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HEADER LYASE 24-AUG-23 8QBH
TITLE ANTI IN COMPLEX WITH 1-NAPHTHOL
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: PLASMID;
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 8QBH 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. 2.05 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) : 2.05
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.68
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.8
REMARK 3 NUMBER OF REFLECTIONS : 23215
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) : 0.192
REMARK 3 R VALUE (WORKING SET) : 0.192
REMARK 3 FREE R VALUE : 0.207
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1221
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) : 2.05
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.10
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1693
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.27
REMARK 3 BIN R VALUE (WORKING SET) : 0.2150
REMARK 3 BIN FREE R VALUE SET COUNT : 89
REMARK 3 BIN FREE R VALUE : 0.2450
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2993
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 11
REMARK 3 SOLVENT ATOMS : 98
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 51.63
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 36.38000
REMARK 3 B22 (A**2) : -18.83000
REMARK 3 B33 (A**2) : -17.56000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.034
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.104
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.246
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.964
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.963
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3098 ; 0.002 ; 0.013
REMARK 3 BOND LENGTHS OTHERS (A): 2818 ; 0.001 ; 0.016
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4210 ; 1.140 ; 1.620
REMARK 3 BOND ANGLES OTHERS (DEGREES): 6473 ; 1.070 ; 1.571
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 382 ; 5.480 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 159 ;28.724 ;23.208
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 495 ;12.262 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 12 ;14.282 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 394 ; 0.037 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3551 ; 0.002 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 759 ; 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): 1513 ; 0.910 ; 3.857
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1512 ; 0.910 ; 3.857
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1891 ; 1.322 ; 5.785
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1892 ; 1.322 ; 5.786
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1585 ; 0.766 ; 3.951
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1586 ; 0.765 ; 3.952
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 2317 ; 1.088 ; 5.897
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 3519 ; 2.106 ;44.980
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 3520 ; 2.105 ;44.978
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 5912 ; 0.224 ; 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 5 A 381
REMARK 3 ORIGIN FOR THE GROUP (A): 12.9955 17.0662 95.0640
REMARK 3 T TENSOR
REMARK 3 T11: 0.0978 T22: 0.0092
REMARK 3 T33: 0.0521 T12: -0.0261
REMARK 3 T13: 0.0487 T23: -0.0181
REMARK 3 L TENSOR
REMARK 3 L11: 1.1684 L22: 2.1031
REMARK 3 L33: 2.8038 L12: 0.2407
REMARK 3 L13: -0.2629 L23: -0.3009
REMARK 3 S TENSOR
REMARK 3 S11: 0.0983 S12: -0.0360 S13: 0.1950
REMARK 3 S21: -0.0622 S22: 0.0164 S23: -0.0466
REMARK 3 S31: -0.4398 S32: 0.0792 S33: -0.1147
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 8QBH 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_1292132984.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-AUG-21
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.9
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 : 24440
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.050
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 (%) : 95.8
REMARK 200 DATA REDUNDANCY : 4.500
REMARK 200 R MERGE (I) : 0.04500
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 17.2900
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.05
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.15
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.66900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.800
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 (%): 43.18
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.16
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM HEPES PH 7.9, 0.1 M NAAC PH
REMARK 280 6.6, 24% PEG 3350, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 293K
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 46.04500
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 46.04500
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 27.97000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 77.36500
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 27.97000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 77.36500
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 46.04500
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 27.97000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 77.36500
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 46.04500
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 27.97000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 77.36500
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: 3970 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26730 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 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 184.18000
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 536 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 598 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 LYS A 382
REMARK 465 LYS A 383
REMARK 465 GLY A 384
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 5 CG OD1 ND2
REMARK 470 LYS A 6 CG CD CE NZ
REMARK 470 ARG A 9 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 144 CG CD CE NZ
REMARK 470 LYS A 155 CG CD CE NZ
REMARK 470 LYS A 158 CG CD CE NZ
REMARK 470 GLU A 160 CG CD OE1 OE2
REMARK 470 GLU A 161 CG CD OE1 OE2
REMARK 470 HIS A 163 CG ND1 CD2 CE1 NE2
REMARK 470 LYS A 226 CG CD CE NZ
REMARK 470 LYS A 261 CG CD CE NZ
REMARK 470 ASP A 278 CG OD1 OD2
REMARK 470 LYS A 279 CG CD CE NZ
REMARK 470 ASP A 309 CG OD1 OD2
REMARK 470 LYS A 336 CG CD CE NZ
REMARK 470 ASP A 343 CG OD1 OD2
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 -128.46 46.71
REMARK 500 ASP A 143 -106.33 63.57
REMARK 500 ILE A 180 -87.84 -107.68
REMARK 500 LYS A 210 -62.11 -91.71
REMARK 500 ASP A 216 59.52 -90.64
REMARK 500 SER A 245 -117.17 59.34
REMARK 500 PRO A 281 152.65 -47.57
REMARK 500 ILE A 328 -65.17 -104.03
REMARK 500 VAL A 356 -4.04 81.06
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 8QBH A 1 384 UNP Q7MZT8 Q7MZT8_PHOLL 1 384
SEQADV 8QBH MET A -15 UNP Q7MZT8 INITIATING METHIONINE
SEQADV 8QBH GLY A -14 UNP Q7MZT8 EXPRESSION TAG
SEQADV 8QBH SER A -13 UNP Q7MZT8 EXPRESSION TAG
SEQADV 8QBH SER A -12 UNP Q7MZT8 EXPRESSION TAG
SEQADV 8QBH HIS A -11 UNP Q7MZT8 EXPRESSION TAG
SEQADV 8QBH HIS A -10 UNP Q7MZT8 EXPRESSION TAG
SEQADV 8QBH HIS A -9 UNP Q7MZT8 EXPRESSION TAG
SEQADV 8QBH HIS A -8 UNP Q7MZT8 EXPRESSION TAG
SEQADV 8QBH HIS A -7 UNP Q7MZT8 EXPRESSION TAG
SEQADV 8QBH HIS A -6 UNP Q7MZT8 EXPRESSION TAG
SEQADV 8QBH SER A -5 UNP Q7MZT8 EXPRESSION TAG
SEQADV 8QBH GLN A -4 UNP Q7MZT8 EXPRESSION TAG
SEQADV 8QBH ASP A -3 UNP Q7MZT8 EXPRESSION TAG
SEQADV 8QBH PRO A -2 UNP Q7MZT8 EXPRESSION TAG
SEQADV 8QBH ASN A -1 UNP Q7MZT8 EXPRESSION TAG
SEQADV 8QBH 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 1NP A 401 11
HETNAM 1NP 1-NAPHTHOL
HETSYN 1NP NAPHTHALEN-1-OL
FORMUL 2 1NP C10 H8 O
FORMUL 3 HOH *98(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 SER A 81 1 25
HELIX 5 AA5 SER A 84 PHE A 104 1 21
HELIX 6 AA6 ASP A 109 ILE A 128 1 20
HELIX 7 AA7 LYS A 129 SER A 131 5 3
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 PRO A 281 MET A 293 1 13
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 PHE A 145 N VAL A 142
SHEET 3 AA1 8 ALA A 195 PHE A 199 -1 O VAL A 196 N ILE A 152
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 LEU A 242 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 55.940 154.730 92.090 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 0.017876 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006463 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010859 0.00000
TER 3003 TYR A 381
MASTER 369 0 1 19 8 0 0 6 3102 1 11 31
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