HEADER AMYLOID PROTEIN 27-JAN-94 1SAC 1SAC 2 COMPND SERUM AMYLOID P COMPONENT (SAP) 1SAC 3 SOURCE HUMAN (HOMO SAPIENS) SERUM 1SAC 4 AUTHOR H.E.WHITE,J.EMSLEY,B.P.O'HARA,G.OLIVA,N.SRINIVASAN, 1SACA 1 AUTHOR 2 I.J.TICKLE,T.L.BLUNDELL,M.B.PEPYS,S.P.WOOD 1SACA 2 REVDAT 2 31-JUL-94 1SAC 1 AUTHOR REMARK HELIX SSBOND 1SACA 3 REVDAT 2 2 SITE 1SACA 4 REVDAT 1 31-MAY-94 1SAC 0 1SAC 7 JRNL AUTH J.EMSLEY,H.E.WHITE,B.P.O'HARA,G.OLIVA,N.SRINIVASAN, 1SAC 8 JRNL AUTH 2 I.J.TICKLE,T.L.BLUNDELL,M.B.PEPYS,S.P.WOOD 1SAC 9 JRNL TITL THE STRUCTURE OF PENTAMERIC HUMAN SERUM AMYLOID P 1SAC 10 JRNL TITL 2 COMPONENT 1SAC 11 JRNL REF NATURE V. 367 338 1994 1SAC 12 JRNL REFN ASTM NATUAS UK ISSN 0028-0836 0006 1SAC 13 REMARK 1 1SAC 14 REMARK 1 REFERENCE 1 1SAC 15 REMARK 1 AUTH S.P.WOOD,G.OLIVA,B.P.O'HARA,H.E.WHITE,T.L.BLUNDELL, 1SAC 16 REMARK 1 AUTH 2 S.J.PERKINS,I.SARDHARWALLA,M.P.PEPYS 1SAC 17 REMARK 1 TITL A PENTAMERIC FORM OF HUMAN SERUM AMYLOID P 1SAC 18 REMARK 1 TITL 2 COMPONENT: CRYSTALLIZATION, X-RAY DIFFRACTION 1SAC 19 REMARK 1 TITL 3 AND NEUTRON SCATTERING STUDIES 1SAC 20 REMARK 1 REF J.MOL.BIOL. V. 202 169 1988 1SAC 21 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 0070 1SAC 22 REMARK 1 REFERENCE 2 1SAC 23 REMARK 1 AUTH B.P.O'HARA,S.P.WOOD,G.OLIVA,H.E.WHITE,M.B.PEPYS 1SAC 24 REMARK 1 TITL CRYSTALLIZATION OF HUMAN SERUM AMYLOID P 1SAC 25 REMARK 1 TITL 2 COMPONENT (SAP) 1SAC 26 REMARK 1 REF J.CRYST.GROWTH V. 90 209 1988 1SAC 27 REMARK 1 REFN ASTM JCRGAE NE ISSN 0022-0248 0229 1SAC 28 REMARK 1 REFERENCE 3 1SACA 5 REMARK 1 AUTH S.OHNISHI,S.MAEDA,K.SHIMADA,T.ARAO 1SACA 6 REMARK 1 TITL ISOLATION AND CHARACTERIZATION OF THE COMPLETE 1SACA 7 REMARK 1 TITL 2 COMPLEMENTARY AND GENOMIC DNA SEQUENCES OF HUMAN 1SACA 8 REMARK 1 TITL 3 SERUM 1SACA 9 REMARK 1 REF J.BIOCHEM.(TOKYO) V. 100 849 1986 1SACA 10 REMARK 1 REFN ASTM JOBIAO JA ISSN 0021-924X 418 1SACA 11 REMARK 2 1SAC 29 REMARK 2 RESOLUTION. 2.0 ANGSTROMS. 1SAC 30 REMARK 3 1SAC 31 REMARK 3 REFINEMENT. 1SAC 32 REMARK 3 PROGRAM 1 X-PLOR 1SAC 33 REMARK 3 AUTHORS 1 BRUNGER 1SAC 34 REMARK 3 PROGRAM 2 RESTRAIN 1SAC 35 REMARK 3 AUTHORS 2 MOSS,DRIESSEN,HANEEF,HOWLIN, 1SAC 36 REMARK 3 AUTHORS 2 HARRIS 1SAC 37 REMARK 3 R VALUE 0.179 1SAC 38 REMARK 3 RMSD BOND DISTANCES 0.017 ANGSTROMS 1SAC 39 REMARK 3 RMSD BOND ANGLES 3.45 DEGREES 1SAC 40 REMARK 3 1SAC 41 REMARK 3 NUMBER OF REFLECTIONS 78910 1SAC 42 REMARK 3 RESOLUTION RANGE 8.0 - 2.0 ANGSTROMS 1SAC 43 REMARK 3 DATA CUTOFF 0.0 SIGMA(F) 1SAC 44 REMARK 3 PERCENT COMPLETION 93.6 1SAC 45 REMARK 3 1SAC 46 REMARK 3 NUMBER OF PROTEIN ATOMS 8240 1SAC 47 REMARK 3 NUMBER OF SOLVENT ATOMS 865 1SAC 48 REMARK 4 1SAC 49 REMARK 4 IN SITES CA1 AND CA2 OF CHAIN C, RESIDUE ACY 300 IS 1SAC 50 REMARK 4 REPLACED BY GLU 167 OF AN ADJACENT MOLECULE. 1SAC 51 REMARK 5 1SAC 52 REMARK 5 THE CHAINS LABELLED *A* TO *E* CORRESPOND TO PROTOMERS 1 1SAC 53 REMARK 5 TO 5 AS DESCRIBED IN THE *JRNL* REFERENCE. 1SAC 54 REMARK 6 1SAC 55 REMARK 6 SAP IS A PENTAMER OF IDENTICAL POLYPEPTIDE CHAINS. THE 1SAC 56 REMARK 6 COORDINATES OF ALL FIVE CHAINS ARE INCLUDED IN THIS ENTRY 1SAC 57 REMARK 6 AND HAVE BEEN ASSIGNED CHAIN INDICATORS *A*, *B*, *C*, *D*, 1SAC 58 REMARK 6 AND *E*. THE TRANSFORMATIONS GIVEN IN THE *MTRIX* RECORDS 1SAC 59 REMARK 6 BELOW REPRESENT THE NON-CRYSTALLOGRAPHIC FIVE-FOLD AXIS. 1SAC 60 REMARK 6 THE TRANSFORMATION PRESENTED ON *MTRIX 1* RECORDS BELOW 1SAC 61 REMARK 6 WILL YIELD APPROXIMATE COORDINATES FOR CHAIN A WHEN APPLIED 1SAC 62 REMARK 6 TO CHAIN B. 1SAC 63 REMARK 6 THE TRANSFORMATION PRESENTED ON *MTRIX 2* RECORDS BELOW 1SAC 64 REMARK 6 WILL YIELD APPROXIMATE COORDINATES FOR CHAIN A WHEN APPLIED 1SAC 65 REMARK 6 TO CHAIN C. 1SAC 66 REMARK 6 THE TRANSFORMATION PRESENTED ON *MTRIX 3* RECORDS BELOW 1SAC 67 REMARK 6 WILL YIELD APPROXIMATE COORDINATES FOR CHAIN A WHEN APPLIED 1SAC 68 REMARK 6 TO CHAIN D. 1SAC 69 REMARK 6 THE TRANSFORMATION PRESENTED ON *MTRIX 4* RECORDS BELOW 1SAC 70 REMARK 6 WILL YIELD APPROXIMATE COORDINATES FOR CHAIN A WHEN APPLIED 1SAC 71 REMARK 6 TO CHAIN E. 1SAC 72 REMARK 7 1SAC 73 REMARK 7 STRANDS A1_ AND A2_ IN ALL FIVE CHAINS ARE DISCONNECTED BUT 1SAC 74 REMARK 7 FORM A CONTINUOUS STRAND IN THE STRUCTURE. 1SAC 75 REMARK 8 1SAC 76 REMARK 8 CROSS REFERENCE TO SEQUENCE DATABASE 1SAC 77 REMARK 8 SWISS-PROT ENTRY NAME PDB ENTRY CHAIN NAME 1SAC 78 REMARK 8 SAMP_HUMAN A 1SAC 79 REMARK 8 SAMP_HUMAN B 1SAC 80 REMARK 8 SAMP_HUMAN C 1SAC 81 REMARK 8 SAMP_HUMAN D 1SAC 82 REMARK 8 SAMP_HUMAN E 1SAC 83 REMARK 9 1SAC 84 REMARK 9 SEQUENCE ADVISORY NOTICE 1SAC 85 REMARK 9 DIFFERENCE BETWEEN SWISS-PROT AND PDB SEQUENCE. 1SAC 86 REMARK 9 1SAC 87 REMARK 9 SWISS-PROT ENTRY NAME: SAMP_HUMAN 1SAC 88 REMARK 9 1SAC 89 REMARK 9 NAME NUMBER NAME CHAIN SEQ 1SAC 90 REMARK 9 PRO 101 SER A 82 1SAC 91 REMARK 9 PRO 101 SER B 82 1SAC 92 REMARK 9 PRO 101 SER C 82 1SAC 93 REMARK 9 PRO 101 SER D 82 1SAC 94 REMARK 9 PRO 101 SER E 82 1SAC 95 REMARK 9 1SAC 96 REMARK 9 THE SEQUENCE BUILT INTO THIS STRUCTURE IS THE AMENDED 1SAC 97 REMARK 9 VERSION WHERE RESIDUE 82 IS A SERINE. SEE REFERENCE 3. 1SAC 98 REMARK 10 1SACA 12 REMARK 10 SITES C1C AND C2C ALSO INCLUDE RESIDUE GLU A 167 FROM A 1SACA 13 REMARK 10 SYMMETRY-RELATED MOLECULE. 1SACA 14 REMARK 11 1SACA 15 REMARK 11 CORRECTION. REVISE AUTHOR, REMARK 9, HELIX, SITE, AND 1SACA 16 REMARK 11 SSBOND RECORDS FOLLOWING AUTHOR INSTRUCTIONS. 31-JUL-94. 1SACA 17 SEQRES 1 A 204 HIS THR ASP LEU SER GLY LYS VAL PHE VAL PHE PRO ARG 1SAC 99 SEQRES 2 A 204 GLU SER VAL THR ASP HIS VAL ASN LEU ILE THR PRO LEU 1SAC 100 SEQRES 3 A 204 GLU LYS PRO LEU GLN ASN PHE THR LEU CYS PHE ARG ALA 1SAC 101 SEQRES 4 A 204 TYR SER ASP LEU SER ARG ALA TYR SER LEU PHE SER TYR 1SAC 102 SEQRES 5 A 204 ASN THR GLN GLY ARG ASP ASN GLU LEU LEU VAL TYR LYS 1SAC 103 SEQRES 6 A 204 GLU ARG VAL GLY GLU TYR SER LEU TYR ILE GLY ARG HIS 1SAC 104 SEQRES 7 A 204 LYS VAL THR SER LYS VAL ILE GLU LYS PHE PRO ALA PRO 1SAC 105 SEQRES 8 A 204 VAL HIS ILE CYS VAL SER TRP GLU SER SER SER GLY ILE 1SAC 106 SEQRES 9 A 204 ALA GLU PHE TRP ILE ASN GLY THR PRO LEU VAL LYS LYS 1SAC 107 SEQRES 10 A 204 GLY LEU ARG GLN GLY TYR PHE VAL GLU ALA GLN PRO LYS 1SAC 108 SEQRES 11 A 204 ILE VAL LEU GLY GLN GLU GLN ASP SER TYR GLY GLY LYS 1SAC 109 SEQRES 12 A 204 PHE ASP ARG SER GLN SER PHE VAL GLY GLU ILE GLY ASP 1SAC 110 SEQRES 13 A 204 LEU TYR MET TRP ASP SER VAL LEU PRO PRO GLU ASN ILE 1SAC 111 SEQRES 14 A 204 LEU SER ALA TYR GLN GLY THR PRO LEU PRO ALA ASN ILE 1SAC 112 SEQRES 15 A 204 LEU ASP TRP GLN ALA LEU ASN TYR GLU ILE ARG GLY TYR 1SAC 113 SEQRES 16 A 204 VAL ILE ILE LYS PRO LEU VAL TRP VAL 1SAC 114 SEQRES 1 B 204 HIS THR ASP LEU SER GLY LYS VAL PHE VAL PHE PRO ARG 1SAC 115 SEQRES 2 B 204 GLU SER VAL THR ASP HIS VAL ASN LEU ILE THR PRO LEU 1SAC 116 SEQRES 3 B 204 GLU LYS PRO LEU GLN ASN PHE THR LEU CYS PHE ARG ALA 1SAC 117 SEQRES 4 B 204 TYR SER ASP LEU SER ARG ALA TYR SER LEU PHE SER TYR 1SAC 118 SEQRES 5 B 204 ASN THR GLN GLY ARG ASP ASN GLU LEU LEU VAL TYR LYS 1SAC 119 SEQRES 6 B 204 GLU ARG VAL GLY GLU TYR SER LEU TYR ILE GLY ARG HIS 1SAC 120 SEQRES 7 B 204 LYS VAL THR SER LYS VAL ILE GLU LYS PHE PRO ALA PRO 1SAC 121 SEQRES 8 B 204 VAL HIS ILE CYS VAL SER TRP GLU SER SER SER GLY ILE 1SAC 122 SEQRES 9 B 204 ALA GLU PHE TRP ILE ASN GLY THR PRO LEU VAL LYS LYS 1SAC 123 SEQRES 10 B 204 GLY LEU ARG GLN GLY TYR PHE VAL GLU ALA GLN PRO LYS 1SAC 124 SEQRES 11 B 204 ILE VAL LEU GLY GLN GLU GLN ASP SER TYR GLY GLY LYS 1SAC 125 SEQRES 12 B 204 PHE ASP ARG SER GLN SER PHE VAL GLY GLU ILE GLY ASP 1SAC 126 SEQRES 13 B 204 LEU TYR MET TRP ASP SER VAL LEU PRO PRO GLU ASN ILE 1SAC 127 SEQRES 14 B 204 LEU SER ALA TYR GLN GLY THR PRO LEU PRO ALA ASN ILE 1SAC 128 SEQRES 15 B 204 LEU ASP TRP GLN ALA LEU ASN TYR GLU ILE ARG GLY TYR 1SAC 129 SEQRES 16 B 204 VAL ILE ILE LYS PRO LEU VAL TRP VAL 1SAC 130 SEQRES 1 C 204 HIS THR ASP LEU SER GLY LYS VAL PHE VAL PHE PRO ARG 1SAC 131 SEQRES 2 C 204 GLU SER VAL THR ASP HIS VAL ASN LEU ILE THR PRO LEU 1SAC 132 SEQRES 3 C 204 GLU LYS PRO LEU GLN ASN PHE THR LEU CYS PHE ARG ALA 1SAC 133 SEQRES 4 C 204 TYR SER ASP LEU SER ARG ALA TYR SER LEU PHE SER TYR 1SAC 134 SEQRES 5 C 204 ASN THR GLN GLY ARG ASP ASN GLU LEU LEU VAL TYR LYS 1SAC 135 SEQRES 6 C 204 GLU ARG VAL GLY GLU TYR SER LEU TYR ILE GLY ARG HIS 1SAC 136 SEQRES 7 C 204 LYS VAL THR SER LYS VAL ILE GLU LYS PHE PRO ALA PRO 1SAC 137 SEQRES 8 C 204 VAL HIS ILE CYS VAL SER TRP GLU SER SER SER GLY ILE 1SAC 138 SEQRES 9 C 204 ALA GLU PHE TRP ILE ASN GLY THR PRO LEU VAL LYS LYS 1SAC 139 SEQRES 10 C 204 GLY LEU ARG GLN GLY TYR PHE VAL GLU ALA GLN PRO LYS 1SAC 140 SEQRES 11 C 204 ILE VAL LEU GLY GLN GLU GLN ASP SER TYR GLY GLY LYS 1SAC 141 SEQRES 12 C 204 PHE ASP ARG SER GLN SER PHE VAL GLY GLU ILE GLY ASP 1SAC 142 SEQRES 13 C 204 LEU TYR MET TRP ASP SER VAL LEU PRO PRO GLU ASN ILE 1SAC 143 SEQRES 14 C 204 LEU SER ALA TYR GLN GLY THR PRO LEU PRO ALA ASN ILE 1SAC 144 SEQRES 15 C 204 LEU ASP TRP GLN ALA LEU ASN TYR GLU ILE ARG GLY TYR 1SAC 145 SEQRES 16 C 204 VAL ILE ILE LYS PRO LEU VAL TRP VAL 1SAC 146 SEQRES 1 D 204 HIS THR ASP LEU SER GLY LYS VAL PHE VAL PHE PRO ARG 1SAC 147 SEQRES 2 D 204 GLU SER VAL THR ASP HIS VAL ASN LEU ILE THR PRO LEU 1SAC 148 SEQRES 3 D 204 GLU LYS PRO LEU GLN ASN PHE THR LEU CYS PHE ARG ALA 1SAC 149 SEQRES 4 D 204 TYR SER ASP LEU SER ARG ALA TYR SER LEU PHE SER TYR 1SAC 150 SEQRES 5 D 204 ASN THR GLN GLY ARG ASP ASN GLU LEU LEU VAL TYR LYS 1SAC 151 SEQRES 6 D 204 GLU ARG VAL GLY GLU TYR SER LEU TYR ILE GLY ARG HIS 1SAC 152 SEQRES 7 D 204 LYS VAL THR SER LYS VAL ILE GLU LYS PHE PRO ALA PRO 1SAC 153 SEQRES 8 D 204 VAL HIS ILE CYS VAL SER TRP GLU SER SER SER GLY ILE 1SAC 154 SEQRES 9 D 204 ALA GLU PHE TRP ILE ASN GLY THR PRO LEU VAL LYS LYS 1SAC 155 SEQRES 10 D 204 GLY LEU ARG GLN GLY TYR PHE VAL GLU ALA GLN PRO LYS 1SAC 156 SEQRES 11 D 204 ILE VAL LEU GLY GLN GLU GLN ASP SER TYR GLY GLY LYS 1SAC 157 SEQRES 12 D 204 PHE ASP ARG SER GLN SER PHE VAL GLY GLU ILE GLY ASP 1SAC 158 SEQRES 13 D 204 LEU TYR MET TRP ASP SER VAL LEU PRO PRO GLU ASN ILE 1SAC 159 SEQRES 14 D 204 LEU SER ALA TYR GLN GLY THR PRO LEU PRO ALA ASN ILE 1SAC 160 SEQRES 15 D 204 LEU ASP TRP GLN ALA LEU ASN TYR GLU ILE ARG GLY TYR 1SAC 161 SEQRES 16 D 204 VAL ILE ILE LYS PRO LEU VAL TRP VAL 1SAC 162 SEQRES 1 E 204 HIS THR ASP LEU SER GLY LYS VAL PHE VAL PHE PRO ARG 1SAC 163 SEQRES 2 E 204 GLU SER VAL THR ASP HIS VAL ASN LEU ILE THR PRO LEU 1SAC 164 SEQRES 3 E 204 GLU LYS PRO LEU GLN ASN PHE THR LEU CYS PHE ARG ALA 1SAC 165 SEQRES 4 E 204 TYR SER ASP LEU SER ARG ALA TYR SER LEU PHE SER TYR 1SAC 166 SEQRES 5 E 204 ASN THR GLN GLY ARG ASP ASN GLU LEU LEU VAL TYR LYS 1SAC 167 SEQRES 6 E 204 GLU ARG VAL GLY GLU TYR SER LEU TYR ILE GLY ARG HIS 1SAC 168 SEQRES 7 E 204 LYS VAL THR SER LYS VAL ILE GLU LYS PHE PRO ALA PRO 1SAC 169 SEQRES 8 E 204 VAL HIS ILE CYS VAL SER TRP GLU SER SER SER GLY ILE 1SAC 170 SEQRES 9 E 204 ALA GLU PHE TRP ILE ASN GLY THR PRO LEU VAL LYS LYS 1SAC 171 SEQRES 10 E 204 GLY LEU ARG GLN GLY TYR PHE VAL GLU ALA GLN PRO LYS 1SAC 172 SEQRES 11 E 204 ILE VAL LEU GLY GLN GLU GLN ASP SER TYR GLY GLY LYS 1SAC 173 SEQRES 12 E 204 PHE ASP ARG SER GLN SER PHE VAL GLY GLU ILE GLY ASP 1SAC 174 SEQRES 13 E 204 LEU TYR MET TRP ASP SER VAL LEU PRO PRO GLU ASN ILE 1SAC 175 SEQRES 14 E 204 LEU SER ALA TYR GLN GLY THR PRO LEU PRO ALA ASN ILE 1SAC 176 SEQRES 15 E 204 LEU ASP TRP GLN ALA LEU ASN TYR GLU ILE ARG GLY TYR 1SAC 177 SEQRES 16 E 204 VAL ILE ILE LYS PRO LEU VAL TRP VAL 1SAC 178 FTNOTE 1 1SAC 179 FTNOTE 1 CIS PROLINE - PRO A 89 1SAC 180 FTNOTE 2 1SAC 181 FTNOTE 2 PHE B 33 - THR B 34 OMEGA = 145.17 1SAC 182 FTNOTE 2 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 1SAC 183 FTNOTE 3 1SAC 184 FTNOTE 3 CIS PROLINE - PRO B 89 1SAC 185 FTNOTE 4 1SAC 186 FTNOTE 4 CIS PROLINE - PRO C 89 1SAC 187 FTNOTE 5 1SAC 188 FTNOTE 5 CIS PROLINE - PRO D 89 1SAC 189 FTNOTE 6 1SAC 190 FTNOTE 6 CIS PROLINE - PRO E 89 1SAC 191 FTNOTE 7 1SAC 192 FTNOTE 7 PRO E 129 - LYS E 130 OMEGA = 148.51 1SAC 193 FTNOTE 7 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 1SAC 194 HET CA A 1 3 CALCIUM ION 1SAC 195 HET CA A 2 3 CALCIUM ION 1SAC 196 HET ACY A 300 3 ACETIC ACID 1SAC 197 HET CA B 1 3 CALCIUM ION 1SAC 198 HET CA B 2 3 CALCIUM ION 1SAC 199 HET ACY B 300 3 ACETIC ACID 1SAC 200 HET CA C 1 3 CALCIUM ION 1SAC 201 HET CA C 2 3 CALCIUM ION 1SAC 202 HET CA D 1 3 CALCIUM ION 1SAC 203 HET CA D 2 3 CALCIUM ION 1SAC 204 HET ACY D 300 3 ACETIC ACID 1SAC 205 HET CA E 1 3 CALCIUM ION 1SAC 206 HET CA E 2 3 CALCIUM ION 1SAC 207 HET ACY E 300 3 ACETIC ACID 1SAC 208 FORMUL 6 CA 10(CA1 ++) 1SAC 209 FORMUL 7 ACY 4(C2 H4 O2) 1SAC 210 HELIX 1 H1A ASP A 145 SER A 149 5 1SACA 18 HELIX 2 H2A PRO A 165 GLN A 174 1 1SACA 19 HELIX 3 H1B ASP B 145 SER B 149 5 1SACA 20 HELIX 4 H2B PRO B 165 GLN B 174 1 1SACA 21 HELIX 5 H1C ASP C 145 SER C 149 5 1SACA 22 HELIX 6 H2C PRO C 165 GLN C 174 1 1SACA 23 HELIX 7 H1D ASP D 145 SER D 149 5 1SACA 24 HELIX 8 H2D PRO D 165 GLN D 174 1 1SACA 25 HELIX 9 H1E ASP E 145 SER E 149 5 1SACA 26 HELIX 10 H2E PRO E 165 GLN E 174 1 1SACA 27 SHEET 1 A1A 7 ILE A 197 LEU A 201 0 1SAC 220 SHEET 2 A1A 7 GLY A 6 VAL A 10 -1 N ASP A 18 O LYS A 199 1SAC 221 SHEET 3 A1A 7 GLY A 152 TRP A 160 -1 N ILE A 154 O PHE A 9 1SAC 222 SHEET 4 A1A 7 GLN A 31 TYR A 40 -1 N ARG A 38 O GLY A 155 1SAC 223 SHEET 5 A1A 7 VAL A 92 SER A 100 -1 N ILE A 94 O PHE A 37 1SAC 224 SHEET 6 A1A 7 GLY A 103 ASN A 110 -1 N TRP A 108 O CYS A 95 1SAC 225 SHEET 7 A1A 7 THR A 112 LEU A 119 -1 N LYS A 117 O ALA A 105 1SAC 226 SHEET 1 A2A 7 ILE A 197 LEU A 201 0 1SAC 227 SHEET 2 A2A 7 LEU A 183 TRP A 185 -1 N ASP A 18 O LYS A 199 1SAC 228 SHEET 3 A2A 7 GLY A 152 TRP A 160 -1 N MET A 159 O LEU A 183 1SAC 229 SHEET 4 A2A 7 GLN A 31 TYR A 40 -1 N ARG A 38 O GLY A 155 1SAC 230 SHEET 5 A2A 7 VAL A 92 SER A 100 -1 N ILE A 94 O PHE A 37 1SAC 231 SHEET 6 A2A 7 GLY A 103 ASN A 110 -1 N TRP A 108 O CYS A 95 1SAC 232 SHEET 7 A2A 7 THR A 112 LEU A 119 -1 N LYS A 117 O ALA A 105 1SAC 233 SHEET 1 BA 7 HIS A 78 VAL A 84 0 1SAC 234 SHEET 2 BA 7 GLY A 69 GLY A 76 -1 N TYR A 71 O SER A 82 1SAC 235 SHEET 3 BA 7 GLU A 60 ARG A 67 -1 N TYR A 64 O SER A 72 1SAC 236 SHEET 4 BA 7 TYR A 47 THR A 54 -1 N TYR A 47 O LYS A 65 1SAC 237 SHEET 5 BA 7 LYS A 130 LEU A 133 -1 N VAL A 132 O SER A 51 1SAC 238 SHEET 6 BA 7 HIS A 19 ILE A 23 -1 N VAL A 20 O LEU A 133 1SAC 239 SHEET 7 BA 7 ASN A 189 ARG A 193 -1 N GLU A 191 O ASN A 21 1SAC 240 SHEET 1 A1B 7 ILE B 197 LEU B 201 0 1SAC 241 SHEET 2 A1B 7 GLY B 6 VAL B 10 -1 N ASP B 18 O LYS B 199 1SAC 242 SHEET 3 A1B 7 GLY B 152 TRP B 160 -1 N ILE B 154 O PHE B 9 1SAC 243 SHEET 4 A1B 7 GLN B 31 TYR B 40 -1 N ARG B 38 O GLY B 155 1SAC 244 SHEET 5 A1B 7 VAL B 92 SER B 100 -1 N ILE B 94 O PHE B 37 1SAC 245 SHEET 6 A1B 7 GLY B 103 ASN B 110 -1 N TRP B 108 O CYS B 95 1SAC 246 SHEET 7 A1B 7 THR B 112 LEU B 119 -1 N LYS B 117 O ALA B 105 1SAC 247 SHEET 1 A2B 7 ILE B 197 LEU B 201 0 1SAC 248 SHEET 2 A2B 7 LEU B 183 TRP B 185 -1 N ASP B 18 O LYS B 199 1SAC 249 SHEET 3 A2B 7 GLY B 152 TRP B 160 -1 N MET B 159 O LEU B 183 1SAC 250 SHEET 4 A2B 7 GLN B 31 TYR B 40 -1 N ARG B 38 O GLY B 155 1SAC 251 SHEET 5 A2B 7 VAL B 92 SER B 100 -1 N ILE B 94 O PHE B 37 1SAC 252 SHEET 6 A2B 7 GLY B 103 ASN B 110 -1 N TRP B 108 O CYS B 95 1SAC 253 SHEET 7 A2B 7 THR B 112 LEU B 119 -1 N LYS B 117 O ALA B 105 1SAC 254 SHEET 1 BB 7 HIS B 78 VAL B 84 0 1SAC 255 SHEET 2 BB 7 GLY B 69 GLY B 76 -1 N TYR B 71 O SER B 82 1SAC 256 SHEET 3 BB 7 GLU B 60 ARG B 67 -1 N TYR B 64 O SER B 72 1SAC 257 SHEET 4 BB 7 TYR B 47 THR B 54 -1 N TYR B 47 O LYS B 65 1SAC 258 SHEET 5 BB 7 LYS B 130 LEU B 133 -1 N VAL B 132 O SER B 51 1SAC 259 SHEET 6 BB 7 HIS B 19 ILE B 23 -1 N VAL B 20 O LEU B 133 1SAC 260 SHEET 7 BB 7 ASN B 189 ARG B 193 -1 N GLU B 191 O ASN B 21 1SAC 261 SHEET 1 A1C 7 ILE C 197 LEU C 201 0 1SAC 262 SHEET 2 A1C 7 GLY C 6 VAL C 10 -1 N ASP C 18 O LYS C 199 1SAC 263 SHEET 3 A1C 7 GLY C 152 TRP C 160 -1 N ILE C 154 O PHE C 9 1SAC 264 SHEET 4 A1C 7 GLN C 31 TYR C 40 -1 N ARG C 38 O GLY C 155 1SAC 265 SHEET 5 A1C 7 VAL C 92 SER C 100 -1 N ILE C 94 O PHE C 37 1SAC 266 SHEET 6 A1C 7 GLY C 103 ASN C 110 -1 N TRP C 108 O CYS C 95 1SAC 267 SHEET 7 A1C 7 THR C 112 LEU C 119 -1 N LYS C 117 O ALA C 105 1SAC 268 SHEET 1 A2C 7 ILE C 197 LEU C 201 0 1SAC 269 SHEET 2 A2C 7 LEU C 183 TRP C 185 -1 N ASP C 18 O LYS C 199 1SAC 270 SHEET 3 A2C 7 GLY C 152 TRP C 160 -1 N MET C 159 O LEU C 183 1SAC 271 SHEET 4 A2C 7 GLN C 31 TYR C 40 -1 N ARG C 38 O GLY C 155 1SAC 272 SHEET 5 A2C 7 VAL C 92 SER C 100 -1 N ILE C 94 O PHE C 37 1SAC 273 SHEET 6 A2C 7 GLY C 103 ASN C 110 -1 N TRP C 108 O CYS C 95 1SAC 274 SHEET 7 A2C 7 THR C 112 LEU C 119 -1 N LYS C 117 O ALA C 105 1SAC 275 SHEET 1 BC 7 HIS C 78 VAL C 84 0 1SAC 276 SHEET 2 BC 7 GLY C 69 GLY C 76 -1 N TYR C 71 O SER C 82 1SAC 277 SHEET 3 BC 7 GLU C 60 ARG C 67 -1 N TYR C 64 O SER C 72 1SAC 278 SHEET 4 BC 7 TYR C 47 THR C 54 -1 N TYR C 47 O LYS C 65 1SAC 279 SHEET 5 BC 7 LYS C 130 LEU C 133 -1 N VAL C 132 O SER C 51 1SAC 280 SHEET 6 BC 7 HIS C 19 ILE C 23 -1 N VAL C 20 O LEU C 133 1SAC 281 SHEET 7 BC 7 ASN C 189 ARG C 193 -1 N GLU C 191 O ASN C 21 1SAC 282 SHEET 1 A1D 7 ILE D 197 LEU D 201 0 1SAC 283 SHEET 2 A1D 7 GLY D 6 VAL D 10 -1 N ASP D 18 O LYS D 199 1SAC 284 SHEET 3 A1D 7 GLY D 152 TRP D 160 -1 N ILE D 154 O PHE D 9 1SAC 285 SHEET 4 A1D 7 GLN D 31 TYR D 40 -1 N ARG D 38 O GLY D 155 1SAC 286 SHEET 5 A1D 7 VAL D 92 SER D 100 -1 N ILE D 94 O PHE D 37 1SAC 287 SHEET 6 A1D 7 GLY D 103 ASN D 110 -1 N TRP D 108 O CYS D 95 1SAC 288 SHEET 7 A1D 7 THR D 112 LEU D 119 -1 N LYS D 117 O ALA D 105 1SAC 289 SHEET 1 A2D 7 ILE D 197 LEU D 201 0 1SAC 290 SHEET 2 A2D 7 LEU D 183 TRP D 185 -1 N ASP D 18 O LYS D 199 1SAC 291 SHEET 3 A2D 7 GLY D 152 TRP D 160 -1 N MET D 159 O LEU D 183 1SAC 292 SHEET 4 A2D 7 GLN D 31 TYR D 40 -1 N ARG D 38 O GLY D 155 1SAC 293 SHEET 5 A2D 7 VAL D 92 SER D 100 -1 N ILE D 94 O PHE D 37 1SAC 294 SHEET 6 A2D 7 GLY D 103 ASN D 110 -1 N TRP D 108 O CYS D 95 1SAC 295 SHEET 7 A2D 7 THR D 112 LEU D 119 -1 N LYS D 117 O ALA D 105 1SAC 296 SHEET 1 BD 7 HIS D 78 VAL D 84 0 1SAC 297 SHEET 2 BD 7 GLY D 69 GLY D 76 -1 N TYR D 71 O SER D 82 1SAC 298 SHEET 3 BD 7 GLU D 60 ARG D 67 -1 N TYR D 64 O SER D 72 1SAC 299 SHEET 4 BD 7 TYR D 47 THR D 54 -1 N TYR D 47 O LYS D 65 1SAC 300 SHEET 5 BD 7 LYS D 130 LEU D 133 -1 N VAL D 132 O SER D 51 1SAC 301 SHEET 6 BD 7 HIS D 19 ILE D 23 -1 N VAL D 20 O LEU D 133 1SAC 302 SHEET 7 BD 7 ASN D 189 ARG D 193 -1 N GLU D 191 O ASN D 21 1SAC 303 SHEET 1 A1E 7 ILE E 197 LEU E 201 0 1SAC 304 SHEET 2 A1E 7 GLY E 6 VAL E 10 -1 N ASP E 18 O LYS E 199 1SAC 305 SHEET 3 A1E 7 GLY E 152 TRP E 160 -1 N ILE E 154 O PHE E 9 1SAC 306 SHEET 4 A1E 7 GLN E 31 TYR E 40 -1 N ARG E 38 O GLY E 155 1SAC 307 SHEET 5 A1E 7 VAL E 92 SER E 100 -1 N ILE E 94 O PHE E 37 1SAC 308 SHEET 6 A1E 7 GLY E 103 ASN E 110 -1 N TRP E 108 O CYS E 95 1SAC 309 SHEET 7 A1E 7 THR E 112 LEU E 119 -1 N LYS E 117 O ALA E 105 1SAC 310 SHEET 1 A2E 7 ILE E 197 LEU E 201 0 1SAC 311 SHEET 2 A2E 7 LEU E 183 TRP E 185 -1 N ASP E 18 O LYS E 199 1SAC 312 SHEET 3 A2E 7 GLY E 152 TRP E 160 -1 N MET E 159 O LEU E 183 1SAC 313 SHEET 4 A2E 7 GLN E 31 TYR E 40 -1 N ARG E 38 O GLY E 155 1SAC 314 SHEET 5 A2E 7 VAL E 92 SER E 100 -1 N ILE E 94 O PHE E 37 1SAC 315 SHEET 6 A2E 7 GLY E 103 ASN E 110 -1 N TRP E 108 O CYS E 95 1SAC 316 SHEET 7 A2E 7 THR E 112 LEU E 119 -1 N LYS E 117 O ALA E 105 1SAC 317 SHEET 1 BE 7 HIS E 78 VAL E 84 0 1SAC 318 SHEET 2 BE 7 GLY E 69 GLY E 76 -1 N TYR E 71 O SER E 82 1SAC 319 SHEET 3 BE 7 GLU E 60 ARG E 67 -1 N TYR E 64 O SER E 72 1SAC 320 SHEET 4 BE 7 TYR E 47 THR E 54 -1 N TYR E 47 O LYS E 65 1SAC 321 SHEET 5 BE 7 LYS E 130 LEU E 133 -1 N VAL E 132 O SER E 51 1SAC 322 SHEET 6 BE 7 HIS E 19 ILE E 23 -1 N VAL E 20 O LEU E 133 1SAC 323 SHEET 7 BE 7 ASN E 189 ARG E 193 -1 N GLU E 191 O ASN E 21 1SAC 324 SSBOND 1 CYS A 36 CYS A 95 1SAC 325 SSBOND 2 CYS B 36 CYS B 95 1SACA 28 SSBOND 3 CYS C 36 CYS C 95 1SACA 29 SSBOND 4 CYS D 36 CYS D 95 1SACA 30 SSBOND 5 CYS E 36 CYS E 95 1SACA 31 SITE 1 C1A 6 ASP A 58 ASN A 59 GLU A 136 GLN A 137 1SACA 32 SITE 2 C1A 6 ASP A 138 ACY A 300 1SACA 33 SITE 1 C2A 4 GLU A 136 ASP A 138 GLN A 148 ACY A 300 1SACA 34 SITE 1 C1B 6 ASP B 58 ASN B 59 GLU B 136 GLN B 137 1SACA 35 SITE 2 C1B 6 ASP B 138 ACY B 300 1SACA 36 SITE 1 C2B 4 GLU B 136 ASP B 138 GLN B 148 ACY B 300 1SACA 37 SITE 1 C1C 5 ASP C 58 ASN C 59 GLU C 136 GLN C 137 1SACA 38 SITE 2 C1C 5 ASP C 138 1SACA 39 SITE 1 C2C 3 GLU C 136 ASP C 138 GLN C 148 1SACA 40 SITE 1 C1D 6 ASP D 58 ASN D 59 GLU D 136 GLN D 137 1SACA 41 SITE 2 C1D 6 ASP D 138 ACY D 300 1SACA 42 SITE 1 C2D 4 GLU D 136 ASP D 138 GLN D 148 ACY D 300 1SACA 43 SITE 1 C1E 6 ASP E 58 ASN E 59 GLU E 136 GLN E 137 1SACA 44 SITE 2 C1E 6 ASP E 138 ACY E 300 1SACA 45 SITE 1 C2E 4 GLU E 136 ASP E 138 GLN E 148 ACY E 300 1SACA 46 CRYST1 68.900 99.300 96.700 90.00 95.90 90.00 P 21 10 1SAC 341 ORIGX1 1.000000 0.000000 0.000000 0.00000 1SAC 342 ORIGX2 0.000000 1.000000 0.000000 0.00000 1SAC 343 ORIGX3 0.000000 0.000000 1.000000 0.00000 1SAC 344 SCALE1 0.014514 0.000000 0.001500 0.00000 1SAC 345 SCALE2 0.000000 0.010070 0.000000 0.00000 1SAC 346 SCALE3 0.000000 0.000000 0.010396 0.00000 1SAC 347 MTRIX1 1 0.499031 -0.291022 0.816257 6.60979 1 1SAC 348 MTRIX2 1 -0.320116 0.813396 0.485709 4.55958 1 1SAC 349 MTRIX3 1 -0.805291 -0.503680 0.312749 41.24557 1 1SAC 350 MTRIX1 2 -0.310617 -0.777136 0.547336 41.93763 1 1SAC 351 MTRIX2 2 -0.819014 0.511060 0.260832 26.04455 1 1SAC 352 MTRIX3 2 -0.482423 -0.367257 -0.795229 47.15978 1 1SAC 353 MTRIX1 3 -0.354165 -0.796676 -0.489770 57.58439 1 1SAC 354 MTRIX2 3 -0.766242 0.547449 -0.336411 34.00153 1 1SAC 355 MTRIX3 3 0.536135 0.256137 -0.804334 9.05447 1 1SAC 356 MTRIX1 4 0.495935 -0.324849 -0.805309 31.44690 1 1SAC 357 MTRIX2 4 -0.289427 0.812525 -0.505999 19.33460 1 1SAC 358 MTRIX3 4 0.818707 0.484020 0.308939 -20.40029 1 1SAC 359 ATOM 1 N HIS A 1 48.948 45.622 46.489 1.00 39.94 1SAC 360 ATOM 2 CA HIS A 1 49.531 44.368 45.990 1.00 37.57 1SAC 361 ATOM 3 C HIS A 1 48.718 43.176 46.503 1.00 35.75 1SAC 362 ATOM 4 O HIS A 1 49.110 42.503 47.467 1.00 36.32 1SAC 363 ATOM 5 CB HIS A 1 50.980 44.241 46.472 1.00 39.85 1SAC 364 ATOM 6 CG HIS A 1 51.785 43.154 45.745 1.00 42.98 1SAC 365 ATOM 7 ND1 HIS A 1 51.419 41.811 45.785 1.00 43.10 1SAC 366 ATOM 8 CD2 HIS A 1 52.914 43.212 44.985 1.00 44.28 1SAC 367 ATOM 9 CE1 HIS A 1 52.300 41.120 45.081 1.00 44.24 1SAC 368 ATOM 10 NE2 HIS A 1 53.198 41.941 44.599 1.00 44.80 1SAC 369 ATOM 11 N THR A 2 47.506 43.088 45.935 1.00 32.61 1SAC 370 ATOM 12 CA THR A 2 46.557 42.013 46.228 1.00 29.25 1SAC 371 ATOM 13 C THR A 2 46.365 41.163 44.974 1.00 26.94 1SAC 372 ATOM 14 O THR A 2 46.289 41.693 43.854 1.00 24.60 1SAC 373 ATOM 15 CB THR A 2 45.199 42.579 46.637 1.00 29.75 1SAC 374 ATOM 16 OG1 THR A 2 45.359 43.523 47.683 1.00 32.05 1SAC 375 ATOM 17 CG2 THR A 2 44.239 41.496 47.133 1.00 29.73 1SAC 376 ATOM 18 N ASP A 3 46.450 39.877 45.140 1.00 25.03 1SAC 377 ATOM 19 CA ASP A 3 46.099 38.931 44.067 1.00 24.43 1SAC 378 ATOM 20 C ASP A 3 44.593 38.798 43.947 1.00 23.70 1SAC 379 ATOM 21 O ASP A 3 43.966 38.171 44.798 1.00 23.38 1SAC 380 ATOM 22 CB ASP A 3 46.725 37.566 44.333 1.00 26.63 1SAC 381 ATOM 23 CG ASP A 3 46.646 36.643 43.122 1.00 27.50 1SAC 382 ATOM 24 OD1 ASP A 3 46.024 36.996 42.110 1.00 25.36 1SAC 383 ATOM 25 OD2 ASP A 3 47.216 35.540 43.169 1.00 30.41 1SAC 384 ATOM 26 N LEU A 4 44.013 39.407 42.923 1.00 21.80 1SAC 385 ATOM 27 CA LEU A 4 42.552 39.337 42.760 1.00 20.65 1SAC 386 ATOM 28 C LEU A 4 42.161 38.214 41.798 1.00 19.68 1SAC 387 ATOM 29 O LEU A 4 41.020 38.197 41.332 1.00 20.58 1SAC 388 ATOM 30 CB LEU A 4 42.001 40.651 42.254 1.00 21.26 1SAC 389 ATOM 31 CG LEU A 4 41.429 41.552 43.316 1.00 22.31 1SAC 390 ATOM 32 CD1 LEU A 4 41.520 41.012 44.720 1.00 22.91 1SAC 391 ATOM 33 CD2 LEU A 4 41.853 43.001 43.207 1.00 22.03 1SAC 392 ATOM 34 N SER A 5 43.056 37.302 41.485 1.00 19.13 1SAC 393 ATOM 35 CA SER A 5 42.807 36.089 40.700 1.00 19.22 1SAC 394 ATOM 36 C SER A 5 41.487 35.435 41.088 1.00 19.21 1SAC 395 ATOM 37 O SER A 5 41.311 35.097 42.256 1.00 18.60 1SAC 396 ATOM 38 CB SER A 5 43.935 35.089 40.879 1.00 19.50 1SAC 397 ATOM 39 OG SER A 5 45.052 35.437 40.067 1.00 23.76 1SAC 398 ATOM 40 N GLY A 6 40.581 35.299 40.139 1.00 18.47 1SAC 399 ATOM 41 CA GLY A 6 39.293 34.627 40.360 1.00 18.63 1SAC 400 ATOM 42 C GLY A 6 38.268 35.512 41.043 1.00 18.58 1SAC 401 ATOM 43 O GLY A 6 37.160 35.059 41.352 1.00 18.17 1SAC 402 ATOM 44 N LYS A 7 38.591 36.773 41.298 1.00 19.39 1SAC 403 ATOM 45 CA LYS A 7 37.611 37.680 41.905 1.00 19.63 1SAC 404 ATOM 46 C LYS A 7 37.197 38.764 40.917 1.00 18.38 1SAC 405 ATOM 47 O LYS A 7 37.905 39.084 39.970 1.00 16.88 1SAC 406 ATOM 48 CB LYS A 7 38.150 38.324 43.163 1.00 23.68 1SAC 407 ATOM 49 CG LYS A 7 38.650 37.196 44.022 1.00 29.57 1SAC 408 ATOM 50 CD LYS A 7 39.372 36.234 44.940 1.00 35.32 1SAC 409 ATOM 51 CE LYS A 7 40.087 35.984 46.258 1.00 37.45 1SAC 410 ATOM 52 NZ LYS A 7 41.451 35.581 46.626 1.00 42.84 1SAC 411 ATOM 53 N VAL A 8 36.088 39.332 41.246 1.00 17.25 1SAC 412 ATOM 54 CA VAL A 8 35.726 40.583 40.570 1.00 15.82 1SAC 413 ATOM 55 C VAL A 8 35.352 41.659 41.562 1.00 14.53 1SAC 414 ATOM 56 O VAL A 8 35.131 41.396 42.749 1.00 14.54 1SAC 415 ATOM 57 CB VAL A 8 34.458 40.412 39.715 1.00 15.81 1SAC 416 ATOM 58 CG1 VAL A 8 34.684 39.577 38.461 1.00 16.08 1SAC 417 ATOM 59 CG2 VAL A 8 33.301 39.737 40.469 1.00 16.41 1SAC 418 ATOM 60 N PHE A 9 35.310 42.841 41.030 1.00 13.11 1SAC 419 ATOM 61 CA PHE A 9 34.767 43.965 41.749 1.00 13.85 1SAC 420 ATOM 62 C PHE A 9 33.328 44.076 41.316 1.00 13.69 1SAC 421 ATOM 63 O PHE A 9 33.012 43.929 40.126 1.00 13.74 1SAC 422 ATOM 64 CB PHE A 9 35.406 45.277 41.337 1.00 14.60 1SAC 423 ATOM 65 CG PHE A 9 36.808 45.495 41.860 1.00 15.56 1SAC 424 ATOM 66 CD1 PHE A 9 37.103 45.287 43.211 1.00 16.86 1SAC 425 ATOM 67 CD2 PHE A 9 37.788 45.917 40.968 1.00 14.73 1SAC 426 ATOM 68 CE1 PHE A 9 38.407 45.505 43.671 1.00 17.11 1SAC 427 ATOM 69 CE2 PHE A 9 39.090 46.134 41.425 1.00 14.37 1SAC 428 ATOM 70 CZ PHE A 9 39.401 45.928 42.777 1.00 16.77 1SAC 429 ATOM 71 N VAL A 10 32.468 44.322 42.257 1.00 12.80 1SAC 430 ATOM 72 CA VAL A 10 31.060 44.521 41.930 1.00 13.42 1SAC 431 ATOM 73 C VAL A 10 30.539 45.765 42.640 1.00 13.75 1SAC 432 ATOM 74 O VAL A 10 30.710 45.927 43.855 1.00 14.13 1SAC 433 ATOM 75 CB VAL A 10 30.213 43.316 42.328 1.00 12.37 1SAC 434 ATOM 76 CG1 VAL A 10 30.902 42.383 43.318 1.00 10.90 1SAC 435 ATOM 77 CG2 VAL A 10 28.889 43.721 42.982 1.00 10.42 1SAC 436 ATOM 78 N PHE A 11 30.313 46.705 41.767 1.00 13.73 1SAC 437 ATOM 79 CA PHE A 11 29.523 47.927 41.973 1.00 12.87 1SAC 438 ATOM 80 C PHE A 11 28.043 47.560 41.925 1.00 13.75 1SAC 439 ATOM 81 O PHE A 11 27.420 47.558 40.856 1.00 15.56 1SAC 440 ATOM 82 CB PHE A 11 29.902 48.948 40.904 1.00 12.23 1SAC 441 ATOM 83 CG PHE A 11 31.421 49.079 40.741 1.00 11.16 1SAC 442 ATOM 84 CD1 PHE A 11 32.121 48.185 39.918 1.00 12.50 1SAC 443 ATOM 85 CD2 PHE A 11 32.114 50.090 41.418 1.00 11.23 1SAC 444 ATOM 86 CE1 PHE A 11 33.510 48.304 39.775 1.00 11.81 1SAC 445 ATOM 87 CE2 PHE A 11 33.502 50.208 41.275 1.00 10.69 1SAC 446 ATOM 88 CZ PHE A 11 34.200 49.315 40.453 1.00 12.29 1SAC 447 ATOM 89 N PRO A 12 27.440 47.248 43.073 1.00 14.64 1SAC 448 ATOM 90 CA PRO A 12 26.079 46.743 43.174 1.00 14.34 1SAC 449 ATOM 91 C PRO A 12 25.012 47.780 43.000 1.00 15.67 1SAC 450 ATOM 92 O PRO A 12 23.801 47.430 42.973 1.00 17.40 1SAC 451 ATOM 93 CB PRO A 12 26.022 46.156 44.562 1.00 15.96 1SAC 452 ATOM 94 CG PRO A 12 27.434 46.206 45.065 1.00 14.72 1SAC 453 ATOM 95 CD PRO A 12 28.060 47.356 44.370 1.00 14.96 1SAC 454 ATOM 96 N ARG A 13 25.342 49.032 42.876 1.00 15.51 1SAC 455 ATOM 97 CA ARG A 13 24.265 50.008 42.684 1.00 17.92 1SAC 456 ATOM 98 C ARG A 13 24.771 51.264 42.016 1.00 18.77 1SAC 457 ATOM 99 O ARG A 13 25.980 51.528 41.987 1.00 19.67 1SAC 458 ATOM 100 CB ARG A 13 23.628 50.375 44.023 1.00 20.22 1SAC 459 ATOM 101 CG ARG A 13 24.647 50.813 45.070 1.00 22.51 1SAC 460 ATOM 102 CD ARG A 13 24.337 52.186 45.664 1.00 26.88 1SAC 461 ATOM 103 NE ARG A 13 25.480 52.764 46.380 1.00 28.79 1SAC 462 ATOM 104 CZ ARG A 13 25.522 52.936 47.706 1.00 30.34 1SAC 463 ATOM 105 NH1 ARG A 13 24.488 52.583 48.481 1.00 31.99 1SAC 464 ATOM 106 NH2 ARG A 13 26.569 53.459 48.358 1.00 30.06 1SAC 465 ATOM 107 N GLU A 14 23.805 51.985 41.498 1.00 20.04 1SAC 466 ATOM 108 CA GLU A 14 24.047 53.251 40.826 1.00 20.68 1SAC 467 ATOM 109 C GLU A 14 24.243 54.349 41.868 1.00 21.00 1SAC 468 ATOM 110 O GLU A 14 23.564 54.372 42.905 1.00 19.97 1SAC 469 ATOM 111 CB GLU A 14 22.859 53.608 39.952 1.00 20.89 1SAC 470 ATOM 112 CG GLU A 14 23.196 54.683 38.933 1.00 23.97 1SAC 471 ATOM 113 CD GLU A 14 21.990 55.073 38.100 1.00 26.09 1SAC 472 ATOM 114 OE1 GLU A 14 21.121 55.890 38.580 1.00 27.71 1SAC 473 ATOM 115 OE2 GLU A 14 21.841 54.576 36.924 1.00 28.84 1SAC 474 ATOM 116 N SER A 15 25.236 55.160 41.665 1.00 20.36 1SAC 475 ATOM 117 CA SER A 15 25.594 56.203 42.632 1.00 21.06 1SAC 476 ATOM 118 C SER A 15 26.490 57.241 41.980 1.00 22.16 1SAC 477 ATOM 119 O SER A 15 26.858 57.108 40.815 1.00 22.36 1SAC 478 ATOM 120 CB SER A 15 26.246 55.627 43.861 1.00 20.00 1SAC 479 ATOM 121 OG SER A 15 27.620 55.306 43.621 1.00 20.03 1SAC 480 ATOM 122 N VAL A 16 26.858 58.232 42.723 1.00 22.69 1SAC 481 ATOM 123 CA VAL A 16 27.942 59.096 42.235 1.00 22.69 1SAC 482 ATOM 124 C VAL A 16 29.104 59.092 43.230 1.00 22.39 1SAC 483 ATOM 125 O VAL A 16 29.971 59.970 43.222 1.00 22.89 1SAC 484 ATOM 126 CB VAL A 16 27.432 60.536 42.068 1.00 24.67 1SAC 485 ATOM 127 CG1 VAL A 16 27.254 61.276 43.397 1.00 24.79 1SAC 486 ATOM 128 CG2 VAL A 16 28.369 61.413 41.232 1.00 23.96 1SAC 487 ATOM 129 N THR A 17 29.139 58.085 44.076 1.00 22.02 1SAC 488 ATOM 130 CA THR A 17 30.175 58.031 45.108 1.00 24.75 1SAC 489 ATOM 131 C THR A 17 31.072 56.798 44.985 1.00 23.28 1SAC 490 ATOM 132 O THR A 17 32.302 56.894 45.078 1.00 24.03 1SAC 491 ATOM 133 CB THR A 17 29.532 58.019 46.488 1.00 27.05 1SAC 492 ATOM 134 OG1 THR A 17 28.229 57.462 46.413 1.00 30.67 1SAC 493 ATOM 135 CG2 THR A 17 29.398 59.419 47.093 1.00 29.80 1SAC 494 ATOM 136 N ASP A 18 30.451 55.657 44.791 1.00 21.81 1SAC 495 ATOM 137 CA ASP A 18 31.180 54.381 44.709 1.00 20.54 1SAC 496 ATOM 138 C ASP A 18 32.178 54.402 43.548 1.00 20.06 1SAC 497 ATOM 139 O ASP A 18 31.794 54.442 42.373 1.00 20.20 1SAC 498 ATOM 140 CB ASP A 18 30.194 53.232 44.529 1.00 20.81 1SAC 499 ATOM 141 CG ASP A 18 29.096 53.234 45.592 1.00 23.78 1SAC 500 ATOM 142 OD1 ASP A 18 29.379 53.546 46.812 1.00 22.67 1SAC 501 ATOM 143 OD2 ASP A 18 27.887 52.929 45.268 1.00 22.10 1SAC 502 ATOM 144 N HIS A 19 33.433 54.101 43.987 1.00 18.96 1SAC 503 ATOM 145 CA HIS A 19 34.421 53.826 42.933 1.00 17.96 1SAC 504 ATOM 146 C HIS A 19 35.659 53.163 43.539 1.00 17.85 1SAC 505 ATOM 147 O HIS A 19 35.735 52.944 44.757 1.00 17.00 1SAC 506 ATOM 148 CB HIS A 19 34.835 55.133 42.250 1.00 17.20 1SAC 507 ATOM 149 CG HIS A 19 35.489 56.138 43.205 1.00 16.97 1SAC 508 ATOM 150 ND1 HIS A 19 34.741 56.916 44.085 1.00 17.12 1SAC 509 ATOM 151 CD2 HIS A 19 36.789 56.484 43.408 1.00 17.05 1SAC 510 ATOM 152 CE1 HIS A 19 35.573 57.682 44.769 1.00 17.67 1SAC 511 ATOM 153 NE2 HIS A 19 36.798 57.437 44.377 1.00 16.20 1SAC 512 ATOM 154 N VAL A 20 36.514 52.672 42.648 1.00 17.18 1SAC 513 ATOM 155 CA VAL A 20 37.858 52.209 43.003 1.00 16.90 1SAC 514 ATOM 156 C VAL A 20 38.930 53.042 42.338 1.00 17.93 1SAC 515 ATOM 157 O VAL A 20 38.896 53.310 41.139 1.00 18.44 1SAC 516 ATOM 158 CB VAL A 20 38.008 50.734 42.623 1.00 13.68 1SAC 517 ATOM 159 CG1 VAL A 20 39.420 50.242 42.943 1.00 13.09 1SAC 518 ATOM 160 CG2 VAL A 20 36.978 49.837 43.329 1.00 14.99 1SAC 519 ATOM 161 N ASN A 21 39.884 53.497 43.100 1.00 17.18 1SAC 520 ATOM 162 CA ASN A 21 41.111 54.094 42.553 1.00 17.87 1SAC 521 ATOM 163 C ASN A 21 42.148 53.004 42.291 1.00 18.13 1SAC 522 ATOM 164 O ASN A 21 42.434 52.174 43.164 1.00 18.05 1SAC 523 ATOM 165 CB ASN A 21 41.679 55.106 43.545 1.00 19.13 1SAC 524 ATOM 166 CG ASN A 21 40.646 56.154 43.944 1.00 20.34 1SAC 525 ATOM 167 OD1 ASN A 21 39.723 56.423 43.173 1.00 21.29 1SAC 526 ATOM 168 ND2 ASN A 21 40.740 56.764 45.107 1.00 22.58 1SAC 527 ATOM 169 N LEU A 22 42.636 53.035 41.074 1.00 19.51 1SAC 528 ATOM 170 CA LEU A 22 43.717 52.109 40.685 1.00 19.48 1SAC 529 ATOM 171 C LEU A 22 45.067 52.832 40.763 1.00 19.09 1SAC 530 ATOM 172 O LEU A 22 45.169 53.932 40.230 1.00 18.49 1SAC 531 ATOM 173 CB LEU A 22 43.486 51.613 39.266 1.00 20.14 1SAC 532 ATOM 174 CG LEU A 22 42.914 50.223 39.163 1.00 21.00 1SAC 533 ATOM 175 CD1 LEU A 22 41.968 49.813 40.266 1.00 21.08 1SAC 534 ATOM 176 CD2 LEU A 22 42.375 49.848 37.798 1.00 19.49 1SAC 535 ATOM 177 N ILE A 23 46.047 52.243 41.427 1.00 19.89 1SAC 536 ATOM 178 CA ILE A 23 47.257 53.005 41.775 1.00 20.65 1SAC 537 ATOM 179 C ILE A 23 48.451 52.530 40.964 1.00 21.17 1SAC 538 ATOM 180 O ILE A 23 48.809 51.362 41.108 1.00 22.31 1SAC 539 ATOM 181 CB ILE A 23 47.564 52.862 43.262 1.00 21.52 1SAC 540 ATOM 182 CG1 ILE A 23 46.425 53.410 44.107 1.00 20.97 1SAC 541 ATOM 183 CG2 ILE A 23 48.882 53.537 43.607 1.00 21.13 1SAC 542 ATOM 184 CD1 ILE A 23 46.374 54.930 44.124 1.00 23.64 1SAC 543 ATOM 185 N THR A 24 49.050 53.405 40.156 1.00 22.77 1SAC 544 ATOM 186 CA THR A 24 50.277 52.980 39.467 1.00 24.22 1SAC 545 ATOM 187 C THR A 24 51.283 54.134 39.431 1.00 25.49 1SAC 546 ATOM 188 O THR A 24 50.910 55.305 39.270 1.00 26.55 1SAC 547 ATOM 189 CB THR A 24 49.948 52.553 38.035 1.00 24.95 1SAC 548 ATOM 190 OG1 THR A 24 51.132 52.150 37.363 1.00 24.80 1SAC 549 ATOM 191 CG2 THR A 24 49.309 53.672 37.212 1.00 22.24 1SAC 550 ATOM 192 N PRO A 25 52.570 53.829 39.646 1.00 27.55 1SAC 551 ATOM 193 CA PRO A 25 53.715 54.725 39.612 1.00 28.94 1SAC 552 ATOM 194 C PRO A 25 54.216 54.892 38.201 1.00 30.14 1SAC 553 ATOM 195 O PRO A 25 55.416 54.576 37.934 1.00 32.04 1SAC 554 ATOM 196 CB PRO A 25 54.706 54.018 40.477 1.00 28.95 1SAC 555 ATOM 197 CG PRO A 25 54.401 52.565 40.262 1.00 28.38 1SAC 556 ATOM 198 CD PRO A 25 52.918 52.479 40.079 1.00 27.92 1SAC 557 ATOM 199 N LEU A 26 53.303 55.354 37.393 1.00 30.48 1SAC 558 ATOM 200 CA LEU A 26 53.490 55.691 35.976 1.00 30.59 1SAC 559 ATOM 201 C LEU A 26 54.088 57.105 35.934 1.00 31.18 1SAC 560 ATOM 202 O LEU A 26 53.351 58.102 35.963 1.00 32.00 1SAC 561 ATOM 203 CB LEU A 26 52.086 55.676 35.357 1.00 30.54 1SAC 562 ATOM 204 CG LEU A 26 52.032 55.612 33.837 1.00 29.87 1SAC 563 ATOM 205 CD1 LEU A 26 53.140 54.762 33.229 1.00 28.55 1SAC 564 ATOM 206 CD2 LEU A 26 50.714 55.017 33.322 1.00 28.45 1SAC 565 ATOM 207 N GLU A 27 55.412 57.164 35.888 1.00 31.86 1SAC 566 ATOM 208 CA GLU A 27 56.150 58.446 35.931 1.00 33.38 1SAC 567 ATOM 209 C GLU A 27 56.714 58.817 34.554 1.00 31.98 1SAC 568 ATOM 210 O GLU A 27 57.159 59.961 34.336 1.00 32.32 1SAC 569 ATOM 211 CB GLU A 27 57.297 58.338 36.949 1.00 37.39 1SAC 570 ATOM 212 CG GLU A 27 56.820 57.824 38.315 1.00 43.81 1SAC 571 ATOM 213 CD GLU A 27 57.829 58.033 39.454 1.00 49.13 1SAC 572 ATOM 214 OE1 GLU A 27 59.006 57.508 39.382 1.00 52.58 1SAC 573 ATOM 215 OE2 GLU A 27 57.499 58.726 40.494 1.00 52.67 1SAC 574 ATOM 216 N LYS A 28 56.477 58.056 33.483 1.00 29.94 1SAC 575 ATOM 217 CA LYS A 28 56.890 58.450 32.104 1.00 28.91 1SAC 576 ATOM 218 C LYS A 28 55.679 58.331 31.134 1.00 25.45 1SAC 577 ATOM 219 O LYS A 28 54.864 57.402 31.228 1.00 23.47 1SAC 578 ATOM 220 CB LYS A 28 58.126 57.620 31.667 1.00 31.66 1SAC 579 ATOM 221 CG LYS A 28 57.814 56.225 31.119 1.00 37.25 1SAC 580 ATOM 222 CD LYS A 28 58.015 55.100 32.145 1.00 39.57 1SAC 581 ATOM 223 CE LYS A 28 56.707 54.368 32.456 1.00 42.01 1SAC 582 ATOM 224 NZ LYS A 28 56.658 52.998 31.922 1.00 43.84 1SAC 583 ATOM 225 N PRO A 29 55.480 59.275 30.168 1.00 23.18 1SAC 584 ATOM 226 CA PRO A 29 54.351 59.245 29.228 1.00 21.24 1SAC 585 ATOM 227 C PRO A 29 54.324 57.954 28.461 1.00 18.85 1SAC 586 ATOM 228 O PRO A 29 55.424 57.373 28.200 1.00 18.35 1SAC 587 ATOM 229 CB PRO A 29 54.611 60.422 28.320 1.00 20.73 1SAC 588 ATOM 230 CG PRO A 29 55.512 61.326 29.108 1.00 22.48 1SAC 589 ATOM 231 CD PRO A 29 56.354 60.423 29.953 1.00 22.41 1SAC 590 ATOM 232 N LEU A 30 53.100 57.567 28.141 1.00 17.74 1SAC 591 ATOM 233 CA LEU A 30 52.798 56.342 27.383 1.00 18.46 1SAC 592 ATOM 234 C LEU A 30 52.928 56.619 25.884 1.00 18.89 1SAC 593 ATOM 235 O LEU A 30 52.277 57.532 25.348 1.00 19.16 1SAC 594 ATOM 236 CB LEU A 30 51.356 55.899 27.663 1.00 18.86 1SAC 595 ATOM 237 CG LEU A 30 51.238 54.764 28.688 1.00 19.41 1SAC 596 ATOM 238 CD1 LEU A 30 52.487 54.595 29.553 1.00 18.58 1SAC 597 ATOM 239 CD2 LEU A 30 50.079 54.969 29.670 1.00 18.41 1SAC 598 ATOM 240 N GLN A 31 53.608 55.809 25.057 1.00 19.69 1SAC 599 ATOM 241 CA GLN A 31 53.554 55.941 23.594 1.00 21.69 1SAC 600 ATOM 242 C GLN A 31 52.659 54.842 23.014 1.00 21.27 1SAC 601 ATOM 243 O GLN A 31 51.971 55.044 22.007 1.00 20.29 1SAC 602 ATOM 244 CB GLN A 31 54.959 55.853 23.022 1.00 23.65 1SAC 603 ATOM 245 CG GLN A 31 55.864 56.971 23.536 1.00 28.32 1SAC 604 ATOM 246 CD GLN A 31 57.312 56.801 23.095 1.00 30.45 1SAC 605 ATOM 247 OE1 GLN A 31 57.560 56.406 21.958 1.00 33.81 1SAC 606 ATOM 248 NE2 GLN A 31 58.291 57.076 23.933 1.00 30.75 1SAC 607 ATOM 249 N ASN A 32 52.706 53.691 23.661 1.00 20.40 1SAC 608 ATOM 250 CA ASN A 32 51.819 52.562 23.327 1.00 19.96 1SAC 609 ATOM 251 C ASN A 32 51.336 51.905 24.623 1.00 17.87 1SAC 610 ATOM 252 O ASN A 32 51.956 52.061 25.687 1.00 16.77 1SAC 611 ATOM 253 CB ASN A 32 52.488 51.467 22.463 1.00 23.87 1SAC 612 ATOM 254 CG ASN A 32 53.909 51.754 21.966 1.00 27.68 1SAC 613 ATOM 255 OD1 ASN A 32 54.088 52.327 20.891 1.00 32.43 1SAC 614 ATOM 256 ND2 ASN A 32 54.948 51.355 22.677 1.00 29.90 1SAC 615 ATOM 257 N PHE A 33 50.232 51.189 24.497 1.00 14.92 1SAC 616 ATOM 258 CA PHE A 33 49.607 50.478 25.628 1.00 13.79 1SAC 617 ATOM 259 C PHE A 33 48.515 49.533 25.125 1.00 13.19 1SAC 618 ATOM 260 O PHE A 33 47.950 49.729 24.041 1.00 13.52 1SAC 619 ATOM 261 CB PHE A 33 48.982 51.481 26.607 1.00 11.92 1SAC 620 ATOM 262 CG PHE A 33 47.642 52.061 26.131 1.00 10.78 1SAC 621 ATOM 263 CD1 PHE A 33 46.461 51.312 26.255 1.00 11.28 1SAC 622 ATOM 264 CD2 PHE A 33 47.591 53.347 25.577 1.00 9.39 1SAC 623 ATOM 265 CE1 PHE A 33 45.239 51.848 25.822 1.00 10.68 1SAC 624 ATOM 266 CE2 PHE A 33 46.370 53.882 25.145 1.00 9.80 1SAC 625 ATOM 267 CZ PHE A 33 45.194 53.133 25.267 1.00 11.05 1SAC 626 ATOM 268 N THR A 34 48.284 48.541 25.968 1.00 13.57 1SAC 627 ATOM 269 CA THR A 34 47.197 47.573 25.786 1.00 12.44 1SAC 628 ATOM 270 C THR A 34 46.484 47.438 27.123 1.00 13.55 1SAC 629 ATOM 271 O THR A 34 47.128 47.344 28.179 1.00 13.22 1SAC 630 ATOM 272 CB THR A 34 47.707 46.201 25.335 1.00 11.34 1SAC 631 ATOM 273 OG1 THR A 34 48.492 46.328 24.161 1.00 12.05 1SAC 632 ATOM 274 CG2 THR A 34 46.563 45.228 25.009 1.00 9.22 1SAC 633 ATOM 275 N LEU A 35 45.176 47.446 27.032 1.00 13.01 1SAC 634 ATOM 276 CA LEU A 35 44.299 47.374 28.203 1.00 13.46 1SAC 635 ATOM 277 C LEU A 35 43.265 46.264 28.012 1.00 14.04 1SAC 636 ATOM 278 O LEU A 35 42.539 46.236 27.009 1.00 13.13 1SAC 637 ATOM 279 CB LEU A 35 43.594 48.720 28.371 1.00 12.50 1SAC 638 ATOM 280 CG LEU A 35 42.515 48.718 29.451 1.00 13.53 1SAC 639 ATOM 281 CD1 LEU A 35 43.065 48.412 30.844 1.00 13.18 1SAC 640 ATOM 282 CD2 LEU A 35 41.797 50.065 29.573 1.00 11.48 1SAC 641 ATOM 283 N CYS A 36 43.265 45.215 28.851 1.00 12.89 1SAC 642 ATOM 284 CA CYS A 36 42.271 44.134 28.743 1.00 11.98 1SAC 643 ATOM 285 C CYS A 36 41.486 44.022 30.048 1.00 12.61 1SAC 644 ATOM 286 O CYS A 36 42.072 44.184 31.115 1.00 13.69 1SAC 645 ATOM 287 CB CYS A 36 42.933 42.789 28.458 1.00 13.44 1SAC 646 ATOM 288 SG CYS A 36 44.089 42.712 27.085 1.00 16.00 1SAC 647 ATOM 289 N PHE A 37 40.205 43.728 29.961 1.00 12.50 1SAC 648 ATOM 290 CA PHE A 37 39.472 43.349 31.194 1.00 13.38 1SAC 649 ATOM 291 C PHE A 37 38.150 42.695 30.826 1.00 14.09 1SAC 650 ATOM 292 O PHE A 37 37.765 42.786 29.654 1.00 14.58 1SAC 651 ATOM 293 CB PHE A 37 39.237 44.592 32.044 1.00 12.92 1SAC 652 ATOM 294 CG PHE A 37 38.612 45.712 31.202 1.00 13.98 1SAC 653 ATOM 295 CD1 PHE A 37 37.230 45.789 31.058 1.00 14.13 1SAC 654 ATOM 296 CD2 PHE A 37 39.461 46.630 30.594 1.00 15.35 1SAC 655 ATOM 297 CE1 PHE A 37 36.656 46.802 30.294 1.00 14.75 1SAC 656 ATOM 298 CE2 PHE A 37 38.888 47.635 29.828 1.00 16.55 1SAC 657 ATOM 299 CZ PHE A 37 37.510 47.717 29.682 1.00 17.33 1SAC 658 ATOM 300 N ARG A 38 37.485 42.044 31.755 1.00 12.54 1SAC 659 ATOM 301 CA ARG A 38 36.136 41.496 31.622 1.00 14.29 1SAC 660 ATOM 302 C ARG A 38 35.115 42.374 32.341 1.00 14.36 1SAC 661 ATOM 303 O ARG A 38 35.395 42.940 33.392 1.00 15.95 1SAC 662 ATOM 304 CB ARG A 38 36.047 40.096 32.236 1.00 14.22 1SAC 663 ATOM 305 CG ARG A 38 37.020 39.138 31.593 1.00 16.01 1SAC 664 ATOM 306 CD ARG A 38 36.651 37.703 32.006 1.00 15.73 1SAC 665 ATOM 307 NE ARG A 38 37.867 36.893 31.847 1.00 17.95 1SAC 666 ATOM 308 CZ ARG A 38 38.099 36.290 30.662 1.00 17.70 1SAC 667 ATOM 309 NH1 ARG A 38 37.109 36.224 29.783 1.00 15.80 1SAC 668 ATOM 310 NH2 ARG A 38 39.300 35.773 30.437 1.00 18.51 1SAC 669 ATOM 311 N ALA A 39 33.921 42.402 31.783 1.00 13.91 1SAC 670 ATOM 312 CA ALA A 39 32.848 43.205 32.362 1.00 12.87 1SAC 671 ATOM 313 C ALA A 39 31.496 42.562 32.142 1.00 14.38 1SAC 672 ATOM 314 O ALA A 39 31.228 41.950 31.109 1.00 13.65 1SAC 673 ATOM 315 CB ALA A 39 32.888 44.624 31.825 1.00 12.66 1SAC 674 ATOM 316 N TYR A 40 30.649 42.656 33.141 1.00 12.58 1SAC 675 ATOM 317 CA TYR A 40 29.279 42.117 33.138 1.00 12.93 1SAC 676 ATOM 318 C TYR A 40 28.323 43.160 33.701 1.00 14.53 1SAC 677 ATOM 319 O TYR A 40 28.379 43.490 34.881 1.00 15.32 1SAC 678 ATOM 320 CB TYR A 40 29.189 40.828 33.911 1.00 11.80 1SAC 679 ATOM 321 CG TYR A 40 27.954 39.977 33.654 1.00 11.80 1SAC 680 ATOM 322 CD1 TYR A 40 27.111 40.168 32.566 1.00 10.24 1SAC 681 ATOM 323 CD2 TYR A 40 27.668 38.964 34.571 1.00 10.24 1SAC 682 ATOM 324 CE1 TYR A 40 25.993 39.348 32.397 1.00 10.50 1SAC 683 ATOM 325 CE2 TYR A 40 26.560 38.146 34.399 1.00 9.98 1SAC 684 ATOM 326 CZ TYR A 40 25.714 38.335 33.308 1.00 10.85 1SAC 685 ATOM 327 OH TYR A 40 24.618 37.507 33.163 1.00 13.55 1SAC 686 ATOM 328 N SER A 41 27.508 43.716 32.831 1.00 13.92 1SAC 687 ATOM 329 CA SER A 41 26.590 44.805 33.224 1.00 13.52 1SAC 688 ATOM 330 C SER A 41 25.271 44.639 32.487 1.00 15.18 1SAC 689 ATOM 331 O SER A 41 25.314 44.059 31.399 1.00 16.92 1SAC 690 ATOM 332 CB SER A 41 27.214 46.149 32.936 1.00 12.82 1SAC 691 ATOM 333 OG SER A 41 26.390 47.217 33.394 1.00 10.23 1SAC 692 ATOM 334 N ASP A 42 24.162 45.058 33.055 1.00 14.03 1SAC 693 ATOM 335 CA ASP A 42 22.859 45.022 32.396 1.00 12.75 1SAC 694 ATOM 336 C ASP A 42 22.266 46.400 32.216 1.00 12.49 1SAC 695 ATOM 337 O ASP A 42 21.070 46.570 31.979 1.00 12.03 1SAC 696 ATOM 338 CB ASP A 42 21.886 44.074 33.048 1.00 14.13 1SAC 697 ATOM 339 CG ASP A 42 21.503 44.344 34.496 1.00 16.62 1SAC 698 ATOM 340 OD1 ASP A 42 21.804 45.367 35.114 1.00 17.75 1SAC 699 ATOM 341 OD2 ASP A 42 20.840 43.472 35.085 1.00 17.46 1SAC 700 ATOM 342 N LEU A 43 23.114 47.401 32.330 1.00 13.39 1SAC 701 ATOM 343 CA LEU A 43 22.807 48.822 32.050 1.00 15.54 1SAC 702 ATOM 344 C LEU A 43 22.537 48.979 30.532 1.00 16.46 1SAC 703 ATOM 345 O LEU A 43 23.404 48.542 29.781 1.00 17.22 1SAC 704 ATOM 346 CB LEU A 43 24.035 49.671 32.368 1.00 15.99 1SAC 705 ATOM 347 CG LEU A 43 24.005 50.497 33.616 1.00 18.39 1SAC 706 ATOM 348 CD1 LEU A 43 22.963 50.142 34.638 1.00 18.39 1SAC 707 ATOM 349 CD2 LEU A 43 25.386 50.743 34.198 1.00 16.41 1SAC 708 ATOM 350 N SER A 44 21.440 49.592 30.152 1.00 18.13 1SAC 709 ATOM 351 CA SER A 44 21.185 49.878 28.729 1.00 20.24 1SAC 710 ATOM 352 C SER A 44 21.789 51.223 28.347 1.00 20.98 1SAC 711 ATOM 353 O SER A 44 22.050 51.475 27.172 1.00 22.78 1SAC 712 ATOM 354 CB SER A 44 19.711 49.861 28.421 1.00 21.67 1SAC 713 ATOM 355 OG SER A 44 18.982 49.031 29.322 1.00 26.77 1SAC 714 ATOM 356 N ARG A 45 22.012 52.063 29.341 1.00 19.14 1SAC 715 ATOM 357 CA ARG A 45 22.552 53.404 29.137 1.00 18.50 1SAC 716 ATOM 358 C ARG A 45 24.043 53.411 28.924 1.00 17.96 1SAC 717 ATOM 359 O ARG A 45 24.733 52.406 29.094 1.00 16.83 1SAC 718 ATOM 360 CB ARG A 45 22.138 54.349 30.245 1.00 18.39 1SAC 719 ATOM 361 CG ARG A 45 22.612 53.899 31.630 1.00 17.79 1SAC 720 ATOM 362 CD ARG A 45 22.828 55.152 32.493 1.00 16.68 1SAC 721 ATOM 363 NE ARG A 45 23.085 54.819 33.893 1.00 16.92 1SAC 722 ATOM 364 CZ ARG A 45 24.342 54.679 34.356 1.00 14.90 1SAC 723 ATOM 365 NH1 ARG A 45 25.366 54.927 33.551 1.00 15.48 1SAC 724 ATOM 366 NH2 ARG A 45 24.544 54.277 35.611 1.00 15.98 1SAC 725 ATOM 367 N ALA A 46 24.595 54.552 28.524 1.00 16.09 1SAC 726 ATOM 368 CA ALA A 46 26.041 54.661 28.324 1.00 17.29 1SAC 727 ATOM 369 C ALA A 46 26.782 54.657 29.647 1.00 17.67 1SAC 728 ATOM 370 O ALA A 46 26.255 54.994 30.711 1.00 17.46 1SAC 729 ATOM 371 CB ALA A 46 26.376 55.903 27.523 1.00 16.82 1SAC 730 ATOM 372 N TYR A 47 28.047 54.263 29.629 1.00 15.54 1SAC 731 ATOM 373 CA TYR A 47 28.785 54.181 30.891 1.00 15.50 1SAC 732 ATOM 374 C TYR A 47 30.277 54.106 30.681 1.00 15.06 1SAC 733 ATOM 375 O TYR A 47 30.770 53.614 29.675 1.00 14.85 1SAC 734 ATOM 376 CB TYR A 47 28.283 53.086 31.778 1.00 14.07 1SAC 735 ATOM 377 CG TYR A 47 28.207 51.685 31.188 1.00 12.84 1SAC 736 ATOM 378 CD1 TYR A 47 29.354 50.895 31.114 1.00 12.72 1SAC 737 ATOM 379 CD2 TYR A 47 26.990 51.178 30.744 1.00 13.05 1SAC 738 ATOM 380 CE1 TYR A 47 29.281 49.611 30.590 1.00 14.03 1SAC 739 ATOM 381 CE2 TYR A 47 26.921 49.890 30.219 1.00 14.26 1SAC 740 ATOM 382 CZ TYR A 47 28.064 49.105 30.143 1.00 13.41 1SAC 741 ATOM 383 OH TYR A 47 28.019 47.824 29.630 1.00 14.13 1SAC 742 ATOM 384 N SER A 48 31.027 54.610 31.642 1.00 14.30 1SAC 743 ATOM 385 CA SER A 48 32.500 54.539 31.644 1.00 12.67 1SAC 744 ATOM 386 C SER A 48 32.960 53.151 32.065 1.00 13.20 1SAC 745 ATOM 387 O SER A 48 32.450 52.624 33.052 1.00 14.07 1SAC 746 ATOM 388 CB SER A 48 33.047 55.580 32.615 1.00 12.74 1SAC 747 ATOM 389 OG SER A 48 34.456 55.691 32.485 1.00 13.08 1SAC 748 ATOM 390 N LEU A 49 33.907 52.540 31.386 1.00 12.29 1SAC 749 ATOM 391 CA LEU A 49 34.517 51.278 31.815 1.00 12.22 1SAC 750 ATOM 392 C LEU A 49 35.870 51.531 32.495 1.00 12.34 1SAC 751 ATOM 393 O LEU A 49 36.186 50.836 33.456 1.00 14.27 1SAC 752 ATOM 394 CB LEU A 49 34.741 50.349 30.629 1.00 12.70 1SAC 753 ATOM 395 CG LEU A 49 33.461 49.631 30.230 1.00 13.56 1SAC 754 ATOM 396 CD1 LEU A 49 33.520 49.066 28.822 1.00 14.99 1SAC 755 ATOM 397 CD2 LEU A 49 33.044 48.592 31.249 1.00 12.82 1SAC 756 ATOM 398 N PHE A 50 36.633 52.478 32.000 1.00 11.13 1SAC 757 ATOM 399 CA PHE A 50 38.000 52.768 32.482 1.00 11.18 1SAC 758 ATOM 400 C PHE A 50 38.282 54.258 32.324 1.00 12.20 1SAC 759 ATOM 401 O PHE A 50 38.250 54.787 31.220 1.00 12.61 1SAC 760 ATOM 402 CB PHE A 50 39.016 51.967 31.695 1.00 10.28 1SAC 761 ATOM 403 CG PHE A 50 40.442 51.997 32.219 1.00 12.47 1SAC 762 ATOM 404 CD1 PHE A 50 40.862 51.080 33.180 1.00 10.39 1SAC 763 ATOM 405 CD2 PHE A 50 41.365 52.924 31.736 1.00 11.39 1SAC 764 ATOM 406 CE1 PHE A 50 42.166 51.074 33.671 1.00 11.15 1SAC 765 ATOM 407 CE2 PHE A 50 42.671 52.919 32.219 1.00 13.17 1SAC 766 ATOM 408 CZ PHE A 50 43.083 52.002 33.185 1.00 11.19 1SAC 767 ATOM 409 N SER A 51 38.527 55.026 33.391 1.00 13.42 1SAC 768 ATOM 410 CA SER A 51 38.744 56.481 33.430 1.00 12.89 1SAC 769 ATOM 411 C SER A 51 40.180 56.776 33.883 1.00 13.92 1SAC 770 ATOM 412 O SER A 51 40.573 56.426 35.008 1.00 12.89 1SAC 771 ATOM 413 CB SER A 51 37.747 57.122 34.391 1.00 13.53 1SAC 772 ATOM 414 OG SER A 51 37.801 58.534 34.273 1.00 13.80 1SAC 773 ATOM 415 N TYR A 52 40.890 57.425 32.975 1.00 11.36 1SAC 774 ATOM 416 CA TYR A 52 42.323 57.764 33.105 1.00 11.05 1SAC 775 ATOM 417 C TYR A 52 42.524 59.261 32.806 1.00 12.58 1SAC 776 ATOM 418 O TYR A 52 42.629 59.669 31.639 1.00 10.24 1SAC 777 ATOM 419 CB TYR A 52 43.071 56.894 32.080 1.00 10.22 1SAC 778 ATOM 420 CG TYR A 52 44.591 57.065 32.037 1.00 8.23 1SAC 779 ATOM 421 CD1 TYR A 52 45.153 58.318 31.770 1.00 20.00 1SAC 780 ATOM 422 CD2 TYR A 52 45.419 55.954 32.249 1.00 20.00 1SAC 781 ATOM 423 CE1 TYR A 52 46.546 58.460 31.711 1.00 20.00 1SAC 782 ATOM 424 CE2 TYR A 52 46.811 56.097 32.188 1.00 20.00 1SAC 783 ATOM 425 CZ TYR A 52 47.375 57.349 31.918 1.00 20.00 1SAC 784 ATOM 426 OH TYR A 52 48.727 57.487 31.854 1.00 20.00 1SAC 785 ATOM 427 N ASN A 53 42.562 60.038 33.881 1.00 12.05 1SAC 786 ATOM 428 CA ASN A 53 42.727 61.504 33.813 1.00 12.74 1SAC 787 ATOM 429 C ASN A 53 44.095 61.913 34.367 1.00 14.13 1SAC 788 ATOM 430 O ASN A 53 44.631 61.275 35.285 1.00 14.43 1SAC 789 ATOM 431 CB ASN A 53 41.635 62.197 34.637 1.00 11.47 1SAC 790 ATOM 432 CG ASN A 53 40.373 62.500 33.824 1.00 13.34 1SAC 791 ATOM 433 OD1 ASN A 53 40.087 61.804 32.852 1.00 15.02 1SAC 792 ATOM 434 ND2 ASN A 53 39.590 63.507 34.167 1.00 12.39 1SAC 793 ATOM 435 N THR A 54 44.676 62.967 33.751 1.00 14.88 1SAC 794 ATOM 436 CA THR A 54 45.897 63.518 34.358 1.00 15.65 1SAC 795 ATOM 437 C THR A 54 45.657 64.962 34.796 1.00 16.97 1SAC 796 ATOM 438 O THR A 54 44.576 65.523 34.568 1.00 16.26 1SAC 797 ATOM 439 CB THR A 54 47.045 63.486 33.347 1.00 15.05 1SAC 798 ATOM 440 OG1 THR A 54 46.670 64.165 32.157 1.00 16.48 1SAC 799 ATOM 441 CG2 THR A 54 47.453 62.066 32.957 1.00 16.41 1SAC 800 ATOM 442 N GLN A 55 46.575 65.544 35.514 1.00 17.10 1SAC 801 ATOM 443 CA GLN A 55 46.402 66.904 36.045 1.00 18.01 1SAC 802 ATOM 444 C GLN A 55 46.156 67.885 34.897 1.00 17.87 1SAC 803 ATOM 445 O GLN A 55 46.995 68.037 33.998 1.00 16.99 1SAC 804 ATOM 446 CB GLN A 55 47.658 67.329 36.803 1.00 20.54 1SAC 805 ATOM 447 CG GLN A 55 47.588 68.754 37.350 1.00 20.13 1SAC 806 ATOM 448 CD GLN A 55 48.772 69.080 38.259 1.00 18.89 1SAC 807 ATOM 449 OE1 GLN A 55 49.901 69.206 37.779 1.00 18.92 1SAC 808 ATOM 450 NE2 GLN A 55 48.585 69.216 39.558 1.00 18.59 1SAC 809 ATOM 451 N GLY A 56 44.999 68.507 34.924 1.00 18.43 1SAC 810 ATOM 452 CA GLY A 56 44.554 69.466 33.920 1.00 19.05 1SAC 811 ATOM 453 C GLY A 56 44.092 68.842 32.621 1.00 19.60 1SAC 812 ATOM 454 O GLY A 56 43.884 69.581 31.653 1.00 18.79 1SAC 813 ATOM 455 N ARG A 57 43.946 67.529 32.550 1.00 18.24 1SAC 814 ATOM 456 CA ARG A 57 43.553 66.883 31.288 1.00 18.35 1SAC 815 ATOM 457 C ARG A 57 42.441 65.882 31.511 1.00 18.34 1SAC 816 ATOM 458 O ARG A 57 42.660 64.796 32.030 1.00 19.70 1SAC 817 ATOM 459 CB ARG A 57 44.748 66.187 30.642 1.00 18.85 1SAC 818 ATOM 460 CG ARG A 57 45.461 67.193 29.739 1.00 21.72 1SAC 819 ATOM 461 CD ARG A 57 46.970 67.059 29.887 1.00 22.91 1SAC 820 ATOM 462 NE ARG A 57 47.543 66.716 28.584 1.00 28.80 1SAC 821 ATOM 463 CZ ARG A 57 48.702 67.237 28.150 1.00 29.10 1SAC 822 ATOM 464 NH1 ARG A 57 49.257 68.276 28.766 1.00 31.63 1SAC 823 ATOM 465 NH2 ARG A 57 49.304 66.705 27.088 1.00 31.20 1SAC 824 ATOM 466 N ASP A 58 41.257 66.269 31.097 1.00 17.96 1SAC 825 ATOM 467 CA ASP A 58 40.108 65.345 31.138 1.00 18.40 1SAC 826 ATOM 468 C ASP A 58 40.184 64.367 29.973 1.00 17.12 1SAC 827 ATOM 469 O ASP A 58 40.680 64.745 28.915 1.00 16.94 1SAC 828 ATOM 470 CB ASP A 58 38.807 66.154 31.033 1.00 19.49 1SAC 829 ATOM 471 CG ASP A 58 37.606 65.246 31.325 1.00 20.35 1SAC 830 ATOM 472 OD1 ASP A 58 37.796 64.294 32.087 1.00 21.45 1SAC 831 ATOM 473 OD2 ASP A 58 36.532 65.527 30.787 1.00 23.02 1SAC 832 ATOM 474 N ASN A 59 39.772 63.139 30.151 1.00 16.54 1SAC 833 ATOM 475 CA ASN A 59 39.600 62.197 29.036 1.00 15.70 1SAC 834 ATOM 476 C ASN A 59 40.927 62.001 28.316 1.00 14.98 1SAC 835 ATOM 477 O ASN A 59 40.983 61.977 27.082 1.00 14.06 1SAC 836 ATOM 478 CB ASN A 59 38.557 62.738 28.064 1.00 16.58 1SAC 837 ATOM 479 CG ASN A 59 37.172 62.687 28.678 1.00 16.77 1SAC 838 ATOM 480 OD1 ASN A 59 37.035 62.199 29.802 1.00 18.06 1SAC 839 ATOM 481 ND2 ASN A 59 36.136 63.155 28.018 1.00 18.19 1SAC 840 ATOM 482 N GLU A 60 41.901 61.748 29.125 1.00 14.32 1SAC 841 ATOM 483 CA GLU A 60 43.274 61.519 28.648 1.00 14.53 1SAC 842 ATOM 484 C GLU A 60 43.376 60.122 27.999 1.00 14.71 1SAC 843