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HEADER LYASE 24-AUG-23 8QBI
TITLE ANTI IN CLOSED STATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHOTORHABDUS LUMINESCENS SUBSP. LAUMONDII TTO1 COMPLETE
COMPND 3 GENOME SEGMENT 15/17;
COMPND 4 CHAIN: A;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PHOTORHABDUS LAUMONDII SUBSP. LAUMONDII TTO1;
SOURCE 3 ORGANISM_TAXID: 243265;
SOURCE 4 GENE: PLU4186;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMIDE;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PCOLADUET
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 8QBI 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. 1.55 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) : 1.55
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.82
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 3 NUMBER OF REFLECTIONS : 53121
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) : 0.162
REMARK 3 R VALUE (WORKING SET) : 0.161
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 : 2796
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) : 1.55
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.59
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3891
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.81
REMARK 3 BIN R VALUE (WORKING SET) : 0.2330
REMARK 3 BIN FREE R VALUE SET COUNT : 205
REMARK 3 BIN FREE R VALUE : 0.2640
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3039
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 21
REMARK 3 SOLVENT ATOMS : 334
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.08
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.43000
REMARK 3 B22 (A**2) : -3.03000
REMARK 3 B33 (A**2) : 5.46000
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): 0.021
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.015
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.037
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.187
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.975
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.973
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3139 ; 0.003 ; 0.013
REMARK 3 BOND LENGTHS OTHERS (A): 2911 ; 0.001 ; 0.016
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4239 ; 1.161 ; 1.623
REMARK 3 BOND ANGLES OTHERS (DEGREES): 6710 ; 1.185 ; 1.574
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 374 ; 6.448 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 167 ;32.192 ;23.234
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 531 ;12.665 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 13 ;18.488 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 389 ; 0.053 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3539 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 755 ; 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): 1500 ; 0.746 ; 1.986
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1498 ; 0.744 ; 1.985
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1872 ; 0.978 ; 2.984
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1873 ; 0.978 ; 2.985
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1639 ; 0.796 ; 2.166
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1640 ; 0.795 ; 2.167
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 2368 ; 1.030 ; 3.183
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 3710 ; 1.714 ;25.157
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 3711 ; 1.714 ;25.166
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 6047 ; 0.477 ; 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 : 1
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 7 A 381
REMARK 3 ORIGIN FOR THE GROUP (A): 13.2440 17.2432 94.2025
REMARK 3 T TENSOR
REMARK 3 T11: 0.0131 T22: 0.0037
REMARK 3 T33: 0.0626 T12: -0.0052
REMARK 3 T13: -0.0050 T23: -0.0071
REMARK 3 L TENSOR
REMARK 3 L11: 0.9300 L22: 1.1872
REMARK 3 L33: 1.3887 L12: 0.1190
REMARK 3 L13: -0.2608 L23: -0.1711
REMARK 3 S TENSOR
REMARK 3 S11: -0.0214 S12: -0.0055 S13: 0.1247
REMARK 3 S21: -0.0174 S22: 0.0283 S23: -0.0254
REMARK 3 S31: -0.1195 S32: 0.0497 S33: -0.0069
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 8QBI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 24-AUG-23.
REMARK 100 THE DEPOSITION ID IS D_1292132986.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-JUL-21
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0-8.0
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 : 55924
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.550
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 (%) : 99.1
REMARK 200 DATA REDUNDANCY : 4.500
REMARK 200 R MERGE (I) : 0.02900
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 22.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.55
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.65
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.56500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.400
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 (%): 41.26
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.09
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM HEPES, 0.1 M NAAC PH 6.6, 22%
REMARK 280 PEG 3350, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 292K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
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 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
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
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 45.68000
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 45.68000
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 27.27000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 77.37000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 27.27000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 77.37000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 45.68000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 27.27000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 77.37000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 45.68000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 27.27000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 77.37000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5000 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 27790 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 KCAL/MOL
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 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 182.72000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 604 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 828 LIES ON A SPECIAL POSITION.
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 -15
REMARK 465 GLY A -14
REMARK 465 SER A -13
REMARK 465 SER A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 HIS A -9
REMARK 465 HIS A -8
REMARK 465 HIS A -7
REMARK 465 HIS A -6
REMARK 465 SER A -5
REMARK 465 GLN A -4
REMARK 465 ASP A -3
REMARK 465 PRO A -2
REMARK 465 ASN A -1
REMARK 465 SER A 0
REMARK 465 MET A 1
REMARK 465 ASN A 2
REMARK 465 ASN A 3
REMARK 465 LYS A 4
REMARK 465 ASN A 5
REMARK 465 LYS A 6
REMARK 465 LYS A 382
REMARK 465 LYS A 383
REMARK 465 GLY A 384
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 PHE A 27 -130.31 44.12
REMARK 500 ASP A 143 -106.04 64.74
REMARK 500 ILE A 180 -90.20 -104.83
REMARK 500 SER A 245 -122.57 58.94
REMARK 500 ARG A 282 -132.68 57.14
REMARK 500 VAL A 356 -0.92 79.40
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 8QBI A 1 384 UNP Q7MZT8 Q7MZT8_PHOLL 1 384
SEQADV 8QBI MET A -15 UNP Q7MZT8 INITIATING METHIONINE
SEQADV 8QBI GLY A -14 UNP Q7MZT8 EXPRESSION TAG
SEQADV 8QBI SER A -13 UNP Q7MZT8 EXPRESSION TAG
SEQADV 8QBI SER A -12 UNP Q7MZT8 EXPRESSION TAG
SEQADV 8QBI HIS A -11 UNP Q7MZT8 EXPRESSION TAG
SEQADV 8QBI HIS A -10 UNP Q7MZT8 EXPRESSION TAG
SEQADV 8QBI HIS A -9 UNP Q7MZT8 EXPRESSION TAG
SEQADV 8QBI HIS A -8 UNP Q7MZT8 EXPRESSION TAG
SEQADV 8QBI HIS A -7 UNP Q7MZT8 EXPRESSION TAG
SEQADV 8QBI HIS A -6 UNP Q7MZT8 EXPRESSION TAG
SEQADV 8QBI SER A -5 UNP Q7MZT8 EXPRESSION TAG
SEQADV 8QBI GLN A -4 UNP Q7MZT8 EXPRESSION TAG
SEQADV 8QBI ASP A -3 UNP Q7MZT8 EXPRESSION TAG
SEQADV 8QBI PRO A -2 UNP Q7MZT8 EXPRESSION TAG
SEQADV 8QBI ASN A -1 UNP Q7MZT8 EXPRESSION TAG
SEQADV 8QBI SER A 0 UNP Q7MZT8 EXPRESSION TAG
SEQRES 1 A 400 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER GLN ASP
SEQRES 2 A 400 PRO ASN SER MET ASN ASN LYS ASN LYS PRO ASN ARG ILE
SEQRES 3 A 400 SER PRO GLU LEU LEU ALA THR CYS GLY TYR PHE MET PRO
SEQRES 4 A 400 ARG ILE PHE PHE LEU ASN SER GLN TYR ALA PRO GLN VAL
SEQRES 5 A 400 HIS TRP GLY ASP VAL VAL ALA ALA LEU SER HIS PHE PRO
SEQRES 6 A 400 ALA GLY ASN LEU ASP LEU SER SER GLU GLU PHE TRP TYR
SEQRES 7 A 400 GLU TRP MET ILE ASN TRP SER LYS VAL GLY ASP SER TYR
SEQRES 8 A 400 ILE ASN ILE ALA ASN SER ALA LYS SER GLU VAL SER HIS
SEQRES 9 A 400 VAL ARG ALA LEU ARG SER ALA ALA ALA CYS TYR HIS TRP
SEQRES 10 A 400 ALA GLU PHE MET TYR PHE SER ASP ARG SER ARG LYS ILE
SEQRES 11 A 400 GLN LEU ARG GLU TYR ILE ARG SER CYS PHE LEU SER SER
SEQRES 12 A 400 ILE LYS TYR SER ASP LEU LEU VAL ASP HIS GLN TYR ILE
SEQRES 13 A 400 VAL VAL ASP LYS PHE HIS MET PRO PHE PHE LEU ILE PHE
SEQRES 14 A 400 PRO LYS GLY TYR LYS GLU GLU GLU ASN HIS PRO LEU PRO
SEQRES 15 A 400 CYS VAL ILE LEU SER ASN GLY LEU ASP SER MET THR GLU
SEQRES 16 A 400 ILE GLU ILE LEU SER LEU ALA GLU PHE PHE LEU GLY LYS
SEQRES 17 A 400 ASN MET ALA VAL ALA ILE PHE ASP GLY PRO GLY GLN GLY
SEQRES 18 A 400 ILE ASN LEU GLY LYS SER PRO ILE ALA ILE ASP MET GLU
SEQRES 19 A 400 LEU TYR VAL SER SER ILE VAL LYS LEU LEU GLU ASP ASP
SEQRES 20 A 400 ALA ARG ILE ASN SER ASN LEU LEU CYS PHE LEU GLY ILE
SEQRES 21 A 400 SER PHE GLY GLY TYR PHE ALA LEU ARG VAL ALA GLN ARG
SEQRES 22 A 400 ILE GLY ASP LYS PHE CYS CYS ILE VAL ASN LEU SER GLY
SEQRES 23 A 400 GLY PRO GLU ILE ALA GLU PHE ASP LYS LEU PRO ARG ARG
SEQRES 24 A 400 LEU LYS GLU ASP PHE GLN PHE ALA PHE MET GLN ASP ASN
SEQRES 25 A 400 SER HIS MET GLN SER ILE PHE ASP GLU ILE LYS LEU ASP
SEQRES 26 A 400 ILE SER LEU PRO CYS LYS THR LYS VAL PHE THR VAL HIS
SEQRES 27 A 400 GLY GLU LEU ASP ASP ILE PHE GLN ILE ASP LYS VAL LYS
SEQRES 28 A 400 LYS LEU ASP GLN LEU TRP GLY ASP ASN HIS GLN LEU LEU
SEQRES 29 A 400 CYS TYR GLU SER GLU ALA HIS VAL CYS LEU ASN LYS ILE
SEQRES 30 A 400 ASN GLU TYR MET ILE GLN VAL SER ASP TRP VAL SER GLU
SEQRES 31 A 400 GLN PHE TRP LEU ASN GLY TYR LYS LYS GLY
HET ACT A 401 4
HET EDO A 402 4
HET PG4 A 403 13
HETNAM ACT ACETATE ION
HETNAM EDO 1,2-ETHANEDIOL
HETNAM PG4 TETRAETHYLENE GLYCOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 ACT C2 H3 O2 1-
FORMUL 3 EDO C2 H6 O2
FORMUL 4 PG4 C8 H18 O5
FORMUL 5 HOH *334(H2 O)
HELIX 1 AA1 SER A 11 CYS A 18 1 8
HELIX 2 AA2 PHE A 21 PHE A 27 1 7
HELIX 3 AA3 HIS A 37 SER A 46 1 10
HELIX 4 AA4 SER A 57 ALA A 82 1 26
HELIX 5 AA5 SER A 84 PHE A 104 1 21
HELIX 6 AA6 ASP A 109 LYS A 129 1 21
HELIX 7 AA7 LYS A 158 ASN A 162 5 5
HELIX 8 AA8 ILE A 180 GLY A 191 1 12
HELIX 9 AA9 GLN A 204 LEU A 208 5 5
HELIX 10 AB1 MET A 217 ASP A 231 1 15
HELIX 11 AB2 SER A 245 ILE A 258 1 14
HELIX 12 AB3 GLY A 259 PHE A 262 5 4
HELIX 13 AB4 GLU A 276 LEU A 280 5 5
HELIX 14 AB5 ARG A 283 MET A 293 1 11
HELIX 15 AB6 ASP A 295 SER A 297 5 3
HELIX 16 AB7 HIS A 298 LYS A 307 1 10
HELIX 17 AB8 GLN A 330 GLY A 342 1 13
HELIX 18 AB9 ALA A 354 ASN A 359 5 6
HELIX 19 AC1 LYS A 360 ASN A 379 1 20
SHEET 1 AA1 8 VAL A 135 VAL A 142 0
SHEET 2 AA1 8 PHE A 145 ILE A 152 -1 O LEU A 151 N ASP A 136
SHEET 3 AA1 8 ALA A 195 PHE A 199 -1 O ILE A 198 N PHE A 150
SHEET 4 AA1 8 LEU A 165 SER A 171 1 N VAL A 168 O ALA A 197
SHEET 5 AA1 8 ILE A 234 ILE A 244 1 O CYS A 240 N ILE A 169
SHEET 6 AA1 8 CYS A 264 LEU A 268 1 O LEU A 268 N GLY A 243
SHEET 7 AA1 8 LYS A 317 GLY A 323 1 O PHE A 319 N ASN A 267
SHEET 8 AA1 8 HIS A 345 TYR A 350 1 O LEU A 348 N THR A 320
CRYST1 54.540 154.740 91.360 90.00 90.00 90.00 C 2 2 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 0.018335 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006462 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010946 0.00000
TER 3040 TYR A 381
MASTER 345 0 3 19 8 0 0 6 3394 1 21 31
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