Документ взят из кэша поисковой машины. Адрес оригинального документа : http://monkey.belozersky.msu.su/npidb/pdb/pdb_new/stride/2f8x.std.txt Дата изменения: Tue Jan 18 08:57:28 2011 Дата индексирования: Fri Feb 11 21:17:18 2011 Кодировка:

REM -------------------------------------------------------------------- 2F8X
REM 2F8X
REM STRIDE: Knowledge-based secondary structure assignment 2F8X
REM Please cite: D.Frishman & P.Argos, Proteins 23, 566-579, 1995 2F8X
REM 2F8X
REM Residue accessible surface area calculation 2F8X
REM Please cite: F.Eisenhaber & P.Argos, J.Comp.Chem. 14, 1272-1280, 1993 2F8X
REM F.Eisenhaber et al., J.Comp.Chem., 1994, submitted 2F8X
REM 2F8X
REM ------------------------ General information ----------------------- 2F8X
REM 2F8X
HDR TRANSCRIPTION/DNA 04-DEC-05 2F8X 2F8X
CMP MOL_ID: 1; 2F8X
CMP MOLECULE: 5'- 2F8X
CMP D(*GP*TP*TP*AP*CP*TP*GP*TP*GP*GP*GP*AP*AP*AP*GP*AP*AP*A)- 2F8X
CMP 3'; 2F8X
CMP CHAIN: X; 2F8X
CMP ENGINEERED: YES; 2F8X
CMP MOL_ID: 2; 2F8X
CMP MOLECULE: 5'- 2F8X
CMP D(*TP*TP*TP*CP*TP*TP*TP*CP*CP*CP*AP*CP*AP*GP*TP*AP*AP*C)- 2F8X
CMP 3'; 2F8X
CMP CHAIN: Y; 2F8X
CMP ENGINEERED: YES; 2F8X
CMP MOL_ID: 3; 2F8X
CMP MOLECULE: RECOMBINING BINDING PROTEIN SUPPRESSOR OF 2F8X
CMP HAIRLESS, ISOFORM 4; 2F8X
CMP CHAIN: C; 2F8X
CMP ENGINEERED: YES; 2F8X
CMP MOL_ID: 4; 2F8X
CMP MOLECULE: NEUROGENIC LOCUS NOTCH HOMOLOG PROTEIN 1; 2F8X
CMP CHAIN: K; 2F8X
CMP FRAGMENT: [CONTAINS: NOTCH 1 EXTRACELLULAR TRUNCATION; 2F8X
CMP NOTCH 1 INTRACELLULAR DOMAIN]; 2F8X
CMP SYNONYM: (NOTCH 1) (HN1) (TRANSLOCATION-ASSOCIATED NOTCH 2F8X
CMP PROTEIN TAN-1); 2F8X
CMP ENGINEERED: YES; 2F8X
CMP MOL_ID: 5; 2F8X
CMP MOLECULE: MASTERMIND-LIKE PROTEIN 1; 2F8X
CMP CHAIN: M; 2F8X
CMP SYNONYM: MAM-1; 2F8X
CMP ENGINEERED: YES 2F8X
SRC MOL_ID: 1; 2F8X
SRC SYNTHETIC: YES; 2F8X
SRC MOL_ID: 2; 2F8X
SRC SYNTHETIC: YES; 2F8X
SRC MOL_ID: 3; 2F8X
SRC ORGANISM_SCIENTIFIC: HOMO SAPIENS; 2F8X
SRC ORGANISM_COMMON: HUMAN; 2F8X
SRC ORGANISM_TAXID: 9606; 2F8X
SRC EXPRESSION_SYSTEM: ESCHERICHIA COLI; 2F8X
SRC EXPRESSION_SYSTEM_TAXID: 562; 2F8X
SRC EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS; 2F8X
SRC EXPRESSION_SYSTEM_PLASMID: PRSETA; 2F8X
SRC MOL_ID: 4; 2F8X
SRC ORGANISM_SCIENTIFIC: HOMO SAPIENS; 2F8X
SRC ORGANISM_COMMON: HUMAN; 2F8X
SRC ORGANISM_TAXID: 9606; 2F8X
SRC GENE: NOTCH1, TAN1; 2F8X
SRC EXPRESSION_SYSTEM: ESCHERICHIA COLI; 2F8X
SRC EXPRESSION_SYSTEM_TAXID: 562; 2F8X
SRC EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS; 2F8X
SRC EXPRESSION_SYSTEM_PLASMID: PET28A; 2F8X
SRC MOL_ID: 5; 2F8X
SRC ORGANISM_SCIENTIFIC: HOMO SAPIENS; 2F8X
SRC ORGANISM_COMMON: HUMAN; 2F8X
SRC ORGANISM_TAXID: 9606; 2F8X
SRC GENE: MAML1, KIAA0200; 2F8X
SRC EXPRESSION_SYSTEM: ESCHERICHIA COLI; 2F8X
SRC EXPRESSION_SYSTEM_TAXID: 562; 2F8X
SRC EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS; 2F8X
SRC EXPRESSION_SYSTEM_PLASMID: PDEST15 2F8X
AUT Y.NAM,P.SLIZ,S.C.BLACKLOW 2F8X
REM 2F8X
REM -------------------- Secondary structure summary ------------------- 2F8X
REM 2F8X
CHN /data/npidb/pdb/pdb_new/all/pdb2f8x.pdb C 2F8X
REM 2F8X
REM . . . . . 2F8X
SEQ 1 RPPPKRLTREAMRNYLKERGDQTVLILHAKVAQKSYGNEKRFFCPPPCVY 50 2F8X
STR HHHHHHHHHH EEEEEEEE EEE TTTT TTTT EEE 2F8X
REM 2F8X
REM . . . . . 2F8X
SEQ 51 LMGSGWKKKKEQMERDGCSEQESQPCAFIGIGNSDQEMQQLNLEGKNYCT 100 2F8X
STR B HHHHHHHHHHGGG TTTTTT EEEEEETTTTT EE TTTT EEE 2F8X
REM 2F8X
REM . . . . . 2F8X
SEQ 101 AKTLYISDSDKRKHFMLSVKMFYGNSDDIGVFLSKRIKVISKPSKKKQSL 150 2F8X
STR TTTT TTTTTTTEE EEEEEETTTT EEEEEE EEEETTT TT 2F8X
REM 2F8X
REM . . . . . 2F8X
SEQ 151 KNADLCIASGTKVALFNRLRSQTVSTRYLHVEGGNFHASSQQWGAFFIHL 200 2F8X
STR TTTTTB BTTEEEEEEETTTTTTTTTEE EEETTEEE TTTT EEEEE 2F8X
REM 2F8X
REM . . . . . 2F8X
SEQ 201 LDDDESEGEEFTVRDGYIHYGQTVKLVCSVTGMALPRLIIRKVDKQTALL 250 2F8X
STR ETTTT TTTT B BTTEEEEEEETTTT EEEEEEEEEEETTEETT 2F8X
REM 2F8X
REM . . . . . 2F8X
SEQ 251 DADDPVSQLHKCAFYLKDTERMYLCLSQERIIQFQATPCPKEPNKEMIND 300 2F8X
STR TT B BTTEEEEEETTTTTTTEEEETTTTEE TTTTTTT B TT 2F8X
REM 2F8X
REM . . . . . 2F8X
SEQ 301 GASWTIISTDKAEYTFYEGMGPVLAPVTPVPVVESLQLNGGGDVAMLELT 350 2F8X
STR TTT EEEEEEEEEEEE TTTT TTTT EEEEEEEE GGG EEEEE 2F8X
REM 2F8X
REM . . . . . 2F8X
SEQ 351 GQNFTPNLRVWFGDVEAETMYRCGESMLCVVPDISAFREGWRWVRQPVQV 400 2F8X
STR EE TTTEEEEETTEEE EEEEETTEEEEE GGGGTTTTTTT EE 2F8X
REM 2F8X
REM . . 2F8X
SEQ 401 PVTLVRNDGIIYSTSLTFTYTPEP 424 2F8X
STR EEEEETTT EEEEEB EE 2F8X
REM 2F8X
CHN /data/npidb/pdb/pdb_new/all/pdb2f8x.pdb K 2F8X
REM 2F8X
REM . . . . . 2F8X
SEQ 1 TPLMIASCSAVISDFIYSLHNQTDRTGETALHLAARYSRSDAAKRLLEAS 50 2F8X
STR HHHHHHHHHHHHHHHH TTTT TTTTT HHHHHHHH HHHHHHHHHTT 2F8X
REM 2F8X
REM . . . . . 2F8X
SEQ 51 ADANIQDNMGRTPLHAAVSADAQGVFQILIRNRATDLDARMHDGTTPLIL 100 2F8X
STR TTTT TTTT HHHHHHHH HHHHHHHHHTTTTTTTT TTTT HHHH 2F8X
REM 2F8X
REM . . . . . 2F8X
SEQ 101 AARLAVEGMLEDLINSHADVNAVDDLGKSALHWAAAVNNVDAAVVLLKNG 150 2F8X
STR HHHH TTTHHHHHHHH TTTTEETTTEEHHHHHHHH HHHHHHHHHH 2F8X
REM 2F8X
REM . . . . . 2F8X
SEQ 151 ANKDMQNNREETPLFLAAREGSYETAKVLLDHFANRDITDHMDRLPRDIA 200 2F8X
STR TTTT BTTTB HHHHHHHH HHHHHHHHHH TTTT BTTTB HHHHH 2F8X
REM 2F8X
REM . 2F8X
SEQ 201 QERMHHDIVRLLDEYNLV 218 2F8X
STR HHH HHHHHHHHHTTT 2F8X
REM 2F8X
CHN /data/npidb/pdb/pdb_new/all/pdb2f8x.pdb M 2F8X
REM 2F8X
REM . . . . . 2F8X
SEQ 1 HSAVMERLRRRIELCRRHHSTCEARYEAVSPERLELERQHTFALHQRCIQ 50 2F8X
STR HHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHH 2F8X
REM 2F8X
REM 2F8X
SEQ 51 AKAKR 55 2F8X
STR HHHH 2F8X
REM 2F8X
REM 2F8X
REM 2F8X
LOC AlphaHelix ARG 19 C GLU 28 C 2F8X
LOC AlphaHelix SER 64 C MET 73 C 2F8X
LOC AlphaHelix THR 1884 K ILE 1915 K 2F8X
LOC AlphaHelix ALA 1932 K TYR 1939 K 2F8X
LOC AlphaHelix SER 1942 K GLU 1950 K 2F8X
LOC AlphaHelix PRO 1965 K ALA 1972 K 2F8X
LOC AlphaHelix GLN 1975 K ARG 1983 K 2F8X
LOC AlphaHelix PRO 1999 K LEU 2006 K 2F8X
LOC AlphaHelix MET 2011 K SER 2018 K 2F8X
LOC AlphaHelix ALA 2032 K VAL 2039 K 2F8X
LOC AlphaHelix VAL 2042 K ASN 2051 K 2F8X
LOC AlphaHelix PRO 2065 K GLU 2072 K 2F8X
LOC AlphaHelix TYR 2075 K HIS 2084 K 2F8X
LOC AlphaHelix PRO 2098 K ARG 2105 K 2F8X
LOC AlphaHelix HIS 2108 K GLU 2116 K 2F8X
LOC AlphaHelix HIS 16 M LYS 69 M 2F8X
LOC 310Helix GLU 74 C ASP 76 C 2F8X
LOC 310Helix GLY 352 C VAL 354 C 2F8X
LOC 310Helix ILE 394 C PHE 397 C 2F8X
LOC Strand GLN 32 C ALA 39 C 2F8X
LOC Strand VAL 41 C GLN 43 C 2F8X
LOC Strand CYS 58 C TYR 60 C 2F8X
LOC Strand CYS 86 C ILE 91 C 2F8X
LOC Strand GLN 99 C GLN 100 C 2F8X
LOC Strand TYR 108 C THR 110 C 2F8X
LOC Strand HIS 124 C PHE 125 C 2F8X
LOC Strand LEU 127 C PHE 132 C 2F8X
LOC Strand ASP 138 C LEU 143 C 2F8X
LOC Strand ILE 147 C ILE 150 C 2F8X
LOC Strand THR 171 C ASN 177 C 2F8X
LOC Strand ARG 187 C TYR 188 C 2F8X
LOC Strand HIS 190 C GLU 192 C 2F8X
LOC Strand ASN 195 C HIS 197 C 2F8X
LOC Strand PHE 206 C LEU 211 C 2F8X
LOC Strand GLN 232 C CYS 238 C 2F8X
LOC Strand ALA 244 C ASP 254 C 2F8X
LOC Strand THR 257 C ALA 258 C 2F8X
LOC Strand HIS 270 C TYR 275 C 2F8X
LOC Strand TYR 283 C LEU 286 C 2F8X
LOC Strand ILE 291 C ILE 292 C 2F8X
LOC Strand THR 315 C PHE 326 C 2F8X
LOC Strand VAL 342 C ASN 349 C 2F8X
LOC Strand MET 356 C GLN 362 C 2F8X
LOC Strand LEU 368 C PHE 372 C 2F8X
LOC Strand VAL 375 C ALA 377 C 2F8X
LOC Strand THR 379 C CYS 383 C 2F8X
LOC Strand SER 386 C VAL 390 C 2F8X
LOC Strand VAL 408 C GLN 409 C 2F8X
LOC Strand VAL 412 C ARG 416 C 2F8X
LOC Strand ILE 421 C SER 425 C 2F8X
LOC Strand THR 429 C TYR 430 C 2F8X
LOC Strand VAL 2025 K ASP 2026 K 2F8X
LOC Strand LYS 2030 K SER 2031 K 2F8X
LOC TurnII' TYR 46 C GLU 49 C 2F8X
LOC TurnIV PHE 53 C PRO 56 C 2F8X
LOC TurnI SER 79 C GLU 82 C 2F8X
LOC TurnI GLU 80 C SER 83 C 2F8X
LOC TurnI GLN 81 C GLN 84 C 2F8X
LOC TurnIV ILE 91 C SER 94 C 2F8X
LOC TurnII LEU 103 C LYS 106 C 2F8X
LOC TurnIV ALA 111 C LEU 114 C 2F8X
LOC TurnI SER 117 C ASP 120 C 2F8X
LOC TurnVIII ASP 118 C LYS 121 C 2F8X
LOC TurnIV ARG 122 C PHE 125 C 2F8X
LOC TurnI TYR 133 C SER 136 C 2F8X
LOC TurnIV ILE 150 C PRO 153 C 2F8X
LOC TurnIV SER 159 C ASN 162 C 2F8X
LOC TurnIV LEU 160 C ALA 163 C 2F8X
LOC TurnIV ALA 163 C CYS 166 C 2F8X
LOC TurnIV ALA 168 C THR 171 C 2F8X
LOC TurnII ARG 178 C SER 181 C 2F8X
LOC TurnI' LEU 179 C GLN 182 C 2F8X
LOC TurnI GLN 182 C SER 185 C 2F8X
LOC TurnI THR 183 C THR 186 C 2F8X
LOC TurnIV VAL 191 C GLY 194 C 2F8X
LOC TurnI' GLU 192 C ASN 195 C 2F8X
LOC TurnIV SER 199 C GLN 202 C 2F8X
LOC TurnIV ASP 212 C GLU 215 C 2F8X
LOC TurnIV GLY 218 C PHE 221 C 2F8X
LOC TurnII HIS 229 C GLN 232 C 2F8X
LOC TurnIV CYS 238 C THR 241 C 2F8X
LOC TurnIV SER 239 C GLY 242 C 2F8X
LOC TurnIV VAL 253 C GLN 256 C 2F8X
LOC TurnI' ASP 254 C THR 257 C 2F8X
LOC TurnIV LEU 259 C ALA 262 C 2F8X
LOC TurnIV SER 267 C HIS 270 C 2F8X
LOC TurnIV LEU 276 C THR 279 C 2F8X
LOC TurnIV ASP 278 C ARG 281 C 2F8X
LOC TurnIV THR 279 C MET 282 C 2F8X
LOC TurnIV LEU 286 C GLU 289 C 2F8X
LOC TurnIV SER 287 C ARG 290 C 2F8X
LOC TurnIV CYS 299 C GLU 302 C 2F8X
LOC TurnIV GLU 302 C LYS 305 C 2F8X
LOC TurnIV ASN 309 C ALA 312 C 2F8X
LOC TurnIV ASP 310 C SER 313 C 2F8X
LOC TurnIV GLU 328 C GLY 331 C 2F8X
LOC TurnIV VAL 337 C VAL 340 C 2F8X
LOC TurnI THR 365 C LEU 368 C 2F8X
LOC TurnIV TRP 371 C ASP 374 C 2F8X
LOC TurnII' PHE 372 C VAL 375 C 2F8X
LOC TurnI CYS 383 C SER 386 C 2F8X
LOC TurnIV ARG 398 C TRP 401 C 2F8X
LOC TurnIV TRP 401 C VAL 404 C 2F8X
LOC TurnI ARG 416 C GLY 419 C 2F8X
LOC GammaInv SER 94 C GLN 96 C 2F8X
LOC TurnIV SER 1920 K ASN 1923 K 2F8X
LOC TurnIV THR 1925 K THR 1928 K 2F8X
LOC TurnI ASP 1926 K GLY 1929 K 2F8X
LOC TurnIV ASP 1954 K ILE 1957 K 2F8X
LOC TurnI ASP 1959 K GLY 1962 K 2F8X
LOC TurnIV ASN 1984 K THR 1987 K 2F8X
LOC TurnI ASP 1988 K ALA 1991 K 2F8X
LOC TurnI MET 1993 K GLY 1996 K 2F8X
LOC TurnII VAL 2008 K MET 2011 K 2F8X
LOC TurnI ASP 2021 K ALA 2024 K 2F8X
LOC TurnI ASP 2026 K GLY 2029 K 2F8X
LOC TurnI ASN 2054 K MET 2057 K 2F8X
LOC TurnI ASN 2059 K GLU 2062 K 2F8X
LOC TurnI ASN 2087 K ILE 2090 K 2F8X
LOC TurnI ASP 2092 K ASP 2095 K 2F8X
LOC TurnIV GLU 2116 K LEU 2119 K 2F8X
LOC GammaInv GLU 1950 K SER 1952 K 2F8X
REM 2F8X
REM --------------- Detailed secondary structure assignment------------- 2F8X
REM 2F8X
REM |---Residue---| |--Structure--| |-Phi-| |-Psi-| |-Area-| 2F8X
ASG ARG C 11 1 C Coil 360.00 142.02 203.1 2F8X
ASG PRO C 12 2 C Coil -58.39 118.81 110.1 2F8X
ASG PRO C 13 3 C Coil -56.93 145.32 92.9 2F8X
ASG PRO C 14 4 C Coil -48.56 133.09 83.9 2F8X
ASG LYS C 15 5 C Coil -110.84 128.51 135.9 2F8X
ASG ARG C 16 6 C Coil -68.21 126.93 122.1 2F8X
ASG LEU C 17 7 C Coil -54.85 136.41 8.4 2F8X
ASG THR C 18 8 C Coil -100.36 160.91 64.5 2F8X
ASG ARG C 19 9 H AlphaHelix -50.87 -51.46 121.1 2F8X
ASG GLU C 20 10 H AlphaHelix -60.22 -44.44 129.5 2F8X
ASG ALA C 21 11 H AlphaHelix -60.25 -34.22 15.6 2F8X
ASG MET C 22 12 H AlphaHelix -68.44 -41.49 0.0 2F8X
ASG ARG C 23 13 H AlphaHelix -60.11 -41.56 118.0 2F8X
ASG ASN C 24 14 H AlphaHelix -60.23 -44.56 87.2 2F8X
ASG TYR C 25 15 H AlphaHelix -62.65 -42.63 1.0 2F8X
ASG LEU C 26 16 H AlphaHelix -61.60 -34.36 46.7 2F8X
ASG LYS C 27 17 H AlphaHelix -71.32 -60.34 166.6 2F8X
ASG GLU C 28 18 H AlphaHelix -73.25 -76.70 118.4 2F8X
ASG ARG C 29 19 C Coil 79.27 60.16 93.4 2F8X
ASG GLY C 30 20 C Coil -100.48 62.57 2.2 2F8X
ASG ASP C 31 21 C Coil -56.61 151.33 24.3 2F8X
ASG GLN C 32 22 E Strand -108.99 136.40 4.0 2F8X
ASG THR C 33 23 E Strand -140.36 127.37 17.8 2F8X
ASG VAL C 34 24 E Strand -86.89 -174.87 0.0 2F8X
ASG LEU C 35 25 E Strand 175.48 128.79 14.4 2F8X
ASG ILE C 36 26 E Strand -128.84 115.84 0.0 2F8X
ASG LEU C 37 27 E Strand -99.40 139.69 30.7 2F8X
ASG HIS C 38 28 E Strand -166.62 172.35 0.8 2F8X
ASG ALA C 39 29 E Strand -81.39 156.60 7.0 2F8X
ASG LYS C 40 30 C Coil -92.20 -13.16 64.6 2F8X
ASG VAL C 41 31 E Strand -120.35 163.87 12.8 2F8X
ASG ALA C 42 32 E Strand -155.29 128.06 5.2 2F8X
ASG GLN C 43 33 E Strand -74.54 114.70 43.6 2F8X
ASG LYS C 44 34 C Coil -66.98 142.05 40.9 2F8X
ASG SER C 45 35 C Coil -101.99 130.95 2.0 2F8X
ASG TYR C 46 36 T Turn -96.87 175.78 87.6 2F8X
ASG GLY C 47 37 T Turn 43.54 -115.44 56.6 2F8X
ASG ASN C 48 38 T Turn -121.67 20.61 163.6 2F8X
ASG GLU C 49 39 T Turn -61.14 -160.66 80.3 2F8X
ASG LYS C 50 40 C Coil -178.25 87.63 109.7 2F8X
ASG ARG C 51 41 C Coil -97.38 92.08 110.1 2F8X
ASG PHE C 52 42 C Coil -52.71 142.97 72.7 2F8X
ASG PHE C 53 43 T Turn -62.72 116.40 16.9 2F8X
ASG CYS C 54 44 T Turn -125.11 127.01 22.4 2F8X
ASG PRO C 55 45 T Turn -62.64 162.80 1.2 2F8X
ASG PRO C 56 46 T Turn -83.02 125.59 3.0 2F8X
ASG PRO C 57 47 C Coil -50.36 108.48 2.0 2F8X
ASG CYS C 58 48 E Strand -83.60 159.63 2.8 2F8X
ASG VAL C 59 49 E Strand -137.76 83.65 0.0 2F8X
ASG TYR C 60 50 E Strand -76.58 155.09 50.7 2F8X
ASG LEU C 61 51 C Coil -123.48 79.06 9.8 2F8X
ASG MET C 62 52 B Bridge -80.19 172.90 77.6 2F8X
ASG GLY C 63 53 C Coil 102.88 129.67 36.6 2F8X
ASG SER C 64 54 H AlphaHelix -61.28 -23.25 78.9 2F8X
ASG GLY C 65 55 H AlphaHelix -60.43 -34.32 2.8 2F8X
ASG TRP C 66 56 H AlphaHelix -60.03 -37.63 24.5 2F8X
ASG LYS C 67 57 H AlphaHelix -70.31 -44.37 144.2 2F8X
ASG LYS C 68 58 H AlphaHelix -60.22 -35.63 78.0 2F8X
ASG LYS C 69 59 H AlphaHelix -70.39 -35.40 13.1 2F8X
ASG LYS C 70 60 H AlphaHelix -65.50 -44.56 55.4 2F8X
ASG GLU C 71 61 H AlphaHelix -65.62 -44.57 86.2 2F8X
ASG GLN C 72 62 H AlphaHelix -60.33 -41.59 46.7 2F8X
ASG MET C 73 63 H AlphaHelix -63.33 -44.50 8.1 2F8X
ASG GLU C 74 64 G 310Helix -64.79 -46.94 67.6 2F8X
ASG ARG C 75 65 G 310Helix -59.43 20.97 176.6 2F8X
ASG ASP C 76 66 G 310Helix -143.35 17.40 118.9 2F8X
ASG GLY C 77 67 C Coil 84.59 55.67 63.0 2F8X
ASG CYS C 78 68 C Coil -125.46 134.05 29.2 2F8X
ASG SER C 79 69 T Turn -58.71 165.31 61.7 2F8X
ASG GLU C 80 70 T Turn -65.85 -31.11 138.3 2F8X
ASG GLN C 81 71 T Turn -79.39 -17.02 119.8 2F8X
ASG GLU C 82 72 T Turn -89.04 -24.01 74.4 2F8X
ASG SER C 83 73 T Turn -109.10 41.92 2.0 2F8X
ASG GLN C 84 74 T Turn -113.01 111.18 40.3 2F8X
ASG PRO C 85 75 C Coil -49.37 127.82 20.1 2F8X
ASG CYS C 86 76 E Strand -105.25 -179.17 12.5 2F8X
ASG ALA C 87 77 E Strand 177.52 133.12 0.0 2F8X
ASG PHE C 88 78 E Strand -126.02 151.45 0.0 2F8X
ASG ILE C 89 79 E Strand -117.42 148.09 0.2 2F8X
ASG GLY C 90 80 E Strand -157.26 -178.74 5.7 2F8X
ASG ILE C 91 81 E Strand -104.38 90.33 20.7 2F8X
ASG GLY C 92 82 T Turn 28.74 -134.77 27.6 2F8X
ASG ASN C 93 83 T Turn -88.09 70.77 132.2 2F8X
ASG SER C 94 84 T Turn -118.45 135.57 35.2 2F8X
ASG ASP C 95 85 T Turn -78.93 63.02 169.9 2F8X
ASG GLN C 96 86 T Turn -121.54 -138.75 101.2 2F8X
ASG GLU C 97 87 C Coil -136.93 130.50 143.4 2F8X
ASG MET C 98 88 C Coil -73.36 137.30 32.1 2F8X
ASG GLN C 99 89 E Strand -93.20 148.75 55.1 2F8X
ASG GLN C 100 90 E Strand -92.54 149.37 75.8 2F8X
ASG LEU C 101 91 C Coil -109.52 132.32 4.5 2F8X
ASG ASN C 102 92 C Coil -86.58 111.37 79.6 2F8X
ASG LEU C 103 93 T Turn -108.46 14.84 8.5 2F8X
ASG GLU C 104 94 T Turn -59.94 123.39 98.3 2F8X
ASG GLY C 105 95 T Turn 67.84 -35.45 86.0 2F8X
ASG LYS C 106 96 T Turn -74.49 153.19 99.4 2F8X
ASG ASN C 107 97 C Coil -96.73 -7.00 92.5 2F8X
ASG TYR C 108 98 E Strand -150.27 -175.05 69.2 2F8X
ASG CYS C 109 99 E Strand -178.26 130.48 7.6 2F8X
ASG THR C 110 100 E Strand -88.33 159.94 28.5 2F8X
ASG ALA C 111 101 T Turn -111.22 73.27 3.6 2F8X
ASG LYS C 112 102 T Turn -55.84 -17.71 97.3 2F8X
ASG THR C 113 103 T Turn -126.35 37.53 65.3 2F8X
ASG LEU C 114 104 T Turn -84.45 140.36 6.4 2F8X
ASG TYR C 115 105 C Coil -155.56 159.89 60.5 2F8X
ASG ILE C 116 106 C Coil -120.25 113.90 3.8 2F8X
ASG SER C 117 107 T Turn -66.63 170.55 15.4 2F8X
ASG ASP C 118 108 T Turn -89.78 -1.70 43.0 2F8X
ASG SER C 119 109 T Turn -65.95 -24.26 92.5 2F8X
ASG ASP C 120 110 T T