HEADER TRANSPORT PROTEIN 10-SEP-07 2R8A
TITLE CRYSTAL STRUCTURE OF THE LONG-CHAIN FATTY ACID TRANSPORTER FADL MUTANT
TITLE 2 DELTA N8
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LONG-CHAIN FATTY ACID TRANSPORT PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: OUTER MEMBRANE FADL PROTEIN, OUTER MEMBRANE FLP PROTEIN;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: FADL, TTR;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: C43(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PBAD22
KEYWDS BETA BARREL, OUTER MEMBRANE PROTEIN, LIPID TRANSPORT, PHAGE
KEYWDS 2 RECOGNITION, TRANSMEMBRANE, TRANSPORT, TRANSPORT PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR E.M.HEARN,D.R.PATEL,B.W.LEPORE,M.INDIC,B.VAN DEN BERG
REVDAT 6 29-NOV-23 2R8A 1 REMARK
REVDAT 5 30-AUG-23 2R8A 1 REMARK SEQADV
REVDAT 4 06-JUL-11 2R8A 1 JRNL
REVDAT 3 01-JUN-11 2R8A 1 JRNL
REVDAT 2 24-FEB-09 2R8A 1 VERSN
REVDAT 1 23-SEP-08 2R8A 0
JRNL AUTH B.W.LEPORE,M.INDIC,H.PHAM,E.M.HEARN,D.R.PATEL,B.VAN DEN BERG
JRNL TITL FROM THE COVER: LIGAND-GATED DIFFUSION ACROSS THE BACTERIAL
JRNL TITL 2 OUTER MEMBRANE.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 108 10121 2011
JRNL REFN ISSN 0027-8424
JRNL PMID 21593406
JRNL DOI 10.1073/PNAS.1018532108
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH B.VAN DEN BERG,P.N.BLACK,W.M.CLEMONS JR.,T.A.RAPOPORT
REMARK 1 TITL CRYSTAL STRUCTURE OF THE LONG-CHAIN FATTY ACID TRANSPORTER
REMARK 1 TITL 2 FADL
REMARK 1 REF SCIENCE V. 304 1506 2004
REMARK 1 REFN ISSN 0036-8075
REMARK 2
REMARK 2 RESOLUTION. 3.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
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) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 80.4
REMARK 3 NUMBER OF REFLECTIONS : 17357
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) : 0.248
REMARK 3 FREE R VALUE : 0.294
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 1360
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) : 3.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.13
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 68.50
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.3520
REMARK 3 BIN FREE R VALUE : 0.3840
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 128
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.034
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5558
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 84
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) : 46.69
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 12.84100
REMARK 3 B22 (A**2) : 12.84100
REMARK 3 B33 (A**2) : -25.68200
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) : 0.41
REMARK 3 ESD FROM SIGMAA (A) : 0.45
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) : 0.50
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.53
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.500
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 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 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 2R8A COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-OCT-07.
REMARK 100 THE DEPOSITION ID IS D_1000044549.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-OCT-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X6A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.1
REMARK 200 MONOCHROMATOR : SI(111) CHANNEL CUT
REMARK 200 MONOCHROMATOR
REMARK 200 OPTICS : NULL
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 : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17938
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000
REMARK 200 RESOLUTION RANGE LOW (A) : 37.930
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 80.6
REMARK 200 DATA REDUNDANCY : 4.100
REMARK 200 R MERGE (I) : 0.05200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.11
REMARK 200 COMPLETENESS FOR SHELL (%) : 68.3
REMARK 200 DATA REDUNDANCY IN SHELL : 3.70
REMARK 200 R MERGE FOR SHELL (I) : 0.51100
REMARK 200 R SYM FOR SHELL (I) : 0.51100
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 1T16
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.94
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.15
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 10000, 8% ETHYLENE GLYCOL,
REMARK 280 0.1M HEPES, PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41
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 -Y,X,Z+1/4
REMARK 290 4555 Y,-X,Z+3/4
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 135.32550
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 67.66275
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 202.98825
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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 LYS A 236
REMARK 465 GLY A 237
REMARK 465 ASN A 238
REMARK 465 TYR A 239
REMARK 465 SER A 240
REMARK 465 SER A 241
REMARK 465 ASP A 242
REMARK 465 LEU A 243
REMARK 465 ASN A 244
REMARK 465 ARG A 245
REMARK 465 ALA A 246
REMARK 465 PHE A 247
REMARK 465 ASN A 248
REMARK 465 ASN A 249
REMARK 465 TYR A 250
REMARK 465 GLY A 251
REMARK 465 LEU A 252
REMARK 465 PRO A 253
REMARK 465 ILE A 254
REMARK 465 PRO A 255
REMARK 465 THR A 256
REMARK 465 ALA A 257
REMARK 465 THR A 258
REMARK 465 GLY A 259
REMARK 465 GLY A 260
REMARK 465 ALA A 261
REMARK 465 THR A 262
REMARK 465 GLN A 263
REMARK 465 SER A 264
REMARK 465 GLY A 265
REMARK 465 TYR A 266
REMARK 465 GLN A 300
REMARK 465 PHE A 301
REMARK 465 GLN A 302
REMARK 465 GLN A 303
REMARK 465 LEU A 304
REMARK 465 LYS A 305
REMARK 465 ALA A 306
REMARK 465 THR A 307
REMARK 465 SER A 308
REMARK 465 THR A 309
REMARK 465 SER A 310
REMARK 465 GLY A 311
REMARK 465 ASP A 312
REMARK 465 THR A 313
REMARK 465 LEU A 314
REMARK 465 PHE A 315
REMARK 465 GLN A 316
REMARK 465 LYS A 317
REMARK 465 HIS A 318
REMARK 465 GLU A 319
REMARK 465 GLY A 320
REMARK 465 PHE A 321
REMARK 465 HIS A 422
REMARK 465 HIS A 423
REMARK 465 HIS A 424
REMARK 465 HIS A 425
REMARK 465 HIS A 426
REMARK 465 HIS A 427
REMARK 465 LYS B 236
REMARK 465 GLY B 237
REMARK 465 ASN B 238
REMARK 465 TYR B 239
REMARK 465 SER B 240
REMARK 465 SER B 241
REMARK 465 ASP B 242
REMARK 465 LEU B 243
REMARK 465 ASN B 244
REMARK 465 ARG B 245
REMARK 465 ALA B 246
REMARK 465 PHE B 247
REMARK 465 ASN B 248
REMARK 465 ASN B 249
REMARK 465 TYR B 250
REMARK 465 GLY B 251
REMARK 465 LEU B 252
REMARK 465 PRO B 253
REMARK 465 ILE B 254
REMARK 465 PRO B 255
REMARK 465 THR B 256
REMARK 465 ALA B 257
REMARK 465 THR B 258
REMARK 465 GLY B 259
REMARK 465 GLY B 260
REMARK 465 ALA B 261
REMARK 465 THR B 262
REMARK 465 GLN B 263
REMARK 465 SER B 264
REMARK 465 GLY B 265
REMARK 465 TYR B 266
REMARK 465 GLN B 300
REMARK 465 PHE B 301
REMARK 465 GLN B 302
REMARK 465 GLN B 303
REMARK 465 LEU B 304
REMARK 465 LYS B 305
REMARK 465 ALA B 306
REMARK 465 THR B 307
REMARK 465 SER B 308
REMARK 465 THR B 309
REMARK 465 SER B 310
REMARK 465 GLY B 311
REMARK 465 ASP B 312
REMARK 465 THR B 313
REMARK 465 LEU B 314
REMARK 465 PHE B 315
REMARK 465 GLN B 316
REMARK 465 LYS B 317
REMARK 465 HIS B 318
REMARK 465 GLU B 319
REMARK 465 GLY B 320
REMARK 465 PHE B 321
REMARK 465 HIS B 422
REMARK 465 HIS B 423
REMARK 465 HIS B 424
REMARK 465 HIS B 425
REMARK 465 HIS B 426
REMARK 465 HIS B 427
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 O ASN B 378 N ASP B 380 2.09
REMARK 500 O ASN A 378 N ASP A 380 2.10
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 TYR A 17 40.28 70.60
REMARK 500 ALA A 22 -10.73 -153.36
REMARK 500 ALA A 24 26.94 -144.79
REMARK 500 LEU A 36 -1.40 -57.76
REMARK 500 THR A 38 26.47 -66.81
REMARK 500 ASP A 55 66.56 -158.87
REMARK 500 ASN A 72 88.47 35.16
REMARK 500 ASP A 90 -16.69 -36.03
REMARK 500 LEU A 104 123.08 165.66
REMARK 500 LEU A 123 108.27 -162.65
REMARK 500 ASN A 137 -164.12 161.89
REMARK 500 ALA A 139 -64.66 -102.10
REMARK 500 ASP A 161 37.88 -79.09
REMARK 500 ALA A 175 -13.39 -49.46
REMARK 500 GLN A 177 97.07 -52.90
REMARK 500 THR A 178 -152.90 4.94
REMARK 500 GLN A 179 81.64 72.68
REMARK 500 GLN A 180 12.96 41.06
REMARK 500 ASN A 194 9.29 -55.29
REMARK 500 ALA A 198 117.18 -179.21
REMARK 500 ASP A 218 163.69 159.31
REMARK 500 LYS A 219 -0.07 -51.00
REMARK 500 VAL A 283 -23.61 -38.32
REMARK 500 TRP A 298 35.53 -80.28
REMARK 500 ASN A 338 -62.22 -92.32
REMARK 500 ALA A 354 0.72 -48.25
REMARK 500 SER A 358 137.33 -172.57
REMARK 500 GLN A 364 143.33 174.36
REMARK 500 ASP A 365 109.07 -32.36
REMARK 500 ASN A 378 129.88 164.38
REMARK 500 LYS A 379 -27.84 7.12
REMARK 500 ASN A 398 52.11 -117.38
REMARK 500 LYS A 409 -169.15 -113.07
REMARK 500 TYR B 17 40.66 70.73
REMARK 500 ALA B 22 -10.23 -153.82
REMARK 500 ALA B 24 26.83 -144.57
REMARK 500 LEU B 36 -1.17 -57.85
REMARK 500 THR B 38 26.49 -67.04
REMARK 500 ASP B 55 66.62 -158.80
REMARK 500 ASN B 72 88.71 34.79
REMARK 500 ASP B 90 -16.73 -36.25
REMARK 500 LEU B 104 123.38 165.76
REMARK 500 LEU B 123 108.26 -162.73
REMARK 500 ASN B 137 -163.88 162.12
REMARK 500 ALA B 139 -65.12 -102.09
REMARK 500 ASP B 161 37.84 -79.15
REMARK 500 ALA B 175 -13.29 -49.58
REMARK 500 GLN B 177 97.23 -52.95
REMARK 500 THR B 178 -153.06 4.77
REMARK 500 GLN B 179 81.50 72.82
REMARK 500
REMARK 500 THIS ENTRY HAS 66 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE C8E A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE C8E B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE C8E B 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE C8E A 504
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1T16 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE BACTERIAL FATTY ACID TRANSPORTER FADL
REMARK 900 (WILD-TYPE, MONOCLINIC SPACE GROUP P21)
REMARK 900 RELATED ID: 1T1L RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE BACTERIAL FATTY ACID TRANSPORTER FADL
REMARK 900 (WILD-TYPE, HEXAGONAL SPACE GROUP P3121)
REMARK 900 RELATED ID: 2R4L RELATED DB: PDB
REMARK 900 FADL MUTANT P34A
REMARK 900 RELATED ID: 2R4M RELATED DB: PDB
REMARK 900 FADL MUTANT A77E/S100R
REMARK 900 RELATED ID: 2R4N RELATED DB: PDB
REMARK 900 FADL MUTANT N33A
REMARK 900 RELATED ID: 2R4O RELATED DB: PDB
REMARK 900 FADL MUTANT DELTA NPA
REMARK 900 RELATED ID: 2R4P RELATED DB: PDB
REMARK 900 FADL MUTANT G212E
REMARK 900 RELATED ID: 2R88 RELATED DB: PDB
REMARK 900 FADL MUTANT DELTA S3 KINK
REMARK 900 RELATED ID: 2R89 RELATED DB: PDB
REMARK 900 FADL MUTANT DELTA N3
REMARK 900 RELATED ID: 3DWO RELATED DB: PDB
REMARK 900 FADL HOMOLOGUE IN PSEUDOMONAS AERUGINOSA
REMARK 900 RELATED ID: 3DWN RELATED DB: PDB
REMARK 900 FADL MUTANT A77E/S100R
DBREF 2R8A A 9 421 UNP P10384 FADL_ECOLI 26 446
DBREF 2R8A B 9 421 UNP P10384 FADL_ECOLI 26 446
SEQADV 2R8A A UNP P10384 PHE 28 DELETION
SEQADV 2R8A A UNP P10384 GLN 29 DELETION
SEQADV 2R8A A UNP P10384 LEU 30 DELETION
SEQADV 2R8A A UNP P10384 ASN 31 DELETION
SEQADV 2R8A A UNP P10384 GLU 32 DELETION
SEQADV 2R8A A UNP P10384 PHE 33 DELETION
SEQADV 2R8A A UNP P10384 SER 34 DELETION
SEQADV 2R8A A UNP P10384 SER 35 DELETION
SEQADV 2R8A THR A 197 UNP P10384 ILE 222 CONFLICT
SEQADV 2R8A HIS A 422 UNP P10384 EXPRESSION TAG
SEQADV 2R8A HIS A 423 UNP P10384 EXPRESSION TAG
SEQADV 2R8A HIS A 424 UNP P10384 EXPRESSION TAG
SEQADV 2R8A HIS A 425 UNP P10384 EXPRESSION TAG
SEQADV 2R8A HIS A 426 UNP P10384 EXPRESSION TAG
SEQADV 2R8A HIS A 427 UNP P10384 EXPRESSION TAG
SEQADV 2R8A B UNP P10384 PHE 28 DELETION
SEQADV 2R8A B UNP P10384 GLN 29 DELETION
SEQADV 2R8A B UNP P10384 LEU 30 DELETION
SEQADV 2R8A B UNP P10384 ASN 31 DELETION
SEQADV 2R8A B UNP P10384 GLU 32 DELETION
SEQADV 2R8A B UNP P10384 PHE 33 DELETION
SEQADV 2R8A B UNP P10384 SER 34 DELETION
SEQADV 2R8A B UNP P10384 SER 35 DELETION
SEQADV 2R8A THR B 197 UNP P10384 ILE 222 CONFLICT
SEQADV 2R8A HIS B 422 UNP P10384 EXPRESSION TAG
SEQADV 2R8A HIS B 423 UNP P10384 EXPRESSION TAG
SEQADV 2R8A HIS B 424 UNP P10384 EXPRESSION TAG
SEQADV 2R8A HIS B 425 UNP P10384 EXPRESSION TAG
SEQADV 2R8A HIS B 426 UNP P10384 EXPRESSION TAG
SEQADV 2R8A HIS B 427 UNP P10384 EXPRESSION TAG
SEQRES 1 A 419 ALA GLY SER GLY LEU GLY ARG ALA TYR SER GLY GLU GLY
SEQRES 2 A 419 ALA ILE ALA ASP ASP ALA GLY ASN VAL SER ARG ASN PRO
SEQRES 3 A 419 ALA LEU ILE THR MET PHE ASP ARG PRO THR PHE SER ALA
SEQRES 4 A 419 GLY ALA VAL TYR ILE ASP PRO ASP VAL ASN ILE SER GLY
SEQRES 5 A 419 THR SER PRO SER GLY ARG SER LEU LYS ALA ASP ASN ILE
SEQRES 6 A 419 ALA PRO THR ALA TRP VAL PRO ASN MET HIS PHE VAL ALA
SEQRES 7 A 419 PRO ILE ASN ASP GLN PHE GLY TRP GLY ALA SER ILE THR
SEQRES 8 A 419 SER ASN TYR GLY LEU ALA THR GLU PHE ASN ASP THR TYR
SEQRES 9 A 419 ALA GLY GLY SER VAL GLY GLY THR THR ASP LEU GLU THR
SEQRES 10 A 419 MET ASN LEU ASN LEU SER GLY ALA TYR ARG LEU ASN ASN
SEQRES 11 A 419 ALA TRP SER PHE GLY LEU GLY PHE ASN ALA VAL TYR ALA
SEQRES 12 A 419 ARG ALA LYS ILE GLU ARG PHE ALA GLY ASP LEU GLY GLN
SEQRES 13 A 419 LEU VAL ALA GLY GLN ILE MET GLN SER PRO ALA GLY GLN
SEQRES 14 A 419 THR GLN GLN GLY GLN ALA LEU ALA ALA THR ALA ASN GLY
SEQRES 15 A 419 ILE ASP SER ASN THR LYS THR ALA HIS LEU ASN GLY ASN
SEQRES 16 A 419 GLN TRP GLY PHE GLY TRP ASN ALA GLY ILE LEU TYR GLU
SEQRES 17 A 419 LEU ASP LYS ASN ASN ARG TYR ALA LEU THR TYR ARG SER
SEQRES 18 A 419 GLU VAL LYS ILE ASP PHE LYS GLY ASN TYR SER SER ASP
SEQRES 19 A 419 LEU ASN ARG ALA PHE ASN ASN TYR GLY LEU PRO ILE PRO
SEQRES 20 A 419 THR ALA THR GLY GLY ALA THR GLN SER GLY TYR LEU THR
SEQRES 21 A 419 LEU ASN LEU PRO GLU MET TRP GLU VAL SER GLY TYR ASN
SEQRES 22 A 419 ARG VAL ASP PRO GLN TRP ALA ILE HIS TYR SER LEU ALA
SEQRES 23 A 419 TYR THR SER TRP SER GLN PHE GLN GLN LEU LYS ALA THR
SEQRES 24 A 419 SER THR SER GLY ASP THR LEU PHE GLN LYS HIS GLU GLY
SEQRES 25 A 419 PHE LYS ASP ALA TYR ARG ILE ALA LEU GLY THR THR TYR
SEQRES 26 A 419 TYR TYR ASP ASP ASN TRP THR PHE ARG THR GLY ILE ALA
SEQRES 27 A 419 PHE ASP ASP SER PRO VAL PRO ALA GLN ASN ARG SER ILE
SEQRES 28 A 419 SER ILE PRO ASP GLN ASP ARG PHE TRP LEU SER ALA GLY
SEQRES 29 A 419 THR THR TYR ALA PHE ASN LYS ASP ALA SER VAL ASP VAL
SEQRES 30 A 419 GLY VAL SER TYR MET HIS GLY GLN SER VAL LYS ILE ASN
SEQRES 31 A 419 GLU GLY PRO TYR GLN PHE GLU SER GLU GLY LYS ALA TRP
SEQRES 32 A 419 LEU PHE GLY THR ASN PHE ASN TYR ALA PHE HIS HIS HIS
SEQRES 33 A 419 HIS HIS HIS
SEQRES 1 B 419 ALA GLY SER GLY LEU GLY ARG ALA TYR SER GLY GLU GLY
SEQRES 2 B 419 ALA ILE ALA ASP ASP ALA GLY ASN VAL SER ARG ASN PRO
SEQRES 3 B 419 ALA LEU ILE THR MET PHE ASP ARG PRO THR PHE SER ALA
SEQRES 4 B 419 GLY ALA VAL TYR ILE ASP PRO ASP VAL ASN ILE SER GLY
SEQRES 5 B 419 THR SER PRO SER GLY ARG SER LEU LYS ALA ASP ASN ILE
SEQRES 6 B 419 ALA PRO THR ALA TRP VAL PRO ASN MET HIS PHE VAL ALA
SEQRES 7 B 419 PRO ILE ASN ASP GLN PHE GLY TRP GLY ALA SER ILE THR
SEQRES 8 B 419 SER ASN TYR GLY LEU ALA THR GLU PHE ASN ASP THR TYR
SEQRES 9 B 419 ALA GLY GLY SER VAL GLY GLY THR THR ASP LEU GLU THR
SEQRES 10 B 419 MET ASN LEU ASN LEU SER GLY ALA TYR ARG LEU ASN ASN
SEQRES 11 B 419 ALA TRP SER PHE GLY LEU GLY PHE ASN ALA VAL TYR ALA
SEQRES 12 B 419 ARG ALA LYS ILE GLU ARG PHE ALA GLY ASP LEU GLY GLN
SEQRES 13 B 419 LEU VAL ALA GLY GLN ILE MET GLN SER PRO ALA GLY GLN
SEQRES 14 B 419 THR GLN GLN GLY GLN ALA LEU ALA ALA THR ALA ASN GLY
SEQRES 15 B 419 ILE ASP SER ASN THR LYS THR ALA HIS LEU ASN GLY ASN
SEQRES 16 B 419 GLN TRP GLY PHE GLY TRP ASN ALA GLY ILE LEU TYR GLU
SEQRES 17 B 419 LEU ASP LYS ASN ASN ARG TYR ALA LEU THR TYR ARG SER
SEQRES 18 B 419 GLU VAL LYS ILE ASP PHE LYS GLY ASN TYR SER SER ASP
SEQRES 19 B 419 LEU ASN ARG ALA PHE ASN ASN TYR GLY LEU PRO ILE PRO
SEQRES 20 B 419 THR ALA THR GLY GLY ALA THR GLN SER GLY TYR LEU THR
SEQRES 21 B 419 LEU ASN LEU PRO GLU MET TRP GLU VAL SER GLY TYR ASN
SEQRES 22 B 419 ARG VAL ASP PRO GLN TRP ALA ILE HIS TYR SER LEU ALA
SEQRES 23 B 419 TYR THR SER TRP SER GLN PHE GLN GLN LEU LYS ALA THR
SEQRES 24 B 419 SER THR SER GLY ASP THR LEU PHE GLN LYS HIS GLU GLY
SEQRES 25 B 419 PHE LYS ASP ALA TYR ARG ILE ALA LEU GLY THR THR TYR
SEQRES 26 B 419 TYR TYR ASP ASP ASN TRP THR PHE ARG THR GLY ILE ALA
SEQRES 27 B 419 PHE ASP ASP SER PRO VAL PRO ALA GLN ASN ARG SER ILE
SEQRES 28 B 419 SER ILE PRO ASP GLN ASP ARG PHE TRP LEU SER ALA GLY
SEQRES 29 B 419 THR THR TYR ALA PHE ASN LYS ASP ALA SER VAL ASP VAL
SEQRES 30 B 419 GLY VAL SER TYR MET HIS GLY GLN SER VAL LYS ILE ASN
SEQRES 31 B 419 GLU GLY PRO TYR GLN PHE GLU SER GLU GLY LYS ALA TRP
SEQRES 32 B 419 LEU PHE GLY THR ASN PHE ASN TYR ALA PHE HIS HIS HIS
SEQRES 33 B 419 HIS HIS HIS
HET C8E A 501 21
HET C8E A 504 21
HET C8E B 502 21
HET C8E B 503 21
HETNAM C8E (HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE
FORMUL 3 C8E 4(C16 H34 O5)
HELIX 1 1 GLY A 10 ARG A 15 1 6
HELIX 2 2 ASP A 26 ARG A 32 5 7
HELIX 3 3 ASN A 33 PHE A 40 5 8
HELIX 4 4 GLY A 114 GLY A 118 5 5
HELIX 5 5 ASP A 161 MET A 171 1 11
HELIX 6 6 GLN A 172 GLN A 177 5 6
HELIX 7 7 GLY A 181 GLY A 190 1 10
HELIX 8 8 GLY B 10 ARG B 15 1 6
HELIX 9 9 ASP B 26 ARG B 32 5 7
HELIX 10 10 ASN B 33 PHE B 40 5 8
HELIX 11 11 GLY B 114 GLY B 118 5 5
HELIX 12 12 ASP B 161 MET B 171 1 11
HELIX 13 13 GLN B 172 GLN B 177 5 6
HELIX 14 14 GLY B 181 GLY B 190 1 10
SHEET 1 A 7 GLY A 103 GLU A 107 0
SHEET 2 A 7 THR A 120 ARG A 135 -1 O THR A 121 N THR A 106
SHEET 3 A 7 PHE A 92 THR A 99 -1 N SER A 97 O ASN A 129
SHEET 4 A 7 ALA A 77 ASN A 89 -1 N ILE A 88 O PHE A 92
SHEET 5 A 7 THR A 44 SER A 59 -1 N ILE A 52 O ALA A 77
SHEET 6 A 7 PHE A 404 ALA A 420 -1 O PHE A 413 N TYR A 51
SHEET 7 A 7 VAL A 395 ILE A 397 -1 N ILE A 397 O PHE A 404
SHEET 1 B13 GLY A 103 GLU A 107 0
SHEET 2 B13 THR A 120 ARG A 135 -1 O THR A 121 N THR A 106
SHEET 3 B13 TRP A 140 PHE A 158 -1 O ALA A 148 N LEU A 128
SHEET 4 B13 LYS A 196 ASP A 218 -1 O ASN A 210 N GLY A 145
SHEET 5 B13 ASN A 221 ARG A 228 -1 O ASN A 221 N LEU A 217
SHEET 6 B13 GLU A 273 ASN A 281 -1 O MET A 274 N ARG A 228
SHEET 7 B13 TRP A 287 SER A 297 -1 O ILE A 289 N ASN A 281
SHEET 8 B13 ALA A 324 TYR A 333 -1 O ARG A 326 N ALA A 294
SHEET 9 B13 PHE A 341 ASP A 348 -1 O PHE A 341 N TYR A 333
SHEET 10 B13 ARG A 366 ASN A 378 -1 O GLY A 372 N ARG A 342
SHEET 11 B13 ALA A 381 GLY A 392 -1 O VAL A 385 N THR A 373
SHEET 12 B13 PHE A 404 ALA A 420 -1 O ASN A 416 N ASP A 384
SHEET 13 B13 VAL A 395 ILE A 397 -1 N ILE A 397 O PHE A 404
SHEET 1 C 2 VAL A 231 ILE A 233 0
SHEET 2 C 2 LEU A 269 LEU A 271 -1 O LEU A 269 N ILE A 233
SHEET 1 D 7 GLY B 103 GLU B 107 0
SHEET 2 D 7 THR B 120 ARG B 135 -1 O THR B 121 N THR B 106
SHEET 3 D 7 PHE B 92 THR B 99 -1 N SER B 97 O ASN B 129
SHEET 4 D 7 ALA B 77 ASN B 89 -1 N ILE B 88 O PHE B 92
SHEET 5 D 7 THR B 44 SER B 59 -1 N ILE B 52 O ALA B 77
SHEET 6 D 7 PHE B 404 ALA B 420 -1 O PHE B 413 N TYR B 51
SHEET 7 D 7 VAL B 395 ILE B 397 -1 N ILE B 397 O PHE B 404
SHEET 1 E13 GLY B 103 GLU B 107 0
SHEET 2 E13 THR B 120 ARG B 135 -1 O THR B 121 N THR B 106
SHEET 3 E13 TRP B 140 PHE B 158 -1 O ALA B 148 N LEU B 128
SHEET 4 E13 LYS B 196 ASP B 218 -1 O ASN B 210 N GLY B 145
SHEET 5 E13 ASN B 221 ARG B 228 -1 O ASN B 221 N LEU B 217
SHEET 6 E13 GLU B 273 ASN B 281 -1 O MET B 274 N ARG B 228
SHEET 7 E13 TRP B 287 SER B 297 -1 O ILE B 289 N ASN B 281
SHEET 8 E13 ALA B 324 TYR B 333 -1 O ARG B 326 N ALA B 294
SHEET 9 E13 PHE B 341 ASP B 348 -1 O PHE B 341 N TYR B 333
SHEET 10 E13 ARG B 366 ASN B 378 -1 O GLY B 372 N ARG B 342
SHEET 11 E13 ALA B 381 GLY B 392 -1 O VAL B 385 N THR B 373
SHEET 12 E13 PHE B 404 ALA B 420 -1 O ASN B 416 N ASP B 384
SHEET 13 E13 VAL B 395 ILE B 397 -1 N ILE B 397 O PHE B 404
SHEET 1 F 2 VAL B 231 ILE B 233 0
SHEET 2 F 2 LEU B 269 LEU B 271 -1 O LEU B 269 N ILE B 233
SITE 1 AC1 9 TYR A 291 LEU A 293 ILE A 327 LEU A 329
SITE 2 AC1 9 TRP B 94 ALA B 96 SER B 97 ILE B 98
SITE 3 AC1 9 PHE B 146
SITE 1 AC2 7 LEU A 225 TRP A 275 ALA B 47 PRO B 80
SITE 2 AC2 7 MET B 82 MET B 126 ARG B 152
SITE 1 AC3 8 ALA B 74 SER B 100 TYR B 102 GLY B 103
SITE 2 AC3 8 LEU B 104 ALA B 105 PRO B 362 MET B 390
SITE 1 AC4 8 ALA A 74 SER A 100 TYR A 102 GLY A 103
SITE 2 AC4 8 LEU A 104 ALA A 105 PRO A 362 MET A 390
CRYST1 64.766 64.766 270.651 90.00 90.00 90.00 P 41 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 0.015440 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015440 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003695 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
