Документ взят из кэша поисковой машины. Адрес оригинального документа : http://monkey.belozersky.msu.ru/npidb/pdb/pdb_new/stride/2kh9.std.txt
Дата изменения: Tue Jan 18 07:22:34 2011
Дата индексирования: Fri Feb 11 17:56:42 2011
Кодировка:
REM -------------------------------------------------------------------- 2KH9
REM 2KH9
REM STRIDE: Knowledge-based secondary structure assignment 2KH9
REM Please cite: D.Frishman & P.Argos, Proteins 23, 566-579, 1995 2KH9
REM 2KH9
REM Residue accessible surface area calculation 2KH9
REM Please cite: F.Eisenhaber & P.Argos, J.Comp.Chem. 14, 1272-1280, 1993 2KH9
REM F.Eisenhaber et al., J.Comp.Chem., 1994, submitted 2KH9
REM 2KH9
REM ------------------------ General information ----------------------- 2KH9
REM 2KH9
HDR SPLICING/RNA 27-MAR-09 2KH9 2KH9
CMP MOL_ID: 1; 2KH9
CMP MOLECULE: U4/U6 SNRNA-ASSOCIATED-SPLICING FACTOR PRP24; 2KH9
CMP CHAIN: A; 2KH9
CMP FRAGMENT: UNP RESIDUES 115-197; 2KH9
CMP SYNONYM: U4/U6 SNRNP PROTEIN; 2KH9
CMP ENGINEERED: YES; 2KH9
CMP MOL_ID: 2; 2KH9
CMP MOLECULE: 5'-R(*AP*GP*AP*GP*AP*U)-3'; 2KH9
CMP CHAIN: B; 2KH9
CMP ENGINEERED: YES 2KH9
SRC MOL_ID: 1; 2KH9
SRC ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE; 2KH9
SRC ORGANISM_COMMON: YEAST; 2KH9
SRC ORGANISM_TAXID: 4932; 2KH9
SRC GENE: PRP24, YMR268C, YM8156.10C; 2KH9
SRC EXPRESSION_SYSTEM: ESCHERICHIA COLI; 2KH9
SRC EXPRESSION_SYSTEM_TAXID: 562; 2KH9
SRC EXPRESSION_SYSTEM_STRAIN: BL21; 2KH9
SRC EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; 2KH9
SRC EXPRESSION_SYSTEM_PLASMID: PET21B; 2KH9
SRC MOL_ID: 2; 2KH9
SRC SYNTHETIC: YES; 2KH9
SRC OTHER_DETAILS: SYNTHETIC RNA 2KH9
AUT S.A.MARTIN-TUMASZ,S.E.BUTCHER 2KH9
REM 2KH9
REM -------------------- Secondary structure summary ------------------- 2KH9
REM 2KH9
CHN /data/npidb/pdb/pdb_new/all/pdb2kh9.pdb A 2KH9
REM 2KH9
REM . . . . . 2KH9
SEQ 1 MTECTLWMTNFPPSYTQRNIRDLLQDINVVALSIRLPSLRFNTSRRFAYI 50 2KH9
STR EEEEEb TTTTTHHHHHHHHHHH EEEEE TTTTTTTT EEE 2KH9
REM 2KH9
REM . . . 2KH9
SEQ 51 DVTSKEDARYCVEKLNGLKIEGYTLVTKVSNPLELE 86 2KH9
STR EETTTHHHHHHHHHHTTEEETTEEEEEEE TTTT 2KH9
REM 2KH9
REM 2KH9
REM 2KH9
LOC AlphaHelix GLN 130 A ILE 140 A 2KH9
LOC AlphaHelix GLU 169 A LEU 178 A 2KH9
LOC Strand THR 118 A THR 122 A 2KH9
LOC Strand ALA 144 A ARG 148 A 2KH9
LOC Strand ALA 161 A VAL 165 A 2KH9
LOC Strand LEU 181 A ILE 183 A 2KH9
LOC Strand TYR 186 A VAL 192 A 2KH9
LOC TurnIV PRO 125 A TYR 128 A 2KH9
LOC TurnVIII PRO 126 A THR 129 A 2KH9
LOC TurnVIII ALA 144 A ILE 147 A 2KH9
LOC TurnIV LEU 152 A ASN 155 A 2KH9
LOC TurnIV THR 156 A ARG 159 A 2KH9
LOC TurnIV VAL 165 A LYS 168 A 2KH9
LOC TurnII LEU 178 A LEU 181 A 2KH9
LOC TurnIV LYS 182 A GLY 185 A 2KH9
LOC TurnI' ILE 183 A TYR 186 A 2KH9
LOC TurnIV PRO 195 A LEU 198 A 2KH9
REM 2KH9
REM --------------- Detailed secondary structure assignment------------- 2KH9
REM 2KH9
REM |---Residue---| |--Structure--| |-Phi-| |-Psi-| |-Area-| 2KH9
ASG MET A 114 1 C Coil 360.00 21.78 123.3 2KH9
ASG THR A 115 2 C Coil -140.74 -7.51 99.8 2KH9
ASG GLU A 116 3 C Coil -105.44 -155.32 14.8 2KH9
ASG CYS A 117 4 C Coil 160.50 -12.97 35.3 2KH9
ASG THR A 118 5 E Strand -104.64 120.88 49.7 2KH9
ASG LEU A 119 6 E Strand -94.49 158.68 0.5 2KH9
ASG TRP A 120 7 E Strand -121.26 125.56 108.2 2KH9
ASG MET A 121 8 E Strand -114.55 129.17 0.2 2KH9
ASG THR A 122 9 E Strand -141.63 154.50 32.9 2KH9
ASG ASN A 123 10 b Bridge 43.47 110.32 75.9 2KH9
ASG PHE A 124 11 C Coil 171.96 138.65 5.8 2KH9
ASG PRO A 125 12 T Turn -60.11 151.07 2.4 2KH9
ASG PRO A 126 13 T Turn -68.15 13.11 61.9 2KH9
ASG SER A 127 14 T Turn -46.25 -39.85 76.2 2KH9
ASG TYR A 128 15 T Turn -87.22 115.71 43.8 2KH9
ASG THR A 129 16 T Turn -125.47 -172.61 55.2 2KH9
ASG GLN A 130 17 H AlphaHelix -60.91 -51.49 107.6 2KH9
ASG ARG A 131 18 H AlphaHelix -70.57 -33.05 131.8 2KH9
ASG ASN A 132 19 H AlphaHelix -79.69 -39.19 58.7 2KH9
ASG ILE A 133 20 H AlphaHelix -63.28 -32.70 1.8 2KH9
ASG ARG A 134 21 H AlphaHelix -77.69 -34.27 88.8 2KH9
ASG ASP A 135 22 H AlphaHelix -70.75 -46.54 66.1 2KH9
ASG LEU A 136 23 H AlphaHelix -61.20 -42.21 22.6 2KH9
ASG LEU A 137 24 H AlphaHelix -73.68 -39.81 0.0 2KH9
ASG GLN A 138 25 H AlphaHelix -79.17 -24.48 63.7 2KH9
ASG ASP A 139 26 H AlphaHelix -105.26 -50.74 125.9 2KH9
ASG ILE A 140 27 H AlphaHelix -69.53 -34.95 64.5 2KH9
ASG ASN A 141 28 C Coil -120.16 1.88 0.2 2KH9
ASG VAL A 142 29 C Coil 77.95 112.46 76.6 2KH9
ASG VAL A 143 30 C Coil 11.29 115.89 71.4 2KH9
ASG ALA A 144 31 E Strand -87.27 115.35 8.0 2KH9
ASG LEU A 145 32 E Strand -57.48 -47.91 96.9 2KH9
ASG SER A 146 33 E Strand -155.61 127.38 49.9 2KH9
ASG ILE A 147 34 E Strand -105.48 118.37 31.8 2KH9
ASG ARG A 148 35 E Strand -88.94 113.35 107.9 2KH9
ASG LEU A 149 36 C Coil -103.03 93.37 86.6 2KH9
ASG PRO A 150 37 C Coil -83.12 -35.72 30.7 2KH9
ASG SER A 151 38 C Coil -98.24 171.74 9.9 2KH9
ASG LEU A 152 39 T Turn 102.30 -1.43 77.0 2KH9
ASG ARG A 153 40 T Turn -81.80 -45.17 181.6 2KH9
ASG PHE A 154 41 T Turn -64.24 -46.47 133.0 2KH9
ASG ASN A 155 42 T Turn -179.60 -175.46 98.4 2KH9
ASG THR A 156 43 T Turn -71.27 17.46 54.8 2KH9
ASG SER A 157 44 T Turn -91.39 133.78 62.9 2KH9
ASG ARG A 158 45 T Turn 68.47 47.42 164.6 2KH9
ASG ARG A 159 46 T Turn -51.07 0.25 67.6 2KH9
ASG PHE A 160 47 C Coil -44.31 145.14 30.0 2KH9
ASG ALA A 161 48 E Strand -139.36 174.52 5.0 2KH9
ASG TYR A 162 49 E Strand -134.68 133.91 84.6 2KH9
ASG ILE A 163 50 E Strand -123.58 148.43 0.2 2KH9
ASG ASP A 164 51 E Strand -112.60 137.72 23.7 2KH9
ASG VAL A 165 52 E Strand -124.95 169.62 0.5 2KH9
ASG THR A 166 53 T Turn -64.94 -33.04 67.4 2KH9
ASG SER A 167 54 T Turn -158.77 -53.15 67.5 2KH9
ASG LYS A 168 55 T Turn 162.86 -38.89 2.2 2KH9
ASG GLU A 169 56 H AlphaHelix -50.13 -38.54 91.5 2KH9
ASG ASP A 170 57 H AlphaHelix -70.88 -56.32 16.7 2KH9
ASG ALA A 171 58 H AlphaHelix -59.74 -55.10 0.0 2KH9
ASG ARG A 172 59 H AlphaHelix -49.54 -31.08 77.6 2KH9
ASG TYR A 173 60 H AlphaHelix -70.56 -49.50 97.1 2KH9
ASG CYS A 174 61 H AlphaHelix -52.93 -54.11 0.0 2KH9
ASG VAL A 175 62 H AlphaHelix -56.56 -38.79 21.0 2KH9
ASG GLU A 176 63 H AlphaHelix -63.57 -43.58 136.7 2KH9
ASG LYS A 177 64 H AlphaHelix -67.84 -46.14 91.3 2KH9
ASG LEU A 178 65 H AlphaHelix -104.28 -11.78 12.0 2KH9
ASG ASN A 179 66 T Turn -67.55 132.09 82.9 2KH9
ASG GLY A 180 67 T Turn 85.56 20.39 29.2 2KH9
ASG LEU A 181 68 E Strand -92.25 126.69 67.6 2KH9
ASG LYS A 182 69 E Strand -97.47 102.50 147.7 2KH9
ASG ILE A 183 70 E Strand -120.18 115.33 33.2 2KH9
ASG GLU A 184 71 T Turn 66.08 17.13 151.6 2KH9
ASG GLY A 185 72 T Turn 103.72 2.35 71.2 2KH9
ASG TYR A 186 73 E Strand -117.81 137.58 101.5 2KH9
ASG THR A 187 74 E Strand -89.95 123.33 65.2 2KH9
ASG LEU A 188 75 E Strand -76.37 138.26 3.2 2KH9
ASG VAL A 189 76 E Strand -111.79 68.86 76.2 2KH9
ASG THR A 190 77 E Strand -87.01 121.61 1.2 2KH9
ASG LYS A 191 78 E Strand -140.33 154.85 94.4 2KH9
ASG VAL A 192 79 E Strand -101.79 168.58 11.0 2KH9
ASG SER A 193 80 C Coil -54.24 166.17 10.0 2KH9
ASG ASN A 194 81 C Coil -51.52 124.27 117.4 2KH9
ASG PRO A 195 82 T Turn -60.02 118.51 67.6 2KH9
ASG LEU A 196 83 T Turn -117.99 31.91 100.9 2KH9
ASG GLU A 197 84 T Turn -126.04 28.70 69.9 2KH9
ASG LEU A 198 85 T Turn -78.38 -55.32 149.4 2KH9
ASG GLU A 199 86 C Coil -144.72 360.00 226.3 2KH9