HEADER MEMBRANE PROTEIN 06-JAN-09 3FPP
TITLE CRYSTAL STRUCTURE OF E.COLI MACA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MACROLIDE-SPECIFIC EFFLUX PROTEIN MACA;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 STRAIN: K12;
SOURCE 5 GENE: MACA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PPROEXHTA
KEYWDS HEXAMERIC ASSEMBLY, MEMBRANE FUSION PROTEIN, DRUG EFFLUX PUMP,
KEYWDS 2 PERIPLASMIC PROTEIN, ANTIBIOTIC RESISTANCE, CELL INNER MEMBRANE,
KEYWDS 3 CELL MEMBRANE, MEMBRANE, TRANSPORT, MEMBRANE PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR S.YUM,Y.XU,S.PIAO,N.-C.HA
REVDAT 3 03-APR-24 3FPP 1 REMARK
REVDAT 2 20-MAR-24 3FPP 1 REMARK
REVDAT 1 28-APR-09 3FPP 0
JRNL AUTH S.YUM,Y.XU,S.PIAO,S.-H.SIM,H.-M.KIM,W.-S.JO,K.-J.KIM,
JRNL AUTH 2 H.-S.KWEON,M.-H.JEONG,H.JEON,K.LEE,N.-C.HA
JRNL TITL CRYSTAL STRUCTURE OF THE PERIPLASMIC COMPONENT OF A
JRNL TITL 2 TRIPARTITE MACROLIDE-SPECIFIC EFFLUX PUMP
JRNL REF J.MOL.BIOL. V. 387 1286 2009
JRNL REFN ISSN 0022-2836
JRNL PMID 19254725
JRNL DOI 10.1016/J.JMB.2009.02.048
REMARK 2
REMARK 2 RESOLUTION. 2.99 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.2
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.99
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.69
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 90818.230
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 92.0
REMARK 3 NUMBER OF REFLECTIONS : 18206
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.283
REMARK 3 FREE R VALUE : 0.349
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.800
REMARK 3 FREE R VALUE TEST SET COUNT : 1950
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.008
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 : 4097
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 0.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.50
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.36000
REMARK 3 B22 (A**2) : 2.36000
REMARK 3 B33 (A**2) : -4.72000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.47
REMARK 3 ESD FROM SIGMAA (A) : 0.67
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.62
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.85
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.600
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.40
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.950
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
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 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.30
REMARK 3 BSOL : 14.10
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED
REMARK 4
REMARK 4 3FPP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 16-JAN-09.
REMARK 100 THE DEPOSITION ID IS D_1000050887.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-MAR-08
REMARK 200 TEMPERATURE (KELVIN) : 293
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PAL/PLS
REMARK 200 BEAMLINE : 6C1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : DOUBLE MIRROR
REMARK 200 OPTICS : DOUBLE MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19873
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.990
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.3
REMARK 200 DATA REDUNDANCY : 2.400
REMARK 200 R MERGE (I) : 0.12300
REMARK 200 R SYM (I) : 0.12300
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.99
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.11
REMARK 200 COMPLETENESS FOR SHELL (%) : 84.9
REMARK 200 DATA REDUNDANCY IN SHELL : 2.00
REMARK 200 R MERGE FOR SHELL (I) : 0.33800
REMARK 200 R SYM FOR SHELL (I) : 0.33800
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: THE UNREFINED STRUCTURE OF ACTINOBACILLUS
REMARK 200 ACTINOMYCETEMCOMITANS MACA
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 65.21
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.54
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1M POTASSIUM SODIUM TARTRATE
REMARK 280 TETRAHYDRATE, 0.1M MES, PH 6.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 287K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 3 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z
REMARK 290 6555 -X,-X+Y,-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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 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 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 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: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 23130 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 78300 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -95.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 350 BIOMT1 2 -0.500000 -0.866025 0.000000 -64.25850
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 111.29899
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 -128.51700
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
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 ALA A 31
REMARK 465 PRO A 32
REMARK 465 VAL A 33
REMARK 465 PRO A 34
REMARK 465 THR A 35
REMARK 465 TYR A 36
REMARK 465 GLN A 37
REMARK 465 THR A 38
REMARK 465 LEU A 39
REMARK 465 ILE A 40
REMARK 465 VAL A 41
REMARK 465 ARG A 42
REMARK 465 ILE A 309
REMARK 465 PRO A 310
REMARK 465 LEU A 311
REMARK 465 SER A 312
REMARK 465 ALA A 313
REMARK 465 LEU A 314
REMARK 465 GLY A 315
REMARK 465 ASP A 316
REMARK 465 PRO A 317
REMARK 465 VAL A 318
REMARK 465 GLY A 319
REMARK 465 ASP A 320
REMARK 465 ASN A 321
REMARK 465 ARG A 322
REMARK 465 TYR A 323
REMARK 465 LYS A 324
REMARK 465 VAL A 325
REMARK 465 LYS A 326
REMARK 465 LEU A 327
REMARK 465 LEU A 328
REMARK 465 ARG A 329
REMARK 465 ASN A 330
REMARK 465 GLY A 331
REMARK 465 GLU A 332
REMARK 465 THR A 333
REMARK 465 ARG A 334
REMARK 465 GLU A 335
REMARK 465 ARG A 336
REMARK 465 GLU A 337
REMARK 465 VAL A 338
REMARK 465 THR A 339
REMARK 465 ILE A 340
REMARK 465 GLY A 341
REMARK 465 ALA A 342
REMARK 465 ARG A 343
REMARK 465 ASN A 344
REMARK 465 ASP A 345
REMARK 465 THR A 346
REMARK 465 ASP A 347
REMARK 465 VAL A 348
REMARK 465 GLU A 349
REMARK 465 ILE A 350
REMARK 465 VAL A 351
REMARK 465 LYS A 352
REMARK 465 GLY A 353
REMARK 465 LEU A 354
REMARK 465 GLU A 355
REMARK 465 ALA A 356
REMARK 465 GLY A 357
REMARK 465 ASP A 358
REMARK 465 GLU A 359
REMARK 465 VAL A 360
REMARK 465 VAL A 361
REMARK 465 ILE A 362
REMARK 465 GLY A 363
REMARK 465 GLU A 364
REMARK 465 ALA A 365
REMARK 465 LYS A 366
REMARK 465 PRO A 367
REMARK 465 GLY A 368
REMARK 465 ALA A 369
REMARK 465 ALA A 370
REMARK 465 GLN A 371
REMARK 465 ALA B 31
REMARK 465 PRO B 32
REMARK 465 VAL B 33
REMARK 465 PRO B 34
REMARK 465 THR B 35
REMARK 465 TYR B 36
REMARK 465 GLN B 37
REMARK 465 THR B 38
REMARK 465 LEU B 39
REMARK 465 ILE B 40
REMARK 465 VAL B 41
REMARK 465 ILE B 309
REMARK 465 PRO B 310
REMARK 465 LEU B 311
REMARK 465 SER B 312
REMARK 465 ALA B 313
REMARK 465 LEU B 314
REMARK 465 GLY B 315
REMARK 465 ASP B 316
REMARK 465 PRO B 317
REMARK 465 VAL B 318
REMARK 465 GLY B 319
REMARK 465 ASP B 320
REMARK 465 ASN B 321
REMARK 465 ARG B 322
REMARK 465 TYR B 323
REMARK 465 LYS B 324
REMARK 465 VAL B 325
REMARK 465 LYS B 326
REMARK 465 LEU B 327
REMARK 465 LEU B 328
REMARK 465 ARG B 329
REMARK 465 ASN B 330
REMARK 465 GLY B 331
REMARK 465 GLU B 332
REMARK 465 THR B 333
REMARK 465 ARG B 334
REMARK 465 GLU B 335
REMARK 465 ARG B 336
REMARK 465 GLU B 337
REMARK 465 VAL B 338
REMARK 465 THR B 339
REMARK 465 ILE B 340
REMARK 465 GLY B 341
REMARK 465 ALA B 342
REMARK 465 ARG B 343
REMARK 465 ASN B 344
REMARK 465 ASP B 345
REMARK 465 THR B 346
REMARK 465 ASP B 347
REMARK 465 VAL B 348
REMARK 465 GLU B 349
REMARK 465 ILE B 350
REMARK 465 VAL B 351
REMARK 465 LYS B 352
REMARK 465 GLY B 353
REMARK 465 LEU B 354
REMARK 465 GLU B 355
REMARK 465 ALA B 356
REMARK 465 GLY B 357
REMARK 465 ASP B 358
REMARK 465 GLU B 359
REMARK 465 VAL B 360
REMARK 465 VAL B 361
REMARK 465 ILE B 362
REMARK 465 GLY B 363
REMARK 465 GLU B 364
REMARK 465 ALA B 365
REMARK 465 LYS B 366
REMARK 465 PRO B 367
REMARK 465 GLY B 368
REMARK 465 ALA B 369
REMARK 465 ALA B 370
REMARK 465 GLN B 371
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OD1 ASN B 283 O LEU B 287 2.17
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 ASP A 86 24.83 89.84
REMARK 500 LEU A 88 104.71 -59.62
REMARK 500 ASP A 93 96.16 -40.61
REMARK 500 GLU A 95 -36.21 -26.15
REMARK 500 TYR A 129 -71.85 -64.24
REMARK 500 ARG A 131 -34.54 -38.69
REMARK 500 LEU A 135 13.68 -67.12
REMARK 500 GLN A 139 113.15 60.45
REMARK 500 ALA A 140 -2.27 175.37
REMARK 500 VAL A 141 -31.64 -147.85
REMARK 500 SER A 142 -130.01 72.77
REMARK 500 GLN A 144 -79.39 -28.94
REMARK 500 MET A 153 -38.91 -36.97
REMARK 500 VAL A 194 96.18 -65.71
REMARK 500 ALA A 208 -52.32 -20.70
REMARK 500 GLN A 210 118.52 172.43
REMARK 500 PRO A 212 -175.04 -68.14
REMARK 500 ILE A 214 -77.39 -80.61
REMARK 500 ALA A 218 138.95 -170.96
REMARK 500 SER A 221 -86.65 -39.72
REMARK 500 MET A 223 -165.49 -103.64
REMARK 500 SER A 230 156.02 -44.92
REMARK 500 ASP A 233 45.21 -154.30
REMARK 500 LYS A 242 -117.90 -32.13
REMARK 500 ALA A 243 131.10 87.44
REMARK 500 THR A 246 -133.63 -96.18
REMARK 500 VAL A 247 46.71 -178.56
REMARK 500 LEU A 248 -100.27 46.68
REMARK 500 ASP A 250 82.06 92.10
REMARK 500 LEU A 252 72.13 172.23
REMARK 500 THR A 253 -27.18 -150.41
REMARK 500 ARG A 254 136.70 44.35
REMARK 500 LYS A 260 9.85 -153.64
REMARK 500 ASP A 271 45.22 93.25
REMARK 500 PHE A 274 -161.51 -112.76
REMARK 500 ASN A 285 -156.48 -110.07
REMARK 500 LEU A 287 140.24 -8.87
REMARK 500 LEU A 288 115.70 75.52
REMARK 500 ASP A 302 -7.82 -159.84
REMARK 500 ASN A 305 91.38 75.56
REMARK 500 VAL A 306 -13.36 -160.49
REMARK 500 LEU A 307 117.94 75.27
REMARK 500 GLN B 47 144.25 179.01
REMARK 500 VAL B 50 111.65 -178.68
REMARK 500 ALA B 52 127.54 -170.12
REMARK 500 ALA B 58 129.43 -39.63
REMARK 500 SER B 69 -151.90 -79.25
REMARK 500 ILE B 79 39.34 -53.09
REMARK 500 ASP B 93 96.96 -35.64
REMARK 500 GLU B 95 -26.29 -37.32
REMARK 500
REMARK 500 THIS ENTRY HAS 83 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THESE RESIDUES DERIVE FROM A VARIANT OF E.COLI K12 STRAIN.
DBREF 3FPP A 31 371 UNP P75830 MACA_ECOLI 31 371
DBREF 3FPP B 31 371 UNP P75830 MACA_ECOLI 31 371
SEQADV 3FPP GLN A 139 UNP P75830 LYS 139 SEE REMARK 999
SEQADV 3FPP ASN A 148 UNP P75830 THR 148 SEE REMARK 999
SEQADV 3FPP GLN A 251 UNP P75830 PRO 251 SEE REMARK 999
SEQADV 3FPP GLN B 139 UNP P75830 LYS 139 SEE REMARK 999
SEQADV 3FPP ASN B 148 UNP P75830 THR 148 SEE REMARK 999
SEQADV 3FPP GLN B 251 UNP P75830 PRO 251 SEE REMARK 999
SEQRES 1 A 341 ALA PRO VAL PRO THR TYR GLN THR LEU ILE VAL ARG PRO
SEQRES 2 A 341 GLY ASP LEU GLN GLN SER VAL LEU ALA THR GLY LYS LEU
SEQRES 3 A 341 ASP ALA LEU ARG LYS VAL ASP VAL GLY ALA GLN VAL SER
SEQRES 4 A 341 GLY GLN LEU LYS THR LEU SER VAL ALA ILE GLY ASP LYS
SEQRES 5 A 341 VAL LYS LYS ASP GLN LEU LEU GLY VAL ILE ASP PRO GLU
SEQRES 6 A 341 GLN ALA GLU ASN GLN ILE LYS GLU VAL GLU ALA THR LEU
SEQRES 7 A 341 MET GLU LEU ARG ALA GLN ARG GLN GLN ALA GLU ALA GLU
SEQRES 8 A 341 LEU LYS LEU ALA ARG VAL THR TYR SER ARG GLN GLN ARG
SEQRES 9 A 341 LEU ALA GLN THR GLN ALA VAL SER GLN GLN ASP LEU ASP
SEQRES 10 A 341 ASN ALA ALA THR GLU MET ALA VAL LYS GLN ALA GLN ILE
SEQRES 11 A 341 GLY THR ILE ASP ALA GLN ILE LYS ARG ASN GLN ALA SER
SEQRES 12 A 341 LEU ASP THR ALA LYS THR ASN LEU ASP TYR THR ARG ILE
SEQRES 13 A 341 VAL ALA PRO MET ALA GLY GLU VAL THR GLN ILE THR THR
SEQRES 14 A 341 LEU GLN GLY GLN THR VAL ILE ALA ALA GLN GLN ALA PRO
SEQRES 15 A 341 ASN ILE LEU THR LEU ALA ASP MET SER ALA MET LEU VAL
SEQRES 16 A 341 LYS ALA GLN VAL SER GLU ALA ASP VAL ILE HIS LEU LYS
SEQRES 17 A 341 PRO GLY GLN LYS ALA TRP PHE THR VAL LEU GLY ASP GLN
SEQRES 18 A 341 LEU THR ARG TYR GLU GLY GLN ILE LYS ASP VAL LEU PRO
SEQRES 19 A 341 THR PRO GLU LYS VAL ASN ASP ALA ILE PHE TYR TYR ALA
SEQRES 20 A 341 ARG PHE GLU VAL PRO ASN PRO ASN GLY LEU LEU ARG LEU
SEQRES 21 A 341 ASP MET THR ALA GLN VAL HIS ILE GLN LEU THR ASP VAL
SEQRES 22 A 341 LYS ASN VAL LEU THR ILE PRO LEU SER ALA LEU GLY ASP
SEQRES 23 A 341 PRO VAL GLY ASP ASN ARG TYR LYS VAL LYS LEU LEU ARG
SEQRES 24 A 341 ASN GLY GLU THR ARG GLU ARG GLU VAL THR ILE GLY ALA
SEQRES 25 A 341 ARG ASN ASP THR ASP VAL GLU ILE VAL LYS GLY LEU GLU
SEQRES 26 A 341 ALA GLY ASP GLU VAL VAL ILE GLY GLU ALA LYS PRO GLY
SEQRES 27 A 341 ALA ALA GLN
SEQRES 1 B 341 ALA PRO VAL PRO THR TYR GLN THR LEU ILE VAL ARG PRO
SEQRES 2 B 341 GLY ASP LEU GLN GLN SER VAL LEU ALA THR GLY LYS LEU
SEQRES 3 B 341 ASP ALA LEU ARG LYS VAL ASP VAL GLY ALA GLN VAL SER
SEQRES 4 B 341 GLY GLN LEU LYS THR LEU SER VAL ALA ILE GLY ASP LYS
SEQRES 5 B 341 VAL LYS LYS ASP GLN LEU LEU GLY VAL ILE ASP PRO GLU
SEQRES 6 B 341 GLN ALA GLU ASN GLN ILE LYS GLU VAL GLU ALA THR LEU
SEQRES 7 B 341 MET GLU LEU ARG ALA GLN ARG GLN GLN ALA GLU ALA GLU
SEQRES 8 B 341 LEU LYS LEU ALA ARG VAL THR TYR SER ARG GLN GLN ARG
SEQRES 9 B 341 LEU ALA GLN THR GLN ALA VAL SER GLN GLN ASP LEU ASP
SEQRES 10 B 341 ASN ALA ALA THR GLU MET ALA VAL LYS GLN ALA GLN ILE
SEQRES 11 B 341 GLY THR ILE ASP ALA GLN ILE LYS ARG ASN GLN ALA SER
SEQRES 12 B 341 LEU ASP THR ALA LYS THR ASN LEU ASP TYR THR ARG ILE
SEQRES 13 B 341 VAL ALA PRO MET ALA GLY GLU VAL THR GLN ILE THR THR
SEQRES 14 B 341 LEU GLN GLY GLN THR VAL ILE ALA ALA GLN GLN ALA PRO
SEQRES 15 B 341 ASN ILE LEU THR LEU ALA ASP MET SER ALA MET LEU VAL
SEQRES 16 B 341 LYS ALA GLN VAL SER GLU ALA ASP VAL ILE HIS LEU LYS
SEQRES 17 B 341 PRO GLY GLN LYS ALA TRP PHE THR VAL LEU GLY ASP GLN
SEQRES 18 B 341 LEU THR ARG TYR GLU GLY GLN ILE LYS ASP VAL LEU PRO
SEQRES 19 B 341 THR PRO GLU LYS VAL ASN ASP ALA ILE PHE TYR TYR ALA
SEQRES 20 B 341 ARG PHE GLU VAL PRO ASN PRO ASN GLY LEU LEU ARG LEU
SEQRES 21 B 341 ASP MET THR ALA GLN VAL HIS ILE GLN LEU THR ASP VAL
SEQRES 22 B 341 LYS ASN VAL LEU THR ILE PRO LEU SER ALA LEU GLY ASP
SEQRES 23 B 341 PRO VAL GLY ASP ASN ARG TYR LYS VAL LYS LEU LEU ARG
SEQRES 24 B 341 ASN GLY GLU THR ARG GLU ARG GLU VAL THR ILE GLY ALA
SEQRES 25 B 341 ARG ASN ASP THR ASP VAL GLU ILE VAL LYS GLY LEU GLU
SEQRES 26 B 341 ALA GLY ASP GLU VAL VAL ILE GLY GLU ALA LYS PRO GLY
SEQRES 27 B 341 ALA ALA GLN
HELIX 1 1 PRO A 94 ARG A 126 1 33
HELIX 2 2 ARG A 126 THR A 138 1 13
HELIX 3 3 GLN A 143 LYS A 156 1 14
HELIX 4 4 LYS A 156 ASN A 170 1 15
HELIX 5 5 ASN A 170 ASP A 175 1 6
HELIX 6 6 SER A 230 VAL A 234 5 5
HELIX 7 7 PRO B 94 THR B 138 1 45
HELIX 8 8 GLN B 143 THR B 151 1 9
HELIX 9 9 THR B 151 TYR B 183 1 33
SHEET 1 A 6 TRP A 244 PHE A 245 0
SHEET 2 A 6 THR A 293 GLN A 299 -1 O HIS A 297 N TRP A 244
SHEET 3 A 6 SER A 49 ALA A 58 -1 N ALA A 52 O VAL A 296
SHEET 4 A 6 ALA A 222 GLN A 228 -1 O LEU A 224 N ASP A 57
SHEET 5 A 6 TYR A 276 PRO A 282 -1 O ALA A 277 N ALA A 227
SHEET 6 A 6 ILE A 259 VAL A 262 -1 N LYS A 260 O ARG A 278
SHEET 1 B 4 LYS A 61 ASP A 63 0
SHEET 2 B 4 LEU A 215 ALA A 218 -1 O LEU A 217 N VAL A 62
SHEET 3 B 4 GLY A 192 ILE A 197 -1 N GLN A 196 O THR A 216
SHEET 4 B 4 LYS A 82 VAL A 83 -1 N VAL A 83 O GLY A 192
SHEET 1 C 4 ARG A 185 VAL A 187 0
SHEET 2 C 4 LEU A 88 ILE A 92 -1 N GLY A 90 O ILE A 186
SHEET 3 C 4 GLY A 70 LEU A 75 -1 N THR A 74 O VAL A 91
SHEET 4 C 4 THR A 204 VAL A 205 -1 O VAL A 205 N GLY A 70
SHEET 1 D 2 PRO B 43 LEU B 46 0
SHEET 2 D 2 VAL B 303 LEU B 307 -1 O VAL B 306 N GLY B 44
SHEET 1 E 7 TYR B 255 GLY B 257 0
SHEET 2 E 7 ALA B 243 VAL B 247 -1 N ALA B 243 O GLY B 257
SHEET 3 E 7 THR B 293 ILE B 298 -1 O GLN B 295 N THR B 246
SHEET 4 E 7 VAL B 50 VAL B 64 -1 N ALA B 52 O VAL B 296
SHEET 5 E 7 LEU B 215 SER B 230 -1 O LEU B 224 N ASP B 57
SHEET 6 E 7 ILE B 273 ALA B 277 -1 O ALA B 277 N ALA B 227
SHEET 7 E 7 GLU B 267 LYS B 268 -1 N GLU B 267 O PHE B 274
SHEET 1 F 6 TYR B 255 GLY B 257 0
SHEET 2 F 6 ALA B 243 VAL B 247 -1 N ALA B 243 O GLY B 257
SHEET 3 F 6 THR B 293 ILE B 298 -1 O GLN B 295 N THR B 246
SHEET 4 F 6 VAL B 50 VAL B 64 -1 N ALA B 52 O VAL B 296
SHEET 5 F 6 LEU B 215 SER B 230 -1 O LEU B 224 N ASP B 57
SHEET 6 F 6 VAL B 281 PRO B 282 -1 O VAL B 281 N MET B 223
SHEET 1 G 2 GLY B 70 GLN B 71 0
SHEET 2 G 2 THR B 204 VAL B 205 -1 O VAL B 205 N GLY B 70
SHEET 1 H 3 THR B 74 LEU B 75 0
SHEET 2 H 3 LEU B 88 VAL B 91 -1 O VAL B 91 N THR B 74
SHEET 3 H 3 ARG B 185 VAL B 187 -1 O ILE B 186 N GLY B 90
CRYST1 128.517 128.517 110.311 90.00 90.00 120.00 P 3 2 1 12
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 0.007781 0.004492 0.000000 0.00000
SCALE2 0.000000 0.008985 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009065 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
