17 NZ LYS A 1 11.871 19.834 51.540 1.00 73.23 1BDM 319
ATOM 18 N ALA A 2 13.087 12.607 50.188 1.00 38.14 1BDM 320
ATOM 19 CA ALA A 2 13.338 11.574 49.200 1.00 33.44 1BDM 321
ATOM 20 C ALA A 2 13.991 12.290 48.013 1.00 31.57 1BDM 322
ATOM 21 O ALA A 2 13.720 13.460 47.713 1.00 26.57 1BDM 323
ATOM 22 CB ALA A 2 11.993 11.034 48.763 1.00 44.16 1BDM 324
ATOM 23 N PRO A 3 14.764 11.589 47.256 1.00 28.38 1BDM 325
ATOM 24 CA PRO A 3 15.455 12.216 46.163 1.00 22.08 1BDM 326
ATOM 25 C PRO A 3 14.495 12.776 45.149 1.00 34.44 1BDM 327
ATOM 26 O PRO A 3 13.418 12.228 45.005 1.00 31.72 1BDM 328
ATOM 27 CB PRO A 3 16.228 11.080 45.517 1.00 17.13 1BDM 329
ATOM 28 CG PRO A 3 16.225 9.903 46.476 1.00 37.05 1BDM 330
ATOM 29 CD PRO A 3 15.037 10.153 47.375 1.00 34.14 1BDM 331
ATOM 30 N VAL A 4 14.883 13.890 44.512 1.00 26.85 1BDM 332
ATOM 31 CA VAL A 4 14.244 14.457 43.331 1.00 24.28 1BDM 333
ATOM 32 C VAL A 4 15.103 14.165 42.098 1.00 24.27 1BDM 334
ATOM 33 O VAL A 4 16.326 14.009 42.162 1.00 19.73 1BDM 335
ATOM 34 CB VAL A 4 13.859 15.931 43.403 1.00 24.03 1BDM 336
ATOM 35 CG1 VAL A 4 12.733 16.041 44.409 1.00 30.72 1BDM 337
ATOM 36 CG2 VAL A 4 15.032 16.778 43.837 1.00 24.33 1BDM 338
ATOM 37 N ARG A 5 14.444 13.930 40.966 1.00 24.23 1BDM 339
ATOM 38 CA ARG A 5 15.165 13.649 39.732 1.00 15.16 1BDM 340
ATOM 39 C ARG A 5 15.267 14.954 38.989 1.00 16.88 1BDM 341
ATOM 40 O ARG A 5 14.276 15.634 38.773 1.00 23.97 1BDM 342
ATOM 41 CB ARG A 5 14.486 12.638 38.851 1.00 23.27 1BDM 343
ATOM 42 CG ARG A 5 14.773 11.252 39.352 1.00 22.14 1BDM 344
ATOM 43 CD ARG A 5 13.710 10.259 38.870 1.00 28.32 1BDM 345
ATOM 44 NE ARG A 5 13.609 9.123 39.785 1.00 33.78 1BDM 346
ATOM 45 CZ ARG A 5 14.411 8.070 39.598 1.00 42.12 1BDM 347
ATOM 46 NH1 ARG A 5 15.215 8.083 38.548 1.00 41.57 1BDM 348
ATOM 47 NH2 ARG A 5 14.444 7.010 40.385 1.00 40.88 1BDM 349
ATOM 48 N VAL A 6 16.479 15.346 38.607 1.00 17.21 1BDM 350
ATOM 49 CA VAL A 6 16.617 16.619 37.943 1.00 16.27 1BDM 351
ATOM 50 C VAL A 6 17.152 16.302 36.562 1.00 25.00 1BDM 352
ATOM 51 O VAL A 6 18.227 15.736 36.466 1.00 16.60 1BDM 353
ATOM 52 CB VAL A 6 17.612 17.525 38.695 1.00 20.39 1BDM 354
ATOM 53 CG1 VAL A 6 17.899 18.794 37.908 1.00 18.68 1BDM 355
ATOM 54 CG2 VAL A 6 17.140 17.929 40.111 1.00 19.04 1BDM 356
ATOM 55 N ALA A 7 16.427 16.621 35.486 1.00 20.12 1BDM 357
ATOM 56 CA ALA A 7 17.007 16.313 34.180 1.00 14.34 1BDM 358
ATOM 57 C ALA A 7 17.683 17.553 33.627 1.00 12.00 1BDM 359
ATOM 58 O ALA A 7 17.158 18.662 33.761 1.00 15.46 1BDM 360
ATOM 59 CB ALA A 7 15.890 15.899 33.201 1.00 20.98 1BDM 361
ATOM 60 N VAL A 8 18.833 17.402 32.957 1.00 20.82 1BDM 362
ATOM 61 CA VAL A 8 19.485 18.611 32.444 1.00 14.11 1BDM 363
ATOM 62 C VAL A 8 19.923 18.272 31.019 1.00 19.43 1BDM 364
ATOM 63 O VAL A 8 20.593 17.247 30.842 1.00 20.96 1BDM 365
ATOM 64 CB VAL A 8 20.825 18.912 33.139 1.00 12.90 1BDM 366
ATOM 65 CG1 VAL A 8 21.391 20.200 32.538 1.00 13.24 1BDM 367
ATOM 66 CG2 VAL A 8 20.649 19.066 34.668 1.00 13.81 1BDM 368
ATOM 67 N THR A 9 19.511 19.085 30.036 1.00 18.15 1BDM 369
ATOM 68 CA THR A 9 19.946 18.811 28.662 1.00 20.93 1BDM 370
ATOM 69 C THR A 9 21.180 19.647 28.359 1.00 27.71 1BDM 371
ATOM 70 O THR A 9 21.439 20.596 29.107 1.00 19.40 1BDM 372
ATOM 71 CB THR A 9 18.815 19.134 27.672 1.00 12.58 1BDM 373
ATOM 72 OG1 THR A 9 18.678 20.543 27.582 1.00 15.08 1BDM 374
ATOM 73 CG2 THR A 9 17.513 18.461 28.116 1.00 17.58 1BDM 375
ATOM 74 N GLY A 10 21.929 19.366 27.271 1.00 15.63 1BDM 376
ATOM 75 CA GLY A 10 23.095 20.215 26.952 1.00 17.03 1BDM 377
ATOM 76 C GLY A 10 24.209 20.126 28.030 1.00 12.24 1BDM 378
ATOM 77 O GLY A 10 25.048 21.040 28.218 1.00 19.25 1BDM 379
ATOM 78 N ALA A 11 24.171 18.983 28.712 1.00 18.31 1BDM 380
ATOM 79 CA ALA A 11 24.989 18.699 29.878 1.00 27.75 1BDM 381
ATOM 80 C ALA A 11 26.483 18.667 29.637 1.00 33.19 1BDM 382
ATOM 81 O ALA A 11 27.272 18.800 30.561 1.00 25.54 1BDM 383
ATOM 82 CB ALA A 11 24.509 17.486 30.655 1.00 14.38 1BDM 384
ATOM 83 N ALA A 12 26.909 18.458 28.415 1.00 22.39 1BDM 385
ATOM 84 CA ALA A 12 28.325 18.438 28.176 1.00 17.73 1BDM 386
ATOM 85 C ALA A 12 28.816 19.783 27.677 1.00 22.50 1BDM 387
ATOM 86 O ALA A 12 29.988 19.895 27.363 1.00 24.69 1BDM 388
ATOM 87 CB ALA A 12 28.603 17.343 27.171 1.00 18.71 1BDM 389
ATOM 88 N GLY A 13 27.951 20.794 27.593 1.00 16.24 1BDM 390
ATOM 89 CA GLY A 13 28.401 22.120 27.213 1.00 12.71 1BDM 391
ATOM 90 C GLY A 13 28.931 23.019 28.308 1.00 16.91 1BDM 392
ATOM 91 O GLY A 13 29.183 22.544 29.438 1.00 20.47 1BDM 393
ATOM 92 N GLN A 14 29.121 24.300 27.961 1.00 16.99 1BDM 394
ATOM 93 CA GLN A 14 29.783 25.257 28.826 1.00 14.58 1BDM 395
ATOM 94 C GLN A 14 28.951 25.566 30.065 1.00 31.82 1BDM 396
ATOM 95 O GLN A 14 29.467 25.512 31.185 1.00 18.35 1BDM 397
ATOM 96 CB GLN A 14 30.173 26.577 28.146 1.00 22.15 1BDM 398
ATOM 97 CG GLN A 14 31.090 26.444 26.901 1.00 36.62 1BDM 399
ATOM 98 CD GLN A 14 30.741 27.510 25.825 1.00 62.75 1BDM 400
ATOM 99 OE1 GLN A 14 31.474 28.504 25.636 1.00 65.02 1BDM 401
ATOM 100 NE2 GLN A 14 29.604 27.347 25.115 1.00 66.62 1BDM 402
ATOM 101 N ILE A 15 27.673 25.903 29.865 1.00 16.06 1BDM 403
ATOM 102 CA ILE A 15 26.789 26.169 31.022 1.00 16.38 1BDM 404
ATOM 103 C ILE A 15 26.687 24.914 31.856 1.00 18.51 1BDM 405
ATOM 104 O ILE A 15 26.827 24.956 33.053 1.00 19.73 1BDM 406
ATOM 105 CB ILE A 15 25.378 26.709 30.643 1.00 13.89 1BDM 407
ATOM 106 CG1 ILE A 15 25.522 28.154 30.132 1.00 16.97 1BDM 408
ATOM 107 CG2 ILE A 15 24.406 26.718 31.841 1.00 10.50 1BDM 409
ATOM 108 CD1 ILE A 15 24.302 28.678 29.410 1.00 22.69 1BDM 410
ATOM 109 N GLY A 16 26.521 23.765 31.211 1.00 12.23 1BDM 411
ATOM 110 CA GLY A 16 26.366 22.499 31.863 1.00 14.46 1BDM 412
ATOM 111 C GLY A 16 27.538 22.253 32.768 1.00 20.58 1BDM 413
ATOM 112 O GLY A 16 27.402 21.768 33.874 1.00 16.57 1BDM 414
ATOM 113 N TYR A 17 28.717 22.489 32.271 1.00 16.13 1BDM 415
ATOM 114 CA TYR A 17 29.907 22.248 33.132 1.00 17.14 1BDM 416
ATOM 115 C TYR A 17 29.955 23.154 34.362 1.00 28.80 1BDM 417
ATOM 116 O TYR A 17 30.558 22.778 35.346 1.00 15.49 1BDM 418
ATOM 117 CB TYR A 17 31.188 22.431 32.318 1.00 10.68 1BDM 419
ATOM 118 CG TYR A 17 32.415 21.850 32.960 1.00 12.61 1BDM 420
ATOM 119 CD1 TYR A 17 32.666 20.467 32.992 1.00 15.10 1BDM 421
ATOM 120 CD2 TYR A 17 33.487 22.709 33.363 1.00 14.96 1BDM 422
ATOM 121 CE1 TYR A 17 33.808 19.919 33.563 1.00 14.59 1BDM 423
ATOM 122 CE2 TYR A 17 34.668 22.138 33.857 1.00 12.16 1BDM 424
ATOM 123 CZ TYR A 17 34.793 20.774 33.959 1.00 10.52 1BDM 425
ATOM 124 OH TYR A 17 35.960 20.225 34.547 1.00 17.27 1BDM 426
ATOM 125 N SER A 18 29.411 24.364 34.338 1.00 12.10 1BDM 427
ATOM 126 CA SER A 18 29.454 25.220 35.541 1.00 21.50 1BDM 428
ATOM 127 C SER A 18 28.204 24.997 36.380 1.00 20.24 1BDM 429
ATOM 128 O SER A 18 28.039 25.609 37.415 1.00 32.60 1BDM 430
ATOM 129 CB SER A 18 29.346 26.689 35.162 1.00 24.85 1BDM 431
ATOM 130 OG SER A 18 30.507 27.173 34.524 1.00 26.01 1BDM 432
ATOM 131 N LEU A 19 27.219 24.231 35.877 1.00 21.22 1BDM 433
ATOM 132 CA LEU A 19 25.900 24.103 36.514 1.00 12.72 1BDM 434
ATOM 133 C LEU A 19 25.826 22.858 37.408 1.00 14.45 1BDM 435
ATOM 134 O LEU A 19 25.324 22.871 38.557 1.00 14.36 1BDM 436
ATOM 135 CB LEU A 19 24.862 24.012 35.357 1.00 15.16 1BDM 437
ATOM 136 CG LEU A 19 23.382 23.864 35.738 1.00 18.44 1BDM 438
ATOM 137 CD1 LEU A 19 22.923 25.081 36.553 1.00 15.69 1BDM 439
ATOM 138 CD2 LEU A 19 22.556 23.793 34.459 1.00 23.83 1BDM 440
ATOM 139 N LEU A 20 26.314 21.754 36.872 1.00 11.45 1BDM 441
ATOM 140 CA LEU A 20 26.052 20.465 37.430 1.00 10.07 1BDM 442
ATOM 141 C LEU A 20 26.667 20.318 38.787 1.00 18.38 1BDM 443
ATOM 142 O LEU A 20 26.094 19.634 39.618 1.00 16.78 1BDM 444
ATOM 143 CB LEU A 20 26.475 19.272 36.547 1.00 14.39 1BDM 445
ATOM 144 CG LEU A 20 25.908 19.324 35.140 1.00 18.94 1BDM 446
ATOM 145 CD1 LEU A 20 26.393 18.086 34.383 1.00 15.17 1BDM 447
ATOM 146 CD2 LEU A 20 24.409 19.233 35.337 1.00 19.57 1BDM 448
ATOM 147 N PHE A 21 27.881 20.756 38.988 1.00 14.38 1BDM 449
ATOM 148 CA PHE A 21 28.522 20.494 40.287 1.00 7.40 1BDM 450
ATOM 149 C PHE A 21 27.843 21.331 41.414 1.00 9.71 1BDM 451
ATOM 150 O PHE A 21 27.746 20.840 42.561 1.00 21.80 1BDM 452
ATOM 151 CB PHE A 21 29.995 20.944 40.225 1.00 13.17 1BDM 453
ATOM 152 CG PHE A 21 30.655 20.133 39.113 1.00 12.74 1BDM 454
ATOM 153 CD1 PHE A 21 30.634 20.601 37.796 1.00 13.02 1BDM 455
ATOM 154 CD2 PHE A 21 31.258 18.926 39.416 1.00 12.01 1BDM 456
ATOM 155 CE1 PHE A 21 31.146 19.778 36.797 1.00 13.24 1BDM 457
ATOM 156 CE2 PHE A 21 31.814 18.116 38.433 1.00 18.19 1BDM 458
ATOM 157 CZ PHE A 21 31.763 18.566 37.119 1.00 15.27 1BDM 459
ATOM 158 N ARG A 22 27.391 22.535 41.133 1.00 13.23 1BDM 460
ATOM 159 CA ARG A 22 26.661 23.277 42.134 1.00 10.94 1BDM 461
ATOM 160 C ARG A 22 25.302 22.671 42.470 1.00 19.59 1BDM 462
ATOM 161 O ARG A 22 24.850 22.728 43.601 1.00 15.84 1BDM 463
ATOM 162 CB ARG A 22 26.533 24.750 41.790 1.00 9.43 1BDM 464
ATOM 163 CG ARG A 22 27.877 25.455 41.932 1.00 12.15 1BDM 465
ATOM 164 CD ARG A 22 27.859 26.900 41.569 1.00 14.33 1BDM 466
ATOM 165 NE ARG A 22 27.140 27.617 42.588 1.00 17.13 1BDM 467
ATOM 166 CZ ARG A 22 26.500 28.784 42.464 1.00 22.04 1BDM 468
ATOM 167 NH1 ARG A 22 26.537 29.408 41.287 1.00 19.35 1BDM 469
ATOM 168 NH2 ARG A 22 25.811 29.327 43.470 1.00 24.08 1BDM 470
ATOM 169 N ILE A 23 24.623 22.058 41.496 1.00 15.90 1BDM 471
ATOM 170 CA ILE A 23 23.388 21.374 41.777 1.00 11.81 1BDM 472
ATOM 171 C ILE A 23 23.629 20.171 42.690 1.00 13.51 1BDM 473
ATOM 172 O ILE A 23 22.913 19.906 43.650 1.00 17.43 1BDM 474
ATOM 173 CB ILE A 23 22.700 20.878 40.494 1.00 18.05 1BDM 475
ATOM 174 CG1 ILE A 23 22.144 22.068 39.716 1.00 17.05 1BDM 476
ATOM 175 CG2 ILE A 23 21.557 19.960 40.914 1.00 13.59 1BDM 477
ATOM 176 CD1 ILE A 23 21.501 21.629 38.385 1.00 18.78 1BDM 478
ATOM 177 N ALA A 24 24.614 19.371 42.317 1.00 11.73 1BDM 479
ATOM 178 CA ALA A 24 24.948 18.201 43.088 1.00 13.43 1BDM 480
ATOM 179 C ALA A 24 25.445 18.507 44.525 1.00 16.81 1BDM 481
ATOM 180 O ALA A 24 25.407 17.642 45.390 1.00 15.33 1BDM 482
ATOM 181 CB ALA A 24 25.960 17.349 42.346 1.00 12.79 1BDM 483
ATOM 182 N ALA A 25 25.935 19.680 44.751 1.00 15.36 1BDM 484
ATOM 183 CA ALA A 25 26.442 20.130 46.011 1.00 19.55 1BDM 485
ATOM 184 C ALA A 25 25.304 20.578 46.893 1.00 20.87 1BDM 486
ATOM 185 O ALA A 25 25.580 20.969 48.011 1.00 18.13 1BDM 487
ATOM 186 CB ALA A 25 27.458 21.253 45.856 1.00 15.40 1BDM 488
ATOM 187 N GLY A 26 24.064 20.616 46.401 1.00 13.48 1BDM 489
ATOM 188 CA GLY A 26 22.893 21.047 47.202 1.00 16.66 1BDM 490
ATOM 189 C GLY A 26 22.588 22.537 47.181 1.00 22.68 1BDM 491
ATOM 190 O GLY A 26 21.748 23.004 47.955 1.00 19.73 1BDM 492
ATOM 191 N GLU A 27 23.146 23.281 46.190 1.00 12.68 1BDM 493
ATOM 192 CA GLU A 27 22.930 24.727 46.072 1.00 13.95 1BDM 494
ATOM 193 C GLU A 27 21.597 25.111 45.434 1.00 13.83 1BDM 495
ATOM 194 O GLU A 27 21.149 26.248 45.520 1.00 18.11 1BDM 496
ATOM 195 CB 1GLU A 27 24.024 25.424 45.148 0.50 10.57 1BDM 497
ATOM 196 CB 2GLU A 27 24.059 25.346 45.149 0.50 10.57 1BDM 498
ATOM 197 CG 1GLU A 27 25.362 25.499 45.817 0.50 10.36 1BDM 499
ATOM 198 CG 2GLU A 27 25.414 25.406 45.802 0.50 10.36 1BDM 500
ATOM 199 CD 1GLU A 27 26.122 26.823 45.623 0.50 27.92 1BDM 501
ATOM 200 CD 2GLU A 27 25.548 26.509 46.860 0.50 27.92 1BDM 502
ATOM 201 OE11GLU A 27 25.516 27.902 45.783 0.50 25.43 1BDM 503
ATOM 202 OE12GLU A 27 25.843 27.662 46.507 0.50 17.06 1BDM 504
ATOM 203 OE21GLU A 27 27.329 26.801 45.361 0.50 17.06 1BDM 505
ATOM 204 OE22GLU A 27 25.368 26.214 48.045 0.50 25.43 1BDM 506
ATOM 205 N MET A 28 20.981 24.171 44.716 1.00 14.90 1BDM 507
ATOM 206 CA MET A 28 19.787 24.566 44.021 1.00 15.71 1BDM 508
ATOM 207 C MET A 28 18.550 24.324 44.878 1.00 16.27 1BDM 509
ATOM 208 O MET A 28 17.696 25.183 44.995 1.00 19.83 1BDM 510
ATOM 209 CB MET A 28 19.654 23.861 42.648 1.00 9.58 1BDM 511
ATOM 210 CG MET A 28 18.538 24.479 41.790 1.00 16.79 1BDM 512
ATOM 211 SD MET A 28 18.580 23.754 40.137 1.00 23.23 1BDM 513
ATOM 212 CE MET A 28 18.108 22.064 40.402 1.00 17.89 1BDM 514
ATOM 213 N LEU A 29 18.445 23.135 45.450 1.00 17.93 1BDM 515
ATOM 214 CA LEU A 29 17.243 22.734 46.200 1.00 16.06 1BDM 516
ATOM 215 C LEU A 29 17.476 22.601 47.711 1.00 19.80 1BDM 517
ATOM 216 O LEU A 29 16.586 22.202 48.460 1.00 22.03 1BDM 518
ATOM 217 CB LEU A 29 16.724 21.395 45.653 1.00 17.93 1BDM 519
ATOM 218 CG LEU A 29 16.313 21.546 44.186 1.00 18.44 1BDM 520
ATOM 219 CD1 LEU A 29 15.921 20.238 43.554 1.00 17.86 1BDM 521
ATOM 220 CD2 LEU A 29 15.229 22.600 43.984 1.00 16.73 1BDM 522
ATOM 221 N GLY A 30 18.687 22.829 48.132 1.00 26.31 1BDM 523
ATOM 222 CA GLY A 30 18.989 22.750 49.548 1.00 21.48 1BDM 524
ATOM 223 C GLY A 30 19.851 21.592 49.955 1.00 17.22 1BDM 525
ATOM 224 O GLY A 30 19.778 20.494 49.451 1.00 16.97 1BDM 526
ATOM 225 N LYS A 31 20.472 21.820 51.095 1.00 21.78 1BDM 527
ATOM 226 CA LYS A 31 21.426 20.882 51.577 1.00 25.16 1BDM 528
ATOM 227 C LYS A 31 20.796 19.646 52.163 1.00 24.72 1BDM 529
ATOM 228 O LYS A 31 21.522 18.764 52.546 1.00 23.04 1BDM 530
ATOM 229 CB LYS A 31 22.368 21.573 52.550 1.00 27.86 1BDM 531
ATOM 230 CG LYS A 31 23.805 21.511 52.073 1.00 38.23 1BDM 532
ATOM 231 CD LYS A 31 24.280 22.811 51.465 1.00 43.19 1BDM 533
ATOM 232 CE LYS A 31 25.574 22.689 50.677 1.00 58.38 1BDM 534
ATOM 233 NZ LYS A 31 25.684 23.702 49.624 1.00 49.91 1BDM 535
ATOM 234 N ASP A 32 19.469 19.527 52.278 1.00 20.13 1BDM 536
ATOM 235 CA ASP A 32 18.917 18.281 52.812 1.00 22.25 1BDM 537
ATOM 236 C ASP A 32 18.130 17.564 51.737 1.00 30.71 1BDM 538
ATOM 237 O ASP A 32 17.356 16.639 51.985 1.00 29.52 1BDM 539
ATOM 238 CB ASP A 32 18.001 18.554 54.014 1.00 29.79 1BDM 540
ATOM 239 CG ASP A 32 16.918 19.562 53.751 1.00 44.65 1BDM 541
ATOM 240 OD1 ASP A 32 17.185 20.370 52.752 1.00 57.29 1BDM 542
ATOM 241 OD2 ASP A 32 15.905 19.642 54.427 1.00 56.48 1BDM 543
ATOM 242 N GLN A 33 18.276 18.055 50.500 1.00 19.84 1BDM 544
ATOM 243 CA GLN A 33 17.498 17.435 49.441 1.00 20.47 1BDM 545
ATOM 244 C GLN A 33 18.410 16.663 48.505 1.00 22.51 1BDM 546
ATOM 245 O GLN A 33 19.158 17.201 47.744 1.00 22.31 1BDM 547
ATOM 246 CB GLN A 33 16.665 18.539 48.734 1.00 23.42 1BDM 548
ATOM 247 CG GLN A 33 16.051 18.019 47.416 1.00 15.21 1BDM 549
ATOM 248 CD GLN A 33 14.986 17.063 47.808 1.00 24.42 1BDM 550
ATOM 249 OE1 GLN A 33 13.967 17.492 48.360 1.00 27.15 1BDM 551
ATOM 250 NE2 GLN A 33 15.275 15.800 47.616 1.00 19.04 1BDM 552
ATOM 251 N PRO A 34 18.480 15.365 48.584 1.00 20.33 1BDM 553
ATOM 252 CA PRO A 34 19.328 14.645 47.644 1.00 17.74 1BDM 554
ATOM 253 C PRO A 34 18.732 14.665 46.234 1.00 21.96 1BDM 555
ATOM 254 O PRO A 34 17.532 14.832 46.040 1.00 17.91 1BDM 556
ATOM 255 CB PRO A 34 19.298 13.195 48.093 1.00 18.76 1BDM 557
ATOM 256 CG PRO A 34 18.470 13.175 49.388 1.00 21.44 1BDM 558
ATOM 257 CD PRO A 34 17.738 14.492 49.553 1.00 24.26 1BDM 559
ATOM 258 N VAL A 35 19.581 14.540 45.227 1.00 18.26 1BDM 560
ATOM 259 CA VAL A 35 19.168 14.757 43.836 1.00 21.09 1BDM 561
ATOM 260 C VAL A 35 19.668 13.631 42.996 1.00 33.34 1BDM 562
ATOM 261 O VAL A 35 20.729 13.045 43.286 1.00 22.70 1BDM 563
ATOM 262 CB VAL A 35 19.711 16.046 43.190 1.00 15.69 1BDM 564
ATOM 263 CG1 VAL A 35 19.327 17.293 43.960 1.00 17.23 1BDM 565
ATOM 264 CG2 VAL A 35 21.207 15.959 43.153 1.00 21.51 1BDM 566
ATOM 265 N ILE A 36 18.850 13.307 42.001 1.00 20.94 1BDM 567
ATOM 266 CA ILE A 36 19.239 12.301 41.027 1.00 18.17 1BDM 568
ATOM 267 C ILE A 36 19.460 13.055 39.729 1.00 28.97 1BDM 569
ATOM 268 O ILE A 36 18.517 13.674 39.286 1.00 19.27 1BDM 570
ATOM 269 CB ILE A 36 18.180 11.186 40.869 1.00 19.88 1BDM 571
ATOM 270 CG1 ILE A 36 18.155 10.312 42.117 1.00 25.24 1BDM 572
ATOM 271 CG2 ILE A 36 18.571 10.216 39.747 1.00 21.10 1BDM 573
ATOM 272 CD1 ILE A 36 16.859 9.534 42.153 1.00 33.20 1BDM 574
ATOM 273 N LEU A 37 20.669 13.047 39.166 1.00 18.52 1BDM 575
ATOM 274 CA LEU A 37 20.906 13.761 37.912 1.00 18.31 1BDM 576
ATOM 275 C LEU A 37 20.783 12.820 36.708 1.00 19.98 1BDM 577
ATOM 276 O LEU A 37 21.403 11.750 36.673 1.00 21.58 1BDM 578
ATOM 277 CB LEU A 37 22.284 14.478 37.810 1.00 12.45 1BDM 579
ATOM 278 CG LEU A 37 22.554 15.661 38.750 1.00 15.09 1BDM 580
ATOM 279 CD1 LEU A 37 24.040 16.046 38.600 1.00 16.15 1BDM 581
ATOM 280 CD2 LEU A 37 21.733 16.893 38.434 1.00 18.93 1BDM 582
ATOM 281 N GLN A 38 19.896 13.255 35.793 1.00 23.78 1BDM 583
ATOM 282 CA GLN A 38 19.536 12.606 34.520 1.00 25.95 1BDM 584
ATOM 283 C GLN A 38 19.919 13.555 33.393 1.00 16.05 1BDM 585
ATOM 284 O GLN A 38 19.342 14.660 33.194 1.00 17.08 1BDM 586
ATOM 285 CB GLN A 38 18.044 12.227 34.506 1.00 17.24 1BDM 587
ATOM 286 CG GLN A 38 17.788 11.200 35.626 1.00 21.53 1BDM 588
ATOM 287 CD GLN A 38 16.349 10.831 35.877 1.00 35.90 1BDM 589
ATOM 288 OE1 GLN A 38 16.085 10.011 36.761 1.00 27.70 1BDM 590
ATOM 289 NE2 GLN A 38 15.419 11.395 35.102 1.00 24.90 1BDM 591
ATOM 290 N LEU A 39 21.063 13.201 32.825 1.00 14.02 1BDM 592
ATOM 291 CA LEU A 39 21.708 14.075 31.838 1.00 21.49 1BDM 593
ATOM 292 C LEU A 39 21.520 13.636 30.372 1.00 15.31 1BDM 594
ATOM 293 O LEU A 39 21.712 12.445 30.023 1.00 22.79 1BDM 595
ATOM 294 CB LEU A 39 23.213 14.171 32.140 1.00 21.68 1BDM 596
ATOM 295 CG LEU A 39 23.560 14.406 33.637 1.00 21.60 1BDM 597
ATOM 296 CD1 LEU A 39 25.069 14.456 33.669 1.00 22.20 1BDM 598
ATOM 297 CD2 LEU A 39 23.045 15.754 34.075 1.00 9.83 1BDM 599
ATOM 298 N LEU A 40 21.184 14.624 29.523 1.00 21.48 1BDM 600
ATOM 299 CA LEU A 40 20.839 14.310 28.127 1.00 17.63 1BDM 601
ATOM 300 C LEU A 40 21.792 15.046 27.217 1.00 20.11 1BDM 602
ATOM 301 O LEU A 40 22.003 16.218 27.429 1.00 17.93 1BDM 603
ATOM 302 CB LEU A 40 19.430 14.812 27.829 1.00 21.71 1BDM 604
ATOM 303 CG LEU A 40 19.063 14.600 26.338 1.00 26.45 1BDM 605
ATOM 304 CD1 LEU A 40 18.854 13.109 26.138 1.00 27.26 1BDM 606
ATOM 305 CD2 LEU A 40 17.724 15.298 26.047 1.00 17.24 1BDM 607
ATOM 306 N GLU A 41 22.423 14.382 26.256 1.00 20.96 1BDM 608
ATOM 307 CA GLU A 41 23.251 15.059 25.270 1.00 21.24 1BDM 609
ATOM 308 C GLU A 41 22.901 14.540 23.850 1.00 36.44 1BDM 610
ATOM 309 O GLU A 41 22.142 13.594 23.683 1.00 26.33 1BDM 611
ATOM 310 CB GLU A 41 24.750 14.828 25.555 1.00 15.64 1BDM 612
ATOM 311 CG GLU A 41 25.455 16.084 26.140 1.00 16.87 1BDM 613
ATOM 312 CD GLU A 41 25.409 17.261 25.218 1.00 28.65 1BDM 614
ATOM 313 OE1 GLU A 41 25.094 17.159 24.049 1.00 30.68 1BDM 615
ATOM 314 OE2 GLU A 41 25.774 18.393 25.778 1.00 24.12 1BDM 616
ATOM 315 N ILE A 42 23.451 15.131 22.792 1.00 27.61 1BDM 617
ATOM 316 CA ILE A 42 23.316 14.525 21.489 1.00 33.53 1BDM 618
ATOM 317 C ILE A 42 24.347 13.402 21.345 1.00 35.43 1BDM 619
ATOM 318 O ILE A 42 25.355 13.417 22.028 1.00 29.92 1BDM 620
ATOM 319 CB ILE A 42 23.419 15.514 20.359 1.00 23.56 1BDM 621
ATOM 320 CG1 ILE A 42 24.724 16.229 20.358 1.00 27.19 1BDM 622
ATOM 321 CG2 ILE A 42 22.338 16.549 20.438 1.00 24.47 1BDM 623
ATOM 322 CD1 ILE A 42 24.595 17.431 19.431 1.00 32.41 1BDM 624
ATOM 323 N PRO A 43 24.137 12.395 20.492 1.00 30.88 1BDM 625
ATOM 324 CA PRO A 43 25.032 11.264 20.495 1.00 28.14 1BDM 626
ATOM 325 C PRO A 43 26.460 11.636 20.204 1.00 30.06 1BDM 627
ATOM 326 O PRO A 43 27.416 11.026 20.661 1.00 32.48 1BDM 628
ATOM 327 CB PRO A 43 24.496 10.305 19.452 1.00 41.03 1BDM 629
ATOM 328 CG PRO A 43 23.073 10.735 19.214 1.00 27.73 1BDM 630
ATOM 329 CD PRO A 43 23.043 12.208 19.503 1.00 25.13 1BDM 631
ATOM 330 N GLN A 44 26.676 12.724 19.514 1.00 27.38 1BDM 632
ATOM 331 CA GLN A 44 28.078 13.033 19.272 1.00 38.80 1BDM 633
ATOM 332 C GLN A 44 28.837 13.661 20.442 1.00 36.14 1BDM 634
ATOM 333 O GLN A 44 30.002 14.010 20.283 1.00 30.95 1BDM 635
ATOM 334 CB GLN A 44 28.236 13.874 17.989 1.00 46.52 1BDM 636
ATOM 335 CG GLN A 44 27.992 13.042 16.695 1.00 65.30 1BDM 637
ATOM 336 CD GLN A 44 28.797 11.743 16.536 1.00 77.18 1BDM 638
ATOM 337 OE1 GLN A 44 29.395 11.489 15.468 1.00 85.15 1BDM 639
ATOM 338 NE2 GLN A 44 28.773 10.880 17.558 1.00 73.92 1BDM 640
ATOM 339 N ALA A 45 28.136 13.997 21.527 1.00 32.01 1BDM 641
ATOM 340 CA ALA A 45 28.765 14.593 22.712 1.00 25.34 1BDM 642
ATOM 341 C ALA A 45 28.710 13.645 23.900 1.00 26.21 1BDM 643
ATOM 342 O ALA A 45 29.141 13.984 25.004 1.00 30.77 1BDM 644
ATOM 343 CB ALA A 45 28.207 15.964 23.053 1.00 25.86 1BDM 645
ATOM 344 N MET A 46 28.309 12.423 23.617 1.00 17.16 1BDM 646
ATOM 345 CA MET A 46 28.247 11.379 24.606 1.00 24.97 1BDM 647
ATOM 346 C MET A 46 29.559 11.026 25.235 1.00 35.92 1BDM 648
ATOM 347 O MET A 46 29.580 10.816 26.441 1.00 30.24 1BDM 649
ATOM 348 CB MET A 46 27.469 10.119 24.241 1.00 22.93 1BDM 650
ATOM 349 CG MET A 46 26.046 10.529 23.912 1.00 34.17 1BDM 651
ATOM 350 SD MET A 46 25.090 10.880 25.406 1.00 38.01 1BDM 652
ATOM 351 CE MET A 46 25.619 9.534 26.490 1.00 22.75 1BDM 653
ATOM 352 N LYS A 47 30.622 10.965 24.454 1.00 27.40 1BDM 654
ATOM 353 CA LYS A 47 31.930 10.744 25.030 1.00 35.88 1BDM 655
ATOM 354 C LYS A 47 32.343 11.830 26.037 1.00 34.65 1BDM 656
ATOM 355 O LYS A 47 32.815 11.548 27.138 1.00 27.39 1BDM 657
ATOM 356 CB LYS A 47 33.023 10.538 24.009 1.00 25.50 1BDM 658
ATOM 357 CG LYS A 47 34.047 9.598 24.629 1.00 49.87 1BDM 659
ATOM 358 CD LYS A 47 34.884 8.849 23.602 1.00 68.26 1BDM 660
ATOM 359 CE LYS A 47 36.028 9.685 23.035 1.00 70.67 1BDM 661
ATOM 360 NZ LYS A 47 37.366 9.194 23.428 1.00 71.62 1BDM 662
ATOM 361 N ALA A 48 32.171 13.083 25.648 1.00 21.35 1BDM 663
ATOM 362 CA ALA A 48 32.470 14.176 26.532 1.00 21.11 1BDM 664
ATOM 363 C ALA A 48 31.602 14.028 27.779 1.00 38.13 1BDM 665
ATOM 364 O ALA A 48 32.042 14.150 28.896 1.00 26.59 1BDM 666
ATOM 365 CB ALA A 48 32.123 15.469 25.846 1.00 17.56 1BDM 667
ATOM 366 N LEU A 49 30.339 13.728 27.573 1.00 21.66 1BDM 668
ATOM 367 CA LEU A 49 29.405 13.579 28.671 1.00 18.22 1BDM 669
ATOM 368 C LEU A 49 29.892 12.532 29.662 1.00 25.69 1BDM 670
ATOM 369 O LEU A 49 29.732 12.694 30.872 1.00 25.83 1BDM 671
ATOM 370 CB LEU A 49 27.937 13.421 28.187 1.00 14.90 1BDM 672
ATOM 371 CG LEU A 49 26.902 13.349 29.287 1.00 17.53 1BDM 673
ATOM 372 CD1 LEU A 49 26.975 14.662 30.086 1.00 19.28 1BDM 674
ATOM 373 CD2 LEU A 49 25.479 13.122 28.765 1.00 20.78 1BDM 675
ATOM 374 N GLU A 50 30.443 11.424 29.191 1.00 19.99 1BDM 676
ATOM 375 CA GLU A 50 30.904 10.414 30.130 1.00 22.37 1BDM 677
ATOM 376 C GLU A 50 32.048 11.015 30.962 1.00 30.87 1BDM 678
ATOM 377 O GLU A 50 32.342 10.579 32.085 1.00 21.81 1BDM 679
ATOM 378 CB GLU A 50 31.488 9.104 29.511 1.00 29.07 1BDM 680
ATOM 379 CG GLU A 50 30.872 8.493 28.224 1.00 61.56 1BDM 681
ATOM 380 CD GLU A 50 29.431 7.995 28.278 1.00 84.78 1BDM 682
ATOM 381 OE1 GLU A 50 29.322 6.788 28.802 1.00 83.14 1BDM 683
ATOM 382 OE2 GLU A 50 28.461 8.621 27.830 1.00 74.19 1BDM 684
ATOM 383 N GLY A 51 32.785 11.960 30.383 1.00 17.92 1BDM 685
ATOM 384 CA GLY A 51 33.894 12.583 31.123 1.00 24.46 1BDM 686
ATOM 385 C GLY A 51 33.375 13.434 32.308 1.00 23.25 1BDM 687
ATOM 386 O GLY A 51 33.979 13.473 33.357 1.00 18.69 1BDM 688
ATOM 387 N VAL A 52 32.256 14.146 32.109 1.00 17.54 1BDM 689
ATOM 388 CA VAL A 52 31.561 14.998 33.062 1.00 17.35 1BDM 690
ATOM 389 C VAL A 52 31.010 14.089 34.154 1.00 27.22 1BDM 691
ATOM 390 O VAL A 52 31.152 14.327 35.317 1.00 19.37 1BDM 692
ATOM 391 CB VAL A 52 30.453 15.881 32.442 1.00 23.19 1BDM 693
ATOM 392 CG1 VAL A 52 29.631 16.707 33.444 1.00 15.59 1BDM 694
ATOM 393 CG2 VAL A 52 31.095 16.884 31.517 1.00 17.23 1BDM 695
ATOM 394 N VAL A 53 30.453 12.961 33.802 1.00 15.27 1BDM 696
ATOM 395 CA VAL A 53 29.969 12.005 34.744 1.00 16.73 1BDM 697
ATOM 396 C VAL A 53 31.114 11.559 35.672 1.00 24.38 1BDM 698
ATOM 397 O VAL A 53 31.028 11.516 36.914 1.00 18.84 1BDM 699
ATOM 398 CB VAL A 53 29.233 10.856 34.032 1.00 20.78 1BDM 700
ATOM 399 CG1 VAL A 53 28.922 9.732 35.022 1.00 18.47 1BDM 701
ATOM 400 CG2 VAL A 53 27.886 11.364 33.507 1.00 19.04 1BDM 702
ATOM 401 N MET A 54 32.234 11.254 35.065 1.00 16.60 1BDM 703
ATOM 402 CA MET A 54 33.404 10.873 35.853 1.00 14.79 1BDM 704
ATOM 403 C MET A 54 33.783 11.981 36.829 1.00 21.07 1BDM 705
ATOM 404 O MET A 54 34.050 11.728 38.021 1.00 17.16 1BDM 706
ATOM 405 CB MET A 54 34.617 10.560 34.964 1.00 17.00 1BDM 707
ATOM 406 CG MET A 54 34.466 9.144 34.417 1.00 25.16 1BDM 708
ATOM 407 SD MET A 54 35.922 8.568 33.503 1.00 29.03 1BDM 709
ATOM 408 CE MET A 54 35.765 9.600 32.062 1.00 21.54 1BDM 710
ATOM 409 N GLU A 55 33.818 13.214 36.375 1.00 12.38 1BDM 711
ATOM 410 CA GLU A 55 34.172 14.285 37.315 1.00 11.83 1BDM 712
ATOM 411 C GLU A 55 33.144 14.421 38.443 1.00 24.31 1BDM 713
ATOM 412 O GLU A 55 33.449 14.724 39.553 1.00 14.24 1BDM 714
ATOM 413 CB GLU A 55 34.283 15.643 36.677 1.00 10.99 1BDM 715
ATOM 414 CG GLU A 55 35.551 15.712 35.810 1.00 11.68 1BDM 716
ATOM 415 CD GLU A 55 35.999 17.101 35.563 1.00 19.44 1BDM 717
ATOM 416 OE1 GLU A 55 36.587 17.651 36.608 1.00 15.66 1BDM 718
ATOM 417 OE2 GLU A 55 35.889 17.654 34.500 1.00 19.25 1BDM 719
ATOM 418 N LEU A 56 31.876 14.209 38.185 1.00 13.70 1BDM 720
ATOM 419 CA LEU A 56 30.871 14.341 39.256 1.00 17.13 1BDM 721
ATOM 420 C LEU A 56 31.124 13.221 40.275 1.00 17.32 1BDM 722
ATOM 421 O LEU A 56 30.901 13.373 41.457 1.00 15.79 1BDM 723
ATOM 422 CB LEU A 56 29.423 14.189 38.670 1.00 13.77 1BDM 724
ATOM 423 CG LEU A 56 28.971 15.458 37.960 1.00 18.96 1BDM 725
ATOM 424 CD1 LEU A 56 27.791 15.104 37.036 1.00 18.81 1BDM 726
ATOM 425 CD2 LEU A 56 28.529 16.416 39.060 1.00 13.58 1BDM 727
ATOM 426 N GLU A 57 31.504 12.040 39.820 1.00 13.98 1BDM 728
ATOM 427 CA GLU A 57 31.727 10.960 40.729 1.00 18.46 1BDM 729
ATOM 428 C GLU A 57 32.881 11.307 41.629 1.00 20.05 1BDM 730
ATOM 429 O GLU A 57 32.940 10.892 42.775 1.00 16.01 1BDM 731
ATOM 430 CB GLU A 57 32.102 9.665 40.011 1.00 16.41 1BDM 732
ATOM 431 CG GLU A 57 30.931 9.106 39.134 1.00 19.98 1BDM 733
ATOM 432 CD GLU A 57 31.384 7.862 38.422 1.00 19.51 1BDM 734
ATOM 433 OE1 GLU A 57 32.502 7.663 38.060 1.00 22.64 1BDM 735
ATOM 434 OE2 GLU A 57 30.458 6.981 38.298 1.00 23.60 1BDM 736
ATOM 435 N ASP A 58 33.850 11.973 41.030 1.00 13.99 1BDM 737
ATOM 436 CA ASP A 58 35.087 12.285 41.714 1.00 16.78 1BDM 738
ATOM 437 C ASP A 58 35.008 13.431 42.717 1.00 16.49 1BDM 739
ATOM 438 O ASP A 58 36.024 13.814 43.306 1.00 19.81 1BDM 740
ATOM 439 CB ASP A 58 36.191 12.575 40.714 1.00 10.17 1BDM 741
ATOM 440 CG ASP A 58 36.589 11.323 39.961 1.00 15.43 1BDM 742
ATOM 441 OD1 ASP A 58 36.211 10.208 40.256 1.00 17.15 1BDM 743
ATOM 442 OD2 ASP A 58 37.420 11.573 38.958 1.00 17.72 1BDM 744
ATOM 443 N CYS A 59 33.803 14.032 42.869 1.00 11.72 1BDM 745
ATOM 444 CA CYS A 59 33.543 15.091 43.852 1.00 11.61 1BDM 746
ATOM 445 C CYS A 59 33.090 14.428 45.141 1.00 13.18 1BDM 747
ATOM 446 O CYS A 59 33.059 15.104 46.127 1.00 20.03 1BDM 748
ATOM 447 CB CYS A 59 32.429 15.965 43.315 1.00 9.10 1BDM 749
ATOM 448 SG CYS A 59 33.164 17.102 42.120 1.00 16.52 1BDM 750
ATOM 449 N ALA A 60 32.652 13.165 45.086 1.00 12.18 1BDM 751
ATOM 450 CA ALA A 60 32.174 12.419 46.243 1.00 16.43 1BDM 752
ATOM 451 C ALA A 60 31.143 13.223 46.978 1.00 21.18 1BDM 753
ATOM 452 O ALA A 60 31.276 13.478 48.165 1.00 18.09 1BDM 754
ATOM 453 CB ALA A 60 33.346 12.113 47.152 1.00 14.05 1BDM 755
ATOM 454 N PHE A 61 30.089 13.615 46.262 1.00 11.82 1BDM 756
ATOM 455 CA PHE A 61 29.046 14.478 46.805 1.00 12.14 1BDM 757
ATOM 456 C PHE A 61 28.070 13.630 47.608 1.00 23.97 1BDM 758
ATOM 457 O PHE A 61 27.550 12.693 47.061 1.00 20.34 1BDM 759
ATOM 458 CB PHE A 61 28.234 15.126 45.658 1.00 11.04 1BDM 760
ATOM 459 CG PHE A 61 28.921 16.304 45.008 1.00 19.97 1BDM 761
ATOM 460 CD1 PHE A 61 29.424 17.374 45.747 1.00 20.12 1BDM 762
ATOM 461 CD2 PHE A 61 29.052 16.358 43.618 1.00 21.23 1BDM 763
ATOM 462 CE1 PHE A 61 29.987 18.509 45.165 1.00 19.96 1BDM 764
ATOM 463 CE2 PHE A 61 29.605 17.485 43.018 1.00 11.62 1BDM 765
ATOM 464 CZ PHE A 61 30.051 18.569 43.778 1.00 15.57 1BDM 766
ATOM 465 N PRO A 62 27.794 13.950 48.871 1.00 20.09 1BDM 767
ATOM 466 CA PRO A 62 26.880 13.119 49.596 1.00 21.16 1BDM 768
ATOM 467 C PRO A 62 25.445 13.242 49.037 1.00 23.31 1BDM 769
ATOM 468 O PRO A 62 24.656 12.329 49.153 1.00 18.62 1BDM 770
ATOM 469 CB PRO A 62 26.986 13.594 51.052 1.00 14.49 1BDM 771
ATOM 470 CG PRO A 62 27.817 14.840 51.059 1.00 21.57 1BDM 772
ATOM 471 CD PRO A 62 28.561 14.850 49.756 1.00 13.61 1BDM 773
ATOM 472 N LEU A 63 25.013 14.346 48.459 1.00 13.18 1BDM 774
ATOM 473 CA LEU A 63 23.615 14.414 48.044 1.00 11.47 1BDM 775
ATOM 474 C LEU A 63 23.374 13.871 46.658 1.00 18.08 1BDM 776
ATOM 475 O LEU A 63 22.253 13.922 46.181 1.00 26.27 1BDM 777
ATOM 476 CB LEU A 63 23.213 15.880 47.994 1.00 14.27 1BDM 778
ATOM 477 CG LEU A 63 23.231 16.526 49.394 1.00 17.68 1BDM 779
ATOM 478 CD1 LEU A 63 22.964 18.014 49.227 1.00 16.13 1BDM 780
ATOM 479 CD2 LEU A 63 22.188 15.887 50.291 1.00 18.00 1BDM 781
ATOM 480 N LEU A 64 24.382 13.352 45.987 1.00 19.93 1BDM 782
ATOM 481 CA LEU A 64 24.169 12.857 44.615 1.00 13.33 1BDM 783
ATOM 482 C LEU A 64 23.708 11.436 44.687 1.00 16.61 1BDM 784
ATOM 483 O LEU A 64 24.543 10.536 44.779 1.00 20.61 1BDM 785
ATOM 484 CB LEU A 64 25.472 12.911 43.785 1.00 15.44 1BDM 786
ATOM 485 CG LEU A 64 25.317 12.494 42.324 1.00 24.54 1BDM 787
ATOM 486 CD1 LEU A 64 24.218 13.359 41.705 1.00 16.26 1BDM 788
ATOM 487 CD2 LEU A 64 26.622 12.778 41.555 1.00 21.87 1BDM 789
ATOM 488 N ALA A 65 22.380 11.229 44.710 1.00 22.46 1BDM 790
ATOM 489 CA ALA A 65 21.800 9.886 44.986 1.00 19.20 1BDM 791
ATOM 490 C ALA A 65 21.766 9.021 43.756 1.00 27.66 1BDM 792
ATOM 491 O ALA A 65 21.443 7.867 43.844 1.00 25.63 1BDM 793
ATOM 492 CB ALA A 65 20.354 9.993 45.475 1.00 16.80 1BDM 794
ATOM 493 N GLY A 66 22.052 9.563 42.584 1.00 25.54 1BDM 795
ATOM 494 CA GLY A 66 22.119 8.764 41.381 1.00 26.61 1BDM 796
ATOM 495 C GLY A 66 22.551 9.640 40.202 1.00 24.08 1BDM 797
ATOM 496 O GLY A 66 22.416 10.857 40.208 1.00 23.64 1BDM 798
ATOM 497 N LEU A 67 23.033 9.051 39.132 1.00 18.62 1BDM 799
ATOM 498 CA LEU A 67 23.498 9.873 38.028 1.00 23.71 1BDM 800
ATOM 499 C LEU A 67 23.294 9.045 36.797 1.00 31.91 1BDM 801
ATOM 500 O LEU A 67 23.811 7.929 36.764 1.00 26.30 1BDM 802
ATOM 501 CB LEU A 67 25.024 9.785 38.068 1.00 26.64 1BDM 803
ATOM 502 CG LEU A 67 25.806 11.044 38.162 1.00 45.75 1BDM 804
ATOM 503 CD1 LEU A 67 27.275 10.651 38.302 1.00 30.04 1BDM 805
ATOM 504 CD2 LEU A 67 25.553 11.816 36.903 1.00 22.82 1BDM 806
ATOM 505 N GLU A 68 22.646 9.566 35.781 1.00 26.01 1BDM 807
ATOM 506 CA GLU A 68 22.567 8.781 34.567 1.00 25.94 1BDM 808
ATOM 507 C GLU A 68 22.730 9.650 33.337 1.00 27.87 1BDM 809
ATOM 508 O GLU A 68 22.241 10.766 33.300 1.00 27.40 1BDM 810
ATOM 509 CB GLU A 68 21.230 8.032 34.539 1.00 40.91 1BDM 811
ATOM 510 CG GLU A 68 20.928 7.475 33.137 1.00 74.90 1BDM 812
ATOM 511 CD GLU A 68 19.826 6.450 33.124 1.00 75.94 1BDM 813
ATOM 512 OE1 GLU A 68 18.709 6.872 33.683 1.00 71.67 1BDM 814
ATOM 513 OE2 GLU A 68 19.980 5.350 32.622 1.00 76.60 1BDM 815
ATOM 514 N ALA A 69 23.435 9.153 32.335 1.00 24.46 1BDM 816
ATOM 515 CA ALA A 69 23.681 9.969 31.175 1.00 29.13 1BDM 817
ATOM 516 C ALA A 69 23.020 9.325 29.970 1.00 29.46 1BDM 818
ATOM 517 O ALA A 69 23.103 8.102 29.819 1.00 24.74 1BDM 819
ATOM 518 CB ALA A 69 25.175 9.938 31.008 1.00 25.63 1BDM 820
ATOM 519 N THR A 70 22.334 10.080 29.125 1.00 26.97 1BDM 821
ATOM 520 CA THR A 70 21.702 9.358 28.004 1.00 28.61 1BDM 822
ATOM 521 C THR A 70 21.598 10.207 26.758 1.00 24.36 1BDM 823
ATOM 522 O THR A 70 21.699 11.418 26.836 1.00 25.93 1BDM 824
ATOM 523 CB THR A 70 20.314 8.822 28.441 1.00 37.04 1BDM 825
ATOM 524 OG1 THR A 70 19.732 7.930 27.518 1.00 32.43 1BDM 826
ATOM 525 CG2 THR A 70 19.350 9.971 28.665 1.00 31.47 1BDM 827
ATOM 526 N ASP A 71 21.331 9.599 25.584 1.00 27.45 1BDM 828
ATOM 527 CA ASP A 71 21.089 10.427 24.401 1.00 30.76 1BDM 829
ATOM 528 C ASP A 71 19.634 10.328 24.002 1.00 29.17 1BDM 830
ATOM 529 O ASP A 71 19.241 10.931 23.015 1.00 38.49 1BDM 831
ATOM 530 CB ASP A 71 21.987 10.124 23.192 1.00 30.55 1BDM 832
ATOM 531 CG ASP A 71 21.915 8.670 22.792 1.00 48.54 1BDM 833
ATOM 532 OD1 ASP A 71 21.092 7.878 23.269 1.00 33.24 1BDM 834
ATOM 533 OD2 ASP A 71 22.873 8.342 21.940 1.00 43.89 1BDM 835
ATOM 534 N ASP A 72 18.836 9.661 24.839 1.00 28.79 1BDM 836
ATOM 535 CA ASP A 72 17.394 9.486 24.645 1.00 22.40 1BDM 837
ATOM 536 C ASP A 72 16.489 10.325 25.534 1.00 22.05 1BDM 838
ATOM 537 O ASP A 72 16.243 9.868 26.637 1.00 34.35 1BDM 839
ATOM 538 CB ASP A 72 17.067 8.039 25.068 1.00 30.50 1BDM 840
ATOM 539 CG ASP A 72 15.698 7.610 24.654 1.00 35.05 1BDM 841
ATOM 540 OD1 ASP A 72 14.803 8.399 24.439 1.00 34.88 1BDM 842
ATOM 541 OD2 ASP A 72 15.600 6.311 24.533 1.00 35.20 1BDM 843
ATOM 542 N PRO A 73 15.792 11.341 25.027 1.00 26.38 1BDM 844
ATOM 543 CA PRO A 73 14.912 12.137 25.874 1.00 26.75 1BDM 845
ATOM 544 C PRO A 73 13.929 11.405 26.756 1.00 30.28 1BDM 846
ATOM 545 O PRO A 73 13.514 11.927 27.812 1.00 35.62 1BDM 847
ATOM 546 CB PRO A 73 14.181 13.162 25.015 1.00 27.61 1BDM 848
ATOM 547 CG PRO A 73 14.958 13.177 23.709 1.00 27.13 1BDM 849
ATOM 548 CD PRO A 73 15.772 11.900 23.646 1.00 22.16 1BDM 850
ATOM 549 N ASP A 74 13.506 10.233 26.301 1.00 31.42 1BDM 851
ATOM 550 CA ASP A 74 12.529 9.509 27.086 1.00 28.71 1BDM 852
ATOM 551 C ASP A 74 13.174 8.861 28.291 1.00 30.72 1BDM 853
ATOM 552 O ASP A 74 12.475 8.598 29.246 1.00 38.29 1BDM 854
ATOM 553 CB ASP A 74 11.810 8.452 26.235 1.00 43.17 1BDM 855
ATOM 554 CG ASP A 74 10.670 9.046 25.474 1.00 59.31 1BDM 856
ATOM 555 OD1 ASP A 74 10.596 10.325 25.737 1.00 84.38 1BDM 857
ATOM 556 OD2 ASP A 74 9.913 8.430 24.726 1.00 58.90 1BDM 858
ATOM 557 N VAL A 75 14.476 8.526 28.209 1.00 34.52 1BDM 859
ATOM 558 CA VAL A 75 15.225 8.081 29.373 1.00 26.87 1BDM 860
ATOM 559 C VAL A 75 15.549 9.247 30.330 1.00 34.82 1BDM 861
ATOM 560 O VAL A 75 15.307 9.224 31.522 1.00 25.99 1BDM 862
ATOM 561 CB VAL A 75 16.509 7.414 28.954 1.00 35.89 1BDM 863
ATOM 562 CG1 VAL A 75 17.268 6.959 30.201 1.00 33.36 1BDM 864
ATOM 563 CG2 VAL A 75 16.140 6.187 28.150 1.00 33.27 1BDM 865
ATOM 564 N ALA A 76 16.078 10.335 29.803 1.00 18.44 1BDM 866
ATOM 565 CA ALA A 76 16.473 11.449 30.621 1.00 25.49 1BDM 867
ATOM 566 C ALA A 76 15.355 12.018 31.431 1.00 34.03 1BDM 868
ATOM 567 O ALA A 76 15.602 12.425 32.545 1.00 22.18 1BDM 869
ATOM 568 CB ALA A 76 17.126 12.534 29.764 1.00 23.96 1BDM 870
ATOM 569 N PHE A 77 14.160 12.147 30.827 1.00 19.04 1BDM 871
ATOM 570 CA PHE A 77 13.060 12.866 31.437 1.00 15.68 1BDM 872
ATOM 571 C PHE A 77 12.130 11.997 32.288 1.00 12.89 1BDM 873
ATOM 572 O PHE A 77 11.201 12.478 32.963 1.00 25.82 1BDM 874
ATOM 573 CB PHE A 77 12.251 13.619 30.360 1.00 24.17 1BDM 875
ATOM 574 CG PHE A 77 12.934 14.692 29.533 1.00 36.36 1BDM 876
ATOM 575 CD1 PHE A 77 13.896 15.551 30.077 1.00 34.80 1BDM 877
ATOM 576 CD2 PHE A 77 12.517 14.924 28.219 1.00 34.75 1BDM 878
ATOM 577 CE1 PHE A 77 14.445 16.593 29.323 1.00 30.47 1BDM 879
ATOM 578 CE2 PHE A 77 13.056 15.963 27.461 1.00 26.68 1BDM 880
ATOM 579 CZ PHE A 77 14.084 16.751 27.986 1.00 22.40 1BDM 881
ATOM 580 N LYS A 78 12.526 10.768 32.412 1.00 19.09 1BDM 882
ATOM 581 CA LYS A 78 11.639 9.872 33.117 1.00 25.09 1BDM 883
ATOM 582 C LYS A 78 11.486 10.173 34.593 1.00 33.67 1BDM 884
ATOM 583 O LYS A 78 12.448 10.249 35.350 1.00 25.80 1BDM 885
ATOM 584 CB LYS A 78 12.071 8.452 32.888 1.00 27.78 1BDM 886
ATOM 585 CG LYS A 78 11.206 7.484 33.666 1.00 34.94 1BDM 887
ATOM 586 CD LYS A 78 11.305 6.092 33.086 1.00 47.25 1BDM 888
ATOM 587 CE LYS A 78 10.472 5.166 33.933 1.00 72.81 1BDM 889
ATOM 588 NZ LYS A 78 9.139 5.750 34.162 1.00 79.04 1BDM 890
ATOM 589 N ASP A 79 10.237 10.262 35.029 1.00 29.07 1BDM 891
ATOM 590 CA ASP A 79 9.932 10.624 36.399 1.00 26.82 1BDM 892
ATOM 591 C ASP A 79 10.620 11.885 36.863 1.00 35.10 1BDM 893
ATOM 592 O ASP A 79 10.682 12.165 38.053 1.00 26.33 1BDM 894
ATOM 593 CB ASP A 79 10.268 9.500 37.362 1.00 30.60 1BDM 895
ATOM 594 CG ASP A 79 9.310 8.393 37.083 1.00 40.36 1BDM 896
ATOM 595 OD1 ASP A 79 8.155 8.655 36.825 1.00 45.25 1BDM 897
ATOM 596 OD2 ASP A 79 9.870 7.203 37.080 1.00 35.33 1BDM 898
ATOM 597 N ALA A 80 10.992 12.727 35.917 1.00 25.89 1BDM 899
ATOM 598 CA ALA A 80 11.594 13.971 36.293 1.00 18.12 1BDM 900
ATOM 599 C ALA A 80 10.678 14.879 37.083 1.00 22.19 1BDM 901
ATOM 600 O ALA A 80 9.536 15.126 36.765 1.00 23.49 1BDM 902
ATOM 601 CB ALA A 80 12.175 14.690 35.065 1.00 28.51 1BDM 903
ATOM 602 N ASP A 81 11.283 15.521 38.053 1.00 21.00 1BDM 904
ATOM 603 CA ASP A 81 10.627 16.485 38.876 1.00 14.84 1BDM 905
ATOM 604 C ASP A 81 11.021 17.869 38.418 1.00 19.37 1BDM 906
ATOM 605 O ASP A 81 10.219 18.812 38.570 1.00 22.03 1BDM 907
ATOM 606 CB ASP A 81 11.135 16.328 40.312 1.00 21.67 1BDM 908
ATOM 607 CG ASP A 81 10.582 15.131 41.011 1.00 24.23 1BDM 909
ATOM 608 OD1 ASP A 81 9.446 15.094 41.366 1.00 31.47 1BDM 910
ATOM 609 OD2 ASP A 81 11.441 14.156 41.229 1.00 25.60 1BDM 911
ATOM 610 N TYR A 82 12.242 18.023 37.843 1.00 15.91 1BDM 912
ATOM 611 CA TYR A 82 12.649 19.339 37.357 1.00 14.83 1BDM 913
ATOM 612 C TYR A 82 13.394 19.082 36.047 1.00 13.76 1BDM 914
ATOM 613 O TYR A 82 13.979 18.003 35.908 1.00 19.87 1BDM 915
ATOM 614 CB TYR A 82 13.673 20.075 38.244 1.00 19.70 1BDM 916
ATOM 615 CG TYR A 82 13.114 20.469 39.569 1.00 19.11 1BDM 917
ATOM 616 CD1 TYR A 82 13.179 19.541 40.609 1.00 26.57 1BDM 918
ATOM 617 CD2 TYR A 82 12.528 21.725 39.744 1.00 16.92 1BDM 919
ATOM 618 CE1 TYR A 82 12.501 19.790 41.797 1.00 22.76 1BDM 920
ATOM 619 CE2 TYR A 82 11.966 22.055 40.971 1.00 23.58 1BDM 921
ATOM 620 CZ TYR A 82 11.948 21.061 41.961 1.00 27.77 1BDM 922
ATOM 621 OH TYR A 82 11.302 21.307 43.121 1.00 30.14 1BDM 923
ATOM 622 N ALA A 83 13.252 20.005 35.045 1.00 17.38 1BDM 924
ATOM 623 CA ALA A 83 13.991 19.800 33.816 1.00 16.99 1BDM 925
ATOM 624 C ALA A 83 14.515 21.141 33.373 1.00 12.51 1BDM 926
ATOM 625 O ALA A 83 13.798 22.146 33.312 1.00 19.57 1BDM 927
ATOM 626 CB ALA A 83 13.128 19.160 32.732 1.00 19.03 1BDM 928
ATOM 627 N LEU A 84 15.835 21.163 33.153 1.00 23.44 1BDM 929
ATOM 628 CA LEU A 84 16.585 22.383 32.806 1.00 18.42 1BDM 930
ATOM 629 C LEU A 84 16.955 22.197 31.346 1.00 15.86 1BDM 931
ATOM 630 O LEU A 84 17.745 21.321 31.079 1.00 20.24 1BDM 932
ATOM 631 CB LEU A 84 17.884 22.480 33.664 1.00 15.69 1BDM 933
ATOM 632 CG LEU A 84 17.553 23.198 34.988 1.00 26.77 1BDM 934
ATOM 633 CD1 LEU A 84 16.772 22.329 35.996 1.00 20.10 1BDM 935
ATOM 634 CD2 LEU A 84 18.799 23.821 35.624 1.00 24.95 1BDM 936
ATOM 635 N LEU A 85 16.276 22.907 30.426 1.00 21.82 1BDM 937
ATOM 636 CA LEU A 85 16.520 22.645 29.025 1.00 20.76 1BDM 938
ATOM 637 C LEU A 85 17.561 23.651 28.526 1.00 16.72 1BDM 939
ATOM 638 O LEU A 85 17.242 24.816 28.198 1.00 18.33 1BDM 940
ATOM 639 CB LEU A 85 15.191 22.754 28.238 1.00 21.64 1BDM 941
ATOM 640 CG LEU A 85 14.098 21.834 28.746 1.00 22.88 1BDM 942
ATOM 641 CD1 LEU A 85 12.899 21.855 27.785 1.00 26.54 1BDM 943
ATOM 642 CD2 LEU A 85 14.595 20.420 28.936 1.00 24.60 1BDM 944
ATOM 643 N VAL A 86 18.814 23.208 28.515 1.00 19.18 1BDM 945
ATOM 644 CA VAL A 86 19.918 24.112 28.177 1.00 29.06 1BDM 946
ATOM 645 C VAL A 86 20.353 23.944 26.722 1.00 19.62 1BDM 947
ATOM 646 O VAL A 86 20.763 24.886 26.053 1.00 20.42 1BDM 948
ATOM 647 CB VAL A 86 21.127 23.833 29.084 1.00 26.17 1BDM 949
ATOM 648 CG1 VAL A 86 22.303 24.747 28.796 1.00 23.35 1BDM 950
ATOM 649 CG2 VAL A 86 20.720 23.951 30.545 1.00 24.64 1BDM 951
ATOM 650 N GLY A 87 20.282 22.730 26.212 1.00 15.83 1BDM 952
ATOM 651 CA GLY A 87 20.767 22.550 24.861 1.00 27.33 1BDM 953
ATOM 652 C GLY A 87 19.770 23.126 23.842 1.00 31.71 1BDM 954
ATOM 653 O GLY A 87 18.539 23.093 24.002 1.00 25.42 1BDM 955
ATOM 654 N ALA A 88 20.320 23.750 22.810 1.00 25.82 1BDM 956
ATOM 655 CA ALA A 88 19.524 24.274 21.720 1.00 28.23 1BDM 957
ATOM 656 C ALA A 88 20.326 24.202 20.426 1.00 56.58 1BDM 958
ATOM 657 O ALA A 88 21.483 23.764 20.417 1.00 35.63 1BDM 959
ATOM 658 CB ALA A 88 18.979 25.660 21.986 1.00 19.14 1BDM 960
ATOM 659 N ALA A 89 19.715 24.642 19.331 1.00 45.75 1BDM 961
ATOM 660 CA ALA A 89 20.403 24.563 18.055 1.00 49.13 1BDM 962
ATOM 661 C ALA A 89 21.537 25.558 18.011 1.00 36.02 1BDM 963
ATOM 662 O ALA A 89 21.348 26.775 18.156 1.00 44.21 1BDM 964
ATOM 663 CB ALA A 89 19.481 24.840 16.878 1.00 48.70 1BDM 965
ATOM 664 N PRO A 90 22.701 24.998 17.702 1.00 37.54 1BDM 966
ATOM 665 CA PRO A 90 23.855 25.815 17.461 1.00 39.39 1BDM 967
ATOM 666 C PRO A 90 23.354 26.747 16.376 1.00 52.36 1BDM 968
ATOM 667 O PRO A 90 22.862 26.448 15.313 1.00 65.78 1BDM 969
ATOM 668 CB PRO A 90 24.910 24.851 16.923 1.00 48.37 1BDM 970
ATOM 669 CG PRO A 90 24.187 23.583 16.456 1.00 48.82 1BDM 971
ATOM 670 CD PRO A 90 22.746 23.711 16.926 1.00 43.37 1BDM 972
ATOM 671 N ARG A 91 24.865 28.704 16.207 1.00 73.19 1BDM 973
ATOM 672 N LEU A 101 14.971 28.652 13.904 1.00 49.91 1BDM 974
ATOM 673 CA LEU A 101 13.538 28.381 14.093 1.00 44.37 1BDM 975
ATOM 674 C LEU A 101 13.132 26.947 13.749 1.00 56.44 1BDM 976
ATOM 675 O LEU A 101 12.541 26.294 14.601 1.00 46.27 1BDM 977
ATOM 676 CB LEU A 101 12.463 29.431 13.660 1.00 54.13 1BDM 978
ATOM 677 CG LEU A 101 12.102 30.507 14.684 1.00 66.46 1BDM 979
ATOM 678 CD1 LEU A 101 13.173 30.541 15.743 1.00 60.97 1BDM 980
ATOM 679 CD2 LEU A 101 12.025 31.913 14.080 1.00 65.63 1BDM 981
ATOM 680 N GLN A 102 13.429 26.423 12.545 1.00 46.17 1BDM 982
ATOM 681 CA GLN A 102 13.025 25.046 12.262 1.00 63.78 1BDM 983
ATOM 682 C GLN A 102 13.774 24.089 13.174 1.00 46.39 1BDM 984
ATOM 683 O GLN A 102 13.215 23.119 13.689 1.00 38.11 1BDM 985
ATOM 684 CB GLN A 102 13.171 24.437 10.822 1.00 45.07 1BDM 986
ATOM 685 CG GLN A 102 12.895 25.282 9.559 1.00 78.85 1BDM 987
ATOM 686 CD GLN A 102 11.447 25.671 9.321 1.00 86.57 1BDM 988
ATOM 687 OE1 GLN A 102 10.547 24.830 9.140 1.00 72.83 1BDM 989
ATOM 688 NE2 GLN A 102 11.238 26.988 9.309 1.00 92.21 1BDM 990
ATOM 689 N VAL A 103 15.094 24.274 13.204 1.00 40.93 1BDM 991
ATOM 690 CA VAL A 103 15.948 23.361 13.916 1.00 36.79 1BDM 992
ATOM 691 C VAL A 103 15.616 23.359 15.396 1.00 35.37 1BDM 993
ATOM 692 O VAL A 103 15.285 22.313 15.928 1.00 45.20 1BDM 994
ATOM 693 CB VAL A 103 17.426 23.496 13.592 1.00 36.17 1BDM 995
ATOM 694 CG1 VAL A 103 17.755 24.922 13.236 1.00 57.03 1BDM 996
ATOM 695 CG2 VAL A 103 18.222 23.125 14.823 1.00 46.49 1BDM 997
ATOM 696 N ASN A 104 15.563 24.534 16.027 1.00 35.77 1BDM 998
ATOM 697 CA ASN A 104 15.064 24.597 17.404 1.00 32.05 1BDM 999
ATOM 698 C ASN A 104 13.694 23.952 17.545 1.00 44.66 1BDM1000
ATOM 699 O ASN A 104 13.487 23.137 18.454 1.00 41.03 1BDM1001