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HEADER OXIDOREDUCTASE (NAD(A)-CHOH(D)) 16-JAN-84 6ADH 6ADH 3
COMPND HOLO-LIVER ALCOHOL DEHYDROGENASE (E.C.1.1.1.1) COMPLEX WITH 6ADH 4
COMPND 1 NAD AND DMSO 6ADH 5
SOURCE HORSE (EQUUS $CABALLUS) LIVER 6ADH 6
AUTHOR H.EKLUND 6ADH 7
REVDAT 3 15-JAN-87 6ADHB 1 REMARK 6ADHB 1
REVDAT 2 04-MAR-85 6ADHA 1 REMARK 6ADHA 1
REVDAT 1 18-JUL-84 6ADH 0 6ADH 8
JRNL AUTH H.EKLUND,J.-*P.SAMAMA,L.WALLEN,C.-*I.BRANDEN, 6ADH 9
JRNL AUTH 2 A.AKESON,T.A.JONES 6ADH 10
JRNL TITL STRUCTURE OF TRICLINIC TERNARY COMPLEX OF HORSE 6ADH 11
JRNL TITL 2 LIVER ALCOHOL DEHYDROGENASE AT 2.9 ANGSTROMS 6ADH 12
JRNL TITL 3 RESOLUTION 6ADH 13
JRNL REF J.MOL.BIOL. V. 146 561 1981 6ADH 14
JRNL REFN ASTM JMOBAK UK ISSN 0022-2836 070 6ADH 15
REMARK 1 6ADH 16
REMARK 1 REFERENCE 1 6ADHB 2
REMARK 1 AUTH F.COLONNA-*CESARI,D.PERAHIA,M.KARPLUS,H.EKLUND, 6ADHB 3
REMARK 1 AUTH 2 C.I.BRANDEN,O.TAPIA 6ADHB 4
REMARK 1 TITL INTERDOMAIN MOTION IN LIVER ALCOHOL DEHYDROGENASE. 6ADHB 5
REMARK 1 TITL 2 STRUCTURAL AND ENERGETIC ANALYSIS OF THE HINGE 6ADHB 6
REMARK 1 TITL 3 BENDING MODE 6ADHB 7
REMARK 1 REF J.BIOL.CHEM. V. 261 15273 1986 6ADHB 8
REMARK 1 REFN ASTM JBCHA3 US ISSN 0021-9258 071 6ADHB 9
REMARK 1 REFERENCE 2 6ADHB 10
REMARK 1 AUTH H.EKLUND,J.-*P.SAMAMA,T.A.JONES 6ADHA 3
REMARK 1 TITL CRYSTALLOGRAPHIC INVESTIGATIONS OF NICOTINAMIDE 6ADHA 4
REMARK 1 TITL 2 ADENINE DINUCLEOTIDE BINDING TO HORSE LIVER ALCOHOL 6ADHA 5
REMARK 1 TITL 3 DEHYDROGENASE 6ADHA 6
REMARK 1 REF BIOCHEMISTRY V. 23 5982 1984 6ADHA 7
REMARK 1 REFN ASTM BICHAW US ISSN 0006-2960 033 6ADHA 8
REMARK 1 REFERENCE 3 6ADHB 11
REMARK 1 AUTH G.SCHNEIDER,H.EKLUND,E.CEDERGREN-*ZEPPEZAUER, 6ADH 18
REMARK 1 AUTH 2 M.ZEPPEZAUER 6ADH 19
REMARK 1 TITL CRYSTAL STRUCTURES OF THE ACTIVE SITE IN 6ADH 20
REMARK 1 TITL 2 SPECIFICALLY METAL-DEPLETED AND COBALT-SUBSTITUTED 6ADH 21
REMARK 1 TITL 3 HORSE LIVER ALCOHOL DEHYDROGENASE DERIVATIVES 6ADH 22
REMARK 1 REF PROC.NAT.ACAD.SCI.USA V. 80 5289 1983 6ADH 23
REMARK 1 REFN ASTM PNASA6 US ISSN 0027-8424 040 6ADH 24
REMARK 1 REFERENCE 4 6ADHB 12
REMARK 1 AUTH B.V.PLAPP,H.EKLUND,T.A.JONES,C.-*I.BRANDEN 6ADH 26
REMARK 1 TITL THREE-DIMENSIONAL STRUCTURE OF ISONICOTINIMIDYLATED 6ADH 27
REMARK 1 TITL 2 LIVER ALCOHOL DEHYDROGENASE 6ADH 28
REMARK 1 REF J.BIOL.CHEM. V. 258 5537 1983 6ADH 29
REMARK 1 REFN ASTM JBCHA3 US ISSN 0021-9258 071 6ADH 30
REMARK 1 REFERENCE 5 6ADHB 13
REMARK 1 AUTH E.CEDERGREN-*ZEPPEZAUER 6ADH 32
REMARK 1 TITL CRYSTAL-*STRUCTURE DETERMINATION OF REDUCED 6ADH 33
REMARK 1 TITL 2 NICOTINAMIDE ADENINE DINUCLEOTIDE COMPLEX WITH 6ADH 34
REMARK 1 TITL 3 HORSE LIVER ALCOHOL DEHYDROGENASE MAINTAINED IN ITS 6ADH 35
REMARK 1 TITL 4 APO CONFORMATION BY ZINC-*BOUND IMIDAZOLE 6ADH 36
REMARK 1 REF BIOCHEMISTRY V. 22 5761 1983 6ADH 37
REMARK 1 REFN ASTM BICHAW US ISSN 0006-2960 033 6ADH 38
REMARK 1 REFERENCE 6 6ADHB 14
REMARK 1 AUTH H.EKLUND,B.V.PLAPP,J.-*P.SAMAMA,C.-*I.BRANDEN 6ADH 40
REMARK 1 TITL BINDING OF SUBSTRATE IN A TERNARY COMPLEX OF HORSE 6ADH 41
REMARK 1 TITL 2 LIVER ALCOHOL DEHYDROGENASE 6ADH 42
REMARK 1 REF J.BIOL.CHEM. V. 257 14349 1982 6ADH 43
REMARK 1 REFN ASTM JBCHA3 US ISSN 0021-9258 071 6ADH 44
REMARK 1 REFERENCE 7 6ADHB 15
REMARK 1 AUTH E.CEDERGREN-*ZEPPEZAUER,J.-*P.SAMAMA,H.EKLUND 6ADH 46
REMARK 1 TITL CRYSTAL STRUCTURE DETERMINATIONS OF COENZYME 6ADH 47
REMARK 1 TITL 2 ANALOGUE AND SUBSTRATE COMPLEXES OF LIVER ALCOHOL 6ADH 48
REMARK 1 TITL 3 DEHYDROGEANSE. BINDING OF 6ADH 49
REMARK 1 TITL 4 1,4,5,6-*TETRAHYDRONICOTINAMIDE ADENINE 6ADH 50
REMARK 1 TITL 5 DINUCLEOTIDE AND 6ADH 51
REMARK 1 TITL 6 $TRANS-4-(N,N-*DIMETHYLAMINO)CINNAMALDEHYDE TO THE 6ADH 52
REMARK 1 TITL 7 ENZYME 6ADH 53
REMARK 1 REF BIOCHEMISTRY V. 21 4895 1982 6ADH 54
REMARK 1 REFN ASTM BICHAW US ISSN 0006-2960 033 6ADH 55
REMARK 1 REFERENCE 8 6ADHB 16
REMARK 1 AUTH H.EKLUND,J.-*P.SAMAMA,L.WALLEN 6ADH 57
REMARK 1 TITL PYRAZOLE BINDING IN CRYSTALLINE BINARY AND TERNARY 6ADH 58
REMARK 1 TITL 2 COMPLEXES WITH LIVER ALCOHOL DEHYDROGENASE 6ADH 59
REMARK 1 REF BIOCHEMISTRY V. 21 4858 1982 6ADH 60
REMARK 1 REFN ASTM BICHAW US ISSN 0006-2960 033 6ADH 61
REMARK 1 REFERENCE 9 6ADHB 17
REMARK 1 AUTH J.-*P.SAMAMA,A.D.WRIXON,J.-*F.BIELLMANN 6ADH 63
REMARK 1 TITL 5-*METHYLNICOTINAMIDE-ADENINE DINUCLEOTIDE. KINETIC 6ADH 64
REMARK 1 TITL 2 INVESTIGATION WITH MAJOR AND MINOR ISOENZYMES OF 6ADH 65
REMARK 1 TITL 3 LIVER ALCOHOL DEHYDROGENASE AND STRUCTURAL 6ADH 66
REMARK 1 TITL 4 DETERMINATION OF ITS BINARY COMPLEX WITH ALCOHOL 6ADH 67
REMARK 1 TITL 5 DEHYDROGENASE 6ADH 68
REMARK 1 REF EUR.J.BIOCHEM. V. 118 479 1981 6ADH 69
REMARK 1 REFN ASTM EJBCAI IX ISSN 0014-2956 262 6ADH 70
REMARK 1 REFERENCE 10 6ADHB 18
REMARK 1 AUTH H.EKLUND,C.-*I.BRANDEN 6ADH 72
REMARK 1 TITL STRUCTURAL DIFFERENCES BETWEEN APO- AND HOLOENZYME 6ADH 73
REMARK 1 TITL 2 OF HORSE LIVER ALCOHOL DEHYDROGENASE 6ADH 74
REMARK 1 REF J.BIOL.CHEM. V. 254 3458 1979 6ADH 75
REMARK 1 REFN ASTM JBCHA3 US ISSN 0021-9258 071 6ADH 76
REMARK 1 REFERENCE 11 6ADHB 19
REMARK 1 AUTH J.-*F.BIELLMANN,J.-*P.SAMAMA,C.I.BRANDEN,H.EKLUND 6ADH 78
REMARK 1 TITL X-*RAY STUDIES OF THE BINDING OF CIBACRON BLUE 6ADH 79
REMARK 1 TITL 2 /F3GA$ TO LIVER ALCOHOL DEHYDROGENASE 6ADH 80
REMARK 1 REF EUR.J.BIOCHEM. V. 102 107 1979 6ADH 81
REMARK 1 REFN ASTM EJBCAI IX ISSN 0014-2956 262 6ADH 82
REMARK 1 REFERENCE 12 6ADHB 20
REMARK 1 AUTH B.V.PLAPP,H.EKLUND,C.-*I.BRANDEN 6ADH 84
REMARK 1 TITL CRYSTALLOGRAPHY OF LIVER ALCOHOL DEHYDROGENASE 6ADH 85
REMARK 1 TITL 2 COMPLEXED WITH SUBSTRATES 6ADH 86
REMARK 1 REF J.MOL.BIOL. V. 122 23 1978 6ADH 87
REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 070 6ADH 88
REMARK 1 REFERENCE 13 6ADHB 21
REMARK 1 AUTH B.V.PLAPP,E.ZEPPEZAUER,C.-*I.BRANDEN 6ADH 90
REMARK 1 TITL CRYSTALLIZATION OF LIVER ALCOHOL DENYDROGENASE 6ADH 91
REMARK 1 TITL 2 ACTIVATED BY THE MODIFICATION OF AMINO GROUPS 6ADH 92
REMARK 1 REF J.MOL.BIOL. V. 119 451 1978 6ADH 93
REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 070 6ADH 94
REMARK 1 REFERENCE 14 6ADHB 22
REMARK 1 AUTH H.JORNVALL,H.EKLUND,C.-*I.BRANDEN 6ADH 96
REMARK 1 TITL SUBUNIT CONFORMATION OF YEAST ALCOHOL DEHYDROGENASE 6ADH 97
REMARK 1 REF J.BIOL.CHEM. V. 253 8414 1978 6ADH 98
REMARK 1 REFN ASTM JBCHA3 US ISSN 0021-9258 071 6ADH 99
REMARK 1 REFERENCE 15 6ADHB 23
REMARK 1 AUTH J.-*P.SAMAMA,E.ZEPPEZAUER,J.-*F.BIELLMANN, 6ADH 101
REMARK 1 AUTH 2 C.-*I.BRANDEN 6ADH 102
REMARK 1 TITL THE CRYSTAL STRUCTURE OF COMPLEXES BETWEEN HORSE 6ADH 103
REMARK 1 TITL 2 LIVER ALCOHOL DEHYDROGENASE AND THE COENZYME 6ADH 104
REMARK 1 TITL 3 ANALOGUES 3-*IODOPYRIDINE-ADENINE DINUCLEOTIDE 6ADH 105
REMARK 1 TITL 4 AND PYRIDINE-ADENINE DINUCLEOTIDE 6ADH 106
REMARK 1 REF EUR.J.BIOCHEM. V. 81 403 1977 6ADH 107
REMARK 1 REFN ASTM EJBCAI IX ISSN 0014-2956 262 6ADH 108
REMARK 1 REFERENCE 16 6ADHB 24
REMARK 1 AUTH T.BOIWE,C.-*I.BRANDEN 6ADH 110
REMARK 1 TITL X-*RAY INVESTIGATION OF THE BINDING OF 6ADH 111
REMARK 1 TITL 2 1,10-*PHENANTHROLINE AND IMIDAZOLE TO HORSE-*LIVER 6ADH 112
REMARK 1 TITL 3 ALCOHOL DEHYDROGENASE 6ADH 113
REMARK 1 REF EUR.J.BIOCHEM. V. 77 173 1977 6ADH 114
REMARK 1 REFN ASTM EJBCAI IX ISSN 0014-2956 262 6ADH 115
REMARK 1 REFERENCE 17 6ADHB 25
REMARK 1 AUTH H.EKLUND,B.NORDSTROM,E.ZEPPEZAUER,G.SODERLUND, 6ADH 117
REMARK 1 AUTH 2 I.OHLSSON,T.BOIWE,B.-*O.SODERBERG,O.TAPIA, 6ADH 118
REMARK 1 AUTH 3 C.-*I.BRANDEN,A.AKESON 6ADH 119
REMARK 1 TITL THREE-DIMENSIONAL STRUCTURE OF HORSE LIVER ALCOHOL 6ADH 120
REMARK 1 TITL 2 DEHYDROGENASE AT 2.4 ANGSTROMS RESOLUTION 6ADH 121
REMARK 1 REF J.MOL.BIOL. V. 102 27 1976 6ADH 122
REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 070 6ADH 123
REMARK 1 REFERENCE 18 6ADHB 26
REMARK 1 AUTH H.EKLUND,C.-*I.BRANDEN,H.JORNVALL 6ADH 125
REMARK 1 TITL STRUCTURAL COMPARISONS OF MAMMALIAN, YEAST AND 6ADH 126
REMARK 1 TITL 2 BACILLAR ALCOHOL DEHYDROGENASES 6ADH 127
REMARK 1 REF J.MOL.BIOL. V. 102 61 1976 6ADH 128
REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 070 6ADH 129
REMARK 1 REFERENCE 19 6ADHB 27
REMARK 1 AUTH B.NORDSTROM,C.-*I.BRANDEN 6ADH 131
REMARK 1 TITL THE BINDING OF NUCLEOTIDES TO HORSE LIVER ALCOHOL 6ADH 132
REMARK 1 TITL 2 DEHYDROGENASE 6ADH 133
REMARK 1 EDIT M.SUNDARALINGAM,S.T.RAO 6ADH 134
REMARK 1 REF STRUCTURE AND CONFORMATION 387 1975 6ADH 135
REMARK 1 REF 2 OF NUCLEIC ACIDS AND 6ADH 136
REMARK 1 REF 3 PROTEIN-NUCLEIC ACID 6ADH 137
REMARK 1 REF 4 INTERACTIONS 6ADH 138
REMARK 1 PUBL UNIVERSITY PARK PRESS, BALTIMORE 6ADH 139
REMARK 1 REFN ISBN 0-8391-0764-1 992 6ADH 140
REMARK 1 REFERENCE 20 6ADHB 28
REMARK 1 AUTH C.-*I.BRANDEN,H.JORNVALL,H.EKLUND,B.FURUGREN 6ADH 142
REMARK 1 TITL ALCOHOL DEHYDROGENASES 6ADH 143
REMARK 1 EDIT P.D.BOYER 6ADH 144
REMARK 1 REF THE ENZYMES,THIRD EDITION V. 11 103 1975 6ADH 145
REMARK 1 PUBL ACADEMIC PRESS,NEW YORK 6ADH 146
REMARK 1 REFN ISBN 0-12-122711-1 436 6ADH 147
REMARK 1 REFERENCE 21 6ADHB 29
REMARK 1 AUTH M.A.ABDALLAH,J.-*F.BIELLMANN,B.NORDSTROM, 6ADH 149
REMARK 1 AUTH 2 C.-*I.BRANDEN 6ADH 150
REMARK 1 TITL THE CONFORMATION OF ADENOSINE DIPHOSPHORIBOSE AND 6ADH 151
REMARK 1 TITL 2 8-*BROMOADENOSINE DIPHOSPHORIBOSE WHEN BOUND TO 6ADH 152
REMARK 1 TITL 3 LIVER ALCOHOL DEHYDROGENASE 6ADH 153
REMARK 1 REF EUR.J.BIOCHEM. V. 50 475 1975 6ADH 154
REMARK 1 REFN ASTM EJBCAI IX ISSN 0014-2956 262 6ADH 155
REMARK 1 REFERENCE 22 6ADHB 30
REMARK 1 AUTH H.EKLUND,B.NORDSTROM,E.ZEPPEZAUER,G.SODERLUND, 6ADH 157
REMARK 1 AUTH 2 I.OHLSSON,T.BOIWE,C.-*I.BRANDEN 6ADH 158
REMARK 1 TITL THE STRUCTURE OF HORSE LIVER ALCOHOL DEHYDROGENASE 6ADH 159
REMARK 1 REF /FEBS$ LETT. V. 44 200 1974 6ADH 160
REMARK 1 REFN ASTM FEBLAL NE ISSN 0014-5793 165 6ADH 161
REMARK 1 REFERENCE 23 6ADHB 31
REMARK 1 AUTH I.OHLSSON,B.NORDSTROM,C.-*I.BRANDEN 6ADH 163
REMARK 1 TITL STRUCTURAL AND FUNCTIONAL SIMILARITIES WITHIN THE 6ADH 164
REMARK 1 TITL 2 COENZYME BINDING DOMAINS OF DEHYDROGENASES 6ADH 165
REMARK 1 REF J.MOL.BIOL. V. 89 339 1974 6ADH 166
REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 070 6ADH 167
REMARK 1 REFERENCE 24 6ADHB 32
REMARK 1 AUTH R.EINARSSON,H.EKLUND,E.ZEPPEZAUER,T.BOIWE, 6ADH 169
REMARK 1 AUTH 2 C.-*I.BRANDEN 6ADH 170
REMARK 1 TITL BINDING OF SALICYLATE IN THE ADENOSINE-*BINDING 6ADH 171
REMARK 1 TITL 2 POCKET OF DEHYDROGENASES 6ADH 172
REMARK 1 REF EUR.J.BIOCHEM. V. 49 41 1974 6ADH 173
REMARK 1 REFN ASTM EJBCAI IX ISSN 0014-2956 262 6ADH 174
REMARK 1 REFERENCE 25 6ADHB 33
REMARK 1 AUTH C.-*I.BRANDEN,H.EKLUND,B.NORDSTROM,T.BOIWE, 6ADH 176
REMARK 1 AUTH 2 G.SODERLUND,E.ZEPPEZAUER,I.OHLSSON,A.AKESON 6ADH 177
REMARK 1 TITL STRUCTURE OF LIVER ALCOHOL DEHYDROGENASE AT 6ADH 178
REMARK 1 TITL 2 2.9-*ANGSTROMS RESOLUTION 6ADH 179
REMARK 1 REF PROC.NAT.ACAD.SCI.USA V. 70 2439 1973 6ADH 180
REMARK 1 REFN ASTM PNASA6 US ISSN 0027-8424 040 6ADH 181
REMARK 1 REFERENCE 26 6ADHB 34
REMARK 1 AUTH C.-*I.BRANDEN 6ADH 183
REMARK 1 TITL STRUCTURE OF HORSE LIVER ALCOHOL DEHYDROGENASE. I. 6ADH 184
REMARK 1 TITL 2 STRUCTURAL SYMMETRY AND CONFORMATIONAL CHANGES 6ADH 185
REMARK 1 REF ARCH.BIOCHEM.BIOPHYS. V. 112 215 1965 6ADH 186
REMARK 1 REFN ASTM ABBIA4 US ISSN 0003-9861 158 6ADH 187
REMARK 1 REFERENCE 27 6ADHB 35
REMARK 1 EDIT M.O.DAYHOFF 6ADH 189
REMARK 1 REF ATLAS OF PROTEIN SEQUENCE V. 5 145 1972 6ADH 190
REMARK 1 REF 2 AND STRUCTURE (DATA SECTION) 6ADH 191
REMARK 1 PUBL NATIONAL BIOMEDICAL RESEARCH FOUNDATION, 6ADH 192
REMARK 1 PUBL 2 SILVER SPRING,MD. 6ADH 193
REMARK 1 REFN ISBN 0-912466-02-2 435 6ADH 194
REMARK 2 6ADH 195
REMARK 2 RESOLUTION. 2.9 ANGSTROMS. 6ADH 196
REMARK 3 6ADH 197
REMARK 3 REFINEMENT. NONE. 6ADH 198
REMARK 4 6ADH 199
REMARK 4 SITE *DMA* COMPRISES THE RESIDUES OF THE *A* CHAIN 6ADH 200
REMARK 4 INTERACTING WITH THE DMSO OF THE *A* CHAIN. SITE *DMB* 6ADH 201
REMARK 4 COMPRISES THE RESIDUES OF THE *B* CHAIN INTERACTING WITH 6ADH 202
REMARK 4 THE DMSO OF THE *B* CHAIN. SITE *NAA* COMPRISES THE 6ADH 203
REMARK 4 RESIDUES OF THE *A* CHAIN INTERACTING WITH THE NAD OF THE 6ADH 204
REMARK 4 *A* CHAIN. SITE *NAB* COMPRISES THE RESIDUES OF THE *B* 6ADH 205
REMARK 4 CHAIN INTERACTING WITH THE NAD OF THE *B* CHAIN. 6ADH 206
REMARK 5 6ADHA 34
REMARK 5 CORRECTION. INSERT NEW PUBLICATION AS REFERENCE 1 AND 6ADHA 35
REMARK 5 RENUMBER THE OTHERS. 04-MAR-85. 6ADHA 36
REMARK 6 6ADHB 36
REMARK 6 CORRECTION. INSERT NEW PUBLICATION AS REFERENCE 1 AND 6ADHB 37
REMARK 6 RENUMBER THE OTHERS. 15-JAN-87. 6ADHB 38
SEQRES 1 A 374 SER THR ALA GLY LYS VAL ILE LYS CYS LYS ALA ALA VAL 6ADH 207
SEQRES 2 A 374 LEU TRP GLU GLU LYS LYS PRO PHE SER ILE GLU GLU VAL 6ADH 208
SEQRES 3 A 374 GLU VAL ALA PRO PRO LYS ALA HIS GLU VAL ARG ILE LYS 6ADH 209
SEQRES 4 A 374 MET VAL ALA THR GLY ILE CYS ARG SER ASP ASP HIS VAL 6ADH 210
SEQRES 5 A 374 VAL SER GLY THR LEU VAL THR PRO LEU PRO VAL ILE ALA 6ADH 211
SEQRES 6 A 374 GLY HIS GLU ALA ALA GLY ILE VAL GLU SER ILE GLY GLU 6ADH 212
SEQRES 7 A 374 GLY VAL THR THR VAL ARG PRO GLY ASP LYS VAL ILE PRO 6ADH 213
SEQRES 8 A 374 LEU PHE THR PRO GLN CYS GLY LYS CYS ARG VAL CYS LYS 6ADH 214
SEQRES 9 A 374 HIS PRO GLU GLY ASN PHE CYS LEU LYS ASN ASP LEU SER 6ADH 215
SEQRES 10 A 374 MET PRO ARG GLY THR MET GLN ASP GLY THR SER ARG PHE 6ADH 216
SEQRES 11 A 374 THR CYS ARG GLY LYS PRO ILE HIS HIS PHE LEU GLY THR 6ADH 217
SEQRES 12 A 374 SER THR PHE SER GLN TYR THR VAL VAL ASP GLU ILE SER 6ADH 218
SEQRES 13 A 374 VAL ALA LYS ILE ASP ALA ALA SER PRO LEU GLU LYS VAL 6ADH 219
SEQRES 14 A 374 CYS LEU ILE GLY CYS GLY PHE SER THR GLY TYR GLY SER 6ADH 220
SEQRES 15 A 374 ALA VAL LYS VAL ALA LYS VAL THR GLN GLY SER THR CYS 6ADH 221
SEQRES 16 A 374 ALA VAL PHE GLY LEU GLY GLY VAL GLY LEU SER VAL ILE 6ADH 222
SEQRES 17 A 374 MET GLY CYS LYS ALA ALA GLY ALA ALA ARG ILE ILE GLY 6ADH 223
SEQRES 18 A 374 VAL ASP ILE ASN LYS ASP LYS PHE ALA LYS ALA LYS GLU 6ADH 224
SEQRES 19 A 374 VAL GLY ALA THR GLU CYS VAL ASN PRO GLN ASP TYR LYS 6ADH 225
SEQRES 20 A 374 LYS PRO ILE GLN GLU VAL LEU THR GLU MET SER ASN GLY 6ADH 226
SEQRES 21 A 374 GLY VAL ASP PHE SER PHE GLU VAL ILE GLY ARG LEU ASP 6ADH 227
SEQRES 22 A 374 THR MET VAL THR ALA LEU SER CYS CYS GLN GLU ALA TYR 6ADH 228
SEQRES 23 A 374 GLY VAL SER VAL ILE VAL GLY VAL PRO PRO ASP SER GLN 6ADH 229
SEQRES 24 A 374 ASN LEU SER MET ASN PRO MET LEU LEU LEU SER GLY ARG 6ADH 230
SEQRES 25 A 374 THR TRP LYS GLY ALA ILE PHE GLY GLY PHE LYS SER LYS 6ADH 231
SEQRES 26 A 374 ASP SER VAL PRO LYS LEU VAL ALA ASP PHE MET ALA LYS 6ADH 232
SEQRES 27 A 374 LYS PHE ALA LEU ASP PRO LEU ILE THR HIS VAL LEU PRO 6ADH 233
SEQRES 28 A 374 PHE GLU LYS ILE ASN GLU GLY PHE ASP LEU LEU ARG SER 6ADH 234
SEQRES 29 A 374 GLY GLU SER ILE ARG THR ILE LEU THR PHE 6ADH 235
SEQRES 1 B 374 SER THR ALA GLY LYS VAL ILE LYS CYS LYS ALA ALA VAL 6ADH 236
SEQRES 2 B 374 LEU TRP GLU GLU LYS LYS PRO PHE SER ILE GLU GLU VAL 6ADH 237
SEQRES 3 B 374 GLU VAL ALA PRO PRO LYS ALA HIS GLU VAL ARG ILE LYS 6ADH 238
SEQRES 4 B 374 MET VAL ALA THR GLY ILE CYS ARG SER ASP ASP HIS VAL 6ADH 239
SEQRES 5 B 374 VAL SER GLY THR LEU VAL THR PRO LEU PRO VAL ILE ALA 6ADH 240
SEQRES 6 B 374 GLY HIS GLU ALA ALA GLY ILE VAL GLU SER ILE GLY GLU 6ADH 241
SEQRES 7 B 374 GLY VAL THR THR VAL ARG PRO GLY ASP LYS VAL ILE PRO 6ADH 242
SEQRES 8 B 374 LEU PHE THR PRO GLN CYS GLY LYS CYS ARG VAL CYS LYS 6ADH 243
SEQRES 9 B 374 HIS PRO GLU GLY ASN PHE CYS LEU LYS ASN ASP LEU SER 6ADH 244
SEQRES 10 B 374 MET PRO ARG GLY THR MET GLN ASP GLY THR SER ARG PHE 6ADH 245
SEQRES 11 B 374 THR CYS ARG GLY LYS PRO ILE HIS HIS PHE LEU GLY THR 6ADH 246
SEQRES 12 B 374 SER THR PHE SER GLN TYR THR VAL VAL ASP GLU ILE SER 6ADH 247
SEQRES 13 B 374 VAL ALA LYS ILE ASP ALA ALA SER PRO LEU GLU LYS VAL 6ADH 248
SEQRES 14 B 374 CYS LEU ILE GLY CYS GLY PHE SER THR GLY TYR GLY SER 6ADH 249
SEQRES 15 B 374 ALA VAL LYS VAL ALA LYS VAL THR GLN GLY SER THR CYS 6ADH 250
SEQRES 16 B 374 ALA VAL PHE GLY LEU GLY GLY VAL GLY LEU SER VAL ILE 6ADH 251
SEQRES 17 B 374 MET GLY CYS LYS ALA ALA GLY ALA ALA ARG ILE ILE GLY 6ADH 252
SEQRES 18 B 374 VAL ASP ILE ASN LYS ASP LYS PHE ALA LYS ALA LYS GLU 6ADH 253
SEQRES 19 B 374 VAL GLY ALA THR GLU CYS VAL ASN PRO GLN ASP TYR LYS 6ADH 254
SEQRES 20 B 374 LYS PRO ILE GLN GLU VAL LEU THR GLU MET SER ASN GLY 6ADH 255
SEQRES 21 B 374 GLY VAL ASP PHE SER PHE GLU VAL ILE GLY ARG LEU ASP 6ADH 256
SEQRES 22 B 374 THR MET VAL THR ALA LEU SER CYS CYS GLN GLU ALA TYR 6ADH 257
SEQRES 23 B 374 GLY VAL SER VAL ILE VAL GLY VAL PRO PRO ASP SER GLN 6ADH 258
SEQRES 24 B 374 ASN LEU SER MET ASN PRO MET LEU LEU LEU SER GLY ARG 6ADH 259
SEQRES 25 B 374 THR TRP LYS GLY ALA ILE PHE GLY GLY PHE LYS SER LYS 6ADH 260
SEQRES 26 B 374 ASP SER VAL PRO LYS LEU VAL ALA ASP PHE MET ALA LYS 6ADH 261
SEQRES 27 B 374 LYS PHE ALA LEU ASP PRO LEU ILE THR HIS VAL LEU PRO 6ADH 262
SEQRES 28 B 374 PHE GLU LYS ILE ASN GLU GLY PHE ASP LEU LEU ARG SER 6ADH 263
SEQRES 29 B 374 GLY GLU SER ILE ARG THR ILE LEU THR PHE 6ADH 264
FTNOTE 1 6ADH 265
FTNOTE 1 RESIDUE 62 OF BOTH THE A AND B CHAINS IS A CIS-PROLINE. 6ADH 266
FTNOTE 2 6ADH 267
FTNOTE 2 THIS ATOM WAS NOT LOCATED IN THE ELECTRON DENSITY MAP. 6ADH 268
FTNOTE 2 COORDINATES WERE GENERATED USING STEREOCHEMICAL CRITERIA. 6ADH 269
HET ZN A 1 1 CATALYTIC ZINC(II) ION 6ADH 270
HET ZN A 2 1 SECOND ZINC(II) ION 6ADH 271
HET NAD A 3 44 NICOTINAMIDE-ADENINE-DINUCLEOTIDE 6ADH 272
HET DMS A 4 4 DIMETHYL SULFOXIDE 6ADH 273
HET ZN B 1 1 CATALYTIC ZINC(II) ION 6ADH 274
HET ZN B 2 1 SECOND ZINC(II) ION 6ADH 275
HET NAD B 3 44 NICOTINAMIDE-ADENINE-DINUCLEOTIDE 6ADH 276
HET DMS B 4 4 DIMETHYL SULFOXIDE 6ADH 277
FORMUL 3 ZN 2(ZN1 ++) 6ADH 278
FORMUL 4 NAD 2(C21 H28 N7 O14 P2) 6ADH 279
FORMUL 5 DMS 2(C2 H6 O1 S1) 6ADH 280
HELIX 1 H1A CYS A 46 VAL A 53 1 6ADH 281
HELIX 2 H2A LYS A 168 GLY A 175 1 CONTIGUOUS WITH HELIX HAA 6ADH 282
HELIX 3 HAA PHE A 176 LYS A 188 1 CONTIGUOUS WITH HELIX H2A 6ADH 283
HELIX 4 HBA GLY A 201 GLY A 215 1 6ADH 284
HELIX 5 HCA PHE A 229 GLY A 236 1 6ADH 285
HELIX 6 CDA ILE A 250 SER A 258 1 6ADH 286
HELIX 7 HEA ARG A 271 CYS A 282 1 6ADH 287
HELIX 8 HSA PRO A 305 GLY A 311 5 3/10 HELIX 6ADH 288
HELIX 9 H3A SER A 324 LYS A 338 1 6ADH 289
HELIX 10 H4A ILE A 355 GLY A 365 1 6ADH 290
HELIX 11 H1B CYS B 46 VAL B 53 1 6ADH 291
HELIX 12 H2B LYS B 168 GLY B 175 1 CONTIGUOUS WITH HELIX HAB 6ADH 292
HELIX 13 HAB PHE B 176 LYS B 188 1 CONTIGUOUS WITH HELIX H2B 6ADH 293
HELIX 14 HBB GLY B 201 GLY B 215 1 6ADH 294
HELIX 15 HCB PHE B 229 GLY B 236 1 6ADH 295
HELIX 16 CDB ILE B 250 SER B 258 1 6ADH 296
HELIX 17 HEB ARG B 271 CYS B 282 1 6ADH 297
HELIX 18 HSB PRO B 305 GLY B 311 5 3/10 HELIX 6ADH 298
HELIX 19 H3B SER B 324 LYS B 338 1 6ADH 299
HELIX 20 H4B ILE B 355 GLY B 365 1 6ADH 300
SHEET 1 S1A 6 SER A 156 ILE A 160 0 6ADH 301
SHEET 2 S1A 6 LYS A 88 LEU A 92 -1 N ILE A 90 O ALA A 158 6ADH 302
SHEET 3 S1A 6 GLU A 68 GLY A 71 -1 N ALA A 69 O PRO A 91 6ADH 303
SHEET 4 S1A 6 VAL A 41 ILE A 45 -1 N ALA A 42 O ALA A 70 6ADH 304
SHEET 5 S1A 6 ARG A 369 PHE A 374 -1 N LEU A 372 O THR A 43 6ADH 305
SHEET 6 S1A 6 THR A 347 PHE A 352 1 N LEU A 350 O ILE A 371 6ADH 306
SHEET 1 S2A 4 GLY A 86 ASP A 87 0 6ADH 307
SHEET 2 S2A 4 ILE A 72 GLU A 78 -1 N VAL A 73 O ASP A 87 6ADH 308
SHEET 3 S2A 4 HIS A 34 MET A 40 -1 N ARG A 37 O SER A 75 6ADH 309
SHEET 4 S2A 4 GLN A 148 VAL A 152 -1 O VAL A 152 N VAL A 36 6ADH 310
SHEET 1 S3A 6 CYS A 9 LEU A 14 0 6ADH 311
SHEET 2 S3A 6 SER A 22 ALA A 29 -1 N ALA A 11 O GLU A 24 6ADH 312
SHEET 3 S3A 6 ARG A 129 CYS A 132 -1 N GLU A 27 O THR A 131 6ADH 313
SHEET 4 S3A 6 LYS A 135 HIS A 138 -1 N CYS A 132 O LYS A 135 6ADH 314
SHEET 5 S3A 6 PRO A 62 ILE A 64 1 N HIS A 138 O PRO A 62 6ADH 315
SHEET 6 S3A 6 CYS A 9 LEU A 14 1 N VAL A 63 O LEU A 14 6ADH 316
SHEET 1 S4A 6 THR A 238 CYS A 240 0 6ADH 317
SHEET 2 S4A 6 ARG A 218 ILE A 224 1 N GLU A 239 O ILE A 219 6ADH 318
SHEET 3 S4A 6 SER A 193 LEU A 200 1 N ILE A 220 O CYS A 195 6ADH 319
SHEET 4 S4A 6 ASP A 263 ILE A 269 1 N ALA A 196 O PHE A 264 6ADH 320
SHEET 5 S4A 6 GLY A 287 GLY A 293 1 N GLU A 267 O VAL A 290 6ADH 321
SHEET 6 S4A 6 ARG A 312 ILE A 318 1 N SER A 289 O THR A 313 6ADH 322
SHEET 1 S1B 6 SER B 156 ILE B 160 0 6ADH 323
SHEET 2 S1B 6 LYS B 88 LEU B 92 -1 N ILE B 90 O ALA B 158 6ADH 324
SHEET 3 S1B 6 GLU B 68 GLY B 71 -1 N ALA B 69 O PRO B 91 6ADH 325
SHEET 4 S1B 6 VAL B 41 ILE B 45 -1 N ALA B 42 O ALA B 70 6ADH 326
SHEET 5 S1B 6 ARG B 369 PHE B 374 -1 N LEU B 372 O THR B 43 6ADH 327
SHEET 6 S1B 6 THR B 347 PHE B 352 1 N LEU B 350 O ILE B 371 6ADH 328
SHEET 1 S2B 4 GLY B 86 ASP B 87 0 6ADH 329
SHEET 2 S2B 4 ILE B 72 GLU B 78 -1 N VAL B 73 O ASP B 87 6ADH 330
SHEET 3 S2B 4 HIS B 34 MET B 40 -1 N ARG B 37 O SER B 75 6ADH 331
SHEET 4 S2B 4 GLN B 148 VAL B 152 -1 O VAL B 152 N VAL B 36 6ADH 332
SHEET 1 S3B 6 CYS B 9 LEU B 14 0 6ADH 333
SHEET 2 S3B 6 SER B 22 ALA B 29 -1 N ALA B 11 O GLU B 24 6ADH 334
SHEET 3 S3B 6 ARG B 129 CYS B 132 -1 N GLU B 27 O THR B 131 6ADH 335
SHEET 4 S3B 6 LYS B 135 HIS B 138 -1 N CYS B 132 O LYS B 135 6ADH 336
SHEET 5 S3B 6 PRO B 62 ILE B 64 1 N HIS B 138 O PRO B 62 6ADH 337
SHEET 6 S3B 6 CYS B 9 LEU B 14 1 N VAL B 63 O LEU B 14 6ADH 338
SHEET 1 S4B 6 THR B 238 CYS B 240 0 6ADH 339
SHEET 2 S4B 6 ARG B 218 ILE B 224 1 N GLU B 239 O ILE B 219 6ADH 340
SHEET 3 S4B 6 SER B 193 LEU B 200 1 N ILE B 220 O CYS B 195 6ADH 341
SHEET 4 S4B 6 ASP B 263 ILE B 269 1 N ALA B 196 O PHE B 264 6ADH 342
SHEET 5 S4B 6 GLY B 287 GLY B 293 1 N GLU B 267 O VAL B 290 6ADH 343
SHEET 6 S4B 6 ARG B 312 ILE B 318 1 N SER B 289 O THR B 313 6ADH 344
TURN 1 T1A LYS A 32 GLU A 35 6ADH 345
TURN 2 T2A VAL A 80 VAL A 83 IMMED. PREC. T3A 6ADH 346
TURN 3 T3A ARG A 84 ASP A 87 IMMED. FOLL. T2A 6ADH 347
TURN 4 T4A MET A 118 GLY A 121 6ADH 348
TURN 5 T5A CYS A 132 LYS A 135 6ADH 349
TURN 6 T6A PHE A 140 THR A 143 6ADH 350
TURN 7 T7A ASP A 153 SER A 156 6ADH 351
TURN 8 T8A PRO A 165 LYS A 168 6ADH 352
TURN 9 T9A THR A 190 SER A 193 6ADH 353
TURN 10 10A GLN A 244 LYS A 247 6ADH 354
TURN 11 11A SER A 258 GLY A 261 6ADH 355
TURN 12 12A GLN A 283 TYR A 286 6ADH 356
TURN 13 13A PRO A 295 SER A 298 6ADH 357
TURN 14 14A PHE A 319 PHE A 322 6ADH 358
TURN 15 15A LYS A 338 ALA A 341 6ADH 359
TURN 16 16A PRO A 344 THR A 347 6ADH 360
TURN 17 17A PRO A 351 LYS A 354 6ADH 361
TURN 18 T1B LYS B 32 GLU B 35 6ADH 362
TURN 19 T2B VAL B 80 VAL B 83 IMMED. PREC. T3B 6ADH 363
TURN 20 T3B ARG B 84 ASP B 87 IMMED. FOLL. T2B 6ADH 364
TURN 21 T4B MET B 118 GLY B 121 6ADH 365
TURN 22 T5B CYS B 132 LYS B 135 6ADH 366
TURN 23 T6B PHE B 140 THR B 143 6ADH 367
TURN 24 T7B ASP B 153 SER B 156 6ADH 368
TURN 25 T8B PRO B 165 LYS B 168 6ADH 369
TURN 26 T9B THR B 190 SER B 193 6ADH 370
TURN 27 10B GLN B 244 LYS B 247 6ADH 371
TURN 28 11B SER B 258 GLY B 261 6ADH 372
TURN 29 12B GLN B 283 TYR B 286 6ADH 373
TURN 30 13B PRO B 295 SER B 298 6ADH 374
TURN 31 14B PHE B 319 PHE B 322 6ADH 375
TURN 32 15B LYS B 338 ALA B 341 6ADH 376
TURN 33 16B PRO B 344 THR B 347 6ADH 377
TURN 34 17B PRO B 351 LYS B 354 6ADH 378
SITE 1 DMA 8 CYS A 46 SER A 48 HIS A 67 PHE A 93 6ADH 379
SITE 2 DMA 8 LEU A 141 CYS A 174 ZN A 1 NAD A 3 6ADH 380
SITE 1 DMB 8 CYS B 46 SER B 48 HIS B 67 PHE B 93 6ADH 381
SITE 2 DMB 8 LEU B 141 CYS B 174 ZN B 1 NAD B 3 6ADH 382
SITE 1 NAA 20 ARG A 47 HIS A 51 THR A 178 PHE A 198 6ADH 383
SITE 2 NAA 20 GLY A 199 LEU A 200 GLY A 202 VAL A 203 6ADH 384
SITE 3 NAA 20 VAL A 222 ASP A 223 ILE A 224 LYS A 228 6ADH 385
SITE 4 NAA 20 ILE A 269 GLY A 270 ARG A 271 VAL A 292 6ADH 386
SITE 5 NAA 20 GLY A 293 VAL A 294 PHE A 319 ARG A 369 6ADH 387
SITE 1 NAB 20 ARG B 47 HIS B 51 THR B 178 PHE B 198 6ADH 388
SITE 2 NAB 20 GLY B 199 LEU B 200 GLY B 202 VAL B 203 6ADH 389
SITE 3 NAB 20 VAL B 222 ASP B 223 ILE B 224 LYS B 228 6ADH 390
SITE 4 NAB 20 ILE B 269 GLY B 270 ARG B 271 VAL B 292 6ADH 391
SITE 5 NAB 20 GLY B 293 VAL B 294 PHE B 319 ARG B 369 6ADH 392
CRYST1 52.000 44.600 94.400 104.40 101.90 70.70 P 1 2 6ADH 393
ORIGX1 1.000000 0.000000 0.000000 0.00000 6ADH 394
ORIGX2 0.000000 1.000000 0.000000 0.00000 6ADH 395
ORIGX3 0.000000 0.000000 1.000000 0.00000 6ADH 396
SCALE1 .019230 -.006730 .002790 0.00000 6ADH 397
SCALE2 0.000000 .023760 .004740 0.00000 6ADH 398
SCALE3 0.000000 0.000000 .011040 0.00000 6ADH 399
ATOM 1 N SER A 1 -1.378 15.208 -4.758 0.00 16.70 2 6ADH 400
ATOM 2 CA SER A 1 -2.113 16.041 -3.850 1.00 16.70 6ADH 401
ATOM 3 C SER A 1 -2.147 17.544 -4.077 0.00 16.70 2 6ADH 402
ATOM 4 O SER A 1 -1.579 18.044 -5.065 0.00 16.70 2 6ADH 403
ATOM 5 CB SER A 1 -1.575 15.919 -2.426 0.00 16.70 2 6ADH 404
ATOM 6 OG SER A 1 -.170 16.120 -2.419 0.00 16.70 2 6ADH 405
ATOM 7 N THR A 2 -2.855 17.977 -3.016 0.00 16.70 2 6ADH 406
ATOM 8 CA THR A 2 -3.410 19.302 -2.636 1.00 16.70 6ADH 407
ATOM 9 C THR A 2 -4.864 19.247 -3.091 1.00 16.70 6ADH 408
ATOM 10 O THR A 2 -5.254 18.358 -3.864 1.00 16.70 6ADH 409
ATOM 11 CB THR A 2 -2.642 20.483 -3.216 0.00 16.70 2 6ADH 410
ATOM 12 OG1 THR A 2 -2.240 21.350 -2.163 0.00 16.70 2 6ADH 411
ATOM 13 CG2 THR A 2 -3.473 21.316 -4.195 0.00 16.70 2 6ADH 412
ATOM 14 N ALA A 3 -5.728 20.157 -2.640 1.00 16.70 6ADH 413
ATOM 15 CA ALA A 3 -7.108 20.035 -3.129 1.00 16.70 6ADH 414
ATOM 16 C ALA A 3 -8.217 20.825 -2.427 1.00 16.70 6ADH 415
ATOM 17 O ALA A 3 -8.010 21.983 -2.035 1.00 16.70 6ADH 416
ATOM 18 CB ALA A 3 -7.581 18.586 -2.962 1.00 16.70 6ADH 417
ATOM 19 N GLY A 4 -9.240 19.950 -2.454 1.00 16.70 6ADH 418
ATOM 20 CA GLY A 4 -10.601 19.989 -1.943 1.00 16.70 6ADH 419
ATOM 21 C GLY A 4 -11.064 18.489 -1.755 1.00 16.70 6ADH 420
ATOM 22 O GLY A 4 -11.736 18.136 -.775 1.00 16.70 6ADH 421
ATOM 23 N LYS A 5 -10.702 17.565 -2.693 1.00 16.70 6ADH 422
ATOM 24 CA LYS A 5 -11.084 16.103 -2.555 1.00 16.70 6ADH 423
ATOM 25 C LYS A 5 -9.888 15.227 -2.081 1.00 16.70 6ADH 424
ATOM 26 O LYS A 5 -8.811 15.736 -1.742 1.00 16.70 6ADH 425
ATOM 27 CB LYS A 5 -11.641 15.510 -3.858 0.00 16.70 2 6ADH 426
ATOM 28 CG LYS A 5 -12.695 14.416 -3.612 0.00 16.70 2 6ADH 427
ATOM 29 CD LYS A 5 -14.136 14.904 -3.810 0.00 16.70 2 6ADH 428
ATOM 30 CE LYS A 5 -15.065 13.819 -4.366 0.00 16.70 2 6ADH 429
ATOM 31 NZ LYS A 5 -15.764 13.064 -3.316 0.00 16.70 2 6ADH 430
ATOM 32 N VAL A 6 -10.139 13.929 -2.095 1.00 16.70 6ADH 431
ATOM 33 CA VAL A 6 -9.245 12.863 -1.572 1.00 16.70 6ADH 432
ATOM 34 C VAL A 6 -7.760 12.953 -2.086 1.00 16.70 6ADH 433
ATOM 35 O VAL A 6 -7.487 12.805 -3.284 1.00 16.70 6ADH 434
ATOM 36 CB VAL A 6 -9.898 11.525 -1.957 1.00 16.70 6ADH 435
ATOM 37 CG1 VAL A 6 -9.071 10.302 -1.560 1.00 16.70 6ADH 436
ATOM 38 CG2 VAL A 6 -11.270 11.324 -1.303 1.00 16.70 6ADH 437
ATOM 39 N ILE A 7 -6.839 13.203 -1.121 1.00 16.70 6ADH 438
ATOM 40 CA ILE A 7 -5.360 13.201 -1.339 1.00 16.70 6ADH 439
ATOM 41 C ILE A 7 -4.885 11.752 -1.203 1.00 16.70 6ADH 440
ATOM 42 O ILE A 7 -5.349 11.014 -.322 1.00 16.70 6ADH 441
ATOM 43 CB ILE A 7 -4.634 14.032 -.257 1.00 16.70 6ADH 442
ATOM 44 CG1 ILE A 7 -5.084 15.494 -.214 1.00 16.70 6ADH 443
ATOM 45 CG2 ILE A 7 -3.114 14.077 -.445 1.00 16.70 6ADH 444
ATOM 46 CD1 ILE A 7 -4.115 16.441 -.921 1.00 16.70 6ADH 445
ATOM 47 N LYS A 8 -3.979 11.362 -2.074 1.00 16.70 6ADH 446
ATOM 48 CA LYS A 8 -3.417 9.999 -2.068 1.00 16.70 6ADH 447
ATOM 49 C LYS A 8 -1.917 10.081 -1.805 1.00 16.70 6ADH 448
ATOM 50 O LYS A 8 -1.105 10.104 -2.736 1.00 16.70 6ADH 449
ATOM 51 CB LYS A 8 -3.619 9.333 -3.438 1.00 16.70 6ADH 450
ATOM 52 CG LYS A 8 -3.655 7.799 -3.365 1.00 16.70 6ADH 451
ATOM 53 CD LYS A 8 -2.439 7.130 -4.016 1.00 16.70 6ADH 452
ATOM 54 CE LYS A 8 -2.328 5.635 -3.692 1.00 16.70 6ADH 453
ATOM 55 NZ LYS A 8 -.968 5.106 -3.878 1.00 16.70 6ADH 454
ATOM 56 N CYS A 9 -1.563 10.109 -.545 1.00 16.70 6ADH 455
ATOM 57 CA CYS A 9 -.161 10.272 -.121 1.00 16.70 6ADH 456
ATOM 58 C CYS A 9 .434 8.994 .489 1.00 16.70 6ADH 457
ATOM 59 O CYS A 9 -.094 7.890 .298 1.00 16.70 6ADH 458
ATOM 60 CB CYS A 9 -.092 11.324 1.000 1.00 16.70 6ADH 459
ATOM 61 SG CYS A 9 -.752 10.672 2.609 1.00 16.70 6ADH 460
ATOM 62 N LYS A 10 1.530 9.222 1.219 1.00 16.70 6ADH 461
ATOM 63 CA LYS A 10 2.322 8.171 1.906 1.00 16.70 6ADH 462
ATOM 64 C LYS A 10 2.245 8.323 3.430 1.00 16.70 6ADH 463
ATOM 65 O LYS A 10 2.051 9.430 3.950 1.00 16.70 6ADH 464
ATOM 66 CB LYS A 10 3.782 8.313 1.535 1.00 16.70 6ADH 465
ATOM 67 CG LYS A 10 4.646 7.199 2.099 1.00 16.70 6ADH 466
ATOM 68 CD LYS A 10 5.609 6.642 1.060 1.00 16.70 6ADH 467
ATOM 69 CE LYS A 10 5.048 6.710 -.359 1.00 16.70 6ADH 468
ATOM 70 NZ LYS A 10 4.971 5.393 -1.006 1.00 16.70 6ADH 469
ATOM 71 N ALA A 11 2.424 7.202 4.128 1.00 16.70 6ADH 470
ATOM 72 CA ALA A 11 2.301 7.162 5.603 1.00 16.70 6ADH 471
ATOM 73 C ALA A 11 3.047 5.954 6.188 1.00 16.70 6ADH 472
ATOM 74 O ALA A 11 3.656 5.162 5.458 1.00 16.70 6ADH 473
ATOM 75 CB ALA A 11 .826 7.027 5.978 1.00 16.70 6ADH 474
ATOM 76 N ALA A 12 2.982 5.824 7.504 1.00 16.70 6ADH 475
ATOM 77 CA ALA A 12 3.617 4.697 8.210 1.00 16.70 6ADH 476
ATOM 78 C ALA A 12 2.620 4.091 9.187 1.00 16.70 6ADH 477
ATOM 79 O ALA A 12 2.510 4.528 10.342 1.00 16.70 6ADH 478
ATOM 80 CB ALA A 12 4.861 5.172 8.960 1.00 16.70 6ADH 479
ATOM 81 N VAL A 13 1.948 3.109 8.648 1.00 16.70 6ADH 480
ATOM 82 CA VAL A 13 .903 2.367 9.326 1.00 16.70 6ADH 481
ATOM 83 C VAL A 13 1.514 1.191 10.128 1.00 16.70 6ADH 482
ATOM 84 O VAL A 13 2.381 .458 9.623 1.00 16.70 6ADH 483
ATOM 85 CB VAL A 13 -.085 1.880 8.242 1.00 16.70 6ADH 484
ATOM 86 CG1 VAL A 13 -.619 .468 8.486 1.00 16.70 6ADH 485
ATOM 87 CG2 VAL A 13 -1.326 2.769 8.115 1.00 16.70 6ADH 486
ATOM 88 N LEU A 14 1.045 1.089 11.372 1.00 16.70 6ADH 487
ATOM 89 CA LEU A 14 1.319 -.049 12.270 1.00 16.70 6ADH 488
ATOM 90 C LEU A 14 .168 -.981 11.942 1.00 16.70 6ADH 489
ATOM 91 O LEU A 14 -.990 -.559 11.826 1.00 16.70 6ADH 490
ATOM 92 CB LEU A 14 1.260 .427 13.754 1.00 16.70 6ADH 491
ATOM 93 CG LEU A 14 2.348 -.148 14.694 1.00 16.70 6ADH 492
ATOM 94 CD1 LEU A 14 1.802 -.562 16.064 1.00 16.70 6ADH 493
ATOM 95 CD2 LEU A 14 3.044 -1.393 14.142 1.00 16.70 6ADH 494
ATOM 96 N TRP A 15 .415 -2.216 11.749 1.00 16.70 6ADH 495
ATOM 97 CA TRP A 15 -.683 -3.106 11.416 1.00 16.70 6ADH 496
ATOM 98 C TRP A 15 -.802 -4.108 12.519 1.00 16.70 6ADH 497
ATOM 99 O TRP A 15 -1.783 -4.861 12.601 1.00 16.70 6ADH 498
ATOM 100 CB TRP A 15 -.374 -3.857 10.107 1.00 16.70 6ADH 499
ATOM 101 CG TRP A 15 -.695 -3.091 8.801 1.00 16.70 6ADH 500
ATOM 102 CD1 TRP A 15 .181 -2.697 7.860 1.00 16.70 6ADH 501
ATOM 103 CD2 TRP A 15 -1.989 -2.682 8.369 1.00 16.70 6ADH 502
ATOM 104 NE1 TRP A 15 -.568 -2.066 6.813 1.00 16.70 6ADH 503
ATOM 105 CE2 TRP A 15 -1.838 -2.079 7.124 1.00 16.70 6ADH 504
ATOM 106 CE3 TRP A 15 -3.271 -2.791 8.920 1.00 16.70 6ADH 505
ATOM 107 CZ2 TRP A 15 -2.914 -1.599 6.368 1.00 16.70 6ADH 506
ATOM 108 CZ3 TRP A 15 -4.349 -2.292 8.157 1.00 16.70 6ADH 507
ATOM 109 CH2 TRP A 15 -4.179 -1.727 6.940 1.00 16.70 6ADH 508
ATOM 110 N GLU A 16 .215 -4.059 13.332 1.00 16.70 6ADH 509
ATOM 111 CA GLU A 16 .367 -5.054 14.342 1.00 16.70 6ADH 510
ATOM 112 C GLU A 16 1.435 -4.629 15.348 1.00 16.70 6ADH 511
ATOM 113 O GLU A 16 2.500 -4.115 14.972 1.00 16.70 6ADH 512
ATOM 114 CB GLU A 16 .653 -6.330 13.542 0.00 16.70 2 6ADH 513
ATOM 115 CG GLU A 16 1.348 -7.462 14.269 0.00 16.70 2 6ADH 514
ATOM 116 CD GLU A 16 1.481 -8.688 13.358 0.00 16.70 2 6ADH 515
ATOM 117 OE1 GLU A 16 1.630 -9.862 13.871 0.00 16.70 2 6ADH 516
ATOM 118 OE2 GLU A 16 1.440 -8.548 12.075 0.00 16.70 2 6ADH 517
ATOM 119 N GLU A 17 1.004 -4.889 16.560 1.00 16.70 6ADH 518
ATOM 120 CA GLU A 17 1.712 -4.668 17.819 1.00 16.70 6ADH 519
ATOM 121 C GLU A 17 3.017 -5.490 17.878 1.00 16.70 6ADH 520
ATOM 122 O GLU A 17 2.989 -6.719 18.027 1.00 16.70 6ADH 521
ATOM 123 CB GLU A 17 .811 -5.177 18.959 0.00 16.70 2 6ADH 522
ATOM 124 CG GLU A 17 .617 -4.193 20.112 0.00 16.70 2 6ADH 523
ATOM 125 CD GLU A 17 -.451 -4.661 21.110 0.00 16.70 2 6ADH 524
ATOM 126 OE1 GLU A 17 -1.517 -3.958 21.291 0.00 16.70 2 6ADH 525
ATOM 127 OE2 GLU A 17 -.285 -5.759 21.767 0.00 16.70 2 6ADH 526
ATOM 128 N LYS A 18 4.125 -4.767 17.752 1.00 16.70 6ADH 527
ATOM 129 CA LYS A 18 5.497 -5.320 17.870 1.00 16.70 6ADH 528
ATOM 130 C LYS A 18 6.184 -5.506 16.527 1.00 16.70 6ADH 529
ATOM 131 O LYS A 18 7.254 -6.123 16.429 1.00 16.70 6ADH 530
ATOM 132 CB LYS A 18 5.494 -6.694 18.550 1.00 16.70 6ADH 531
ATOM 133 CG LYS A 18 5.295 -6.618 20.071 1.00 16.70 6ADH 532
ATOM 134 CD LYS A 18 6.501 -7.129 20.869 1.00 16.70 6ADH 533
ATOM 135 CE LYS A 18 6.113 -8.076 22.008 1.00 16.70 6ADH 534
ATOM 136 NZ LYS A 18 6.294 -9.495 21.665 1.00 16.70 6ADH 535
ATOM 137 N LYS A 19 5.600 -4.993 15.498 1.00 16.70 6ADH 536
ATOM 138 CA LYS A 19 6.229 -5.096 14.193 1.00 16.70 6ADH 537
ATOM 139 C LYS A 19 6.629 -3.710 13.743 1.00 16.70 6ADH 538
ATOM 140 O LYS A 19 6.070 -2.709 14.214 1.00 16.70 6ADH 539
ATOM 141 CB LYS A 19 5.270 -5.758 13.235 1.00 16.70 6ADH 540
ATOM 142 CG LYS A 19 4.719 -7.046 13.829 1.00 16.70 6ADH 541
ATOM 143 CD LYS A 19 4.050 -7.931 12.796 1.00 16.70 6ADH 542
ATOM 144 CE LYS A 19 4.872 -9.159 12.425 1.00 16.70 6ADH 543
ATOM 145 NZ LYS A 19 4.043 -10.360 12.251 1.00 16.70 6ADH 544
ATOM 146 N PRO A 20 7.620 -3.585 12.841 1.00 16.70 6ADH 545
ATOM 147 CA PRO A 20 8.039 -2.285 12.345 1.00 16.70 6ADH 546
ATOM 148 C PRO A 20 6.898 -1.651 11.593 1.00 16.70 6ADH 547
ATOM 149 O PRO A 20 5.776 -2.241 11.564 1.00 16.70 6ADH 548
ATOM 150 CB PRO A 20 9.190 -2.596 11.423 1.00 16.70 6ADH 549
ATOM 151 CG PRO A 20 9.376 -4.106 11.402 1.00 16.70 6ADH 550
ATOM 152 CD PRO A 20 8.340 -4.733 12.283 1.00 16.70 6ADH 551
ATOM 153 N PHE A 21 7.167 -.498 11.001 1.00 16.70 6ADH 552
ATOM 154 CA PHE A 21 6.146 .253 10.242 1.00 16.70 6ADH 553
ATOM 155 C PHE A 21 6.248 -.011 8.746 1.00 16.70 6ADH 554
ATOM 156 O PHE A 21 7.348 -.133 8.189 1.00 16.70 6ADH 555
ATOM 157 CB PHE A 21 6.317 1.764 10.420 1.00 16.70 6ADH 556
ATOM 158 CG PHE A 21 5.832 2.283 11.774 1.00 16.70 6ADH 557
ATOM 159 CD1 PHE A 21 6.736 2.400 12.834 1.00 16.70 6ADH 558
ATOM 160 CD2 PHE A 21 4.491 2.646 11.954 1.00 16.70 6ADH 559
ATOM 161 CE1 PHE A 21 6.303 2.878 14.075 1.00 16.70 6ADH 560
ATOM 162 CE2 PHE A 21 4.056 3.126 13.196 1.00 16.70 6ADH 561
ATOM 163 CZ PHE A 21 4.963 3.243 14.257 1.00 16.70 6ADH 562
ATOM 164 N SER A 22 5.083 -.085 8.167 1.00 16.70 6ADH 563
ATOM 165 CA SER A 22 4.923 -.258 6.742 1.00 16.70 6ADH 564
ATOM 166 C SER A 22 4.681 1.114 6.134 1.00 16.70 6ADH 565
ATOM 167 O SER A 22 3.589 1.685 6.277 1.00 16.70 6ADH 566
ATOM 168 CB SER A 22 3.699 -1.149 6.468 1.00 16.70 6ADH 567
ATOM 169 OG SER A 22 4.001 -2.111 5.468 1.00 16.70 6ADH 568
ATOM 170 N ILE A 23 5.702 1.663 5.485 1.00 16.70 6ADH 569
ATOM 171 CA ILE A 23 5.500 2.921 4.758 1.00 16.70 6ADH 570
ATOM 172 C ILE A 23 4.608 2.533 3.587 1.00 16.70 6ADH 571
ATOM 173 O ILE A 23 4.884 1.557 2.874 1.00 16.70 6ADH 572
ATOM 174 CB ILE A 23 6.834 3.543 4.328 1.00 16.70 6ADH 573
ATOM 175 CG1 ILE A 23 7.772 3.834 5.504 1.00 16.70 6ADH 574
ATOM 176 CG2 ILE A 23 6.658 4.882 3.606 1.00 16.70 6ADH 575
ATOM 177 CD1 ILE A 23 8.782 4.945 5.205 1.00 16.70 6ADH 576
ATOM 178 N GLU A 24 3.550 3.295 3.414 1.00 16.70 6ADH 577
ATOM 179 CA GLU A 24 2.529 2.941 2.432 1.00 16.70 6ADH 578
ATOM 180 C GLU A 24 1.791 4.124 1.821 1.00 16.70 6ADH 579
ATOM 181 O GLU A 24 2.081 5.286 2.155 1.00 16.70 6ADH 580
ATOM 182 CB GLU A 24 1.409 2.137 3.104 1.00 16.70 6ADH 581
ATOM 183 CG GLU A 24 1.906 1.020 4.018 1.00 16.70 6ADH 582
ATOM 184 CD GLU A 24 1.113 -.277 3.836 1.00 16.70 6ADH 583
ATOM 185 OE1 GLU A 24 -.168 -.236 3.684 1.00 16.70 6ADH 584
ATOM 186 OE2 GLU A 24 1.724 -1.412 3.834 1.00 16.70 6ADH 585
ATOM 187 N GLU A 25 .882 3.659 .953 1.00 16.70 6ADH 586
ATOM 188 CA GLU A 25 -.129 4.446 .240 1.00 16.70 6ADH 587
ATOM 189 C GLU A 25 -1.429 4.361 1.043 1.00 16.70 6ADH 588
ATOM 190 O GLU A 25 -1.955 3.264 1.279 1.00 16.70 6ADH 589
ATOM 191 CB GLU A 25 -.498 3.811 -1.119 0.00 16.70 2 6ADH 590
ATOM 192 CG GLU A 25 .613 3.812 -2.166 0.00 16.70 2 6ADH 591
ATOM 193 CD GLU A 25 .500 2.633 -3.143 0.00 16.70 2 6ADH 592
ATOM 194 OE1 GLU A 25 1.549 1.949 -3.452 0.00 16.70 2 6ADH 593
ATOM 195 OE2 GLU A 25 -.644 2.322 -3.655 0.00 16.70 2 6ADH 594
ATOM 196 N VAL A 26 -1.916 5.506 1.447 1.00 16.70 6ADH 595
ATOM 197 CA VAL A 26 -3.188 5.641 2.197 1.00 16.70 6ADH 596
ATOM 198 C VAL A 26 -3.955 6.774 1.511 1.00 16.70 6ADH 597
ATOM 199 O VAL A 26 -3.386 7.588 .775 1.00 16.70 6ADH 598
ATOM 200 CB VAL A 26 -2.876 6.008 3.656 1.00 16.70 6ADH 599
ATOM 201 CG1 VAL A 26 -1.965 4.994 4.352 1.00 16.70 6ADH 600
ATOM 202 CG2 VAL A 26 -2.169 7.359 3.799 1.00 16.70 6ADH 601
ATOM 203 N GLU A 27 -5.241 6.930 1.673 1.00 16.70 6ADH 602
ATOM 204 CA GLU A 27 -5.872 8.080 .985 1.00 16.70 6ADH 603
ATOM 205 C GLU A 27 -6.742 8.875 2.033 1.00 16.70 6ADH 604
ATOM 206 O GLU A 27 -7.769 8.380 2.518 1.00 16.70 6ADH 605
ATOM 207 CB GLU A 27 -6.496 7.568 -.365 1.00 16.70 6ADH 606
ATOM 208 CG GLU A 27 -7.932 6.999 -.284 1.00 16.70 6ADH 607
ATOM 209 CD GLU A 27 -8.105 5.614 -.951 1.00 16.70 6ADH 608
ATOM 210 OE1 GLU A 27 -7.141 4.756 -.925 1.00 16.70 6ADH 609
ATOM 211 OE2 GLU A 27 -9.215 5.306 -1.536 1.00 16.70 6ADH 610
ATOM 212 N VAL A 28 -6.223 10.107 2.333 1.00 16.70 6ADH 611
ATOM 213 CA VAL A 28 -6.771 11.097 3.323 1.00 16.70 6ADH 612
ATOM 214 C VAL A 28 -7.881 11.914 2.690 1.00 16.70 6ADH 613
ATOM 215 O VAL A 28 -7.657 12.672 1.734 1.00 16.70 6ADH 614
ATOM 216 CB VAL A 28 -5.665 12.057 3.780 1.00 16.70 6ADH 615
ATOM 217 CG1 VAL A 28 -5.757 12.429 5.262 1.00 16.70 6ADH 616
ATOM 218 CG2 VAL A 28 -4.262 11.479 3.587 1.00 16.70 6ADH 617
ATOM 219 N ALA A 29 -9.034 11.716 3.249 1.00 16.70 6ADH 618
ATOM 220 CA ALA A 29 -10.235 12.337 2.758 1.00 16.70 6ADH 619
ATOM 221 C ALA A 29 -10.240 13.794 3.098 1.00 16.70 6ADH 620
ATOM 222 O ALA A 29 -9.706 14.204 4.148 1.00 16.70 6ADH 621
ATOM 223 CB ALA A 29 -11.467 11.674 3.372 1.00 16.70 6ADH 622
ATOM 224 N PRO A 30 -10.873 14.583 2.241 1.00 16.70 6ADH 623
ATOM 225 CA PRO A 30 -10.934 16.009 2.453 1.00 16.70 6ADH 624
ATOM 226 C PRO A 30 -11.582 16.259 3.806 1.00 16.70 6ADH 625
ATOM 227 O PRO A 30 -12.422 15.411 4.237 1.00 16.70 6ADH 626
ATOM 228 CB PRO A 30 -11.812 16.490 1.321 1.00 16.70 6ADH 627
ATOM 229 CG PRO A 30 -12.218 15.283 .489 1.00 16.70 6ADH 628
ATOM 230 CD PRO A 30 -11.574 14.064 1.058 1.00 16.70 6ADH 629
ATOM 231 N PRO A 31 -11.287 17.376 4.569 1.00 16.70 6ADH 630
ATOM 232 CA PRO A 31 -11.886 17.618 5.884 1.00 16.70 6ADH 631
ATOM 233 C PRO A 31 -13.368 17.797 5.884 1.00 16.70 6ADH 632
ATOM 234 O PRO A 31 -13.946 18.127 4.800 0.00 16.70 2 6ADH 633
ATOM 235 CB PRO A 31 -11.282 18.899 6.386 1.00 16.70 6ADH 634
ATOM 236 CG PRO A 31 -10.327 19.399 5.317 1.00 16.70 6ADH 635
ATOM 237 CD PRO A 31 -10.326 18.423 4.177 1.00 16.70 6ADH 636
ATOM 238 N LYS A 32 -13.815 17.576 7.113 1.00 16.70 6ADH 637
ATOM 239 CA LYS A 32 -15.204 17.622 7.543 1.00 16.70 6ADH 638
ATOM 240 C LYS A 32 -15.384 18.712 8.606 1.00 16.70 6ADH 639
ATOM 241 O LYS A 32 -14.815 18.618 9.708 0.00 16.70 2 6ADH 640
ATOM 242 CB LYS A 32 -15.596 16.264 8.124 1.00 16.70 6ADH 641
ATOM 243 CG LYS A 32 -16.679 15.548 7.315 1.00 16.70 6ADH 642
ATOM 244 CD LYS A 32 -17.421 14.489 8.131 0.00 16.70 2 6ADH 643
ATOM 245 CE LYS A 32 -18.001 13.365 7.270 0.00 16.70 2 6ADH 644
ATOM 246 NZ LYS A 32 -17.798 12.030 7.853 0.00 16.70 2 6ADH 645
ATOM 247 N ALA A 33 -16.186 19.674 8.153 1.00 16.70 6ADH 646
ATOM 248 CA ALA A 33 -16.589 20.878 8.889 1.00 16.70 6ADH 647
ATOM 249 C ALA A 33 -15.912 20.915 10.244 1.00 16.70 6ADH 648
ATOM 250 O ALA A 33 -16.172 20.061 11.105 0.00 16.70 2 6ADH 649
ATOM 251 CB ALA A 33 -18.107 20.887 9.083 1.00 16.70 6ADH 650
ATOM 252 N HIS A 34 -15.061 21.910 10.361 1.00 16.70 6ADH 651
ATOM 253 CA HIS A 34 -14.286 22.180 11.578 1.00 16.70 6ADH 652
ATOM 254 C HIS A 34 -13.046 21.325 11.677 1.00 16.70 6ADH 653
ATOM 255 O HIS A 34 -12.497 21.117 12.767 1.00 16.70 6ADH 654
ATOM 256 CB HIS A 34 -15.068 21.843 12.831 1.00 16.70 6ADH 655
ATOM 257 CG HIS A 34 -16.198 22.811 13.107 1.00 16.70 6ADH 656
ATOM 258 ND1 HIS A 34 -17.503 22.371 13.244 1.00 16.70 6ADH 657
ATOM 259 CD2 HIS A 34 -16.219 24.158 13.268 1.00 16.70 6ADH 658
ATOM 260 CE1 HIS A 34 -18.263 23.423 13.476 1.00 16.70 6ADH 659
ATOM 261 NE2 HIS A 34 -17.512 24.499 13.493 1.00 16.70 6ADH 660
ATOM 262 N GLU A 35 -12.618 20.818 10.569 1.00 16.70 6ADH 661
ATOM 263 CA GLU A 35 -11.389 20.057 10.552 1.00 16.70 6ADH 662
ATOM 264 C GLU A 35 -10.435 20.748 9.651 1.00 16.70 6ADH 663
ATOM 265 O GLU A 35 -10.819 21.635 8.875 1.00 16.70 6ADH 664
ATOM 266 CB GLU A 35 -11.619 18.647 10.105 1.00 16.70 6ADH 665
ATOM 267 CG GLU A 35 -11.945 17.741 11.272 1.00 16.70 6ADH 666
ATOM 268 CD GLU A 35 -12.741 16.530 10.833 1.00 16.70 6ADH 667
ATOM 269 OE1 GLU A 35 -12.342 15.837 9.823 1.00 16.70 6ADH 668
ATOM 270 OE2 GLU A 35 -13.811 16.199 11.471 1.00 16.70 6ADH 669
ATOM 271 N VAL A 36 -9.233 20.321 9.768 1.00 16.70 6ADH 670
ATOM 272 CA VAL A 36 -8.172 20.997 9.107 1.00 16.70 6ADH 671
ATOM 273 C VAL A 36 -7.053 20.023 8.764 1.00 16.70 6ADH 672
ATOM 274 O VAL A 36 -6.202 19.709 9.611 0.00 16.70 2 6ADH 673
ATOM 275 CB VAL A 36 -7.731 22.096 10.079 1.00 16.70 6ADH 674
ATOM 276 CG1 VAL A 36 -6.331 22.637 9.796 1.00 16.70 6ADH 675
ATOM 277 CG2 VAL A 36 -8.659 23.313 10.063 1.00 16.70 6ADH 676
ATOM 278 N ARG A 37 -7.094 19.557 7.511 1.00 16.70 6ADH 677
ATOM 279 CA ARG A 37 -6.030 18.688 6.995 1.00 16.70 6ADH 678
ATOM 280 C ARG A 37 -4.833 19.633 6.752 1.00 16.70 6ADH 679
ATOM 281 O ARG A 37 -4.998 20.747 6.229 1.00 16.70 6ADH 680
ATOM 282 CB ARG A 37 -6.562 17.746 5.843 1.00 16.70 6ADH 681
ATOM 283 CG ARG A 37 -6.597 18.301 4.396 1.00 16.70 6ADH 682
ATOM 284 CD ARG A 37 -5.813 17.431 3.360 1.00 16.70 6ADH 683
ATOM 285 NE ARG A 37 -6.585 16.333 2.693 1.00 16.70 6ADH 684
ATOM 286 CZ ARG A 37 -7.345 16.475 1.579 1.00 16.70 6ADH 685
ATOM 287 NH1 ARG A 37 -7.494 17.669 .988 1.00 16.70 6ADH 686
ATOM 288 NH2 ARG A 37 -7.981 15.465 .967 1.00 16.70 6ADH 687
ATOM 289 N ILE A 38 -3.705 19.080 7.193 1.00 16.70 6ADH 688
ATOM 290 CA ILE A 38 -2.388 19.742 7.302 1.00 16.70 6ADH 689
ATOM 291 C ILE A 38 -1.267 18.953 6.567 1.00 16.70 6ADH 690
ATOM 292 O ILE A 38 -1.024 17.775 6.861 1.00 16.70 6ADH 691
ATOM 293 CB ILE A 38 -2.006 19.730 8.801 1.00 16.70 6ADH 692
ATOM 294 CG1 ILE A 38 -2.920 20.587 9.688 1.00 16.70 6ADH 693
ATOM 295 CG2 ILE A 38 -.588 20.231 9.074 1.00 16.70 6ADH 694
ATOM 296 CD1 ILE A 38 -3.017 20.067 11.126 1.00 16.70 6ADH 695
ATOM 297 N LYS A 39 -.583 19.621 5.624 1.00 16.70 6ADH 696
ATOM 298 CA LYS A 39 .571 19.027 4.867 1.00 16.70 6ADH 697
ATOM 299 C LYS A 39 1.829 18.962 5.764 1.00 16.70 6ADH 698
ATOM 300 O LYS A 39 2.465 19.985 6.052 1.00 16.70 6ADH 699
ATOM 301 CB LYS A 39 .938 19.888 3.653 1.00 16.70 6ADH 700
ATOM 302 CG LYS A 39 2.393 19.693 3.202 1.00 16.70 6ADH 701
ATOM 303 CD LYS A 39 2.511 19.062 1.810 1.00 16.70 6ADH 702
ATOM 304 CE LYS A 39 3.956 18.738 1.415 1.00 16.70 6ADH 703
ATOM 305 NZ LYS A 39 4.916 19.761 1.853 1.00 16.70 6ADH 704
ATOM 306 N MET A 40 2.177 17.758 6.184 1.00 16.70 6ADH 705
ATOM 307 CA MET A 40 3.302 17.514 7.121 1.00 16.70 6ADH 706
ATOM 308 C MET A 40 4.692 17.781 6.519 1.00 16.70 6ADH 707
ATOM 309 O MET A 40 5.024 17.277 5.439 0.00 16.70 2 6ADH 708
ATOM 310 CB MET A 40 3.305 16.058 7.589 1.00 16.70 6ADH 709
ATOM 311 CG MET A 40 2.245 15.767 8.655 1.00 16.70 6ADH 710
ATOM 312 SD MET A 40 2.477 16.707 10.148 1.00 16.70 6ADH 711
ATOM 313 CE MET A 40 .922 16.902 10.991 1.00 16.70 6ADH 712
ATOM 314 N VAL A 41 5.418 18.566 7.313 1.00 16.70 6ADH 713
ATOM 315 CA VAL A 41 6.809 18.973 7.088 1.00 16.70 6ADH 714
ATOM 316 C VAL A 41 7.753 18.072 7.963 1.00 16.70 6ADH 715
ATOM 317 O VAL A 41 8.505 17.238 7.438 0.00 16.70 2 6ADH 716
ATOM 318 CB VAL A 41 6.956 20.469 7.439 1.00 16.70 6ADH 717
ATOM 319 CG1 VAL A 41 8.379 21.001 7.255 1.00 16.70 6ADH 718
ATOM 320 CG2 VAL A 41 6.067 21.374 6.582 1.00 16.70 6ADH 719
ATOM 321 N ALA A 42 7.701 18.233 9.314 1.00 16.70 6ADH 720
ATOM 322 CA ALA A 42 8.602 17.468 10.266 1.00 16.70 6ADH 721
ATOM 323 C ALA A 42 7.841 16.778 11.436 1.00 16.70 6ADH 722
ATOM 324 O ALA A 42 6.753 17.203 11.840 1.00 16.70 6ADH 723
ATOM 325 CB ALA A 42 9.611 18.417 10.915 1.00 16.70 6ADH 724
ATOM 326 N THR A 43 8.458 15.719 11.976 1.00 16.70 6ADH 725
ATOM 327 CA THR A 43 7.878 14.912 13.085 1.00 16.70 6ADH 726
ATOM 328 C THR A 43 8.936 14.548 14.123 1.00 16.70 6ADH 727
ATOM 329 O THR A 43 10.145 14.669 13.873 1.00 16.70 6ADH 728
ATOM 330 CB THR A 43 7.330 13.591 12.551 1.00 16.70 6ADH 729
ATOM 331 OG1 THR A 43 7.402 13.577 11.134 1.00 16.70 6ADH 730
ATOM 332 CG2 THR A 43 5.873 13.346 12.943 1.00 16.70 6ADH 731
ATOM 333 N GLY A 44 8.444 14.103 15.261 1.00 16.70 6ADH 732
ATOM 334 CA GLY A 44 9.301 13.723 16.382 1.00 16.70 6ADH 733
ATOM 335 C GLY A 44 8.970 12.320 16.871 1.00 16.70 6ADH 734
ATOM 336 O GLY A 44 7.795 11.916 16.897 1.00 16.70 6ADH 735
ATOM 337 N ILE A 45 10.047 11.643 17.234 1.00 16.70 6ADH 736
ATOM 338 CA ILE A 45 9.972 10.300 17.785 1.00 16.70 6ADH 737
ATOM 339 C ILE A 45 10.194 10.369 19.297 1.00 16.70 6ADH 738
ATOM 340 O ILE A 45 11.345 10.396 19.767 1.00 16.70 6ADH 739
ATOM 341 CB ILE A 45 10.945 9.353 17.077 1.00 16.70 6ADH 740
ATOM 342 CG1 ILE A 45 11.080 9.655 15.582 1.00 16.70 6ADH 741
ATOM 343 CG2 ILE A 45 10.515 7.884 17.162 1.00 16.70 6ADH 742
ATOM 344 CD1 ILE A 45 12.273 8.950 14.933 1.00 16.70 6ADH 743
ATOM 345 N CYS A 46 8.996 10.409 19.865 1.00 16.70 6ADH 744
ATOM 346 CA CYS A 46 8.666 10.354 21.281 1.00 16.70 6ADH 745
ATOM 347 C CYS A 46 8.693 8.867 21.630 1.00 16.70 6ADH 746
ATOM 348 O CYS A 46 8.923 8.015 20.760 1.00 16.70 6ADH 747
ATOM 349 CB CYS A 46 7.238 10.925 21.445 1.00 16.70 6ADH 748
ATOM 350 SG CYS A 46 6.890 11.653 23.115 1.00 16.70 6ADH 749
ATOM 351 N ARG A 47 8.468 8.555 22.878 1.00 16.70 6ADH 750
ATOM 352 CA ARG A 47 8.454 7.157 23.328 1.00 16.70 6ADH 751
ATOM 353 C ARG A 47 7.034 6.644 23.307 1.00 16.70 6ADH 752
ATOM 354 O ARG A 47 6.777 5.479 22.965 1.00 16.70 6ADH 753
ATOM 355 CB ARG A 47 8.977 7.059 24.756 1.00 16.70 6ADH 754
ATOM 356 CG ARG A 47 9.395 5.646 25.134 1.00 16.70 6ADH 755
ATOM 357 CD ARG A 47 10.499 5.120 24.229 1.00 16.70 6ADH 756
ATOM 358 NE ARG A 47 10.882 3.740 24.518 1.00 16.70 6ADH 757
ATOM 359 CZ ARG A 47 12.150 3.338 24.601 1.00 16.70 6ADH 758
ATOM 360 NH1 ARG A 47 13.157 4.207 24.432 1.00 16.70 6ADH 759
ATOM 361 NH2 ARG A 47 12.521 2.076 24.844 1.00 16.70 6ADH 760
ATOM 362 N SER A 48 6.167 7.549 23.680 1.00 16.70 6ADH 761
ATOM 363 CA SER A 48 4.744 7.284 23.716 1.00 16.70 6ADH 762
ATOM 364 C SER A 48 4.257 6.968 22.301 1.00 16.70 6ADH 763
ATOM 365 O SER A 48 3.059 6.768 22.064 1.00 16.70 6ADH 764
ATOM 366 CB SER A 48 3.997 8.489 24.287 1.00 16.70 6ADH 765
ATOM 367 OG SER A 48 3.517 8.187 25.590 1.00 16.70 6ADH 766
ATOM 368 N ASP A 49 5.193 6.934 21.378 1.00 16.70 6ADH 767
ATOM 369 CA ASP A 49 4.900 6.559 19.988 1.00 16.70 6ADH 768
ATOM 370 C ASP A 49 5.353 5.119 19.800 1.00 16.70 6ADH 769
ATOM 371 O ASP A 49 4.877 4.408 18.905 1.00 16.70 6ADH 770
ATOM 372 CB ASP A 49 5.653 7.469 19.012 1.00 16.70 6ADH 771
ATOM 373 CG ASP A 49 4.790 8.595 18.435 1.00 16.70 6ADH 772
ATOM 374 OD1 ASP A 49 5.329 9.512 17.706 1.00 16.70 6ADH 773
ATOM 375 OD2 ASP A 49 3.522 8.628 18.677 1.00 16.70 6ADH 774
ATOM 376 N ASP A 50 6.263 4.763 20.674 1.00 16.70 6ADH 775
ATOM 377 CA ASP A 50 6.859 3.439 20.717 1.00 16.70 6ADH 776
ATOM 378 C ASP A 50 6.088 2.579 21.718 1.00 16.70 6ADH 777
ATOM 379 O ASP A 50 6.055 1.345 21.613 1.00 16.70 6ADH 778
ATOM 380 CB ASP A 50 8.330 3.561 21.116 1.00 16.70 6ADH 779
ATOM 381 CG ASP A 50 9.065 2.221 21.187 1.00 16.70 6ADH 780
ATOM 382 OD1 ASP A 50 8.592 1.190 20.574 1.00 16.70 6ADH 781
ATOM 383 OD2 ASP A 50 10.160 2.125 21.861 1.00 16.70 6ADH 782
ATOM 384 N HIS A 51 5.462 3.222 22.700 1.00 16.70 6ADH 783
ATOM 385 CA HIS A 51 4.644 2.463 23.659 1.00 16.70 6ADH 784
ATOM 386 C HIS A 51 3.534 1.768 22.875 1.00 16.70 6ADH 785
ATOM 387 O HIS A 51 2.999 .735 23.300 0.00 16.70 2 6ADH 786
ATOM 388 CB HIS A 51 3.916 3.347 24.684 1.00 16.70 6ADH 787
ATOM 389 CG HIS A 51 4.775 4.041 25.750 1.00 16.70 6ADH 788
ATOM 390 ND1 HIS A 51 5.872 3.436 26.371 1.00 16.70 6ADH 789
ATOM 391 CD2 HIS A 51 4.666 5.279 26.292 1.00 16.70 6ADH 790
ATOM 392 CE1 HIS A 51 6.376 4.302 27.238 1.00 16.70 6ADH 791
ATOM 393 NE2 HIS A 51 5.668 5.402 27.202 1.00 16.70 6ADH 792
ATOM 394 N VAL A 52 3.222 2.374 21.735 1.00 16.70 6ADH 793
ATOM 395 CA VAL A 52 2.168 1.881 20.840 1.00 16.70 6ADH 794
ATOM 396 C VAL A 52 2.618 .684 19.999 1.00 16.70 6ADH 795
ATOM 397 O VAL A 52 1.802 -.112 19.520 1.00 16.70 6ADH 796
ATOM 398 CB VAL A 52 1.700 2.946 19.841 1.00 16.70 6ADH 797
ATOM 399 CG1 VAL A 52 .731 2.393 18.791 1.00 16.70 6ADH 798
ATOM 400 CG2 VAL A 52 .966 4.115 20.499 1.00 16.70 6ADH 799
ATOM 401 N VAL A 53 3.892 .489 19.752 1.00 16.70 6ADH 800
ATOM 402 CA VAL A 53 4.255 -.696 18.955 1.00 16.70 6ADH 801
ATOM 403 C VAL A 53 4.396 -1.881 19.894 1.00 16.70 6ADH 802
ATOM 404 O VAL A 53 4.223 -3.041 19.497 0.00 16.70 2 6ADH 803
ATOM 405 CB VAL A 53 5.517 -.476 18.120 1.00 16.70 6ADH 804
ATOM 406 CG1 VAL A 53 6.054 .953 18.207 1.00 16.70 6ADH 805
ATOM 407 CG2 VAL A 53 6.674 -1.387 18.533 1.00 16.70 6ADH 806
ATOM 408 N SER A 54 4.706 -1.583 21.131 1.00 16.70 6ADH 807
ATOM 409 CA SER A 54 4.760 -2.624 22.149 1.00 16.70 6ADH 808
ATOM 410 C SER A 54 3.338 -2.858 22.613 1.00 16.70 6ADH 809
ATOM 411 O SER A 54 2.851 -3.997 22.645 1.00 16.70 6ADH 810
ATOM 412 CB SER A 54 5.634 -2.206 23.331 1.00 16.70 6ADH 811
ATOM 413 OG SER A 54 6.231 -.944 23.074 1.00 16.70 6ADH 812
ATOM 414 N GLY A 55 2.704 -1.761 22.950 1.00 16.70 6ADH 813
ATOM 415 CA GLY A 55 1.318 -1.782 23.407 1.00 16.70 6ADH 814
ATOM 416 C GLY A 55 1.260 -1.483 24.898 1.00 16.70 6ADH 815
ATOM 417 O GLY A 55 .384 -1.992 25.613 1.00 16.70 6ADH 816
ATOM 418 N THR A 56 2.213 -.659 25.301 1.00 16.70 6ADH 817
ATOM 419 CA THR A 56 2.333 -.175 26.684 1.00 16.70 6ADH 818
ATOM 420 C THR A 56 1.316 .965 26.878 1.00 16.70 6ADH 819
ATOM 421 O THR A 56 .883 1.254 28.001 1.00 16.70 6ADH 820
ATOM 422 CB THR A 56 3.766 .301 26.933 1.00 16.70 6ADH 821
ATOM 423 OG1 THR A 56 4.557 -.771 27.426 1.00 16.70 6ADH 822
ATOM 424 CG2 THR A 56 3.852 1.436 27.955 1.00 16.70 6ADH 823
ATOM 425 N LEU A 57 1.006 1.559 25.749 1.00 16.70 6ADH 824
ATOM 426 CA LEU A 57 -.021 2.596 25.574 1.00 16.70 6ADH 825
ATOM 427 C LEU A 57 -.970 1.948 24.578 1.00 16.70 6ADH 826
ATOM 428 O LEU A 57 -.573 1.582 23.465 1.00 16.70 6ADH 827
ATOM 429 CB LEU A 57 .655 3.873 25.034 1.00 16.70 6ADH 828
ATOM 430 CG LEU A 57 -.311 4.917 24.456 1.00 16.70 6ADH 829
ATOM 431 CD1 LEU A 57 -1.744 4.768 24.970 1.00 16.70 6ADH 830
ATOM 432 CD2 LEU A 57 .098 6.355 24.788 1.00 16.70 6ADH 831
ATOM 433 N VAL A 58 -2.202 1.789 24.940 1.00 16.70 6ADH 832
ATOM 434 CA VAL A 58 -3.123 1.004 24.109 1.00 16.70 6ADH 833
ATOM 435 C VAL A 58 -4.104 1.893 23.319 1.00 16.70 6ADH 834
ATOM 436 O VAL A 58 -4.876 2.671 23.897 1.00 16.70 6ADH 835
ATOM 437 CB VAL A 58 -3.869 .055 25.054 1.00 16.70 6ADH 836
ATOM 438 CG1 VAL A 58 -5.011 -.703 24.379 1.00 16.70 6ADH 837
ATOM 439 CG2 VAL A 58 -2.958 -1.019 25.658 1.00 16.70 6ADH 838
ATOM 440 N THR A 59 -4.064 1.776 21.997 1.00 16.70 6ADH 839
ATOM 441 CA THR A 59 -5.006 2.512 21.123 1.00 16.70 6ADH 840
ATOM 442 C THR A 59 -5.473 1.565 20.020 1.00 16.70 6ADH 841
ATOM 443 O THR A 59 -4.788 .593 19.675 1.00 16.70 6ADH 842
ATOM 444 CB THR A 59 -4.359 3.787 20.543 1.00 16.70 6ADH 843
ATOM 445 OG1 THR A 59 -5.188 4.338 19.530 1.00 16.70 6ADH 844
ATOM 446 CG2 THR A 59 -2.982 3.547 19.920 1.00 16.70 6ADH 845
ATOM 447 N PRO A 60 -6.647 1.750 19.427 1.00 16.70 6ADH 846
ATOM 448 CA PRO A 60 -7.091 .866 18.377 1.00 16.70 6ADH 847
ATOM 449 C PRO A 60 -6.184 .873 17.155 1.00 16.70 6ADH 848
ATOM 450 O PRO A 60 -6.149 1.912 16.423 0.00 16.70 2 6ADH 849
ATOM 451 CB PRO A 60 -8.470 1.372 18.029 1.00 16.70 6ADH 850
ATOM 452 CG PRO A 60 -8.761 2.573 18.916 1.00 16.70 6ADH 851
ATOM 453 CD PRO A 60 -7.575 2.820 19.796 1.00 16.70 6ADH 852
ATOM 454 N LEU A 61 -5.499 -.276 17.002 1.00 16.70 6ADH 853
ATOM 455 CA LEU A 61 -4.705 -.620 15.793 1.00 16.70 6ADH 854
ATOM 456 C LEU A 61 -5.728 -1.171 14.781 1.00 16.70 6ADH 855
ATOM 457 O LEU A 61 -6.740 -1.770 15.179 1.00 16.70 6ADH 856
ATOM 458 CB LEU A 61 -3.697 -1.759 16.081 1.00 16.70 6ADH 857
ATOM 459 CG LEU A 61 -2.641 -1.452 17.148 1.00 16.70 6ADH 858
ATOM 460 CD1 LEU A 61 -1.586 -2.555 17.274 1.00 16.70 6ADH 859
ATOM 461 CD2 LEU A 61 -1.861 -.166 16.871 1.00 16.70 6ADH 860
ATOM 462 N PRO A 62 -5.593 -1.064 13.416 1.00 16.70 1 6ADH 861
ATOM 463 CA PRO A 62 -4.433 -.456 12.704 1.00 16.70 1 6ADH 862
ATOM 464 C PRO A 62 -4.436 1.039 12.830 1.00 16.70 1 6ADH 863
ATOM 465 O PRO A 62 -5.540 1.664 12.846 1.00 16.70 1 6ADH 864
ATOM 466 CB PRO A 62 -4.652 -.895 11.278 1.00 16.70 1 6ADH 865
ATOM 467 CG PRO A 62 -6.137 -1.110 11.148 1.00 16.70 1 6ADH 866
ATOM 468 CD PRO A 62 -6.622 -1.559 12.488 1.00 16.70 1 6ADH 867
ATOM 469 N VAL A 63 -3.264 1.645 12.896 1.00 16.70 6ADH 868
ATOM 470 CA VAL A 63 -3.240 3.088 13.158 1.00 16.70 6ADH 869
ATOM 471 C VAL A 63 -2.005 3.816 12.615 1.00 16.70 6ADH 870
ATOM 472 O VAL A 63 -.886 3.276 12.625 1.00 16.70 6ADH 871
ATOM 473 CB VAL A 63 -3.260 3.284 14.679 1.00 16.70 6ADH 872
ATOM 474 CG1 VAL A 63 -1.931 2.924 15.348 1.00 16.70 6ADH 873
ATOM 475 CG2 VAL A 63 -3.559 4.724 15.098 1.00 16.70 6ADH 874
ATOM 476 N ILE A 64 -2.265 5.045 12.146 1.00 16.70 6ADH 875
ATOM 477 CA ILE A 64 -1.181 5.965 11.755 1.00 16.70 6ADH 876
ATOM 478 C ILE A 64 -.746 6.725 13.018 1.00 16.70 6ADH 877
ATOM 479 O ILE A 64 -1.248 7.818 13.304 1.00 16.70 6ADH 878
ATOM 480 CB ILE A 64 -1.610 7.036 10.720 1.00 16.70 6ADH 879
ATOM 481 CG1 ILE A 64 -2.609 6.528 9.676 1.00 16.70 6ADH 880
ATOM 482 CG2 ILE A 64 -.430 7.601 9.923 1.00 16.70 6ADH 881
ATOM 483 CD1 ILE A 64 -1.952 5.717 8.558 1.00 16.70 6ADH 882
ATOM 484 N ALA A 65 .176 6.121 13.763 1.00 16.70 6ADH 883
ATOM 485 CA ALA A 65 .750 6.720 15.000 1.00 16.70 6ADH 884
ATOM 486 C ALA A 65 1.245 8.156 14.702 1.00 16.70 6ADH 885
ATOM 487 O ALA A 65 .874 8.761 13.687 1.00 16.70 6ADH 886
ATOM 488 CB ALA A 65 1.932 5.875 15.481 1.00 16.70 6ADH 887
ATOM 489 N GLY A 66 2.082 8.692 15.592 1.00 16.70 6ADH 888
ATOM 490 CA GLY A 66 2.676 10.051 15.431 1.00 16.70 6ADH 889
ATOM 491 C GLY A 66 1.775 11.113 16.071 1.00 16.70 6ADH 890
ATOM 492 O GLY A 66 .540 11.042 15.980 0.00 16.70 2 6ADH 891
ATOM 493 N HIS A 67 2.401 12.104 16.706 1.00 16.70 6ADH 892
ATOM 494 CA HIS A 67 1.619 13.134 17.409 1.00 16.70 6ADH 893
ATOM 495 C HIS A 67 2.417 14.400 17.795 1.00 16.70 6ADH 894
ATOM 496 O HIS A 67 1.844 15.425 18.189 1.00 16.70 6ADH 895
ATOM 497 CB HIS A 67 1.086 12.536 18.697 1.00 16.70 6ADH 896
ATOM 498 CG HIS A 67 2.199 12.290 19.705 1.00 16.70 6ADH 897
ATOM 499 ND1 HIS A 67 2.966 11.129 19.693 1.00 16.70 6ADH 898
ATOM 500 CD2 HIS A 67 2.664 13.047 20.731 1.00 16.70 6ADH 899
ATOM 501 CE1 HIS A 67 3.842 11.209 20.676 1.00 16.70 6ADH 900
ATOM 502 NE2 HIS A 67 3.674 12.346 21.304 1.00 16.70 6ADH 901
ATOM 503 N GLU A 68 3.713 14.344 17.694 1.00 16.70 6ADH 902
ATOM 504 CA GLU A 68 4.571 15.485 18.054 1.00 16.70 6ADH 903
ATOM 505 C GLU A 68 5.175 16.041 16.766 1.00 16.70 6ADH 904
ATOM 506 O GLU A 68 6.330 15.747 16.421 1.00 16.70 6ADH 905
ATOM 507 CB GLU A 68 5.637 14.952 19.006 1.00 16.70 6ADH 906
ATOM 508 CG GLU A 68 6.573 16.012 19.558 1.00 16.70 6ADH 907
ATOM 509 CD GLU A 68 7.906 15.411 19.992 1.00 16.70 6ADH 908
ATOM 510 OE1 GLU A 68 8.952 15.566 19.256 1.00 16.70 6ADH 909
ATOM 511 OE2 GLU A 68 7.983 14.747 21.096 1.00 16.70 6ADH 910
ATOM 512 N ALA A 69 4.391 16.841 16.055 1.00 16.70 6ADH 911
ATOM 513 CA ALA A 69 4.830 17.310 14.729 1.00 16.70 6ADH 912
ATOM 514 C ALA A 69 4.316 18.711 14.359 1.00 16.70 6ADH 913
ATOM 515 O ALA A 69 3.353 19.220 14.946 1.00 16.70 6ADH 914
ATOM 516 CB ALA A 69 4.305 16.349 13.662 1.00 16.70 6ADH 915
ATOM 517 N ALA A 70 4.998 19.274 13.375 1.00 16.70 6ADH 916
ATOM 518 CA ALA A 70 4.673 20.588 12.779 1.00 16.70 6ADH 917
ATOM 519 C ALA A 70 4.442 20.373 11.260 1.00 16.70 6ADH 918
ATOM 520 O ALA A 70 4.905 19.384 10.679 1.00 16.70 6ADH 919
ATOM 521 CB ALA A 70 5.832 21.562 13.012 1.00 16.70 6ADH 920
ATOM 522 N GLY A 71 3.726 21.297 10.620 1.00 16.70 6ADH 921
ATOM 523 CA GLY A 71 3.425 21.227 9.156 1.00 16.70 6ADH 922
ATOM 524 C GLY A 71 2.589 22.455 8.726 1.00 16.70 6ADH 923
ATOM 525 O GLY A 71 2.277 23.322 9.558 1.00 16.70 6ADH 924
ATOM 526 N ILE A 72 2.248 22.502 7.413 1.00 16.70 6ADH 925
ATOM 527 CA ILE A 72 1.408 23.597 6.823 1.00 16.70 6ADH 926
ATOM 528 C ILE A 72 .039 23.052 6.360 1.00 16.70 6ADH 927
ATOM 529 O ILE A 72 -.073 21.906 5.901 1.00 16.70 6ADH 928
ATOM 530 CB ILE A 72 2.089 24.254 5.611 1.00 16.70 6ADH 929
ATOM 531 CG1 ILE A 72 3.391 24.974 5.969 1.00 16.70 6ADH 930
ATOM 532 CG2 ILE A 72 1.211 25.311 4.933 1.00 16.70 6ADH 931
ATOM 533 CD1 ILE A 72 4.637 24.227 5.490 1.00 16.70 6ADH 932
ATOM 534 N VAL A 73 -.950 23.925 6.500 1.00 16.70 6ADH 933
ATOM 535 CA VAL A 73 -2.368 23.654 6.174 1.00 16.70 6ADH 934
ATOM 536 C VAL A 73 -2.662 23.891 4.679 1.00 16.70 6ADH 935
ATOM 537 O VAL A 73 -2.026 24.742 4.036 1.00 16.70 6ADH 936
ATOM 538 CB VAL A 73 -3.257 24.625 6.967 1.00 16.70 6ADH 937
ATOM 539 CG1 VAL A 73 -4.741 24.250 6.936 1.00 16.70 6ADH 938
ATOM 540 CG2 VAL A 73 -2.885 24.707 8.450 1.00 16.70 6ADH 939
ATOM 541 N GLU A 74 -3.633 23.120 4.169 1.00 16.70 6ADH 940
ATOM 542 CA GLU A 74 -4.140 23.252 2.777 1.00 16.70 6ADH 941
ATOM 543 C GLU A 74 -5.647 23.553 2.808 1.00 16.70 6ADH 942
ATOM 544 O GLU A 74 -6.076 24.682 2.524 1.00 16.70 6ADH 943
ATOM 545 CB GLU A 74 -3.912 21.964 1.981 0.00 16.70 2 6ADH 944
ATOM 546 CG GLU A 74 -5.196 21.377 1.388 0.00 16.70 2 6ADH 945
ATOM 547 CD GLU A 74 -5.111 19.861 1.199 0.00 16.70 2 6ADH 946
ATOM 548 OE1 GLU A 74 -5.764 19.290 .245 0.00 16.70 2 6ADH 947
ATOM 549 OE2 GLU A 74 -4.383 19.155 1.997 0.00 16.70 2 6ADH 948
ATOM 550 N SER A 75 -6.395 22.517 3.163 1.00 16.70 6ADH 949
ATOM 551 CA SER A 75 -7.863 22.567 3.268 1.00 16.70 6ADH 950
ATOM 552 C SER A 75 -8.295 22.720 4.738 1.00 16.70 6ADH 951
ATOM 553 O SER A 75 -7.663 22.158 5.646 1.00 16.70 6ADH 952
ATOM 554 CB SER A 75 -8.463 21.253 2.738 1.00 16.70 6ADH 953
ATOM 555 OG SER A 75 -9.707 21.500 2.098 1.00 16.70 6ADH 954
ATOM 556 N ILE A 76 -9.365 23.493 4.912 1.00 16.70 6ADH 955
ATOM 557 CA ILE A 76 -10.053 23.687 6.216 1.00 16.70 6ADH 956
ATOM 558 C ILE A 76 -11.540 23.354 5.986 1.00 16.70 6ADH 957
ATOM 559 O ILE A 76 -11.978 23.149 4.846 1.00 16.70 6ADH 958
ATOM 560 CB ILE A 76 -9.886 25.118 6.741 1.00 16.70 6ADH 959
ATOM 561 CG1 ILE A 76 -10.737 26.139 5.988 1.00 16.70 6ADH 960
ATOM 562 CG2 ILE A 76 -8.448 25.631 6.646 1.00 16.70 6ADH 961
ATOM 563 CD1 ILE A 76 -10.125 27.541 5.991 1.00 16.70 6ADH 962
ATOM 564 N GLY A 77 -12.319 23.305 7.056 1.00 16.70 6ADH 963
ATOM 565 CA GLY A 77 -13.740 22.892 6.974 1.00 16.70 6ADH 964
ATOM 566 C GLY A 77 -14.714 24.075 7.010 1.00 16.70 6ADH 965
ATOM 567 O GLY A 77 -14.359 25.209 6.657 1.00 16.70 6ADH 966
ATOM 568 N GLU A 78 -15.919 23.735 7.449 1.00 16.70 6ADH 967
ATOM 569 CA GLU A 78 -17.039 24.675 7.547 1.00 16.70 6ADH 968
ATOM 570 C GLU A 78 -17.107 25.331 8.928 1.00 16.70 6ADH 969
ATOM 571 O GLU A 78 -17.266 24.649 9.953 0.00 16.70 2 6ADH 970
ATOM 572 CB GLU A 78 -18.362 23.943 7.306 1.00 16.70 6ADH 971
ATOM 573 CG GLU A 78 -18.947 24.210 5.919 1.00 16.70 6ADH 972
ATOM 574 CD GLU A 78 -20.284 24.953 5.966 1.00 16.70 6ADH 973
ATOM 575 OE1 GLU A 78 -21.193 24.588 6.804 0.00 16.70 2 6ADH 974
ATOM 576 OE2 GLU A 78 -20.500 25.942 5.167 0.00 16.70 2 6ADH 975
ATOM 577 N GLY A 79 -16.978 26.649 8.886 1.00 16.70 6ADH 976
ATOM 578 CA GLY A 79 -17.101 27.519 10.075 1.00 16.70 6ADH 977
ATOM 579 C GLY A 79 -15.764 27.717 10.809 1.00 16.70 6ADH 978
ATOM 580 O GLY A 79 -15.700 28.427 11.822 1.00 16.70 6ADH 979
ATOM 581 N VAL A 80 -14.734 27.076 10.274 1.00 16.70 6ADH 980
ATOM 582 CA VAL A 80 -13.357 27.133 10.820 1.00 16.70 6ADH 981
ATOM 583 C VAL A 80 -12.917 28.605 10.949 1.00 16.70 6ADH 982
ATOM 584 O VAL A 80 -12.779 29.323 9.948 1.00 16.70 6ADH 983
ATOM 585 CB VAL A 80 -12.418 26.362 9.880 1.00 16.70 6ADH 984
ATOM 586 CG1 VAL A 80 -10.939 26.518 10.241 1.00 16.70 6ADH 985
ATOM 587 CG2 VAL A 80 -12.682 24.855 9.873 1.00 16.70 6ADH 986
ATOM 588 N THR A 81 -12.706 29.012 12.190 1.00 16.70 6ADH 987
ATOM 589 CA THR A 81 -12.341 30.399 12.531 1.00 16.70 6ADH 988
ATOM 590 C THR A 81 -10.837 30.540 12.794 1.00 16.70 6ADH 989
ATOM 591 O THR A 81 -10.159 31.376 12.176 1.00 16.70 6ADH 990
ATOM 592 CB THR A 81 -13.070 30.816 13.815 1.00 16.70 6ADH 991
ATOM 593 OG1 THR A 81 -12.566 30.078 14.921 1.00 16.70 6ADH 992
ATOM 594 CG2 THR A 81 -14.578 30.568 13.756 1.00 16.70 6ADH 993
ATOM 595 N THR A 82 -10.396 29.685 13.696 1.00 16.70 6ADH 994
ATOM 596 CA THR A 82 -9.028 29.680 14.261 1.00 16.70 6ADH 995
ATOM 597 C THR A 82 -7.877 29.717 13.153 1.00 16.70 6ADH 996
ATOM 598 O THR A 82 -7.231 30.752 12.945 1.00 16.70 6ADH 997
ATOM 599 CB THR A 82 -8.931 28.526 15.263 1.00 16.70 6ADH 998
ATOM 600 OG1 THR A 82 -8.313 27.405 14.659 1.00 16.70 6ADH 999
ATOM 601 CG2 THR A 82 -10.299 28.073 15.785 1.00 16.70 6ADH1000
ATOM 602 N VAL A 83 -7.544 28.627 12.381 1.00 16.70 6ADH1001
ATOM 603 CA VAL A 83 -6.395 28.698 11.343 1.00 16.70 6ADH1002
ATOM 604 C VAL A 83 -6.866 28.726 9.844 1.00 16.70 6ADH1003
ATOM 605 O VAL A 83 -7.744 27.957 9.433 1.00 16.70 6ADH1004
ATOM 606 CB VAL A 83 -5.443 27.474 11.403 1.00 16.70 6ADH1005
ATOM 607 CG1 VAL A 83 -5.413 26.786 12.768 1.00 16.70 6ADH1006
ATOM 608 CG2 VAL A 83 -5.806 26.374 10.401 1.00 16.70 6ADH1007
ATOM 609 N ARG A 84 -6.247 29.626 9.038 1.00 16.70 6ADH1008
ATOM 610 CA ARG A 84 -6.492 29.755 7.546 1.00 16.70 6ADH1009
ATOM 611 C ARG A 84 -5.333 29.044 6.766 1.00 16.70 6ADH1010
ATOM 612 O ARG A 84 -4.179 29.037 7.213 1.00 16.70 6ADH1011
ATOM 613 CB ARG A 84 -6.447 31.227 7.101 1.00 16.70 6ADH1012
ATOM 614 CG ARG A 84 -7.515 32.129 7.718 1.00 16.70 6ADH1013
ATOM 615 CD ARG A 84 -7.483 33.541 7.119 0.00 16.70 2 6ADH1014
ATOM 616 NE ARG A 84 -8.327 34.506 7.837 0.00 16.70 2 6ADH1015
ATOM 617 CZ ARG A 84 -8.906 35.566 7.257 1.00 16.70 6ADH1016
ATOM 618 NH1 ARG A 84 -8.742 35.813 5.950 0.00 16.70 2 6ADH1017
ATOM 619 NH2 ARG A 84 -9.677 36.447 7.908 0.00 16.70 2 6ADH1018
ATOM 620 N PRO A 85 -5.515 28.388 5.565 1.00 16.70 6ADH1019
ATOM 621 CA PRO A 85 -4.415 27.658 4.870 1.00 16.70 6ADH1020
ATOM 622 C PRO A 85 -3.230 28.499 4.427 1.00 16.70 6ADH1021
ATOM 623 O PRO A 85 -3.393 29.738 4.192 1.00 16.70 6ADH1022
ATOM 624 CB PRO A 85 -5.059 27.040 3.662 1.00 16.70 6ADH1023
ATOM 625 CG PRO A 85 -6.529 27.438 3.665 1.00 16.70 6ADH1024
ATOM 626 CD PRO A 85 -6.803 28.311 4.857 1.00 16.70 6ADH1025
ATOM 627 N GLY A 86 -2.125 27.759 4.321 1.00 16.70 6ADH1026
ATOM 628 CA GLY A 86 -.794 28.292 4.005 1.00 16.70 6ADH1027
ATOM 629 C GLY A 86 -.144 28.615 5.339 1.00 16.70 6ADH1028
ATOM 630 O GLY A 86 .973 29.153 5.392 1.00 16.70 6ADH1029
ATOM 631 N ASP A 87 -.931 28.248 6.334 1.00 16.70 6ADH1030
ATOM 632 CA ASP A 87 -.643 28.458 7.748 1.00 16.70 6ADH1031
ATOM 633 C ASP A 87 .218 27.347 8.318 1.00 16.70 6ADH1032
ATOM 634 O ASP A 87 -.020 26.158 8.063 0.00 16.70 2 6ADH1033
ATOM 635 CB ASP A 87 -1.948 28.439 8.555 1.00 16.70 6ADH1034
ATOM 636 CG ASP A 87 -2.445 29.832 8.935 1.00 16.70 6ADH1035
ATOM 637 OD1 ASP A 87 -2.178 30.839 8.177 1.00 16.70 6ADH1036
ATOM 638 OD2 ASP A 87 -3.132 29.999 10.014 1.00 16.70 6ADH1037
ATOM 639 N LYS A 88 1.195 27.785 9.066 1.00 16.70 6ADH1038
ATOM 640 CA LYS A 88 2.037 26.886 9.829 1.00 16.70 6ADH1039
ATOM 641 C LYS A 88 1.285 26.653 11.130 1.00 16.70 6ADH1040
ATOM 642 O LYS A 88 .985 27.596 11.876 1.00 16.70 6ADH1041
ATOM 643 CB LYS A 88 3.405 27.529 10.078 1.00 16.70 6ADH1042
ATOM 644 CG LYS A 88 3.951 28.271 8.855 1.00 16.70 6ADH1043
ATOM 645 CD LYS A 88 5.346 27.798 8.437 1.00 16.70 6ADH1044
ATOM 646 CE LYS A 88 6.470 28.458 9.241 1.00 16.70 6ADH1045
ATOM 647 NZ LYS A 88 7.629 28.825 8.415 1.00 16.70 6ADH1046
ATOM 648 N VAL A 89 .970 25.425 11.380 1.00 16.70 6ADH1047
ATOM 649 CA VAL A 89 .214 25.051 12.572 1.00 16.70 6ADH1048
ATOM 650 C VAL A 89 .914 23.889 13.232 1.00 16.70 6ADH1049
ATOM 651 O VAL A 89 1.670 23.147 12.594 1.00 16.70 6ADH1050
ATOM 652 CB VAL A 89 -1.180 24.581 12.144 1.00 16.70 6ADH1051
ATOM 653 CG1 VAL A 89 -2.013 25.683 11.486 1.00 16.70 6ADH1052
ATOM 654 CG2 VAL A 89 -1.135 23.437 11.127 1.00 16.70 6ADH1053
ATOM 655 N ILE A 90 .710 23.682 14.498 1.00 16.70 6ADH1054
ATOM 656 CA ILE A 90 1.284 22.472 15.089 1.00 16.70 6ADH1055
ATOM 657 C ILE A 90 .170 21.688 15.810 1.00 16.70 6ADH1056
ATOM 658 O ILE A 90 -.448 22.192 16.763 1.00 16.70 6ADH1057
ATOM 659 CB ILE A 90 2.539 22.780 15.944 1.00 16.70 6ADH1058
ATOM 660 CG1 ILE A 90 2.317 23.697 17.144 1.00 16.70 6ADH1059
ATOM 661 CG2 ILE A 90 3.652 23.466 15.145 1.00 16.70 6ADH1060
ATOM 662 CD1 ILE A 90 3.598 23.937 17.949 1.00 16.70 6ADH1061
ATOM 663 N PRO A 91 -.103 20.436 15.330 1.00 16.70 6ADH1062
ATOM 664 CA PRO A 91 -1.134 19.529 15.908 1.00 16.70 6ADH1063
ATOM 665 C PRO A 91 -.961 19.241 17.421 1.00 16.70 6ADH1064
ATOM 666 O PRO A 91 .221 19.098 17.877 0.00 16.70 2 6ADH1065
ATOM 667 CB PRO A 91 -1.036 18.284 15.052 1.00 16.70 6ADH1066
ATOM 668 CG PRO A 91 .029 18.517 13.987 1.00 16.70 6ADH1067
ATOM 669 CD PRO A 91 .588 19.895 14.147 1.00 16.70 6ADH1068
ATOM 670 N LEU A 92 -2.187 19.154 18.081 1.00 16.70 6ADH1069
ATOM 671 CA LEU A 92 -2.423 19.003 19.584 1.00 16.70 6ADH1070
ATOM 672 C LEU A 92 -3.095 17.646 20.015 1.00 16.70 6ADH1071
ATOM 673 O LEU A 92 -4.303 17.436 19.804 1.00 16.70 6ADH1072
ATOM 674 CB LEU A 92 -3.377 20.111 20.070 1.00 16.70 6ADH1073
ATOM 675 CG LEU A 92 -2.879 21.521 19.746 1.00 16.70 6ADH1074
ATOM 676 CD1 LEU A 92 -3.905 22.612 20.063 1.00 16.70 6ADH1075
ATOM 677 CD2 LEU A 92 -1.620 21.901 20.526 1.00 16.70 6ADH1076
ATOM 678 N PHE A 93 -2.261 16.774 20.640 1.00 16.70 6ADH1077
ATOM 679 CA PHE A 93 -2.663 15.409 21.120 1.00 16.70 6ADH1078
ATOM 680 C PHE A 93 -3.647 15.524 22.339 1.00 16.70 6ADH1079
ATOM 681 O PHE A 93 -4.469 14.628 22.580 1.00 16.70 6ADH1080
ATOM 682 CB PHE A 93 -1.400 14.533 21.379 1.00 16.70 6ADH1081
ATOM 683 CG PHE A 93 -.560 14.884 22.617 1.00 16.70 6ADH1082
ATOM 684 CD1 PHE A 93 .644 15.595 22.479 1.00 16.70 6ADH1083
ATOM 685 CD2 PHE A 93 -.981 14.473 23.887 1.00 16.70 6ADH1084
ATOM 686 CE1 PHE A 93 1.412 15.904 23.610 1.00 16.70 6ADH1085
ATOM 687 CE2 PHE A 93 -.211 14.782 25.016 1.00 16.70 6ADH1086
ATOM 688 CZ PHE A 93 .983 15.498 24.878 1.00 16.70 6ADH1087
ATOM 689 N THR A 94 -3.538 16.644 23.070 1.00 16.70 6ADH1088
ATOM 690 CA THR A 94 -4.468 17.047 24.176 1.00 16.70 6ADH1089
ATOM 691 C THR A 94 -5.242 18.295 23.668 1.00 16.70 6ADH1090
ATOM 692 O THR A 94 -4.718 19.415 23.681 1.00 16.70 6ADH1091
ATOM 693 CB THR A 94 -3.671 17.457 25.437 1.00 16.70 6ADH1092
ATOM 694 OG1 THR A 94 -2.868 16.377 25.889 1.00 16.70 6ADH1093
ATOM 695 CG2 THR A 94 -4.565 17.875 26.608 1.00 16.70 6ADH1094
ATOM 696 N PRO A 95 -6.506 18.238 23.163 1.00 16.70 6ADH1095
ATOM 697 CA PRO A 95 -7.189 19.442 22.600 1.00 16.70 6ADH1096
ATOM 698 C PRO A 95 -7.586 20.480 23.656 1.00 16.70 6ADH1097
ATOM 699 O PRO A 95 -7.314 20.268 24.875 1.00 16.70 6ADH1098
ATOM 700 CB PRO A 95 -8.479 18.894 22.041 1.00 16.70 6ADH1099
ATOM 701 CG PRO A 95 -8.536 17.401 22.358 1.00 16.70 6ADH1100
ATOM 702 CD PRO A 95 -7.309 17.008 23.128 1.00 16.70 6ADH1101
ATOM 703 N GLN A 96 -8.207 21.571 23.197 1.00 16.70 6ADH1102
ATOM 704 CA GLN A 96 -8.844 22.603 24.078 1.00 16.70 6ADH1103
ATOM 705 C GLN A 96 -10.248 22.817 23.500 1.00 16.70 6ADH1104
ATOM 706 O GLN A 96 -10.602 22.257 22.455 1.00 16.70 6ADH1105
ATOM 707 CB GLN A 96 -8.077 23.940 24.106 1.00 16.70 6ADH1106
ATOM 708 CG GLN A 96 -8.960 25.101 24.617 1.00 16.70 6ADH1107
ATOM 709 CD GLN A 96 -8.190 26.229 25.320 1.00 16.70 6ADH1108
ATOM 710 OE1 GLN A 96 -8.633 27.377 25.306 1.00 16.70 6ADH1109
ATOM 711 NE2 GLN A 96 -7.053 25.972 25.940 1.00 16.70 6ADH1110
ATOM 712 N CYS A 97 -11.084 23.599 24.131 1.00 16.70 6ADH1111
ATOM 713 CA CYS A 97 -12.437 23.827 23.575 1.00 16.70 6ADH1112
ATOM 714 C CYS A 97 -13.083 25.026 24.274 1.00 16.70 6ADH1113
ATOM 715 O CYS A 97 -12.649 26.174 24.109 1.00 16.70 6ADH1114
ATOM 716 CB CYS A 97 -13.290 22.543 23.683 1.00 16.70 6ADH1115
ATOM 717 SG CYS A 97 -13.773 22.129 25.422 1.00 16.70 6ADH1116
ATOM 718 N GLY A 98 -14.115 24.779 25.048 1.00 16.70 6ADH1117
ATOM 719 CA GLY A 98 -14.787 25.876 25.765 1.00 16.70 6ADH1118
ATOM 720 C GLY A 98 -16.171 25.459 26.254 1.00 16.70 6ADH1119
ATOM 721 O GLY A 98 -17.162 25.551 25.515 1.00 16.70 6ADH1120
ATOM 722 N LYS A 99 -16.170 25.028 27.493 1.00 16.70 6ADH1121
ATOM 723 CA LYS A 99 -17.371 24.581 28.208 1.00 16.70 6ADH1122
ATOM 724 C LYS A 99 -16.954 23.613 29.298 1.00 16.70 6ADH1123
ATOM 725 O LYS A 99 -16.997 23.942 30.494 0.00 16.70 2 6ADH1124
ATOM 726 CB LYS A 99 -18.342 23.871 27.259 1.00 16.70 6ADH1125
ATOM 727 CG LYS A 99 -19.748 23.707 27.853 0.00 16.70 2 6ADH1126
ATOM 728 CD LYS A 99 -19.976 22.336 28.498 0.00 16.70 2 6ADH1127
ATOM 729 CE LYS A 99 -20.894 22.395 29.723 0.00 16.70 2 6ADH1128
ATOM 730 NZ LYS A 99 -22.313 22.208 29.387 0.00 16.70 2 6ADH1129
ATOM 731 N CYS A 100 -16.552 22.434 28.849 1.00 16.70 6ADH1130
ATOM 732 CA CYS A 100 -16.106 21.385 29.767 1.00 16.70 6ADH1131
ATOM 733 C CYS A 100 -15.287 22.067 30.873 1.00 16.70 6ADH1132
ATOM 734 O CYS A 100 -14.199 22.606 30.624 1.00 16.70 6ADH1133
ATOM 735 CB CYS A 100 -15.320 20.297 29.001 1.00 16.70 6ADH1134
ATOM 736 SG CYS A 100 -13.569 20.771 28.625 1.00 16.70 6ADH1135
ATOM 737 N ARG A 101 -15.866 22.014 32.059 1.00 16.70 6ADH1136
ATOM 738 CA ARG A 101 -15.335 22.655 33.282 1.00 16.70 6ADH1137
ATOM 739 C ARG A 101 -13.790 22.560 33.383 1.00 16.70 6ADH1138
ATOM 740 O ARG A 101 -13.147 23.344 34.098 1.00 16.70 6ADH1139
ATOM 741 CB ARG A 101 -15.978 22.032 34.533 1.00 16.70 6ADH1140
ATOM 742 CG ARG A 101 -16.531 23.059 35.556 0.00 16.70 2 6ADH1141
ATOM 743 CD ARG A 101 -16.528 24.519 35.076 0.00 16.70 2 6ADH1142
ATOM 744 NE ARG A 101 -15.843 25.453 36.006 0.00 16.70 2 6ADH1143
ATOM 745 CZ ARG A 101 -16.436 26.105 37.029 0.00 16.70 2 6ADH1144
ATOM 746 NH1 ARG A 101 -17.736 25.931 37.303 0.00 16.70 2 6ADH1145
ATOM 747 NH2 ARG A 101 -15.804 26.974 37.831 0.00 16.70 2 6ADH1146
ATOM 748 N VAL A 102 -13.148 21.617 32.683 1.00 16.70 6ADH1147
ATOM 749 CA VAL A 102 -11.662 21.553 32.726 1.00 16.70 6ADH1148
ATOM 750 C VAL A 102 -11.067 22.628 31.822 1.00 16.70 6ADH1149
ATOM 751 O VAL A 102 -10.048 23.250 32.146 1.00 16.70 6ADH1150
ATOM 752 CB VAL A 102 -11.082 20.211 32.262 1.00 16.70 6ADH1151
ATOM 753 CG1 VAL A 102 -9.557 20.143 32.405 1.00 16.70 6ADH1152
ATOM 754 CG2 VAL A 102 -11.620 19.015 33.048 1.00 16.70 6ADH1153
ATOM 755 N CYS A 103 -11.698 22.856 30.696 1.00 16.70 6ADH1154
ATOM 756 CA CYS A 103 -11.302 23.935 29.784 1.00 16.70 6ADH1155
ATOM 757 C CYS A 103 -11.568 25.294 30.428 1.00 16.70 6ADH1156
ATOM 758 O CYS A 103 -10.936 26.300 30.074 1.00 16.70 6ADH1157
ATOM 759 CB CYS A 103 -12.024 23.812 28.453 1.00 16.70 6ADH1158
ATOM 760 SG CYS A 103 -10.909 22.965 27.246 1.00 16.70 6ADH1159
ATOM 761 N LYS A 104 -12.508 25.286 31.382 1.00 16.70 6ADH1160
ATOM 762 CA LYS A 104 -12.972 26.533 32.055 1.00 16.70 6ADH1161
ATOM 763 C LYS A 104 -12.543 26.659 33.552 1.00 16.70 6ADH1162
ATOM 764 O LYS A 104 -13.125 27.445 34.315 1.00 16.70 6ADH1163
ATOM 765 CB LYS A 104 -14.504 26.625 32.001 1.00 16.70 6ADH1164
ATOM 766 CG LYS A 104 -14.987 27.860 31.229 1.00 16.70 6ADH1165
ATOM 767 CD LYS A 104 -16.511 27.969 31.140 0.00 16.70 2 6ADH1166
ATOM 768 CE LYS A 104 -16.979 28.794 29.937 0.00 16.70 2 6ADH1167
ATOM 769 NZ LYS A 104 -18.435 28.995 29.906 0.00 16.70 2 6ADH1168
ATOM 770 N HIS A 105 -11.519 25.896 33.948 1.00 16.70 6ADH1169
ATOM 771 CA HIS A 105 -10.953 25.888 35.343 1.00 16.70 6ADH1170
ATOM 772 C HIS A 105 -9.589 26.612 35.319 1.00 16.70 6ADH1171
ATOM 773 O HIS A 105 -8.766 26.399 34.423 1.00 16.70 6ADH1172
ATOM 774 CB HIS A 105 -10.735 24.424 35.771 1.00 16.70 6ADH1173
ATOM 775 CG HIS A 105 -10.198 24.248 37.198 1.00 16.70 6ADH1174
ATOM 776 ND1 HIS A 105 -8.963 23.651 37.454 1.00 16.70 6ADH1175
ATOM 777 CD2 HIS A 105 -10.717 24.573 38.410 1.00 16.70 6ADH1176
ATOM 778 CE1 HIS A 105 -8.777 23.634 38.762 1.00 16.70 6ADH1177
ATOM 779 NE2 HIS A 105 -9.813 24.179 39.346 1.00 16.70 6ADH1178
ATOM 780 N PRO A 106 -9.161 27.489 36.257 1.00 16.70 6ADH1179
ATOM 781 CA PRO A 106 -7.881 28.179 36.084 1.00 16.70 6ADH1180
ATOM 782 C PRO A 106 -6.710 27.222 35.926 1.00 16.70 6ADH1181
ATOM 783 O PRO A 106 -5.738 27.550 35.178 1.00 16.70 6ADH1182
ATOM 784 CB PRO A 106 -7.730 29.003 37.338 1.00 16.70 6ADH1183
ATOM 785 CG PRO A 106 -8.959 28.762 38.206 1.00 16.70 6ADH1184
ATOM 786 CD PRO A 106 -9.890 27.826 37.491 1.00 16.70 6ADH1185
ATOM 787 N GLU A 107 -6.818 26.090 36.599 1.00 16.70 6ADH1186
ATOM 788 CA GLU A 107 -5.752 25.071 36.655 1.00 16.70 6ADH1187
ATOM 789 C GLU A 107 -6.242 23.731 36.115 1.00 16.70 6ADH1188
ATOM 790 O GLU A 107 -6.457 22.771 36.869 1.00 16.70 6ADH1189
ATOM 791 CB GLU A 107 -5.390 24.838 38.128 0.00 16.70 2 6ADH1190
ATOM 792 CG GLU A 107 -3.919 24.490 38.344 0.00 16.70 2 6ADH1191
ATOM 793 CD GLU A 107 -3.705 23.032 38.756 0.00 16.70 2 6ADH1192
ATOM 794 OE1 GLU A 107 -4.450 22.104 38.257 0.00 16.70 2 6ADH1193
ATOM 795 OE2 GLU A 107 -2.778 22.731 39.600 0.00 16.70 2 6ADH1194
ATOM 796 N GLY A 108 -6.422 23.616 34.827 1.00 16.70 6ADH1195
ATOM 797 CA GLY A 108 -6.959 22.355 34.285 1.00 16.70 6ADH1196
ATOM 798 C GLY A 108 -5.894 21.545 33.529 1.00 16.70 6ADH1197
ATOM 799 O GLY A 108 -5.172 20.741 34.139 1.00 16.70 6ADH1198
ATOM 800 N ASN A 109 -5.943 21.860 32.230 1.00 16.70 6ADH1199
ATOM 801 CA ASN A 109 -5.135 21.332 31.088 1.00 16.70 6ADH1200
ATOM 802 C ASN A 109 -5.949 20.334 30.215 1.00 16.70 6ADH1201
ATOM 803 O ASN A 109 -6.478 20.716 29.163 1.00 16.70 6ADH1202
ATOM 804 CB ASN A 109 -3.876 20.569 31.478 1.00 16.70 6ADH1203
ATOM 805 CG ASN A 109 -3.184 19.989 30.230 1.00 16.70 6ADH1204
ATOM 806 OD1 ASN A 109 -3.519 18.889 29.794 1.00 16.70 6ADH1205
ATOM 807 ND2 ASN A 109 -2.233 20.672 29.620 1.00 16.70 6ADH1206
ATOM 808 N PHE A 110 -5.973 19.094 30.759 1.00 16.70 6ADH1207
ATOM 809 CA PHE A 110 -6.587 17.821 30.213 1.00 16.70 6ADH1208
ATOM 810 C PHE A 110 -8.089 17.960 29.851 1.00 16.70 6ADH1209
ATOM 811 O PHE A 110 -8.971 17.715 30.686 1.00 16.70 6ADH1210
ATOM 812 CB PHE A 110 -6.476 16.736 31.308 1.00 16.70 6ADH1211
ATOM 813 CG PHE A 110 -6.484 15.287 30.802 1.00 16.70 6ADH1212
ATOM 814 CD1 PHE A 110 -5.749 14.927 29.664 1.00 16.70 6ADH1213
ATOM 815 CD2 PHE A 110 -7.224 14.315 31.490 1.00 16.70 6ADH1214
ATOM 816 CE1 PHE A 110 -5.760 13.599 29.213 1.00 16.70 6ADH1215
ATOM 817 CE2 PHE A 110 -7.233 12.987 31.038 1.00 16.70 6ADH1216
ATOM 818 CZ PHE A 110 -6.503 12.630 29.900 1.00 16.70 6ADH1217
ATOM 819 N CYS A 111 -8.313 18.343 28.593 1.00 16.70 6ADH1218
ATOM 820 CA CYS A 111 -9.656 18.583 28.002 1.00 16.70 6ADH1219
ATOM 821 C CYS A 111 -10.485 17.303 27.972 1.00 16.70 6ADH1220
ATOM 822 O CYS A 111 -10.049 16.269 27.442 1.00 16.70 6ADH1221
ATOM 823 CB CYS A 111 -9.507 19.078 26.551 1.00 16.70 6ADH1222
ATOM 824 SG CYS A 111 -11.134 19.450 25.736 1.00 16.70 6ADH1223
ATOM 825 N LEU A 112 -11.665 17.407 28.531 1.00 16.70 6ADH1224
ATOM 826 CA LEU A 112 -12.586 16.280 28.590 1.00 16.70 6ADH1225
ATOM 827 C LEU A 112 -12.692 15.602 27.221 1.00 16.70 6ADH1226
ATOM 828 O LEU A 112 -12.932 14.389 27.123 1.00 16.70 6ADH1227
ATOM 829 CB LEU A 112 -13.986 16.753 29.001 1.00 16.70 6ADH1228
ATOM 830 CG LEU A 112 -14.366 16.353 30.428 1.00 16.70 6ADH1229
ATOM 831 CD1 LEU A 112 -13.220 16.538 31.425 1.00 16.70 6ADH1230
ATOM 832 CD2 LEU A 112 -15.535 17.167 30.985 1.00 16.70 6ADH1231
ATOM 833 N LYS A 113 -12.505 16.368 26.161 1.00 16.70 6ADH1232
ATOM 834 CA LYS A 113 -12.692 15.827 24.801 1.00 16.70 6ADH1233
ATOM 835 C LYS A 113 -11.449 15.111 24.233 1.00 16.70 6ADH1234
ATOM 836 O LYS A 113 -11.310 14.937 23.014 1.00 16.70 6ADH1235
ATOM 837 CB LYS A 113 -13.108 16.936 23.835 1.00 16.70 6ADH1236
ATOM 838 CG LYS A 113 -14.597 16.860 23.470 1.00 16.70 6ADH1237
ATOM 839 CD LYS A 113 -15.222 18.228 23.187 1.00 16.70 6ADH1238
ATOM 840 CE LYS A 113 -16.682 18.326 23.636 1.00 16.70 6ADH1239
ATOM 841 NZ LYS A 113 -17.164 19.712 23.723 1.00 16.70 6ADH1240
ATOM 842 N ASN A 114 -10.542 14.666 25.082 1.00 16.70 6ADH1241
ATOM 843 CA ASN A 114 -9.356 13.942 24.578 1.00 16.70 6ADH1242
ATOM 844 C ASN A 114 -9.777 12.542 24.075 1.00 16.70 6ADH1243
ATOM 845 O ASN A 114 -10.975 12.239 23.965 0.00 16.70 2 6ADH1244
ATOM 846 CB ASN A 114 -8.272 13.816 25.661 1.00 16.70 6ADH1245
ATOM 847 CG ASN A 114 -8.761 13.169 26.956 1.00 16.70 6ADH1246
ATOM 848 OD1 ASN A 114 -9.473 13.804 27.731 1.00 16.70 6ADH1247
ATOM 849 ND2 ASN A 114 -8.417 11.926 27.243 1.00 16.70 6ADH1248
ATOM 850 N ASP A 115 -8.745 11.755 23.788 1.00 16.70 6ADH1249
ATOM 851 CA ASP A 115 -8.839 10.368 23.275 1.00 16.70 6ADH1250
ATOM 852 C ASP A 115 -7.637 9.581 23.813 1.00 16.70 6ADH1251
ATOM 853 O ASP A 115 -7.173 8.614 23.186 1.00 16.70 6ADH1252
ATOM 854 CB ASP A 115 -8.802 10.401 21.736 1.00 16.70 6ADH1253
ATOM 855 CG ASP A 115 -9.100 9.050 21.076 1.00 16.70 6ADH1254
ATOM 856 OD1 ASP A 115 -8.152 8.391 20.501 1.00 16.70 6ADH1255
ATOM 857 OD2 ASP A 115 -10.298 8.573 21.094 1.00 16.70 6ADH1256
ATOM 858 N LEU A 116 -7.196 10.050 24.972 1.00 16.70 6ADH1257
ATOM 859 CA LEU A 116 -6.013 9.530 25.666 1.00 16.70 6ADH1258
ATOM 860 C LEU A 116 -6.390 8.655 26.866 1.00 16.70 6ADH1259
ATOM 861 O LEU A 116 -5.739 7.638 27.148 1.00 16.70 6ADH1260
ATOM 862 CB LEU A 116 -5.161 10.698 26.167 1.00 16.70 6ADH1261
ATOM 863 CG LEU A 116 -3.675 10.355 26.291 1.00 16.70 6ADH1262
ATOM 864 CD1 LEU A 116 -3.103 10.678 27.673 1.00 16.70 6ADH1263
ATOM 865 CD2 LEU A 116 -3.381 8.872 26.056 1.00 16.70 6ADH1264
ATOM 866 N SER A 117 -7.439 9.034 27.571 1.00 16.70 6ADH1265
ATOM 867 CA SER A 117 -7.850 8.270 28.760 1.00 16.70 6ADH1266
ATOM 868 C SER A 117 -8.667 6.990 28.374 1.00 16.70 6ADH1267
ATOM 869 O SER A 117 -8.830 6.068 29.185 1.00 16.70 6ADH1268
ATOM 870 CB SER A 117 -8.611 9.164 29.752 1.00 16.70 6ADH1269
ATOM 871 OG SER A 117 -9.882 9.514 29.232 1.00 16.70 6ADH1270
ATOM 872 N MET A 118 -9.206 6.877 27.144 1.00 16.70 6ADH1271
ATOM 873 CA MET A 118 -9.916 5.606 26.715 1.00 16.70 6ADH1272
ATOM 874 C MET A 118 -10.398 5.726 25.250 1.00 16.70 6ADH1273
ATOM 875 O MET A 118 -11.579 6.032 25.000 0.00 16.70 2 6ADH1274
ATOM 876 CB MET A 118 -10.979 5.214 27.731 1.00 16.70 6ADH1275
ATOM 877 CG MET A 118 -12.257 6.024 27.625 1.00 16.70 6ADH1276
ATOM 878 SD MET A 118 -13.695 5.004 27.377 1.00 16.70 6ADH1277
ATOM 879 CE MET A 118 -13.551 3.504 28.326 1.00 16.70 6ADH1278
ATOM 880 N PRO A 119 -9.353 5.428 24.456 1.00 16.70 6ADH1279
ATOM 881 CA PRO A 119 -9.257 5.564 22.984 1.00 16.70 6ADH1280
ATOM 882 C PRO A 119 -10.265 4.805 22.130 1.00 16.70 6ADH1281
ATOM 883 O PRO A 119 -10.410 3.555 22.314 1.00 16.70 6ADH1282
ATOM 884 CB PRO A 119 -7.844 5.097 22.680 1.00 16.70 6ADH1283
ATOM 885 CG PRO A 119 -7.168 4.713 23.984 1.00 16.70 6ADH1284
ATOM 886 CD PRO A 119 -8.136 4.906 25.095 1.00 16.70 6ADH1285
ATOM 887 N ARG A 120 -10.872 5.640 21.252 1.00 16.70 6ADH1286
ATOM 888 CA ARG A 120 -11.826 5.241 20.190 1.00 16.70 6ADH1287
ATOM 889 C ARG A 120 -11.006 4.866 18.949 1.00 16.70 6ADH1288
ATOM 890 O ARG A 120 -11.298 3.878 18.260 1.00 16.70 6ADH1289
ATOM 891 CB ARG A 120 -12.760 6.411 19.810 1.00 16.70 6ADH1290
ATOM 892 CG ARG A 120 -13.445 7.084 21.009 1.00 16.70 6ADH1291
ATOM 893 CD ARG A 120 -14.886 7.528 20.704 1.00 16.70 6ADH1292
ATOM 894 NE ARG A 120 -15.175 8.908 21.130 1.00 16.70 6ADH1293
ATOM 895 CZ ARG A 120 -14.852 9.998 20.418 1.00 16.70 6ADH1294
ATOM 896 NH1 ARG A 120 -14.231 9.893 19.235 1.00 16.70 6ADH1295
ATOM 897 NH2 ARG A 120 -15.109 11.255 20.812 1.00 16.70 6ADH1296
ATOM 898 N GLY A 121 -9.994 5.693 18.726 1.00 16.70 6ADH1297
ATOM 899 CA GLY A 121 -9.021 5.515 17.637 1.00 16.70 6ADH1298
ATOM 900 C GLY A 121 -9.529 6.121 16.336 1.00 16.70 6ADH1299
ATOM 901 O GLY A 121 -9.316 5.573 15.245 0.00 16.70 2 6ADH1300
ATOM 902 N THR A 122 -10.188 7.244 16.461 1.00 16.70 6ADH1301
ATOM 903 CA THR A 122 -10.749 7.915 15.295 1.00 16.70 6ADH1302
ATOM 904 C THR A 122 -10.813 9.414 15.487 1.00 16.70 6ADH1303
ATOM 905 O THR A 122 -10.164 9.971 16.385 1.00 16.70 6ADH1304
ATOM 906 CB THR A 122 -12.181 7.435 15.054 1.00 16.70 6ADH1305
ATOM 907 OG1 THR A 122 -12.919 7.486 16.266 1.00 16.70 6ADH1306
ATOM 908 CG2 THR A 122 -12.252 5.998 14.534 1.00 16.70 6ADH1307
ATOM 909 N MET A 123 -11.607 9.976 14.607 1.00 16.70 6ADH1308
ATOM 910 CA MET A 123 -11.895 11.395 14.575 1.00 16.70 6ADH1309
ATOM 911 C MET A 123 -12.858 11.713 15.707 1.00 16.70 6ADH1310
ATOM 912 O MET A 123 -13.212 10.835 16.507 1.00 16.70 6ADH1311
ATOM 913 CB MET A 123 -12.528 11.763 13.234 1.00 16.70 6ADH1312
ATOM 914 CG MET A 123 -12.299 13.223 12.841 1.00 16.70 6ADH1313
ATOM 915 SD MET A 123 -10.620 13.557 12.357 1.00 16.70 6ADH1314
ATOM 916 CE MET A 123 -10.338 15.315 12.317 1.00 16.70 6ADH1315
ATOM 917 N GLN A 124 -13.261 12.959 15.720 1.00 16.70 6ADH1316
ATOM 918 CA GLN A 124 -14.135 13.481 16.760 1.00 16.70 6ADH1317
ATOM 919 C GLN A 124 -15.613 13.159 16.500 1.00 16.70 6ADH1318
ATOM 920 O GLN A 124 -16.505 13.590 17.241 1.00 16.70 6ADH1319
ATOM 921 CB GLN A 124 -13.967 14.994 16.889 1.00 16.70 6ADH1320
ATOM 922 CG GLN A 124 -13.801 15.455 18.339 1.00 16.70 6ADH1321
ATOM 923 CD GLN A 124 -14.636 16.694 18.662 1.00 16.70 6ADH1322
ATOM 924 OE1 GLN A 124 -15.476 17.094 17.859 1.00 16.70 6ADH1323
ATOM 925 NE2 GLN A 124 -14.454 17.334 19.803 1.00 16.70 6ADH1324
ATOM 926 N ASP A 125 -15.941 12.415 15.455 1.00 16.70 6ADH1325
ATOM 927 CA ASP A 125 -17.355 11.986 15.312 1.00 16.70 6ADH1326
ATOM 928 C ASP A 125 -17.435 10.465 15.346 1.00 16.70 6ADH1327
ATOM 929 O ASP A 125 -18.529 9.885 15.412 1.00 16.70 6ADH1328
ATOM 930 CB ASP A 125 -18.081 12.533 14.065 1.00 16.70 6ADH1329
ATOM 931 CG ASP A 125 -17.271 12.568 12.773 1.00 16.70 6ADH1330
ATOM 932 OD1 ASP A 125 -16.528 11.566 12.449 1.00 16.70 6ADH1331
ATOM 933 OD2 ASP A 125 -17.337 13.602 12.005 1.00 16.70 6ADH1332
ATOM 934 N GLY A 126 -16.268 9.852 15.302 1.00 16.70 6ADH1333
ATOM 935 CA GLY A 126 -16.144 8.394 15.408 1.00 16.70 6ADH1334
ATOM 936 C GLY A 126 -15.589 7.751 14.129 1.00 16.70 6ADH1335
ATOM 937 O GLY A 126 -15.357 6.535 14.077 1.00 16.70 6ADH1336
ATOM 938 N THR A 127 -15.363 8.553 13.095 1.00 16.70 6ADH1337
ATOM 939 CA THR A 127 -14.880 8.011 11.795 1.00 16.70 6ADH1338
ATOM 940 C THR A 127 -13.410 8.394 11.480 1.00 16.70 6ADH1339
ATOM 941 O THR A 127 -12.810 9.231 12.173 1.00 16.70 6ADH1340
ATOM 942 CB THR A 127 -15.762 8.508 10.644 1.00 16.70 6ADH1341
ATOM 943 OG1 THR A 127 -15.337 9.795 10.221 1.00 16.70 6ADH1342
ATOM 944 CG2 THR A 127 -17.241 8.619 11.024 1.00 16.70 6ADH1343
ATOM 945 N SER A 128 -12.920 7.723 10.407 1.00 16.70 6ADH1344
ATOM 946 CA SER A 128 -11.544 7.855 9.866 1.00 16.70 6ADH1345
ATOM 947 C SER A 128 -11.477 8.932 8.778 1.00 16.70 6ADH1346
ATOM 948 O SER A 128 -12.482 9.592 8.473 0.00 16.70 2 6ADH1347
ATOM 949 CB SER A 128 -11.068 6.527 9.266 1.00 16.70 6ADH1348
ATOM 950 OG SER A 128 -9.900 6.077 9.940 1.00 16.70 6ADH1349
ATOM 951 N ARG A 129 -10.276 9.028 8.259 1.00 16.70 6ADH1350
ATOM 952 CA ARG A 129 -9.848 10.052 7.314 1.00 16.70 6ADH1351
ATOM 953 C ARG A 129 -8.550 9.530 6.708 1.00 16.70 6ADH1352
ATOM 954 O ARG A 129 -7.725 10.303 6.194 0.00 16.70 2 6ADH1353
ATOM 955 CB ARG A 129 -9.616 11.306 8.161 1.00 16.70 6ADH1354
ATOM 956 CG ARG A 129 -9.886 12.604 7.412 1.00 16.70 6ADH1355
ATOM 957 CD ARG A 129 -11.160 13.317 7.875 1.00 16.70 6ADH1356
ATOM 958 NE ARG A 129 -12.133 12.423 8.519 1.00 16.70 6ADH1357
ATOM 959 CZ ARG A 129 -13.344 12.820 8.933 1.00 16.70 6ADH1358
ATOM 960 NH1 ARG A 129 -13.744 14.089 8.778 1.00 16.70 6ADH1359
ATOM 961 NH2 ARG A 129 -14.237 12.013 9.523 1.00 16.70 6ADH1360
ATOM 962 N PHE A 130 -8.523 8.229 6.851 1.00 16.70 6ADH1361
ATOM 963 CA PHE A 130 -7.414 7.362 6.551 1.00 16.70 6ADH1362
ATOM 964 C PHE A 130 -7.958 5.978 6.191 1.00 16.70 6ADH1363
ATOM 965 O PHE A 130 -8.510 5.270 7.044 1.00 16.70 6ADH1364
ATOM 966 CB PHE A 130 -6.579 7.223 7.827 1.00 16.70 6ADH1365
ATOM 967 CG PHE A 130 -5.723 8.449 8.168 1.00 16.70 6ADH1366
ATOM 968 CD1 PHE A 130 -4.922 9.033 7.185 1.00 16.70 6ADH1367
ATOM 969 CD2 PHE A 130 -5.726 8.978 9.470 1.00 16.70 6ADH1368
ATOM 970 CE1 PHE A 130 -4.106 10.127 7.501 1.00 16.70 6ADH1369
ATOM 971 CE2 PHE A 130 -4.908 10.071 9.789 1.00 16.70 6ADH1370
ATOM 972 CZ PHE A 130 -4.094 10.643 8.803 1.00 16.70 6ADH1371
ATOM 973 N THR A 131 -7.777 5.674 4.945 1.00 16.70 6ADH1372
ATOM 974 CA THR A 131 -8.186 4.426 4.320 1.00 16.70 6ADH1373
ATOM 975 C THR A 131 -6.986 3.889 3.592 1.00 16.70 6ADH1374
ATOM 976 O THR A 131 -6.427 4.570 2.724 1.00 16.70 6ADH1375
ATOM 977 CB THR A 131 -9.201 4.747 3.222 1.00 16.70 6ADH1376
ATOM 978 OG1 THR A 131 -9.597 6.107 3.320 1.00 16.70 6ADH1377
ATOM 979 CG2 THR A 131 -10.465 3.891 3.283 1.00 16.70 6ADH1378
ATOM 980 N CYS A 132 -6.536 2.692 3.900 1.00 16.70 6ADH1379
ATOM 981 CA CYS A 132 -5.383 2.160 3.148 1.00 16.70 6ADH1380
ATOM 982 C CYS A 132 -5.865 1.274 1.990 1.00 16.70 6ADH1381
ATOM 983 O CYS A 132 -6.541 1.747 1.066 0.00 16.70 2 6ADH1382
ATOM 984 CB CYS A 132 -4.403 1.397 4.028 1.00 16.70 6ADH1383
ATOM 985 SG CYS A 132 -2.659 1.587 3.409 1.00 16.70 6ADH1384
ATOM 986 N ARG A 133 -5.517 .002 2.036 1.00 16.70 6ADH1385
ATOM 987 CA ARG A 133 -5.865 -.939 .957 1.00 16.70 6ADH1386
ATOM 988 C ARG A 133 -7.355 -.713 .556 1.00 16.70 6ADH1387
ATOM 989 O ARG A 133 -7.681 -.533 -.627 1.00 16.70 6ADH1388
ATOM 990 CB ARG A 133 -5.466 -2.363 1.413 1.00 16.70 6ADH1389
ATOM 991 CG ARG A 133 -3.928 -2.603 1.316 1.00 16.70 6ADH1390
ATOM 992 CD ARG A 133 -3.312 -3.378 2.506 1.00 16.70 6ADH1391
ATOM 993 NE ARG A 133 -1.857 -3.127 2.698 1.00 16.70 6ADH1392
ATOM 994 CZ ARG A 133 -.914 -4.093 2.798 1.00 16.70 6ADH1393
ATOM 995 NH1 ARG A 133 -1.241 -5.391 2.717 1.00 16.70 6ADH1394
ATOM 996 NH2 ARG A 133 .391 -3.854 2.987 1.00 16.70 6ADH1395
ATOM 997 N GLY A 134 -8.211 -.709 1.552 1.00 16.70 6ADH1396
ATOM 998 CA GLY A 134 -9.657 -.470 1.402 1.00 16.70 6ADH1397
ATOM 999 C GLY A 134 -10.241 -.475 2.795 1.00 16.70 6ADH1398
ATOM 1000 O GLY A 134 -11.458 -.336 2.987 1.00 16.70 6ADH1399
ATOM 1001 N LYS A 135 -9.309 -.632 3.694 1.00 16.70 6ADH1400
ATOM 1002 CA LYS A 135 -9.581 -.732 5.114 1.00 16.70 6ADH1401
ATOM 1003 C LYS A 135 -9.165 .569 5.799 1.00 16.70 6ADH1402
ATOM 1004 O LYS A 135 -7.978 .936 5.794 1.00 16.70 6ADH1403
ATOM 1005 CB LYS A 135 -8.821 -1.937 5.664 1.00 16.70 6ADH1404
ATOM 1006 CG LYS A 135 -9.135 -3.228 4.902 1.00 16.70 6ADH1405
ATOM 1007 CD LYS A 135 -8.703 -4.488 5.654 1.00 16.70 6ADH1406
ATOM 1008 CE LYS A 135 -7.497 -5.180 5.017 1.00 16.70 6ADH1407
ATOM 1009 NZ LYS A 135 -6.250 -4.968 5.767 1.00 16.70 6ADH1408
ATOM 1010 N PRO A 136 -10.114 1.328 6.400 1.00 16.70 6ADH1409
ATOM 1011 CA PRO A 136 -9.772 2.569 7.058 1.00 16.70 6ADH1410
ATOM 1012 C PRO A 136 -8.796 2.288 8.147 1.00 16.70 6ADH1411
ATOM 1013 O PRO A 136 -8.999 1.311 8.929 1.00 16.70 6ADH1412
ATOM 1014 CB PRO A 136 -11.093 3.095 7.575 1.00 16.70 6ADH1413
ATOM 1015 CG PRO A 136 -12.175 2.104 7.175 1.00 16.70 6ADH1414
ATOM 1016 CD PRO A 136 -11.538 .969 6.435 1.00 16.70 6ADH1415
ATOM 1017 N ILE A 137 -7.773 3.094 8.197 1.00 16.70 6ADH1416
ATOM 1018 CA ILE A 137 -6.772 2.950 9.239 1.00 16.70 6ADH1417
ATOM 1019 C ILE A 137 -7.070 4.001 10.307 1.00 16.70 6ADH1418
ATOM 1020 O ILE A 137 -7.539 5.108 10.001 1.00 16.70 6ADH1419
ATOM 1021 CB ILE A 137 -5.376 3.031 8.628 1.00 16.70 6ADH1420
ATOM 1022 CG1 ILE A 137 -5.029 1.780 7.809 1.00 16.70 6ADH1421
ATOM 1023 CG2 ILE A 137 -4.268 3.154 9.675 1.00 16.70 6ADH1422
ATOM 1024 CD1 ILE A 137 -4.310 2.099 6.497 1.00 16.70 6ADH1423
ATOM 1025 N HIS A 138 -6.796 3.596 11.521 1.00 16.70 6ADH1424
ATOM 1026 CA HIS A 138 -7.072 4.382 12.739 1.00 16.70 6ADH1425
ATOM 1027 C HIS A 138 -6.126 5.593 12.899 1.00 16.70 6ADH1426
ATOM 1028 O HIS A 138 -4.918 5.498 12.636 1.00 16.70 6ADH1427
ATOM 1029 CB HIS A 138 -6.802 3.500 13.974 1.00 16.70 6ADH1428
ATOM 1030 CG HIS A 138 -8.007 2.695 14.481 1.00 16.70 6ADH1429
ATOM 1031 ND1 HIS A 138 -8.032 1.301 14.444 1.00 16.70 6ADH1430
ATOM 1032 CD2 HIS A 138 -9.188 3.077 15.034 1.00 16.70 6ADH1431
ATOM 1033 CE1 HIS A 138 -9.180 .895 14.957 1.00 16.70 6ADH1432
ATOM 1034 NE2 HIS A 138 -9.880 1.941 15.313 1.00 16.70 6ADH1433
ATOM 1035 N HIS A 139 -6.688 6.744 13.327 1.00 16.70 6ADH1434
ATOM 1036 CA HIS A 139 -5.842 7.908 13.713 1.00 16.70 6ADH1435
ATOM 1037 C HIS A 139 -5.420 7.643 15.198 1.00 16.70 6ADH1436
ATOM 1038 O HIS A 139 -6.035 6.830 15.902 1.00 16.70 6ADH1437
ATOM 1039 CB HIS A 139 -6.574 9.301 13.662 1.00 16.70 6ADH1438
ATOM 1040 CG HIS A 139 -7.664 9.582 12.574 1.00 16.70 6ADH1439
ATOM 1041 ND1 HIS A 139 -8.049 10.895 12.254 1.00 16.70 6ADH1440
ATOM 1042 CD2 HIS A 139 -8.438 8.790 11.775 1.00 16.70 6ADH1441
ATOM 1043 CE1 HIS A 139 -8.993 10.856 11.331 1.00 16.70 6ADH1442
ATOM 1044 NE2 HIS A 139 -9.237 9.610 11.033 1.00 16.70 6ADH1443
ATOM 1045 N PHE A 140 -4.374 8.310 15.688 1.00 16.70 6ADH1444
ATOM 1046 CA PHE A 140 -3.884 8.130 17.099 1.00 16.70 6ADH1445
ATOM 1047 C PHE A 140 -4.101 9.424 17.859 1.00 16.70 6ADH1446
ATOM 1048 O PHE A 140 -3.752 10.510 17.374 1.00 16.70 6ADH1447
ATOM 1049 CB PHE A 140 -2.391 7.763 17.077 1.00 16.70 6ADH1448
ATOM 1050 CG PHE A 140 -1.633 7.783 18.429 1.00 16.70 6ADH1449
ATOM 1051 CD1 PHE A 140 -2.300 7.895 19.668 1.00 16.70 6ADH1450
ATOM 1052 CD2 PHE A 140 -.235 7.677 18.409 1.00 16.70 6ADH1451
ATOM 1053 CE1 PHE A 140 -1.561 7.899 20.869 1.00 16.70 6ADH1452
ATOM 1054 CE2 PHE A 140 .495 7.681 19.608 1.00 16.70 6ADH1453
ATOM 1055 CZ PHE A 140 -.165 7.791 20.836 1.00 16.70 6ADH1454
ATOM 1056 N LEU A 141 -4.666 9.268 19.034 1.00 16.70 6ADH1455
ATOM 1057 CA LEU A 141 -5.047 10.407 19.854 1.00 16.70 6ADH1456
ATOM 1058 C LEU A 141 -5.911 11.305 18.967 1.00 16.70 6ADH1457
ATOM 1059 O LEU A 141 -7.147 11.273 19.026 1.00 16.70 6ADH1458
ATOM 1060 CB LEU A 141 -3.804 11.108 20.406 0.00 16.70 2 6ADH1459
ATOM 1061 CG LEU A 141 -3.076 10.277 21.473 1.00 16.70 6ADH1460
ATOM 1062 CD1 LEU A 141 -1.693 10.829 21.819 1.00 16.70 6ADH1461
ATOM 1063 CD2 LEU A 141 -3.834 10.202 22.801 1.00 16.70 6ADH1462
ATOM 1064 N GLY A 142 -5.316 12.102 18.121 1.00 16.70 6ADH1463
ATOM 1065 CA GLY A 142 -6.129 12.956 17.233 1.00 16.70 6ADH1464
ATOM 1066 C GLY A 142 -5.240 13.874 16.433 1.00 16.70 6ADH1465
ATOM 1067 O GLY A 142 -5.566 15.055 16.236 1.00 16.70 6ADH1466
ATOM 1068 N THR A 143 -4.154 13.264 16.000 1.00 16.70 6ADH1467
ATOM 1069 CA THR A 143 -3.103 13.954 15.263 1.00 16.70 6ADH1468
ATOM 1070 C THR A 143 -2.526 13.084 14.120 1.00 16.70 6ADH1469
ATOM 1071 O THR A 143 -2.411 13.537 12.973 1.00 16.70 6ADH1470
ATOM 1072 CB THR A 143 -1.983 14.319 16.233 1.00 16.70 6ADH1471
ATOM 1073 OG1 THR A 143 -1.364 13.140 16.726 1.00 16.70 6ADH1472
ATOM 1074 CG2 THR A 143 -2.480 15.114 17.443 1.00 16.70 6ADH1473
ATOM 1075 N SER A 144 -2.160 11.842 14.440 1.00 16.70 6ADH1474
ATOM 1076 CA SER A 144 -1.558 10.905 13.446 1.00 16.70 6ADH1475
ATOM 1077 C SER A 144 -.680 11.704 12.461 1.00 16.70 6ADH1476
ATOM 1078 O SER A 144 -1.144 12.143 11.400 1.00 16.70 6ADH1477
ATOM 1079 CB SER A 144 -2.665 10.208 12.639 1.00 16.70 6ADH1478
ATOM 1080 OG SER A 144 -3.555 9.529 13.513 1.00 16.70 6ADH1479
ATOM 1081 N THR A 145 .596 11.894 12.792 1.00 16.70 6ADH1480
ATOM 1082 CA THR A 145 1.470 12.764 11.962 1.00 16.70 6ADH1481
ATOM 1083 C THR A 145 2.671 12.029 11.331 1.00 16.70 6ADH1482
ATOM 1084 O THR A 145 3.746 12.617 11.132 1.00 16.70 6ADH1483
ATOM 1085 CB THR A 145 1.984 13.928 12.810 1.00 16.70 6ADH1484
ATOM 1086 OG1 THR A 145 2.608 13.438 13.988 1.00 16.70 6ADH1485
ATOM 1087 CG2 THR A 145 .868 14.879 13.248 1.00 16.70 6ADH1486
ATOM 1088 N PHE A 146 2.453 10.757 11.018 1.00 16.70 6ADH1487
ATOM 1089 CA PHE A 146 3.464 9.917 10.347 1.00 16.70 6ADH1488
ATOM 1090 C PHE A 146 3.029 9.679 8.891 1.00 16.70 6ADH1489
ATOM 1091 O PHE A 146 3.611 8.856 8.171 1.00 16.70 6ADH1490
ATOM 1092 CB PHE A 146 3.641 8.585 11.085 1.00 16.70 6ADH1491
ATOM 1093 CG PHE A 146 4.513 8.709 12.344 1.00 16.70 6ADH1492
ATOM 1094 CD1 PHE A 146 4.821 7.572 13.103 1.00 16.70 6ADH1493
ATOM 1095 CD2 PHE A 146 5.001 9.962 12.739 1.00 16.70 6ADH1494
ATOM 1096 CE1 PHE A 146 5.605 7.689 14.258 1.00 16.70 6ADH1495
ATOM 1097 CE2 PHE A 146 5.784 10.078 13.895 1.00 16.70 6ADH1496
ATOM 1098 CZ PHE A 146 6.085 8.943 14.655 1.00 16.70 6ADH1497
ATOM 1099 N SER A 147 2.001 10.416 8.510 1.00 16.70 6ADH1498
ATOM 1100 CA SER A 147 1.469 10.431 7.135 1.00 16.70 6ADH1499
ATOM 1101 C SER A 147 2.161 11.596 6.419 1.00 16.70 6ADH1500
ATOM 1102 O SER A 147 3.093 12.213 6.953 1.00 16.70 6ADH1501
ATOM 1103 CB SER A 147 -.047 10.658 7.176 1.00 16.70 6ADH1502
ATOM 1104 OG SER A 147 -.715 9.647 6.437 1.00 16.70 6ADH1503
ATOM 1105 N GLN A 148 1.732 11.914 5.219 1.00 16.70 6ADH1504
ATOM 1106 CA GLN A 148 2.293 13.076 4.500 1.00 16.70 6ADH1505
ATOM 1107 C GLN A 148 1.291 14.214 4.630 1.00 16.70 6ADH1506
ATOM 1108 O GLN A 148 1.621 15.381 4.370 1.00 16.70 6ADH1507
ATOM 1109 CB GLN A 148 2.569 12.725 3.044 1.00 16.70 6ADH1508
ATOM 1110 CG GLN A 148 4.040 12.921 2.669 1.00 16.70 6ADH1509
ATOM 1111 CD GLN A 148 4.539 11.897 1.652 1.00 16.70 6ADH1510
ATOM 1112 OE1 GLN A 148 3.774 11.462 .793 1.00 16.70 6ADH1511
ATOM 1113 NE2 GLN A 148 5.791 11.479 1.696 1.00 16.70 6ADH1512
ATOM 1114 N TYR A 149 .122 13.746 5.035 1.00 16.70 6ADH1513
ATOM 1115 CA TYR A 149 -1.048 14.551 5.352 1.00 16.70 6ADH1514
ATOM 1116 C TYR A 149 -1.757 13.923 6.516 1.00 16.70 6ADH1515
ATOM 1117 O TYR A 149 -1.539 12.753 6.860 1.00 16.70 6ADH1516
ATOM 1118 CB TYR A 149 -2.026 14.609 4.185 1.00 16.70 6ADH1517
ATOM 1119 CG TYR A 149 -1.445 15.402 3.041 1.00 16.70 6ADH1518
ATOM 1120 CD1 TYR A 149 -1.810 16.737 2.859 1.00 16.70 6ADH1519
ATOM 1121 CD2 TYR A 149 -.532 14.782 2.192 1.00 16.70 6ADH1520
ATOM 1122 CE1 TYR A 149 -1.239 17.468 1.817 1.00 16.70 6ADH1521
ATOM 1123 CE2 TYR A 149 .041 15.512 1.152 1.00 16.70 6ADH1522
ATOM 1124 CZ TYR A 149 -.309 16.855 .967 1.00 16.70 6ADH1523
ATOM 1125 OH TYR A 149 .261 17.567 -.043 1.00 16.70 6ADH1524
ATOM 1126 N THR A 150 -2.567 14.714 7.087 1.00 16.70 6ADH1525
ATOM 1127 CA THR A 150 -3.394 14.289 8.183 1.00 16.70 6ADH1526
ATOM 1128 C THR A 150 -4.574 15.232 8.267 1.00 16.70 6ADH1527
ATOM 1129 O THR A 150 -4.519 16.364 7.765 1.00 16.70 6ADH1528
ATOM 1130 CB THR A 150 -2.598 14.335 9.487 1.00 16.70 6ADH1529
ATOM 1131 OG1 THR A 150 -2.987 13.257 10.326 1.00 16.70 6ADH1530
ATOM 1132 CG2 THR A 150 -2.814 15.629 10.273 1.00 16.70 6ADH1531
ATOM 1133 N VAL A 151 -5.637 14.761 8.889 1.00 16.70 6ADH1532
ATOM 1134 CA VAL A 151 -6.817 15.611 9.146 1.00 16.70 6ADH1533
ATOM 1135 C VAL A 151 -7.178 15.592 10.622 1.00 16.70 6ADH1534
ATOM 1136 O VAL A 151 -7.717 14.607 11.141 1.00 16.70 6ADH1535
ATOM 1137 CB VAL A 151 -8.086 15.148 8.430 1.00 16.70 6ADH1536
ATOM 1138 CG1 VAL A 151 -9.283 16.062 8.712 1.00 16.70 6ADH1537
ATOM 1139 CG2 VAL A 151 -7.948 15.112 6.908 1.00 16.70 6ADH1538
ATOM 1140 N VAL A 152 -6.885 16.684 11.255 1.00 16.70 6ADH1539
ATOM 1141 CA VAL A 152 -7.170 16.896 12.679 1.00 16.70 6ADH1540
ATOM 1142 C VAL A 152 -8.472 17.763 12.787 1.00 16.70 6ADH1541
ATOM 1143 O VAL A 152 -8.846 18.453 11.825 1.00 16.70 6ADH1542
ATOM 1144 CB VAL A 152 -5.948 17.614 13.264 1.00 16.70 6ADH1543
ATOM 1145 CG1 VAL A 152 -4.639 17.234 12.560 1.00 16.70 6ADH1544
ATOM 1146 CG2 VAL A 152 -6.044 19.136 13.154 1.00 16.70 6ADH1545
ATOM 1147 N ASP A 153 -9.188 17.727 13.959 1.00 16.70 6ADH1546
ATOM 1148 CA ASP A 153 -10.406 18.603 14.181 1.00 16.70 6ADH1547
ATOM 1149 C ASP A 153 -9.894 20.051 14.271 1.00 16.70 6ADH1548
ATOM 1150 O ASP A 153 -8.773 20.358 13.841 1.00 16.70 6ADH1549
ATOM 1151 CB ASP A 153 -11.178 18.224 15.475 1.00 16.70 6ADH1550
ATOM 1152 CG ASP A 153 -12.424 17.341 15.239 1.00 16.70 6ADH1551
ATOM 1153 OD1 ASP A 153 -13.597 17.877 15.149 1.00 16.70 6ADH1552
ATOM 1154 OD2 ASP A 153 -12.298 16.063 15.135 1.00 16.70 6ADH1553
ATOM 1155 N GLU A 154 -10.681 20.952 14.818 1.00 16.70 6ADH1554
ATOM 1156 CA GLU A 154 -10.243 22.355 14.911 1.00 16.70 6ADH1555
ATOM 1157 C GLU A 154 -9.732 22.650 16.307 1.00 16.70 6ADH1556
ATOM 1158 O GLU A 154 -8.774 23.402 16.505 1.00 16.70 6ADH1557
ATOM 1159 CB GLU A 154 -11.383 23.298 14.562 1.00 16.70 6ADH1558
ATOM 1160 CG GLU A 154 -10.916 24.730 14.321 1.00 16.70 6ADH1559
ATOM 1161 CD GLU A 154 -12.085 25.699 14.185 1.00 16.70 6ADH1560
ATOM 1162 OE1 GLU A 154 -13.294 25.250 14.205 1.00 16.70 6ADH1561
ATOM 1163 OE2 GLU A 154 -11.863 26.962 14.050 1.00 16.70 6ADH1562
ATOM 1164 N ILE A 155 -10.343 22.046 17.262 1.00 16.70 6ADH1563
ATOM 1165 CA ILE A 155 -9.946 22.255 18.639 1.00 16.70 6ADH1564
ATOM 1166 C ILE A 155 -8.560 21.707 18.955 1.00 16.70 6ADH1565
ATOM 1167 O ILE A 155 -8.065 21.817 20.083 1.00 16.70 6ADH1566
ATOM 1168 CB ILE A 155 -10.864 21.518 19.583 1.00 16.70 6ADH1567
ATOM 1169 CG1 ILE A 155 -10.960 20.034 19.240 1.00 16.70 6ADH1568
ATOM 1170 CG2 ILE A 155 -12.294 22.056 19.567 1.00 16.70 6ADH1569
ATOM 1171 CD1 ILE A 155 -11.571 19.201 20.365 1.00 16.70 6ADH1570
ATOM 1172 N SER A 156 -7.873 21.100 18.032 1.00 16.70 6ADH1571
ATOM 1173 CA SER A 156 -6.547 20.573 18.401 1.00 16.70 6ADH1572
ATOM 1174 C SER A 156 -5.486 20.941 17.392 1.00 16.70 6ADH1573
ATOM 1175 O SER A 156 -4.580 20.151 17.097 1.00 16.70 6ADH1574
ATOM 1176 CB SER A 156 -6.577 19.048 18.521 1.00 16.70 6ADH1575
ATOM 1177 OG SER A 156 -7.267 18.486 17.416 1.00 16.70 6ADH1576
ATOM 1178 N VAL A 157 -5.610 22.116 16.888 1.00 16.70 6ADH1577
ATOM 1179 CA VAL A 157 -4.668 22.631 15.927 1.00 16.70 6ADH1578
ATOM 1180 C VAL A 157 -4.284 24.026 16.388 1.00 16.70 6ADH1579
ATOM 1181 O VAL A 157 -5.108 24.947 16.357 1.00 16.70 6ADH1580
ATOM 1182 CB VAL A 157 -5.348 22.681 14.554 1.00 16.70 6ADH1581
ATOM 1183 CG1 VAL A 157 -6.606 23.550 14.550 1.00 16.70 6ADH1582
ATOM 1184 CG2 VAL A 157 -4.451 23.248 13.452 1.00 16.70 6ADH1583
ATOM 1185 N ALA A 158 -3.050 24.173 16.831 1.00 16.70 6ADH1584
ATOM 1186 CA ALA A 158 -2.523 25.484 17.256 1.00 16.70 6ADH1585
ATOM 1187 C ALA A 158 -1.755 26.092 16.075 1.00 16.70 6ADH1586
ATOM 1188 O ALA A 158 -1.085 25.377 15.317 1.00 16.70 6ADH1587
ATOM 1189 CB ALA A 158 -1.605 25.320 18.470 1.00 16.70 6ADH1588
ATOM 1190 N LYS A 159 -1.883 27.395 15.957 1.00 16.70 6ADH1589
ATOM 1191 CA LYS A 159 -1.311 28.178 14.846 1.00 16.70 6ADH1590
ATOM 1192 C LYS A 159 -.199 29.094 15.378 1.00 16.70 6ADH1591
ATOM 1193 O LYS A 159 -.442 29.958 16.235 1.00 16.70 6ADH1592
ATOM 1194 CB LYS A 159 -2.455 28.990 14.246 1.00 16.70 6ADH1593
ATOM 1195 CG LYS A 159 -2.044 29.832 13.054 1.00 16.70 6ADH1594
ATOM 1196 CD LYS A 159 -2.743 31.186 13.030 1.00 16.70 6ADH1595
ATOM 1197 CE LYS A 159 -1.981 32.225 12.212 1.00 16.70 6ADH1596
ATOM 1198 NZ LYS A 159 -2.590 33.562 12.272 1.00 16.70 6ADH1597
ATOM 1199 N ILE A 160 1.016 28.905 14.850 1.00 16.70 6ADH1598
ATOM 1200 CA ILE A 160 2.207 29.632 15.365 1.00 16.70 6ADH1599
ATOM 1201 C ILE A 160 2.661 30.825 14.427 1.00 16.70 6ADH1600
ATOM 1202 O ILE A 160 1.831 31.526 13.836 1.00 16.70 6ADH1601
ATOM 1203 CB ILE A 160 3.288 28.598 15.709 1.00 16.70 6ADH1602
ATOM 1204 CG1 ILE A 160 4.252 28.315 14.561 1.00 16.70 6ADH1603
ATOM 1205 CG2 ILE A 160 2.701 27.238 16.101 1.00 16.70 6ADH1604
ATOM 1206 CD1 ILE A 160 3.939 27.008 13.830 1.00 16.70 6ADH1605
ATOM 1207 N ASP A 161 3.985 31.058 14.311 1.00 16.70 6ADH1606
ATOM 1208 CA ASP A 161 4.587 32.298 13.660 1.00 16.70 6ADH1607
ATOM 1209 C ASP A 161 4.323 32.504 12.140 1.00 16.70 6ADH1608
ATOM 1210 O ASP A 161 3.354 33.163 11.742 1.00 16.70 6ADH1609
ATOM 1211 CB ASP A 161 6.101 32.326 13.824 1.00 16.70 6ADH1610
ATOM 1212 CG ASP A 161 6.646 33.740 14.052 1.00 16.70 6ADH1611
ATOM 1213 OD1 ASP A 161 7.448 33.970 15.035 1.00 16.70 6ADH1612
ATOM 1214 OD2 ASP A 161 6.305 34.702 13.260 1.00 16.70 6ADH1613
ATOM 1215 N ALA A 162 5.206 31.959 11.317 1.00 16.70 6ADH1614
ATOM 1216 CA ALA A 162 5.140 32.087 9.835 1.00 16.70 6ADH1615
ATOM 1217 C ALA A 162 6.556 32.304 9.289 1.00 16.70 6ADH1616
ATOM 1218 O ALA A 162 6.764 32.396 8.071 1.00 16.70 6ADH1617
ATOM 1219 CB ALA A 162 4.249 33.268 9.442 1.00 16.70 6ADH1618
ATOM 1220 N ALA A 163 7.443 32.372 10.256 1.00 16.70 6ADH1619
ATOM 1221 CA ALA A 163 8.888 32.509 10.071 1.00 16.70 6ADH1620
ATOM 1222 C ALA A 163 9.552 31.496 10.997 1.00 16.70 6ADH1621
ATOM 1223 O ALA A 163 10.748 31.588 11.299 1.00 16.70 6ADH1622
ATOM 1224 CB ALA A 163 9.333 33.918 10.471 1.00 16.70 6ADH1623
ATOM 1225 N SER A 164 8.727 30.560 11.412 1.00 16.70 6ADH1624
ATOM 1226 CA SER A 164 9.081 29.568 12.438 1.00 16.70 6ADH1625
ATOM 1227 C SER A 164 9.828 28.341 11.924 1.00 16.70 6ADH1626
ATOM 1228 O SER A 164 9.402 27.690 10.957 1.00 16.70 6ADH1627
ATOM 1229 CB SER A 164 7.817 29.032 13.109 1.00 16.70 6ADH1628
ATOM 1230 OG SER A 164 6.779 29.997 13.027 1.00 16.70 6ADH1629
ATOM 1231 N PRO A 165 10.953 28.008 12.571 1.00 16.70 6ADH1630
ATOM 1232 CA PRO A 165 11.696 26.781 12.265 1.00 16.70 6ADH1631
ATOM 1233 C PRO A 165 10.866 25.512 12.546 1.00 16.70 6ADH1632
ATOM 1234 O PRO A 165 10.843 25.021 13.711 0.00 16.70 2 6ADH1633
ATOM 1235 CB PRO A 165 12.872 26.848 13.229 1.00 16.70 6ADH1634
ATOM 1236 CG PRO A 165 12.759 28.134 14.039 1.00 16.70 6ADH1635
ATOM 1237 CD PRO A 165 11.536 28.875 13.605 1.00 16.70 6ADH1636
ATOM 1238 N LEU A 166 10.185 24.897 11.568 1.00 16.70 6ADH1637
ATOM 1239 CA LEU A 166 9.379 23.672 11.881 1.00 16.70 6ADH1638
ATOM 1240 C LEU A 166 10.245 22.409 11.941 1.00 16.70 6ADH1639
ATOM 1241 O LEU A 166 9.767 21.317 12.273 1.00 16.70 6ADH1640
ATOM 1242 CB LEU A 166 8.312 23.352 10.821 1.00 16.70 6ADH1641
ATOM 1243 CG LEU A 166 7.419 24.531 10.422 1.00 16.70 6ADH1642
ATOM 1244 CD1 LEU A 166 6.214 24.102 9.580 1.00 16.70 6ADH1643
ATOM 1245 CD2 LEU A 166 6.837 25.284 11.620 1.00 16.70 6ADH1644
ATOM 1246 N GLU A 167 11.503 22.544 11.600 1.00 16.70 6ADH1645
ATOM 1247 CA GLU A 167 12.436 21.411 11.686 1.00 16.70 6ADH1646
ATOM 1248 C GLU A 167 12.997 21.392 13.114 1.00 16.70 6ADH1647
ATOM 1249 O GLU A 167 13.636 20.416 13.531 1.00 16.70 6ADH1648
ATOM 1250 CB GLU A 167 13.544 21.556 10.644 1.00 16.70 6ADH1649
ATOM 1251 CG GLU A 167 13.767 20.278 9.832 1.00 16.70 6ADH1650
ATOM 1252 CD GLU A 167 15.110 20.266 9.103 1.00 16.70 6ADH1651
ATOM 1253 OE1 GLU A 167 16.186 19.950 9.740 0.00 16.70 2 6ADH1652
ATOM 1254 OE2 GLU A 167 15.167 20.574 7.852 0.00 16.70 2 6ADH1653
ATOM 1255 N LYS A 168 12.693 22.508 13.769 1.00 16.70 6ADH1654
ATOM 1256 CA LYS A 168 13.045 22.812 15.161 1.00 16.70 6ADH1655
ATOM 1257 C LYS A 168 11.824 22.739 16.034 1.00 16.70 6ADH1656
ATOM 1258 O LYS A 168 11.565 21.731 16.708 1.00 16.70 6ADH1657
ATOM 1259 CB LYS A 168 13.452 24.285 15.291 1.00 16.70 6ADH1658
ATOM 1260 CG LYS A 168 14.916 24.486 15.623 1.00 16.70 6ADH1659
ATOM 1261 CD LYS A 168 15.772 24.651 14.374 1.00 16.70 6ADH1660
ATOM 1262 CE LYS A 168 17.243 24.320 14.613 1.00 16.70 6ADH1661
ATOM 1263 NZ LYS A 168 17.472 22.896 14.894 1.00 16.70 6ADH1662
ATOM 1264 N VAL A 169 11.181 23.835 15.935 1.00 16.70 6ADH1663
ATOM 1265 CA VAL A 169 10.003 24.177 16.678 1.00 16.70 6ADH1664
ATOM 1266 C VAL A 169 8.875 23.098 16.637 1.00 16.70 6ADH1665
ATOM 1267 O VAL A 169 7.687 23.403 16.799 1.00 16.70 6ADH1666
ATOM 1268 CB VAL A 169 9.490 25.501 16.106 1.00 16.70 6ADH1667
ATOM 1269 CG1 VAL A 169 8.302 25.335 15.158 1.00 16.70 6ADH1668
ATOM 1270 CG2 VAL A 169 9.028 26.477 17.188 1.00 16.70 6ADH1669
ATOM 1271 N CYS A 170 9.194 21.825 16.452 1.00 16.70 6ADH1670
ATOM 1272 CA CYS A 170 8.183 20.729 16.424 1.00 16.70 6ADH1671
ATOM 1273 C CYS A 170 8.185 19.899 17.692 1.00 16.70 6ADH1672
ATOM 1274 O CYS A 170 7.319 19.030 17.881 1.00 16.70 6ADH1673
ATOM 1275 CB CYS A 170 8.485 20.017 15.016 1.00 16.70 6ADH1674
ATOM 1276 SG CYS A 170 9.714 18.675 15.220 1.00 16.70 6ADH1675
ATOM 1277 N LEU A 171 9.186 20.246 18.462 1.00 16.70 6ADH1676
ATOM 1278 CA LEU A 171 9.500 19.686 19.773 1.00 16.70 6ADH1677
ATOM 1279 C LEU A 171 8.623 20.391 20.845 1.00 16.70 6ADH1678
ATOM 1280 O LEU A 171 8.776 20.164 22.052 1.00 16.70 6ADH1679
ATOM 1281 CB LEU A 171 10.990 20.014 20.093 1.00 16.70 6ADH1680
ATOM 1282 CG LEU A 171 11.954 18.809 20.171 1.00 16.70 6ADH1681
ATOM 1283 CD1 LEU A 171 11.341 17.502 19.667 1.00 16.70 6ADH1682
ATOM 1284 CD2 LEU A 171 13.231 19.006 19.347 1.00 16.70 6ADH1683
ATOM 1285 N ILE A 172 7.705 21.243 20.380 1.00 16.70 6ADH1684
ATOM 1286 CA ILE A 172 6.857 22.090 21.267 1.00 16.70 6ADH1685
ATOM 1287 C ILE A 172 5.418 21.585 21.286 1.00 16.70 6ADH1686
ATOM 1288 O ILE A 172 4.628 21.951 22.173 1.00 16.70 6ADH1687
ATOM 1289 CB ILE A 172 6.932 23.527 20.773 1.00 16.70 6ADH1688
ATOM 1290 CG1 ILE A 172 8.084 24.294 21.422 1.00 16.70 6ADH1689
ATOM 1291 CG2 ILE A 172 5.665 24.331 21.066 1.00 16.70 6ADH1690
ATOM 1292 CD1 ILE A 172 8.295 25.683 20.820 1.00 16.70 6ADH1691
ATOM 1293 N GLY A 173 5.181 20.764 20.288 1.00 16.70 6ADH1692
ATOM 1294 CA GLY A 173 3.929 20.051 20.110 1.00 16.70 6ADH1693
ATOM 1295 C GLY A 173 3.951 18.816 21.028 1.00 16.70 6ADH1694
ATOM 1296 O GLY A 173 3.123 17.904 20.892 1.00 16.70 6ADH1695
ATOM 1297 N CYS A 174 4.926 18.815 21.953 1.00 16.70 6ADH1696
ATOM 1298 CA CYS A 174 5.079 17.738 22.974 1.00 16.70 6ADH1697
ATOM 1299 C CYS A 174 6.463 17.781 23.705 1.00 16.70 6ADH1698
ATOM 1300 O CYS A 174 6.623 18.449 24.732 1.00 16.70 6ADH1699
ATOM 1301 CB CYS A 174 4.918 16.347 22.349 1.00 16.70 6ADH1700
ATOM 1302 SG CYS A 174 4.375 15.135 23.632 1.00 16.70 6ADH1701
ATOM 1303 N GLY A 175 7.423 17.042 23.150 1.00 16.70 6ADH1702
ATOM 1304 CA GLY A 175 8.834 16.896 23.650 1.00 16.70 6ADH1703
ATOM 1305 C GLY A 175 9.224 17.877 24.794 1.00 16.70 6ADH1704
ATOM 1306 O GLY A 175 9.221 17.502 25.976 1.00 16.70 6ADH1705
ATOM 1307 N PHE A 176 9.554 19.101 24.362 1.00 16.70 6ADH1706
ATOM 1308 CA PHE A 176 10.032 20.225 25.218 1.00 16.70 6ADH1707
ATOM 1309 C PHE A 176 8.993 20.644 26.248 1.00 16.70 6ADH1708
ATOM 1310 O PHE A 176 9.131 20.371 27.450 1.00 16.70 6ADH1709
ATOM 1311 CB PHE A 176 10.350 21.457 24.326 1.00 16.70 6ADH1710
ATOM 1312 CG PHE A 176 10.725 22.768 25.070 1.00 16.70 6ADH1711
ATOM 1313 CD1 PHE A 176 9.889 23.898 24.979 1.00 16.70 6ADH1712
ATOM 1314 CD2 PHE A 176 11.909 22.861 25.820 1.00 16.70 6ADH1713
ATOM 1315 CE1 PHE A 176 10.234 25.096 25.627 1.00 16.70 6ADH1714
ATOM 1316 CE2 PHE A 176 12.253 24.062 26.466 1.00 16.70 6ADH1715
ATOM 1317 CZ PHE A 176 11.416 25.178 26.368 1.00 16.70 6ADH1716
ATOM 1318 N SER A 177 7.967 21.295 25.767 1.00 16.70 6ADH1717
ATOM 1319 CA SER A 177 6.968 21.884 26.659 1.00 16.70 6ADH1718
ATOM 1320 C SER A 177 6.073 20.865 27.401 1.00 16.70 6ADH1719
ATOM 1321 O SER A 177 4.873 21.102 27.609 1.00 16.70 6ADH1720
ATOM 1322 CB SER A 177 6.064 22.870 25.915 1.00 16.70 6ADH1721
ATOM 1323 OG SER A 177 5.492 22.251 24.776 1.00 16.70 6ADH1722
ATOM 1324 N THR A 178 6.630 19.725 27.806 1.00 16.70 6ADH1723
ATOM 1325 CA THR A 178 5.924 18.818 28.771 1.00 16.70 6ADH1724
ATOM 1326 C THR A 178 6.909 18.530 29.899 1.00 16.70 6ADH1725
ATOM 1327 O THR A 178 6.520 18.268 31.046 1.00 16.70 6ADH1726
ATOM 1328 CB THR A 178 5.385 17.476 28.211 1.00 16.70 6ADH1727
ATOM 1329 OG1 THR A 178 6.361 16.457 28.353 1.00 16.70 6ADH1728
ATOM 1330 CG2 THR A 178 4.985 17.523 26.736 1.00 16.70 6ADH1729
ATOM 1331 N GLY A 179 8.157 18.597 29.503 1.00 16.70 6ADH1730
ATOM 1332 CA GLY A 179 9.291 18.450 30.400 1.00 16.70 6ADH1731
ATOM 1333 C GLY A 179 9.651 19.838 30.944 1.00 16.70 6ADH1732
ATOM 1334 O GLY A 179 10.264 19.971 32.009 1.00 16.70 6ADH1733
ATOM 1335 N TYR A 180 9.248 20.851 30.196 1.00 16.70 6ADH1734
ATOM 1336 CA TYR A 180 9.492 22.261 30.552 1.00 16.70 6ADH1735
ATOM 1337 C TYR A 180 8.472 22.721 31.598 1.00 16.70 6ADH1736
ATOM 1338 O TYR A 180 8.849 23.235 32.663 0.00 16.70 2 6ADH1737
ATOM 1339 CB TYR A 180 9.296 23.149 29.314 1.00 16.70 6ADH1738
ATOM 1340 CG TYR A 180 9.731 24.597 29.540 1.00 16.70 6ADH1739
ATOM 1341 CD1 TYR A 180 8.775 25.623 29.599 1.00 16.70 6ADH1740
ATOM 1342 CD2 TYR A 180 11.088 24.893 29.686 1.00 16.70 6ADH1741
ATOM 1343 CE1 TYR A 180 9.186 26.947 29.810 1.00 16.70 6ADH1742
ATOM 1344 CE2 TYR A 180 11.497 26.213 29.895 1.00 16.70 6ADH1743
ATOM 1345 CZ TYR A 180 10.547 27.239 29.959 1.00 16.70 6ADH1744
ATOM 1346 OH TYR A 180 10.949 28.522 30.164 1.00 16.70 6ADH1745
ATOM 1347 N GLY A 181 7.224 22.480 31.184 1.00 16.70 6ADH1746
ATOM 1348 CA GLY A 181 5.974 22.867 31.887 1.00 16.70 6ADH1747
ATOM 1349 C GLY A 181 5.733 22.083 33.188 1.00 16.70 6ADH1748
ATOM 1350 O GLY A 181 4.920 22.487 34.031 1.00 16.70 6ADH1749
ATOM 1351 N SER A 182 6.433 20.976 33.317 1.00 16.70 6ADH1750
ATOM 1352 CA SER A 182 6.357 20.117 34.512 1.00 16.70 6ADH1751
ATOM 1353 C SER A 182 7.058 20.798 35.672 1.00 16.70 6ADH1752
ATOM 1354 O SER A 182 6.515 20.887 36.785 0.00 16.70 2 6ADH1753
ATOM 1355 CB SER A 182 7.117 18.810 34.267 1.00 16.70 6ADH1754
ATOM 1356 OG SER A 182 6.287 17.880 33.590 1.00 16.70 6ADH1755
ATOM 1357 N ALA A 183 8.238 21.236 35.307 1.00 16.70 6ADH1756
ATOM 1358 CA ALA A 183 9.205 21.860 36.204 1.00 16.70 6ADH1757
ATOM 1359 C ALA A 183 8.824 23.294 36.610 1.00 16.70 6ADH1758
ATOM 1360 O ALA A 183 9.226 23.781 37.675 1.00 16.70 6ADH1759
ATOM 1361 CB ALA A 183 10.570 21.932 35.516 1.00 16.70 6ADH1760
ATOM 1362 N VAL A 184 8.046 23.963 35.775 1.00 16.70 6ADH1761
ATOM 1363 CA VAL A 184 7.723 25.390 35.997 1.00 16.70 6ADH1762
ATOM 1364 C VAL A 184 6.216 25.664 36.224 1.00 16.70 6ADH1763
ATOM 1365 O VAL A 184 5.822 26.789 36.572 1.00 16.70 6ADH1764
ATOM 1366 CB VAL A 184 8.154 26.196 34.765 1.00 16.70 6ADH1765
ATOM 1367 CG1 VAL A 184 7.224 27.371 34.462 1.00 16.70 6ADH1766
ATOM 1368 CG2 VAL A 184 9.554 26.798 34.901 1.00 16.70 6ADH1767
ATOM 1369 N LYS A 185 5.386 24.634 36.032 1.00 16.70 6ADH1768
ATOM 1370 CA LYS A 185 3.904 24.771 36.151 1.00 16.70 6ADH1769
ATOM 1371 C LYS A 185 3.277 23.803 37.188 1.00 16.70 6ADH1770
ATOM 1372 O LYS A 185 2.618 24.236 38.144 1.00 16.70 6ADH1771
ATOM 1373 CB LYS A 185 3.241 24.451 34.804 1.00 16.70 6ADH1772
ATOM 1374 CG LYS A 185 2.332 25.576 34.300 1.00 16.70 6ADH1773
ATOM 1375 CD LYS A 185 1.018 25.067 33.702 1.00 16.70 6ADH1774
ATOM 1376 CE LYS A 185 .231 26.158 32.973 1.00 16.70 6ADH1775
ATOM 1377 NZ LYS A 185 -1.117 26.360 33.525 1.00 16.70 6ADH1776
ATOM 1378 N VAL A 186 3.527 22.529 36.929 1.00 16.70 6ADH1777
ATOM 1379 CA VAL A 186 2.981 21.360 37.663 1.00 16.70 6ADH1778
ATOM 1380 C VAL A 186 3.694 21.062 39.007 1.00 16.70 6ADH1779
ATOM 1381 O VAL A 186 3.078 20.587 39.972 0.00 16.70 2 6ADH1780
ATOM 1382 CB VAL A 186 3.145 20.123 36.781 1.00 16.70 6ADH1781
ATOM 1383 CG1 VAL A 186 2.759 18.823 37.488 1.00 16.70 6ADH1782
ATOM 1384 CG2 VAL A 186 2.294 20.179 35.512 1.00 16.70 6ADH1783
ATOM 1385 N ALA A 187 4.988 21.311 39.060 1.00 16.70 6ADH1784
ATOM 1386 CA ALA A 187 5.793 21.096 40.290 1.00 16.70 6ADH1785
ATOM 1387 C ALA A 187 6.052 22.452 40.933 1.00 16.70 6ADH1786
ATOM 1388 O ALA A 187 5.815 22.647 42.136 1.00 16.70 6ADH1787
ATOM 1389 CB ALA A 187 7.122 20.429 39.941 1.00 16.70 6ADH1788
ATOM 1390 N LYS A 188 6.552 23.334 40.084 1.00 16.70 6ADH1789
ATOM 1391 CA LYS A 188 6.712 24.763 40.403 1.00 16.70 6ADH1790
ATOM 1392 C LYS A 188 8.049 25.124 41.086 1.00 16.70 6ADH1791
ATOM 1393 O LYS A 188 8.125 26.103 41.846 1.00 16.70 6ADH1792
ATOM 1394 CB LYS A 188 5.560 25.189 41.300 1.00 16.70 6ADH1793
ATOM 1395 CG LYS A 188 4.243 25.319 40.536 1.00 16.70 6ADH1794
ATOM 1396 CD LYS A 188 3.446 26.556 40.948 1.00 16.70 6ADH1795
ATOM 1397 CE LYS A 188 2.517 27.068 39.847 1.00 16.70 6ADH1796
ATOM 1398 NZ LYS A 188 1.276 27.656 40.373 1.00 16.70 6ADH1797
ATOM 1399 N VAL A 189 9.061 24.332 40.772 1.00 16.70 6ADH1798
ATOM 1400 CA VAL A 189 10.439 24.533 41.250 1.00 16.70 6ADH1799
ATOM 1401 C VAL A 189 10.598 25.970 41.803 1.00 16.70 6ADH1800
ATOM 1402 O VAL A 189 10.467 26.950 41.053 0.00 16.70 2 6ADH1801
ATOM 1403 CB VAL A 189 11.398 24.287 40.070 1.00 16.70 6ADH1802
ATOM 1404 CG1 VAL A 189 12.874 24.266 40.473 1.00 16.70 6ADH1803
ATOM 1405 CG2 VAL A 189 11.149 22.950 39.367 1.00 16.70 6ADH1804
ATOM 1406 N THR A 190 10.864 25.994 43.115 1.00 16.70 6ADH1805
ATOM 1407 CA THR A 190 11.102 27.212 43.923 1.00 16.70 6ADH1806
ATOM 1408 C THR A 190 12.535 27.695 43.652 1.00 16.70 6ADH1807
ATOM 1409 O THR A 190 13.472 26.889 43.552 1.00 16.70 6ADH1808
ATOM 1410 CB THR A 190 10.918 26.857 45.404 1.00 16.70 6ADH1809
ATOM 1411 OG1 THR A 190 12.138 26.367 45.943 1.00 16.70 6ADH1810
ATOM 1412 CG2 THR A 190 9.856 25.776 45.627 1.00 16.70 6ADH1811
ATOM 1413 N GLN A 191 12.691 28.997 43.535 1.00 16.70 6ADH1812
ATOM 1414 CA GLN A 191 13.993 29.617 43.199 1.00 16.70 6ADH1813
ATOM 1415 C GLN A 191 15.096 29.250 44.244 1.00 16.70 6ADH1814
ATOM 1416 O GLN A 191 15.150 29.803 45.347 1.00 16.70 6ADH1815
ATOM 1417 CB GLN A 191 13.792 31.151 43.091 0.00 16.70 2 6ADH1816
ATOM 1418 CG GLN A 191 14.985 31.990 43.575 0.00 16.70 2 6ADH1817
ATOM 1419 CD GLN A 191 15.285 33.206 42.681 0.00 16.70 2 6ADH1818
ATOM 1420 OE1 GLN A 191 14.396 34.017 42.419 0.00 16.70 2 6ADH1819
ATOM 1421 NE2 GLN A 191 16.499 33.384 42.193 0.00 16.70 2 6ADH1820
ATOM 1422 N GLY A 192 15.969 28.288 43.871 1.00 16.70 6ADH1821
ATOM 1423 CA GLY A 192 17.176 27.896 44.675 1.00 16.70 6ADH1822
ATOM 1424 C GLY A 192 17.143 26.449 45.258 1.00 16.70 6ADH1823
ATOM 1425 O GLY A 192 17.805 26.148 46.259 1.00 16.70 6ADH1824
ATOM 1426 N SER A 193 16.416 25.530 44.634 1.00 16.70 6ADH1825
ATOM 1427 CA SER A 193 16.186 24.166 45.217 1.00 16.70 6ADH1826
ATOM 1428 C SER A 193 17.074 23.036 44.684 1.00 16.70 6ADH1827
ATOM 1429 O SER A 193 17.969 23.262 43.857 1.00 16.70 6ADH1828
ATOM 1430 CB SER A 193 14.757 23.721 44.904 1.00 16.70 6ADH1829
ATOM 1431 OG SER A 193 14.269 24.418 43.767 1.00 16.70 6ADH1830
ATOM 1432 N THR A 194 16.767 21.844 45.222 1.00 16.70 6ADH1831
ATOM 1433 CA THR A 194 17.408 20.583 44.814 1.00 16.70 6ADH1832
ATOM 1434 C THR A 194 16.369 19.680 44.170 1.00 16.70 6ADH1833
ATOM 1435 O THR A 194 15.426 19.218 44.839 0.00 16.70 2 6ADH1834
ATOM 1436 CB THR A 194 18.089 19.855 45.969 1.00 16.70 6ADH1835
ATOM 1437 OG1 THR A 194 19.094 20.682 46.534 1.00 16.70 6ADH1836
ATOM 1438 CG2 THR A 194 18.766 18.554 45.529 1.00 16.70 6ADH1837
ATOM 1439 N CYS A 195 16.699 19.523 42.892 1.00 16.70 6ADH1838
ATOM 1440 CA CYS A 195 15.931 18.793 41.908 1.00 16.70 6ADH1839
ATOM 1441 C CYS A 195 16.686 17.541 41.448 1.00 16.70 6ADH1840
ATOM 1442 O CYS A 195 17.883 17.596 41.124 1.00 16.70 6ADH1841
ATOM 1443 CB CYS A 195 15.697 19.682 40.647 1.00 16.70 6ADH1842
ATOM 1444 SG CYS A 195 14.977 21.266 40.482 1.00 16.70 6ADH1843
ATOM 1445 N ALA A 196 15.931 16.470 41.441 1.00 16.70 6ADH1844
ATOM 1446 CA ALA A 196 16.374 15.166 40.951 1.00 16.70 6ADH1845
ATOM 1447 C ALA A 196 15.457 14.767 39.784 1.00 16.70 6ADH1846
ATOM 1448 O ALA A 196 14.226 14.731 39.922 1.00 16.70 6ADH1847
ATOM 1449 CB ALA A 196 16.264 14.123 42.066 1.00 16.70 6ADH1848
ATOM 1450 N VAL A 197 16.067 14.473 38.645 1.00 16.70 6ADH1849
ATOM 1451 CA VAL A 197 15.312 14.090 37.434 1.00 16.70 6ADH1850
ATOM 1452 C VAL A 197 15.723 12.695 36.935 1.00 16.70 6ADH1851
ATOM 1453 O VAL A 197 16.800 12.519 36.347 1.00 16.70 6ADH1852
ATOM 1454 CB VAL A 197 15.558 15.094 36.302 1.00 16.70 6ADH1853
ATOM 1455 CG1 VAL A 197 14.640 14.874 35.097 1.00 16.70 6ADH1854
ATOM 1456 CG2 VAL A 197 15.335 16.546 36.730 1.00 16.70 6ADH1855
ATOM 1457 N PHE A 198 14.828 11.745 37.201 1.00 16.70 6ADH1856
ATOM 1458 CA PHE A 198 14.973 10.341 36.768 1.00 16.70 6ADH1857
ATOM 1459 C PHE A 198 14.595 10.253 35.282 1.00 16.70 6ADH1858
ATOM 1460 O PHE A 198 13.481 10.626 34.882 1.00 16.70 6ADH1859
ATOM 1461 CB PHE A 198 14.019 9.427 37.560 1.00 16.70 6ADH1860
ATOM 1462 CG PHE A 198 14.402 9.201 39.035 1.00 16.70 6ADH1861
ATOM 1463 CD1 PHE A 198 14.770 7.921 39.479 1.00 16.70 6ADH1862
ATOM 1464 CD2 PHE A 198 14.373 10.264 39.949 1.00 16.70 6ADH1863
ATOM 1465 CE1 PHE A 198 15.100 7.705 40.825 1.00 16.70 6ADH1864
ATOM 1466 CE2 PHE A 198 14.702 10.048 41.295 1.00 16.70 6ADH1865
ATOM 1467 CZ PHE A 198 15.064 8.769 41.732 1.00 16.70 6ADH1866
ATOM 1468 N GLY A 199 15.532 9.758 34.500 1.00 16.70 6ADH1867
ATOM 1469 CA GLY A 199 15.379 9.663 33.043 1.00 16.70 6ADH1868
ATOM 1470 C GLY A 199 15.923 10.952 32.428 1.00 16.70 6ADH1869
ATOM 1471 O GLY A 199 15.399 12.049 32.676 1.00 16.70 6ADH1870
ATOM 1472 N LEU A 200 16.969 10.792 31.642 1.00 16.70 6ADH1871
ATOM 1473 CA LEU A 200 17.669 11.926 31.012 1.00 16.70 6ADH1872
ATOM 1474 C LEU A 200 17.456 11.978 29.500 1.00 16.70 6ADH1873
ATOM 1475 O LEU A 200 18.393 12.265 28.743 1.00 16.70 6ADH1874
ATOM 1476 CB LEU A 200 19.183 11.791 31.184 1.00 16.70 6ADH1875
ATOM 1477 CG LEU A 200 19.646 11.851 32.635 1.00 16.70 6ADH1876
ATOM 1478 CD1 LEU A 200 21.111 11.444 32.806 1.00 16.70 6ADH1877
ATOM 1479 CD2 LEU A 200 19.529 13.250 33.240 1.00 16.70 6ADH1878
ATOM 1480 N GLY A 201 16.230 11.705 29.089 1.00 16.70 6ADH1879
ATOM 1481 CA GLY A 201 15.849 11.679 27.664 1.00 16.70 6ADH1880
ATOM 1482 C GLY A 201 15.376 13.060 27.184 1.00 16.70 6ADH1881
ATOM 1483 O GLY A 201 15.639 14.085 27.830 0.00 16.70 2 6ADH1882
ATOM 1484 N GLY A 202 14.682 13.016 26.056 1.00 16.70 6ADH1883
ATOM 1485 CA GLY A 202 14.144 14.205 25.366 1.00 16.70 6ADH1884
ATOM 1486 C GLY A 202 13.320 15.093 26.313 1.00 16.70 6ADH1885
ATOM 1487 O GLY A 202 13.620 16.282 26.496 1.00 16.70 6ADH1886
ATOM 1488 N VAL A 203 12.298 14.488 26.889 1.00 16.70 6ADH1887
ATOM 1489 CA VAL A 203 11.360 15.176 27.798 1.00 16.70 6ADH1888
ATOM 1490 C VAL A 203 12.006 15.483 29.157 1.00 16.70 6ADH1889
ATOM 1491 O VAL A 203 11.578 16.400 29.874 1.00 16.70 6ADH1890
ATOM 1492 CB VAL A 203 10.143 14.285 28.066 1.00 16.70 6ADH1891
ATOM 1493 CG1 VAL A 203 9.115 14.937 28.993 1.00 16.70 6ADH1892
ATOM 1494 CG2 VAL A 203 9.377 13.915 26.794 1.00 16.70 6ADH1893
ATOM 1495 N GLY A 204 13.030 14.701 29.466 1.00 16.70 6ADH1894
ATOM 1496 CA GLY A 204 13.734 14.760 30.764 1.00 16.70 6ADH1895
ATOM 1497 C GLY A 204 14.949 15.698 30.753 1.00 16.70 6ADH1896
ATOM 1498 O GLY A 204 15.752 15.715 31.697 1.00 16.70 6ADH1897
ATOM 1499 N LEU A 205 15.083 16.460 29.697 1.00 16.70 6ADH1898
ATOM 1500 CA LEU A 205 16.174 17.437 29.589 1.00 16.70 6ADH1899
ATOM 1501 C LEU A 205 15.557 18.819 29.627 1.00 16.70 6ADH1900
ATOM 1502 O LEU A 205 16.194 19.793 30.055 1.00 16.70 6ADH1901
ATOM 1503 CB LEU A 205 16.954 17.213 28.300 1.00 16.70 6ADH1902
ATOM 1504 CG LEU A 205 18.031 16.139 28.454 1.00 16.70 6ADH1903
ATOM 1505 CD1 LEU A 205 18.731 15.799 27.136 1.00 16.70 6ADH1904
ATOM 1506 CD2 LEU A 205 19.145 16.541 29.422 1.00 16.70 6ADH1905
ATOM 1507 N SER A 206 14.329 18.816 29.174 1.00 16.70 6ADH1906
ATOM 1508 CA SER A 206 13.492 19.997 29.158 1.00 16.70 6ADH1907
ATOM 1509 C SER A 206 12.986 20.238 30.584 1.00 16.70 6ADH1908
ATOM 1510 O SER A 206 12.700 21.379 30.978 0.00 16.70 2 6ADH1909
ATOM 1511 CB SER A 206 12.327 19.781 28.190 1.00 16.70 6ADH1910
ATOM 1512 OG SER A 206 12.769 19.043 27.058 1.00 16.70 6ADH1911
ATOM 1513 N VAL A 207 12.890 19.144 31.335 1.00 16.70 6ADH1912
ATOM 1514 CA VAL A 207 12.440 19.190 32.740 1.00 16.70 6ADH1913
ATOM 1515 C VAL A 207 13.585 19.632 33.645 1.00 16.70 6ADH1914
ATOM 1516 O VAL A 207 13.365 20.103 34.771 0.00 16.70 2 6ADH1915
ATOM 1517 CB VAL A 207 11.959 17.822 33.226 1.00 16.70 6ADH1916
ATOM 1518 CG1 VAL A 207 12.129 17.634 34.735 1.00 16.70 6ADH1917
ATOM 1519 CG2 VAL A 207 10.476 17.574 32.942 1.00 16.70 6ADH1918
ATOM 1520 N ILE A 208 14.788 19.466 33.138 1.00 16.70 6ADH1919
ATOM 1521 CA ILE A 208 15.990 19.884 33.863 1.00 16.70 6ADH1920
ATOM 1522 C ILE A 208 16.404 21.266 33.377 1.00 16.70 6ADH1921
ATOM 1523 O ILE A 208 17.213 21.953 34.017 1.00 16.70 6ADH1922
ATOM 1524 CB ILE A 208 17.135 18.892 33.658 1.00 16.70 6ADH1923
ATOM 1525 CG1 ILE A 208 18.319 19.490 32.898 1.00 16.70 6ADH1924
ATOM 1526 CG2 ILE A 208 16.720 17.650 32.870 1.00 16.70 6ADH1925
ATOM 1527 CD1 ILE A 208 19.547 18.577 32.891 1.00 16.70 6ADH1926
ATOM 1528 N MET A 209 15.841 21.653 32.243 1.00 16.70 6ADH1927
ATOM 1529 CA MET A 209 16.103 22.983 31.697 1.00 16.70 6ADH1928
ATOM 1530 C MET A 209 14.917 23.902 32.026 1.00 16.70 6ADH1929
ATOM 1531 O MET A 209 14.849 25.050 31.567 1.00 16.70 6ADH1930
ATOM 1532 CB MET A 209 16.445 22.939 30.192 1.00 16.70 6ADH1931
ATOM 1533 CG MET A 209 15.378 22.312 29.298 1.00 16.70 6ADH1932
ATOM 1534 SD MET A 209 15.830 22.337 27.574 1.00 16.70 6ADH1933
ATOM 1535 CE MET A 209 15.566 23.961 26.894 1.00 16.70 6ADH1934
ATOM 1536 N GLY A 210 14.026 23.356 32.829 1.00 16.70 6ADH1935
ATOM 1537 CA GLY A 210 12.867 24.078 33.352 1.00 16.70 6ADH1936
ATOM 1538 C GLY A 210 13.155 24.405 34.816 1.00 16.70 6ADH1937
ATOM 1539 O GLY A 210 12.715 25.434 35.347 1.00 16.70 6ADH1938
ATOM 1540 N CYS A 211 13.896 23.505 35.427 1.00 16.70 6ADH1939
ATOM 1541 CA CYS A 211 14.319 23.651 36.823 1.00 16.70 6ADH1940
ATOM 1542 C CYS A 211 15.394 24.742 36.908 1.00 16.70 6ADH1941
ATOM 1543 O CYS A 211 15.402 25.557 37.842 1.00 16.70 6ADH1942
ATOM 1544 CB CYS A 211 14.925 22.330 37.342 1.00 16.70 6ADH1943
ATOM 1545 SG CYS A 211 13.741 20.899 37.275 1.00 16.70 6ADH1944
ATOM 1546 N LYS A 212 16.261 24.701 35.901 1.00 16.70 6ADH1945
ATOM 1547 CA LYS A 212 17.426 25.602 35.772 1.00 16.70 6ADH1946
ATOM 1548 C LYS A 212 17.009 27.042 35.472 1.00 16.70 6ADH1947
ATOM 1549 O LYS A 212 17.793 27.985 35.646 0.00 16.70 2 6ADH1948
ATOM 1550 CB LYS A 212 18.344 25.128 34.647 1.00 16.70 6ADH1949
ATOM 1551 CG LYS A 212 19.827 25.349 34.958 1.00 16.70 6ADH1950
ATOM 1552 CD LYS A 212 20.537 26.210 33.912 1.00 16.70 6ADH1951
ATOM 1553 CE LYS A 212 22.037 26.357 34.177 1.00 16.70 6ADH1952
ATOM 1554 NZ LYS A 212 22.347 26.632 35.588 1.00 16.70 6ADH1953
ATOM 1555 N ALA A 213 15.791 27.198 35.019 1.00 16.70 6ADH1954
ATOM 1556 CA ALA A 213 15.236 28.528 34.755 1.00 16.70 6ADH1955
ATOM 1557 C ALA A 213 14.448 28.966 35.986 1.00 16.70 6ADH1956
ATOM 1558 O ALA A 213 14.383 30.159 36.314 0.00 16.70 2 6ADH1957
ATOM 1559 CB ALA A 213 14.315 28.484 33.536 1.00 16.70 6ADH1958
ATOM 1560 N ALA A 214 13.878 27.958 36.621 1.00 16.70 6ADH1959
ATOM 1561 CA ALA A 214 13.067 28.121 37.835 1.00 16.70 6ADH1960
ATOM 1562 C ALA A 214 13.941 28.619 38.988 1.00 16.70 6ADH1961
ATOM 1563 O ALA A 214 13.439 28.944 40.074 1.00 16.70 6ADH1962
ATOM 1564 CB ALA A 214 12.453 26.776 38.234 1.00 16.70 6ADH1963
ATOM 1565 N GLY A 215 15.224 28.658 38.694 1.00 16.70 6ADH1964
ATOM 1566 CA GLY A 215 16.268 29.045 39.651 1.00 16.70 6ADH1965
ATOM 1567 C GLY A 215 17.159 27.824 39.908 1.00 16.70 6ADH1966
ATOM 1568 O GLY A 215 18.306 27.765 39.445 1.00 16.70 6ADH1967
ATOM 1569 N ALA A 216 16.571 26.891 40.641 1.00 16.70 6ADH1968
ATOM 1570 CA ALA A 216 17.187 25.594 41.003 1.00 16.70 6ADH1969
ATOM 1571 C ALA A 216 18.718 25.692 41.069 1.00 16.70 6ADH1970
ATOM 1572 O ALA A 216 19.398 25.767 40.034 0.00 16.70 2 6ADH1971
ATOM 1573 CB ALA A 216 16.811 24.532 39.969 1.00 16.70 6ADH1972
ATOM 1574 N ALA A 217 19.177 25.675 42.315 1.00 16.70 6ADH1973
ATOM 1575 CA ALA A 217 20.601 25.778 42.681 1.00 16.70 6ADH1974
ATOM 1576 C ALA A 217 21.337 24.457 42.424 1.00 16.70 6ADH1975
ATOM 1577 O ALA A 217 22.553 24.438 42.186 1.00 16.70 6ADH1976
ATOM 1578 CB ALA A 217 20.732 26.117 44.167 0.00 16.70 2 6ADH1977
ATOM 1579 N ARG A 218 20.578 23.386 42.486 1.00 16.70 6ADH1978
ATOM 1580 CA ARG A 218 21.090 22.026 42.256 1.00 16.70 6ADH1979
ATOM 1581 C ARG A 218 20.108 21.266 41.371 1.00 16.70 6ADH1980
ATOM 1582 O ARG A 218 18.913 21.587 41.319 1.00 16.70 6ADH1981
ATOM 1583 CB ARG A 218 21.229 21.280 43.585 1.00 16.70 6ADH1982
ATOM 1584 CG ARG A 218 22.036 19.981 43.473 1.00 16.70 6ADH1983
ATOM 1585 CD ARG A 218 23.259 19.976 44.393 1.00 16.70 6ADH1984
ATOM 1586 NE ARG A 218 23.757 18.631 44.725 1.00 16.70 6ADH1985
ATOM 1587 CZ ARG A 218 23.524 18.012 45.892 1.00 16.70 6ADH1986
ATOM 1588 NH1 ARG A 218 22.776 18.586 46.844 1.00 16.70 6ADH1987
ATOM 1589 NH2 ARG A 218 24.020 16.808 46.215 1.00 16.70 6ADH1988
ATOM 1590 N ILE A 219 20.632 20.278 40.696 1.00 16.70 6ADH1989
ATOM 1591 CA ILE A 219 19.849 19.441 39.777 1.00 16.70 6ADH1990
ATOM 1592 C ILE A 219 20.674 18.217 39.400 1.00 16.70 6ADH1991
ATOM 1593 O ILE A 219 21.705 18.326 38.729 1.00 16.70 6ADH1992
ATOM 1594 CB ILE A 219 19.560 20.211 38.493 1.00 16.70 6ADH1993
ATOM 1595 CG1 ILE A 219 18.629 21.405 38.690 1.00 16.70 6ADH1994
ATOM 1596 CG2 ILE A 219 18.896 19.347 37.421 1.00 16.70 6ADH1995
ATOM 1597 CD1 ILE A 219 18.215 22.059 37.370 1.00 16.70 6ADH1996
ATOM 1598 N ILE A 220 20.205 17.082 39.818 1.00 16.70 6ADH1997
ATOM 1599 CA ILE A 220 20.903 15.809 39.625 1.00 16.70 6ADH1998
ATOM 1600 C ILE A 220 20.228 15.080 38.461 1.00 16.70 6ADH1999
ATOM 1601 O ILE A 220 19.118 15.412 38.039 1.00 16.70 6ADH2000
ATOM 1602 CB ILE A 220 20.771 15.079 40.957 1.00 16.70 6ADH2001
ATOM 1603 CG1 ILE A 220 20.630 16.062 42.130 1.00 16.70 6ADH2002
ATOM 1604 CG2 ILE A 220 21.965 14.181 41.275 1.00 16.70 6ADH2003
ATOM 1605 CD1 ILE A 220 21.149 15.501 43.455 1.00 16.70 6ADH2004
ATOM 1606 N GLY A 221 20.833 14.096 37.892 1.00 16.70 6ADH2005
ATOM 1607 CA GLY A 221 20.177 13.383 36.795 1.00 16.70 6ADH2006
ATOM 1608 C GLY A 221 20.456 11.912 36.963 1.00 16.70 6ADH2007
ATOM 1609 O GLY A 221 21.615 11.503 37.094 1.00 16.70 6ADH2008
ATOM 1610 N VAL A 222 19.406 11.124 36.970 1.00 16.70 6ADH2009
ATOM 1611 CA VAL A 222 19.553 9.672 37.126 1.00 16.70 6ADH2010
ATOM 1612 C VAL A 222 19.120 8.953 35.865 1.00 16.70 6ADH2011
ATOM 1613 O VAL A 222 17.945 8.997 35.476 1.00 16.70 6ADH2012
ATOM 1614 CB VAL A 222 18.698 9.144 38.275 1.00 16.70 6ADH2013
ATOM 1615 CG1 VAL A 222 19.254 7.855 38.886 1.00 16.70 6ADH2014
ATOM 1616 CG2 VAL A 222 18.575 10.133 39.434 1.00 16.70 6ADH2015
ATOM 1617 N ASP A 223 20.093 8.316 35.282 1.00 16.70 6ADH2016
ATOM 1618 CA ASP A 223 19.918 7.520 34.077 1.00 16.70 6ADH2017
ATOM 1619 C ASP A 223 20.883 6.335 34.163 1.00 16.70 6ADH2018
ATOM 1620 O ASP A 223 21.986 6.450 34.714 1.00 16.70 6ADH2019
ATOM 1621 CB ASP A 223 20.190 8.385 32.857 1.00 16.70 6ADH2020
ATOM 1622 CG ASP A 223 19.344 7.963 31.667 1.00 16.70 6ADH2021
ATOM 1623 OD1 ASP A 223 18.577 8.820 31.083 1.00 16.70 6ADH2022
ATOM 1624 OD2 ASP A 223 19.395 6.746 31.247 1.00 16.70 6ADH2023
ATOM 1625 N ILE A 224 20.469 5.201 33.629 1.00 16.70 6ADH2024
ATOM 1626 CA ILE A 224 21.278 3.960 33.706 1.00 16.70 6ADH2025
ATOM 1627 C ILE A 224 22.183 3.831 32.475 1.00 16.70 6ADH2026
ATOM 1628 O ILE A 224 22.836 2.793 32.277 1.00 16.70 6ADH2027
ATOM 1629 CB ILE A 224 20.349 2.755 33.830 1.00 16.70 6ADH2028
ATOM 1630 CG1 ILE A 224 19.362 2.632 32.670 1.00 16.70 6ADH2029
ATOM 1631 CG2 ILE A 224 19.494 2.795 35.099 1.00 16.70 6ADH2030
ATOM 1632 CD1 ILE A 224 19.022 1.179 32.330 1.00 16.70 6ADH2031
ATOM 1633 N ASN A 225 22.149 4.926 31.739 1.00 16.70 6ADH2032
ATOM 1634 CA ASN A 225 22.900 5.156 30.499 1.00 16.70 6ADH2033
ATOM 1635 C ASN A 225 23.819 6.364 30.709 1.00 16.70 6ADH2034
ATOM 1636 O ASN A 225 23.476 7.502 30.353 1.00 16.70 6ADH2035
ATOM 1637 CB ASN A 225 21.892 5.474 29.383 1.00 16.70 6ADH2036
ATOM 1638 CG ASN A 225 22.476 5.401 27.973 1.00 16.70 6ADH2037
ATOM 1639 OD1 ASN A 225 21.836 5.843 27.020 1.00 16.70 6ADH2038
ATOM 1640 ND2 ASN A 225 23.665 4.863 27.778 1.00 16.70 6ADH2039
ATOM 1641 N LYS A 226 24.976 6.115 31.292 1.00 16.70 6ADH2040
ATOM 1642 CA LYS A 226 25.924 7.197 31.596 1.00 16.70 6ADH2041
ATOM 1643 C LYS A 226 26.219 8.016 30.335 1.00 16.70 6ADH2042
ATOM 1644 O LYS A 226 26.746 9.135 30.409 1.00 16.70 6ADH2043
ATOM 1645 CB LYS A 226 27.229 6.640 32.174 1.00 16.70 6ADH2044
ATOM 1646 CG LYS A 226 27.852 5.541 31.313 1.00 16.70 6ADH2045
ATOM 1647 CD LYS A 226 28.741 6.090 30.195 1.00 16.70 6ADH2046
ATOM 1648 CE LYS A 226 30.234 5.904 30.472 1.00 16.70 6ADH2047
ATOM 1649 NZ LYS A 226 30.965 7.176 30.561 1.00 16.70 6ADH2048
ATOM 1650 N ASP A 227 25.867 7.451 29.198 1.00 16.70 6ADH2049
ATOM 1651 CA ASP A 227 26.069 8.114 27.903 1.00 16.70 6ADH2050
ATOM 1652 C ASP A 227 25.234 9.418 27.819 1.00 16.70 6ADH2051
ATOM 1653 O ASP A 227 25.547 10.325 27.033 1.00 16.70 6ADH2052
ATOM 1654 CB ASP A 227 25.614 7.196 26.746 1.00 16.70 6ADH2053
ATOM 1655 CG ASP A 227 26.724 6.302 26.168 1.00 16.70 6ADH2054
ATOM 1656 OD1 ASP A 227 26.555 5.718 25.029 1.00 16.70 6ADH2055
ATOM 1657 OD2 ASP A 227 27.825 6.133 26.817 1.00 16.70 6ADH2056
ATOM 1658 N LYS A 228 24.171 9.513 28.634 1.00 16.70 6ADH2057
ATOM 1659 CA LYS A 228 23.218 10.672 28.575 1.00 16.70 6ADH2058
ATOM 1660 C LYS A 228 23.632 11.887 29.428 1.00 16.70 6ADH2059
ATOM 1661 O LYS A 228 23.097 12.994 29.261 1.00 16.70 6ADH2060
ATOM 1662 CB LYS A 228 21.836 10.283 29.125 1.00 16.70 6ADH2061
ATOM 1663 CG LYS A 228 21.231 9.060 28.438 1.00 16.70 6ADH2062
ATOM 1664 CD LYS A 228 19.998 9.394 27.600 1.00 16.70 6ADH2063
ATOM 1665 CE LYS A 228 19.815 8.455 26.407 1.00 16.70 6ADH2064
ATOM 1666 NZ LYS A 228 19.028 7.256 26.733 1.00 16.70 6ADH2065
ATOM 1667 N PHE A 229 24.575 11.646 30.302 1.00 16.70 6ADH2066
ATOM 1668 CA PHE A 229 25.015 12.601 31.347 1.00 16.70 6ADH2067
ATOM 1669 C PHE A 229 25.557 13.942 30.818 1.00 16.70 6ADH2068
ATOM 1670 O PHE A 229 25.510 14.964 31.526 0.00 16.70 2 6ADH2069
ATOM 1671 CB PHE A 229 26.093 11.938 32.184 1.00 16.70 6ADH2070
ATOM 1672 CG PHE A 229 25.511 10.816 33.038 1.00 16.70 6ADH2071
ATOM 1673 CD1 PHE A 229 24.128 10.606 33.048 1.00 16.70 6ADH2072
ATOM 1674 CD2 PHE A 229 26.351 10.006 33.807 1.00 16.70 6ADH2073
ATOM 1675 CE1 PHE A 229 23.582 9.588 33.835 1.00 16.70 6ADH2074
ATOM 1676 CE2 PHE A 229 25.805 8.988 34.595 1.00 16.70 6ADH2075
ATOM 1677 CZ PHE A 229 24.420 8.781 34.611 1.00 16.70 6ADH2076
ATOM 1678 N ALA A 230 26.051 13.901 29.589 1.00 16.70 6ADH2077
ATOM 1679 CA ALA A 230 26.684 15.065 28.928 1.00 16.70 6ADH2078
ATOM 1680 C ALA A 230 25.660 16.062 28.345 1.00 16.70 6ADH2079
ATOM 1681 O ALA A 230 25.683 17.261 28.656 1.00 16.70 6ADH2080
ATOM 1682 CB ALA A 230 27.577 14.597 27.777 1.00 16.70 6ADH2081
ATOM 1683 N LYS A 231 24.776 15.585 27.489 1.00 16.70 6ADH2082
ATOM 1684 CA LYS A 231 23.756 16.456 26.851 1.00 16.70 6ADH2083
ATOM 1685 C LYS A 231 22.929 17.134 27.931 1.00 16.70 6ADH2084
ATOM 1686 O LYS A 231 22.169 18.075 27.643 1.00 16.70 6ADH2085
ATOM 1687 CB LYS A 231 22.806 15.610 26.014 1.00 16.70 6ADH2086
ATOM 1688 CG LYS A 231 22.520 16.219 24.649 1.00 16.70 6ADH2087
ATOM 1689 CD LYS A 231 22.728 15.229 23.509 1.00 16.70 6ADH2088
ATOM 1690 CE LYS A 231 21.422 14.812 22.836 0.00 16.70 2 6ADH2089
ATOM 1691 NZ LYS A 231 21.361 15.196 21.419 0.00 16.70 2 6ADH2090
ATOM 1692 N ALA A 232 23.182 16.549 29.100 1.00 16.70 6ADH2091
ATOM 1693 CA ALA A 232 22.517 16.831 30.382 1.00 16.70 6ADH2092
ATOM 1694 C ALA A 232 23.250 17.906 31.175 1.00 16.70 6ADH2093
ATOM 1695 O ALA A 232 22.735 19.013 31.383 1.00 16.70 6ADH2094
ATOM 1696 CB ALA A 232 22.478 15.557 31.224 1.00 16.70 6ADH2095
ATOM 1697 N LYS A 233 24.436 17.583 31.640 1.00 16.70 6ADH2096
ATOM 1698 CA LYS A 233 25.239 18.583 32.332 1.00 16.70 6ADH2097
ATOM 1699 C LYS A 233 25.271 19.820 31.458 1.00 16.70 6ADH2098
ATOM 1700 O LYS A 233 25.294 20.956 31.951 1.00 16.70 6ADH2099
ATOM 1701 CB LYS A 233 26.682 18.110 32.513 1.00 16.70 6ADH2100
ATOM 1702 CG LYS A 233 26.789 16.723 33.137 1.00 16.70 6ADH2101
ATOM 1703 CD LYS A 233 27.843 16.651 34.240 1.00 16.70 6ADH2102
ATOM 1704 CE LYS A 233 27.766 15.358 35.053 1.00 16.70 6ADH2103
ATOM 1705 NZ LYS A 233 28.942 14.496 34.871 1.00 16.70 6ADH2104
ATOM 1706 N GLU A 234 25.269 19.550 30.172 1.00 16.70 6ADH2105
ATOM 1707 CA GLU A 234 25.322 20.603 29.169 1.00 16.70 6ADH2106
ATOM 1708 C GLU A 234 24.026 21.414 29.171 1.00 16.70 6ADH2107
ATOM 1709 O GLU A 234 24.004 22.584 28.760 1.00 16.70 6ADH2108
ATOM 1710 CB GLU A 234 25.547 20.025 27.777 1.00 16.70 6ADH2109
ATOM 1711 CG GLU A 234 25.886 21.102 26.745 1.00 16.70 6ADH2110
ATOM 1712 CD GLU A 234 25.294 20.810 25.368 1.00 16.70 6ADH2111
ATOM 1713 OE1 GLU A 234 24.805 21.770 24.658 1.00 16.70 6ADH2112
ATOM 1714 OE2 GLU A 234 25.283 19.602 24.915 1.00 16.70 6ADH2113
ATOM 1715 N VAL A 235 22.941 20.807 29.640 1.00 16.70 6ADH2114
ATOM 1716 CA VAL A 235 21.652 21.527 29.686 1.00 16.70 6ADH2115
ATOM 1717 C VAL A 235 21.435 22.262 31.023 1.00 16.70 6ADH2116
ATOM 1718 O VAL A 235 20.545 23.109 31.156 0.00 16.70 2 6ADH2117
ATOM 1719 CB VAL A 235 20.444 20.609 29.464 1.00 16.70 6ADH2118
ATOM 1720 CG1 VAL A 235 19.928 20.640 28.022 1.00 16.70 6ADH2119
ATOM 1721 CG2 VAL A 235 20.734 19.140 29.770 1.00 16.70 6ADH2120
ATOM 1722 N GLY A 236 22.218 21.984 32.039 1.00 16.70 6ADH2121
ATOM 1723 CA GLY A 236 22.059 22.700 33.331 1.00 16.70 6ADH2122
ATOM 1724 C GLY A 236 21.890 21.702 34.470 1.00 16.70 6ADH2123
ATOM 1725 O GLY A 236 21.292 22.024 35.510 0.00 16.70 2 6ADH2124
ATOM 1726 N ALA A 237 22.448 20.535 34.180 1.00 16.70 6ADH2125
ATOM 1727 CA ALA A 237 22.459 19.364 35.071 1.00 16.70 6ADH2126
ATOM 1728 C ALA A 237 23.820 19.270 35.775 1.00 16.70 6ADH2127
ATOM 1729 O ALA A 237 24.810 18.798 35.193 0.00 16.70 2 6ADH2128
ATOM 1730 CB ALA A 237 22.202 18.097 34.257 1.00 16.70 6ADH2129
ATOM 1731 N THR A 238 23.734 19.726 36.999 1.00 16.70 6ADH2130
ATOM 1732 CA THR A 238 24.833 19.924 37.950 1.00 16.70 6ADH2131
ATOM 1733 C THR A 238 25.536 18.596 38.400 1.00 16.70 6ADH2132
ATOM 1734 O THR A 238 26.771 18.483 38.367 0.00 16.70 2 6ADH2133
ATOM 1735 CB THR A 238 24.227 20.709 39.120 1.00 16.70 6ADH2134
ATOM 1736 OG1 THR A 238 24.525 22.091 38.980 1.00 16.70 6ADH2135
ATOM 1737 CG2 THR A 238 24.744 20.265 40.487 1.00 16.70 6ADH2136
ATOM 1738 N GLU A 239 24.759 17.600 38.815 1.00 16.70 6ADH2137
ATOM 1739 CA GLU A 239 25.294 16.292 39.305 1.00 16.70 6ADH2138
ATOM 1740 C GLU A 239 24.491 15.144 38.696 1.00 16.70 6ADH2139
ATOM 1741 O GLU A 239 23.259 15.092 38.817 0.00 16.70 2 6ADH2140
ATOM 1742 CB GLU A 239 25.135 16.232 40.828 1.00 16.70 6ADH2141
ATOM 1743 CG GLU A 239 25.928 15.115 41.504 1.00 16.70 6ADH2142
ATOM 1744 CD GLU A 239 26.263 15.452 42.958 1.00 16.70 6ADH2143
ATOM 1745 OE1 GLU A 239 25.712 16.473 43.523 1.00 16.70 6ADH2144
ATOM 1746 OE2 GLU A 239 27.094 14.720 43.618 1.00 16.70 6ADH2145
ATOM 1747 N CYS A 240 25.154 14.242 38.039 1.00 16.70 6ADH2146
ATOM 1748 CA CYS A 240 24.511 13.078 37.362 1.00 16.70 6ADH2147
ATOM 1749 C CYS A 240 24.851 11.775 38.107 1.00 16.70 6ADH2148
ATOM 1750 O CYS A 240 26.027 11.468 38.355 1.00 16.70 6ADH2149
ATOM 1751 CB CYS A 240 25.075 12.905 35.920 1.00 16.70 6ADH2150
ATOM 1752 SG CYS A 240 23.991 14.120 34.869 1.00 16.70 6ADH2151
ATOM 1753 N VAL A 241 23.807 11.022 38.441 1.00 16.70 6ADH2152
ATOM 1754 CA VAL A 241 23.951 9.744 39.168 1.00 16.70 6ADH2153
ATOM 1755 C VAL A 241 23.370 8.572 38.361 1.00 16.70 6ADH2154
ATOM 1756 O VAL A 241 22.256 8.658 37.823 0.00 16.70 2 6ADH2155
ATOM 1757 CB VAL A 241 23.228 9.814 40.517 1.00 16.70 6ADH2156
ATOM 1758 CG1 VAL A 241 22.091 10.838 40.536 1.00 16.70 6ADH2157
ATOM 1759 CG2 VAL A 241 22.594 8.484 40.926 1.00 16.70 6ADH2158
ATOM 1760 N ASN A 242 24.186 7.529 38.329 1.00 16.70 6ADH2159
ATOM 1761 CA ASN A 242 23.888 6.248 37.670 1.00 16.70 6ADH2160
ATOM 1762 C ASN A 242 23.644 5.209 38.766 1.00 16.70 6ADH2161
ATOM 1763 O ASN A 242 24.583 4.766 39.446 1.00 16.70 6ADH2162
ATOM 1764 CB ASN A 242 25.081 5.849 36.790 1.00 16.70 6ADH2163
ATOM 1765 CG ASN A 242 24.915 4.494 36.096 1.00 16.70 6ADH2164
ATOM 1766 OD1 ASN A 242 25.839 4.030 35.429 1.00 16.70 6ADH2165
ATOM 1767 ND2 ASN A 242 23.784 3.824 36.212 1.00 16.70 6ADH2166
ATOM 1768 N PRO A 243 22.391 4.796 38.975 1.00 16.70 6ADH2167
ATOM 1769 CA PRO A 243 22.040 3.880 40.055 1.00 16.70 6ADH2168
ATOM 1770 C PRO A 243 22.737 2.529 39.992 1.00 16.70 6ADH2169
ATOM 1771 O PRO A 243 22.697 1.770 41.009 1.00 16.70 6ADH2170
ATOM 1772 CB PRO A 243 20.547 3.696 39.905 1.00 16.70 6ADH2171
ATOM 1773 CG PRO A 243 20.085 4.536 38.724 1.00 16.70 6ADH2172
ATOM 1774 CD PRO A 243 21.270 5.239 38.139 1.00 16.70 6ADH2173
ATOM 1775 N GLN A 244 23.353 2.229 38.861 1.00 16.70 6ADH2174
ATOM 1776 CA GLN A 244 23.995 .909 38.621 1.00 16.70 6ADH2175
ATOM 1777 C GLN A 244 25.388 .807 39.240 1.00 16.70 6ADH2176
ATOM 1778 O GLN A 244 25.905 -.299 39.466 1.00 16.70 6ADH2177
ATOM 1779 CB GLN A 244 24.195 .685 37.128 0.00 16.70 2 6ADH2178
ATOM 1780 CG GLN A 244 23.027 -.025 36.455 0.00 16.70 2 6ADH2179
ATOM 1781 CD GLN A 244 23.198 -.099 34.940 0.00 16.70 2 6ADH2180
ATOM 1782 OE1 GLN A 244 22.744 -1.057 34.316 0.00 16.70 2 6ADH2181
ATOM 1783 NE2 GLN A 244 23.834 .865 34.302 0.00 16.70 2 6ADH2182
ATOM 1784 N ASP A 245 25.950 1.971 39.488 1.00 16.70 6ADH2183
ATOM 1785 CA ASP A 245 27.304 2.099 40.046 1.00 16.70 6ADH2184
ATOM 1786 C ASP A 245 27.282 1.966 41.569 1.00 16.70 6ADH2185
ATOM 1787 O ASP A 245 28.337 1.982 42.221 1.00 16.70 6ADH2186
ATOM 1788 CB ASP A 245 27.875 3.486 39.729 1.00 16.70 6ADH2187
ATOM 1789 CG ASP A 245 28.119 3.721 38.238 1.00 16.70 6ADH2188
ATOM 1790 OD1 ASP A 245 28.142 4.922 37.770 1.00 16.70 6ADH2189
ATOM 1791 OD2 ASP A 245 28.303 2.716 37.449 1.00 16.70 6ADH2190
ATOM 1792 N TYR A 246 26.065 1.832 42.079 1.00 16.70 6ADH2191
ATOM 1793 CA TYR A 246 25.789 1.817 43.532 1.00 16.70 6ADH2192
ATOM 1794 C TYR A 246 25.278 .479 44.075 1.00 16.70 6ADH2193
ATOM 1795 O TYR A 246 24.489 -.218 43.419 1.00 16.70 6ADH2194
ATOM 1796 CB TYR A 246 24.692 2.819 43.846 1.00 16.70 6ADH2195
ATOM 1797 CG TYR A 246 25.141 4.247 43.616 1.00 16.70 6ADH2196
ATOM 1798 CD1 TYR A 246 24.615 4.980 42.550 1.00 16.70 6ADH2197
ATOM 1799 CD2 TYR A 246 26.084 4.810 44.476 1.00 16.70 6ADH2198
ATOM 1800 CE1 TYR A 246 25.032 6.298 42.348 1.00 16.70 6ADH2199
ATOM 1801 CE2 TYR A 246 26.501 6.127 44.274 1.00 16.70 6ADH2200
ATOM 1802 CZ TYR A 246 25.974 6.870 43.211 1.00 16.70 6ADH2201
ATOM 1803 OH TYR A 246 26.379 8.155 43.020 1.00 16.70 6ADH2202
ATOM 1804 N LYS A 247 25.755 .212 45.290 1.00 16.70 6ADH2203
ATOM 1805 CA LYS A 247 25.409 -.984 46.077 1.00 16.70 6ADH2204
ATOM 1806 C LYS A 247 24.050 -.773 46.783 1.00 16.70 6ADH2205
ATOM 1807 O LYS A 247 23.106 -1.554 46.598 1.00 16.70 6ADH2206
ATOM 1808 CB LYS A 247 26.496 -1.247 47.134 1.00 16.70 6ADH2207
ATOM 1809 CG LYS A 247 27.239 -2.577 46.932 1.00 16.70 6ADH2208
ATOM 1810 CD LYS A 247 28.720 -2.392 46.579 1.00 16.70 6ADH2209
ATOM 1811 CE LYS A 247 29.662 -3.183 47.491 1.00 16.70 6ADH2210
ATOM 1812 NZ LYS A 247 29.144 -4.515 47.838 1.00 16.70 6ADH2211
ATOM 1813 N LYS A 248 23.973 .296 47.584 1.00 16.70 6ADH2212
ATOM 1814 CA LYS A 248 22.748 .640 48.357 1.00 16.70 6ADH2213
ATOM 1815 C LYS A 248 21.647 1.201 47.431 1.00 16.70 6ADH2214
ATOM 1816 O LYS A 248 21.938 1.734 46.350 1.00 16.70 6ADH2215
ATOM 1817 CB LYS A 248 23.061 1.679 49.446 1.00 16.70 6ADH2216
ATOM 1818 CG LYS A 248 24.135 2.690 49.034 0.00 16.70 2 6ADH2217
ATOM 1819 CD LYS A 248 24.140 3.950 49.908 0.00 16.70 2 6ADH2218
ATOM 1820 CE LYS A 248 23.020 3.964 50.952 0.00 16.70 2 6ADH2219
ATOM 1821 NZ LYS A 248 23.363 4.740 52.152 0.00 16.70 2 6ADH2220
ATOM 1822 N PRO A 249 20.352 1.107 47.832 1.00 16.70 6ADH2221
ATOM 1823 CA PRO A 249 19.235 1.584 47.003 1.00 16.70 6ADH2222
ATOM 1824 C PRO A 249 19.469 3.035 46.647 1.00 16.70 6ADH2223
ATOM 1825 O PRO A 249 20.172 3.753 47.420 1.00 16.70 6ADH2224
ATOM 1826 CB PRO A 249 18.018 1.322 47.859 1.00 16.70 6ADH2225
ATOM 1827 CG PRO A 249 18.484 .681 49.160 1.00 16.70 6ADH2226
ATOM 1828 CD PRO A 249 19.973 .538 49.127 1.00 16.70 6ADH2227
ATOM 1829 N ILE A 250 18.897 3.462 45.526 1.00 16.70 6ADH2228
ATOM 1830 CA ILE A 250 19.177 4.811 44.969 1.00 16.70 6ADH2229
ATOM 1831 C ILE A 250 18.411 5.957 45.675 1.00 16.70 6ADH2230
ATOM 1832 O ILE A 250 18.853 7.116 45.672 1.00 16.70 6ADH2231
ATOM 1833 CB ILE A 250 18.928 4.814 43.456 1.00 16.70 6ADH2232
ATOM 1834 CG1 ILE A 250 20.214 5.025 42.654 1.00 16.70 6ADH2233
ATOM 1835 CG2 ILE A 250 17.976 5.918 42.996 1.00 16.70 6ADH2234
ATOM 1836 CD1 ILE A 250 20.892 6.364 42.960 1.00 16.70 6ADH2235
ATOM 1837 N GLN A 251 17.279 5.671 46.285 1.00 16.70 6ADH2236
ATOM 1838 CA GLN A 251 16.538 6.714 47.026 1.00 16.70 6ADH2237
ATOM 1839 C GLN A 251 17.466 7.284 48.124 1.00 16.70 6ADH2238
ATOM 1840 O GLN A 251 17.538 8.506 48.328 0.00 16.70 2 6ADH2239
ATOM 1841 CB GLN A 251 15.277 6.111 47.653 1.00 16.70 6ADH2240
ATOM 1842 CG GLN A 251 14.551 5.139 46.718 1.00 16.70 6ADH2241
ATOM 1843 CD GLN A 251 14.371 3.746 47.328 1.00 16.70 6ADH2242
ATOM 1844 OE1 GLN A 251 13.737 3.608 48.372 1.00 16.70 6ADH2243
ATOM 1845 NE2 GLN A 251 14.898 2.691 46.732 1.00 16.70 6ADH2244
ATOM 1846 N GLU A 252 18.144 6.334 48.769 1.00 16.70 6ADH2245
ATOM 1847 CA GLU A 252 19.116 6.566 49.865 1.00 16.70 6ADH2246
ATOM 1848 C GLU A 252 20.201 7.573 49.448 1.00 16.70 6ADH2247
ATOM 1849 O GLU A 252 20.335 8.648 50.053 1.00 16.70 6ADH2248
ATOM 1850 CB GLU A 252 19.835 5.265 50.194 1.00 16.70 6ADH2249
ATOM 1851 CG GLU A 252 18.895 4.130 50.572 1.00 16.70 6ADH2250
ATOM 1852 CD GLU A 252 19.540 3.173 51.567 1.00 16.70 6ADH2251
ATOM 1853 OE1 GLU A 252 19.031 2.005 51.764 1.00 16.70 6ADH2252
ATOM 1854 OE2 GLU A 252 20.598 3.535 52.211 1.00 16.70 6ADH2253
ATOM 1855 N VAL A 253 20.938 7.148 48.417 1.00 16.70 6ADH2254
ATOM 1856 CA VAL A 253 22.021 7.927 47.780 1.00 16.70 6ADH2255
ATOM 1857 C VAL A 253 21.515 9.315 47.435 1.00 16.70 6ADH2256
ATOM 1858 O VAL A 253 22.129 10.330 47.796 1.00 16.70 6ADH2257
ATOM 1859 CB VAL A 253 22.440 7.258 46.468 1.00 16.70 6ADH2258
ATOM 1860 CG1 VAL A 253 23.724 7.845 45.876 1.00 16.70 6ADH2259
ATOM 1861 CG2 VAL A 253 22.699 5.757 46.614 1.00 16.70 6ADH2260
ATOM 1862 N LEU A 254 20.405 9.296 46.732 1.00 16.70 6ADH2261
ATOM 1863 CA LEU A 254 19.725 10.508 46.318 1.00 16.70 6ADH2262
ATOM 1864 C LEU A 254 19.305 11.274 47.546 1.00 16.70 6ADH2263
ATOM 1865 O LEU A 254 19.272 12.513 47.552 1.00 16.70 6ADH2264
ATOM 1866 CB LEU A 254 18.462 10.173 45.514 1.00 16.70 6ADH2265
ATOM 1867 CG LEU A 254 18.558 10.565 44.036 1.00 16.70 6ADH2266
ATOM 1868 CD1 LEU A 254 17.856 11.887 43.718 1.00 16.70 6ADH2267
ATOM 1869 CD2 LEU A 254 20.001 10.736 43.557 1.00 16.70 6ADH2268
ATOM 1870 N THR A 255 18.995 10.533 48.577 1.00 16.70 6ADH2269
ATOM 1871 CA THR A 255 18.513 11.163 49.790 1.00 16.70 6ADH2270
ATOM 1872 C THR A 255 19.708 11.528 50.737 1.00 16.70 6ADH2271
ATOM 1873 O THR A 255 19.558 12.360 51.633 1.00 16.70 6ADH2272
ATOM 1874 CB THR A 255 17.382 10.305 50.396 1.00 16.70 6ADH2273
ATOM 1875 OG1 THR A 255 17.709 8.924 50.330 1.00 16.70 6ADH2274
ATOM 1876 CG2 THR A 255 16.052 10.485 49.655 1.00 16.70 6ADH2275
ATOM 1877 N GLU A 256 20.899 10.928 50.505 1.00 16.70 6ADH2276
ATOM 1878 CA GLU A 256 22.156 11.194 51.299 1.00 16.70 6ADH2277
ATOM 1879 C GLU A 256 22.934 12.395 50.701 1.00 16.70 6ADH2278
ATOM 1880 O GLU A 256 23.806 12.986 51.360 1.00 16.70 6ADH2279
ATOM 1881 CB GLU A 256 23.091 9.966 51.229 1.00 16.70 6ADH2280
ATOM 1882 CG GLU A 256 23.420 9.335 52.588 1.00 16.70 6ADH2281
ATOM 1883 CD GLU A 256 24.606 8.361 52.521 1.00 16.70 6ADH2282
ATOM 1884 OE1 GLU A 256 24.505 7.263 51.850 0.00 16.70 2 6ADH2283
ATOM 1885 OE2 GLU A 256 25.707 8.639 53.134 0.00 16.70 2 6ADH2284
ATOM 1886 N MET A 257 22.588 12.695 49.450 1.00 16.70 6ADH2285
ATOM 1887 CA MET A 257 23.176 13.811 48.674 1.00 16.70 6ADH2286
ATOM 1888 C MET A 257 22.631 15.128 49.222 1.00 16.70 6ADH2287
ATOM 1889 O MET A 257 23.377 15.942 49.788 1.00 16.70 6ADH2288
ATOM 1890 CB MET A 257 22.804 13.666 47.197 1.00 16.70 6ADH2289
ATOM 1891 CG MET A 257 24.004 13.328 46.312 1.00 16.70 6ADH2290
ATOM 1892 SD MET A 257 23.538 12.621 44.747 1.00 16.70 6ADH2291
ATOM 1893 CE MET A 257 24.226 10.986 44.588 1.00 16.70 6ADH2292
ATOM 1894 N SER A 258 21.334 15.269 49.039 1.00 16.70 6ADH2293
ATOM 1895 CA SER A 258 20.556 16.401 49.558 1.00 16.70 6ADH2294
ATOM 1896 C SER A 258 20.035 16.055 51.016 1.00 16.70 6ADH2295
ATOM 1897 O SER A 258 19.260 16.819 51.612 1.00 16.70 6ADH2296
ATOM 1898 CB SER A 258 19.348 16.647 48.624 1.00 16.70 6ADH2297
ATOM 1899 OG SER A 258 19.142 18.040 48.429 1.00 16.70 6ADH2298
ATOM 1900 N ASN A 259 20.505 14.892 51.578 1.00 16.70 6ADH2299
ATOM 1901 CA ASN A 259 20.025 14.264 52.896 1.00 16.70 6ADH2300
ATOM 1902 C ASN A 259 18.824 14.977 53.492 1.00 16.70 6ADH2301
ATOM 1903 O ASN A 259 18.929 16.115 53.976 0.00 16.70 2 6ADH2302
ATOM 1904 CB ASN A 259 21.065 14.155 54.021 0.00 16.70 2 6ADH2303
ATOM 1905 CG ASN A 259 20.749 12.980 54.991 0.00 16.70 2 6ADH2304
ATOM 1906 OD1 ASN A 259 21.506 12.011 55.060 0.00 16.70 2 6ADH2305
ATOM 1907 ND2 ASN A 259 19.665 13.008 55.747 0.00 16.70 2 6ADH2306
ATOM 1908 N GLY A 260 17.780 14.196 53.411 1.00 16.70 6ADH2307
ATOM 1909 CA GLY A 260 16.430 14.545 53.791 1.00 16.70 6ADH2308
ATOM 1910 C GLY A 260 15.588 14.285 52.562 1.00 16.70 6ADH2309
ATOM 1911 O GLY A 260 14.445 13.817 52.659 1.00 16.70 6ADH2310
ATOM 1912 N GLY A 261 16.227 14.603 51.459 1.00 16.70 6ADH2311
ATOM 1913 CA GLY A 261 15.644 14.456 50.138 1.00 16.70 6ADH2312
ATOM 1914 C GLY A 261 15.645 15.804 49.434 1.00 16.70 6ADH2313
ATOM 1915 O GLY A 261 15.867 16.849 50.063 1.00 16.70 6ADH2314
ATOM 1916 N VAL A 262 15.387 15.684 48.161 1.00 16.70 6ADH2315
ATOM 1917 CA VAL A 262 15.355 16.785 47.202 1.00 16.70 6ADH2316
ATOM 1918 C VAL A 262 13.975 17.475 47.250 1.00 16.70 6ADH2317
ATOM 1919 O VAL A 262 12.930 16.817 47.335 1.00 16.70 6ADH2318
ATOM 1920 CB VAL A 262 15.637 16.168 45.830 1.00 16.70 6ADH2319
ATOM 1921 CG1 VAL A 262 16.359 14.820 45.925 1.00 16.70 6ADH2320
ATOM 1922 CG2 VAL A 262 14.368 15.896 45.019 1.00 16.70 6ADH2321
ATOM 1923 N ASP A 263 13.983 18.800 47.197 1.00 16.70 6ADH2322
ATOM 1924 CA ASP A 263 12.735 19.595 47.241 1.00 16.70 6ADH2323
ATOM 1925 C ASP A 263 11.722 19.045 46.217 1.00 16.70 6ADH2324
ATOM 1926 O ASP A 263 10.568 18.748 46.557 1.00 16.70 6ADH2325
ATOM 1927 CB ASP A 263 13.031 21.067 46.937 1.00 16.70 6ADH2326
ATOM 1928 CG ASP A 263 13.752 21.781 48.085 1.00 16.70 6ADH2327
ATOM 1929 OD1 ASP A 263 15.041 21.777 48.138 1.00 16.70 6ADH2328
ATOM 1930 OD2 ASP A 263 13.072 22.387 48.999 1.00 16.70 6ADH2329
ATOM 1931 N PHE A 264 12.194 18.921 44.977 1.00 16.70 6ADH2330
ATOM 1932 CA PHE A 264 11.392 18.397 43.843 1.00 16.70 6ADH2331
ATOM 1933 C PHE A 264 12.135 17.279 43.106 1.00 16.70 6ADH2332
ATOM 1934 O PHE A 264 13.369 17.287 42.993 1.00 16.70 6ADH2333
ATOM 1935 CB PHE A 264 11.132 19.491 42.810 1.00 16.70 6ADH2334
ATOM 1936 CG PHE A 264 10.533 20.749 43.418 1.00 16.70 6ADH2335
ATOM 1937 CD1 PHE A 264 11.356 21.652 44.095 1.00 16.70 6ADH2336
ATOM 1938 CD2 PHE A 264 9.161 20.993 43.298 1.00 16.70 6ADH2337
ATOM 1939 CE1 PHE A 264 10.806 22.807 44.656 1.00 16.70 6ADH2338
ATOM 1940 CE2 PHE A 264 8.611 22.148 43.859 1.00 16.70 6ADH2339
ATOM 1941 CZ PHE A 264 9.433 23.055 44.539 1.00 16.70 6ADH2340
ATOM 1942 N SER A 265 11.358 16.344 42.617 1.00 16.70 6ADH2341
ATOM 1943 CA SER A 265 11.870 15.203 41.848 1.00 16.70 6ADH2342
ATOM 1944 C SER A 265 10.852 14.867 40.771 1.00 16.70 6ADH2343
ATOM 1945 O SER A 265 9.636 14.949 40.986 1.00 16.70 6ADH2344
ATOM 1946 CB SER A 265 12.061 13.998 42.767 1.00 16.70 6ADH2345
ATOM 1947 OG SER A 265 10.851 13.260 42.858 1.00 16.70 6ADH2346
ATOM 1948 N PHE A 266 11.327 14.492 39.620 1.00 16.70 6ADH2347
ATOM 1949 CA PHE A 266 10.427 14.174 38.514 1.00 16.70 6ADH2348
ATOM 1950 C PHE A 266 10.804 12.829 37.886 1.00 16.70 6ADH2349
ATOM 1951 O PHE A 266 11.988 12.523 37.689 1.00 16.70 6ADH2350
ATOM 1952 CB PHE A 266 10.515 15.274 37.435 1.00 16.70 6ADH2351
ATOM 1953 CG PHE A 266 10.361 16.717 37.973 1.00 16.70 6ADH2352
ATOM 1954 CD1 PHE A 266 11.429 17.352 38.629 1.00 16.70 6ADH2353
ATOM 1955 CD2 PHE A 266 9.154 17.414 37.801 1.00 16.70 6ADH2354
ATOM 1956 CE1 PHE A 266 11.289 18.667 39.107 1.00 16.70 6ADH2355
ATOM 1957 CE2 PHE A 266 9.016 18.728 38.279 1.00 16.70 6ADH2356
ATOM 1958 CZ PHE A 266 10.084 19.354 38.932 1.00 16.70 6ADH2357
ATOM 1959 N GLU A 267 9.783 12.058 37.587 1.00 16.70 6ADH2358
ATOM 1960 CA GLU A 267 9.949 10.768 36.898 1.00 16.70 6ADH2359
ATOM 1961 C GLU A 267 9.541 10.953 35.413 1.00 16.70 6ADH2360
ATOM 1962 O GLU A 267 8.368 11.228 35.111 1.00 16.70 6ADH2361
ATOM 1963 CB GLU A 267 9.057 9.700 37.565 1.00 16.70 6ADH2362
ATOM 1964 CG GLU A 267 9.599 8.268 37.421 1.00 16.70 6ADH2363
ATOM 1965 CD GLU A 267 9.124 7.571 36.140 1.00 16.70 6ADH2364
ATOM 1966 OE1 GLU A 267 9.267 6.296 36.006 1.00 16.70 6ADH2365
ATOM 1967 OE2 GLU A 267 8.579 8.260 35.196 1.00 16.70 6ADH2366
ATOM 1968 N VAL A 268 10.528 10.814 34.491 1.00 16.70 6ADH2367
ATOM 1969 CA VAL A 268 10.267 10.883 33.012 1.00 16.70 6ADH2368
ATOM 1970 C VAL A 268 10.891 9.657 32.295 1.00 16.70 6ADH2369
ATOM 1971 O VAL A 268 11.846 9.791 31.514 1.00 16.70 6ADH2370
ATOM 1972 CB VAL A 268 10.795 12.180 32.368 1.00 16.70 6ADH2371
ATOM 1973 CG1 VAL A 268 9.803 12.801 31.378 1.00 16.70 6ADH2372
ATOM 1974 CG2 VAL A 268 11.101 13.285 33.381 1.00 16.70 6ADH2373
ATOM 1975 N ILE A 269 10.279 8.524 32.635 1.00 16.70 6ADH2374
ATOM 1976 CA ILE A 269 10.556 7.175 32.094 1.00 16.70 6ADH2375
ATOM 1977 C ILE A 269 9.220 6.460 31.965 1.00 16.70 6ADH2376
ATOM 1978 O ILE A 269 8.812 6.058 30.864 1.00 16.70 6ADH2377
ATOM 1979 CB ILE A 269 11.425 6.351 33.055 1.00 16.70 6ADH2378
ATOM 1980 CG1 ILE A 269 12.779 6.993 33.349 1.00 16.70 6ADH2379
ATOM 1981 CG2 ILE A 269 11.736 4.946 32.530 1.00 16.70 6ADH2380
ATOM 1982 CD1 ILE A 269 13.013 7.231 34.842 1.00 16.70 6ADH2381
ATOM 1983 N GLY A 270 8.599 6.340 33.127 1.00 16.70 6ADH2382
ATOM 1984 CA GLY A 270 7.273 5.726 33.269 1.00 16.70 6ADH2383
ATOM 1985 C GLY A 270 7.373 4.250 33.677 1.00 16.70 6ADH2384
ATOM 1986 O GLY A 270 6.870 3.361 32.974 1.00 16.70 6ADH2385
ATOM 1987 N ARG A 271 8.025 4.049 34.806 1.00 16.70 6ADH2386
ATOM 1988 CA ARG A 271 8.200 2.731 35.438 1.00 16.70 6ADH2387
ATOM 1989 C ARG A 271 7.632 2.802 36.854 1.00 16.70 6ADH2388
ATOM 1990 O ARG A 271 8.073 3.617 37.678 1.00 16.70 6ADH2389
ATOM 1991 CB ARG A 271 9.684 2.390 35.545 1.00 16.70 6ADH2390
ATOM 1992 CG ARG A 271 10.252 1.682 34.321 1.00 16.70 6ADH2391
ATOM 1993 CD ARG A 271 11.630 1.075 34.595 1.00 16.70 6ADH2392
ATOM 1994 NE ARG A 271 11.532 -.313 35.054 1.00 16.70 6ADH2393
ATOM 1995 CZ ARG A 271 12.531 -1.200 35.033 1.00 16.70 6ADH2394
ATOM 1996 NH1 ARG A 271 13.758 -.855 34.619 1.00 16.70 6ADH2395
ATOM 1997 NH2 ARG A 271 12.390 -2.485 35.380 1.00 16.70 6ADH2396
ATOM 1998 N LEU A 272 6.676 1.944 37.092 1.00 16.70 6ADH2397
ATOM 1999 CA LEU A 272 5.951 1.879 38.365 1.00 16.70 6ADH2398
ATOM 2000 C LEU A 272 6.896 1.912 39.577 1.00 16.70 6ADH2399
ATOM 2001 O LEU A 272 6.546 2.457 40.638 1.00 16.70 6ADH2400
ATOM 2002 CB LEU A 272 5.131 .594 38.410 1.00 16.70 6ADH2401
ATOM 2003 CG LEU A 272 3.956 .641 37.437 1.00 16.70 6ADH2402
ATOM 2004 CD1 LEU A 272 3.652 2.057 36.948 1.00 16.70 6ADH2403
ATOM 2005 CD2 LEU A 272 4.189 -.193 36.175 1.00 16.70 6ADH2404
ATOM 2006 N ASP A 273 8.087 1.336 39.390 1.00 16.70 6ADH2405
ATOM 2007 CA ASP A 273 9.082 1.196 40.484 1.00 16.70 6ADH2406
ATOM 2008 C ASP A 273 9.852 2.515 40.735 1.00 16.70 6ADH2407
ATOM 2009 O ASP A 273 10.139 2.872 41.888 1.00 16.70 6ADH2408
ATOM 2010 CB ASP A 273 10.040 .011 40.203 1.00 16.70 6ADH2409
ATOM 2011 CG ASP A 273 11.026 .212 39.044 1.00 16.70 6ADH2410
ATOM 2012 OD1 ASP A 273 10.800 1.109 38.147 1.00 16.70 6ADH2411
ATOM 2013 OD2 ASP A 273 12.087 -.521 38.967 1.00 16.70 6ADH2412
ATOM 2014 N THR A 274 10.157 3.214 39.646 1.00 16.70 6ADH2413
ATOM 2015 CA THR A 274 10.886 4.507 39.678 1.00 16.70 6ADH2414
ATOM 2016 C THR A 274 9.915 5.642 40.015 1.00 16.70 6ADH2415
ATOM 2017 O THR A 274 10.320 6.701 40.518 1.00 16.70 6ADH2416
ATOM 2018 CB THR A 274 11.494 4.796 38.301 1.00 16.70 6ADH2417
ATOM 2019 OG1 THR A 274 12.464 3.811 37.977 1.00 16.70 6ADH2418
ATOM 2020 CG2 THR A 274 12.187 6.158 38.224 1.00 16.70 6ADH2419
ATOM 2021 N MET A 275 8.666 5.348 39.702 1.00 16.70 6ADH2420
ATOM 2022 CA MET A 275 7.532 6.244 39.916 1.00 16.70 6ADH2421
ATOM 2023 C MET A 275 7.270 6.346 41.420 1.00 16.70 6ADH2422
ATOM 2024 O MET A 275 6.585 7.265 41.894 1.00 16.70 6ADH2423
ATOM 2025 CB MET A 275 6.312 5.695 39.159 1.00 16.70 6ADH2424
ATOM 2026 CG MET A 275 5.290 6.774 38.778 1.00 16.70 6ADH2425
ATOM 2027 SD MET A 275 4.265 6.309 37.397 1.00 16.70 6ADH2426
ATOM 2028 CE MET A 275 5.272 6.024 35.957 1.00 16.70 6ADH2427
ATOM 2029 N VAL A 276 7.822 5.402 42.155 1.00 16.70 6ADH2428
ATOM 2030 CA VAL A 276 7.744 5.461 43.615 1.00 16.70 6ADH2429
ATOM 2031 C VAL A 276 9.142 5.862 44.164 1.00 16.70 6ADH2430
ATOM 2032 O VAL A 276 9.253 6.702 45.066 1.00 16.70 6ADH2431
ATOM 2033 CB VAL A 276 7.194 4.147 44.204 1.00 16.70 6ADH2432
ATOM 2034 CG1 VAL A 276 7.960 3.668 45.439 1.00 16.70 6ADH2433
ATOM 2035 CG2 VAL A 276 5.734 4.265 44.657 1.00 16.70 6ADH2434
ATOM 2036 N THR A 277 10.220 5.295 43.612 1.00 16.70 6ADH2435
ATOM 2037 CA THR A 277 11.613 5.603 44.078 1.00 16.70 6ADH2436
ATOM 2038 C THR A 277 11.882 7.124 44.095 1.00 16.70 6ADH2437
ATOM 2039 O THR A 277 12.720 7.615 44.869 1.00 16.70 6ADH2438
ATOM 2040 CB THR A 277 12.665 4.962 43.162 1.00 16.70 6ADH2439
ATOM 2041 OG1 THR A 277 12.312 3.616 42.881 1.00 16.70 6ADH2440
ATOM 2042 CG2 THR A 277 14.066 4.945 43.779 1.00 16.70 6ADH2441
ATOM 2043 N ALA A 278 11.154 7.823 43.232 1.00 16.70 6ADH2442
ATOM 2044 CA ALA A 278 11.265 9.290 43.067 1.00 16.70 6ADH2443
ATOM 2045 C ALA A 278 10.514 10.033 44.188 1.00 16.70 6ADH2444
ATOM 2046 O ALA A 278 10.835 11.184 44.518 1.00 16.70 6ADH2445
ATOM 2047 CB ALA A 278 10.674 9.709 41.720 1.00 16.70 6ADH2446
ATOM 2048 N LEU A 279 9.528 9.340 44.740 1.00 16.70 6ADH2447
ATOM 2049 CA LEU A 279 8.682 9.849 45.840 1.00 16.70 6ADH2448
ATOM 2050 C LEU A 279 9.392 9.655 47.186 1.00 16.70 6ADH2449
ATOM 2051 O LEU A 279 9.273 10.484 48.100 1.00 16.70 6ADH2450
ATOM 2052 CB LEU A 279 7.359 9.069 45.881 1.00 16.70 6ADH2451
ATOM 2053 CG LEU A 279 6.166 9.903 46.360 1.00 16.70 6ADH2452
ATOM 2054 CD1 LEU A 279 5.163 9.094 47.185 1.00 16.70 6ADH2453
ATOM 2055 CD2 LEU A 279 6.574 11.081 47.246 1.00 16.70 6ADH2454
ATOM 2056 N SER A 280 10.117 8.556 47.258 1.00 16.70 6ADH2455
ATOM 2057 CA SER A 280 10.864 8.157 48.461 1.00 16.70 6ADH2456
ATOM 2058 C SER A 280 12.125 9.013 48.648 1.00 16.70 6ADH2457
ATOM 2059 O SER A 280 12.612 9.201 49.772 1.00 16.70 6ADH2458
ATOM 2060 CB SER A 280 11.314 6.698 48.336 1.00 16.70 6ADH2459
ATOM 2061 OG SER A 280 10.540 5.872 49.192 1.00 16.70 6ADH2460
ATOM 2062 N CYS A 281 12.623 9.520 47.536 1.00 16.70 6ADH2461
ATOM 2063 CA CYS A 281 13.876 10.292 47.509 1.00 16.70 6ADH2462
ATOM 2064 C CYS A 281 13.674 11.791 47.823 1.00 16.70 6ADH2463
ATOM 2065 O CYS A 281 14.644 12.551 47.957 1.00 16.70 6ADH2464
ATOM 2066 CB CYS A 281 14.552 10.165 46.138 1.00 16.70 6ADH2465
ATOM 2067 SG CYS A 281 14.014 11.485 44.954 1.00 16.70 6ADH2466
ATOM 2068 N CYS A 282 12.427 12.262 47.940 1.00 16.70 6ADH2467
ATOM 2069 CA CYS A 282 12.205 13.686 48.346 1.00 16.70 6ADH2468
ATOM 2070 C CYS A 282 11.902 13.746 49.882 1.00 16.70 6ADH2469
ATOM 2071 O CYS A 282 12.050 12.742 50.598 1.00 16.70 6ADH2470
ATOM 2072 CB CYS A 282 11.135 14.410 47.481 1.00 16.70 6ADH2471
ATOM 2073 SG CYS A 282 9.541 13.493 47.317 1.00 16.70 6ADH2472
ATOM 2074 N GLN A 283 11.477 14.954 50.325 1.00 16.70 6ADH2473
ATOM 2075 CA GLN A 283 11.297 15.330 51.774 1.00 16.70 6ADH2474
ATOM 2076 C GLN A 283 9.870 15.152 52.363 1.00 16.70 6ADH2475
ATOM 2077 O GLN A 283 8.921 15.840 51.954 0.00 16.70 2 6ADH2476
ATOM 2078 CB GLN A 283 11.655 16.801 51.970 1.00 16.70 6ADH2477
ATOM 2079 CG GLN A 283 13.007 16.996 52.652 1.00 16.70 6ADH2478
ATOM 2080 CD GLN A 283 12.879 17.235 54.155 1.00 16.70 6ADH2479
ATOM 2081 OE1 GLN A 283 13.809 16.944 54.906 1.00 16.70 6ADH2480
ATOM 2082 NE2 GLN A 283 11.771 17.756 54.648 1.00 16.70 6ADH2481
ATOM 2083 N GLU A 284 9.866 14.224 53.338 1.00 16.70 6ADH2482
ATOM 2084 CA GLU A 284 8.700 13.771 54.146 1.00 16.70 6ADH2483
ATOM 2085 C GLU A 284 7.637 14.839 54.332 1.00 16.70 6ADH2484
ATOM 2086 O GLU A 284 6.433 14.566 54.212 1.00 16.70 6ADH2485
ATOM 2087 CB GLU A 284 9.078 13.506 55.629 1.00 16.70 6ADH2486
ATOM 2088 CG GLU A 284 10.250 12.549 55.867 1.00 16.70 6ADH2487
ATOM 2089 CD GLU A 284 10.813 12.658 57.297 1.00 16.70 6ADH2488
ATOM 2090 OE1 GLU A 284 10.976 11.598 58.013 1.00 16.70 6ADH2489
ATOM 2091 OE2 GLU A 284 11.121 13.813 57.783 1.00 16.70 6ADH2490
ATOM 2092 N ALA A 285 8.173 16.008 54.622 1.00 16.70 6ADH2491
ATOM 2093 CA ALA A 285 7.406 17.168 55.093 1.00 16.70 6ADH2492
ATOM 2094 C ALA A 285 7.053 18.222 54.042 1.00 16.70 6ADH2493
ATOM 2095 O ALA A 285 6.139 19.036 54.240 1.00 16.70 6ADH2494
ATOM 2096 CB ALA A 285 8.210 17.904 56.164 1.00 16.70 6ADH2495
ATOM 2097 N TYR A 286 7.755 18.251 52.936 1.00 16.70 6ADH2496
ATOM 2098 CA TYR A 286 7.446 19.249 51.905 1.00 16.70 6ADH2497
ATOM 2099 C TYR A 286 8.061 18.874 50.556 1.00 16.70 6ADH2498
ATOM 2100 O TYR A 286 8.386 19.744 49.736 1.00 16.70 6ADH2499
ATOM 2101 CB TYR A 286 7.922 20.662 52.348 1.00 16.70 6ADH2500
ATOM 2102 CG TYR A 286 9.421 20.811 52.728 1.00 16.70 6ADH2501
ATOM 2103 CD1 TYR A 286 10.368 21.175 51.754 1.00 16.70 6ADH2502
ATOM 2104 CD2 TYR A 286 9.851 20.617 54.053 1.00 16.70 6ADH2503
ATOM 2105 CE1 TYR A 286 11.722 21.343 52.101 1.00 16.70 6ADH2504
ATOM 2106 CE2 TYR A 286 11.204 20.789 54.399 1.00 16.70 6ADH2505
ATOM 2107 CZ TYR A 286 12.139 21.154 53.424 1.00 16.70 6ADH2506
ATOM 2108 OH TYR A 286 13.447 21.329 53.757 1.00 16.70 6ADH2507
ATOM 2109 N GLY A 287 8.207 17.580 50.332 1.00 16.70 6ADH2508
ATOM 2110 CA GLY A 287 8.779 17.057 49.069 1.00 16.70 6ADH2509
ATOM 2111 C GLY A 287 7.662 16.822 48.026 1.00 16.70 6ADH2510
ATOM 2112 O GLY A 287 6.764 15.995 48.247 1.00 16.70 6ADH2511
ATOM 2113 N VAL A 288 7.784 17.573 46.898 1.00 16.70 6ADH2512
ATOM 2114 CA VAL A 288 6.801 17.573 45.756 1.00 16.70 6ADH2513
ATOM 2115 C VAL A 288 7.286 16.794 44.500 1.00 16.70 6ADH2514
ATOM 2116 O VAL A 288 7.852 17.369 43.556 1.00 16.70 6ADH2515
ATOM 2117 CB VAL A 288 6.505 19.007 45.300 1.00 16.70 6ADH2516
ATOM 2118 CG1 VAL A 288 5.493 19.068 44.155 1.00 16.70 6ADH2517
ATOM 2119 CG2 VAL A 288 5.921 19.876 46.415 1.00 16.70 6ADH2518
ATOM 2120 N SER A 289 7.030 15.495 44.516 1.00 16.70 6ADH2519
ATOM 2121 CA SER A 289 7.389 14.586 43.410 1.00 16.70 6ADH2520
ATOM 2122 C SER A 289 6.233 14.518 42.394 1.00 16.70 6ADH2521
ATOM 2123 O SER A 289 5.078 14.246 42.757 1.00 16.70 6ADH2522
ATOM 2124 CB SER A 289 7.668 13.185 43.965 1.00 16.70 6ADH2523
ATOM 2125 OG SER A 289 7.407 12.206 42.971 1.00 16.70 6ADH2524
ATOM 2126 N VAL A 290 6.590 14.771 41.142 1.00 16.70 6ADH2525
ATOM 2127 CA VAL A 290 5.644 14.771 40.006 1.00 16.70 6ADH2526
ATOM 2128 C VAL A 290 6.055 13.714 38.978 1.00 16.70 6ADH2527
ATOM 2129 O VAL A 290 7.249 13.502 38.722 1.00 16.70 6ADH2528
ATOM 2130 CB VAL A 290 5.663 16.136 39.311 1.00 16.70 6ADH2529
ATOM 2131 CG1 VAL A 290 4.825 16.169 38.032 1.00 16.70 6ADH2530
ATOM 2132 CG2 VAL A 290 5.122 17.265 40.190 1.00 16.70 6ADH2531
ATOM 2133 N ILE A 291 5.057 13.067 38.404 1.00 16.70 6ADH2532
ATOM 2134 CA ILE A 291 5.291 12.043 37.378 1.00 16.70 6ADH2533
ATOM 2135 C ILE A 291 4.764 12.529 36.033 1.00 16.70 6ADH2534
ATOM 2136 O ILE A 291 3.584 12.890 35.903 1.00 16.70 6ADH2535
ATOM 2137 CB ILE A 291 4.637 10.716 37.768 1.00 16.70 6ADH2536
ATOM 2138 CG1 ILE A 291 3.182 10.593 37.321 1.00 16.70 6ADH2537
ATOM 2139 CG2 ILE A 291 4.618 10.481 39.280 1.00 16.70 6ADH2538
ATOM 2140 CD1 ILE A 291 2.488 9.353 37.888 1.00 16.70 6ADH2539
ATOM 2141 N VAL A 292 5.697 12.503 35.109 1.00 16.70 6ADH2540
ATOM 2142 CA VAL A 292 5.509 12.947 33.730 1.00 16.70 6ADH2541
ATOM 2143 C VAL A 292 5.172 11.759 32.812 1.00 16.70 6ADH2542
ATOM 2144 O VAL A 292 4.249 11.903 31.982 1.00 16.70 6ADH2543
ATOM 2145 CB VAL A 292 6.812 13.590 33.242 1.00 16.70 6ADH2544
ATOM 2146 CG1 VAL A 292 6.766 13.998 31.770 1.00 16.70 6ADH2545
ATOM 2147 CG2 VAL A 292 7.182 14.857 34.014 1.00 16.70 6ADH2546
ATOM 2148 N GLY A 293 5.964 10.689 33.068 1.00 16.70 6ADH2547
ATOM 2149 CA GLY A 293 6.002 9.367 32.335 1.00 16.70 6ADH2548
ATOM 2150 C GLY A 293 4.611 8.736 32.065 1.00 16.70 6ADH2549
ATOM 2151 O GLY A 293 3.571 9.300 32.432 1.00 16.70 6ADH2550
ATOM 2152 N VAL A 294 4.644 7.543 31.419 1.00 16.70 6ADH2551
ATOM 2153 CA VAL A 294 3.414 6.789 30.977 1.00 16.70 6ADH2552
ATOM 2154 C VAL A 294 3.558 5.248 31.143 1.00 16.70 6ADH2553
ATOM 2155 O VAL A 294 4.064 4.553 30.250 1.00 16.70 6ADH2554
ATOM 2156 CB VAL A 294 3.188 7.038 29.493 1.00 16.70 6ADH2555
ATOM 2157 CG1 VAL A 294 2.097 6.145 28.902 1.00 16.70 6ADH2556
ATOM 2158 CG2 VAL A 294 2.768 8.476 29.190 1.00 16.70 6ADH2557
ATOM 2159 N PRO A 295 3.132 4.638 32.276 1.00 16.70 6ADH2558
ATOM 2160 CA PRO A 295 3.362 3.211 32.550 1.00 16.70 6ADH2559
ATOM 2161 C PRO A 295 2.633 2.169 31.717 1.00 16.70 6ADH2560
ATOM 2162 O PRO A 295 1.634 2.519 31.015 1.00 16.70 6ADH2561
ATOM 2163 CB PRO A 295 2.884 3.003 33.958 1.00 16.70 6ADH2562
ATOM 2164 CG PRO A 295 2.315 4.324 34.454 1.00 16.70 6ADH2563
ATOM 2165 CD PRO A 295 2.422 5.341 33.357 1.00 16.70 6ADH2564
ATOM 2166 N PRO A 296 3.174 .938 31.863 1.00 16.70 6ADH2565
ATOM 2167 CA PRO A 296 2.666 -.254 31.238 1.00 16.70 6ADH2566
ATOM 2168 C PRO A 296 1.298 -.455 31.792 1.00 16.70 6ADH2567
ATOM 2169 O PRO A 296 1.189 -.944 32.960 0.00 16.70 2 6ADH2568
ATOM 2170 CB PRO A 296 3.628 -1.335 31.671 1.00 16.70 6ADH2569
ATOM 2171 CG PRO A 296 4.656 -.701 32.588 1.00 16.70 6ADH2570
ATOM 2172 CD PRO A 296 4.323 .740 32.739 1.00 16.70 6ADH2571
ATOM 2173 N ASP A 297 .386 -.044 30.932 1.00 16.70 6ADH2572
ATOM 2174 CA ASP A 297 -1.077 -.019 31.126 1.00 16.70 6ADH2573
ATOM 2175 C ASP A 297 -1.514 -.119 32.577 1.00 16.70 6ADH2574
ATOM 2176 O ASP A 297 -.877 .460 33.471 1.00 16.70 6ADH2575
ATOM 2177 CB ASP A 297 -1.756 -1.186 30.416 1.00 16.70 6ADH2576
ATOM 2178 CG ASP A 297 -2.852 -.715 29.462 1.00 16.70 6ADH2577
ATOM 2179 OD1 ASP A 297 -2.603 .216 28.606 1.00 16.70 6ADH2578
ATOM 2180 OD2 ASP A 297 -4.027 -1.247 29.514 1.00 16.70 6ADH2579
ATOM 2181 N SER A 298 -2.610 -.869 32.666 1.00 16.70 6ADH2580
ATOM 2182 CA SER A 298 -3.324 -1.206 33.903 1.00 16.70 6ADH2581
ATOM 2183 C SER A 298 -2.385 -1.940 34.863 1.00 16.70 6ADH2582
ATOM 2184 O SER A 298 -2.558 -3.138 35.132 1.00 16.70 6ADH2583
ATOM 2185 CB SER A 298 -4.502 -2.137 33.582 1.00 16.70 6ADH2584
ATOM 2186 OG SER A 298 -5.425 -1.480 32.726 1.00 16.70 6ADH2585
ATOM 2187 N GLN A 299 -1.406 -1.197 35.355 1.00 16.70 6ADH2586
ATOM 2188 CA GLN A 299 -.384 -1.739 36.272 1.00 16.70 6ADH2587
ATOM 2189 C GLN A 299 -.322 -.924 37.554 1.00 16.70 6ADH2588
ATOM 2190 O GLN A 299 -.277 .316 37.521 1.00 16.70 6ADH2589
ATOM 2191 CB GLN A 299 .982 -1.717 35.613 1.00 16.70 6ADH2590
ATOM 2192 CG GLN A 299 1.696 -3.057 35.731 1.00 16.70 6ADH2591
ATOM 2193 CD GLN A 299 1.798 -3.788 34.396 1.00 16.70 6ADH2592
ATOM 2194 OE1 GLN A 299 .953 -4.628 34.089 1.00 16.70 6ADH2593
ATOM 2195 NE2 GLN A 299 2.793 -3.517 33.573 1.00 16.70 6ADH2594
ATOM 2196 N ASN A 300 -.304 -1.653 38.649 1.00 16.70 6ADH2595
ATOM 2197 CA ASN A 300 -.390 -1.051 39.979 1.00 16.70 6ADH2596
ATOM 2198 C ASN A 300 .930 -1.026 40.730 1.00 16.70 6ADH2597
ATOM 2199 O ASN A 300 1.648 -2.038 40.796 1.00 16.70 6ADH2598
ATOM 2200 CB ASN A 300 -1.415 -1.808 40.795 1.00 16.70 6ADH2599
ATOM 2201 CG ASN A 300 -2.794 -1.722 40.152 1.00 16.70 6ADH2600
ATOM 2202 OD1 ASN A 300 -3.702 -2.452 40.543 1.00 16.70 6ADH2601
ATOM 2203 ND2 ASN A 300 -3.008 -.863 39.174 1.00 16.70 6ADH2602
ATOM 2204 N LEU A 301 1.169 .170 41.268 1.00 16.70 6ADH2603
ATOM 2205 CA LEU A 301 2.336 .444 42.105 1.00 16.70 6ADH2604
ATOM 2206 C LEU A 301 1.961 .145 43.558 1.00 16.70 6ADH2605
ATOM 2207 O LEU A 301 .846 .454 44.008 1.00 16.70 6ADH2606
ATOM 2208 CB LEU A 301 2.869 1.899 41.907 1.00 16.70 6ADH2607
ATOM 2209 CG LEU A 301 1.891 3.041 42.239 1.00 16.70 6ADH2608
ATOM 2210 CD1 LEU A 301 1.864 3.402 43.726 1.00 16.70 6ADH2609
ATOM 2211 CD2 LEU A 301 2.232 4.348 41.513 1.00 16.70 6ADH2610
ATOM 2212 N SER A 302 2.919 -.467 44.230 1.00 16.70 6ADH2611
ATOM 2213 CA SER A 302 2.791 -.853 45.638 1.00 16.70 6ADH2612
ATOM 2214 C SER A 302 3.484 .188 46.517 1.00 16.70 6ADH2613
ATOM 2215 O SER A 302 4.703 .119 46.745 1.00 16.70 6ADH2614
ATOM 2216 CB SER A 302 3.420 -2.230 45.866 1.00 16.70 6ADH2615
ATOM 2217 OG SER A 302 2.474 -3.102 46.469 1.00 16.70 6ADH2616
ATOM 2218 N MET A 303 2.652 1.117 46.970 1.00 16.70 6ADH2617
ATOM 2219 CA MET A 303 3.072 2.236 47.825 1.00 16.70 6ADH2618
ATOM 2220 C MET A 303 2.449 2.158 49.219 1.00 16.70 6ADH2619
ATOM 2221 O MET A 303 1.414 1.501 49.416 1.00 16.70 6ADH2620
ATOM 2222 CB MET A 303 2.603 3.569 47.265 1.00 16.70 6ADH2621
ATOM 2223 CG MET A 303 2.005 4.458 48.357 1.00 16.70 6ADH2622
ATOM 2224 SD MET A 303 .900 5.698 47.729 1.00 16.70 6ADH2623
ATOM 2225 CE MET A 303 1.493 7.315 48.178 1.00 16.70 6ADH2624
ATOM 2226 N ASN A 304 3.135 2.857 50.105 1.00 16.70 6ADH2625
ATOM 2227 CA ASN A 304 2.782 2.995 51.525 1.00 16.70 6ADH2626
ATOM 2228 C ASN A 304 2.125 4.362 51.739 1.00 16.70 6ADH2627
ATOM 2229 O ASN A 304 2.749 5.412 51.525 1.00 16.70 6ADH2628
ATOM 2230 CB ASN A 304 4.065 2.909 52.361 1.00 16.70 6ADH2629
ATOM 2231 CG ASN A 304 3.814 2.646 53.845 1.00 16.70 6ADH2630
ATOM 2232 OD1 ASN A 304 4.336 1.677 54.394 1.00 16.70 6ADH2631
ATOM 2233 ND2 ASN A 304 3.038 3.459 54.538 1.00 16.70 6ADH2632
ATOM 2234 N PRO A 305 .863 4.433 52.170 1.00 16.70 6ADH2633
ATOM 2235 CA PRO A 305 .186 5.714 52.342 1.00 16.70 6ADH2634
ATOM 2236 C PRO A 305 .884 6.617 53.353 1.00 16.70 6ADH2635
ATOM 2237 O PRO A 305 .441 7.788 53.569 1.00 16.70 6ADH2636
ATOM 2238 CB PRO A 305 -1.193 5.324 52.829 1.00 16.70 6ADH2637
ATOM 2239 CG PRO A 305 -1.250 3.804 52.920 1.00 16.70 6ADH2638
ATOM 2240 CD PRO A 305 .072 3.244 52.499 1.00 16.70 6ADH2639
ATOM 2241 N MET A 306 1.938 6.127 53.964 1.00 16.70 6ADH2640
ATOM 2242 CA MET A 306 2.654 6.884 55.022 1.00 16.70 6ADH2641
ATOM 2243 C MET A 306 3.688 7.848 54.414 1.00 16.70 6ADH2642
ATOM 2244 O MET A 306 4.039 8.867 55.033 1.00 16.70 6ADH2643
ATOM 2245 CB MET A 306 3.365 5.908 55.955 1.00 16.70 6ADH2644
ATOM 2246 CG MET A 306 2.934 6.061 57.413 1.00 16.70 6ADH2645
ATOM 2247 SD MET A 306 3.773 7.393 58.242 1.00 16.70 6ADH2646
ATOM 2248 CE MET A 306 2.630 8.281 59.280 1.00 16.70 6ADH2647
ATOM 2249 N LEU A 307 4.122 7.449 53.219 1.00 16.70 6ADH2648
ATOM 2250 CA LEU A 307 5.083 8.183 52.370 1.00 16.70 6ADH2649
ATOM 2251 C LEU A 307 4.570 9.605 52.147 1.00 16.70 6ADH2650
ATOM 2252 O LEU A 307 5.341 10.576 52.180 1.00 16.70 6ADH2651
ATOM 2253 CB LEU A 307 5.158 7.491 50.991 1.00 16.70 6ADH2652
ATOM 2254 CG LEU A 307 6.579 7.280 50.459 1.00 16.70 6ADH2653
ATOM 2255 CD1 LEU A 307 7.586 6.936 51.559 1.00 16.70 6ADH2654
ATOM 2256 CD2 LEU A 307 6.673 6.141 49.441 1.00 16.70 6ADH2655
ATOM 2257 N LEU A 308 3.267 9.630 51.939 1.00 16.70 6ADH2656
ATOM 2258 CA LEU A 308 2.492 10.841 51.640 1.00 16.70 6ADH2657
ATOM 2259 C LEU A 308 2.040 11.591 52.910 1.00 16.70 6ADH2658
ATOM 2260 O LEU A 308 1.941 12.826 52.919 1.00 16.70 6ADH2659
ATOM 2261 CB LEU A 308 1.190 10.459 50.915 1.00 16.70 6ADH2660
ATOM 2262 CG LEU A 308 1.310 10.418 49.390 1.00 16.70 6ADH2661
ATOM 2263 CD1 LEU A 308 -.032 10.618 48.682 1.00 16.70 6ADH2662
ATOM 2264 CD2 LEU A 308 2.237 11.499 48.834 1.00 16.70 6ADH2663
ATOM 2265 N LEU A 309 1.781 10.822 53.959 1.00 16.70 6ADH2664
ATOM 2266 CA LEU A 309 1.167 11.329 55.221 1.00 16.70 6ADH2665
ATOM 2267 C LEU A 309 1.951 12.445 55.963 1.00 16.70 6ADH2666
ATOM 2268 O LEU A 309 1.349 13.333 56.584 1.00 16.70 6ADH2667
ATOM 2269 CB LEU A 309 .957 10.208 56.221 1.00 16.70 6ADH2668
ATOM 2270 CG LEU A 309 -.167 10.537 57.203 1.00 16.70 6ADH2669
ATOM 2271 CD1 LEU A 309 -1.455 9.759 56.921 1.00 16.70 6ADH2670
ATOM 2272 CD2 LEU A 309 .199 10.226 58.654 1.00 16.70 6ADH2671
ATOM 2273 N SER A 310 3.279 12.399 55.908 1.00 16.70 6ADH2672
ATOM 2274 CA SER A 310 4.138 13.419 56.557 1.00 16.70 6ADH2673
ATOM 2275 C SER A 310 3.980 14.772 55.847 1.00 16.70 6ADH2674
ATOM 2276 O SER A 310 4.049 15.840 56.474 1.00 16.70 6ADH2675
ATOM 2277 CB SER A 310 5.605 13.001 56.513 1.00 16.70 6ADH2676
ATOM 2278 OG SER A 310 5.714 11.681 56.005 1.00 16.70 6ADH2677
ATOM 2279 N GLY A 311 3.776 14.753 54.532 1.00 16.70 6ADH2678
ATOM 2280 CA GLY A 311 3.493 16.024 53.835 1.00 16.70 6ADH2679
ATOM 2281 C GLY A 311 4.050 16.137 52.411 1.00 16.70 6ADH2680
ATOM 2282 O GLY A 311 4.497 17.214 51.985 1.00 16.70 6ADH2681
ATOM 2283 N ARG A 312 4.031 15.062 51.659 1.00 16.70 6ADH2682
ATOM 2284 CA ARG A 312 4.485 15.134 50.263 1.00 16.70 6ADH2683
ATOM 2285 C ARG A 312 3.299 15.219 49.329 1.00 16.70 6ADH2684
ATOM 2286 O ARG A 312 2.360 14.416 49.413 1.00 16.70 6ADH2685
ATOM 2287 CB ARG A 312 5.205 13.870 49.814 1.00 16.70 6ADH2686
ATOM 2288 CG ARG A 312 6.435 13.512 50.627 1.00 16.70 6ADH2687
ATOM 2289 CD ARG A 312 6.843 12.060 50.386 1.00 16.70 6ADH2688
ATOM 2290 NE ARG A 312 8.280 11.825 50.512 1.00 16.70 6ADH2689
ATOM 2291 CZ ARG A 312 8.816 11.073 51.475 1.00 16.70 6ADH2690
ATOM 2292 NH1 ARG A 312 8.044 10.490 52.402 1.00 16.70 6ADH2691
ATOM 2293 NH2 ARG A 312 10.129 10.837 51.598 1.00 16.70 6ADH2692
ATOM 2294 N THR A 313 3.355 16.175 48.452 1.00 16.70 6ADH2693
ATOM 2295 CA THR A 313 2.324 16.317 47.447 1.00 16.70 6ADH2694
ATOM 2296 C THR A 313 2.841 15.539 46.185 1.00 16.70 6ADH2695
ATOM 2297 O THR A 313 3.952 15.792 45.695 1.00 16.70 6ADH2696
ATOM 2298 CB THR A 313 2.007 17.833 47.297 1.00 16.70 6ADH2697
ATOM 2299 OG1 THR A 313 2.326 18.293 45.993 1.00 16.70 6ADH2698
ATOM 2300 CG2 THR A 313 2.784 18.716 48.280 1.00 16.70 6ADH2699
ATOM 2301 N TRP A 314 2.004 14.576 45.731 1.00 16.70 6ADH2700
ATOM 2302 CA TRP A 314 2.221 13.729 44.502 1.00 16.70 6ADH2701
ATOM 2303 C TRP A 314 1.284 14.271 43.413 1.00 16.70 6ADH2702
ATOM 2304 O TRP A 314 .075 14.435 43.633 1.00 16.70 6ADH2703
ATOM 2305 CB TRP A 314 1.830 12.236 44.784 1.00 16.70 6ADH2704
ATOM 2306 CG TRP A 314 2.731 11.128 44.134 1.00 16.70 6ADH2705
ATOM 2307 CD1 TRP A 314 3.855 11.290 43.408 1.00 16.70 6ADH2706
ATOM 2308 CD2 TRP A 314 2.490 9.710 44.211 1.00 16.70 6ADH2707
ATOM 2309 NE1 TRP A 314 4.340 9.980 43.053 1.00 16.70 6ADH2708
ATOM 2310 CE2 TRP A 314 3.534 9.071 43.542 1.00 16.70 6ADH2709
ATOM 2311 CE3 TRP A 314 1.492 8.924 44.808 1.00 16.70 6ADH2710
ATOM 2312 CZ2 TRP A 314 3.654 7.675 43.455 1.00 16.70 6ADH2711
ATOM 2313 CZ3 TRP A 314 1.616 7.519 44.706 1.00 16.70 6ADH2712
ATOM 2314 CH2 TRP A 314 2.649 6.925 44.063 1.00 16.70 6ADH2713
ATOM 2315 N LYS A 315 1.842 14.547 42.260 1.00 16.70 6ADH2714
ATOM 2316 CA LYS A 315 1.070 15.083 41.133 1.00 16.70 6ADH2715
ATOM 2317 C LYS A 315 1.388 14.289 39.876 1.00 16.70 6ADH2716
ATOM 2318 O LYS A 315 2.118 13.289 39.920 1.00 16.70 6ADH2717
ATOM 2319 CB LYS A 315 1.418 16.559 40.920 1.00 16.70 6ADH2718
ATOM 2320 CG LYS A 315 .854 17.470 42.016 1.00 16.70 6ADH2719
ATOM 2321 CD LYS A 315 1.208 18.945 41.812 1.00 16.70 6ADH2720
ATOM 2322 CE LYS A 315 .680 19.847 42.929 1.00 16.70 6ADH2721
ATOM 2323 NZ LYS A 315 1.716 20.721 43.500 1.00 16.70 6ADH2722
ATOM 2324 N GLY A 316 .826 14.753 38.804 1.00 16.70 6ADH2723
ATOM 2325 CA GLY A 316 1.002 14.136 37.505 1.00 16.70 6ADH2724
ATOM 2326 C GLY A 316 .569 15.116 36.465 1.00 16.70 6ADH2725
ATOM 2327 O GLY A 316 -.150 16.086 36.762 1.00 16.70 6ADH2726
ATOM 2328 N ALA A 317 1.006 14.849 35.275 1.00 16.70 6ADH2727
ATOM 2329 CA ALA A 317 .676 15.743 34.210 1.00 16.70 6ADH2728
ATOM 2330 C ALA A 317 .941 15.185 32.843 1.00 16.70 6ADH2729
ATOM 2331 O ALA A 317 1.961 14.513 32.611 1.00 16.70 6ADH2730
ATOM 2332 CB ALA A 317 1.507 17.022 34.328 1.00 16.70 6ADH2731
ATOM 2333 N ILE A 318 -.034 15.525 32.045 1.00 16.70 6ADH2732
ATOM 2334 CA ILE A 318 -.004 15.348 30.608 1.00 16.70 6ADH2733
ATOM 2335 C ILE A 318 .200 16.758 30.044 1.00 16.70 6ADH2734
ATOM 2336 O ILE A 318 -.544 17.689 30.383 1.00 16.70 6ADH2735
ATOM 2337 CB ILE A 318 -1.295 14.731 30.100 1.00 16.70 6ADH2736
ATOM 2338 CG1 ILE A 318 -1.053 13.523 29.191 1.00 16.70 6ADH2737
ATOM 2339 CG2 ILE A 318 -2.129 15.713 29.277 1.00 16.70 6ADH2738
ATOM 2340 CD1 ILE A 318 -1.081 12.192 29.944 1.00 16.70 6ADH2739
ATOM 2341 N PHE A 319 1.206 16.834 29.190 1.00 16.70 6ADH2740
ATOM 2342 CA PHE A 319 1.740 18.090 28.662 1.00 16.70 6ADH2741
ATOM 2343 C PHE A 319 2.486 18.700 29.839 1.00 16.70 6ADH2742
ATOM 2344 O PHE A 319 3.051 17.980 30.674 1.00 16.70 6ADH2743
ATOM 2345 CB PHE A 319 .636 18.986 28.099 1.00 16.70 6ADH2744
ATOM 2346 CG PHE A 319 1.083 19.675 26.806 1.00 16.70 6ADH2745
ATOM 2347 CD1 PHE A 319 2.175 19.167 26.090 1.00 16.70 6ADH2746
ATOM 2348 CD2 PHE A 319 .411 20.812 26.340 1.00 16.70 6ADH2747
ATOM 2349 CE1 PHE A 319 2.598 19.796 24.914 1.00 16.70 6ADH2748
ATOM 2350 CE2 PHE A 319 .834 21.441 25.164 1.00 16.70 6ADH2749
ATOM 2351 CZ PHE A 319 1.927 20.933 24.451 1.00 16.70 6ADH2750
ATOM 2352 N GLY A 320 2.499 19.994 29.915 1.00 16.70 6ADH2751
ATOM 2353 CA GLY A 320 3.129 20.680 31.040 1.00 16.70 6ADH2752
ATOM 2354 C GLY A 320 2.026 21.316 31.869 1.00 16.70 6ADH2753
ATOM 2355 O GLY A 320 2.268 22.259 32.636 1.00 16.70 6ADH2754
ATOM 2356 N GLY A 321 .843 20.760 31.679 1.00 16.70 6ADH2755
ATOM 2357 CA GLY A 321 -.375 21.277 32.307 1.00 16.70 6ADH2756
ATOM 2358 C GLY A 321 -.697 22.598 31.616 1.00 16.70 6ADH2757
ATOM 2359 O GLY A 321 -1.356 23.474 32.193 1.00 16.70 6ADH2758
ATOM 2360 N PHE A 322 -.188 22.642 30.400 1.00 16.70 6ADH2759
ATOM 2361 CA PHE A 322 -.293 23.778 29.486 1.00 16.70 6ADH2760
ATOM 2362 C PHE A 322 -1.615 23.697 28.703 1.00 16.70 6ADH2761
ATOM 2363 O PHE A 322 -1.848 22.748 27.939 1.00 16.70 6ADH2762
ATOM 2364 CB PHE A 322 .886 23.727 28.478 1.00 16.70 6ADH2763
ATOM 2365 CG PHE A 322 2.215 24.333 28.993 1.00 16.70 6ADH2764
ATOM 2366 CD1 PHE A 322 2.248 25.644 29.491 1.00 16.70 6ADH2765
ATOM 2367 CD2 PHE A 322 3.405 23.584 28.958 1.00 16.70 6ADH2766
ATOM 2368 CE1 PHE A 322 3.454 26.200 29.949 1.00 16.70 6ADH2767
ATOM 2369 CE2 PHE A 322 4.611 24.141 29.415 1.00 16.70 6ADH2768
ATOM 2370 CZ PHE A 322 4.635 25.450 29.910 1.00 16.70 6ADH2769
ATOM 2371 N LYS A 323 -2.463 24.696 28.921 1.00 16.70 6ADH2770
ATOM 2372 CA LYS A 323 -3.718 24.819 28.162 1.00 16.70 6ADH2771
ATOM 2373 C LYS A 323 -3.298 24.836 26.676 1.00 16.70 6ADH2772
ATOM 2374 O LYS A 323 -2.766 25.837 26.177 1.00 16.70 6ADH2773
ATOM 2375 CB LYS A 323 -4.458 26.105 28.589 1.00 16.70 6ADH2774
ATOM 2376 CG LYS A 323 -5.886 25.846 29.110 1.00 16.70 6ADH2775
ATOM 2377 CD LYS A 323 -6.084 26.243 30.583 1.00 16.70 6ADH2776
ATOM 2378 CE LYS A 323 -7.526 26.656 30.907 1.00 16.70 6ADH2777
ATOM 2379 NZ LYS A 323 -8.013 26.106 32.181 1.00 16.70 6ADH2778
ATOM 2380 N SER A 324 -3.557 23.713 26.036 1.00 16.70 6ADH2779
ATOM 2381 CA SER A 324 -3.123 23.390 24.651 1.00 16.70 6ADH2780
ATOM 2382 C SER A 324 -3.244 24.518 23.590 1.00 16.70 6ADH2781
ATOM 2383 O SER A 324 -2.255 24.913 22.956 1.00 16.70 6ADH2782
ATOM 2384 CB SER A 324 -3.911 22.198 24.102 1.00 16.70 6ADH2783
ATOM 2385 OG SER A 324 -3.033 21.104 23.874 1.00 16.70 6ADH2784
ATOM 2386 N LYS A 325 -4.423 25.067 23.357 1.00 16.70 6ADH2785
ATOM 2387 CA LYS A 325 -4.590 25.995 22.206 1.00 16.70 6ADH2786
ATOM 2388 C LYS A 325 -4.267 27.478 22.486 1.00 16.70 6ADH2787
ATOM 2389 O LYS A 325 -4.479 28.349 21.628 1.00 16.70 6ADH2788
ATOM 2390 CB LYS A 325 -5.996 25.871 21.636 1.00 16.70 6ADH2789
ATOM 2391 CG LYS A 325 -6.146 24.599 20.795 1.00 16.70 6ADH2790
ATOM 2392 CD LYS A 325 -7.299 24.663 19.793 1.00 16.70 6ADH2791
ATOM 2393 CE LYS A 325 -7.441 26.031 19.124 1.00 16.70 6ADH2792
ATOM 2394 NZ LYS A 325 -8.614 26.117 18.243 1.00 16.70 6ADH2793
ATOM 2395 N ASP A 326 -3.765 27.798 23.663 1.00 16.70 6ADH2794
ATOM 2396 CA ASP A 326 -3.270 29.173 23.889 1.00 16.70 6ADH2795
ATOM 2397 C ASP A 326 -1.944 29.152 24.601 1.00 16.70 6ADH2796
ATOM 2398 O ASP A 326 -1.442 30.183 25.067 1.00 16.70 6ADH2797
ATOM 2399 CB ASP A 326 -4.212 30.103 24.674 1.00 16.70 6ADH2798
ATOM 2400 CG ASP A 326 -5.041 29.439 25.763 1.00 16.70 6ADH2799
ATOM 2401 OD1 ASP A 326 -6.303 29.685 25.841 1.00 16.70 6ADH2800
ATOM 2402 OD2 ASP A 326 -4.481 28.639 26.606 1.00 16.70 6ADH2801
ATOM 2403 N SER A 327 -1.368 28.002 24.685 1.00 16.70 6ADH2802
ATOM 2404 CA SER A 327 -.052 27.909 25.280 1.00 16.70 6ADH2803
ATOM 2405 C SER A 327 1.013 27.500 24.221 1.00 16.70 6ADH2804
ATOM 2406 O SER A 327 2.196 27.830 24.351 1.00 16.70 6ADH2805
ATOM 2407 CB SER A 327 -.048 26.898 26.422 0.00 16.70 2 6ADH2806
ATOM 2408 OG SER A 327 1.173 26.176 26.421 0.00 16.70 2 6ADH2807
ATOM 2409 N VAL A 328 .615 26.783 23.151 1.00 16.70 6ADH2808
ATOM 2410 CA VAL A 328 1.582 26.290 22.105 1.00 16.70 6ADH2809
ATOM 2411 C VAL A 328 2.047 27.449 21.187 1.00 16.70 6ADH2810
ATOM 2412 O VAL A 328 3.230 27.541 20.823 1.00 16.70 6ADH2811
ATOM 2413 CB VAL A 328 .957 25.158 21.281 1.00 16.70 6ADH2812
ATOM 2414 CG1 VAL A 328 1.128 25.344 19.773 1.00 16.70 6ADH2813
ATOM 2415 CG2 VAL A 328 1.563 23.788 21.598 1.00 16.70 6ADH2814
ATOM 2416 N PRO A 329 1.162 28.372 20.767 1.00 16.70 6ADH2815
ATOM 2417 CA PRO A 329 1.567 29.550 19.991 1.00 16.70 6ADH2816
ATOM 2418 C PRO A 329 2.474 30.481 20.781 1.00 16.70 6ADH2817
ATOM 2419 O PRO A 329 3.477 31.004 20.203 1.00 16.70 6ADH2818
ATOM 2420 CB PRO A 329 .274 30.271 19.714 1.00 16.70 6ADH2819
ATOM 2421 CG PRO A 329 -.853 29.474 20.355 1.00 16.70 6ADH2820
ATOM 2422 CD PRO A 329 -.277 28.262 21.021 1.00 16.70 6ADH2821
ATOM 2423 N LYS A 330 2.092 30.667 22.038 1.00 16.70 6ADH2822
ATOM 2424 CA LYS A 330 2.781 31.556 22.996 1.00 16.70 6ADH2823
ATOM 2425 C LYS A 330 4.175 31.053 23.300 1.00 16.70 6ADH2824
ATOM 2426 O LYS A 330 5.102 31.836 23.554 1.00 16.70 6ADH2825
ATOM 2427 CB LYS A 330 2.013 31.576 24.322 1.00 16.70 6ADH2826
ATOM 2428 CG LYS A 330 2.110 32.909 25.064 1.00 16.70 6ADH2827
ATOM 2429 CD LYS A 330 .741 33.553 25.301 1.00 16.70 6ADH2828
ATOM 2430 CE LYS A 330 .482 33.893 26.769 1.00 16.70 6ADH2829
ATOM 2431 NZ LYS A 330 -.019 35.261 26.961 1.00 16.70 6ADH2830
ATOM 2432 N LEU A 331 4.285 29.762 23.263 1.00 16.70 6ADH2831
ATOM 2433 CA LEU A 331 5.533 29.100 23.587 1.00 16.70 6ADH2832
ATOM 2434 C LEU A 331 6.493 29.055 22.390 1.00 16.70 6ADH2833
ATOM 2435 O LEU A 331 7.590 28.487 22.472 1.00 16.70 6ADH2834
ATOM 2436 CB LEU A 331 5.261 27.674 24.054 1.00 16.70 6ADH2835
ATOM 2437 CG LEU A 331 5.883 27.382 25.419 1.00 16.70 6ADH2836
ATOM 2438 CD1 LEU A 331 5.452 26.032 25.996 1.00 16.70 6ADH2837
ATOM 2439 CD2 LEU A 331 7.412 27.349 25.381 1.00 16.70 6ADH2838
ATOM 2440 N VAL A 332 6.108 29.652 21.274 1.00 16.70 6ADH2839
ATOM 2441 CA VAL A 332 6.966 29.638 20.063 1.00 16.70 6ADH2840
ATOM 2442 C VAL A 332 7.667 30.994 19.847 1.00 16.70 6ADH2841
ATOM 2443 O VAL A 332 8.842 31.048 19.452 1.00 16.70 6ADH2842
ATOM 2444 CB VAL A 332 6.137 29.321 18.816 1.00 16.70 6ADH2843
ATOM 2445 CG1 VAL A 332 6.852 29.688 17.514 1.00 16.70 6ADH2844
ATOM 2446 CG2 VAL A 332 5.789 27.835 18.691 1.00 16.70 6ADH2845
ATOM 2447 N ALA A 333 6.913 32.053 20.112 1.00 16.70 6ADH2846
ATOM 2448 CA ALA A 333 7.378 33.455 19.955 1.00 16.70 6ADH2847
ATOM 2449 C ALA A 333 8.578 33.729 20.873 1.00 16.70 6ADH2848
ATOM 2450 O ALA A 333 9.253 34.762 20.743 0.00 16.70 2 6ADH2849
ATOM 2451 CB ALA A 333 6.251 34.418 20.336 1.00 16.70 6ADH2850
ATOM 2452 N ASP A 334 8.757 32.751 21.751 1.00 16.70 6ADH2851
ATOM 2453 CA ASP A 334 9.766 32.734 22.832 1.00 16.70 6ADH2852
ATOM 2454 C ASP A 334 11.086 32.110 22.389 1.00 16.70 6ADH2853
ATOM 2455 O ASP A 334 12.171 32.607 22.726 0.00 16.70 2 6ADH2854
ATOM 2456 CB ASP A 334 9.258 31.863 23.966 1.00 16.70 6ADH2855
ATOM 2457 CG ASP A 334 8.539 32.655 25.046 1.00 16.70 6ADH2856
ATOM 2458 OD1 ASP A 334 8.717 32.350 26.285 1.00 16.70 6ADH2857
ATOM 2459 OD2 ASP A 334 7.755 33.625 24.719 1.00 16.70 6ADH2858
ATOM 2460 N PHE A 335 10.924 31.024 21.672 1.00 16.70 6ADH2859
ATOM 2461 CA PHE A 335 12.029 30.272 21.085 1.00 16.70 6ADH2860
ATOM 2462 C PHE A 335 12.620 31.150 20.017 1.00 16.70 6ADH2861
ATOM 2463 O PHE A 335 13.847 31.238 19.866 0.00 16.70 2 6ADH2862
ATOM 2464 CB PHE A 335 11.463 28.985 20.484 1.00 16.70 6ADH2863
ATOM 2465 CG PHE A 335 12.396 28.289 19.498 1.00 16.70 6ADH2864
ATOM 2466 CD1 PHE A 335 12.334 28.598 18.133 1.00 16.70 6ADH2865
ATOM 2467 CD2 PHE A 335 13.303 27.333 19.963 1.00 16.70 6ADH2866
ATOM 2468 CE1 PHE A 335 13.180 27.943 17.232 1.00 16.70 6ADH2867
ATOM 2469 CE2 PHE A 335 14.148 26.678 19.062 1.00 16.70 6ADH2868
ATOM 2470 CZ PHE A 335 14.087 26.981 17.696 1.00 16.70 6ADH2869
ATOM 2471 N MET A 336 11.683 31.756 19.340 1.00 16.70 6ADH2870
ATOM 2472 CA MET A 336 11.965 32.708 18.293 1.00 16.70 6ADH2871
ATOM 2473 C MET A 336 12.631 33.926 18.912 1.00 16.70 6ADH2872
ATOM 2474 O MET A 336 13.329 34.687 18.231 1.00 16.70 6ADH2873
ATOM 2475 CB MET A 336 10.663 33.158 17.633 1.00 16.70 6ADH2874
ATOM 2476 CG MET A 336 9.957 32.034 16.878 1.00 16.70 6ADH2875
ATOM 2477 SD MET A 336 10.328 32.037 15.139 1.00 16.70 6ADH2876
ATOM 2478 CE MET A 336 11.152 33.551 14.694 1.00 16.70 6ADH2877
ATOM 2479 N ALA A 337 12.396 34.076 20.204 1.00 16.70 6ADH2878
ATOM 2480 CA ALA A 337 12.914 35.219 20.974 1.00 16.70 6ADH2879
ATOM 2481 C ALA A 337 13.977 34.783 21.988 1.00 16.70 6ADH2880
ATOM 2482 O ALA A 337 14.218 35.463 22.992 1.00 16.70 6ADH2881
ATOM 2483 CB ALA A 337 11.779 35.902 21.735 1.00 16.70 6ADH2882
ATOM 2484 N LYS A 338 14.558 33.650 21.687 1.00 16.70 6ADH2883
ATOM 2485 CA LYS A 338 15.714 33.087 22.411 1.00 16.70 6ADH2884
ATOM 2486 C LYS A 338 15.502 32.980 23.937 1.00 16.70 6ADH2885
ATOM 2487 O LYS A 338 16.421 33.267 24.722 1.00 16.70 6ADH2886
ATOM 2488 CB LYS A 338 16.935 33.946 22.093 1.00 16.70 6ADH2887
ATOM 2489 CG LYS A 338 16.699 34.894 20.907 1.00 16.70 6ADH2888
ATOM 2490 CD LYS A 338 17.140 34.310 19.561 1.00 16.70 6ADH2889
ATOM 2491 CE LYS A 338 18.292 33.311 19.688 1.00 16.70 6ADH2890
ATOM 2492 NZ LYS A 338 18.096 32.104 18.874 0.00 16.70 2 6ADH2891
ATOM 2493 N LYS A 339 14.277 32.559 24.241 1.00 16.70 6ADH2892
ATOM 2494 CA LYS A 339 13.842 32.211 25.583 1.00 16.70 6ADH2893
ATOM 2495 C LYS A 339 14.555 30.880 25.917 1.00 16.70 6ADH2894
ATOM 2496 O LYS A 339 15.171 30.726 26.974 1.00 16.70 6ADH2895
ATOM 2497 CB LYS A 339 12.304 32.087 25.611 1.00 16.70 6ADH2896
ATOM 2498 CG LYS A 339 11.580 33.438 25.540 1.00 16.70 6ADH2897
ATOM 2499 CD LYS A 339 12.535 34.632 25.497 1.00 16.70 6ADH2898
ATOM 2500 CE LYS A 339 13.360 34.784 26.776 1.00 16.70 6ADH2899
ATOM 2501 NZ LYS A 339 12.552 35.183 27.937 1.00 16.70 6ADH2900
ATOM 2502 N PHE A 340 14.497 29.921 24.993 1.00 16.70 6ADH2901
ATOM 2503 CA PHE A 340 15.162 28.616 25.197 1.00 16.70 6ADH2902
ATOM 2504 C PHE A 340 15.854 28.141 23.920 1.00 16.70 6ADH2903
ATOM 2505 O PHE A 340 15.926 28.873 22.920 1.00 16.70 6ADH2904
ATOM 2506 CB PHE A 340 14.158 27.537 25.649 1.00 16.70 6ADH2905
ATOM 2507 CG PHE A 340 12.770 27.630 24.998 1.00 16.70 6ADH2906
ATOM 2508 CD1 PHE A 340 11.770 28.419 25.585 1.00 16.70 6ADH2907
ATOM 2509 CD2 PHE A 340 12.493 26.916 23.825 1.00 16.70 6ADH2908
ATOM 2510 CE1 PHE A 340 10.498 28.492 24.998 1.00 16.70 6ADH2909
ATOM 2511 CE2 PHE A 340 11.221 26.989 23.240 1.00 16.70 6ADH2910
ATOM 2512 CZ PHE A 340 10.224 27.778 23.827 1.00 16.70 6ADH2911
ATOM 2513 N ALA A 341 16.340 26.924 24.024 1.00 16.70 6ADH2912
ATOM 2514 CA ALA A 341 17.046 26.249 22.940 1.00 16.70 6ADH2913
ATOM 2515 C ALA A 341 16.518 24.835 22.788 1.00 16.70 6ADH2914
ATOM 2516 O ALA A 341 16.493 24.057 23.753 0.00 16.70 2 6ADH2915
ATOM 2517 CB ALA A 341 18.544 26.185 23.244 1.00 16.70 6ADH2916
ATOM 2518 N LEU A 342 16.130 24.581 21.568 1.00 16.70 6ADH2917
ATOM 2519 CA LEU A 342 15.575 23.302 21.140 1.00 16.70 6ADH2918
ATOM 2520 C LEU A 342 16.652 22.406 20.516 1.00 16.70 6ADH2919
ATOM 2521 O LEU A 342 16.416 21.225 20.234 0.00 16.70 2 6ADH2920
ATOM 2522 CB LEU A 342 14.582 23.536 19.987 1.00 16.70 6ADH2921
ATOM 2523 CG LEU A 342 13.117 23.270 20.329 1.00 16.70 6ADH2922
ATOM 2524 CD1 LEU A 342 12.844 23.246 21.833 1.00 16.70 6ADH2923
ATOM 2525 CD2 LEU A 342 12.174 24.327 19.751 1.00 16.70 6ADH2924
ATOM 2526 N ASP A 343 17.822 22.973 20.293 1.00 16.70 6ADH2925
ATOM 2527 CA ASP A 343 18.906 22.299 19.524 1.00 16.70 6ADH2926
ATOM 2528 C ASP A 343 19.683 21.249 20.295 1.00 16.70 6ADH2927
ATOM 2529 O ASP A 343 19.989 20.169 19.767 1.00 16.70 6ADH2928
ATOM 2530 CB ASP A 343 19.912 23.320 19.055 1.00 16.70 6ADH2929
ATOM 2531 CG ASP A 343 19.385 24.117 17.876 1.00 16.70 6ADH2930
ATOM 2532 OD1 ASP A 343 19.906 23.956 16.709 1.00 16.70 6ADH2931
ATOM 2533 OD2 ASP A 343 18.417 24.951 18.047 1.00 16.70 6ADH2932
ATOM 2534 N PRO A 344 20.036 21.511 21.529 1.00 16.70 6ADH2933
ATOM 2535 CA PRO A 344 20.775 20.554 22.334 1.00 16.70 6ADH2934
ATOM 2536 C PRO A 344 20.064 19.191 22.524 1.00 16.70 6ADH2935
ATOM 2537 O PRO A 344 20.722 18.213 22.996 1.00 16.70 6ADH2936
ATOM 2538 CB PRO A 344 20.965 21.280 23.646 1.00 16.70 6ADH2937
ATOM 2539 CG PRO A 344 20.317 22.652 23.527 1.00 16.70 6ADH2938
ATOM 2540 CD PRO A 344 19.726 22.790 22.162 1.00 16.70 6ADH2939
ATOM 2541 N LEU A 345 18.772 19.076 22.185 1.00 16.70 6ADH2940
ATOM 2542 CA LEU A 345 18.003 17.788 22.347 1.00 16.70 6ADH2941
ATOM 2543 C LEU A 345 18.266 16.856 21.138 1.00 16.70 6ADH2942
ATOM 2544 O LEU A 345 18.815 15.754 21.291 0.00 16.70 2 6ADH2943
ATOM 2545 CB LEU A 345 16.500 18.092 22.437 1.00 16.70 6ADH2944
ATOM 2546 CG LEU A 345 16.159 19.078 23.560 1.00 16.70 6ADH2945
ATOM 2547 CD1 LEU A 345 14.665 19.395 23.648 1.00 16.70 6ADH2946
ATOM 2548 CD2 LEU A 345 16.555 18.565 24.945 1.00 16.70 6ADH2947
ATOM 2549 N ILE A 346 17.832 17.415 20.020 1.00 16.70 6ADH2948
ATOM 2550 CA ILE A 346 17.940 16.904 18.632 1.00 16.70 6ADH2949
ATOM 2551 C ILE A 346 19.314 16.253 18.356 1.00 16.70 6ADH2950
ATOM 2552 O ILE A 346 20.357 16.918 18.389 1.00 16.70 6ADH2951
ATOM 2553 CB ILE A 346 17.846 18.123 17.719 1.00 16.70 6ADH2952
ATOM 2554 CG1 ILE A 346 16.419 18.434 17.274 1.00 16.70 6ADH2953
ATOM 2555 CG2 ILE A 346 18.672 17.977 16.441 1.00 16.70 6ADH2954
ATOM 2556 CD1 ILE A 346 15.953 19.827 17.704 1.00 16.70 6ADH2955
ATOM 2557 N THR A 347 19.314 14.966 18.057 1.00 16.70 6ADH2956
ATOM 2558 CA THR A 347 20.567 14.197 17.868 1.00 16.70 6ADH2957
ATOM 2559 C THR A 347 20.741 13.735 16.416 1.00 16.70 6ADH2958
ATOM 2560 O THR A 347 21.863 13.453 15.967 1.00 16.70 6ADH2959
ATOM 2561 CB THR A 347 20.513 12.956 18.760 1.00 16.70 6ADH2960
ATOM 2562 OG1 THR A 347 19.234 12.858 19.370 1.00 16.70 6ADH2961
ATOM 2563 CG2 THR A 347 21.552 12.976 19.882 1.00 16.70 6ADH2962
ATOM 2564 N HIS A 348 19.599 13.678 15.760 1.00 16.70 6ADH2963
ATOM 2565 CA HIS A 348 19.466 13.236 14.370 1.00 16.70 6ADH2964
ATOM 2566 C HIS A 348 18.287 13.942 13.703 1.00 16.70 6ADH2965
ATOM 2567 O HIS A 348 17.397 14.476 14.377 1.00 16.70 6ADH2966
ATOM 2568 CB HIS A 348 19.118 11.746 14.304 1.00 16.70 6ADH2967
ATOM 2569 CG HIS A 348 20.050 10.833 15.098 1.00 16.70 6ADH2968
ATOM 2570 ND1 HIS A 348 20.245 10.977 16.469 1.00 16.70 6ADH2969
ATOM 2571 CD2 HIS A 348 20.815 9.778 14.712 1.00 16.70 6ADH2970
ATOM 2572 CE1 HIS A 348 21.092 10.042 16.863 1.00 16.70 6ADH2971
ATOM 2573 NE2 HIS A 348 21.440 9.320 15.827 1.00 16.70 6ADH2972
ATOM 2574 N VAL A 349 18.331 13.904 12.404 1.00 16.70 6ADH2973
ATOM 2575 CA VAL A 349 17.297 14.442 11.521 1.00 16.70 6ADH2974
ATOM 2576 C VAL A 349 17.287 13.524 10.301 1.00 16.70 6ADH2975
ATOM 2577 O VAL A 349 18.031 13.739 9.336 1.00 16.70 6ADH2976
ATOM 2578 CB VAL A 349 17.651 15.887 11.134 1.00 16.70 6ADH2977
ATOM 2579 CG1 VAL A 349 16.489 16.639 10.483 1.00 16.70 6ADH2978
ATOM 2580 CG2 VAL A 349 18.076 16.744 12.331 1.00 16.70 6ADH2979
ATOM 2581 N LEU A 350 16.450 12.507 10.372 1.00 16.70 6ADH2980
ATOM 2582 CA LEU A 350 16.378 11.437 9.340 1.00 16.70 6ADH2981
ATOM 2583 C LEU A 350 15.303 11.686 8.277 1.00 16.70 6ADH2982
ATOM 2584 O LEU A 350 14.313 12.390 8.519 1.00 16.70 6ADH2983
ATOM 2585 CB LEU A 350 15.917 10.122 9.984 1.00 16.70 6ADH2984
ATOM 2586 CG LEU A 350 17.034 9.310 10.638 1.00 16.70 6ADH2985
ATOM 2587 CD1 LEU A 350 18.018 10.174 11.429 1.00 16.70 6ADH2986
ATOM 2588 CD2 LEU A 350 16.508 8.266 11.625 1.00 16.70 6ADH2987
ATOM 2589 N PRO A 351 15.392 11.150 7.030 1.00 16.70 6ADH2988
ATOM 2590 CA PRO A 351 14.268 11.240 6.106 1.00 16.70 6ADH2989
ATOM 2591 C PRO A 351 13.134 10.394 6.633 1.00 16.70 6ADH2990
ATOM 2592 O PRO A 351 13.397 9.332 7.274 1.00 16.70 6ADH2991
ATOM 2593 CB PRO A 351 14.762 10.587 4.842 1.00 16.70 6ADH2992
ATOM 2594 CG PRO A 351 16.184 10.107 5.093 1.00 16.70 6ADH2993
ATOM 2595 CD PRO A 351 16.589 10.483 6.488 1.00 16.70 6ADH2994
ATOM 2596 N PHE A 352 11.917 10.798 6.375 1.00 16.70 6ADH2995
ATOM 2597 CA PHE A 352 10.724 10.035 6.825 1.00 16.70 6ADH2996
ATOM 2598 C PHE A 352 10.994 8.474 6.724 1.00 16.70 6ADH2997
ATOM 2599 O PHE A 352 11.325 7.815 7.719 0.00 16.70 2 6ADH2998
ATOM 2600 CB PHE A 352 9.524 10.531 5.985 1.00 16.70 6ADH2999
ATOM 2601 CG PHE A 352 8.171 9.864 6.287 1.00 16.70 6ADH3000
ATOM 2602 CD1 PHE A 352 7.601 9.012 5.336 1.00 16.70 6ADH3001
ATOM 2603 CD2 PHE A 352 7.488 10.109 7.491 1.00 16.70 6ADH3002
ATOM 2604 CE1 PHE A 352 6.368 8.398 5.583 1.00 16.70 6ADH3003
ATOM 2605 CE2 PHE A 352 6.251 9.495 7.741 1.00 16.70 6ADH3004
ATOM 2606 CZ PHE A 352 5.692 8.637 6.786 1.00 16.70 6ADH3005
ATOM 2607 N GLU A 353 10.863 7.953 5.507 1.00 16.70 6ADH3006
ATOM 2608 CA GLU A 353 10.978 6.502 5.078 1.00 16.70 6ADH3007
ATOM 2609 C GLU A 353 12.050 5.597 5.830 1.00 16.70 6ADH3008
ATOM 2610 O GLU A 353 12.078 4.369 5.640 0.00 16.70 2 6ADH3009
ATOM 2611 CB GLU A 353 11.268 6.514 3.577 1.00 16.70 6ADH3010
ATOM 2612 CG GLU A 353 10.310 7.444 2.806 1.00 16.70 6ADH3011
ATOM 2613 CD GLU A 353 10.823 8.887 2.661 1.00 16.70 6ADH3012
ATOM 2614 OE1 GLU A 353 12.023 9.186 3.025 1.00 16.70 6ADH3013
ATOM 2615 OE2 GLU A 353 10.053 9.801 2.173 1.00 16.70 6ADH3014
ATOM 2616 N LYS A 354 12.887 6.251 6.659 1.00 16.70 6ADH3015
ATOM 2617 CA LYS A 354 13.952 5.628 7.512 1.00 16.70 6ADH3016
ATOM 2618 C LYS A 354 13.544 5.774 8.947 1.00 16.70 6ADH3017
ATOM 2619 O LYS A 354 14.387 5.779 9.859 1.00 16.70 6ADH3018
ATOM 2620 CB LYS A 354 15.252 6.410 7.404 1.00 16.70 6ADH3019
ATOM 2621 CG LYS A 354 16.020 6.151 6.122 1.00 16.70 6ADH3020
ATOM 2622 CD LYS A 354 17.479 6.582 6.231 1.00 16.70 6ADH3021
ATOM 2623 CE LYS A 354 18.283 6.292 4.966 0.00 16.70 2 6ADH3022
ATOM 2624 NZ LYS A 354 19.125 7.422 4.552 0.00 16.70 2 6ADH3023
ATOM 2625 N ILE A 355 12.271 5.922 9.030 1.00 16.70 6ADH3024
ATOM 2626 CA ILE A 355 11.591 6.116 10.265 1.00 16.70 6ADH3025
ATOM 2627 C ILE A 355 11.667 4.844 11.067 1.00 16.70 6ADH3026
ATOM 2628 O ILE A 355 11.207 4.768 12.210 1.00 16.70 6ADH3027
ATOM 2629 CB ILE A 355 10.143 6.494 9.975 1.00 16.70 6ADH3028
ATOM 2630 CG1 ILE A 355 9.150 5.837 10.930 1.00 16.70 6ADH3029
ATOM 2631 CG2 ILE A 355 9.695 6.097 8.568 1.00 16.70 6ADH3030
ATOM 2632 CD1 ILE A 355 8.197 6.840 11.584 1.00 16.70 6ADH3031
ATOM 2633 N ASN A 356 12.251 3.829 10.505 1.00 16.70 6ADH3032
ATOM 2634 CA ASN A 356 12.348 2.587 11.253 1.00 16.70 6ADH3033
ATOM 2635 C ASN A 356 13.733 2.454 11.935 1.00 16.70 6ADH3034
ATOM 2636 O ASN A 356 13.960 1.549 12.748 0.00 16.70 2 6ADH3035
ATOM 2637 CB ASN A 356 11.993 1.400 10.365 1.00 16.70 6ADH3036
ATOM 2638 CG ASN A 356 10.595 .852 10.697 1.00 16.70 6ADH3037
ATOM 2639 OD1 ASN A 356 9.714 .847 9.839 1.00 16.70 6ADH3038
ATOM 2640 ND2 ASN A 356 10.338 .387 11.906 1.00 16.70 6ADH3039
ATOM 2641 N GLU A 357 14.666 3.349 11.618 1.00 16.70 6ADH3040
ATOM 2642 CA GLU A 357 16.000 3.377 12.292 1.00 16.70 6ADH3041
ATOM 2643 C GLU A 357 15.946 4.461 13.341 1.00 16.70 6ADH3042
ATOM 2644 O GLU A 357 16.752 4.472 14.287 1.00 16.70 6ADH3043
ATOM 2645 CB GLU A 357 17.125 3.733 11.319 1.00 16.70 6ADH3044
ATOM 2646 CG GLU A 357 17.082 2.928 10.022 1.00 16.70 6ADH3045
ATOM 2647 CD GLU A 357 18.288 2.000 9.848 1.00 16.70 6ADH3046
ATOM 2648 OE1 GLU A 357 19.439 2.337 10.324 1.00 16.70 6ADH3047
ATOM 2649 OE2 GLU A 357 18.153 .880 9.222 1.00 16.70 6ADH3048
ATOM 2650 N GLY A 358 14.972 5.298 13.055 1.00 16.70 6ADH3049
ATOM 2651 CA GLY A 358 14.601 6.430 13.878 1.00 16.70 6ADH3050
ATOM 2652 C GLY A 358 14.195 5.918 15.250 1.00 16.70 6ADH3051
ATOM 2653 O GLY A 358 14.677 6.406 16.280 1.00 16.70 6ADH3052
ATOM 2654 N PHE A 359 13.312 4.937 15.242 1.00 16.70 6ADH3053
ATOM 2655 CA PHE A 359 12.823 4.325 16.488 1.00 16.70 6ADH3054
ATOM 2656 C PHE A 359 13.910 3.486 17.115 1.00 16.70 6ADH3055
ATOM 2657 O PHE A 359 14.096 3.480 18.338 1.00 16.70 6ADH3056
ATOM 2658 CB PHE A 359 11.656 3.394 16.214 1.00 16.70 6ADH3057
ATOM 2659 CG PHE A 359 10.321 4.107 16.263 1.00 16.70 6ADH3058
ATOM 2660 CD1 PHE A 359 9.985 5.000 15.247 1.00 16.70 6ADH3059
ATOM 2661 CD2 PHE A 359 9.442 3.869 17.323 1.00 16.70 6ADH3060
ATOM 2662 CE1 PHE A 359 8.753 5.656 15.281 1.00 16.70 6ADH3061
ATOM 2663 CE2 PHE A 359 8.209 4.525 17.360 1.00 16.70 6ADH3062
ATOM 2664 CZ PHE A 359 7.864 5.418 16.337 1.00 16.70 6ADH3063
ATOM 2665 N ASP A 360 14.583 2.819 16.244 1.00 16.70 6ADH3064
ATOM 2666 CA ASP A 360 15.669 1.913 16.584 1.00 16.70 6ADH3065
ATOM 2667 C ASP A 360 16.931 2.632 17.169 1.00 16.70 6ADH3066
ATOM 2668 O ASP A 360 17.967 2.001 17.405 1.00 16.70 6ADH3067
ATOM 2669 CB ASP A 360 16.122 1.192 15.313 1.00 16.70 6ADH3068
ATOM 2670 CG ASP A 360 15.490 -.189 15.140 1.00 16.70 6ADH3069
ATOM 2671 OD1 ASP A 360 14.430 -.327 14.416 1.00 16.70 6ADH3070
ATOM 2672 OD2 ASP A 360 16.018 -1.214 15.717 1.00 16.70 6ADH3071
ATOM 2673 N LEU A 361 16.876 3.956 17.392 1.00 16.70 6ADH3072
ATOM 2674 CA LEU A 361 18.032 4.759 17.952 1.00 16.70 6ADH3073
ATOM 2675 C LEU A 361 17.760 5.111 19.381 1.00 16.70 6ADH3074
ATOM 2676 O LEU A 361 18.664 5.066 20.233 1.00 16.70 6ADH3075
ATOM 2677 CB LEU A 361 18.117 6.122 17.279 1.00 16.70 6ADH3076
ATOM 2678 CG LEU A 361 18.805 6.094 15.927 1.00 16.70 6ADH3077
ATOM 2679 CD1 LEU A 361 18.620 7.395 15.144 1.00 16.70 6ADH3078
ATOM 2680 CD2 LEU A 361 20.315 5.878 16.036 1.00 16.70 6ADH3079
ATOM 2681 N LEU A 362 16.511 5.455 19.429 1.00 16.70 6ADH3080
ATOM 2682 CA LEU A 362 15.787 5.816 20.596 1.00 16.70 6ADH3081
ATOM 2683 C LEU A 362 15.776 4.645 21.504 1.00 16.70 6ADH3082
ATOM 2684 O LEU A 362 16.244 4.698 22.648 0.00 16.70 2 6ADH3083
ATOM 2685 CB LEU A 362 14.341 6.119 20.184 1.00 16.70 6ADH3084
ATOM 2686 CG LEU A 362 13.382 6.240 21.364 1.00 16.70 6ADH3085
ATOM 2687 CD1 LEU A 362 13.275 7.670 21.891 1.00 16.70 6ADH3086
ATOM 2688 CD2 LEU A 362 11.952 5.814 21.023 1.00 16.70 6ADH3087
ATOM 2689 N ARG A 363 15.241 3.613 20.998 1.00 16.70 6ADH3088
ATOM 2690 CA ARG A 363 15.100 2.441 21.793 1.00 16.70 6ADH3089
ATOM 2691 C ARG A 363 16.283 1.562 21.672 1.00 16.70 6ADH3090
ATOM 2692 O ARG A 363 16.722 .927 22.636 1.00 16.70 6ADH3091
ATOM 2693 CB ARG A 363 13.927 1.638 21.328 1.00 16.70 6ADH3092
ATOM 2694 CG ARG A 363 14.218 .974 19.998 1.00 16.70 6ADH3093
ATOM 2695 CD ARG A 363 13.109 .041 19.561 1.00 16.70 6ADH3094
ATOM 2696 NE ARG A 363 11.991 .737 18.929 1.00 16.70 6ADH3095
ATOM 2697 CZ ARG A 363 11.176 .153 18.050 1.00 16.70 6ADH3096
ATOM 2698 NH1 ARG A 363 11.356 -1.125 17.690 1.00 16.70 6ADH3097
ATOM 2699 NH2 ARG A 363 10.134 .764 17.470 1.00 16.70 6ADH3098
ATOM 2700 N SER A 364 16.824 1.460 20.525 1.00 16.70 6ADH3099
ATOM 2701 CA SER A 364 17.956 .599 20.461 1.00 16.70 6ADH3100
ATOM 2702 C SER A 364 19.114 1.288 21.160 1.00 16.70 6ADH3101
ATOM 2703 O SER A 364 20.268 .849 21.067 1.00 16.70 6ADH3102
ATOM 2704 CB SER A 364 18.279 .176 19.040 0.00 16.70 2 6ADH3103
ATOM 2705 OG SER A 364 18.342 -1.244 18.973 0.00 16.70 2 6ADH3104
ATOM 2706 N GLY A 365 18.829 2.376 21.875 1.00 16.70 6ADH3105
ATOM 2707 CA GLY A 365 19.891 2.982 22.707 1.00 16.70 6ADH3106
ATOM 2708 C GLY A 365 19.885 4.503 22.793 1.00 16.70 6ADH3107
ATOM 2709 O GLY A 365 18.824 5.149 22.797 0.00 16.70 2 6ADH3108
ATOM 2710 N GLU A 366 21.113 4.966 22.877 1.00 16.70 6ADH3109
ATOM 2711 CA GLU A 366 21.441 6.377 22.992 1.00 16.70 6ADH3110
ATOM 2712 C GLU A 366 21.384 7.052 21.612 1.00 16.70 6ADH3111
ATOM 2713 O GLU A 366 21.927 6.523 20.630 1.00 16.70 6ADH3112
ATOM 2714 CB GLU A 366 22.855 6.531 23.565 1.00 16.70 6ADH3113
ATOM 2715 CG GLU A 366 23.322 7.988 23.637 0.00 16.70 2 6ADH3114
ATOM 2716 CD GLU A 366 24.442 8.308 22.645 0.00 16.70 2 6ADH3115
ATOM 2717 OE1 GLU A 366 25.272 9.264 22.894 0.00 16.70 2 6ADH3116
ATOM 2718 OE2 GLU A 366 24.558 7.622 21.559 0.00 16.70 2 6ADH3117
ATOM 2719 N SER A 367 20.702 8.209 21.632 1.00 16.70 6ADH3118
ATOM 2720 CA SER A 367 20.519 9.159 20.474 1.00 16.70 6ADH3119
ATOM 2721 C SER A 367 19.008 9.576 20.398 1.00 16.70 6ADH3120
ATOM 2722 O SER A 367 18.271 9.115 19.512 1.00 16.70 6ADH3121
ATOM 2723 CB SER A 367 21.148 8.585 19.220 0.00 16.70 2 6ADH3122
ATOM 2724 OG SER A 367 22.408 9.209 19.007 0.00 16.70 2 6ADH3123
ATOM 2725 N ILE A 368 18.861 10.445 21.411 1.00 16.70 6ADH3124
ATOM 2726 CA ILE A 368 17.713 11.145 22.111 1.00 16.70 6ADH3125
ATOM 2727 C ILE A 368 16.467 11.713 21.314 1.00 16.70 6ADH3126
ATOM 2728 O ILE A 368 15.323 11.293 21.542 1.00 16.70 6ADH3127
ATOM 2729 CB ILE A 368 18.383 12.215 22.959 1.00 16.70 6ADH3128
ATOM 2730 CG1 ILE A 368 17.912 13.625 22.662 1.00 16.70 6ADH3129
ATOM 2731 CG2 ILE A 368 19.905 12.230 22.791 1.00 16.70 6ADH3130
ATOM 2732 CD1 ILE A 368 17.518 14.385 23.929 1.00 16.70 6ADH3131
ATOM 2733 N ARG A 369 16.597 12.681 20.413 1.00 16.70 6ADH3132
ATOM 2734 CA ARG A 369 15.421 13.131 19.604 1.00 16.70 6ADH3133
ATOM 2735 C ARG A 369 15.829 13.371 18.162 1.00 16.70 6ADH3134
ATOM 2736 O ARG A 369 16.444 14.396 17.843 1.00 16.70 6ADH3135
ATOM 2737 CB ARG A 369 14.777 14.436 20.101 1.00 16.70 6ADH3136
ATOM 2738 CG ARG A 369 13.236 14.437 19.957 1.00 16.70 6ADH3137
ATOM 2739 CD ARG A 369 12.564 14.787 21.288 1.00 16.70 6ADH3138
ATOM 2740 NE ARG A 369 11.143 14.429 21.433 1.00 16.70 6ADH3139
ATOM 2741 CZ ARG A 369 10.685 13.571 22.364 1.00 16.70 6ADH3140
ATOM 2742 NH1 ARG A 369 11.524 12.899 23.165 1.00 16.70 6ADH3141
ATOM 2743 NH2 ARG A 369 9.388 13.371 22.623 1.00 16.70 6ADH3142
ATOM 2744 N THR A 370 15.475 12.384 17.362 1.00 16.70 6ADH3143
ATOM 2745 CA THR A 370 15.639 12.414 15.909 1.00 16.70 6ADH3144
ATOM 2746 C THR A 370 14.473 13.208 15.364 1.00 16.70 6ADH3145
ATOM 2747 O THR A 370 13.452 13.385 16.042 1.00 16.70 6ADH3146
ATOM 2748 CB THR A 370 15.524 10.990 15.342 1.00 16.70 6ADH3147
ATOM 2749 OG1 THR A 370 16.418 10.118 16.015 1.00 16.70 6ADH3148
ATOM 2750 CG2 THR A 370 15.843 10.907 13.847 1.00 16.70 6ADH3149
ATOM 2751 N ILE A 371 14.599 13.687 14.168 1.00 16.70 6ADH3150
ATOM 2752 CA ILE A 371 13.480 14.376 13.541 1.00 16.70 6ADH3151
ATOM 2753 C ILE A 371 13.404 13.993 12.090 1.00 16.70 6ADH3152
ATOM 2754 O ILE A 371 14.187 14.479 11.260 1.00 16.70 6ADH3153
ATOM 2755 CB ILE A 371 13.591 15.892 13.660 1.00 16.70 6ADH3154
ATOM 2756 CG1 ILE A 371 12.886 16.442 14.900 1.00 16.70 6ADH3155
ATOM 2757 CG2 ILE A 371 12.968 16.629 12.473 1.00 16.70 6ADH3156
ATOM 2758 CD1 ILE A 371 13.827 16.623 16.093 1.00 16.70 6ADH3157
ATOM 2759 N LEU A 372 12.461 13.125 11.860 1.00 16.70 6ADH3158
ATOM 2760 CA LEU A 372 12.149 12.648 10.528 1.00 16.70 6ADH3159
ATOM 2761 C LEU A 372 11.585 13.810 9.734 1.00 16.70 6ADH3160
ATOM 2762 O LEU A 372 10.623 14.467 10.158 1.00 16.70 6ADH3161
ATOM 2763 CB LEU A 372 11.049 11.582 10.598 1.00 16.70 6ADH3162
ATOM 2764 CG LEU A 372 11.573 10.155 10.755 1.00 16.70 6ADH3163
ATOM 2765 CD1 LEU A 372 12.882 10.078 11.544 1.00 16.70 6ADH3164
ATOM 2766 CD2 LEU A 372 10.591 9.241 11.492 1.00 16.70 6ADH3165
ATOM 2767 N THR A 373 12.170 14.077 8.595 1.00 16.70 6ADH3166
ATOM 2768 CA THR A 373 11.654 15.149 7.731 1.00 16.70 6ADH3167
ATOM 2769 C THR A 373 10.899 14.516 6.550 1.00 16.70 6ADH3168
ATOM 2770 O THR A 373 11.305 13.468 6.023 1.00 16.70 6ADH3169
ATOM 2771 CB THR A 373 12.788 16.063 7.268 1.00 16.70 6ADH3170
ATOM 2772 OG1 THR A 373 14.015 15.351 7.250 1.00 16.70 6ADH3171
ATOM 2773 CG2 THR A 373 12.978 17.279 8.180 1.00 16.70 6ADH3172
ATOM 2774 N PHE A 374 9.813 15.201 6.176 1.00 16.70 6ADH3173
ATOM 2775 CA PHE A 374 8.860 14.720 5.149 1.00 16.70 6ADH3174
ATOM 2776 C PHE A 374 9.123 15.129 3.729 1.00 16.70 6ADH3175
ATOM 2777 O PHE A 374 8.581 14.506 2.796 1.00 16.70 6ADH3176
ATOM 2778 CB PHE A 374 7.476 15.237 5.379 1.00 16.70 6ADH3177
ATOM 2779 CG PHE A 374 6.829 14.422 6.438 1.00 16.70 6ADH3178
ATOM 2780 CD1 PHE A 374 6.800 14.916 7.728 1.00 16.70 6ADH3179
ATOM 2781 CD2 PHE A 374 6.304 13.174 6.110 1.00 16.70 6ADH3180
ATOM 2782 CE1 PHE A 374 6.228 14.148 8.734 1.00 16.70 6ADH3181
ATOM 2783 CE2 PHE A 374 5.731 12.398 7.112 1.00 16.70 6ADH3182
ATOM 2784 CZ PHE A 374 5.694 12.885 8.428 1.00 16.70 6ADH3183
TER 2786 PHE A 374 6ADH3184
HETATM 2787 ZN ZN A 1 4.858 12.898 23.138 1.00 16.70 6ADH3185
HETATM 2788 ZN ZN A 2 -12.113 21.184 26.866 1.00 16.70 6ADH3186
HETATM 2789 AP NAD A 3 12.938 8.143 26.174 1.00 16.70 6ADH3187
HETATM 2790 AO1 NAD A 3 12.927 6.689 25.926 1.00 16.70 6ADH3188
HETATM 2791 AO2 NAD A 3 13.783 8.793 25.141 1.00 16.70 6ADH3189
HETATM 2792 AO5* NAD A 3 13.525 8.451 27.626 1.00 16.70 6ADH3190
HETATM 2793 AC5* NAD A 3 13.647 7.400 28.616 1.00 16.70 6ADH3191
HETATM 2794 AC4* NAD A 3 14.846 7.728 29.432 1.00 16.70 6ADH3192
HETATM 2795 AO4* NAD A 3 14.843 7.049 30.719 1.00 16.70 6ADH3193
HETATM 2796 AC3* NAD A 3 16.165 7.371 28.781 1.00 16.70 6ADH3194
HETATM 2797 AO3* NAD A 3 17.099 8.449 28.906 1.00 16.70 6ADH3195
HETATM 2798 AC2* NAD A 3 16.527 6.079 29.511 1.00 16.70 6ADH3196
HETATM 2799 AO2* NAD A 3 17.942 5.824 29.492 1.00 16.70 6ADH3197
HETATM 2800 AC1* NAD A 3 16.047 6.360 30.901 1.00 16.70 6ADH3198
HETATM 2801 AN9 NAD A 3 15.863 5.177 31.701 1.00 16.70 6ADH3199
HETATM 2802 AC8 NAD A 3 15.451 3.936 31.330 1.00 16.70 6ADH3200
HETATM 2803 AN7 NAD A 3 15.373 3.099 32.361 1.00 16.70 6ADH3201
HETATM 2804 AC5 NAD A 3 15.758 3.866 33.452 1.00 16.70 6ADH3202
HETATM 2805 AC6 NAD A 3 15.880 3.569 34.816 1.00 16.70 6ADH3203
HETATM 2806 AN6 NAD A 3 15.590 2.385 35.350 1.00 16.70 6ADH3204
HETATM 2807 AN1 NAD A 3 16.327 4.566 35.627 1.00 16.70 6ADH3205
HETATM 2808 AC2 NAD A 3 16.612 5.786 35.081 1.00 16.70 6ADH3206
HETATM 2809 AN3 NAD A 3 16.526 6.161 33.840 1.00 16.70 6ADH3207
HETATM 2810 AC4 NAD A 3 16.087 5.144 33.061 1.00 16.70 6ADH3208
HETATM 2811 O3 NAD A 3 11.522 8.792 26.324 1.00 16.70 6ADH3209
HETATM 2812 NP NAD A 3 10.966 10.337 26.133 1.00 16.70 6ADH3210
HETATM 2813 NO1 NAD A 3 10.590 10.567 24.714 1.00 16.70 6ADH3211
HETATM 2814 NO2 NAD A 3 12.022 11.308 26.513 1.00 16.70 6ADH3212
HETATM 2815 NO5* NAD A 3 9.685 10.356 27.109 1.00 16.70 6ADH3213
HETATM 2816 NC5* NAD A 3 9.852 10.073 28.510 1.00 16.70 6ADH3214
HETATM 2817 NC4* NAD A 3 8.625 9.342 29.031 1.00 16.70 6ADH3215
HETATM 2818 NO4* NAD A 3 7.565 10.288 29.346 1.00 16.70 6ADH3216
HETATM 2819 NC3* NAD A 3 8.009 8.308 28.089 1.00 16.70 6ADH3217
HETATM 2820 NO3* NAD A 3 7.501 7.123 28.720 1.00 16.70 6ADH3218
HETATM 2821 NC2* NAD A 3 6.885 9.140 27.452 1.00 16.70 6ADH3219
HETATM 2822 NO2* NAD A 3 5.880 8.237 26.964 1.00 16.70 6ADH3220
HETATM 2823 NC1* NAD A 3 6.412 9.992 28.597 1.00 16.70 6ADH3221
HETATM 2824 NN1 NAD A 3 5.782 11.257 28.149 1.00 16.70 6ADH3222
HETATM 2825 NC2 NAD A 3 4.674 11.736 28.793 1.00 16.70 6ADH3223
HETATM 2826 NC3 NAD A 3 4.126 12.931 28.398 1.00 16.70 6ADH3224
HETATM 2827 NC7 NAD A 3 2.898 13.573 29.134 1.00 16.70 6ADH3225
HETATM 2828 NO7 NAD A 3 2.098 14.238 28.507 1.00 16.70 6ADH3226
HETATM 2829 NN7 NAD A 3 2.825 13.341 30.459 1.00 16.70 6ADH3227
HETATM 2830 NC4 NAD A 3 4.651 13.695 27.327 1.00 16.70 6ADH3228
HETATM 2831 NC5 NAD A 3 5.767 13.106 26.732 1.00 16.70 6ADH3229
HETATM 2832 NC6 NAD A 3 6.372 11.933 27.072 1.00 16.70 6ADH3230
HETATM 2833 S DMS A 4 1.971 11.798 24.743 1.00 16.70 6ADH3231
HETATM 2834 O DMS A 4 3.375 11.900 24.321 1.00 16.70 6ADH3232
HETATM 2835 C1 DMS A 4 1.129 10.696 23.583 1.00 16.70 6ADH3233
HETATM 2836 C2 DMS A 4 1.927 10.736 26.184 1.00 16.70 6ADH3234
ATOM 2837 N SER B 1 1.485 20.443 95.871 0.00 16.70 2 6ADH3235
ATOM 2838 CA SER B 1 2.400 19.913 94.866 0.00 16.70 2 6ADH3236
ATOM 2839 C SER B 1 3.750 19.901 95.354 0.00 16.70 2 6ADH3237
ATOM 2840 O SER B 1 4.494 18.931 95.153 0.00 16.70 2 6ADH3238
ATOM 2841 CB SER B 1 2.212 20.687 93.555 0.00 16.70 2 6ADH3239
ATOM 2842 OG SER B 1 .905 21.237 93.499 0.00 16.70 2 6ADH3240
ATOM 2843 N THR B 2 4.113 20.937 95.983 0.00 16.70 2 6ADH3241
ATOM 2844 CA THR B 2 5.370 20.819 96.573 0.00 16.70 2 6ADH3242
ATOM 2845 C THR B 2 6.279 20.223 95.457 0.00 16.70 2 6ADH3243
ATOM 2846 O THR B 2 6.631 19.037 95.490 0.00 16.70 2 6ADH3244
ATOM 2847 CB THR B 2 5.083 19.833 97.718 0.00 16.70 2 6ADH3245
ATOM 2848 OG1 THR B 2 3.913 20.236 98.423 0.00 16.70 2 6ADH3246
ATOM 2849 CG2 THR B 2 6.214 19.729 98.737 0.00 16.70 2 6ADH3247
ATOM 2850 N ALA B 3 6.638 21.072 94.472 0.00 16.70 2 6ADH3248
ATOM 2851 CA ALA B 3 7.383 20.635 93.247 0.00 16.70 2 6ADH3249
ATOM 2852 C ALA B 3 8.866 21.016 93.241 1.00 16.70 6ADH3250
ATOM 2853 O ALA B 3 9.221 22.205 93.174 1.00 16.70 6ADH3251
ATOM 2854 CB ALA B 3 6.763 21.261 91.997 0.00 16.70 2 6ADH3252
ATOM 2855 N GLY B 4 9.637 19.944 93.296 1.00 16.70 6ADH3253
ATOM 2856 CA GLY B 4 11.090 19.981 93.296 1.00 16.70 6ADH3254
ATOM 2857 C GLY B 4 11.664 18.602 92.928 1.00 16.70 6ADH3255
ATOM 2858 O GLY B 4 12.741 18.500 92.322 1.00 16.70 6ADH3256
ATOM 2859 N LYS B 5 10.953 17.521 93.284 1.00 16.70 6ADH3257
ATOM 2860 CA LYS B 5 11.503 16.176 93.008 1.00 16.70 6ADH3258
ATOM 2861 C LYS B 5 10.556 14.988 93.333 1.00 16.70 6ADH3259
ATOM 2862 O LYS B 5 10.349 14.636 94.504 1.00 16.70 6ADH3260
ATOM 2863 CB LYS B 5 12.768 15.994 93.831 0.00 16.70 2 6ADH3261
ATOM 2864 CG LYS B 5 13.571 14.768 93.429 0.00 16.70 2 6ADH3262
ATOM 2865 CD LYS B 5 14.000 13.936 94.633 0.00 16.70 2 6ADH3263
ATOM 2866 CE LYS B 5 14.924 12.778 94.259 0.00 16.70 2 6ADH3264
ATOM 2867 NZ LYS B 5 16.288 13.216 93.931 0.00 16.70 2 6ADH3265
ATOM 2868 N VAL B 6 10.075 14.454 92.224 1.00 16.70 6ADH3266
ATOM 2869 CA VAL B 6 9.220 13.262 92.089 1.00 16.70 6ADH3267
ATOM 2870 C VAL B 6 7.950 13.308 92.864 1.00 16.70 6ADH3268
ATOM 2871 O VAL B 6 7.885 13.883 93.963 1.00 16.70 6ADH3269
ATOM 2872 CB VAL B 6 9.935 11.979 92.454 1.00 16.70 6ADH3270
ATOM 2873 CG1 VAL B 6 9.071 10.737 92.218 1.00 16.70 6ADH3271
ATOM 2874 CG2 VAL B 6 11.208 11.769 91.636 1.00 16.70 6ADH3272
ATOM 2875 N ILE B 7 7.092 12.665 92.165 1.00 16.70 6ADH3273
ATOM 2876 CA ILE B 7 5.724 12.595 92.448 1.00 16.70 6ADH3274
ATOM 2877 C ILE B 7 5.216 11.228 92.062 1.00 16.70 6ADH3275
ATOM 2878 O ILE B 7 5.891 10.476 91.341 1.00 16.70 6ADH3276
ATOM 2879 CB ILE B 7 5.087 13.669 91.584 1.00 16.70 6ADH3277
ATOM 2880 CG1 ILE B 7 4.276 14.683 92.374 1.00 16.70 6ADH3278
ATOM 2881 CG2 ILE B 7 4.136 13.106 90.529 1.00 16.70 6ADH3279
ATOM 2882 CD1 ILE B 7 3.573 15.701 91.475 1.00 16.70 6ADH3280
ATOM 2883 N LYS B 8 4.052 10.988 92.568 1.00 16.70 6ADH3281
ATOM 2884 CA LYS B 8 3.325 9.759 92.342 1.00 16.70 6ADH3282
ATOM 2885 C LYS B 8 1.889 10.107 92.054 1.00 16.70 6ADH3283
ATOM 2886 O LYS B 8 1.322 11.026 92.669 1.00 16.70 6ADH3284
ATOM 2887 CB LYS B 8 3.357 8.903 93.601 1.00 16.70 6ADH3285
ATOM 2888 CG LYS B 8 4.557 7.966 93.655 1.00 16.70 6ADH3286
ATOM 2889 CD LYS B 8 4.526 7.044 94.871 1.00 16.70 6ADH3287
ATOM 2890 CE LYS B 8 5.019 5.632 94.562 1.00 16.70 6ADH3288
ATOM 2891 NZ LYS B 8 6.073 5.180 95.481 1.00 16.70 6ADH3289
ATOM 2892 N CYS B 9 1.327 9.383 91.128 1.00 16.70 6ADH3290
ATOM 2893 CA CYS B 9 .006 9.652 90.697 1.00 16.70 6ADH3291
ATOM 2894 C CYS B 9 -.588 8.567 89.862 1.00 16.70 6ADH3292
ATOM 2895 O CYS B 9 .016 7.499 89.674 1.00 16.70 6ADH3293
ATOM 2896 CB CYS B 9 -.425 11.192 90.062 1.00 16.70 6ADH3294
ATOM 2897 SG CYS B 9 .875 11.311 88.638 1.00 16.70 6ADH3295
ATOM 2898 N LYS B 10 -1.756 8.920 89.410 1.00 16.70 6ADH3296
ATOM 2899 CA LYS B 10 -2.561 8.065 88.603 1.00 16.70 6ADH3297
ATOM 2900 C LYS B 10 -2.340 8.371 87.163 1.00 16.70 6ADH3298
ATOM 2901 O LYS B 10 -2.411 9.542 86.753 1.00 16.70 6ADH3299
ATOM 2902 CB LYS B 10 -4.016 8.233 88.968 1.00 16.70 6ADH3300
ATOM 2903 CG LYS B 10 -4.381 7.394 90.180 1.00 16.70 6ADH3301
ATOM 2904 CD LYS B 10 -5.872 7.143 90.293 1.00 16.70 6ADH3302
ATOM 2905 CE LYS B 10 -6.432 7.588 91.636 1.00 16.70 6ADH3303
ATOM 2906 NZ LYS B 10 -6.865 8.984 91.653 1.00 16.70 6ADH3304
ATOM 2907 N ALA B 11 -2.084 7.243 86.570 1.00 16.70 6ADH3305
ATOM 2908 CA ALA B 11 -1.833 7.067 85.179 1.00 16.70 6ADH3306
ATOM 2909 C ALA B 11 -2.580 5.838 84.720 1.00 16.70 6ADH3307
ATOM 2910 O ALA B 11 -2.706 4.860 85.476 0.00 16.70 2 6ADH3308
ATOM 2911 CB ALA B 11 -.335 6.875 84.934 1.00 16.70 6ADH3309
ATOM 2912 N ALA B 12 -3.018 6.017 83.501 1.00 16.70 6ADH3310
ATOM 2913 CA ALA B 12 -3.723 5.025 82.715 1.00 16.70 6ADH3311
ATOM 2914 C ALA B 12 -2.707 4.351 81.787 1.00 16.70 6ADH3312
ATOM 2915 O ALA B 12 -2.508 4.777 80.639 1.00 16.70 6ADH3313
ATOM 2916 CB ALA B 12 -4.800 5.716 81.874 1.00 16.70 6ADH3314
ATOM 2917 N VAL B 13 -2.061 3.307 82.285 1.00 16.70 6ADH3315
ATOM 2918 CA VAL B 13 -1.055 2.577 81.483 1.00 16.70 6ADH3316
ATOM 2919 C VAL B 13 -1.754 1.519 80.607 1.00 16.70 6ADH3317
ATOM 2920 O VAL B 13 -2.911 1.148 80.859 1.00 16.70 6ADH3318
ATOM 2921 CB VAL B 13 .001 1.915 82.379 1.00 16.70 6ADH3319
ATOM 2922 CG1 VAL B 13 .949 .996 81.604 1.00 16.70 6ADH3320
ATOM 2923 CG2 VAL B 13 .905 2.925 83.093 1.00 16.70 6ADH3321
ATOM 2924 N LEU B 14 -1.002 1.091 79.605 1.00 16.70 6ADH3322
ATOM 2925 CA LEU B 14 -1.431 .120 78.574 1.00 16.70 6ADH3323
ATOM 2926 C LEU B 14 -.266 -.852 78.375 1.00 16.70 6ADH3324
ATOM 2927 O LEU B 14 .503 -.753 77.404 0.00 16.70 2 6ADH3325
ATOM 2928 CB LEU B 14 -1.795 .940 77.322 1.00 16.70 6ADH3326
ATOM 2929 CG LEU B 14 -2.381 .139 76.156 1.00 16.70 6ADH3327
ATOM 2930 CD1 LEU B 14 -1.315 -.324 75.162 1.00 16.70 6ADH3328
ATOM 2931 CD2 LEU B 14 -3.118 -1.128 76.594 1.00 16.70 6ADH3329
ATOM 2932 N TRP B 15 -.220 -1.728 79.333 1.00 16.70 6ADH3330
ATOM 2933 CA TRP B 15 .841 -2.705 79.511 1.00 16.70 6ADH3331
ATOM 2934 C TRP B 15 .972 -3.654 78.321 1.00 16.70 6ADH3332
ATOM 2935 O TRP B 15 2.063 -4.175 78.041 1.00 16.70 6ADH3333
ATOM 2936 CB TRP B 15 .533 -3.490 80.788 1.00 16.70 6ADH3334
ATOM 2937 CG TRP B 15 .853 -2.678 82.048 1.00 16.70 6ADH3335
ATOM 2938 CD1 TRP B 15 .011 -1.937 82.795 1.00 16.70 6ADH3336
ATOM 2939 CD2 TRP B 15 2.134 -2.586 82.624 1.00 16.70 6ADH3337
ATOM 2940 NE1 TRP B 15 .787 -1.367 83.861 1.00 16.70 6ADH3338
ATOM 2941 CE2 TRP B 15 2.032 -1.764 83.737 1.00 16.70 6ADH3339
ATOM 2942 CE3 TRP B 15 3.369 -3.139 82.282 1.00 16.70 6ADH3340
ATOM 2943 CZ2 TRP B 15 3.130 -1.454 84.551 1.00 16.70 6ADH3341
ATOM 2944 CZ3 TRP B 15 4.465 -2.822 83.106 1.00 16.70 6ADH3342
ATOM 2945 CH2 TRP B 15 4.352 -2.018 84.187 1.00 16.70 6ADH3343
ATOM 2946 N GLU B 16 -.134 -3.840 77.644 1.00 16.70 6ADH3344
ATOM 2947 CA GLU B 16 -.228 -4.821 76.570 1.00 16.70 6ADH3345
ATOM 2948 C GLU B 16 -1.237 -4.382 75.504 1.00 16.70 6ADH3346
ATOM 2949 O GLU B 16 -2.296 -3.822 75.830 1.00 16.70 6ADH3347
ATOM 2950 CB GLU B 16 -.731 -6.122 77.202 1.00 16.70 6ADH3348
ATOM 2951 CG GLU B 16 -.155 -7.402 76.615 1.00 16.70 6ADH3349
ATOM 2952 CD GLU B 16 -.972 -8.626 77.038 1.00 16.70 6ADH3350
ATOM 2953 OE1 GLU B 16 -1.117 -9.618 76.225 0.00 16.70 2 6ADH3351
ATOM 2954 OE2 GLU B 16 -1.518 -8.664 78.206 0.00 16.70 2 6ADH3352
ATOM 2955 N GLU B 17 -.823 -4.673 74.278 1.00 16.70 6ADH3353
ATOM 2956 CA GLU B 17 -1.616 -4.480 73.061 1.00 16.70 6ADH3354
ATOM 2957 C GLU B 17 -2.865 -5.351 73.176 1.00 16.70 6ADH3355
ATOM 2958 O GLU B 17 -2.771 -6.578 73.327 1.00 16.70 6ADH3356
ATOM 2959 CB GLU B 17 -.803 -5.013 71.866 0.00 16.70 2 6ADH3357
ATOM 2960 CG GLU B 17 -.869 -4.162 70.600 0.00 16.70 2 6ADH3358
ATOM 2961 CD GLU B 17 .279 -4.473 69.631 0.00 16.70 2 6ADH3359
ATOM 2962 OE1 GLU B 17 .801 -3.529 68.924 0.00 16.70 2 6ADH3360
ATOM 2963 OE2 GLU B 17 .724 -5.680 69.522 0.00 16.70 2 6ADH3361
ATOM 2964 N LYS B 18 -4.029 -4.738 73.122 1.00 16.70 6ADH3362
ATOM 2965 CA LYS B 18 -5.283 -5.510 73.140 1.00 16.70 6ADH3363
ATOM 2966 C LYS B 18 -6.059 -5.404 74.466 1.00 16.70 6ADH3364
ATOM 2967 O LYS B 18 -7.279 -5.617 74.510 1.00 16.70 6ADH3365
ATOM 2968 CB LYS B 18 -4.970 -6.994 72.933 0.00 16.70 2 6ADH3366
ATOM 2969 CG LYS B 18 -5.992 -7.704 72.045 0.00 16.70 2 6ADH3367
ATOM 2970 CD LYS B 18 -6.893 -8.665 72.820 0.00 16.70 2 6ADH3368
ATOM 2971 CE LYS B 18 -8.012 -9.256 71.963 0.00 16.70 2 6ADH3369
ATOM 2972 NZ LYS B 18 -8.377 -10.625 72.356 0.00 16.70 2 6ADH3370
ATOM 2973 N LYS B 19 -5.366 -5.082 75.542 1.00 16.70 6ADH3371
ATOM 2974 CA LYS B 19 -6.000 -5.020 76.880 1.00 16.70 6ADH3372
ATOM 2975 C LYS B 19 -6.316 -3.591 77.308 1.00 16.70 6ADH3373
ATOM 2976 O LYS B 19 -5.680 -2.631 76.849 1.00 16.70 6ADH3374
ATOM 2977 CB LYS B 19 -5.074 -5.603 77.940 1.00 16.70 6ADH3375
ATOM 2978 CG LYS B 19 -4.032 -6.550 77.356 1.00 16.70 6ADH3376
ATOM 2979 CD LYS B 19 -4.641 -7.595 76.421 1.00 16.70 6ADH3377
ATOM 2980 CE LYS B 19 -4.125 -9.009 76.694 1.00 16.70 6ADH3378
ATOM 2981 NZ LYS B 19 -5.196 -9.952 77.046 1.00 16.70 6ADH3379
ATOM 2982 N PRO B 20 -7.307 -3.397 78.193 1.00 16.70 6ADH3380
ATOM 2983 CA PRO B 20 -7.663 -2.072 78.676 1.00 16.70 6ADH3381
ATOM 2984 C PRO B 20 -6.512 -1.390 79.391 1.00 16.70 6ADH3382
ATOM 2985 O PRO B 20 -5.475 -2.066 79.682 1.00 16.70 6ADH3383
ATOM 2986 CB PRO B 20 -8.828 -2.321 79.606 1.00 16.70 6ADH3384
ATOM 2987 CG PRO B 20 -9.104 -3.817 79.622 1.00 16.70 6ADH3385
ATOM 2988 CD PRO B 20 -8.121 -4.497 78.721 1.00 16.70 6ADH3386
ATOM 2989 N PHE B 21 -6.758 -.104 79.631 1.00 16.70 6ADH3387
ATOM 2990 CA PHE B 21 -5.833 .821 80.313 1.00 16.70 6ADH3388
ATOM 2991 C PHE B 21 -5.945 .620 81.863 1.00 16.70 6ADH3389
ATOM 2992 O PHE B 21 -7.033 .734 82.446 1.00 16.70 6ADH3390
ATOM 2993 CB PHE B 21 -6.213 2.296 79.935 1.00 16.70 6ADH3391
ATOM 2994 CG PHE B 21 -5.991 2.702 78.436 1.00 16.70 6ADH3392
ATOM 2995 CD1 PHE B 21 -6.970 2.436 77.452 1.00 16.70 6ADH3393
ATOM 2996 CD2 PHE B 21 -4.812 3.364 78.040 1.00 16.70 6ADH3394
ATOM 2997 CE1 PHE B 21 -6.761 2.807 76.108 1.00 16.70 6ADH3395
ATOM 2998 CE2 PHE B 21 -4.609 3.733 76.695 1.00 16.70 6ADH3396
ATOM 2999 CZ PHE B 21 -5.581 3.453 75.731 1.00 16.70 6ADH3397
ATOM 3000 N SER B 22 -4.814 .308 82.512 1.00 16.70 6ADH3398
ATOM 3001 CA SER B 22 -4.756 .187 83.986 1.00 16.70 6ADH3399
ATOM 3002 C SER B 22 -4.197 1.441 84.595 1.00 16.70 6ADH3400
ATOM 3003 O SER B 22 -3.034 1.798 84.346 0.00 16.70 2 6ADH3401
ATOM 3004 CB SER B 22 -3.802 -.909 84.474 1.00 16.70 6ADH3402
ATOM 3005 OG SER B 22 -4.073 -2.133 83.816 1.00 16.70 6ADH3403
ATOM 3006 N ILE B 23 -5.098 1.998 85.341 1.00 16.70 6ADH3404
ATOM 3007 CA ILE B 23 -4.877 3.152 86.136 1.00 16.70 6ADH3405
ATOM 3008 C ILE B 23 -4.222 2.635 87.401 1.00 16.70 6ADH3406
ATOM 3009 O ILE B 23 -4.903 2.305 88.378 1.00 16.70 6ADH3407
ATOM 3010 CB ILE B 23 -6.221 3.855 86.322 1.00 16.70 6ADH3408
ATOM 3011 CG1 ILE B 23 -7.192 3.523 85.184 1.00 16.70 6ADH3409
ATOM 3012 CG2 ILE B 23 -6.111 5.383 86.362 1.00 16.70 6ADH3410
ATOM 3013 CD1 ILE B 23 -8.446 4.398 85.185 1.00 16.70 6ADH3411
ATOM 3014 N GLU B 24 -2.944 2.586 87.198 1.00 16.70 6ADH3412
ATOM 3015 CA GLU B 24 -1.919 2.278 88.149 1.00 16.70 6ADH3413
ATOM 3016 C GLU B 24 -1.557 3.580 88.807 1.00 16.70 6ADH3414
ATOM 3017 O GLU B 24 -1.924 4.655 88.308 1.00 16.70 6ADH3415
ATOM 3018 CB GLU B 24 -.657 1.914 87.340 1.00 16.70 6ADH3416
ATOM 3019 CG GLU B 24 .067 .668 87.806 1.00 16.70 6ADH3417
ATOM 3020 CD GLU B 24 -.734 -.594 87.539 1.00 16.70 6ADH3418
ATOM 3021 OE1 GLU B 24 -1.336 -1.184 88.513 1.00 16.70 6ADH3419
ATOM 3022 OE2 GLU B 24 -.809 -1.069 86.342 1.00 16.70 6ADH3420
ATOM 3023 N GLU B 25 -.867 3.467 89.908 1.00 16.70 6ADH3421
ATOM 3024 CA GLU B 25 -.193 4.621 90.457 1.00 16.70 6ADH3422
ATOM 3025 C GLU B 25 1.120 4.579 89.698 1.00 16.70 6ADH3423
ATOM 3026 O GLU B 25 1.629 3.497 89.367 1.00 16.70 6ADH3424
ATOM 3027 CB GLU B 25 -.023 4.541 91.987 1.00 16.70 6ADH3425
ATOM 3028 CG GLU B 25 .743 5.755 92.558 0.00 16.70 2 6ADH3426
ATOM 3029 CD GLU B 25 .503 6.008 94.055 0.00 16.70 2 6ADH3427
ATOM 3030 OE1 GLU B 25 .745 5.078 94.916 0.00 16.70 2 6ADH3428
ATOM 3031 OE2 GLU B 25 .059 7.152 94.455 0.00 16.70 2 6ADH3429
ATOM 3032 N VAL B 26 1.621 5.723 89.426 1.00 16.70 6ADH3430
ATOM 3033 CA VAL B 26 2.809 5.863 88.619 1.00 16.70 6ADH3431
ATOM 3034 C VAL B 26 3.588 7.023 89.204 1.00 16.70 6ADH3432
ATOM 3035 O VAL B 26 3.013 8.054 89.578 1.00 16.70 6ADH3433
ATOM 3036 CB VAL B 26 2.323 6.123 87.186 1.00 16.70 6ADH3434
ATOM 3037 CG1 VAL B 26 3.084 7.245 86.480 1.00 16.70 6ADH3435
ATOM 3038 CG2 VAL B 26 2.447 4.900 86.276 1.00 16.70 6ADH3436
ATOM 3039 N GLU B 27 4.879 6.885 89.300 1.00 16.70 6ADH3437
ATOM 3040 CA GLU B 27 5.678 7.957 89.896 1.00 16.70 6ADH3438
ATOM 3041 C GLU B 27 6.565 8.606 88.808 1.00 16.70 6ADH3439
ATOM 3042 O GLU B 27 7.485 7.966 88.274 1.00 16.70 6ADH3440
ATOM 3043 CB GLU B 27 6.375 7.379 91.122 1.00 16.70 6ADH3441
ATOM 3044 CG GLU B 27 7.815 7.809 91.298 1.00 16.70 6ADH3442
ATOM 3045 CD GLU B 27 8.658 6.681 91.883 1.00 16.70 6ADH3443
ATOM 3046 OE1 GLU B 27 8.742 5.555 91.261 1.00 16.70 6ADH3444
ATOM 3047 OE2 GLU B 27 9.282 6.853 92.999 1.00 16.70 6ADH3445
ATOM 3048 N VAL B 28 6.165 9.876 88.594 1.00 16.70 6ADH3446
ATOM 3049 CA VAL B 28 6.663 10.846 87.568 1.00 16.70 6ADH3447
ATOM 3050 C VAL B 28 7.712 11.845 88.145 1.00 16.70 6ADH3448
ATOM 3051 O VAL B 28 7.408 12.658 89.029 1.00 16.70 6ADH3449
ATOM 3052 CB VAL B 28 5.450 11.661 87.111 1.00 16.70 6ADH3450
ATOM 3053 CG1 VAL B 28 5.815 12.797 86.157 1.00 16.70 6ADH3451
ATOM 3054 CG2 VAL B 28 4.406 10.816 86.379 1.00 16.70 6ADH3452
ATOM 3055 N ALA B 29 8.937 11.800 87.614 1.00 16.70 6ADH3453
ATOM 3056 CA ALA B 29 10.062 12.605 88.147 1.00 16.70 6ADH3454
ATOM 3057 C ALA B 29 10.109 14.040 87.636 1.00 16.70 6ADH3455
ATOM 3058 O ALA B 29 9.406 14.402 86.678 1.00 16.70 6ADH3456
ATOM 3059 CB ALA B 29 11.405 11.974 87.788 1.00 16.70 6ADH3457
ATOM 3060 N PRO B 30 10.949 14.822 88.312 1.00 16.70 6ADH3458
ATOM 3061 CA PRO B 30 11.107 16.246 88.059 1.00 16.70 6ADH3459
ATOM 3062 C PRO B 30 11.605 16.584 86.671 1.00 16.70 6ADH3460
ATOM 3063 O PRO B 30 12.366 15.762 86.070 1.00 16.70 6ADH3461
ATOM 3064 CB PRO B 30 12.110 16.692 89.098 1.00 16.70 6ADH3462
ATOM 3065 CG PRO B 30 12.510 15.477 89.920 1.00 16.70 6ADH3463
ATOM 3066 CD PRO B 30 11.783 14.285 89.395 1.00 16.70 6ADH3464
ATOM 3067 N PRO B 31 11.198 17.773 86.151 1.00 16.70 6ADH3465
ATOM 3068 CA PRO B 31 11.644 18.266 84.844 1.00 16.70 6ADH3466
ATOM 3069 C PRO B 31 13.147 18.429 84.851 1.00 16.70 6ADH3467
ATOM 3070 O PRO B 31 13.716 18.941 85.859 1.00 16.70 6ADH3468
ATOM 3071 CB PRO B 31 10.933 19.595 84.700 1.00 16.70 6ADH3469
ATOM 3072 CG PRO B 31 10.087 19.818 85.945 1.00 16.70 6ADH3470
ATOM 3073 CD PRO B 31 10.270 18.659 86.870 1.00 16.70 6ADH3471
ATOM 3074 N LYS B 32 13.787 18.027 83.780 1.00 16.70 6ADH3472
ATOM 3075 CA LYS B 32 15.247 18.083 83.706 1.00 16.70 6ADH3473
ATOM 3076 C LYS B 32 15.737 19.366 83.100 1.00 16.70 6ADH3474
ATOM 3077 O LYS B 32 15.049 20.397 83.136 0.00 16.70 2 6ADH3475
ATOM 3078 CB LYS B 32 15.776 16.964 82.823 1.00 16.70 6ADH3476
ATOM 3079 CG LYS B 32 16.143 15.719 83.618 1.00 16.70 6ADH3477
ATOM 3080 CD LYS B 32 16.688 14.597 82.741 1.00 16.70 6ADH3478
ATOM 3081 CE LYS B 32 17.879 13.878 83.370 1.00 16.70 6ADH3479
ATOM 3082 NZ LYS B 32 17.950 12.457 83.001 1.00 16.70 6ADH3480
ATOM 3083 N ALA B 33 16.910 19.207 82.572 1.00 16.70 6ADH3481
ATOM 3084 CA ALA B 33 17.610 20.269 81.909 1.00 16.70 6ADH3482
ATOM 3085 C ALA B 33 16.823 20.750 80.684 1.00 16.70 6ADH3483
ATOM 3086 O ALA B 33 17.197 20.470 79.539 0.00 16.70 2 6ADH3484
ATOM 3087 CB ALA B 33 18.981 19.775 81.439 0.00 16.70 2 6ADH3485
ATOM 3088 N HIS B 34 15.716 21.461 80.929 1.00 16.70 6ADH3486
ATOM 3089 CA HIS B 34 14.984 22.152 79.833 1.00 16.70 6ADH3487
ATOM 3090 C HIS B 34 13.450 21.945 79.785 1.00 16.70 6ADH3488
ATOM 3091 O HIS B 34 12.702 22.843 79.372 1.00 16.70 6ADH3489
ATOM 3092 CB HIS B 34 15.572 21.772 78.484 1.00 16.70 6ADH3490
ATOM 3093 CG HIS B 34 16.419 22.922 77.949 1.00 16.70 6ADH3491
ATOM 3094 ND1 HIS B 34 17.770 23.041 78.252 1.00 16.70 6ADH3492
ATOM 3095 CD2 HIS B 34 16.106 23.990 77.171 1.00 16.70 6ADH3493
ATOM 3096 CE1 HIS B 34 18.225 24.137 77.672 1.00 16.70 6ADH3494
ATOM 3097 NE2 HIS B 34 17.244 24.714 77.024 1.00 16.70 6ADH3495
ATOM 3098 N GLU B 35 12.981 20.794 80.206 1.00 16.70 6ADH3496
ATOM 3099 CA GLU B 35 11.536 20.441 80.149 1.00 16.70 6ADH3497
ATOM 3100 C GLU B 35 10.669 21.247 81.168 1.00 16.70 6ADH3498
ATOM 3101 O GLU B 35 11.193 22.063 81.943 1.00 16.70 6ADH3499
ATOM 3102 CB GLU B 35 11.391 18.940 80.450 1.00 16.70 6ADH3500
ATOM 3103 CG GLU B 35 12.313 18.062 79.582 1.00 16.70 6ADH3501
ATOM 3104 CD GLU B 35 13.148 17.051 80.383 1.00 16.70 6ADH3502
ATOM 3105 OE1 GLU B 35 12.862 16.808 81.617 1.00 16.70 6ADH3503
ATOM 3106 OE2 GLU B 35 14.138 16.441 79.821 1.00 16.70 6ADH3504
ATOM 3107 N VAL B 36 9.346 20.954 81.088 1.00 16.70 6ADH3505
ATOM 3108 CA VAL B 36 8.274 21.494 81.985 1.00 16.70 6ADH3506
ATOM 3109 C VAL B 36 7.292 20.353 82.379 1.00 16.70 6ADH3507
ATOM 3110 O VAL B 36 6.924 19.516 81.540 1.00 16.70 6ADH3508
ATOM 3111 CB VAL B 36 7.462 22.622 81.306 1.00 16.70 6ADH3509
ATOM 3112 CG1 VAL B 36 8.113 23.155 80.029 1.00 16.70 6ADH3510
ATOM 3113 CG2 VAL B 36 6.052 22.188 80.896 1.00 16.70 6ADH3511
ATOM 3114 N ARG B 37 6.930 20.388 83.669 1.00 16.70 6ADH3512
ATOM 3115 CA ARG B 37 5.978 19.459 84.311 1.00 16.70 6ADH3513
ATOM 3116 C ARG B 37 4.621 20.118 84.354 1.00 16.70 6ADH3514
ATOM 3117 O ARG B 37 4.498 21.306 84.680 1.00 16.70 6ADH3515
ATOM 3118 CB ARG B 37 6.403 19.156 85.734 1.00 16.70 6ADH3516
ATOM 3119 CG ARG B 37 6.588 17.668 85.945 1.00 16.70 6ADH3517
ATOM 3120 CD ARG B 37 5.815 17.123 87.130 1.00 16.70 6ADH3518
ATOM 3121 NE ARG B 37 6.666 16.282 87.958 1.00 16.70 6ADH3519
ATOM 3122 CZ ARG B 37 7.506 16.768 88.871 1.00 16.70 6ADH3520
ATOM 3123 NH1 ARG B 37 7.586 18.086 89.102 1.00 16.70 6ADH3521
ATOM 3124 NH2 ARG B 37 8.336 16.011 89.598 1.00 16.70 6ADH3522
ATOM 3125 N ILE B 38 3.650 19.340 84.043 1.00 16.70 6ADH3523
ATOM 3126 CA ILE B 38 2.304 19.822 83.893 1.00 16.70 6ADH3524
ATOM 3127 C ILE B 38 1.361 18.880 84.692 1.00 16.70 6ADH3525
ATOM 3128 O ILE B 38 1.595 17.668 84.765 1.00 16.70 6ADH3526
ATOM 3129 CB ILE B 38 2.092 19.830 82.353 1.00 16.70 6ADH3527
ATOM 3130 CG1 ILE B 38 3.223 20.573 81.611 1.00 16.70 6ADH3528
ATOM 3131 CG2 ILE B 38 .792 20.499 81.906 1.00 16.70 6ADH3529
ATOM 3132 CD1 ILE B 38 2.972 20.726 80.109 1.00 16.70 6ADH3530
ATOM 3133 N LYS B 39 .332 19.462 85.329 1.00 16.70 6ADH3531
ATOM 3134 CA LYS B 39 -.796 18.695 85.941 1.00 16.70 6ADH3532
ATOM 3135 C LYS B 39 -1.909 18.913 84.959 1.00 16.70 6ADH3533
ATOM 3136 O LYS B 39 -2.112 20.031 84.468 1.00 16.70 6ADH3534
ATOM 3137 CB LYS B 39 -1.130 19.187 87.381 1.00 16.70 6ADH3535
ATOM 3138 CG LYS B 39 -2.566 19.696 87.627 1.00 16.70 6ADH3536
ATOM 3139 CD LYS B 39 -2.715 20.431 88.984 1.00 16.70 6ADH3537
ATOM 3140 CE LYS B 39 -3.080 19.508 90.160 1.00 16.70 6ADH3538
ATOM 3141 NZ LYS B 39 -3.225 20.226 91.438 1.00 16.70 6ADH3539
ATOM 3142 N MET B 40 -2.591 17.860 84.662 1.00 16.70 6ADH3540
ATOM 3143 CA MET B 40 -3.596 17.886 83.614 1.00 16.70 6ADH3541
ATOM 3144 C MET B 40 -4.947 18.340 84.090 1.00 16.70 6ADH3542
ATOM 3145 O MET B 40 -5.440 17.889 85.135 1.00 16.70 6ADH3543
ATOM 3146 CB MET B 40 -3.802 16.483 83.056 1.00 16.70 6ADH3544
ATOM 3147 CG MET B 40 -3.808 16.446 81.530 1.00 16.70 6ADH3545
ATOM 3148 SD MET B 40 -2.171 16.371 80.836 1.00 16.70 6ADH3546
ATOM 3149 CE MET B 40 -1.673 17.986 80.279 1.00 16.70 6ADH3547
ATOM 3150 N VAL B 41 -5.498 19.218 83.289 1.00 16.70 6ADH3548
ATOM 3151 CA VAL B 41 -6.864 19.651 83.471 1.00 16.70 6ADH3549
ATOM 3152 C VAL B 41 -7.740 18.618 82.654 1.00 16.70 6ADH3550
ATOM 3153 O VAL B 41 -8.312 17.685 83.228 1.00 16.70 6ADH3551
ATOM 3154 CB VAL B 41 -6.984 21.147 83.133 1.00 16.70 6ADH3552
ATOM 3155 CG1 VAL B 41 -8.103 21.847 83.911 1.00 16.70 6ADH3553
ATOM 3156 CG2 VAL B 41 -5.712 21.937 83.458 1.00 16.70 6ADH3554
ATOM 3157 N ALA B 42 -7.842 18.720 81.288 1.00 16.70 6ADH3555
ATOM 3158 CA ALA B 42 -8.673 17.739 80.438 1.00 16.70 6ADH3556
ATOM 3159 C ALA B 42 -7.823 16.983 79.319 1.00 16.70 6ADH3557
ATOM 3160 O ALA B 42 -6.634 17.264 79.126 1.00 16.70 6ADH3558
ATOM 3161 CB ALA B 42 -9.813 18.485 79.738 1.00 16.70 6ADH3559
ATOM 3162 N THR B 43 -8.503 16.016 78.611 1.00 16.70 6ADH3560
ATOM 3163 CA THR B 43 -7.950 15.132 77.496 1.00 16.70 6ADH3561
ATOM 3164 C THR B 43 -9.078 14.539 76.661 1.00 16.70 6ADH3562
ATOM 3165 O THR B 43 -10.148 14.199 77.184 1.00 16.70 6ADH3563
ATOM 3166 CB THR B 43 -7.310 13.842 78.030 1.00 16.70 6ADH3564
ATOM 3167 OG1 THR B 43 -7.559 13.718 79.420 1.00 16.70 6ADH3565
ATOM 3168 CG2 THR B 43 -5.796 13.774 77.823 1.00 16.70 6ADH3566
ATOM 3169 N GLY B 44 -8.843 14.403 75.392 1.00 16.70 6ADH3567
ATOM 3170 CA GLY B 44 -9.821 13.776 74.512 1.00 16.70 6ADH3568
ATOM 3171 C GLY B 44 -9.257 12.448 74.039 1.00 16.70 6ADH3569
ATOM 3172 O GLY B 44 -8.038 12.225 74.063 1.00 16.70 6ADH3570
ATOM 3173 N ILE B 45 -10.152 11.590 73.630 1.00 16.70 6ADH3571
ATOM 3174 CA ILE B 45 -9.775 10.284 73.102 1.00 16.70 6ADH3572
ATOM 3175 C ILE B 45 -9.846 10.323 71.593 1.00 16.70 6ADH3573
ATOM 3176 O ILE B 45 -10.930 10.218 70.997 1.00 16.70 6ADH3574
ATOM 3177 CB ILE B 45 -10.744 9.201 73.577 1.00 16.70 6ADH3575
ATOM 3178 CG1 ILE B 45 -11.395 9.524 74.921 1.00 16.70 6ADH3576
ATOM 3179 CG2 ILE B 45 -10.075 7.837 73.759 1.00 16.70 6ADH3577
ATOM 3180 CD1 ILE B 45 -10.842 8.678 76.070 1.00 16.70 6ADH3578
ATOM 3181 N CYS B 46 -8.723 10.480 70.982 1.00 16.70 6ADH3579
ATOM 3182 CA CYS B 46 -8.439 10.693 69.514 1.00 16.70 6ADH3580
ATOM 3183 C CYS B 46 -8.268 9.054 69.144 1.00 16.70 6ADH3581
ATOM 3184 O CYS B 46 -7.595 8.337 69.902 0.00 16.70 2 6ADH3582
ATOM 3185 CB CYS B 46 -8.375 11.548 68.238 1.00 16.70 6ADH3583
ATOM 3186 SG CYS B 46 -6.725 11.647 67.481 1.00 16.70 6ADH3584
ATOM 3187 N ARG B 47 -8.715 8.669 67.980 1.00 16.70 6ADH3585
ATOM 3188 CA ARG B 47 -8.544 7.302 67.476 1.00 16.70 6ADH3586
ATOM 3189 C ARG B 47 -7.105 6.815 67.512 1.00 16.70 6ADH3587
ATOM 3190 O ARG B 47 -6.840 5.624 67.730 0.00 16.70 2 6ADH3588
ATOM 3191 CB ARG B 47 -9.000 7.207 66.021 1.00 16.70 6ADH3589
ATOM 3192 CG ARG B 47 -9.414 5.790 65.622 1.00 16.70 6ADH3590
ATOM 3193 CD ARG B 47 -10.805 5.419 66.135 1.00 16.70 6ADH3591
ATOM 3194 NE ARG B 47 -11.038 3.970 66.181 1.00 16.70 6ADH3592
ATOM 3195 CZ ARG B 47 -12.256 3.415 66.167 1.00 16.70 6ADH3593
ATOM 3196 NH1 ARG B 47 -13.360 4.173 66.107 1.00 16.70 6ADH3594
ATOM 3197 NH2 ARG B 47 -12.478 2.094 66.209 1.00 16.70 6ADH3595
ATOM 3198 N SER B 48 -6.215 7.754 67.284 1.00 16.70 6ADH3596
ATOM 3199 CA SER B 48 -4.777 7.478 67.259 1.00 16.70 6ADH3597
ATOM 3200 C SER B 48 -4.342 6.955 68.622 1.00 16.70 6ADH3598
ATOM 3201 O SER B 48 -3.353 6.216 68.737 1.00 16.70 6ADH3599
ATOM 3202 CB SER B 48 -4.015 8.744 66.884 1.00 16.70 6ADH3600
ATOM 3203 OG SER B 48 -4.077 8.943 65.479 1.00 16.70 6ADH3601
ATOM 3204 N ASP B 49 -5.099 7.353 69.622 1.00 16.70 6ADH3602
ATOM 3205 CA ASP B 49 -4.892 6.877 70.990 1.00 16.70 6ADH3603
ATOM 3206 C ASP B 49 -5.355 5.385 71.069 1.00 16.70 6ADH3604
ATOM 3207 O ASP B 49 -4.973 4.649 71.989 1.00 16.70 6ADH3605
ATOM 3208 CB ASP B 49 -5.751 7.707 71.988 1.00 16.70 6ADH3606
ATOM 3209 CG ASP B 49 -5.221 9.123 72.297 1.00 16.70 6ADH3607
ATOM 3210 OD1 ASP B 49 -5.945 10.159 72.031 1.00 16.70 6ADH3608
ATOM 3211 OD2 ASP B 49 -4.054 9.279 72.827 1.00 16.70 6ADH3609
ATOM 3212 N ASP B 50 -6.176 5.001 70.067 1.00 16.70 6ADH3610
ATOM 3213 CA ASP B 50 -6.862 3.661 69.949 1.00 16.70 6ADH3611
ATOM 3214 C ASP B 50 -6.038 2.657 69.125 1.00 16.70 6ADH3612
ATOM 3215 O ASP B 50 -6.097 1.439 69.363 0.00 16.70 2 6ADH3613
ATOM 3216 CB ASP B 50 -8.202 3.876 69.238 1.00 16.70 6ADH3614
ATOM 3217 CG ASP B 50 -9.167 2.703 69.368 1.00 16.70 6ADH3615
ATOM 3218 OD1 ASP B 50 -10.283 2.715 68.724 1.00 16.70 6ADH3616
ATOM 3219 OD2 ASP B 50 -8.865 1.700 70.122 1.00 16.70 6ADH3617
ATOM 3220 N HIS B 51 -5.323 3.273 68.206 1.00 16.70 6ADH3618
ATOM 3221 CA HIS B 51 -4.402 2.621 67.284 1.00 16.70 6ADH3619
ATOM 3222 C HIS B 51 -3.268 1.961 68.065 1.00 16.70 6ADH3620
ATOM 3223 O HIS B 51 -2.909 .800 67.817 1.00 16.70 6ADH3621
ATOM 3224 CB HIS B 51 -3.798 3.663 66.349 1.00 16.70 6ADH3622
ATOM 3225 CG HIS B 51 -4.750 4.107 65.240 1.00 16.70 6ADH3623
ATOM 3226 ND1 HIS B 51 -5.815 3.315 64.821 1.00 16.70 6ADH3624
ATOM 3227 CD2 HIS B 51 -4.790 5.234 64.483 1.00 16.70 6ADH3625
ATOM 3228 CE1 HIS B 51 -6.446 3.957 63.854 1.00 16.70 6ADH3626
ATOM 3229 NE2 HIS B 51 -5.848 5.103 63.641 1.00 16.70 6ADH3627
ATOM 3230 N VAL B 52 -2.694 2.699 69.005 1.00 16.70 6ADH3628
ATOM 3231 CA VAL B 52 -1.629 2.119 69.830 1.00 16.70 6ADH3629
ATOM 3232 C VAL B 52 -2.131 .828 70.460 1.00 16.70 6ADH3630
ATOM 3233 O VAL B 52 -1.371 -.125 70.666 1.00 16.70 6ADH3631
ATOM 3234 CB VAL B 52 -1.225 3.010 71.010 1.00 16.70 6ADH3632
ATOM 3235 CG1 VAL B 52 -.592 2.216 72.158 1.00 16.70 6ADH3633
ATOM 3236 CG2 VAL B 52 -.199 4.084 70.641 1.00 16.70 6ADH3634
ATOM 3237 N VAL B 53 -3.410 .821 70.760 1.00 16.70 6ADH3635
ATOM 3238 CA VAL B 53 -4.055 -.309 71.441 1.00 16.70 6ADH3636
ATOM 3239 C VAL B 53 -4.288 -1.520 70.507 1.00 16.70 6ADH3637
ATOM 3240 O VAL B 53 -4.110 -2.680 70.904 1.00 16.70 6ADH3638
ATOM 3241 CB VAL B 53 -5.405 .135 72.022 1.00 16.70 6ADH3639
ATOM 3242 CG1 VAL B 53 -6.007 -.882 72.995 1.00 16.70 6ADH3640
ATOM 3243 CG2 VAL B 53 -5.317 1.448 72.804 1.00 16.70 6ADH3641
ATOM 3244 N SER B 54 -4.689 -1.258 69.281 1.00 16.70 6ADH3642
ATOM 3245 CA SER B 54 -5.022 -2.333 68.312 1.00 16.70 6ADH3643
ATOM 3246 C SER B 54 -3.806 -3.216 68.049 1.00 16.70 6ADH3644
ATOM 3247 O SER B 54 -3.841 -4.429 68.322 0.00 16.70 2 6ADH3645
ATOM 3248 CB SER B 54 -5.491 -1.703 67.003 1.00 16.70 6ADH3646
ATOM 3249 OG SER B 54 -6.603 -.855 67.256 1.00 16.70 6ADH3647
ATOM 3250 N GLY B 55 -2.838 -2.468 67.550 1.00 16.70 6ADH3648
ATOM 3251 CA GLY B 55 -1.519 -2.908 67.128 1.00 16.70 6ADH3649
ATOM 3252 C GLY B 55 -1.183 -2.205 65.806 1.00 16.70 6ADH3650
ATOM 3253 O GLY B 55 -.220 -2.560 65.113 1.00 16.70 6ADH3651
ATOM 3254 N THR B 56 -1.973 -1.200 65.472 1.00 16.70 6ADH3652
ATOM 3255 CA THR B 56 -1.837 -.516 64.170 1.00 16.70 6ADH3653
ATOM 3256 C THR B 56 -1.010 .792 64.247 1.00 16.70 6ADH3654
ATOM 3257 O THR B 56 -.663 1.390 63.218 1.00 16.70 6ADH3655
ATOM 3258 CB THR B 56 -3.231 -.247 63.594 1.00 16.70 6ADH3656
ATOM 3259 OG1 THR B 56 -3.780 .935 64.155 1.00 16.70 6ADH3657
ATOM 3260 CG2 THR B 56 -4.216 -1.385 63.873 1.00 16.70 6ADH3658
ATOM 3261 N LEU B 57 -.702 1.226 65.450 1.00 16.70 6ADH3659
ATOM 3262 CA LEU B 57 .126 2.434 65.681 1.00 16.70 6ADH3660
ATOM 3263 C LEU B 57 1.152 2.065 66.752 1.00 16.70 6ADH3661
ATOM 3264 O LEU B 57 .884 2.190 67.955 1.00 16.70 6ADH3662
ATOM 3265 CB LEU B 57 -.772 3.608 66.100 1.00 16.70 6ADH3663
ATOM 3266 CG LEU B 57 -.045 4.962 66.146 1.00 16.70 6ADH3664
ATOM 3267 CD1 LEU B 57 1.083 5.076 65.119 1.00 16.70 6ADH3665
ATOM 3268 CD2 LEU B 57 -.972 6.149 65.871 1.00 16.70 6ADH3666
ATOM 3269 N VAL B 58 2.290 1.618 66.222 1.00 16.70 6ADH3667
ATOM 3270 CA VAL B 58 3.365 1.038 67.013 1.00 16.70 6ADH3668
ATOM 3271 C VAL B 58 4.496 1.941 67.393 1.00 16.70 6ADH3669
ATOM 3272 O VAL B 58 5.430 2.154 66.594 0.00 16.70 2 6ADH3670
ATOM 3273 CB VAL B 58 4.039 -.140 66.317 1.00 16.70 6ADH3671
ATOM 3274 CG1 VAL B 58 4.649 -1.152 67.294 1.00 16.70 6ADH3672
ATOM 3275 CG2 VAL B 58 3.076 -.938 65.443 1.00 16.70 6ADH3673
ATOM 3276 N THR B 59 4.231 2.328 68.614 1.00 16.70 6ADH3674
ATOM 3277 CA THR B 59 5.193 2.849 69.522 1.00 16.70 6ADH3675
ATOM 3278 C THR B 59 5.406 1.727 70.508 1.00 16.70 6ADH3676
ATOM 3279 O THR B 59 4.540 .851 70.664 1.00 16.70 6ADH3677
ATOM 3280 CB THR B 59 4.721 4.027 70.384 1.00 16.70 6ADH3678
ATOM 3281 OG1 THR B 59 4.811 5.242 69.658 1.00 16.70 6ADH3679
ATOM 3282 CG2 THR B 59 5.564 4.195 71.654 1.00 16.70 6ADH3680
ATOM 3283 N PRO B 60 6.549 1.740 71.118 1.00 16.70 6ADH3681
ATOM 3284 CA PRO B 60 6.908 .816 72.180 1.00 16.70 6ADH3682
ATOM 3285 C PRO B 60 6.040 .915 73.427 1.00 16.70 6ADH3683
ATOM 3286 O PRO B 60 5.389 1.990 73.640 0.00 16.70 2 6ADH3684
ATOM 3287 CB PRO B 60 8.341 1.166 72.470 1.00 16.70 6ADH3685
ATOM 3288 CG PRO B 60 8.749 2.300 71.544 1.00 16.70 6ADH3686
ATOM 3289 CD PRO B 60 7.582 2.670 70.698 1.00 16.70 6ADH3687
ATOM 3290 N LEU B 61 6.134 -.230 74.139 1.00 16.70 6ADH3688
ATOM 3291 CA LEU B 61 5.382 -.548 75.366 1.00 16.70 6ADH3689
ATOM 3292 C LEU B 61 6.264 -1.147 76.475 1.00 16.70 6ADH3690
ATOM 3293 O LEU B 61 7.373 -1.646 76.212 1.00 16.70 6ADH3691
ATOM 3294 CB LEU B 61 4.304 -1.594 75.048 1.00 16.70 6ADH3692
ATOM 3295 CG LEU B 61 2.958 -.962 74.694 1.00 16.70 6ADH3693
ATOM 3296 CD1 LEU B 61 3.104 .395 74.005 1.00 16.70 6ADH3694
ATOM 3297 CD2 LEU B 61 2.119 -1.821 73.746 1.00 16.70 6ADH3695
ATOM 3298 N PRO B 62 5.754 -1.105 77.733 1.00 16.70 1 6ADH3696
ATOM 3299 CA PRO B 62 4.454 -.449 78.037 1.00 16.70 1 6ADH3697
ATOM 3300 C PRO B 62 4.498 1.080 77.916 1.00 16.70 1 6ADH3698
ATOM 3301 O PRO B 62 5.625 1.656 78.071 1.00 16.70 1 6ADH3699
ATOM 3302 CB PRO B 62 4.211 -.764 79.486 1.00 16.70 1 6ADH3700
ATOM 3303 CG PRO B 62 5.408 -1.557 80.001 1.00 16.70 1 6ADH3701
ATOM 3304 CD PRO B 62 6.405 -1.730 78.891 1.00 16.70 1 6ADH3702
ATOM 3305 N VAL B 63 3.268 1.706 77.675 1.00 16.70 6ADH3703
ATOM 3306 CA VAL B 63 3.125 3.225 77.514 1.00 16.70 6ADH3704
ATOM 3307 C VAL B 63 1.837 3.924 78.050 1.00 16.70 6ADH3705
ATOM 3308 O VAL B 63 .723 3.377 77.983 1.00 16.70 6ADH3706
ATOM 3309 CB VAL B 63 3.059 3.686 76.040 1.00 16.70 6ADH3707
ATOM 3310 CG1 VAL B 63 1.889 3.082 75.254 1.00 16.70 6ADH3708
ATOM 3311 CG2 VAL B 63 2.892 5.203 75.903 1.00 16.70 6ADH3709
ATOM 3312 N ILE B 64 2.059 5.153 78.569 1.00 16.70 6ADH3710
ATOM 3313 CA ILE B 64 .949 6.086 78.846 1.00 16.70 6ADH3711
ATOM 3314 C ILE B 64 .610 6.710 77.499 1.00 16.70 6ADH3712
ATOM 3315 O ILE B 64 1.407 7.466 76.927 1.00 16.70 6ADH3713
ATOM 3316 CB ILE B 64 1.339 7.291 79.741 1.00 16.70 6ADH3714
ATOM 3317 CG1 ILE B 64 2.374 6.958 80.813 1.00 16.70 6ADH3715
ATOM 3318 CG2 ILE B 64 .144 7.896 80.488 1.00 16.70 6ADH3716
ATOM 3319 CD1 ILE B 64 1.771 6.246 82.024 1.00 16.70 6ADH3717
ATOM 3320 N ALA B 65 -.545 6.408 76.968 1.00 16.70 6ADH3718
ATOM 3321 CA ALA B 65 -.957 7.000 75.675 1.00 16.70 6ADH3719
ATOM 3322 C ALA B 65 -1.330 8.496 75.895 1.00 16.70 6ADH3720
ATOM 3323 O ALA B 65 -.813 9.151 76.812 1.00 16.70 6ADH3721
ATOM 3324 CB ALA B 65 -2.155 6.233 75.113 1.00 16.70 6ADH3722
ATOM 3325 N GLY B 66 -2.224 9.012 75.027 1.00 16.70 6ADH3723
ATOM 3326 CA GLY B 66 -2.772 10.417 75.101 1.00 16.70 6ADH3724
ATOM 3327 C GLY B 66 -1.826 11.481 74.468 1.00 16.70 6ADH3725
ATOM 3328 O GLY B 66 -.595 11.378 74.566 1.00 16.70 6ADH3726
ATOM 3329 N HIS B 67 -2.448 12.509 73.824 1.00 16.70 6ADH3727
ATOM 3330 CA HIS B 67 -1.707 13.637 73.160 1.00 16.70 6ADH3728
ATOM 3331 C HIS B 67 -2.598 14.902 72.917 1.00 16.70 6ADH3729
ATOM 3332 O HIS B 67 -2.110 15.955 72.478 1.00 16.70 6ADH3730
ATOM 3333 CB HIS B 67 -1.126 13.188 71.799 1.00 16.70 6ADH3731
ATOM 3334 CG HIS B 67 -2.176 12.757 70.759 1.00 16.70 6ADH3732
ATOM 3335 ND1 HIS B 67 -2.721 11.476 70.748 1.00 16.70 6ADH3733
ATOM 3336 CD2 HIS B 67 -2.757 13.420 69.721 1.00 16.70 6ADH3734
ATOM 3337 CE1 HIS B 67 -3.583 11.399 69.747 1.00 16.70 6ADH3735
ATOM 3338 NE2 HIS B 67 -3.616 12.550 69.125 1.00 16.70 6ADH3736
ATOM 3339 N GLU B 68 -3.884 14.776 73.211 1.00 16.70 6ADH3737
ATOM 3340 CA GLU B 68 -4.895 15.857 73.039 1.00 16.70 6ADH3738
ATOM 3341 C GLU B 68 -5.307 16.360 74.430 1.00 16.70 6ADH3739
ATOM 3342 O GLU B 68 -6.283 15.877 75.022 1.00 16.70 6ADH3740
ATOM 3343 CB GLU B 68 -6.102 15.237 72.305 1.00 16.70 6ADH3741
ATOM 3344 CG GLU B 68 -7.209 16.214 71.907 1.00 16.70 6ADH3742
ATOM 3345 CD GLU B 68 -8.246 15.556 70.985 1.00 16.70 6ADH3743
ATOM 3346 OE1 GLU B 68 -9.506 15.738 71.190 1.00 16.70 6ADH3744
ATOM 3347 OE2 GLU B 68 -7.856 14.818 70.000 1.00 16.70 6ADH3745
ATOM 3348 N ALA B 69 -4.566 17.332 74.961 1.00 16.70 6ADH3746
ATOM 3349 CA ALA B 69 -4.830 17.794 76.341 1.00 16.70 6ADH3747
ATOM 3350 C ALA B 69 -4.322 19.214 76.643 1.00 16.70 6ADH3748
ATOM 3351 O ALA B 69 -3.316 19.673 76.085 1.00 16.70 6ADH3749
ATOM 3352 CB ALA B 69 -4.115 16.871 77.331 1.00 16.70 6ADH3750
ATOM 3353 N ALA B 70 -5.047 19.865 77.536 1.00 16.70 6ADH3751
ATOM 3354 CA ALA B 70 -4.674 21.184 78.083 1.00 16.70 6ADH3752
ATOM 3355 C ALA B 70 -4.426 21.002 79.594 1.00 16.70 6ADH3753
ATOM 3356 O ALA B 70 -5.006 20.104 80.222 1.00 16.70 6ADH3754
ATOM 3357 CB ALA B 70 -5.802 22.195 77.863 1.00 16.70 6ADH3755
ATOM 3358 N GLY B 71 -3.570 21.875 80.159 1.00 16.70 6ADH3756
ATOM 3359 CA GLY B 71 -3.189 21.835 81.610 1.00 16.70 6ADH3757
ATOM 3360 C GLY B 71 -2.446 23.130 82.048 1.00 16.70 6ADH3758
ATOM 3361 O GLY B 71 -2.444 24.137 81.328 1.00 16.70 6ADH3759
ATOM 3362 N ILE B 72 -1.847 23.069 83.249 1.00 16.70 6ADH3760
ATOM 3363 CA ILE B 72 -1.011 24.164 83.804 1.00 16.70 6ADH3761
ATOM 3364 C ILE B 72 .257 23.558 84.427 1.00 16.70 6ADH3762
ATOM 3365 O ILE B 72 .256 22.398 84.864 1.00 16.70 6ADH3763
ATOM 3366 CB ILE B 72 -1.782 25.015 84.843 1.00 16.70 6ADH3764
ATOM 3367 CG1 ILE B 72 -3.287 25.093 84.566 1.00 16.70 6ADH3765
ATOM 3368 CG2 ILE B 72 -1.309 26.473 84.901 1.00 16.70 6ADH3766
ATOM 3369 CD1 ILE B 72 -4.139 24.890 85.820 1.00 16.70 6ADH3767
ATOM 3370 N VAL B 73 1.262 24.419 84.389 1.00 16.70 6ADH3768
ATOM 3371 CA VAL B 73 2.586 24.169 84.905 1.00 16.70 6ADH3769
ATOM 3372 C VAL B 73 2.637 24.402 86.397 1.00 16.70 6ADH3770
ATOM 3373 O VAL B 73 1.922 25.275 86.913 1.00 16.70 6ADH3771
ATOM 3374 CB VAL B 73 3.627 25.078 84.235 1.00 16.70 6ADH3772
ATOM 3375 CG1 VAL B 73 5.014 24.437 84.121 1.00 16.70 6ADH3773
ATOM 3376 CG2 VAL B 73 3.242 25.475 82.810 1.00 16.70 6ADH3774
ATOM 3377 N GLU B 74 3.505 23.538 86.788 1.00 16.70 6ADH3775
ATOM 3378 CA GLU B 74 4.030 23.228 88.064 1.00 16.70 6ADH3776
ATOM 3379 C GLU B 74 5.466 23.682 88.036 1.00 16.70 6ADH3777
ATOM 3380 O GLU B 74 5.772 24.861 88.258 1.00 16.70 6ADH3778
ATOM 3381 CB GLU B 74 4.104 21.711 88.074 1.00 16.70 6ADH3779
ATOM 3382 CG GLU B 74 3.248 21.031 89.100 1.00 16.70 6ADH3780
ATOM 3383 CD GLU B 74 4.048 19.961 89.817 1.00 16.70 6ADH3781
ATOM 3384 OE1 GLU B 74 3.597 19.446 90.907 1.00 16.70 6ADH3782
ATOM 3385 OE2 GLU B 74 5.178 19.572 89.331 1.00 16.70 6ADH3783
ATOM 3386 N SER B 75 6.242 22.679 87.728 1.00 16.70 6ADH3784
ATOM 3387 CA SER B 75 7.662 22.788 87.554 1.00 16.70 6ADH3785
ATOM 3388 C SER B 75 7.954 23.309 86.155 1.00 16.70 6ADH3786
ATOM 3389 O SER B 75 7.066 23.332 85.290 1.00 16.70 6ADH3787
ATOM 3390 CB SER B 75 8.309 21.409 87.709 1.00 16.70 6ADH3788
ATOM 3391 OG SER B 75 9.149 21.387 88.853 1.00 16.70 6ADH3789
ATOM 3392 N ILE B 76 9.192 23.687 86.071 1.00 16.70 6ADH3790
ATOM 3393 CA ILE B 76 9.863 24.200 84.896 1.00 16.70 6ADH3791
ATOM 3394 C ILE B 76 11.362 24.039 85.236 1.00 16.70 6ADH3792
ATOM 3395 O ILE B 76 11.784 24.332 86.366 1.00 16.70 6ADH3793
ATOM 3396 CB ILE B 76 9.361 25.633 84.623 1.00 16.70 6ADH3794
ATOM 3397 CG1 ILE B 76 8.801 25.817 83.205 1.00 16.70 6ADH3795
ATOM 3398 CG2 ILE B 76 10.448 26.698 84.773 1.00 16.70 6ADH3796
ATOM 3399 CD1 ILE B 76 9.496 26.936 82.426 0.00 16.70 2 6ADH3797
ATOM 3400 N GLY B 77 12.095 23.550 84.226 1.00 16.70 6ADH3798
ATOM 3401 CA GLY B 77 13.544 23.206 84.306 1.00 16.70 6ADH3799
ATOM 3402 C GLY B 77 14.451 24.423 84.076 1.00 16.70 6ADH3800
ATOM 3403 O GLY B 77 14.048 25.574 84.293 0.00 16.70 2 6ADH3801
ATOM 3404 N GLU B 78 15.673 24.140 83.631 1.00 16.70 6ADH3802
ATOM 3405 CA GLU B 78 16.698 25.190 83.431 1.00 16.70 6ADH3803
ATOM 3406 C GLU B 78 17.031 25.407 81.937 1.00 16.70 6ADH3804
ATOM 3407 O GLU B 78 17.111 24.446 81.155 0.00 16.70 2 6ADH3805
ATOM 3408 CB GLU B 78 17.967 24.826 84.211 1.00 16.70 6ADH3806
ATOM 3409 CG GLU B 78 18.381 23.357 84.051 1.00 16.70 6ADH3807
ATOM 3410 CD GLU B 78 17.600 22.390 84.951 1.00 16.70 6ADH3808
ATOM 3411 OE1 GLU B 78 17.861 21.126 84.918 1.00 16.70 6ADH3809
ATOM 3412 OE2 GLU B 78 16.684 22.837 85.741 1.00 16.70 6ADH3810
ATOM 3413 N GLY B 79 17.218 26.705 81.639 1.00 16.70 6ADH3811
ATOM 3414 CA GLY B 79 17.486 27.239 80.279 1.00 16.70 6ADH3812
ATOM 3415 C GLY B 79 16.134 27.441 79.603 1.00 16.70 6ADH3813
ATOM 3416 O GLY B 79 15.906 26.969 78.479 1.00 16.70 6ADH3814
ATOM 3417 N VAL B 80 15.292 28.154 80.335 1.00 16.70 6ADH3815
ATOM 3418 CA VAL B 80 13.875 28.290 79.990 1.00 16.70 6ADH3816
ATOM 3419 C VAL B 80 13.294 29.700 80.257 1.00 16.70 6ADH3817
ATOM 3420 O VAL B 80 13.599 30.338 81.275 0.00 16.70 2 6ADH3818
ATOM 3421 CB VAL B 80 13.123 27.309 80.894 1.00 16.70 6ADH3819
ATOM 3422 CG1 VAL B 80 11.765 27.834 81.358 1.00 16.70 6ADH3820
ATOM 3423 CG2 VAL B 80 12.846 25.964 80.222 1.00 16.70 6ADH3821
ATOM 3424 N THR B 81 12.457 30.134 79.317 1.00 16.70 6ADH3822
ATOM 3425 CA THR B 81 11.694 31.404 79.408 1.00 16.70 6ADH3823
ATOM 3426 C THR B 81 10.656 31.433 78.263 1.00 16.70 6ADH3824
ATOM 3427 O THR B 81 10.525 32.438 77.544 0.00 16.70 2 6ADH3825
ATOM 3428 CB THR B 81 12.634 32.622 79.425 1.00 16.70 6ADH3826
ATOM 3429 OG1 THR B 81 11.882 33.813 79.610 1.00 16.70 6ADH3827
ATOM 3430 CG2 THR B 81 13.443 32.790 78.138 1.00 16.70 6ADH3828
ATOM 3431 N THR B 82 9.976 30.280 78.193 1.00 16.70 6ADH3829
ATOM 3432 CA THR B 82 8.876 29.981 77.250 1.00 16.70 6ADH3830
ATOM 3433 C THR B 82 7.532 29.950 78.044 1.00 16.70 6ADH3831
ATOM 3434 O THR B 82 6.633 30.772 77.807 1.00 16.70 6ADH3832
ATOM 3435 CB THR B 82 9.138 28.632 76.559 1.00 16.70 6ADH3833
ATOM 3436 OG1 THR B 82 9.975 27.822 77.370 1.00 16.70 6ADH3834
ATOM 3437 CG2 THR B 82 9.828 28.779 75.200 1.00 16.70 6ADH3835
ATOM 3438 N VAL B 83 7.431 28.994 78.989 1.00 16.70 6ADH3836
ATOM 3439 CA VAL B 83 6.244 28.830 79.899 1.00 16.70 6ADH3837
ATOM 3440 C VAL B 83 6.707 28.721 81.380 1.00 16.70 6ADH3838
ATOM 3441 O VAL B 83 7.424 27.780 81.756 0.00 16.70 2 6ADH3839
ATOM 3442 CB VAL B 83 5.462 27.546 79.569 1.00 16.70 6ADH3840
ATOM 3443 CG1 VAL B 83 4.991 27.481 78.115 1.00 16.70 6ADH3841
ATOM 3444 CG2 VAL B 83 6.279 26.272 79.796 1.00 16.70 6ADH3842
ATOM 3445 N ARG B 84 6.278 29.691 82.202 1.00 16.70 6ADH3843
ATOM 3446 CA ARG B 84 6.642 29.775 83.657 1.00 16.70 6ADH3844
ATOM 3447 C ARG B 84 5.627 29.000 84.542 1.00 16.70 6ADH3845
ATOM 3448 O ARG B 84 4.464 28.808 84.163 1.00 16.70 6ADH3846
ATOM 3449 CB ARG B 84 6.646 31.239 84.108 0.00 16.70 2 6ADH3847
ATOM 3450 CG ARG B 84 8.012 31.908 83.957 0.00 16.70 2 6ADH3848
ATOM 3451 CD ARG B 84 9.132 31.141 84.662 0.00 16.70 2 6ADH3849
ATOM 3452 NE ARG B 84 10.396 31.887 84.709 0.00 16.70 2 6ADH3850
ATOM 3453 CZ ARG B 84 11.322 31.732 85.665 0.00 16.70 2 6ADH3851
ATOM 3454 NH1 ARG B 84 11.143 30.859 86.665 0.00 16.70 2 6ADH3852
ATOM 3455 NH2 ARG B 84 12.474 32.414 85.708 0.00 16.70 2 6ADH3853
ATOM 3456 N PRO B 85 5.995 28.515 85.763 1.00 16.70 6ADH3854
ATOM 3457 CA PRO B 85 5.069 27.726 86.619 1.00 16.70 6ADH3855
ATOM 3458 C PRO B 85 3.750 28.458 86.986 1.00 16.70 6ADH3856
ATOM 3459 O PRO B 85 3.815 29.640 87.450 0.00 16.70 2 6ADH3857
ATOM 3460 CB PRO B 85 5.901 27.404 87.844 1.00 16.70 6ADH3858
ATOM 3461 CG PRO B 85 7.286 28.016 87.653 1.00 16.70 6ADH3859
ATOM 3462 CD PRO B 85 7.337 28.719 86.330 1.00 16.70 6ADH3860
ATOM 3463 N GLY B 86 2.621 27.705 86.765 1.00 16.70 6ADH3861
ATOM 3464 CA GLY B 86 1.184 28.122 87.041 1.00 16.70 6ADH3862
ATOM 3465 C GLY B 86 .572 28.821 85.798 1.00 16.70