Документ взят из кэша поисковой машины. Адрес оригинального документа : http://monkey.belozersky.msu.ru/npidb/pdb/pdb_new/stride/1cit.std.txt Дата изменения: Thu Jan 20 13:22:18 2011 Дата индексирования: Fri Feb 11 17:45:48 2011 Кодировка:

REM -------------------------------------------------------------------- 1CIT
REM 1CIT
REM STRIDE: Knowledge-based secondary structure assignment 1CIT
REM Please cite: D.Frishman & P.Argos, Proteins 23, 566-579, 1995 1CIT
REM 1CIT
REM Residue accessible surface area calculation 1CIT
REM Please cite: F.Eisenhaber & P.Argos, J.Comp.Chem. 14, 1272-1280, 1993 1CIT
REM F.Eisenhaber et al., J.Comp.Chem., 1994, submitted 1CIT
REM 1CIT
REM ------------------------ General information ----------------------- 1CIT
REM 1CIT
HDR TRANSCRIPTION/DNA 05-APR-99 1CIT 1CIT
CMP MOL_ID: 1; 1CIT
CMP MOLECULE: DNA (5'- 1CIT
CMP D(*CP*CP*GP*AP*AP*AP*AP*GP*GP*TP*CP*AP*TP*GP*CP*G)-3'); 1CIT
CMP CHAIN: B; 1CIT
CMP ENGINEERED: YES; 1CIT
CMP MOL_ID: 2; 1CIT
CMP MOLECULE: DNA (5'- 1CIT
CMP D(*CP*GP*CP*AP*TP*GP*AP*CP*CP*TP*TP*TP*TP*CP*GP*G)-3'); 1CIT
CMP CHAIN: C; 1CIT
CMP ENGINEERED: YES; 1CIT
CMP MOL_ID: 3; 1CIT
CMP MOLECULE: PROTEIN (ORPHAN NUCLEAR RECEPTOR NGFI-B); 1CIT
CMP CHAIN: A; 1CIT
CMP FRAGMENT: DNA-BINDING DOMAIN AND C-TERMINAL EXTENSION; 1CIT
CMP SYNONYM: NGFI-B; 1CIT
CMP ENGINEERED: YES 1CIT
SRC MOL_ID: 1; 1CIT
SRC SYNTHETIC: YES; 1CIT
SRC MOL_ID: 2; 1CIT
SRC SYNTHETIC: YES; 1CIT
SRC MOL_ID: 3; 1CIT
SRC ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS; 1CIT
SRC ORGANISM_COMMON: NORWAY RAT; 1CIT
SRC ORGANISM_TAXID: 10116; 1CIT
SRC ORGAN: BRAIN; 1CIT
SRC CELLULAR_LOCATION: NUCLEUS; 1CIT
SRC EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); 1CIT
SRC EXPRESSION_SYSTEM_TAXID: 469008; 1CIT
SRC EXPRESSION_SYSTEM_STRAIN: BL21(DE3); 1CIT
SRC EXPRESSION_SYSTEM_PLASMID: PET11A 1CIT
AUT G.MEINKE,P.B.SIGLER 1CIT
REM 1CIT
REM -------------------- Secondary structure summary ------------------- 1CIT
REM 1CIT
CHN /data/npidb/pdb/pdb_new/all/pdb1cit.pdb A 1CIT
REM 1CIT
REM . . . . . 1CIT
SEQ 1 GRCAVCGDNASCQHYGVRTCEGCKGFFKRTVQKSAKYICLANKDCPVDKR 50 1CIT
STR TTTTT EEETTEEE HHHHHHHHHHHHH TTTT TTT 1CIT
REM 1CIT
REM . . . 1CIT
SEQ 51 RRNRCQFCRFQKCLAVGMVKEVVRTDSLKGRRGRLPSKP 89 1CIT
STR TTTTTHHHHHHHHHHH GGG GGGTTT 1CIT
REM 1CIT
REM 1CIT
REM 1CIT
LOC AlphaHelix GLU 250 A LYS 262 A 1CIT
LOC AlphaHelix GLN 285 A VAL 295 A 1CIT
LOC 310Helix LYS 299 A VAL 301 A 1CIT
LOC 310Helix ASP 305 A LEU 307 A 1CIT
LOC Strand CYS 241 A HIS 243 A 1CIT
LOC Strand VAL 246 A THR 248 A 1CIT
LOC TurnIV CYS 232 A CYS 235 A 1CIT
LOC TurnIV ALA 233 A GLY 236 A 1CIT
LOC TurnIV GLN 242 A GLY 245 A 1CIT
LOC TurnI' HIS 243 A VAL 246 A 1CIT
LOC TurnIV CYS 268 A ASN 271 A 1CIT
LOC TurnI ASP 277 A ARG 280 A 1CIT
LOC TurnI LYS 278 A ARG 281 A 1CIT
LOC TurnI ARG 280 A ARG 283 A 1CIT
LOC TurnIV ARG 281 A CYS 284 A 1CIT
LOC TurnVIII ASN 282 A GLN 285 A 1CIT
LOC TurnII LEU 307 A ARG 310 A 1CIT
REM 1CIT
REM --------------- Detailed secondary structure assignment------------- 1CIT
REM 1CIT
REM |---Residue---| |--Structure--| |-Phi-| |-Psi-| |-Area-| 1CIT
ASG GLY A 230 1 C Coil 360.00 -178.20 87.8 1CIT
ASG ARG A 231 2 C Coil -129.77 -14.92 155.0 1CIT
ASG CYS A 232 3 T Turn -67.02 123.47 6.6 1CIT
ASG ALA A 233 4 T Turn -71.32 -2.09 43.7 1CIT
ASG VAL A 234 5 T Turn -107.49 -62.52 3.7 1CIT
ASG CYS A 235 6 T Turn -99.71 -20.48 8.4 1CIT
ASG GLY A 236 7 T Turn 97.41 -3.33 30.9 1CIT
ASG ASP A 237 8 C Coil -57.83 -176.92 20.5 1CIT
ASG ASN A 238 9 C Coil -79.76 143.50 118.7 1CIT
ASG ALA A 239 10 C Coil -138.19 141.21 15.8 1CIT
ASG SER A 240 11 C Coil -109.03 -23.20 94.6 1CIT
ASG CYS A 241 12 E Strand -158.41 -172.19 55.4 1CIT
ASG GLN A 242 13 E Strand -81.10 148.45 116.3 1CIT
ASG HIS A 243 14 E Strand -145.13 117.89 22.8 1CIT
ASG TYR A 244 15 T Turn 50.34 46.71 40.3 1CIT
ASG GLY A 245 16 T Turn 85.36 -11.80 48.2 1CIT
ASG VAL A 246 17 E Strand -131.65 141.19 15.9 1CIT
ASG ARG A 247 18 E Strand -56.84 103.27 77.6 1CIT
ASG THR A 248 19 E Strand -135.37 167.26 0.6 1CIT
ASG CYS A 249 20 C Coil -94.92 166.38 4.1 1CIT
ASG GLU A 250 21 H AlphaHelix -59.08 -29.16 128.3 1CIT
ASG GLY A 251 22 H AlphaHelix -63.97 -67.74 22.4 1CIT
ASG CYS A 252 23 H AlphaHelix -58.09 -32.65 0.0 1CIT
ASG LYS A 253 24 H AlphaHelix -46.35 -70.48 57.9 1CIT
ASG GLY A 254 25 H AlphaHelix -58.35 -37.08 8.8 1CIT
ASG PHE A 255 26 H AlphaHelix -56.09 -52.42 7.0 1CIT
ASG PHE A 256 27 H AlphaHelix -56.58 -46.22 0.0 1CIT
ASG LYS A 257 28 H AlphaHelix -59.21 -65.92 78.4 1CIT
ASG ARG A 258 29 H AlphaHelix -46.66 -48.77 124.1 1CIT
ASG THR A 259 30 H AlphaHelix -52.50 -57.88 1.6 1CIT
ASG VAL A 260 31 H AlphaHelix -59.89 -40.59 25.8 1CIT
ASG GLN A 261 32 H AlphaHelix -63.74 -68.37 97.2 1CIT
ASG LYS A 262 33 H AlphaHelix -56.40 -11.00 158.3 1CIT
ASG SER A 263 34 C Coil 59.17 27.74 96.9 1CIT
ASG ALA A 264 35 C Coil -52.05 144.65 37.2 1CIT
ASG LYS A 265 36 C Coil -118.41 118.10 96.8 1CIT
ASG TYR A 266 37 C Coil -99.65 167.00 44.2 1CIT
ASG ILE A 267 38 C Coil -144.08 132.01 142.1 1CIT
ASG CYS A 268 39 T Turn -89.72 124.91 14.1 1CIT
ASG LEU A 269 40 T Turn -71.99 -34.55 176.0 1CIT
ASG ALA A 270 41 T Turn -83.30 -122.22 54.6 1CIT
ASG ASN A 271 42 T Turn -129.76 45.82 147.4 1CIT
ASG LYS A 272 43 C Coil 51.05 38.81 101.8 1CIT
ASG ASP A 273 44 C Coil -152.59 25.65 140.5 1CIT
ASG CYS A 274 45 C Coil -54.46 155.35 33.0 1CIT
ASG PRO A 275 46 C Coil -70.94 122.84 69.9 1CIT
ASG VAL A 276 47 C Coil -110.91 96.79 28.5 1CIT
ASG ASP A 277 48 T Turn -141.04 176.78 31.5 1CIT
ASG LYS A 278 49 T Turn -55.78 -27.57 114.2 1CIT
ASG ARG A 279 50 T Turn -93.16 -31.25 181.1 1CIT
ASG ARG A 280 51 T Turn -116.40 24.48 92.8 1CIT
ASG ARG A 281 52 T Turn -72.15 -20.87 33.8 1CIT
ASG ASN A 282 53 T Turn -96.12 -8.55 115.5 1CIT
ASG ARG A 283 54 T Turn -64.67 -35.63 209.8 1CIT
ASG CYS A 284 55 T Turn -137.27 126.66 21.1 1CIT
ASG GLN A 285 56 H AlphaHelix -78.65 -59.33 104.4 1CIT
ASG PHE A 286 57 H AlphaHelix -35.85 -58.69 41.4 1CIT
ASG CYS A 287 58 H AlphaHelix -57.11 -34.97 3.1 1CIT
ASG ARG A 288 59 H AlphaHelix -70.68 -39.46 8.2 1CIT
ASG PHE A 289 60 H AlphaHelix -71.83 -39.63 30.3 1CIT
ASG GLN A 290 61 H AlphaHelix -52.93 -46.75 83.7 1CIT
ASG LYS A 291 62 H AlphaHelix -68.60 -40.30 78.3 1CIT
ASG CYS A 292 63 H AlphaHelix -48.11 -42.61 0.0 1CIT
ASG LEU A 293 64 H AlphaHelix -76.23 -40.99 69.2 1CIT
ASG ALA A 294 65 H AlphaHelix -52.24 -47.87 81.5 1CIT
ASG VAL A 295 66 H AlphaHelix -79.39 7.28 45.1 1CIT
ASG GLY A 296 67 C Coil 77.37 45.19 39.2 1CIT
ASG MET A 297 68 C Coil -80.97 131.09 6.6 1CIT
ASG VAL A 298 69 C Coil -86.84 114.29 46.8 1CIT
ASG LYS A 299 70 G 310Helix -63.18 -26.19 109.7 1CIT
ASG GLU A 300 71 G 310Helix -70.99 -23.65 174.2 1CIT
ASG VAL A 301 72 G 310Helix -76.00 -11.73 73.6 1CIT
ASG VAL A 302 73 C Coil -79.79 103.00 5.2 1CIT
ASG ARG A 303 74 C Coil -46.39 144.23 71.4 1CIT
ASG THR A 304 75 C Coil -153.65 174.44 67.9 1CIT
ASG ASP A 305 76 G 310Helix 48.86 -132.36 128.4 1CIT
ASG SER A 306 77 G 310Helix -48.37 -29.44 126.9 1CIT
ASG LEU A 307 78 G 310Helix -90.53 0.18 66.1 1CIT
ASG LYS A 308 79 T Turn -65.20 131.38 169.2 1CIT
ASG GLY A 309 80 T Turn 85.18 -11.34 75.0 1CIT
ASG ARG A 310 81 T Turn -74.85 125.52 106.8 1CIT
ASG ARG A 311 82 C Coil -103.52 -177.93 220.3 1CIT
ASG GLY A 312 83 C Coil 56.51 -175.16 54.9 1CIT
ASG ARG A 313 84 C Coil -73.06 142.40 226.4 1CIT
ASG LEU A 314 85 C Coil -80.44 163.67 70.3 1CIT
ASG PRO A 315 86 C Coil -85.06 144.37 107.4 1CIT
ASG SER A 316 87 C Coil -125.58 -22.75 123.1 1CIT
ASG LYS A 317 88 C Coil -108.41 133.21 77.0 1CIT
ASG PRO A 318 89 C Coil -54.17 360.00 198.6 1CIT