HEADER TRANSLATION 05-AUG-15 5ABB
TITLE VISUALIZATION OF A POLYTOPIC MEMBRANE PROTEIN DURING SECY-MEDIATED
TITLE 2 MEMBRANE INSERTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN TRANSLOCASE SUBUNIT SECY;
COMPND 3 CHAIN: A;
COMPND 4 MOL_ID: 2;
COMPND 5 MOLECULE: PROTEIN TRANSLOCASE SUBUNIT SECE;
COMPND 6 CHAIN: B;
COMPND 7 FRAGMENT: UNP RESIDUES 12-127;
COMPND 8 MOL_ID: 3;
COMPND 9 MOLECULE: GREEN-LIGHT ABSORBING PROTEORHODOPSIN;
COMPND 10 CHAIN: Z;
COMPND 11 FRAGMENT: UNP RESIDUES 19-83;
COMPND 12 SYNONYM: GPR
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 MOL_ID: 2;
SOURCE 5 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 6 ORGANISM_TAXID: 562;
SOURCE 7 MOL_ID: 3;
SOURCE 8 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 9 ORGANISM_TAXID: 562
KEYWDS TRANSLATION, RIBOSOME, MEMBRANE PROTEIN, TRANSLOCON
EXPDTA ELECTRON MICROSCOPY
AUTHOR L.BISCHOFF,S.WICKLES,O.BERNINGHAUSEN,E.VANDERSLUIS,R.BECKMANN
REVDAT 2 30-AUG-17 5ABB 1 REMARK
REVDAT 1 19-AUG-15 5ABB 0
JRNL AUTH L.BISCHOFF,S.WICKLES,O.BERNINGHAUSEN,E.O.VAN DER SLUIS,
JRNL AUTH 2 R.BECKMANN
JRNL TITL VISUALIZATION OF A POLYTOPIC MEMBRANE PROTEIN DURING
JRNL TITL 2 SECY-MEDIATED MEMBRANE INSERTION.
JRNL REF NAT.COMMUN. V. 5 4103 2014
JRNL REFN ESSN 2041-1723
JRNL PMID 24912953
JRNL DOI 10.1038/NCOMMS5103
REMARK 2
REMARK 2 RESOLUTION. 8.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 SOFTWARE PACKAGES : COOT, SPIDER
REMARK 3 RECONSTRUCTION SCHEMA : NULL
REMARK 3
REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT
REMARK 3 PDB ENTRY : NULL
REMARK 3 REFINEMENT SPACE : NULL
REMARK 3 REFINEMENT PROTOCOL : NULL
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL
REMARK 3
REMARK 3 FITTING PROCEDURE : NULL
REMARK 3
REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS
REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : NULL
REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL
REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 8.000
REMARK 3 NUMBER OF PARTICLES : 47471
REMARK 3 CTF CORRECTION METHOD : NULL
REMARK 3
REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL
REMARK 3
REMARK 3 OTHER DETAILS: NULL
REMARK 4
REMARK 4 5ABB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE.
REMARK 100 THE DEPOSITION ID IS D_1290064597.
REMARK 245
REMARK 245 EXPERIMENTAL DETAILS
REMARK 245 RECONSTRUCTION METHOD : SINGLE PARTICLE
REMARK 245 SPECIMEN TYPE : NULL
REMARK 245
REMARK 245 ELECTRON MICROSCOPE SAMPLE
REMARK 245 SAMPLE TYPE : PARTICLE
REMARK 245 PARTICLE TYPE : POINT
REMARK 245 NAME OF SAMPLE : TNAC STALLED E.COLI RIBOSOME IN
REMARK 245 COMPLEX WITH SECYE
REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : NULL
REMARK 245 SAMPLE SUPPORT DETAILS : HOLEY CARBON
REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL
REMARK 245 SAMPLE BUFFER : 20 MM TRIS 150 MM NH4CL 10 MM
REMARK 245 MGCL2 0.05%DDM 125 MM SUCROSE
REMARK 245 PH : 7.50
REMARK 245 SAMPLE DETAILS : NULL
REMARK 245
REMARK 245 DATA ACQUISITION
REMARK 245 DATE OF EXPERIMENT : 21-MAY-12
REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL
REMARK 245 TEMPERATURE (KELVIN) : NULL
REMARK 245 MICROSCOPE MODEL : FEI TITAN KRIOS
REMARK 245 DETECTOR TYPE : TVIPS TEMCAM-F416 (4K X 4K)
REMARK 245 MINIMUM DEFOCUS (NM) : 1000.00
REMARK 245 MAXIMUM DEFOCUS (NM) : 3500.00
REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 NOMINAL CS : NULL
REMARK 245 IMAGING MODE : BRIGHT FIELD
REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 20.00
REMARK 245 ILLUMINATION MODE : SPOT SCAN
REMARK 245 NOMINAL MAGNIFICATION : 148721
REMARK 245 CALIBRATED MAGNIFICATION : NULL
REMARK 245 SOURCE : FIELD EMISSION GUN
REMARK 245 ACCELERATION VOLTAGE (KV) : 200
REMARK 245 IMAGING DETAILS : NULL
REMARK 247
REMARK 247 ELECTRON MICROSCOPY
REMARK 247 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON
REMARK 247 MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE
REMARK 247 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES
REMARK 247 ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION
REMARK 247 OF THE STRUCTURE FACTORS.
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, Z
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 MET A 1 CB CG SD CE
REMARK 470 ALA A 2 CB
REMARK 470 LYS A 3 CB CG CD CE NZ
REMARK 470 GLN A 4 CB CG CD OE1 NE2
REMARK 470 PRO A 5 CB CG CD
REMARK 470 LEU A 7 CB CG CD1 CD2
REMARK 470 ASP A 8 CB CG OD1 OD2
REMARK 470 PHE A 9 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLN A 10 CB CG CD OE1 NE2
REMARK 470 SER A 11 CB OG
REMARK 470 ALA A 12 CB
REMARK 470 LYS A 13 CB CG CD CE NZ
REMARK 470 LEU A 16 CB CG CD1 CD2
REMARK 470 GLU A 18 CB CG CD OE1 OE2
REMARK 470 LEU A 19 CB CG CD1 CD2
REMARK 470 LYS A 20 CB CG CD CE NZ
REMARK 470 ARG A 21 CB CG CD NE CZ NH1 NH2
REMARK 470 ARG A 22 CB CG CD NE CZ NH1 NH2
REMARK 470 LEU A 23 CB CG CD1 CD2
REMARK 470 LEU A 24 CB CG CD1 CD2
REMARK 470 PHE A 25 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 470 VAL A 26 CB CG1 CG2
REMARK 470 ILE A 27 CB CG1 CG2 CD1
REMARK 470 ALA A 29 CB
REMARK 470 LEU A 30 CB CG CD1 CD2
REMARK 470 ILE A 31 CB CG1 CG2 CD1
REMARK 470 VAL A 32 CB CG1 CG2
REMARK 470 PHE A 33 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG A 34 CB CG CD NE CZ NH1 NH2
REMARK 470 ILE A 35 CB CG1 CG2 CD1
REMARK 470 SER A 37 CB OG
REMARK 470 PHE A 38 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ILE A 39 CB CG1 CG2 CD1
REMARK 470 PRO A 40 CB CG CD
REMARK 470 ILE A 41 CB CG1 CG2 CD1
REMARK 470 PRO A 42 CB CG CD
REMARK 470 ILE A 44 CB CG1 CG2 CD1
REMARK 470 ASP A 45 CB CG OD1 OD2
REMARK 470 ALA A 46 CB
REMARK 470 ALA A 47 CB
REMARK 470 VAL A 48 CB CG1 CG2
REMARK 470 LEU A 49 CB CG CD1 CD2
REMARK 470 ALA A 50 CB
REMARK 470 LYS A 51 CB CG CD CE NZ
REMARK 470 LEU A 52 CB CG CD1 CD2
REMARK 470 LEU A 53 CB CG CD1 CD2
REMARK 470 GLU A 54 CB CG CD OE1 OE2
REMARK 470 GLN A 55 CB CG CD OE1 NE2
REMARK 470 GLN A 56 CB CG CD OE1 NE2
REMARK 470 ARG A 57 CB CG CD NE CZ NH1 NH2
REMARK 470 THR A 59 CB OG1 CG2
REMARK 470 ILE A 60 CB CG1 CG2 CD1
REMARK 470 ILE A 61 CB CG1 CG2 CD1
REMARK 470 GLU A 62 CB CG CD OE1 OE2
REMARK 470 MET A 63 CB CG SD CE
REMARK 470 PHE A 64 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASN A 65 CB CG OD1 ND2
REMARK 470 MET A 66 CB CG SD CE
REMARK 470 PHE A 67 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 470 SER A 68 CB OG
REMARK 470 ALA A 71 CB
REMARK 470 LEU A 72 CB CG CD1 CD2
REMARK 470 SER A 73 CB OG
REMARK 470 ARG A 74 CB CG CD NE CZ NH1 NH2
REMARK 470 ALA A 75 CB
REMARK 470 SER A 76 CB OG
REMARK 470 ILE A 77 CB CG1 CG2 CD1
REMARK 470 PHE A 78 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ALA A 79 CB
REMARK 470 LEU A 80 CB CG CD1 CD2
REMARK 470 ILE A 82 CB CG1 CG2 CD1
REMARK 470 MET A 83 CB CG SD CE
REMARK 470 PRO A 84 CB CG CD
REMARK 470 TYR A 85 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 470 TYR A 85 OH
REMARK 470 ILE A 86 CB CG1 CG2 CD1
REMARK 470 SER A 87 CB OG
REMARK 470 ALA A 88 CB
REMARK 470 SER A 89 CB OG
REMARK 470 ILE A 90 CB CG1 CG2 CD1
REMARK 470 ILE A 91 CB CG1 CG2 CD1
REMARK 470 ILE A 92 CB CG1 CG2 CD1
REMARK 470 GLN A 93 CB CG CD OE1 NE2
REMARK 470 LEU A 94 CB CG CD1 CD2
REMARK 470 LEU A 95 CB CG CD1 CD2
REMARK 470 THR A 96 CB OG1 CG2
REMARK 470 VAL A 97 CB CG1 CG2
REMARK 470 VAL A 98 CB CG1 CG2
REMARK 470 HIS A 99 CB CG ND1 CD2 CE1 NE2
REMARK 470 PRO A 100 CB CG CD
REMARK 470 THR A 101 CB OG1 CG2
REMARK 470 LEU A 102 CB CG CD1 CD2
REMARK 470 ALA A 103 CB
REMARK 470 GLU A 104 CB CG CD OE1 OE2
REMARK 470 ILE A 105 CB CG1 CG2 CD1
REMARK 470 LYS A 106 CB CG CD CE NZ
REMARK 470 LYS A 107 CB CG CD CE NZ
REMARK 470 GLU A 108 CB CG CD OE1 OE2
REMARK 470 GLU A 110 CB CG CD OE1 OE2
REMARK 470 SER A 111 CB OG
REMARK 470 ARG A 113 CB CG CD NE CZ NH1 NH2
REMARK 470 ARG A 114 CB CG CD NE CZ NH1 NH2
REMARK 470 LYS A 115 CB CG CD CE NZ
REMARK 470 ILE A 116 CB CG1 CG2 CD1
REMARK 470 SER A 117 CB OG
REMARK 470 GLN A 118 CB CG CD OE1 NE2
REMARK 470 TYR A 119 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 470 TYR A 119 OH
REMARK 470 THR A 120 CB OG1 CG2
REMARK 470 ARG A 121 CB CG CD NE CZ NH1 NH2
REMARK 470 TYR A 122 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 470 TYR A 122 OH
REMARK 470 THR A 124 CB OG1 CG2
REMARK 470 LEU A 125 CB CG CD1 CD2
REMARK 470 VAL A 126 CB CG1 CG2
REMARK 470 LEU A 127 CB CG CD1 CD2
REMARK 470 ALA A 128 CB
REMARK 470 ILE A 129 CB CG1 CG2 CD1
REMARK 470 PHE A 130 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLN A 131 CB CG CD OE1 NE2
REMARK 470 SER A 132 CB OG
REMARK 470 ILE A 133 CB CG1 CG2 CD1
REMARK 470 ILE A 135 CB CG1 CG2 CD1
REMARK 470 ALA A 136 CB
REMARK 470 THR A 137 CB OG1 CG2
REMARK 470 LEU A 139 CB CG CD1 CD2
REMARK 470 PRO A 140 CB CG CD
REMARK 470 ASN A 141 CB CG OD1 ND2
REMARK 470 MET A 142 CB CG SD CE
REMARK 470 PRO A 143 CB CG CD
REMARK 470 MET A 145 CB CG SD CE
REMARK 470 GLN A 146 CB CG CD OE1 NE2
REMARK 470 LEU A 148 CB CG CD1 CD2
REMARK 470 VAL A 149 CB CG1 CG2
REMARK 470 ILE A 150 CB CG1 CG2 CD1
REMARK 470 ASN A 151 CB CG OD1 ND2
REMARK 470 PRO A 152 CB CG CD
REMARK 470 PHE A 154 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ALA A 155 CB
REMARK 470 PHE A 156 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 470 TYR A 157 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 470 TYR A 157 OH
REMARK 470 PHE A 158 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 470 THR A 159 CB OG1 CG2
REMARK 470 ALA A 160 CB
REMARK 470 VAL A 161 CB CG1 CG2
REMARK 470 VAL A 162 CB CG1 CG2
REMARK 470 SER A 163 CB OG
REMARK 470 LEU A 164 CB CG CD1 CD2
REMARK 470 VAL A 165 CB CG1 CG2
REMARK 470 THR A 166 CB OG1 CG2
REMARK 470 THR A 168 CB OG1 CG2
REMARK 470 MET A 169 CB CG SD CE
REMARK 470 PHE A 170 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LEU A 171 CB CG CD1 CD2
REMARK 470 MET A 172 CB CG SD CE
REMARK 470 TRP A 173 CB CG CD1 CD2 NE1 CE2 CE3
REMARK 470 TRP A 173 CZ2 CZ3 CH2
REMARK 470 LEU A 174 CB CG CD1 CD2
REMARK 470 GLU A 176 CB CG CD OE1 OE2
REMARK 470 GLN A 177 CB CG CD OE1 NE2
REMARK 470 ILE A 178 CB CG1 CG2 CD1
REMARK 470 THR A 179 CB OG1 CG2
REMARK 470 GLU A 180 CB CG CD OE1 OE2
REMARK 470 ARG A 181 CB CG CD NE CZ NH1 NH2
REMARK 470 ILE A 183 CB CG1 CG2 CD1
REMARK 470 ASN A 185 CB CG OD1 ND2
REMARK 470 ILE A 187 CB CG1 CG2 CD1
REMARK 470 SER A 188 CB OG
REMARK 470 ILE A 189 CB CG1 CG2 CD1
REMARK 470 ILE A 190 CB CG1 CG2 CD1
REMARK 470 ILE A 191 CB CG1 CG2 CD1
REMARK 470 PHE A 192 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ALA A 193 CB
REMARK 470 ILE A 195 CB CG1 CG2 CD1
REMARK 470 VAL A 196 CB CG1 CG2
REMARK 470 ALA A 197 CB
REMARK 470 LEU A 199 CB CG CD1 CD2
REMARK 470 PRO A 200 CB CG CD
REMARK 470 PRO A 201 CB CG CD
REMARK 470 ALA A 202 CB
REMARK 470 ILE A 203 CB CG1 CG2 CD1
REMARK 470 ALA A 204 CB
REMARK 470 HIS A 205 CB CG ND1 CD2 CE1 NE2
REMARK 470 THR A 206 CB OG1 CG2
REMARK 470 ILE A 207 CB CG1 CG2 CD1
REMARK 470 GLU A 208 CB CG CD OE1 OE2
REMARK 470 GLN A 209 CB CG CD OE1 NE2
REMARK 470 ALA A 210 CB
REMARK 470 ARG A 211 CB CG CD NE CZ NH1 NH2
REMARK 470 GLN A 212 CB CG CD OE1 NE2
REMARK 470 ASP A 214 CB CG OD1 OD2
REMARK 470 LEU A 215 CB CG CD1 CD2
REMARK 470 HIS A 216 CB CG ND1 CD2 CE1 NE2
REMARK 470 PHE A 217 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LEU A 218 CB CG CD1 CD2
REMARK 470 VAL A 219 CB CG1 CG2
REMARK 470 LEU A 220 CB CG CD1 CD2
REMARK 470 LEU A 221 CB CG CD1 CD2
REMARK 470 LEU A 222 CB CG CD1 CD2
REMARK 470 VAL A 223 CB CG1 CG2
REMARK 470 ALA A 224 CB
REMARK 470 VAL A 225 CB CG1 CG2
REMARK 470 LEU A 226 CB CG CD1 CD2
REMARK 470 VAL A 227 CB CG1 CG2
REMARK 470 PHE A 228 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ALA A 229 CB
REMARK 470 VAL A 230 CB CG1 CG2
REMARK 470 THR A 231 CB OG1 CG2
REMARK 470 PHE A 232 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 470 PHE A 233 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 470 VAL A 234 CB CG1 CG2
REMARK 470 VAL A 235 CB CG1 CG2
REMARK 470 PHE A 236 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 470 VAL A 237 CB CG1 CG2
REMARK 470 GLU A 238 CB CG CD OE1 OE2
REMARK 470 ARG A 239 CB CG CD NE CZ NH1 NH2
REMARK 470 GLN A 241 CB CG CD OE1 NE2
REMARK 470 ARG A 242 CB CG CD NE CZ NH1 NH2
REMARK 470 ARG A 243 CB CG CD NE CZ NH1 NH2
REMARK 470 ILE A 244 CB CG1 CG2 CD1
REMARK 470 VAL A 245 CB CG1 CG2
REMARK 470 VAL A 246 CB CG1 CG2
REMARK 470 ASN A 247 CB CG OD1 ND2
REMARK 470 TYR A 248 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 470 TYR A 248 OH
REMARK 470 ALA A 249 CB
REMARK 470 LYS A 250 CB CG CD CE NZ
REMARK 470 ARG A 251 CB CG CD NE CZ NH1 NH2
REMARK 470 GLN A 252 CB CG CD OE1 NE2
REMARK 470 GLN A 253 CB CG CD OE1 NE2
REMARK 470 ARG A 255 CB CG CD NE CZ NH1 NH2
REMARK 470 ARG A 256 CB CG CD NE CZ NH1 NH2
REMARK 470 VAL A 257 CB CG1 CG2
REMARK 470 TYR A 258 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 470 TYR A 258 OH
REMARK 470 ALA A 259 CB
REMARK 470 ALA A 260 CB
REMARK 470 GLN A 261 CB CG CD OE1 NE2
REMARK 470 SER A 262 CB OG
REMARK 470 THR A 263 CB OG1 CG2
REMARK 470 HIS A 264 CB CG ND1 CD2 CE1 NE2
REMARK 470 LEU A 265 CB CG CD1 CD2
REMARK 470 PRO A 266 CB CG CD
REMARK 470 LEU A 267 CB CG CD1 CD2
REMARK 470 LYS A 268 CB CG CD CE NZ
REMARK 470 VAL A 269 CB CG1 CG2
REMARK 470 ASN A 270 CB CG OD1 ND2
REMARK 470 MET A 271 CB CG SD CE
REMARK 470 ALA A 272 CB
REMARK 470 VAL A 274 CB CG1 CG2
REMARK 470 ILE A 275 CB CG1 CG2 CD1
REMARK 470 PRO A 276 CB CG CD
REMARK 470 ALA A 277 CB
REMARK 470 ILE A 278 CB CG1 CG2 CD1
REMARK 470 PHE A 279 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ALA A 280 CB
REMARK 470 SER A 281 CB OG
REMARK 470 SER A 282 CB OG
REMARK 470 ILE A 283 CB CG1 CG2 CD1
REMARK 470 ILE A 284 CB CG1 CG2 CD1
REMARK 470 LEU A 285 CB CG CD1 CD2
REMARK 470 PHE A 286 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 470 PRO A 287 CB CG CD
REMARK 470 ALA A 288 CB
REMARK 470 THR A 289 CB OG1 CG2
REMARK 470 ILE A 290 CB CG1 CG2 CD1
REMARK 470 ALA A 291 CB
REMARK 470 SER A 292 CB OG
REMARK 470 TRP A 293 CB CG CD1 CD2 NE1 CE2 CE3
REMARK 470 TRP A 293 CZ2 CZ3 CH2
REMARK 470 PHE A 294 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 470 THR A 298 CB OG1 CG2
REMARK 470 TRP A 300 CB CG CD1 CD2 NE1 CE2 CE3
REMARK 470 TRP A 300 CZ2 CZ3 CH2
REMARK 470 ASN A 301 CB CG OD1 ND2
REMARK 470 TRP A 302 CB CG CD1 CD2 NE1 CE2 CE3
REMARK 470 TRP A 302 CZ2 CZ3 CH2
REMARK 470 LEU A 303 CB CG CD1 CD2
REMARK 470 THR A 304 CB OG1 CG2
REMARK 470 THR A 305 CB OG1 CG2
REMARK 470 ILE A 306 CB CG1 CG2 CD1
REMARK 470 SER A 307 CB OG
REMARK 470 LEU A 308 CB CG CD1 CD2
REMARK 470 TYR A 309 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 470 TYR A 309 OH
REMARK 470 LEU A 310 CB CG CD1 CD2
REMARK 470 GLN A 311 CB CG CD OE1 NE2
REMARK 470 PRO A 312 CB CG CD
REMARK 470 GLN A 314 CB CG CD OE1 NE2
REMARK 470 PRO A 315 CB CG CD
REMARK 470 LEU A 316 CB CG CD1 CD2
REMARK 470 TYR A 317 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 470 TYR A 317 OH
REMARK 470 VAL A 318 CB CG1 CG2
REMARK 470 LEU A 319 CB CG CD1 CD2
REMARK 470 LEU A 320 CB CG CD1 CD2
REMARK 470 TYR A 321 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 470 TYR A 321 OH
REMARK 470 ALA A 322 CB
REMARK 470 SER A 323 CB OG
REMARK 470 ALA A 324 CB
REMARK 470 ILE A 325 CB CG1 CG2 CD1
REMARK 470 ILE A 326 CB CG1 CG2 CD1
REMARK 470 PHE A 327 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 470 PHE A 328 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 470 CYS A 329 CB SG
REMARK 470 PHE A 330 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 470 PHE A 331 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 470 TYR A 332 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 470 TYR A 332 OH
REMARK 470 THR A 333 CB OG1 CG2
REMARK 470 ALA A 334 CB
REMARK 470 LEU A 335 CB CG CD1 CD2
REMARK 470 VAL A 336 CB CG1 CG2
REMARK 470 PHE A 337 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASN A 338 CB CG OD1 ND2
REMARK 470 PRO A 339 CB CG CD
REMARK 470 ARG A 340 CB CG CD NE CZ NH1 NH2
REMARK 470 GLU A 341 CB CG CD OE1 OE2
REMARK 470 THR A 342 CB OG1 CG2
REMARK 470 ALA A 343 CB
REMARK 470 ASP A 344 CB CG OD1 OD2
REMARK 470 ASN A 345 CB CG OD1 ND2
REMARK 470 LEU A 346 CB CG CD1 CD2
REMARK 470 LYS A 347 CB CG CD CE NZ
REMARK 470 LYS A 348 CB CG CD CE NZ
REMARK 470 SER A 349 CB OG
REMARK 470 ALA A 351 CB
REMARK 470 PHE A 352 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 470 VAL A 353 CB CG1 CG2
REMARK 470 PRO A 354 CB CG CD
REMARK 470 ILE A 356 CB CG1 CG2 CD1
REMARK 470 ARG A 357 CB CG CD NE CZ NH1 NH2
REMARK 470 PRO A 358 CB CG CD
REMARK 470 GLU A 360 CB CG CD OE1 OE2
REMARK 470 GLN A 361 CB CG CD OE1 NE2
REMARK 470 THR A 362 CB OG1 CG2
REMARK 470 ALA A 363 CB
REMARK 470 LYS A 364 CB CG CD CE NZ
REMARK 470 TYR A 365 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 470 TYR A 365 OH
REMARK 470 ILE A 366 CB CG1 CG2 CD1
REMARK 470 ASP A 367 CB CG OD1 OD2
REMARK 470 LYS A 368 CB CG CD CE NZ
REMARK 470 VAL A 369 CB CG1 CG2
REMARK 470 MET A 370 CB CG SD CE
REMARK 470 THR A 371 CB OG1 CG2
REMARK 470 ARG A 372 CB CG CD NE CZ NH1 NH2
REMARK 470 LEU A 373 CB CG CD1 CD2
REMARK 470 THR A 374 CB OG1 CG2
REMARK 470 LEU A 375 CB CG CD1 CD2
REMARK 470 VAL A 376 CB CG1 CG2
REMARK 470 ALA A 378 CB
REMARK 470 LEU A 379 CB CG CD1 CD2
REMARK 470 TYR A 380 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 470 TYR A 380 OH
REMARK 470 ILE A 381 CB CG1 CG2 CD1
REMARK 470 THR A 382 CB OG1 CG2
REMARK 470 PHE A 383 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ILE A 384 CB CG1 CG2 CD1
REMARK 470 CYS A 385 CB SG
REMARK 470 LEU A 386 CB CG CD1 CD2
REMARK 470 ILE A 387 CB CG1 CG2 CD1
REMARK 470 PRO A 388 CB CG CD
REMARK 470 GLU A 389 CB CG CD OE1 OE2
REMARK 470 PHE A 390 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 470 MET A 391 CB CG SD CE
REMARK 470 ARG A 392 CB CG CD NE CZ NH1 NH2
REMARK 470 ASP A 393 CB CG OD1 OD2
REMARK 470 ALA A 394 CB
REMARK 470 MET A 395 CB CG SD CE
REMARK 470 LYS A 396 CB CG CD CE NZ
REMARK 470 VAL A 397 CB CG1 CG2
REMARK 470 PRO A 398 CB CG CD
REMARK 470 PHE A 399 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 470 TYR A 400 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 470 TYR A 400 OH
REMARK 470 PHE A 401 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 470 THR A 404 CB OG1 CG2
REMARK 470 SER A 405 CB OG
REMARK 470 LEU A 406 CB CG CD1 CD2
REMARK 470 LEU A 407 CB CG CD1 CD2
REMARK 470 ILE A 408 CB CG1 CG2 CD1
REMARK 470 VAL A 409 CB CG1 CG2
REMARK 470 VAL A 410 CB CG1 CG2
REMARK 470 VAL A 411 CB CG1 CG2
REMARK 470 VAL A 412 CB CG1 CG2
REMARK 470 ILE A 413 CB CG1 CG2 CD1
REMARK 470 MET A 414 CB CG SD CE
REMARK 470 ASP A 415 CB CG OD1 OD2
REMARK 470 PHE A 416 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 470 MET A 417 CB CG SD CE
REMARK 470 ALA A 418 CB
REMARK 470 GLN A 419 CB CG CD OE1 NE2
REMARK 470 VAL A 420 CB CG1 CG2
REMARK 470 GLN A 421 CB CG CD OE1 NE2
REMARK 470 THR A 422 CB OG1 CG2
REMARK 470 LEU A 423 CB CG CD1 CD2
REMARK 470 MET A 424 CB CG SD CE
REMARK 470 MET A 425 CB CG SD CE
REMARK 470 SER A 426 CB OG
REMARK 470 SER A 427 CB OG
REMARK 470 GLN A 428 CB CG CD OE1 NE2
REMARK 470 TYR A 429 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 470 TYR A 429 OH
REMARK 470 GLU A 430 CB CG CD OE1 OE2
REMARK 470 SER A 431 CB OG
REMARK 470 ALA A 432 CB
REMARK 470 LEU A 433 CB CG CD1 CD2
REMARK 470 LYS A 434 CB CG CD CE NZ
REMARK 470 LYS A 435 CB CG CD CE NZ
REMARK 470 ALA A 436 CB
REMARK 470 ASN A 437 CB CG OD1 ND2
REMARK 470 LEU A 438 CB CG CD1 CD2
REMARK 470 LYS A 439 CB CG CD CE NZ
REMARK 470 TYR A 441 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 470 TYR A 441 OH
REMARK 470 ARG A 443 CB CG CD NE CZ NH1 NH2
REMARK 470 ARG B 12 CB CG CD NE CZ NH1 NH2
REMARK 470 LEU B 14 CB CG CD1 CD2
REMARK 470 GLU B 15 CB CG CD OE1 OE2
REMARK 470 ALA B 16 CB
REMARK 470 MET B 17 CB CG SD CE
REMARK 470 LYS B 18 CB CG CD CE NZ
REMARK 470 TRP B 19 CB CG CD1 CD2 NE1 CE2 CE3
REMARK 470 TRP B 19 CZ2 CZ3 CH2
REMARK 470 VAL B 20 CB CG1 CG2
REMARK 470 VAL B 21 CB CG1 CG2
REMARK 470 VAL B 22 CB CG1 CG2
REMARK 470 VAL B 23 CB CG1 CG2
REMARK 470 ALA B 24 CB
REMARK 470 LEU B 25 CB CG CD1 CD2
REMARK 470 LEU B 26 CB CG CD1 CD2
REMARK 470 LEU B 27 CB CG CD1 CD2
REMARK 470 VAL B 28 CB CG1 CG2
REMARK 470 ALA B 29 CB
REMARK 470 ILE B 30 CB CG1 CG2 CD1
REMARK 470 VAL B 31 CB CG1 CG2
REMARK 470 ASN B 33 CB CG OD1 ND2
REMARK 470 TYR B 34 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 470 TYR B 34 OH
REMARK 470 LEU B 35 CB CG CD1 CD2
REMARK 470 TYR B 36 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 470 TYR B 36 OH
REMARK 470 ARG B 37 CB CG CD NE CZ NH1 NH2
REMARK 470 ASP B 38 CB CG OD1 OD2
REMARK 470 ILE B 39 CB CG1 CG2 CD1
REMARK 470 MET B 40 CB CG SD CE
REMARK 470 LEU B 41 CB CG CD1 CD2
REMARK 470 PRO B 42 CB CG CD
REMARK 470 LEU B 43 CB CG CD1 CD2
REMARK 470 ARG B 44 CB CG CD NE CZ NH1 NH2
REMARK 470 ALA B 45 CB
REMARK 470 LEU B 46 CB CG CD1 CD2
REMARK 470 ALA B 47 CB
REMARK 470 VAL B 48 CB CG1 CG2
REMARK 470 VAL B 49 CB CG1 CG2
REMARK 470 ILE B 50 CB CG1 CG2 CD1
REMARK 470 LEU B 51 CB CG CD1 CD2
REMARK 470 ILE B 52 CB CG1 CG2 CD1
REMARK 470 ALA B 53 CB
REMARK 470 ALA B 54 CB
REMARK 470 ALA B 55 CB
REMARK 470 VAL B 58 CB CG1 CG2
REMARK 470 ALA B 59 CB
REMARK 470 LEU B 60 CB CG CD1 CD2
REMARK 470 LEU B 61 CB CG CD1 CD2
REMARK 470 THR B 62 CB OG1 CG2
REMARK 470 THR B 63 CB OG1 CG2
REMARK 470 LYS B 64 CB CG CD CE NZ
REMARK 470 LYS B 66 CB CG CD CE NZ
REMARK 470 ALA B 67 CB
REMARK 470 THR B 68 CB OG1 CG2
REMARK 470 VAL B 69 CB CG1 CG2
REMARK 470 ALA B 70 CB
REMARK 470 PHE B 71 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ALA B 72 CB
REMARK 470 ARG B 73 CB CG CD NE CZ NH1 NH2
REMARK 470 GLU B 74 CB CG CD OE1 OE2
REMARK 470 ALA B 75 CB
REMARK 470 ARG B 76 CB CG CD NE CZ NH1 NH2
REMARK 470 THR B 77 CB OG1 CG2
REMARK 470 GLU B 78 CB CG CD OE1 OE2
REMARK 470 VAL B 79 CB CG1 CG2
REMARK 470 ARG B 80 CB CG CD NE CZ NH1 NH2
REMARK 470 LYS B 81 CB CG CD CE NZ
REMARK 470 VAL B 82 CB CG1 CG2
REMARK 470 ILE B 83 CB CG1 CG2 CD1
REMARK 470 TRP B 84 CB CG CD1 CD2 NE1 CE2 CE3
REMARK 470 TRP B 84 CZ2 CZ3 CH2
REMARK 470 PRO B 85 CB CG CD
REMARK 470 THR B 86 CB OG1 CG2
REMARK 470 ARG B 87 CB CG CD NE CZ NH1 NH2
REMARK 470 GLN B 88 CB CG CD OE1 NE2
REMARK 470 GLU B 89 CB CG CD OE1 OE2
REMARK 470 THR B 90 CB OG1 CG2
REMARK 470 LEU B 91 CB CG CD1 CD2
REMARK 470 HIS B 92 CB CG ND1 CD2 CE1 NE2
REMARK 470 THR B 93 CB OG1 CG2
REMARK 470 THR B 94 CB OG1 CG2
REMARK 470 LEU B 95 CB CG CD1 CD2
REMARK 470 ILE B 96 CB CG1 CG2 CD1
REMARK 470 VAL B 97 CB CG1 CG2
REMARK 470 ALA B 98 CB
REMARK 470 ALA B 99 CB
REMARK 470 VAL B 100 CB CG1 CG2
REMARK 470 THR B 101 CB OG1 CG2
REMARK 470 ALA B 102 CB
REMARK 470 VAL B 103 CB CG1 CG2
REMARK 470 MET B 104 CB CG SD CE
REMARK 470 SER B 105 CB OG
REMARK 470 LEU B 106 CB CG CD1 CD2
REMARK 470 ILE B 107 CB CG1 CG2 CD1
REMARK 470 LEU B 108 CB CG CD1 CD2
REMARK 470 TRP B 109 CB CG CD1 CD2 NE1 CE2 CE3
REMARK 470 TRP B 109 CZ2 CZ3 CH2
REMARK 470 LEU B 111 CB CG CD1 CD2
REMARK 470 ASP B 112 CB CG OD1 OD2
REMARK 470 ILE B 114 CB CG1 CG2 CD1
REMARK 470 LEU B 115 CB CG CD1 CD2
REMARK 470 VAL B 116 CB CG1 CG2
REMARK 470 ARG B 117 CB CG CD NE CZ NH1 NH2
REMARK 470 LEU B 118 CB CG CD1 CD2
REMARK 470 VAL B 119 CB CG1 CG2
REMARK 470 SER B 120 CB OG
REMARK 470 PHE B 121 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ILE B 122 CB CG1 CG2 CD1
REMARK 470 THR B 123 CB OG1 CG2
REMARK 470 LEU B 125 CB CG CD1 CD2
REMARK 470 ARG B 126 CB CG CD NE CZ NH1 NH2
REMARK 470 PHE B 127 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASP Z 22 CB CG OD1 OD2
REMARK 470 LEU Z 23 CB CG CD1 CD2
REMARK 470 ASP Z 24 CB CG OD1 OD2
REMARK 470 ALA Z 25 CB
REMARK 470 SER Z 26 CB OG
REMARK 470 ASP Z 27 CB CG OD1 OD2
REMARK 470 TYR Z 28 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 470 TYR Z 28 OH
REMARK 470 THR Z 29 CB OG1 CG2
REMARK 470 VAL Z 31 CB CG1 CG2
REMARK 470 SER Z 32 CB OG
REMARK 470 PHE Z 33 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 470 TRP Z 34 CB CG CD1 CD2 NE1 CE2 CE3
REMARK 470 TRP Z 34 CZ2 CZ3 CH2
REMARK 470 LEU Z 35 CB CG CD1 CD2
REMARK 470 VAL Z 36 CB CG1 CG2
REMARK 470 THR Z 37 CB OG1 CG2
REMARK 470 ALA Z 38 CB
REMARK 470 ALA Z 39 CB
REMARK 470 LEU Z 40 CB CG CD1 CD2
REMARK 470 LEU Z 41 CB CG CD1 CD2
REMARK 470 ALA Z 42 CB
REMARK 470 SER Z 43 CB OG
REMARK 470 THR Z 44 CB OG1 CG2
REMARK 470 VAL Z 45 CB CG1 CG2
REMARK 470 PHE Z 46 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 470 PHE Z 47 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 470 PHE Z 48 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 470 VAL Z 49 CB CG1 CG2
REMARK 470 GLU Z 50 CB CG CD OE1 OE2
REMARK 470 ARG Z 51 CB CG CD NE CZ NH1 NH2
REMARK 470 ASP Z 52 CB CG OD1 OD2
REMARK 470 ARG Z 53 CB CG CD NE CZ NH1 NH2
REMARK 470 VAL Z 54 CB CG1 CG2
REMARK 470 SER Z 55 CB OG
REMARK 470 ALA Z 56 CB
REMARK 470 LYS Z 57 CB CG CD CE NZ
REMARK 470 TRP Z 58 CB CG CD1 CD2 NE1 CE2 CE3
REMARK 470 TRP Z 58 CZ2 CZ3 CH2
REMARK 470 LYS Z 59 CB CG CD CE NZ
REMARK 470 THR Z 60 CB OG1 CG2
REMARK 470 SER Z 61 CB OG
REMARK 470 LEU Z 62 CB CG CD1 CD2
REMARK 470 THR Z 63 CB OG1 CG2
REMARK 470 VAL Z 64 CB CG1 CG2
REMARK 470 SER Z 65 CB OG
REMARK 470 LEU Z 67 CB CG CD1 CD2
REMARK 470 VAL Z 68 CB CG1 CG2
REMARK 470 THR Z 69 CB OG1 CG2
REMARK 470 ILE Z 71 CB CG1 CG2 CD1
REMARK 470 ALA Z 72 CB
REMARK 470 PHE Z 73 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 470 TRP Z 74 CB CG CD1 CD2 NE1 CE2 CE3
REMARK 470 TRP Z 74 CZ2 CZ3 CH2
REMARK 470 HIS Z 75 CB CG ND1 CD2 CE1 NE2
REMARK 470 TYR Z 76 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 470 TYR Z 76 OH
REMARK 470 MET Z 77 CB CG SD CE
REMARK 470 TYR Z 78 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 470 TYR Z 78 OH
REMARK 470 MET Z 79 CB CG SD CE
REMARK 470 ARG Z 80 CB CG CD NE CZ NH1 NH2
REMARK 470 VAL Z 82 CB CG1 CG2
REMARK 470 TRP Z 83 CB CG CD1 CD2 NE1 CE2 CE3
REMARK 470 TRP Z 83 CZ2 CZ3 CH2
REMARK 470 THR Z 84 CB OG1 CG2
REMARK 470 ALA Z 85 CB
REMARK 470 ARG Z 87 CB CG CD NE CZ NH1 NH2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ASN A 301 C - N - CA ANGL. DEV. = 18.0 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 PHE A 9 108.34 -58.44
REMARK 500 LEU A 16 -52.23 -147.54
REMARK 500 GLU A 18 -88.75 -79.60
REMARK 500 PRO A 42 22.76 -78.49
REMARK 500 GLN A 55 -9.67 -57.19
REMARK 500 GLN A 56 -14.76 59.89
REMARK 500 ARG A 57 -8.46 -144.12
REMARK 500 THR A 59 -8.00 -155.75
REMARK 500 ILE A 60 178.29 59.83
REMARK 500 ILE A 61 -41.95 64.50
REMARK 500 GLU A 62 -35.36 60.86
REMARK 500 MET A 63 -32.93 -38.69
REMARK 500 PHE A 64 -15.27 -46.91
REMARK 500 ALA A 79 -6.41 -56.98
REMARK 500 ILE A 82 -13.72 57.97
REMARK 500 PRO A 143 48.04 -108.06
REMARK 500 MET A 145 7.96 -153.95
REMARK 500 PHE A 217 -172.05 -59.41
REMARK 500 LEU A 218 -12.16 67.69
REMARK 500 VAL A 246 -44.02 -138.40
REMARK 500 ASN A 247 83.66 42.81
REMARK 500 GLN A 252 -111.84 -110.74
REMARK 500 GLN A 253 -44.98 -154.29
REMARK 500 ARG A 255 20.77 -71.27
REMARK 500 VAL A 257 142.86 55.38
REMARK 500 SER A 262 165.54 59.65
REMARK 500 LYS A 268 -163.12 -123.99
REMARK 500 PHE A 294 36.18 -89.32
REMARK 500 ASN A 301 143.23 69.10
REMARK 500 THR A 304 -52.61 54.61
REMARK 500 THR A 305 -103.18 -40.65
REMARK 500 ILE A 306 59.07 -68.79
REMARK 500 SER A 307 -63.90 -15.70
REMARK 500 PRO A 312 101.53 -5.69
REMARK 500 VAL A 336 -5.03 -57.78
REMARK 500 PHE A 337 27.43 94.98
REMARK 500 ARG A 340 -53.05 -122.12
REMARK 500 ALA A 343 -36.45 -142.95
REMARK 500 ALA A 351 -176.25 58.73
REMARK 500 THR A 371 5.96 -65.71
REMARK 500 MET A 395 -109.98 -153.12
REMARK 500 LYS A 396 -43.72 -148.64
REMARK 500 VAL A 397 105.98 -22.76
REMARK 500 SER A 427 50.46 -163.25
REMARK 500 TYR A 429 -85.48 -57.83
REMARK 500 GLU A 430 52.60 26.05
REMARK 500 ALA A 432 69.09 -157.27
REMARK 500 LEU A 433 97.35 -65.70
REMARK 500 LYS A 435 -55.22 -142.01
REMARK 500 ASN A 437 -178.94 55.27
REMARK 500
REMARK 500 THIS ENTRY HAS 79 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 HIS A 99 PRO A 100 -146.54
REMARK 500 ILE A 183 GLY A 184 137.04
REMARK 500 GLU A 238 ARG A 239 145.63
REMARK 500 ALA A 272 GLY A 273 -148.77
REMARK 500 GLY A 299 TRP A 300 -145.85
REMARK 500 GLU B 15 ALA B 16 -149.71
REMARK 500 LEU B 61 THR B 62 136.15
REMARK 500 THR B 62 THR B 63 -105.25
REMARK 500 ASP B 112 GLY B 113 149.34
REMARK 500 VAL Z 64 SER Z 65 -147.88
REMARK 500 VAL Z 82 TRP Z 83 -149.72
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 LEU A 16 -10.55
REMARK 500 ASN A 65 -13.39
REMARK 500 LYS A 115 -12.85
REMARK 500 ILE A 183 -12.12
REMARK 500 ALA A 204 -10.81
REMARK 500 LEU A 218 -10.36
REMARK 500 PHE A 286 -11.86
REMARK 500 TRP A 300 -11.20
REMARK 500 THR A 305 14.04
REMARK 500 PRO A 312 -11.99
REMARK 500 ARG A 340 -11.89
REMARK 500 ILE A 366 -10.12
REMARK 500 MET A 370 -14.10
REMARK 500 LEU A 373 -11.07
REMARK 500 LEU A 375 -10.57
REMARK 500 GLU A 389 -12.70
REMARK 500 ASP A 393 -10.97
REMARK 500 GLY A 403 -11.40
REMARK 500 TRP B 19 -11.58
REMARK 500 PRO B 42 10.88
REMARK 500 ALA B 59 -10.27
REMARK 500 LEU B 61 -16.68
REMARK 500 THR B 62 -11.36
REMARK 500 ASP B 112 -10.70
REMARK 500 TRP Z 58 -10.79
REMARK 500 LEU Z 67 -13.38
REMARK 500 ILE Z 71 11.83
REMARK 500 ALA Z 72 -10.37
REMARK 500 TYR Z 78 -10.98
REMARK 500 ARG Z 80 -10.60
REMARK 500 VAL Z 82 13.08
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: EMD-2446 RELATED DB: EMDB
DBREF 5ABB A 1 443 UNP B7MCR5 B7MCR5_ECO45 1 443
DBREF 5ABB B 12 127 UNP B7MIW7 B7MIW7_ECO45 12 127
DBREF 5ABB Z 19 83 UNP Q9F7P4 PRRG_PRB01 19 83
SEQADV 5ABB THR Z 84 UNP Q9F7P4 EXPRESSION TAG
SEQADV 5ABB ALA Z 85 UNP Q9F7P4 EXPRESSION TAG
SEQADV 5ABB GLY Z 86 UNP Q9F7P4 EXPRESSION TAG
SEQADV 5ABB ARG Z 87 UNP Q9F7P4 EXPRESSION TAG
SEQRES 1 A 443 MET ALA LYS GLN PRO GLY LEU ASP PHE GLN SER ALA LYS
SEQRES 2 A 443 GLY GLY LEU GLY GLU LEU LYS ARG ARG LEU LEU PHE VAL
SEQRES 3 A 443 ILE GLY ALA LEU ILE VAL PHE ARG ILE GLY SER PHE ILE
SEQRES 4 A 443 PRO ILE PRO GLY ILE ASP ALA ALA VAL LEU ALA LYS LEU
SEQRES 5 A 443 LEU GLU GLN GLN ARG GLY THR ILE ILE GLU MET PHE ASN
SEQRES 6 A 443 MET PHE SER GLY GLY ALA LEU SER ARG ALA SER ILE PHE
SEQRES 7 A 443 ALA LEU GLY ILE MET PRO TYR ILE SER ALA SER ILE ILE
SEQRES 8 A 443 ILE GLN LEU LEU THR VAL VAL HIS PRO THR LEU ALA GLU
SEQRES 9 A 443 ILE LYS LYS GLU GLY GLU SER GLY ARG ARG LYS ILE SER
SEQRES 10 A 443 GLN TYR THR ARG TYR GLY THR LEU VAL LEU ALA ILE PHE
SEQRES 11 A 443 GLN SER ILE GLY ILE ALA THR GLY LEU PRO ASN MET PRO
SEQRES 12 A 443 GLY MET GLN GLY LEU VAL ILE ASN PRO GLY PHE ALA PHE
SEQRES 13 A 443 TYR PHE THR ALA VAL VAL SER LEU VAL THR GLY THR MET
SEQRES 14 A 443 PHE LEU MET TRP LEU GLY GLU GLN ILE THR GLU ARG GLY
SEQRES 15 A 443 ILE GLY ASN GLY ILE SER ILE ILE ILE PHE ALA GLY ILE
SEQRES 16 A 443 VAL ALA GLY LEU PRO PRO ALA ILE ALA HIS THR ILE GLU
SEQRES 17 A 443 GLN ALA ARG GLN GLY ASP LEU HIS PHE LEU VAL LEU LEU
SEQRES 18 A 443 LEU VAL ALA VAL LEU VAL PHE ALA VAL THR PHE PHE VAL
SEQRES 19 A 443 VAL PHE VAL GLU ARG GLY GLN ARG ARG ILE VAL VAL ASN
SEQRES 20 A 443 TYR ALA LYS ARG GLN GLN GLY ARG ARG VAL TYR ALA ALA
SEQRES 21 A 443 GLN SER THR HIS LEU PRO LEU LYS VAL ASN MET ALA GLY
SEQRES 22 A 443 VAL ILE PRO ALA ILE PHE ALA SER SER ILE ILE LEU PHE
SEQRES 23 A 443 PRO ALA THR ILE ALA SER TRP PHE GLY GLY GLY THR GLY
SEQRES 24 A 443 TRP ASN TRP LEU THR THR ILE SER LEU TYR LEU GLN PRO
SEQRES 25 A 443 GLY GLN PRO LEU TYR VAL LEU LEU TYR ALA SER ALA ILE
SEQRES 26 A 443 ILE PHE PHE CYS PHE PHE TYR THR ALA LEU VAL PHE ASN
SEQRES 27 A 443 PRO ARG GLU THR ALA ASP ASN LEU LYS LYS SER GLY ALA
SEQRES 28 A 443 PHE VAL PRO GLY ILE ARG PRO GLY GLU GLN THR ALA LYS
SEQRES 29 A 443 TYR ILE ASP LYS VAL MET THR ARG LEU THR LEU VAL GLY
SEQRES 30 A 443 ALA LEU TYR ILE THR PHE ILE CYS LEU ILE PRO GLU PHE
SEQRES 31 A 443 MET ARG ASP ALA MET LYS VAL PRO PHE TYR PHE GLY GLY
SEQRES 32 A 443 THR SER LEU LEU ILE VAL VAL VAL VAL ILE MET ASP PHE
SEQRES 33 A 443 MET ALA GLN VAL GLN THR LEU MET MET SER SER GLN TYR
SEQRES 34 A 443 GLU SER ALA LEU LYS LYS ALA ASN LEU LYS GLY TYR GLY
SEQRES 35 A 443 ARG
SEQRES 1 B 116 ARG GLY LEU GLU ALA MET LYS TRP VAL VAL VAL VAL ALA
SEQRES 2 B 116 LEU LEU LEU VAL ALA ILE VAL GLY ASN TYR LEU TYR ARG
SEQRES 3 B 116 ASP ILE MET LEU PRO LEU ARG ALA LEU ALA VAL VAL ILE
SEQRES 4 B 116 LEU ILE ALA ALA ALA GLY GLY VAL ALA LEU LEU THR THR
SEQRES 5 B 116 LYS GLY LYS ALA THR VAL ALA PHE ALA ARG GLU ALA ARG
SEQRES 6 B 116 THR GLU VAL ARG LYS VAL ILE TRP PRO THR ARG GLN GLU
SEQRES 7 B 116 THR LEU HIS THR THR LEU ILE VAL ALA ALA VAL THR ALA
SEQRES 8 B 116 VAL MET SER LEU ILE LEU TRP GLY LEU ASP GLY ILE LEU
SEQRES 9 B 116 VAL ARG LEU VAL SER PHE ILE THR GLY LEU ARG PHE
SEQRES 1 Z 69 GLY GLY GLY ASP LEU ASP ALA SER ASP TYR THR GLY VAL
SEQRES 2 Z 69 SER PHE TRP LEU VAL THR ALA ALA LEU LEU ALA SER THR
SEQRES 3 Z 69 VAL PHE PHE PHE VAL GLU ARG ASP ARG VAL SER ALA LYS
SEQRES 4 Z 69 TRP LYS THR SER LEU THR VAL SER GLY LEU VAL THR GLY
SEQRES 5 Z 69 ILE ALA PHE TRP HIS TYR MET TYR MET ARG GLY VAL TRP
SEQRES 6 Z 69 THR ALA GLY ARG
HELIX 1 1 LEU A 19 SER A 37 1 19
HELIX 2 2 ALA A 46 GLN A 55 1 10
HELIX 3 3 ASN A 65 GLY A 69 5 5
HELIX 4 4 ILE A 82 HIS A 99 1 18
HELIX 5 5 HIS A 99 GLY A 109 1 11
HELIX 6 6 GLY A 109 LEU A 139 1 31
HELIX 7 7 GLY A 153 ARG A 181 1 29
HELIX 8 8 ASN A 185 ALA A 197 1 13
HELIX 9 9 GLY A 198 ARG A 211 1 14
HELIX 10 10 LEU A 218 GLN A 241 1 24
HELIX 11 11 GLY A 273 PHE A 294 1 22
HELIX 12 12 GLN A 314 LEU A 335 1 22
HELIX 13 13 GLU A 360 ALA A 394 1 35
HELIX 14 14 PRO A 398 GLY A 402 5 5
HELIX 15 15 GLY A 403 MET A 425 1 23
HELIX 16 16 ARG B 12 ALA B 16 5 5
HELIX 17 17 LYS B 18 VAL B 23 1 6
HELIX 18 18 VAL B 23 GLY B 32 1 10
HELIX 19 19 PRO B 42 VAL B 48 1 7
HELIX 20 20 VAL B 49 LEU B 60 1 12
HELIX 21 21 ALA B 75 TRP B 84 1 10
HELIX 22 22 THR B 90 ALA B 99 1 10
HELIX 23 23 VAL B 100 LEU B 111 1 12
HELIX 24 24 ILE B 114 PHE B 121 1 8
HELIX 25 25 LEU Z 23 VAL Z 49 1 27
HELIX 26 26 VAL Z 64 THR Z 84 1 21
CISPEP 1 GLY A 14 GLY A 15 0 -17.14
CISPEP 2 ARG A 251 GLN A 252 0 -2.63
CISPEP 3 GLN A 261 SER A 262 0 3.61
CISPEP 4 ASN A 301 TRP A 302 0 -10.15
CISPEP 5 GLY A 313 GLN A 314 0 -0.28
CISPEP 6 GLY A 350 ALA A 351 0 -6.97
CISPEP 7 ALA A 351 PHE A 352 0 -2.99
CISPEP 8 GLU A 430 SER A 431 0 10.35
CISPEP 9 LYS A 434 LYS A 435 0 -6.93
CISPEP 10 MET B 17 LYS B 18 0 19.68
CISPEP 11 GLN B 88 GLU B 89 0 17.92
CISPEP 12 SER Z 55 ALA Z 56 0 -2.89
CISPEP 13 TRP Z 58 LYS Z 59 0 -28.02
CISPEP 14 THR Z 84 ALA Z 85 0 -6.43
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
