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HEADER LYASE 28-AUG-23 8QD8
TITLE WDYG1P IN COMPLEX WITH 1,3-DIHYDROXYNAPHTHALENE
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 8QD8 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. 1.65 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) : 1.65
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.57
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 3 NUMBER OF REFLECTIONS : 106353
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) : 0.165
REMARK 3 R VALUE (WORKING SET) : 0.163
REMARK 3 FREE R VALUE : 0.188
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 5598
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) : 1.65
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.69
REMARK 3 REFLECTION IN BIN (WORKING SET) : 7695
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.25
REMARK 3 BIN R VALUE (WORKING SET) : 0.2530
REMARK 3 BIN FREE R VALUE SET COUNT : 405
REMARK 3 BIN FREE R VALUE : 0.3080
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6604
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 32
REMARK 3 SOLVENT ATOMS : 757
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.51
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.99000
REMARK 3 B22 (A**2) : 9.47000
REMARK 3 B33 (A**2) : -11.47000
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): 0.025
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.018
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.045
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.778
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.973
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.966
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6871 ; 0.003 ; 0.013
REMARK 3 BOND LENGTHS OTHERS (A): 6419 ; 0.001 ; 0.016
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9303 ; 1.160 ; 1.645
REMARK 3 BOND ANGLES OTHERS (DEGREES): 14904 ; 1.174 ; 1.580
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 833 ; 6.096 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 336 ;30.242 ;22.798
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1198 ;11.841 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 32 ;14.600 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 854 ; 0.055 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7657 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1519 ; 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): 3323 ; 0.706 ; 1.800
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 3322 ; 0.704 ; 1.800
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4159 ; 0.915 ; 2.706
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 4160 ; 0.915 ; 2.706
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3548 ; 0.762 ; 1.968
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 3549 ; 0.762 ; 1.969
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 5145 ; 0.971 ; 2.892
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 8206 ; 1.715 ;22.823
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 8207 ; 1.715 ;22.823
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 13290 ; 0.482 ; 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 1 A 411
REMARK 3 ORIGIN FOR THE GROUP (A): 2.445 17.612 21.880
REMARK 3 T TENSOR
REMARK 3 T11: 0.0749 T22: 0.0182
REMARK 3 T33: 0.1003 T12: 0.0140
REMARK 3 T13: 0.0032 T23: -0.0117
REMARK 3 L TENSOR
REMARK 3 L11: 0.8465 L22: 0.7210
REMARK 3 L33: 1.0928 L12: -0.0778
REMARK 3 L13: 0.2441 L23: 0.1511
REMARK 3 S TENSOR
REMARK 3 S11: -0.0009 S12: 0.1057 S13: -0.0568
REMARK 3 S21: -0.0614 S22: -0.0605 S23: 0.0763
REMARK 3 S31: 0.0186 S32: 0.0139 S33: 0.0614
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 1 B 412
REMARK 3 ORIGIN FOR THE GROUP (A): 42.701 23.275 44.261
REMARK 3 T TENSOR
REMARK 3 T11: 0.0501 T22: 0.1127
REMARK 3 T33: 0.1344 T12: -0.0016
REMARK 3 T13: 0.0048 T23: 0.0531
REMARK 3 L TENSOR
REMARK 3 L11: 1.1043 L22: 0.5089
REMARK 3 L33: 0.6864 L12: 0.0807
REMARK 3 L13: 0.1412 L23: 0.0093
REMARK 3 S TENSOR
REMARK 3 S11: -0.0208 S12: 0.0972 S13: 0.1245
REMARK 3 S21: -0.0437 S22: -0.0184 S23: -0.1012
REMARK 3 S31: -0.0457 S32: 0.1626 S33: 0.0392
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 8QD8 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_1292132999.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-SEP-21
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.7
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 : 111963
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.650
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 (%) : 98.7
REMARK 200 DATA REDUNDANCY : 4.400
REMARK 200 R MERGE (I) : 0.05800
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 11.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.75
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.4
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.65200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.100
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 (%): 48.36
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.38
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM TRIS PH 8.7, 24% 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 42.90000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 61.52500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 44.42500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 61.52500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 42.90000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 44.42500
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 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 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 ASN A 170 CG OD1 ND2
REMARK 470 ARG A 412 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 412 CG CD NE CZ NH1 NH2
REMARK 470 THR B 413 OG1 CG2
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 -127.40 58.36
REMARK 500 LYS A 29 -44.06 -141.07
REMARK 500 PHE A 43 -4.42 69.31
REMARK 500 TYR A 189 -164.33 -109.45
REMARK 500 SER A 256 -121.99 59.10
REMARK 500 ALA A 283 -31.56 -160.44
REMARK 500 HIS A 284 -69.06 -153.98
REMARK 500 LEU A 298 -148.20 -103.68
REMARK 500 PHE A 302 -133.45 -122.38
REMARK 500 THR A 340 -173.85 -69.39
REMARK 500 LYS A 377 -153.59 -94.54
REMARK 500 MET A 379 -13.41 86.17
REMARK 500 ARG B 9 -127.19 60.56
REMARK 500 LYS B 29 -49.32 -143.63
REMARK 500 TYR B 189 -165.07 -109.51
REMARK 500 SER B 256 -122.47 60.06
REMARK 500 ALA B 283 -32.52 -154.63
REMARK 500 HIS B 284 -67.68 -153.23
REMARK 500 LEU B 298 -147.18 -103.22
REMARK 500 PHE B 302 -136.35 -118.60
REMARK 500 THR B 340 -176.42 -68.74
REMARK 500 LYS B 377 -154.47 -96.39
REMARK 500 MET B 379 -14.07 86.76
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH B 954 DISTANCE = 6.52 ANGSTROMS
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 8QD8 A 2 414 UNP Q6BCB5 Q6BCB5_EXODE 2 414
DBREF 8QD8 B 2 414 UNP Q6BCB5 Q6BCB5_EXODE 2 414
SEQADV 8QD8 MET A -16 UNP Q6BCB5 INITIATING METHIONINE
SEQADV 8QD8 GLY A -15 UNP Q6BCB5 EXPRESSION TAG
SEQADV 8QD8 TRP A -14 UNP Q6BCB5 EXPRESSION TAG
SEQADV 8QD8 SER A -13 UNP Q6BCB5 EXPRESSION TAG
SEQADV 8QD8 HIS A -12 UNP Q6BCB5 EXPRESSION TAG
SEQADV 8QD8 PRO A -11 UNP Q6BCB5 EXPRESSION TAG
SEQADV 8QD8 GLN A -10 UNP Q6BCB5 EXPRESSION TAG
SEQADV 8QD8 PHE A -9 UNP Q6BCB5 EXPRESSION TAG
SEQADV 8QD8 GLU A -8 UNP Q6BCB5 EXPRESSION TAG
SEQADV 8QD8 LYS A -7 UNP Q6BCB5 EXPRESSION TAG
SEQADV 8QD8 GLU A -6 UNP Q6BCB5 EXPRESSION TAG
SEQADV 8QD8 ASN A -5 UNP Q6BCB5 EXPRESSION TAG
SEQADV 8QD8 LEU A -4 UNP Q6BCB5 EXPRESSION TAG
SEQADV 8QD8 TYR A -3 UNP Q6BCB5 EXPRESSION TAG
SEQADV 8QD8 PHE A -2 UNP Q6BCB5 EXPRESSION TAG
SEQADV 8QD8 GLN A -1 UNP Q6BCB5 EXPRESSION TAG
SEQADV 8QD8 GLY A 0 UNP Q6BCB5 EXPRESSION TAG
SEQADV 8QD8 SER A 1 UNP Q6BCB5 EXPRESSION TAG
SEQADV 8QD8 MET B -16 UNP Q6BCB5 INITIATING METHIONINE
SEQADV 8QD8 GLY B -15 UNP Q6BCB5 EXPRESSION TAG
SEQADV 8QD8 TRP B -14 UNP Q6BCB5 EXPRESSION TAG
SEQADV 8QD8 SER B -13 UNP Q6BCB5 EXPRESSION TAG
SEQADV 8QD8 HIS B -12 UNP Q6BCB5 EXPRESSION TAG
SEQADV 8QD8 PRO B -11 UNP Q6BCB5 EXPRESSION TAG
SEQADV 8QD8 GLN B -10 UNP Q6BCB5 EXPRESSION TAG
SEQADV 8QD8 PHE B -9 UNP Q6BCB5 EXPRESSION TAG
SEQADV 8QD8 GLU B -8 UNP Q6BCB5 EXPRESSION TAG
SEQADV 8QD8 LYS B -7 UNP Q6BCB5 EXPRESSION TAG
SEQADV 8QD8 GLU B -6 UNP Q6BCB5 EXPRESSION TAG
SEQADV 8QD8 ASN B -5 UNP Q6BCB5 EXPRESSION TAG
SEQADV 8QD8 LEU B -4 UNP Q6BCB5 EXPRESSION TAG
SEQADV 8QD8 TYR B -3 UNP Q6BCB5 EXPRESSION TAG
SEQADV 8QD8 PHE B -2 UNP Q6BCB5 EXPRESSION TAG
SEQADV 8QD8 GLN B -1 UNP Q6BCB5 EXPRESSION TAG
SEQADV 8QD8 GLY B 0 UNP Q6BCB5 EXPRESSION TAG
SEQADV 8QD8 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 SER
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 SER
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
HET EDO A 501 4
HET EDO A 502 4
HET QPI A 503 12
HET QPI B 501 12
HETNAM EDO 1,2-ETHANEDIOL
HETNAM QPI NAPHTHALENE-1,3-DIOL
HETSYN EDO ETHYLENE GLYCOL
HETSYN QPI 1,3-DIHYDROXYNAPHTHALENE
FORMUL 3 EDO 2(C2 H6 O2)
FORMUL 5 QPI 2(C10 H8 O2)
FORMUL 7 HOH *757(H2 O)
HELIX 1 AA1 SER A 1 LYS A 5 5 5
HELIX 2 AA2 ILE A 8 LYS A 14 5 7
HELIX 3 AA3 ALA A 16 GLU A 20 5 5
HELIX 4 AA4 SER A 21 LYS A 29 1 9
HELIX 5 AA5 TRP A 30 GLY A 37 1 8
HELIX 6 AA6 SER A 45 GLY A 60 1 16
HELIX 7 AA7 ASP A 66 MET A 73 1 8
HELIX 8 AA8 TYR A 74 ALA A 91 1 18
HELIX 9 AA9 GLU A 93 ARG A 112 1 20
HELIX 10 AB1 SER A 118 LEU A 138 1 21
HELIX 11 AB2 TYR A 189 ALA A 194 1 6
HELIX 12 AB3 TRP A 196 LYS A 203 1 8
HELIX 13 AB4 THR A 226 GLN A 242 1 17
HELIX 14 AB5 THR A 257 HIS A 269 1 13
HELIX 15 AB6 LYS A 270 LEU A 273 5 4
HELIX 16 AB7 HIS A 284 PHE A 287 5 4
HELIX 17 AB8 ASP A 288 ASN A 296 1 9
HELIX 18 AB9 ASP A 303 PHE A 312 1 10
HELIX 19 AC1 ASP A 316 SER A 324 1 9
HELIX 20 AC2 SER A 325 SER A 328 5 4
HELIX 21 AC3 GLY A 333 LYS A 337 5 5
HELIX 22 AC4 ILE A 355 GLU A 363 1 9
HELIX 23 AC5 PRO A 382 GLY A 397 1 16
HELIX 24 AC6 LYS A 401 ALA A 407 1 7
HELIX 25 AC7 SER B 1 LYS B 5 5 5
HELIX 26 AC8 ILE B 8 LYS B 14 5 7
HELIX 27 AC9 ALA B 16 GLU B 20 5 5
HELIX 28 AD1 SER B 21 LYS B 29 1 9
HELIX 29 AD2 TRP B 30 GLY B 37 1 8
HELIX 30 AD3 SER B 45 GLY B 60 1 16
HELIX 31 AD4 ASP B 66 MET B 73 1 8
HELIX 32 AD5 TYR B 74 ALA B 91 1 18
HELIX 33 AD6 GLU B 93 ARG B 112 1 20
HELIX 34 AD7 SER B 118 LEU B 138 1 21
HELIX 35 AD8 TYR B 189 ALA B 194 1 6
HELIX 36 AD9 TRP B 196 LYS B 203 1 8
HELIX 37 AE1 THR B 226 GLN B 242 1 17
HELIX 38 AE2 THR B 257 HIS B 269 1 13
HELIX 39 AE3 LYS B 270 LEU B 273 5 4
HELIX 40 AE4 HIS B 284 PHE B 287 5 4
HELIX 41 AE5 ASP B 288 ASN B 296 1 9
HELIX 42 AE6 ASP B 303 PHE B 312 1 10
HELIX 43 AE7 ASP B 316 SER B 324 1 9
HELIX 44 AE8 SER B 325 SER B 328 5 4
HELIX 45 AE9 GLY B 333 LYS B 337 5 5
HELIX 46 AF1 ILE B 355 GLU B 363 1 9
HELIX 47 AF2 PRO B 382 GLY B 397 1 16
HELIX 48 AF3 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 LEU A 343 N SER A 278
SHEET 8 AA116 LYS A 368 VAL A 373 1 O LEU A 369 N LEU A 344
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 VAL B 146 O VAL B 163
CISPEP 1 TYR A 39 PRO A 40 0 -0.27
CISPEP 2 GLU A 63 PRO A 64 0 -4.37
CISPEP 3 PHE A 113 PRO A 114 0 -1.89
CISPEP 4 GLU A 381 PRO A 382 0 0.03
CISPEP 5 TYR B 39 PRO B 40 0 -0.32
CISPEP 6 GLU B 63 PRO B 64 0 -3.39
CISPEP 7 PHE B 113 PRO B 114 0 -1.44
CISPEP 8 GLU B 381 PRO B 382 0 -0.51
CRYST1 85.800 88.850 123.050 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 0.011655 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011255 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008127 0.00000
TER 3331 ARG A 412
TER 6644 THR B 413
MASTER 389 0 4 48 16 0 0 6 7393 2 32 68
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