HEADER ELONGATION FACTOR 29-MAY-87 1EFM
TITLE STRUCTURE OF THE GDP DOMAIN OF EF-TU AND LOCATION OF THE AMINO ACIDS
TITLE 2 HOMOLOGOUS TO RAS ONCOGENE PROTEINS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ELONGATION FACTOR TU;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562
KEYWDS ELONGATION FACTOR
EXPDTA X-RAY DIFFRACTION
MDLTYP CA ATOMS ONLY, CHAIN A
AUTHOR F.JURNAK
REVDAT 4 07-FEB-24 1EFM 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1EFM 1 VERSN
REVDAT 2 15-OCT-91 1EFM 1 REMARK
REVDAT 1 16-JUL-87 1EFM 0
JRNL AUTH F.JURNAK
JRNL TITL STRUCTURE OF THE GDP DOMAIN OF EF-TU AND LOCATION OF THE
JRNL TITL 2 AMINO ACIDS HOMOLOGOUS TO RAS ONCOGENE PROTEINS.
JRNL REF SCIENCE V. 230 32 1985
JRNL REFN ISSN 0036-8075
JRNL PMID 3898365
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH F.JURNAK,A.MCPHERSON,A.H.J.WANG,A.RICH
REMARK 1 TITL BIOCHEMICAL AND STRUCTURAL STUDIES OF THE TETRAGONAL
REMARK 1 TITL 2 CRYSTALLINE MODIFICATION OF THE ESCHERICHIA COLI ELONGATION
REMARK 1 TITL 3 FACTOR TU
REMARK 1 REF J.BIOL.CHEM. V. 255 6751 1980
REMARK 1 REFN ISSN 0021-9258
REMARK 1 REFERENCE 2
REMARK 1 AUTH F.JURNAK,A.RICH,D.MILLER
REMARK 1 TITL PRELIMINARY X-RAY DIFFRACTION DATA FOR TETRAGONAL CRYSTALS
REMARK 1 TITL 2 OF TRYPSINIZED ESCHERICHIA COLI ELONGATION FACTOR
REMARK 1 REF J.MOL.BIOL. V. 115 103 1977
REMARK 1 REFN ISSN 0022-2836
REMARK 1 REFERENCE 3
REMARK 1 AUTH K.ARAI,B.F.C.CLARK,L.DUFFY,M.D.JONES,Y.KAZIRO,R.A.LAURSEN,
REMARK 1 AUTH 2 J.L'ITALIEN,D.L.MILLER,S.NAGARKATTI,S.NAKAMURA,K.M.NIELSEN,
REMARK 1 AUTH 3 T.E.PETERSEN,K.TAKAHASHI,M.WADE
REMARK 1 TITL PRIMARY STRUCTURE OF ELONGATION FACTOR TU FROM ESCHERICHIA
REMARK 1 TITL 2 COLI
REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 77 1326 1980
REMARK 1 REFN ISSN 0027-8424
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NULL
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : NULL
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : NULL
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : NULL
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 158
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 29
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1EFM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000173034.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : NULL
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 74.77
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.88
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 81.23250
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 81.23250
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 49.30450
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 50.40350
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 49.30450
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 50.40350
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 81.23250
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 49.30450
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 50.40350
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 81.23250
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 49.30450
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 50.40350
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 400
REMARK 400 COMPOUND
REMARK 400 TRYPSIN-MODIFIED EF-TU CONTAINS TWO MAJOR FRAGMENTS
REMARK 400 CONSISTING OF RESIDUES 1-44 AND 59-393. RESIDUES 45-58
REMARK 400 HAVE BEEN EXCISED. TO CLARIFY THIS RELATIONSHIP, THE
REMARK 400 PROTEIN IS REPRESENTED BY ONE SET OF SEQRES RECORDS WITH
REMARK 400 EXC IN PLACE OF RESIDUES 45-58.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 SER A 1
REMARK 465 LYS A 2
REMARK 465 GLU A 3
REMARK 465 LYS A 4
REMARK 465 PHE A 5
REMARK 465 GLU A 6
REMARK 465 ARG A 7
REMARK 465 THR A 8
REMARK 465 LYS A 9
REMARK 465 PRO A 10
REMARK 465 HIS A 11
REMARK 465 GLY A 40
REMARK 465 GLY A 41
REMARK 465 ALA A 42
REMARK 465 ALA A 43
REMARK 465 ARG A 44
REMARK 465 GLY A 59
REMARK 465 ILE A 60
REMARK 465 LEU A 191
REMARK 465 ALA A 192
REMARK 465 GLY A 193
REMARK 465 PHE A 194
REMARK 465 LEU A 195
REMARK 465 ASP A 196
REMARK 465 SER A 197
REMARK 465 TYR A 198
REMARK 465 ILE A 199
REMARK 465 PRO A 200
REMARK 465 GLU A 201
REMARK 465 PRO A 202
REMARK 465 GLU A 203
REMARK 465 ARG A 204
REMARK 465 ALA A 205
REMARK 465 ILE A 206
REMARK 465 ASP A 207
REMARK 465 LYS A 208
REMARK 465 PRO A 209
REMARK 465 PHE A 210
REMARK 465 LEU A 211
REMARK 465 LEU A 212
REMARK 465 PRO A 213
REMARK 465 ILE A 214
REMARK 465 GLU A 215
REMARK 465 ASP A 216
REMARK 465 VAL A 217
REMARK 465 PHE A 218
REMARK 465 SER A 219
REMARK 465 ILE A 220
REMARK 465 SER A 221
REMARK 465 GLY A 222
REMARK 465 ARG A 223
REMARK 465 GLY A 224
REMARK 465 THR A 225
REMARK 465 VAL A 226
REMARK 465 VAL A 227
REMARK 465 THR A 228
REMARK 465 GLY A 229
REMARK 465 ARG A 230
REMARK 465 VAL A 231
REMARK 465 GLU A 232
REMARK 465 ARG A 233
REMARK 465 GLY A 234
REMARK 465 ILE A 235
REMARK 465 ILE A 236
REMARK 465 LYS A 237
REMARK 465 VAL A 238
REMARK 465 GLY A 239
REMARK 465 GLU A 240
REMARK 465 GLU A 241
REMARK 465 VAL A 242
REMARK 465 GLU A 243
REMARK 465 ILE A 244
REMARK 465 VAL A 245
REMARK 465 GLY A 246
REMARK 465 ILE A 247
REMARK 465 LYS A 248
REMARK 465 GLU A 249
REMARK 465 THR A 250
REMARK 465 GLN A 251
REMARK 465 LYS A 252
REMARK 465 SER A 253
REMARK 465 THR A 254
REMARK 465 CYS A 255
REMARK 465 THR A 256
REMARK 465 GLY A 257
REMARK 465 VAL A 258
REMARK 465 GLU A 259
REMARK 465 MET A 260
REMARK 465 PHE A 261
REMARK 465 ARG A 262
REMARK 465 LYS A 263
REMARK 465 LEU A 264
REMARK 465 LEU A 265
REMARK 465 ASP A 266
REMARK 465 GLU A 267
REMARK 465 GLY A 268
REMARK 465 ARG A 269
REMARK 465 ALA A 270
REMARK 465 GLY A 271
REMARK 465 GLU A 272
REMARK 465 ASN A 273
REMARK 465 VAL A 274
REMARK 465 GLY A 275
REMARK 465 VAL A 276
REMARK 465 LEU A 277
REMARK 465 LEU A 278
REMARK 465 ARG A 279
REMARK 465 GLY A 280
REMARK 465 ILE A 281
REMARK 465 LYS A 282
REMARK 465 ARG A 283
REMARK 465 GLU A 284
REMARK 465 GLU A 285
REMARK 465 ILE A 286
REMARK 465 GLU A 287
REMARK 465 ARG A 288
REMARK 465 GLY A 289
REMARK 465 GLN A 290
REMARK 465 VAL A 291
REMARK 465 LEU A 292
REMARK 465 ALA A 293
REMARK 465 LYS A 294
REMARK 465 PRO A 295
REMARK 465 GLY A 296
REMARK 465 THR A 297
REMARK 465 ILE A 298
REMARK 465 LYS A 299
REMARK 465 PRO A 300
REMARK 465 HIS A 301
REMARK 465 THR A 302
REMARK 465 LYS A 303
REMARK 465 PHE A 304
REMARK 465 GLU A 305
REMARK 465 SER A 306
REMARK 465 GLU A 307
REMARK 465 VAL A 308
REMARK 465 TYR A 309
REMARK 465 ILE A 310
REMARK 465 LEU A 311
REMARK 465 SER A 312
REMARK 465 LYS A 313
REMARK 465 ASP A 314
REMARK 465 GLU A 315
REMARK 465 GLY A 316
REMARK 465 GLY A 317
REMARK 465 ARG A 318
REMARK 465 HIS A 319
REMARK 465 THR A 320
REMARK 465 PRO A 321
REMARK 465 PHE A 322
REMARK 465 PHE A 323
REMARK 465 LYS A 324
REMARK 465 GLY A 325
REMARK 465 TYR A 326
REMARK 465 ARG A 327
REMARK 465 PRO A 328
REMARK 465 GLN A 329
REMARK 465 PHE A 330
REMARK 465 TYR A 331
REMARK 465 PHE A 332
REMARK 465 ARG A 333
REMARK 465 THR A 334
REMARK 465 THR A 335
REMARK 465 ASP A 336
REMARK 465 VAL A 337
REMARK 465 THR A 338
REMARK 465 GLY A 339
REMARK 465 THR A 340
REMARK 465 ILE A 341
REMARK 465 GLU A 342
REMARK 465 LEU A 343
REMARK 465 PRO A 344
REMARK 465 GLU A 345
REMARK 465 GLY A 346
REMARK 465 VAL A 347
REMARK 465 GLU A 348
REMARK 465 MET A 349
REMARK 465 VAL A 350
REMARK 465 MET A 351
REMARK 465 PRO A 352
REMARK 465 GLY A 353
REMARK 465 ASP A 354
REMARK 465 ASN A 355
REMARK 465 ILE A 356
REMARK 465 LYS A 357
REMARK 465 MET A 358
REMARK 465 VAL A 359
REMARK 465 VAL A 360
REMARK 465 THR A 361
REMARK 465 LEU A 362
REMARK 465 ILE A 363
REMARK 465 HIS A 364
REMARK 465 PRO A 365
REMARK 465 ILE A 366
REMARK 465 ALA A 367
REMARK 465 MET A 368
REMARK 465 ASP A 369
REMARK 465 ASP A 370
REMARK 465 GLY A 371
REMARK 465 LEU A 372
REMARK 465 ARG A 373
REMARK 465 PHE A 374
REMARK 465 ALA A 375
REMARK 465 ILE A 376
REMARK 465 ARG A 377
REMARK 465 GLU A 378
REMARK 465 GLY A 379
REMARK 465 GLY A 380
REMARK 465 ARG A 381
REMARK 465 THR A 382
REMARK 465 VAL A 383
REMARK 465 GLY A 384
REMARK 465 ALA A 385
REMARK 465 GLY A 386
REMARK 465 VAL A 387
REMARK 465 VAL A 388
REMARK 465 ALA A 389
REMARK 465 LYS A 390
REMARK 465 VAL A 391
REMARK 465 LEU A 392
REMARK 465 SER A 393
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 394
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP A 395
DBREF 1EFM A 1 393 UNP P02990 EFTU_ECOLI 1 393
SEQADV 1EFM A UNP P02990 ALA 43 DELETION
SEQADV 1EFM A UNP P02990 ARG 44 DELETION
SEQADV 1EFM A UNP P02990 ALA 45 DELETION
SEQADV 1EFM A UNP P02990 PHE 46 DELETION
SEQADV 1EFM A UNP P02990 ASP 47 DELETION
SEQADV 1EFM A UNP P02990 GLN 48 DELETION
SEQADV 1EFM A UNP P02990 ILE 49 DELETION
SEQADV 1EFM A UNP P02990 ASP 50 DELETION
SEQADV 1EFM A UNP P02990 ASN 51 DELETION
SEQADV 1EFM A UNP P02990 ALA 52 DELETION
SEQADV 1EFM A UNP P02990 PRO 53 DELETION
SEQADV 1EFM A UNP P02990 GLU 54 DELETION
SEQADV 1EFM A UNP P02990 GLU 55 DELETION
SEQADV 1EFM A UNP P02990 LYS 56 DELETION
SEQRES 1 A 379 SER LYS GLU LYS PHE GLU ARG THR LYS PRO HIS VAL ASN
SEQRES 2 A 379 VAL GLY THR ILE GLY HIS VAL ASP HIS GLY LYS THR THR
SEQRES 3 A 379 LEU THR ALA ALA ILE THR THR VAL LEU ALA LYS THR TYR
SEQRES 4 A 379 GLY GLY ALA ALA ARG GLY ILE THR ILE ASN THR SER HIS
SEQRES 5 A 379 VAL GLU TYR ASP THR PRO THR ARG HIS TYR ALA HIS VAL
SEQRES 6 A 379 ASP CYS PRO GLY HIS ALA ASP TYR VAL LYS ASN MET ILE
SEQRES 7 A 379 THR GLY ALA ALA GLN MET ASP GLY ALA ILE LEU VAL VAL
SEQRES 8 A 379 ALA ALA THR ASP GLY PRO MET PRO GLN THR ARG GLU HIS
SEQRES 9 A 379 ILE LEU LEU GLY ARG GLN VAL GLY VAL PRO TYR ILE ILE
SEQRES 10 A 379 VAL PHE LEU ASN LYS CYS ASP MET VAL ASP ASP GLU GLU
SEQRES 11 A 379 LEU LEU GLU LEU VAL GLU MET GLU VAL ARG GLU LEU LEU
SEQRES 12 A 379 SER GLN TYR ASP PHE PRO GLY ASP ASP THR PRO ILE VAL
SEQRES 13 A 379 ARG GLY SER ALA LEU LYS ALA LEU GLU GLY ASP ALA GLU
SEQRES 14 A 379 TRP GLU ALA LYS ILE LEU GLU LEU ALA GLY PHE LEU ASP
SEQRES 15 A 379 SER TYR ILE PRO GLU PRO GLU ARG ALA ILE ASP LYS PRO
SEQRES 16 A 379 PHE LEU LEU PRO ILE GLU ASP VAL PHE SER ILE SER GLY
SEQRES 17 A 379 ARG GLY THR VAL VAL THR GLY ARG VAL GLU ARG GLY ILE
SEQRES 18 A 379 ILE LYS VAL GLY GLU GLU VAL GLU ILE VAL GLY ILE LYS
SEQRES 19 A 379 GLU THR GLN LYS SER THR CYS THR GLY VAL GLU MET PHE
SEQRES 20 A 379 ARG LYS LEU LEU ASP GLU GLY ARG ALA GLY GLU ASN VAL
SEQRES 21 A 379 GLY VAL LEU LEU ARG GLY ILE LYS ARG GLU GLU ILE GLU
SEQRES 22 A 379 ARG GLY GLN VAL LEU ALA LYS PRO GLY THR ILE LYS PRO
SEQRES 23 A 379 HIS THR LYS PHE GLU SER GLU VAL TYR ILE LEU SER LYS
SEQRES 24 A 379 ASP GLU GLY GLY ARG HIS THR PRO PHE PHE LYS GLY TYR
SEQRES 25 A 379 ARG PRO GLN PHE TYR PHE ARG THR THR ASP VAL THR GLY
SEQRES 26 A 379 THR ILE GLU LEU PRO GLU GLY VAL GLU MET VAL MET PRO
SEQRES 27 A 379 GLY ASP ASN ILE LYS MET VAL VAL THR LEU ILE HIS PRO
SEQRES 28 A 379 ILE ALA MET ASP ASP GLY LEU ARG PHE ALA ILE ARG GLU
SEQRES 29 A 379 GLY GLY ARG THR VAL GLY ALA GLY VAL VAL ALA LYS VAL
SEQRES 30 A 379 LEU SER
HET MG A 394 1
HET GDP A 395 28
HETNAM MG MAGNESIUM ION
HETNAM GDP GUANOSINE-5'-DIPHOSPHATE
FORMUL 2 MG MG 2+
FORMUL 3 GDP C10 H15 N5 O11 P2
SITE 1 AC1 1 GDP A 395
SITE 1 AC2 7 VAL A 20 ASP A 21 GLY A 23 LYS A 24
SITE 2 AC2 7 THR A 25 LEU A 175 MG A 394
CRYST1 98.609 100.807 162.465 90.00 90.00 90.00 C 2 2 21 8
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 0.010141 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009920 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006155 0.00000
(ATOM LINES ARE NOT SHOWN.)
END