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HEADER LYASE 16-OCT-18 6HXA
TITLE ANTI FROM P. LUMINESCENS CATALYSES TERMINAL POLYKETIDE SHORTENING IN
TITLE 2 THE BIOSYNTHESIS OF ANTHRAQUINONES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ANTI;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PHOTORHABDUS LUMINESCENS;
SOURCE 3 ORGANISM_TAXID: 29488;
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: PCOLA
KEYWDS NATURAL PRODUCT BIOSYNTHESIS, TYPE II POLYKETIDE SYNTHASE SYSTEM,
KEYWDS 2 LYASE, ALPHA, BETA-HYDROLASE FOLD, CASCADE REACTION, RETRO CLAISEN
KEYWDS 3 REACTION, DIECKMANN CONDENSATION
EXPDTA X-RAY DIFFRACTION
AUTHOR Q.ZHOU,A.BRAEUER,G.GRAMMBITTER,M.SCHMALHOFER,P.SAURA,H.ADIHOU,
AUTHOR 2 V.R.I.KAILA,M.GROLL,H.BODE
REVDAT 1 07-AUG-19 6HXA 0
JRNL AUTH Q.ZHOU,A.BRAUER,H.ADIHOU,M.SCHMALHOFER,P.SAURA,
JRNL AUTH 2 G.L.C.GRAMMBITTER,V.R.I.KAILA,M.GROLL,H.B.BODE
JRNL TITL MOLECULAR MECHANISM OF POLYKETIDE SHORTENING IN
JRNL TITL 2 ANTHRAQUINONE BIOSYNTHESIS OFPHOTORHABDUS LUMINESCENS.
JRNL REF CHEM SCI V. 10 6341 2019
JRNL REFN ISSN 2041-6520
JRNL PMID 31341589
JRNL DOI 10.1039/C9SC00749K
REMARK 2
REMARK 2 RESOLUTION. 1.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0230
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 31340
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) : 0.170
REMARK 3 R VALUE (WORKING SET) : 0.168
REMARK 3 FREE R VALUE : 0.204
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1649
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) : 2295
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2890
REMARK 3 BIN FREE R VALUE SET COUNT : 120
REMARK 3 BIN FREE R VALUE : 0.2960
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 : 23
REMARK 3 SOLVENT ATOMS : 182
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 37.11
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.36000
REMARK 3 B22 (A**2) : -4.11000
REMARK 3 B33 (A**2) : 3.75000
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): 0.390
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.126
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.093
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.206
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.971
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.960
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3153 ; 0.003 ; 0.014
REMARK 3 BOND LENGTHS OTHERS (A): 2808 ; 0.001 ; 0.017
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4259 ; 0.789 ; 1.638
REMARK 3 BOND ANGLES OTHERS (DEGREES): 6568 ; 0.740 ; 1.647
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 376 ; 6.310 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 168 ;31.921 ;23.214
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 532 ;12.712 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 13 ;16.324 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 390 ; 0.039 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3512 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 644 ; 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): 1501 ; 1.039 ; 3.425
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1500 ; 1.037 ; 3.424
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1875 ; 1.495 ; 5.134
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1876 ; 1.494 ; 5.136
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1652 ; 1.043 ; 3.708
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1652 ; 1.043 ; 3.708
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 2384 ; 1.384 ; 5.455
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 3655 ; 2.325 ;39.954
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 3623 ; 2.246 ;39.701
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 5956 ; 0.352 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 85 ;31.382 ; 5.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 5976 ;18.333 ; 5.000
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): 13.0990 17.1772 94.0862
REMARK 3 T TENSOR
REMARK 3 T11: 0.0005 T22: 0.0400
REMARK 3 T33: 0.0195 T12: 0.0004
REMARK 3 T13: 0.0016 T23: -0.0003
REMARK 3 L TENSOR
REMARK 3 L11: 0.1063 L22: 0.0949
REMARK 3 L33: 0.0125 L12: 0.0423
REMARK 3 L13: 0.0011 L23: -0.0118
REMARK 3 S TENSOR
REMARK 3 S11: -0.0013 S12: -0.0016 S13: 0.0199
REMARK 3 S21: 0.0003 S22: 0.0017 S23: 0.0085
REMARK 3 S31: 0.0015 S32: 0.0058 S33: -0.0004
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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 6HXA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 16-OCT-18.
REMARK 100 THE DEPOSITION ID IS D_1200012442.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-JUN-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
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 : 33019
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.850
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 6.700
REMARK 200 R MERGE (I) : 0.05700
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 18.9000
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 (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.56000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: SHARP
REMARK 200 STARTING MODEL: SEMET DERIVATIVE; COORDINATES NOT DEPOSITED
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.08
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM HEPES, 0.1 M NAAC, 22% PEG
REMARK 280 3350, PH 7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 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 45.62000
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 45.62000
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 27.05500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 77.17000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 27.05500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 77.17000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 45.62000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 27.05500
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 77.17000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 45.62000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 27.05500
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 77.17000
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: 4510 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28100 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 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 182.48000
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 617 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 676 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 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 GLY A -4
REMARK 465 ASP A -3
REMARK 465 PRO A -2
REMARK 465 ALA 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: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 682 O HOH A 682 3656 1.82
REMARK 500 OH TYR A 20 CD GLU A 160 1455 2.12
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 PHE A 27 -128.51 48.48
REMARK 500 ASP A 143 -106.36 65.31
REMARK 500 ILE A 180 -87.92 -100.87
REMARK 500 SER A 245 -122.86 56.84
REMARK 500 VAL A 356 -0.10 81.08
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 ARG A 117 0.09 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 PGE A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PG4 A 402
DBREF 6HXA A 1 384 UNP Q7MZT8 Q7MZT8_PHOLL 1 384
SEQADV 6HXA GLY A -14 UNP Q7MZT8 EXPRESSION TAG
SEQADV 6HXA SER A -13 UNP Q7MZT8 EXPRESSION TAG
SEQADV 6HXA SER A -12 UNP Q7MZT8 EXPRESSION TAG
SEQADV 6HXA HIS A -11 UNP Q7MZT8 EXPRESSION TAG
SEQADV 6HXA HIS A -10 UNP Q7MZT8 EXPRESSION TAG
SEQADV 6HXA HIS A -9 UNP Q7MZT8 EXPRESSION TAG
SEQADV 6HXA HIS A -8 UNP Q7MZT8 EXPRESSION TAG
SEQADV 6HXA HIS A -7 UNP Q7MZT8 EXPRESSION TAG
SEQADV 6HXA HIS A -6 UNP Q7MZT8 EXPRESSION TAG
SEQADV 6HXA SER A -5 UNP Q7MZT8 EXPRESSION TAG
SEQADV 6HXA GLY A -4 UNP Q7MZT8 EXPRESSION TAG
SEQADV 6HXA ASP A -3 UNP Q7MZT8 EXPRESSION TAG
SEQADV 6HXA PRO A -2 UNP Q7MZT8 EXPRESSION TAG
SEQADV 6HXA ALA A -1 UNP Q7MZT8 EXPRESSION TAG
SEQADV 6HXA SER A 0 UNP Q7MZT8 EXPRESSION TAG
SEQRES 1 A 399 GLY SER SER HIS HIS HIS HIS HIS HIS SER GLY ASP PRO
SEQRES 2 A 399 ALA SER MET ASN ASN LYS ASN LYS PRO ASN ARG ILE SER
SEQRES 3 A 399 PRO GLU LEU LEU ALA THR CYS GLY TYR PHE MET PRO ARG
SEQRES 4 A 399 ILE PHE PHE LEU ASN SER GLN TYR ALA PRO GLN VAL HIS
SEQRES 5 A 399 TRP GLY ASP VAL VAL ALA ALA LEU SER HIS PHE PRO ALA
SEQRES 6 A 399 GLY ASN LEU ASP LEU SER SER GLU GLU PHE TRP TYR GLU
SEQRES 7 A 399 TRP MET ILE ASN TRP SER LYS VAL GLY ASP SER TYR ILE
SEQRES 8 A 399 ASN ILE ALA ASN SER ALA LYS SER GLU VAL SER HIS VAL
SEQRES 9 A 399 ARG ALA LEU ARG SER ALA ALA ALA CYS TYR HIS TRP ALA
SEQRES 10 A 399 GLU PHE MET TYR PHE SER ASP ARG SER ARG LYS ILE GLN
SEQRES 11 A 399 LEU ARG GLU TYR ILE ARG SER CYS PHE LEU SER SER ILE
SEQRES 12 A 399 LYS TYR SER ASP LEU LEU VAL ASP HIS GLN TYR ILE VAL
SEQRES 13 A 399 VAL ASP LYS PHE HIS MET PRO PHE PHE LEU ILE PHE PRO
SEQRES 14 A 399 LYS GLY TYR LYS GLU GLU GLU ASN HIS PRO LEU PRO CYS
SEQRES 15 A 399 VAL ILE LEU SER ASN GLY LEU ASP SER MET THR GLU ILE
SEQRES 16 A 399 GLU ILE LEU SER LEU ALA GLU PHE PHE LEU GLY LYS ASN
SEQRES 17 A 399 MET ALA VAL ALA ILE PHE ASP GLY PRO GLY GLN GLY ILE
SEQRES 18 A 399 ASN LEU GLY LYS SER PRO ILE ALA ILE ASP MET GLU LEU
SEQRES 19 A 399 TYR VAL SER SER ILE VAL LYS LEU LEU GLU ASP ASP ALA
SEQRES 20 A 399 ARG ILE ASN SER ASN LEU LEU CYS PHE LEU GLY ILE SER
SEQRES 21 A 399 PHE GLY GLY TYR PHE ALA LEU ARG VAL ALA GLN ARG ILE
SEQRES 22 A 399 GLY ASP LYS PHE CYS CYS ILE VAL ASN LEU SER GLY GLY
SEQRES 23 A 399 PRO GLU ILE ALA GLU PHE ASP LYS LEU PRO ARG ARG LEU
SEQRES 24 A 399 LYS GLU ASP PHE GLN PHE ALA PHE MET GLN ASP ASN SER
SEQRES 25 A 399 HIS MET GLN SER ILE PHE ASP GLU ILE LYS LEU ASP ILE
SEQRES 26 A 399 SER LEU PRO CYS LYS THR LYS VAL PHE THR VAL HIS GLY
SEQRES 27 A 399 GLU LEU ASP ASP ILE PHE GLN ILE ASP LYS VAL LYS LYS
SEQRES 28 A 399 LEU ASP GLN LEU TRP GLY ASP ASN HIS GLN LEU LEU CYS
SEQRES 29 A 399 TYR GLU SER GLU ALA HIS VAL CYS LEU ASN LYS ILE ASN
SEQRES 30 A 399 GLU TYR MET ILE GLN VAL SER ASP TRP VAL SER GLU GLN
SEQRES 31 A 399 PHE TRP LEU ASN GLY TYR LYS LYS GLY
HET PGE A 401 10
HET PG4 A 402 13
HETNAM PGE TRIETHYLENE GLYCOL
HETNAM PG4 TETRAETHYLENE GLYCOL
FORMUL 2 PGE C6 H14 O4
FORMUL 3 PG4 C8 H18 O5
FORMUL 4 HOH *182(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 TYR A 130 1 22
HELIX 7 AA7 ILE A 180 GLY A 191 1 12
HELIX 8 AA8 GLN A 204 LEU A 208 5 5
HELIX 9 AA9 MET A 217 ASP A 231 1 15
HELIX 10 AB1 SER A 245 GLY A 259 1 15
HELIX 11 AB2 ASP A 260 PHE A 262 5 3
HELIX 12 AB3 GLU A 276 LEU A 280 5 5
HELIX 13 AB4 PRO A 281 MET A 293 1 13
HELIX 14 AB5 ASP A 295 SER A 297 5 3
HELIX 15 AB6 HIS A 298 LYS A 307 1 10
HELIX 16 AB7 GLN A 330 GLY A 342 1 13
HELIX 17 AB8 ALA A 354 ASN A 359 5 6
HELIX 18 AB9 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 ASN A 235 N LEU A 165
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
SITE 1 AC1 3 TYR A 99 TYR A 119 HOH A 584
SITE 1 AC2 4 ALA A 82 SER A 84 TYR A 130 HOH A 614
CRYST1 54.110 154.340 91.240 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 0.018481 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006479 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010960 0.00000
TER 3049 TYR A 381
MASTER 383 0 2 18 8 0 2 6 3244 1 23 31
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