HEADER TRANSPORT PROTEIN 21-DEC-07 3BRZ
TITLE CRYSTAL STRUCTURE OF THE PSEUDOMONAS PUTIDA TOLUENE TRANSPORTER TODX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TODX;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SEQUENCE DATABASE RESIDUES 21-453;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS PUTIDA;
SOURCE 3 STRAIN: F1;
SOURCE 4 GENE: TODX;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: C43(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PBAD22
KEYWDS BETA BARREL, OUTER MEMBRANE PROTEIN, TRANSPORT PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR E.M.HEARN,D.R.PATEL,B.VAN DEN BERG
REVDAT 4 21-FEB-24 3BRZ 1 REMARK SEQADV
REVDAT 3 24-FEB-09 3BRZ 1 VERSN
REVDAT 2 15-JUL-08 3BRZ 1 JRNL
REVDAT 1 10-JUN-08 3BRZ 0
JRNL AUTH E.M.HEARN,D.R.PATEL,B.VAN DEN BERG
JRNL TITL OUTER-MEMBRANE TRANSPORT OF AROMATIC HYDROCARBONS AS A FIRST
JRNL TITL 2 STEP IN BIODEGRADATION.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 105 8601 2008
JRNL REFN ISSN 0027-8424
JRNL PMID 18559855
JRNL DOI 10.1073/PNAS.0801264105
REMARK 2
REMARK 2 RESOLUTION. 3.20 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) : 3.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.00
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) (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 12784
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) : 0.256
REMARK 3 FREE R VALUE : 0.300
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 969
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) : 3.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.34
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.70
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.3450
REMARK 3 BIN FREE R VALUE : 0.4310
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 121
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.039
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3037
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) : 83.09
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -33.16500
REMARK 3 B22 (A**2) : 16.36100
REMARK 3 B33 (A**2) : 16.80400
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) : 0.45
REMARK 3 ESD FROM SIGMAA (A) : 0.57
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) : 0.55
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.75
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.900
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 3BRZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-JAN-08.
REMARK 100 THE DEPOSITION ID IS D_1000045894.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-JUL-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.6
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) : 0.9785
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 : 15800
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.100
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 11.30
REMARK 200 R MERGE (I) : 0.09600
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) : 3.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.21
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.1
REMARK 200 DATA REDUNDANCY IN SHELL : 9.50
REMARK 200 R MERGE FOR SHELL (I) : 0.89400
REMARK 200 R SYM FOR SHELL (I) : NULL
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: SAD
REMARK 200 SOFTWARE USED: SHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 71.30
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.29
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG 4000, 0.2 M AMMONIUM SULFATE,
REMARK 280 0.1 M SODIUM ACETATE, PH 4.6, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
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+1/2
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 0.00000
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 0.00000
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 39.15100
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 61.67200
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 83.56700
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 39.15100
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 61.67200
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 83.56700
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 39.15100
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 61.67200
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 83.56700
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 39.15100
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 61.67200
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 83.56700
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 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 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 ASP A 61
REMARK 465 SER A 62
REMARK 465 HIS A 63
REMARK 465 ARG A 72
REMARK 465 SER A 73
REMARK 465 ASN A 74
REMARK 465 ASN A 75
REMARK 465 ARG A 76
REMARK 465 GLY A 77
REMARK 465 ARG A 206
REMARK 465 ASN A 207
REMARK 465 SER A 208
REMARK 465 THR A 209
REMARK 465 GLN A 359
REMARK 465 ALA A 360
REMARK 465 LEU A 361
REMARK 465 ASP A 362
REMARK 465 SER A 363
REMARK 465 GLU A 364
REMARK 465 GLN A 405
REMARK 465 THR A 406
REMARK 465 PRO A 407
REMARK 465 SER A 408
REMARK 465 TYR A 409
REMARK 465 LEU A 410
REMARK 465 ALA A 411
REMARK 465 GLY A 412
REMARK 465 THR A 413
REMARK 465 GLU A 414
REMARK 465 HIS A 434
REMARK 465 HIS A 435
REMARK 465 HIS A 436
REMARK 465 HIS A 437
REMARK 465 HIS A 438
REMARK 465 HIS A 439
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 THR A 1 N - CA - C ANGL. DEV. = 23.3 DEGREES
REMARK 500 PHE A 4 CB - CA - C ANGL. DEV. = 29.4 DEGREES
REMARK 500 PHE A 4 CA - C - N ANGL. DEV. = 14.7 DEGREES
REMARK 500 PRO A 82 C - N - CA ANGL. DEV. = 12.3 DEGREES
REMARK 500 PRO A 278 C - N - CA ANGL. DEV. = 9.2 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 GLN A 2 114.11 7.78
REMARK 500 VAL A 3 42.63 -61.28
REMARK 500 PHE A 4 -119.75 179.37
REMARK 500 MET A 16 40.13 -96.36
REMARK 500 SER A 20 -41.14 -166.09
REMARK 500 SER A 21 -70.77 -31.06
REMARK 500 TYR A 23 -168.85 161.95
REMARK 500 THR A 25 31.44 -149.26
REMARK 500 SER A 32 -65.96 -135.78
REMARK 500 ASN A 33 82.57 -161.21
REMARK 500 PHE A 46 88.56 -166.56
REMARK 500 SER A 70 -55.38 160.88
REMARK 500 PRO A 82 -173.50 -59.03
REMARK 500 GLN A 83 40.76 -177.05
REMARK 500 LEU A 90 102.14 -162.45
REMARK 500 ASP A 91 120.59 8.22
REMARK 500 ASP A 92 -15.93 55.89
REMARK 500 SER A 102 148.40 -171.52
REMARK 500 SER A 103 -169.21 -102.61
REMARK 500 GLU A 108 71.98 -154.66
REMARK 500 LYS A 112 -35.70 -170.16
REMARK 500 ARG A 131 112.82 -169.73
REMARK 500 PHE A 141 172.27 176.67
REMARK 500 THR A 146 43.08 -161.70
REMARK 500 SER A 147 28.84 42.16
REMARK 500 LYS A 148 -44.11 -155.41
REMARK 500 GLU A 165 76.35 -155.05
REMARK 500 SER A 171 -74.24 -29.11
REMARK 500 PHE A 193 -29.87 151.41
REMARK 500 THR A 196 26.90 -54.87
REMARK 500 ALA A 199 140.88 169.27
REMARK 500 ALA A 213 -16.44 66.92
REMARK 500 VAL A 214 73.02 66.52
REMARK 500 ARG A 222 119.58 -168.19
REMARK 500 LYS A 228 88.01 -63.44
REMARK 500 ASN A 232 18.18 -155.50
REMARK 500 ALA A 237 144.13 -171.28
REMARK 500 LYS A 251 151.10 -44.86
REMARK 500 ASN A 274 60.07 62.35
REMARK 500 PRO A 278 171.28 -48.20
REMARK 500 PHE A 289 32.54 -96.08
REMARK 500 ASN A 290 121.94 179.37
REMARK 500 GLU A 291 56.00 -68.94
REMARK 500 ARG A 292 -67.33 -162.13
REMARK 500 ALA A 297 118.27 -169.00
REMARK 500 ASP A 309 -166.87 -75.67
REMARK 500 HIS A 328 -74.94 -70.46
REMARK 500 ALA A 341 108.63 -169.63
REMARK 500 ASN A 345 -174.08 175.38
REMARK 500 ASN A 346 10.17 -60.68
REMARK 500
REMARK 500 THIS ENTRY HAS 60 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 PHE A 4 0.12 SIDE CHAIN
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 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE C8E A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE C8E A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE C8E A 503
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3BRY RELATED DB: PDB
REMARK 900 RELATED ID: 3BS0 RELATED DB: PDB
DBREF 3BRZ A 1 433 UNP Q51971 Q51971_PSEPU 21 453
SEQADV 3BRZ ALA A 67 UNP Q51971 PRO 87 VARIANT
SEQADV 3BRZ GLY A 77 UNP Q51971 ALA 97 VARIANT
SEQADV 3BRZ HIS A 434 UNP Q51971 EXPRESSION TAG
SEQADV 3BRZ HIS A 435 UNP Q51971 EXPRESSION TAG
SEQADV 3BRZ HIS A 436 UNP Q51971 EXPRESSION TAG
SEQADV 3BRZ HIS A 437 UNP Q51971 EXPRESSION TAG
SEQADV 3BRZ HIS A 438 UNP Q51971 EXPRESSION TAG
SEQADV 3BRZ HIS A 439 UNP Q51971 EXPRESSION TAG
SEQRES 1 A 439 THR GLN VAL PHE ASP LEU GLU GLY TYR GLY ALA ILE SER
SEQRES 2 A 439 ARG ALA MET GLY GLY THR SER SER SER TYR TYR THR GLY
SEQRES 3 A 439 ASN ALA ALA LEU ILE SER ASN PRO ALA THR LEU SER PHE
SEQRES 4 A 439 ALA PRO ASP GLY ASN GLN PHE GLU LEU GLY LEU ASP VAL
SEQRES 5 A 439 VAL THR THR ASP ILE LYS VAL HIS ASP SER HIS GLY ALA
SEQRES 6 A 439 GLU ALA LYS SER SER THR ARG SER ASN ASN ARG GLY PRO
SEQRES 7 A 439 TYR VAL GLY PRO GLN LEU SER TYR VAL ALA GLN LEU ASP
SEQRES 8 A 439 ASP TRP ARG PHE GLY ALA GLY LEU PHE VAL SER SER GLY
SEQRES 9 A 439 LEU GLY THR GLU TYR GLY SER LYS SER PHE LEU SER GLN
SEQRES 10 A 439 THR GLU ASN GLY ILE GLN THR SER PHE ASP ASN SER SER
SEQRES 11 A 439 ARG LEU ILE VAL LEU ARG ALA PRO ILE GLY PHE SER TYR
SEQRES 12 A 439 GLN ALA THR SER LYS LEU THR PHE GLY ALA SER VAL ASP
SEQRES 13 A 439 LEU VAL TRP THR SER LEU ASN LEU GLU LEU LEU LEU PRO
SEQRES 14 A 439 SER SER GLN VAL GLY ALA LEU THR ALA GLN GLY ASN LEU
SEQRES 15 A 439 SER GLY GLY LEU VAL PRO SER LEU ALA GLY PHE VAL GLY
SEQRES 16 A 439 THR GLY GLY ALA ALA HIS PHE SER LEU SER ARG ASN SER
SEQRES 17 A 439 THR ALA GLY GLY ALA VAL ASP ALA VAL GLY TRP GLY GLY
SEQRES 18 A 439 ARG LEU GLY LEU THR TYR LYS LEU THR ASP ASN THR VAL
SEQRES 19 A 439 LEU GLY ALA MET TYR ASN PHE LYS THR SER VAL GLY ASP
SEQRES 20 A 439 LEU GLU GLY LYS ALA THR LEU SER ALA ILE SER GLY ASP
SEQRES 21 A 439 GLY ALA VAL LEU PRO LEU ASP GLY ASP ILE ARG VAL LYS
SEQRES 22 A 439 ASN PHE GLU MET PRO ALA SER LEU THR LEU GLY LEU ALA
SEQRES 23 A 439 HIS GLN PHE ASN GLU ARG TRP VAL VAL ALA ALA ASP ILE
SEQRES 24 A 439 LYS ARG ALA TYR TRP GLY ASP VAL MET ASP SER MET ASN
SEQRES 25 A 439 VAL ALA PHE ILE SER GLN LEU GLY GLY ILE ASP VAL ALA
SEQRES 26 A 439 LEU PRO HIS ARG TYR GLN ASP ILE THR VAL ALA SER ILE
SEQRES 27 A 439 GLY THR ALA TYR LYS TYR ASN ASN ASP LEU THR LEU ARG
SEQRES 28 A 439 ALA GLY TYR SER TYR ALA GLN GLN ALA LEU ASP SER GLU
SEQRES 29 A 439 LEU ILE LEU PRO VAL ILE PRO ALA TYR LEU LYS ARG HIS
SEQRES 30 A 439 VAL THR PHE GLY GLY GLU TYR ASP PHE ASP LYS ASP SER
SEQRES 31 A 439 ARG ILE ASN LEU ALA ILE SER PHE GLY LEU ARG GLU ARG
SEQRES 32 A 439 VAL GLN THR PRO SER TYR LEU ALA GLY THR GLU MET LEU
SEQRES 33 A 439 ARG GLN SER HIS SER GLN ILE ASN ALA VAL VAL SER TYR
SEQRES 34 A 439 SER LYS ASN PHE HIS HIS HIS HIS HIS HIS
HET C8E A 500 21
HET C8E A 501 21
HET C8E A 502 21
HET C8E A 503 21
HETNAM C8E (HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE
FORMUL 2 C8E 4(C16 H34 O5)
HELIX 1 1 GLY A 10 MET A 16 1 7
HELIX 2 2 THR A 25 SER A 32 5 8
HELIX 3 3 ALA A 35 ALA A 40 5 6
HELIX 4 4 SER A 113 LEU A 115 5 3
HELIX 5 5 SER A 170 GLN A 179 1 10
HELIX 6 6 GLY A 185 ALA A 191 1 7
HELIX 7 7 VAL A 194 GLY A 197 5 4
SHEET 1 A 6 GLN A 45 GLU A 47 0
SHEET 2 A 6 SER A 85 LEU A 90 -1 O SER A 85 N GLU A 47
SHEET 3 A 6 TRP A 93 GLY A 98 -1 O PHE A 95 N ALA A 88
SHEET 4 A 6 ILE A 139 GLN A 144 -1 O SER A 142 N ARG A 94
SHEET 5 A 6 LEU A 149 PRO A 169 -1 O PHE A 151 N TYR A 143
SHEET 6 A 6 ALA A 199 SER A 203 -1 O ALA A 200 N LEU A 168
SHEET 1 B12 PHE A 100 GLU A 108 0
SHEET 2 B12 SER A 129 ARG A 136 -1 O ARG A 136 N PHE A 100
SHEET 3 B12 LEU A 149 PRO A 169 -1 O SER A 161 N ILE A 133
SHEET 4 B12 ASP A 215 LYS A 228 -1 O ALA A 216 N THR A 160
SHEET 5 B12 THR A 233 ASN A 240 -1 O TYR A 239 N LEU A 223
SHEET 6 B12 ALA A 279 HIS A 287 -1 O GLY A 284 N GLY A 236
SHEET 7 B12 VAL A 294 TYR A 303 -1 O TYR A 303 N ALA A 279
SHEET 8 B12 ILE A 333 TYR A 342 -1 O VAL A 335 N LYS A 300
SHEET 9 B12 LEU A 348 ALA A 357 -1 O LEU A 350 N TYR A 342
SHEET 10 B12 HIS A 377 TYR A 384 -1 O GLY A 381 N ARG A 351
SHEET 11 B12 ASN A 393 GLY A 399 -1 O PHE A 398 N VAL A 378
SHEET 12 B12 ILE A 423 SER A 428 -1 O ASN A 424 N SER A 397
SHEET 1 C 2 ASP A 51 VAL A 52 0
SHEET 2 C 2 VAL A 80 GLY A 81 -1 O GLY A 81 N ASP A 51
SHEET 1 D 3 LYS A 58 HIS A 60 0
SHEET 2 D 3 ARG A 417 HIS A 420 -1 O ARG A 417 N HIS A 60
SHEET 3 D 3 GLU A 402 VAL A 404 -1 N GLU A 402 O HIS A 420
SHEET 1 E 2 GLN A 117 THR A 118 0
SHEET 2 E 2 ILE A 122 GLN A 123 -1 O ILE A 122 N THR A 118
SHEET 1 F 5 LEU A 182 SER A 183 0
SHEET 2 F 5 GLY A 321 PRO A 327 -1 O ASP A 323 N SER A 183
SHEET 3 F 5 SER A 310 ILE A 316 -1 N MET A 311 O LEU A 326
SHEET 4 F 5 VAL A 263 LYS A 273 -1 N LYS A 273 O ASN A 312
SHEET 5 F 5 LEU A 248 ILE A 257 -1 N ALA A 256 O LEU A 264
SITE 1 AC1 3 LEU A 164 GLN A 172 LEU A 176
SITE 1 AC2 3 ALA A 191 ALA A 200 ILE A 322
SITE 1 AC3 3 ALA A 336 TYR A 356 GLN A 358
SITE 1 AC4 2 LEU A 50 LEU A 394
CRYST1 78.302 123.344 167.134 90.00 90.00 90.00 I 2 2 2 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 0.012771 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008107 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005983 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
