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HEADER LYASE 28-AUG-23 8QDA
TITLE WDYG1P SER256DHA (PMSF)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: YELLOWISH-GREEN 1-LIKE PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: EXOPHIALA DERMATITIDIS;
SOURCE 3 ORGANISM_TAXID: 5970;
SOURCE 4 GENE: YG1;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PCDFDUET
KEYWDS NATURAL PRODUCT BIOSYNTHESIS, POLYKETIDE SYNTHASE SYSTEM, ALPHA,
KEYWDS 2 BETA-HYDROLASE FOLD, POLYKETIDE SHORTENING, RETRO CLAISEN REACTION,
KEYWDS 3 LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.SCHMALHOFER,A.L.VAGSTAD,Q.ZHOU,H.B.BODE,M.GROLL
REVDAT 1 13-MAR-24 8QDA 0
JRNL AUTH M.SCHMALHOFER,A.L.VAGSTAD,Q.ZHOU,H.B.BODE,M.GROLL
JRNL TITL POLYKETIDE TRIMMING SHAPES DIHYDROXYNAPHTHALENE-MELANIN AND
JRNL TITL 2 ANTHRAQUINONE PIGMENTS
JRNL REF ADV SCI 2024
JRNL REFN ESSN 2198-3844
JRNL DOI 10.1002/ADVS.202400184
REMARK 2
REMARK 2 RESOLUTION. 1.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0267
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.40
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 75482
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 + TEST SET) : 0.148
REMARK 3 R VALUE (WORKING SET) : 0.147
REMARK 3 FREE R VALUE : 0.180
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3973
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.85
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.90
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5518
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.64
REMARK 3 BIN R VALUE (WORKING SET) : 0.1720
REMARK 3 BIN FREE R VALUE SET COUNT : 291
REMARK 3 BIN FREE R VALUE : 0.2420
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6551
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 22
REMARK 3 SOLVENT ATOMS : 706
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.94
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -3.30000
REMARK 3 B22 (A**2) : 2.87000
REMARK 3 B33 (A**2) : 0.44000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.050
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.022
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.055
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.880
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.973
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.964
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6755 ; 0.003 ; 0.013
REMARK 3 BOND LENGTHS OTHERS (A): 6297 ; 0.001 ; 0.016
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9144 ; 1.175 ; 1.646
REMARK 3 BOND ANGLES OTHERS (DEGREES): 14598 ; 1.168 ; 1.579
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 820 ; 6.202 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 330 ;30.924 ;22.788
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1154 ;11.941 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 30 ;16.060 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 845 ; 0.057 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7524 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1484 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 3286 ; 0.815 ; 2.045
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 3285 ; 0.814 ; 2.044
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4104 ; 1.112 ; 3.068
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 4105 ; 1.112 ; 3.069
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3469 ; 0.922 ; 2.227
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 3470 ; 0.922 ; 2.227
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 5041 ; 1.196 ; 3.268
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 8000 ; 2.092 ;25.463
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 8001 ; 2.093 ;25.469
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 13052 ; 0.484 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 2 A 410
REMARK 3 ORIGIN FOR THE GROUP (A): 2.280 17.650 21.665
REMARK 3 T TENSOR
REMARK 3 T11: 0.0136 T22: 0.0221
REMARK 3 T33: 0.0203 T12: 0.0078
REMARK 3 T13: 0.0005 T23: -0.0145
REMARK 3 L TENSOR
REMARK 3 L11: 0.7314 L22: 0.8775
REMARK 3 L33: 1.0506 L12: -0.1543
REMARK 3 L13: 0.1619 L23: 0.2405
REMARK 3 S TENSOR
REMARK 3 S11: 0.0031 S12: 0.1147 S13: -0.0855
REMARK 3 S21: -0.0736 S22: -0.0737 S23: 0.0813
REMARK 3 S31: 0.0580 S32: 0.0433 S33: 0.0706
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 2 B 412
REMARK 3 ORIGIN FOR THE GROUP (A): 42.659 23.177 44.083
REMARK 3 T TENSOR
REMARK 3 T11: 0.0064 T22: 0.0667
REMARK 3 T33: 0.0443 T12: 0.0004
REMARK 3 T13: 0.0081 T23: 0.0438
REMARK 3 L TENSOR
REMARK 3 L11: 1.2472 L22: 0.4848
REMARK 3 L33: 0.6456 L12: 0.1240
REMARK 3 L13: 0.0719 L23: 0.0092
REMARK 3 S TENSOR
REMARK 3 S11: -0.0129 S12: 0.1123 S13: 0.1338
REMARK 3 S21: -0.0510 S22: -0.0176 S23: -0.0724
REMARK 3 S31: -0.0250 S32: 0.1091 S33: 0.0305
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 8QDA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 30-AUG-23.
REMARK 100 THE DEPOSITION ID IS D_1292133001.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-MAR-21
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 9.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 79470
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.850
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : 0.05200
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 15.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.95
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.53800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: REFMAC
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.81
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.36
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM TRIS PH 9.2, 22% PEG 3350,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 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 42.81500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 61.23500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 44.23500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 61.23500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 42.81500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 44.23500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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 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 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 MET A -16
REMARK 465 GLY A -15
REMARK 465 TRP A -14
REMARK 465 SER A -13
REMARK 465 HIS A -12
REMARK 465 PRO A -11
REMARK 465 GLN A -10
REMARK 465 PHE A -9
REMARK 465 GLU A -8
REMARK 465 LYS A -7
REMARK 465 GLU A -6
REMARK 465 ASN A -5
REMARK 465 LEU A -4
REMARK 465 TYR A -3
REMARK 465 PHE A -2
REMARK 465 GLN A -1
REMARK 465 GLY A 0
REMARK 465 SER A 1
REMARK 465 ARG A 412
REMARK 465 THR A 413
REMARK 465 LYS A 414
REMARK 465 MET B -16
REMARK 465 GLY B -15
REMARK 465 TRP B -14
REMARK 465 SER B -13
REMARK 465 HIS B -12
REMARK 465 PRO B -11
REMARK 465 GLN B -10
REMARK 465 PHE B -9
REMARK 465 GLU B -8
REMARK 465 LYS B -7
REMARK 465 GLU B -6
REMARK 465 ASN B -5
REMARK 465 LEU B -4
REMARK 465 TYR B -3
REMARK 465 PHE B -2
REMARK 465 GLN B -1
REMARK 465 GLY B 0
REMARK 465 SER B 1
REMARK 465 LYS B 414
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 GLU A 4 CG CD OE1 OE2
REMARK 470 LYS A 14 CG CD CE NZ
REMARK 470 GLU A 93 CG CD OE1 OE2
REMARK 470 ASN A 170 CG OD1 ND2
REMARK 470 GLU B 4 CG CD OE1 OE2
REMARK 470 LYS B 58 CG CD CE NZ
REMARK 470 LYS B 83 CG CD CE NZ
REMARK 470 LYS B 297 CG CD CE NZ
REMARK 470 LYS B 394 CG CD CE NZ
REMARK 470 LYS B 403 CG CD CE NZ
REMARK 470 ARG B 412 CG CD NE CZ NH1 NH2
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 ARG A 9 -120.67 58.25
REMARK 500 LYS A 29 -45.40 -136.73
REMARK 500 PHE A 43 -1.06 68.99
REMARK 500 TYR A 189 -164.81 -110.69
REMARK 500 ALA A 283 -35.32 -155.98
REMARK 500 HIS A 284 -68.01 -152.63
REMARK 500 LEU A 298 -147.34 -106.24
REMARK 500 PHE A 302 -137.32 -120.37
REMARK 500 THR A 340 -171.67 -68.73
REMARK 500 LYS A 377 -152.75 -92.74
REMARK 500 MET A 379 -12.25 87.94
REMARK 500 ARG B 9 -118.60 53.18
REMARK 500 LYS B 29 -47.27 -137.85
REMARK 500 PHE B 43 -0.07 72.27
REMARK 500 TYR B 189 -164.71 -110.42
REMARK 500 ALA B 283 -31.96 -156.63
REMARK 500 HIS B 284 -69.00 -153.73
REMARK 500 LEU B 298 -147.20 -108.61
REMARK 500 PHE B 302 -141.47 -124.26
REMARK 500 THR B 340 -175.43 -69.42
REMARK 500 LYS B 377 -153.66 -93.13
REMARK 500 MET B 379 -16.36 84.95
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6HXA RELATED DB: PDB
REMARK 900 ANTI FROM P. LUMINESCENS CATALYSES TERMINAL POLYKETIDE SHORTENING
REMARK 900 IN THE BIOSYNTHESIS OF ANTHRAQUINONES
DBREF 8QDA A 2 414 UNP Q6BCB5 Q6BCB5_EXODE 2 414
DBREF 8QDA B 2 414 UNP Q6BCB5 Q6BCB5_EXODE 2 414
SEQADV 8QDA MET A -16 UNP Q6BCB5 INITIATING METHIONINE
SEQADV 8QDA GLY A -15 UNP Q6BCB5 EXPRESSION TAG
SEQADV 8QDA TRP A -14 UNP Q6BCB5 EXPRESSION TAG
SEQADV 8QDA SER A -13 UNP Q6BCB5 EXPRESSION TAG
SEQADV 8QDA HIS A -12 UNP Q6BCB5 EXPRESSION TAG
SEQADV 8QDA PRO A -11 UNP Q6BCB5 EXPRESSION TAG
SEQADV 8QDA GLN A -10 UNP Q6BCB5 EXPRESSION TAG
SEQADV 8QDA PHE A -9 UNP Q6BCB5 EXPRESSION TAG
SEQADV 8QDA GLU A -8 UNP Q6BCB5 EXPRESSION TAG
SEQADV 8QDA LYS A -7 UNP Q6BCB5 EXPRESSION TAG
SEQADV 8QDA GLU A -6 UNP Q6BCB5 EXPRESSION TAG
SEQADV 8QDA ASN A -5 UNP Q6BCB5 EXPRESSION TAG
SEQADV 8QDA LEU A -4 UNP Q6BCB5 EXPRESSION TAG
SEQADV 8QDA TYR A -3 UNP Q6BCB5 EXPRESSION TAG
SEQADV 8QDA PHE A -2 UNP Q6BCB5 EXPRESSION TAG
SEQADV 8QDA GLN A -1 UNP Q6BCB5 EXPRESSION TAG
SEQADV 8QDA GLY A 0 UNP Q6BCB5 EXPRESSION TAG
SEQADV 8QDA SER A 1 UNP Q6BCB5 EXPRESSION TAG
SEQADV 8QDA MET B -16 UNP Q6BCB5 INITIATING METHIONINE
SEQADV 8QDA GLY B -15 UNP Q6BCB5 EXPRESSION TAG
SEQADV 8QDA TRP B -14 UNP Q6BCB5 EXPRESSION TAG
SEQADV 8QDA SER B -13 UNP Q6BCB5 EXPRESSION TAG
SEQADV 8QDA HIS B -12 UNP Q6BCB5 EXPRESSION TAG
SEQADV 8QDA PRO B -11 UNP Q6BCB5 EXPRESSION TAG
SEQADV 8QDA GLN B -10 UNP Q6BCB5 EXPRESSION TAG
SEQADV 8QDA PHE B -9 UNP Q6BCB5 EXPRESSION TAG
SEQADV 8QDA GLU B -8 UNP Q6BCB5 EXPRESSION TAG
SEQADV 8QDA LYS B -7 UNP Q6BCB5 EXPRESSION TAG
SEQADV 8QDA GLU B -6 UNP Q6BCB5 EXPRESSION TAG
SEQADV 8QDA ASN B -5 UNP Q6BCB5 EXPRESSION TAG
SEQADV 8QDA LEU B -4 UNP Q6BCB5 EXPRESSION TAG
SEQADV 8QDA TYR B -3 UNP Q6BCB5 EXPRESSION TAG
SEQADV 8QDA PHE B -2 UNP Q6BCB5 EXPRESSION TAG
SEQADV 8QDA GLN B -1 UNP Q6BCB5 EXPRESSION TAG
SEQADV 8QDA GLY B 0 UNP Q6BCB5 EXPRESSION TAG
SEQADV 8QDA SER B 1 UNP Q6BCB5 EXPRESSION TAG
SEQRES 1 A 431 MET GLY TRP SER HIS PRO GLN PHE GLU LYS GLU ASN LEU
SEQRES 2 A 431 TYR PHE GLN GLY SER ALA THR GLU LYS TYR TYR ILE ARG
SEQRES 3 A 431 ASP ALA ILE THR LYS PRO ALA VAL HIS HIS GLU SER TYR
SEQRES 4 A 431 GLN LYS LEU TRP GLU THR LYS TRP LYS LYS PRO CYS GLU
SEQRES 5 A 431 MET GLY VAL TYR PRO PHE MET PHE GLY SER ILE LYS ASP
SEQRES 6 A 431 PHE GLU PRO VAL ALA GLN GLU ILE ILE LYS LYS GLY LEU
SEQRES 7 A 431 LYS GLU PRO TYR ASP TRP ASP GLU TYR ALA GLN MET TYR
SEQRES 8 A 431 PHE PRO LYS ALA GLU GLU LEU ALA LYS ILE ALA GLU GLU
SEQRES 9 A 431 ALA GLU ALA ALA GLY GLU LYS GLU LYS ALA SER GLU TYR
SEQRES 10 A 431 TYR LEU ARG SER SER ALA VAL TYR ARG ILE SER ARG PHE
SEQRES 11 A 431 PRO THR PRO ARG SER GLU LYS GLN LYS TYR ALA TRP ARG
SEQRES 12 A 431 LYS GLY CYS GLU VAL PHE TYR LYS GLY ALA ALA LEU MET
SEQRES 13 A 431 GLU TYR PRO ILE LYS GLU VAL ARG ILE PRO HIS LYS HIS
SEQRES 14 A 431 GLY ILE GLU GLY GLU GLY ASP VAL VAL PRO VAL ASN PHE
SEQRES 15 A 431 LEU LEU PRO PRO ASN ALA SER GLU THR SER PRO VAL PRO
SEQRES 16 A 431 CYS VAL LEU ILE ILE THR GLY LEU ASP GLY TYR ARG THR
SEQRES 17 A 431 GLU LEU ALA VAL TRP GLN GLN GLY TRP ARG SER LYS GLY
SEQRES 18 A 431 VAL ALA THR VAL ILE ALA GLU ILE PRO GLY THR GLY ASP
SEQRES 19 A 431 SER PRO ALA LEU ARG GLN ASP PRO THR SER PRO ASP ARG
SEQRES 20 A 431 GLN TRP SER SER VAL LEU ASP TRP ILE GLU SER GLN LYS
SEQRES 21 A 431 ALA VAL ASP SER LYS LYS ILE VAL ALA TRP GLY PHE DHA
SEQRES 22 A 431 THR GLY GLY TYR TYR ALA LEU ARG MET ALA HIS THR HIS
SEQRES 23 A 431 LYS ASP ARG LEU LEU ALA THR ILE SER LEU GLY GLY GLY
SEQRES 24 A 431 ALA HIS HIS MET PHE ASP ARG GLU TRP LEU GLU HIS ALA
SEQRES 25 A 431 ASN LYS LEU GLU TYR PRO PHE ASP LEU SER ASN THR LEU
SEQRES 26 A 431 ALA TYR LYS PHE GLY TYR PRO ASP LEU GLU SER PHE ILE
SEQRES 27 A 431 GLU GLU SER SER LYS PHE SER LEU LEU ASN ASP GLY THR
SEQRES 28 A 431 LEU GLN LYS PRO CYS THR LYS VAL LEU LEU VAL ASN GLY
SEQRES 29 A 431 ASN ASP ASP GLU ILE PHE PRO ILE ASP ASP MET PHE VAL
SEQRES 30 A 431 SER LEU GLU ASN GLY GLN PRO LYS LEU ALA ARG MET VAL
SEQRES 31 A 431 LYS GLY LYS LYS HIS MET GLY GLU PRO GLU SER PHE SER
SEQRES 32 A 431 ILE ILE LEU GLU TRP ILE HIS LYS LEU LEU GLY LEU ASP
SEQRES 33 A 431 GLY LYS ILE LYS GLU GLN LEU ALA MET ILE PRO SER ARG
SEQRES 34 A 431 THR LYS
SEQRES 1 B 431 MET GLY TRP SER HIS PRO GLN PHE GLU LYS GLU ASN LEU
SEQRES 2 B 431 TYR PHE GLN GLY SER ALA THR GLU LYS TYR TYR ILE ARG
SEQRES 3 B 431 ASP ALA ILE THR LYS PRO ALA VAL HIS HIS GLU SER TYR
SEQRES 4 B 431 GLN LYS LEU TRP GLU THR LYS TRP LYS LYS PRO CYS GLU
SEQRES 5 B 431 MET GLY VAL TYR PRO PHE MET PHE GLY SER ILE LYS ASP
SEQRES 6 B 431 PHE GLU PRO VAL ALA GLN GLU ILE ILE LYS LYS GLY LEU
SEQRES 7 B 431 LYS GLU PRO TYR ASP TRP ASP GLU TYR ALA GLN MET TYR
SEQRES 8 B 431 PHE PRO LYS ALA GLU GLU LEU ALA LYS ILE ALA GLU GLU
SEQRES 9 B 431 ALA GLU ALA ALA GLY GLU LYS GLU LYS ALA SER GLU TYR
SEQRES 10 B 431 TYR LEU ARG SER SER ALA VAL TYR ARG ILE SER ARG PHE
SEQRES 11 B 431 PRO THR PRO ARG SER GLU LYS GLN LYS TYR ALA TRP ARG
SEQRES 12 B 431 LYS GLY CYS GLU VAL PHE TYR LYS GLY ALA ALA LEU MET
SEQRES 13 B 431 GLU TYR PRO ILE LYS GLU VAL ARG ILE PRO HIS LYS HIS
SEQRES 14 B 431 GLY ILE GLU GLY GLU GLY ASP VAL VAL PRO VAL ASN PHE
SEQRES 15 B 431 LEU LEU PRO PRO ASN ALA SER GLU THR SER PRO VAL PRO
SEQRES 16 B 431 CYS VAL LEU ILE ILE THR GLY LEU ASP GLY TYR ARG THR
SEQRES 17 B 431 GLU LEU ALA VAL TRP GLN GLN GLY TRP ARG SER LYS GLY
SEQRES 18 B 431 VAL ALA THR VAL ILE ALA GLU ILE PRO GLY THR GLY ASP
SEQRES 19 B 431 SER PRO ALA LEU ARG GLN ASP PRO THR SER PRO ASP ARG
SEQRES 20 B 431 GLN TRP SER SER VAL LEU ASP TRP ILE GLU SER GLN LYS
SEQRES 21 B 431 ALA VAL ASP SER LYS LYS ILE VAL ALA TRP GLY PHE DHA
SEQRES 22 B 431 THR GLY GLY TYR TYR ALA LEU ARG MET ALA HIS THR HIS
SEQRES 23 B 431 LYS ASP ARG LEU LEU ALA THR ILE SER LEU GLY GLY GLY
SEQRES 24 B 431 ALA HIS HIS MET PHE ASP ARG GLU TRP LEU GLU HIS ALA
SEQRES 25 B 431 ASN LYS LEU GLU TYR PRO PHE ASP LEU SER ASN THR LEU
SEQRES 26 B 431 ALA TYR LYS PHE GLY TYR PRO ASP LEU GLU SER PHE ILE
SEQRES 27 B 431 GLU GLU SER SER LYS PHE SER LEU LEU ASN ASP GLY THR
SEQRES 28 B 431 LEU GLN LYS PRO CYS THR LYS VAL LEU LEU VAL ASN GLY
SEQRES 29 B 431 ASN ASP ASP GLU ILE PHE PRO ILE ASP ASP MET PHE VAL
SEQRES 30 B 431 SER LEU GLU ASN GLY GLN PRO LYS LEU ALA ARG MET VAL
SEQRES 31 B 431 LYS GLY LYS LYS HIS MET GLY GLU PRO GLU SER PHE SER
SEQRES 32 B 431 ILE ILE LEU GLU TRP ILE HIS LYS LEU LEU GLY LEU ASP
SEQRES 33 B 431 GLY LYS ILE LYS GLU GLN LEU ALA MET ILE PRO SER ARG
SEQRES 34 B 431 THR LYS
MODRES 8QDA DHA A 256 SER MODIFIED RESIDUE
MODRES 8QDA DHA B 256 SER MODIFIED RESIDUE
HET DHA A 256 5
HET DHA B 256 5
HET EDO A 501 4
HET EDO A 502 4
HET EDO A 503 4
HET PGE B 501 10
HETNAM DHA 2-AMINO-ACRYLIC ACID
HETNAM EDO 1,2-ETHANEDIOL
HETNAM PGE TRIETHYLENE GLYCOL
HETSYN DHA 2,3-DIDEHYDROALANINE
HETSYN EDO ETHYLENE GLYCOL
FORMUL 1 DHA 2(C3 H5 N O2)
FORMUL 3 EDO 3(C2 H6 O2)
FORMUL 6 PGE C6 H14 O4
FORMUL 7 HOH *706(H2 O)
HELIX 1 AA1 ILE A 8 LYS A 14 5 7
HELIX 2 AA2 ALA A 16 GLU A 20 5 5
HELIX 3 AA3 SER A 21 LYS A 29 1 9
HELIX 4 AA4 TRP A 30 GLY A 37 1 8
HELIX 5 AA5 SER A 45 GLY A 60 1 16
HELIX 6 AA6 ASP A 66 MET A 73 1 8
HELIX 7 AA7 TYR A 74 ALA A 91 1 18
HELIX 8 AA8 GLU A 93 ARG A 112 1 20
HELIX 9 AA9 SER A 118 LEU A 138 1 21
HELIX 10 AB1 TYR A 189 ALA A 194 1 6
HELIX 11 AB2 TRP A 196 LYS A 203 1 8
HELIX 12 AB3 THR A 226 GLN A 242 1 17
HELIX 13 AB4 DHA A 256 HIS A 269 1 14
HELIX 14 AB5 LYS A 270 LEU A 273 5 4
HELIX 15 AB6 HIS A 284 PHE A 287 5 4
HELIX 16 AB7 ASP A 288 ASN A 296 1 9
HELIX 17 AB8 ASP A 303 PHE A 312 1 10
HELIX 18 AB9 ASP A 316 SER A 324 1 9
HELIX 19 AC1 SER A 325 SER A 328 5 4
HELIX 20 AC2 GLY A 333 LYS A 337 5 5
HELIX 21 AC3 ILE A 355 GLU A 363 1 9
HELIX 22 AC4 PRO A 382 GLY A 397 1 16
HELIX 23 AC5 LYS A 401 ALA A 407 1 7
HELIX 24 AC6 ILE B 8 LYS B 14 5 7
HELIX 25 AC7 ALA B 16 GLU B 20 5 5
HELIX 26 AC8 SER B 21 LYS B 29 1 9
HELIX 27 AC9 TRP B 30 GLY B 37 1 8
HELIX 28 AD1 SER B 45 GLY B 60 1 16
HELIX 29 AD2 ASP B 66 MET B 73 1 8
HELIX 30 AD3 TYR B 74 ALA B 91 1 18
HELIX 31 AD4 GLU B 93 ARG B 112 1 20
HELIX 32 AD5 SER B 118 ALA B 137 1 20
HELIX 33 AD6 TYR B 189 ALA B 194 1 6
HELIX 34 AD7 TRP B 196 LYS B 203 1 8
HELIX 35 AD8 THR B 226 GLN B 242 1 17
HELIX 36 AD9 THR B 257 HIS B 269 1 13
HELIX 37 AE1 LYS B 270 LEU B 273 5 4
HELIX 38 AE2 HIS B 284 PHE B 287 5 4
HELIX 39 AE3 ASP B 288 ASN B 296 1 9
HELIX 40 AE4 ASP B 303 PHE B 312 1 10
HELIX 41 AE5 ASP B 316 SER B 324 1 9
HELIX 42 AE6 SER B 325 SER B 328 5 4
HELIX 43 AE7 GLY B 333 LYS B 337 5 5
HELIX 44 AE8 ILE B 355 GLU B 363 1 9
HELIX 45 AE9 LYS B 377 GLU B 381 5 5
HELIX 46 AF1 PRO B 382 GLY B 397 1 16
HELIX 47 AF2 LYS B 401 ALA B 407 1 7
SHEET 1 AA116 LYS A 144 PRO A 149 0
SHEET 2 AA116 VAL A 160 LEU A 166 -1 O VAL A 161 N ILE A 148
SHEET 3 AA116 ALA A 206 ALA A 210 -1 O THR A 207 N LEU A 166
SHEET 4 AA116 VAL A 177 ILE A 183 1 N ILE A 182 O VAL A 208
SHEET 5 AA116 VAL A 245 PHE A 255 1 O ASP A 246 N VAL A 177
SHEET 6 AA116 ALA A 275 LEU A 279 1 O ILE A 277 N GLY A 254
SHEET 7 AA116 LYS A 341 GLY A 347 1 O VAL A 345 N SER A 278
SHEET 8 AA116 LYS A 368 VAL A 373 1 O LEU A 369 N VAL A 342
SHEET 9 AA116 LYS B 368 VAL B 373 -1 O LYS B 368 N ALA A 370
SHEET 10 AA116 LYS B 341 GLY B 347 1 N VAL B 342 O LEU B 369
SHEET 11 AA116 ALA B 275 LEU B 279 1 N SER B 278 O VAL B 345
SHEET 12 AA116 VAL B 245 PHE B 255 1 N GLY B 254 O ILE B 277
SHEET 13 AA116 VAL B 177 ILE B 183 1 N VAL B 177 O ASP B 246
SHEET 14 AA116 ALA B 206 ALA B 210 1 O VAL B 208 N ILE B 182
SHEET 15 AA116 VAL B 160 LEU B 166 -1 N LEU B 166 O THR B 207
SHEET 16 AA116 LYS B 144 PRO B 149 -1 N ILE B 148 O VAL B 161
LINK C PHE A 255 N DHA A 256 1555 1555 1.33
LINK C DHA A 256 N THR A 257 1555 1555 1.34
LINK C PHE B 255 N DHA B 256 1555 1555 1.34
LINK C DHA B 256 N THR B 257 1555 1555 1.34
CISPEP 1 TYR A 39 PRO A 40 0 0.78
CISPEP 2 GLU A 63 PRO A 64 0 -2.94
CISPEP 3 PHE A 113 PRO A 114 0 -0.76
CISPEP 4 GLU A 381 PRO A 382 0 -1.47
CISPEP 5 TYR B 39 PRO B 40 0 -0.27
CISPEP 6 GLU B 63 PRO B 64 0 -4.47
CISPEP 7 PHE B 113 PRO B 114 0 -2.26
CISPEP 8 GLU B 381 PRO B 382 0 -3.47
CRYST1 85.630 88.470 122.470 90.00 90.00 90.00 P 21 21 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 0.011678 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011303 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008165 0.00000
TER 3275 SER A 411
TER 6553 THR B 413
MASTER 385 0 6 47 16 0 0 6 7279 2 36 68
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