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HEADER LYASE 28-AUG-23 8QD3
TITLE AYG1P IN COMPLEX WITH 1,3,6,8-TETRAHYDROXYNAPHTHALENE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PIGMENT BIOSYNTHESIS PROTEIN YELLOWISH-GREEN 1;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ASPERGILLUS FUMIGATUS;
SOURCE 3 ORGANISM_TAXID: 746128;
SOURCE 4 GENE: AYG1;
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: PRSET A
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 8QD3 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. 1.70 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) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.48
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.9
REMARK 3 NUMBER OF REFLECTIONS : 164908
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) : 0.198
REMARK 3 R VALUE (WORKING SET) : 0.196
REMARK 3 FREE R VALUE : 0.221
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 8775
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.74
REMARK 3 REFLECTION IN BIN (WORKING SET) : 11047
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 85.87
REMARK 3 BIN R VALUE (WORKING SET) : 0.1980
REMARK 3 BIN FREE R VALUE SET COUNT : 611
REMARK 3 BIN FREE R VALUE : 0.2640
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 12386
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 204
REMARK 3 SOLVENT ATOMS : 1027
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.79
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -22.38000
REMARK 3 B22 (A**2) : 37.13000
REMARK 3 B33 (A**2) : -14.74000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 10.63000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.042
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.024
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.053
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.265
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.957
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.950
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 13091 ; 0.002 ; 0.013
REMARK 3 BOND LENGTHS OTHERS (A): 11824 ; 0.001 ; 0.015
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 17927 ; 1.194 ; 1.642
REMARK 3 BOND ANGLES OTHERS (DEGREES): 27239 ; 1.132 ; 1.574
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1624 ; 6.222 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 658 ;32.132 ;21.641
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1919 ;12.529 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 77 ;12.302 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1666 ; 0.049 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 15002 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 3024 ; 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): 6415 ; 1.032 ; 2.169
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 6414 ; 1.032 ; 2.168
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 8027 ; 1.392 ; 3.257
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 8028 ; 1.392 ; 3.257
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 6676 ; 0.928 ; 2.256
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 6677 ; 0.927 ; 2.256
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 9888 ; 1.213 ; 3.352
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 15447 ; 2.269 ;25.974
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 15448 ; 2.269 ;25.974
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 24913 ; 0.474 ; 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 : NULL
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 8QD3 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_1292132996.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-NOV-21
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
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 : 173708
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
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 (%) : 94.6
REMARK 200 DATA REDUNDANCY : 3.200
REMARK 200 R MERGE (I) : 0.09400
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 6.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.80
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.7
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.60000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.900
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 (%): 45.18
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.24
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM K/NA TARTRATE, 25.5% PEG 3350,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 53.72000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
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 ARG A -15
REMARK 465 GLY A -14
REMARK 465 SER A -13
REMARK 465 HIS 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 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 PRO A 2
REMARK 465 PRO A 401
REMARK 465 SER A 402
REMARK 465 LYS A 403
REMARK 465 THR A 404
REMARK 465 LYS A 405
REMARK 465 ASN A 406
REMARK 465 MET B -16
REMARK 465 ARG B -15
REMARK 465 GLY B -14
REMARK 465 SER B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 HIS B -10
REMARK 465 HIS B -9
REMARK 465 HIS B -8
REMARK 465 HIS 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 PRO B 2
REMARK 465 PRO B 401
REMARK 465 SER B 402
REMARK 465 LYS B 403
REMARK 465 THR B 404
REMARK 465 LYS B 405
REMARK 465 ASN B 406
REMARK 465 MET C -16
REMARK 465 ARG C -15
REMARK 465 GLY C -14
REMARK 465 SER C -13
REMARK 465 HIS C -12
REMARK 465 HIS C -11
REMARK 465 HIS C -10
REMARK 465 HIS C -9
REMARK 465 HIS C -8
REMARK 465 HIS C -7
REMARK 465 GLU C -6
REMARK 465 ASN C -5
REMARK 465 LEU C -4
REMARK 465 TYR C -3
REMARK 465 PHE C -2
REMARK 465 GLN C -1
REMARK 465 GLY C 0
REMARK 465 SER C 1
REMARK 465 PRO C 2
REMARK 465 PRO C 401
REMARK 465 SER C 402
REMARK 465 LYS C 403
REMARK 465 THR C 404
REMARK 465 LYS C 405
REMARK 465 ASN C 406
REMARK 465 MET D -16
REMARK 465 ARG D -15
REMARK 465 GLY D -14
REMARK 465 SER D -13
REMARK 465 HIS D -12
REMARK 465 HIS D -11
REMARK 465 HIS D -10
REMARK 465 HIS D -9
REMARK 465 HIS D -8
REMARK 465 HIS D -7
REMARK 465 GLU D -6
REMARK 465 ASN D -5
REMARK 465 LEU D -4
REMARK 465 TYR D -3
REMARK 465 PHE D -2
REMARK 465 GLN D -1
REMARK 465 GLY D 0
REMARK 465 SER D 1
REMARK 465 PRO D 2
REMARK 465 PRO D 401
REMARK 465 SER D 402
REMARK 465 LYS D 403
REMARK 465 THR D 404
REMARK 465 LYS D 405
REMARK 465 ASN D 406
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 ARG A 3 CG CD NE CZ NH1 NH2
REMARK 470 ASP A 8 CG OD1 OD2
REMARK 470 LYS A 57 CG CD CE NZ
REMARK 470 GLN A 87 CG CD OE1 NE2
REMARK 470 GLU A 92 CG CD OE1 OE2
REMARK 470 GLN A 242 CG CD OE1 NE2
REMARK 470 GLU A 291 CG CD OE1 OE2
REMARK 470 SER A 400 OG
REMARK 470 ARG B 3 CG CD NE CZ NH1 NH2
REMARK 470 ASP B 8 CG OD1 OD2
REMARK 470 LEU B 86 CG CD1 CD2
REMARK 470 GLN B 87 CG CD OE1 NE2
REMARK 470 GLU B 92 CG CD OE1 OE2
REMARK 470 LYS B 135 CG CD CE NZ
REMARK 470 LEU B 139 CG CD1 CD2
REMARK 470 GLN B 242 CG CD OE1 NE2
REMARK 470 GLU B 291 CG CD OE1 OE2
REMARK 470 LYS B 316 CG CD CE NZ
REMARK 470 GLU B 320 CG CD OE1 OE2
REMARK 470 ARG C 3 CG CD NE CZ NH1 NH2
REMARK 470 ASP C 8 CG OD1 OD2
REMARK 470 LYS C 57 CG CD CE NZ
REMARK 470 ASN C 58 CG OD1 ND2
REMARK 470 GLN C 87 CG CD OE1 NE2
REMARK 470 HIS C 91 CG ND1 CD2 CE1 NE2
REMARK 470 GLU C 92 CG CD OE1 OE2
REMARK 470 GLU C 93 CG CD OE1 OE2
REMARK 470 GLN C 131 CG CD OE1 NE2
REMARK 470 LEU C 139 CG CD1 CD2
REMARK 470 ARG C 145 CG CD NE CZ NH1 NH2
REMARK 470 GLN C 174 CG CD OE1 NE2
REMARK 470 ASN C 176 CG OD1 ND2
REMARK 470 GLN C 242 CG CD OE1 NE2
REMARK 470 LYS C 316 CG CD CE NZ
REMARK 470 LYS C 327 CG CD CE NZ
REMARK 470 SER C 400 OG
REMARK 470 ARG D 3 CG CD NE CZ NH1 NH2
REMARK 470 ASP D 8 CG OD1 OD2
REMARK 470 LYS D 34 CG CD CE NZ
REMARK 470 LYS D 57 CG CD CE NZ
REMARK 470 GLN D 87 CG CD OE1 NE2
REMARK 470 HIS D 91 CG ND1 CD2 CE1 NE2
REMARK 470 GLN D 174 CG CD OE1 NE2
REMARK 470 GLU D 291 CG CD OE1 OE2
REMARK 470 LYS D 316 CG CD CE NZ
REMARK 470 GLU D 319 CG CD OE1 OE2
REMARK 470 LYS D 327 CG CD CE NZ
REMARK 470 SER D 400 OG
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 27 -65.17 -131.61
REMARK 500 ASP A 41 -10.33 78.96
REMARK 500 TYR A 190 -168.73 -114.34
REMARK 500 ASN A 194 25.04 -141.90
REMARK 500 ALA A 217 -120.17 47.31
REMARK 500 SER A 257 -107.12 57.64
REMARK 500 CYS A 284 -10.05 -152.50
REMARK 500 HIS A 285 -73.52 -160.44
REMARK 500 HIS A 299 -152.82 -106.62
REMARK 500 ASP A 338 52.29 -93.56
REMARK 500 ASP A 351 34.96 -93.30
REMARK 500 MET A 381 -30.57 87.14
REMARK 500 ARG B 27 -65.24 -122.29
REMARK 500 ARG B 27 -66.67 -121.31
REMARK 500 ASP B 41 -1.97 80.35
REMARK 500 LYS B 90 77.87 -109.44
REMARK 500 TYR B 190 -168.15 -115.14
REMARK 500 ALA B 217 -118.63 45.99
REMARK 500 SER B 257 -112.62 57.36
REMARK 500 CYS B 284 -13.17 -152.55
REMARK 500 HIS B 285 -68.91 -157.76
REMARK 500 HIS B 299 -148.82 -112.63
REMARK 500 ASP B 338 50.60 -91.36
REMARK 500 ASP B 351 37.31 -94.50
REMARK 500 PRO B 379 -166.54 -78.85
REMARK 500 MET B 381 -22.43 88.68
REMARK 500 ARG C 27 -68.12 -141.53
REMARK 500 ASP C 41 -2.01 84.27
REMARK 500 THR C 185 -169.68 -79.65
REMARK 500 ASN C 194 27.12 -141.27
REMARK 500 ALA C 217 -119.18 44.78
REMARK 500 SER C 257 -106.86 59.48
REMARK 500 CYS C 284 -4.66 -155.62
REMARK 500 HIS C 285 -70.67 -162.22
REMARK 500 HIS C 299 -150.37 -108.00
REMARK 500 ASP C 351 40.40 -97.27
REMARK 500 HIS C 380 126.77 -36.72
REMARK 500 MET C 381 -22.96 84.23
REMARK 500 ASP D 11 36.89 -91.71
REMARK 500 ARG D 27 -66.96 -128.92
REMARK 500 ARG D 27 -66.57 -130.60
REMARK 500 ASP D 41 -7.64 86.40
REMARK 500 TYR D 190 -168.08 -116.45
REMARK 500 ASN D 194 32.02 -140.38
REMARK 500 ALA D 217 -124.16 48.06
REMARK 500 SER D 257 -112.86 55.75
REMARK 500 CYS D 284 -14.30 -152.12
REMARK 500 HIS D 285 -70.75 -159.69
REMARK 500 HIS D 299 -152.80 -105.75
REMARK 500 ASP D 338 54.70 -90.36
REMARK 500
REMARK 500 THIS ENTRY HAS 52 RAMACHANDRAN OUTLIERS.
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 8QD3 A 2 406 UNP Q9UVV1 Q9UVV1_ASPFM 2 406
DBREF 8QD3 B 2 406 UNP Q9UVV1 Q9UVV1_ASPFM 2 406
DBREF 8QD3 C 2 406 UNP Q9UVV1 Q9UVV1_ASPFM 2 406
DBREF 8QD3 D 2 406 UNP Q9UVV1 Q9UVV1_ASPFM 2 406
SEQADV 8QD3 MET A -16 UNP Q9UVV1 INITIATING METHIONINE
SEQADV 8QD3 ARG A -15 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD3 GLY A -14 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD3 SER A -13 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD3 HIS A -12 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD3 HIS A -11 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD3 HIS A -10 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD3 HIS A -9 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD3 HIS A -8 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD3 HIS A -7 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD3 GLU A -6 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD3 ASN A -5 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD3 LEU A -4 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD3 TYR A -3 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD3 PHE A -2 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD3 GLN A -1 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD3 GLY A 0 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD3 SER A 1 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD3 MET B -16 UNP Q9UVV1 INITIATING METHIONINE
SEQADV 8QD3 ARG B -15 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD3 GLY B -14 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD3 SER B -13 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD3 HIS B -12 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD3 HIS B -11 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD3 HIS B -10 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD3 HIS B -9 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD3 HIS B -8 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD3 HIS B -7 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD3 GLU B -6 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD3 ASN B -5 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD3 LEU B -4 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD3 TYR B -3 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD3 PHE B -2 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD3 GLN B -1 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD3 GLY B 0 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD3 SER B 1 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD3 MET C -16 UNP Q9UVV1 INITIATING METHIONINE
SEQADV 8QD3 ARG C -15 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD3 GLY C -14 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD3 SER C -13 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD3 HIS C -12 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD3 HIS C -11 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD3 HIS C -10 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD3 HIS C -9 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD3 HIS C -8 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD3 HIS C -7 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD3 GLU C -6 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD3 ASN C -5 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD3 LEU C -4 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD3 TYR C -3 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD3 PHE C -2 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD3 GLN C -1 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD3 GLY C 0 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD3 SER C 1 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD3 MET D -16 UNP Q9UVV1 INITIATING METHIONINE
SEQADV 8QD3 ARG D -15 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD3 GLY D -14 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD3 SER D -13 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD3 HIS D -12 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD3 HIS D -11 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD3 HIS D -10 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD3 HIS D -9 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD3 HIS D -8 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD3 HIS D -7 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD3 GLU D -6 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD3 ASN D -5 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD3 LEU D -4 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD3 TYR D -3 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD3 PHE D -2 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD3 GLN D -1 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD3 GLY D 0 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD3 SER D 1 UNP Q9UVV1 EXPRESSION TAG
SEQRES 1 A 423 MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLU ASN LEU
SEQRES 2 A 423 TYR PHE GLN GLY SER PRO ARG TRP ILE LEU GLY ASP LYS
SEQRES 3 A 423 PHE ASP THR VAL PHE PRO HIS LYS GLY SER LEU LYS VAL
SEQRES 4 A 423 LEU TRP GLU SER ARG TRP LYS PHE ALA CYS SER LYS SER
SEQRES 5 A 423 VAL TYR PRO PHE HIS ASP GLY SER ILE GLU ASP PHE GLU
SEQRES 6 A 423 PRO ILE PHE ASN HIS LEU ILE SER LYS ASN ILE ASN ASP
SEQRES 7 A 423 ALA ALA SER ASP GLU TYR THR GLN ALA PHE LEU PRO THR
SEQRES 8 A 423 ALA SER ALA LEU GLU GLU LYS ALA ALA GLN ALA LEU GLN
SEQRES 9 A 423 ALA GLY LYS HIS GLU GLU ALA SER ASN LEU LEU CYS ARG
SEQRES 10 A 423 ALA ALA VAL VAL TYR ARG ILE SER ARG PHE PRO TYR VAL
SEQRES 11 A 423 ASP ILE THR LYS PRO ASN SER ILE LYS ARG VAL ALA PHE
SEQRES 12 A 423 GLU ARG GLN LYS GLN ALA TYR LEU LYS ALA THR SER LEU
SEQRES 13 A 423 TRP THR GLN PRO ILE ARG GLU VAL THR VAL PRO HIS THR
SEQRES 14 A 423 TYR ARG THR GLY ASN ASP GLY ALA HIS ILE PRO ILE TYR
SEQRES 15 A 423 ILE ARG THR PRO ALA GLY ALA ASP GLN SER ASN PRO VAL
SEQRES 16 A 423 PRO ILE VAL LEU ILE MET THR GLY LEU ASP GLY TYR ARG
SEQRES 17 A 423 PRO ASP ASN SER GLN ARG THR HIS GLU ILE LEU ALA ARG
SEQRES 18 A 423 GLY TRP ALA ALA VAL VAL ALA GLU ILE PRO GLY THR ALA
SEQRES 19 A 423 ASP CYS PRO ALA ASP PRO ALA ASP PRO ALA SER PRO ASP
SEQRES 20 A 423 ARG LEU TRP ASP SER VAL LEU SER TYR LEU ASP GLN ARG
SEQRES 21 A 423 PRO GLU LEU ASN THR ALA LYS MET VAL VAL TRP GLY LEU
SEQRES 22 A 423 SER ALA GLY GLY TYR TYR ALA ILE ARG ALA ALA HIS THR
SEQRES 23 A 423 HIS ARG ASP ARG LEU LEU GLY ALA ILE ALA HIS GLY PRO
SEQRES 24 A 423 GLY CYS HIS TYR TYR LEU ASP PRO GLU TRP LEU ALA LYS
SEQRES 25 A 423 VAL ASN ASP HIS GLU TYR PRO PHE GLU ILE THR ALA ALA
SEQRES 26 A 423 TRP ALA THR LYS HIS GLY TYR LYS THR VAL GLU GLU PHE
SEQRES 27 A 423 VAL ALA GLY ALA GLN LYS LYS PHE SER LEU VAL GLU THR
SEQRES 28 A 423 GLY ILE VAL ASP GLN PRO SER CYS ARG LEU LEU LEU LEU
SEQRES 29 A 423 ASN GLY VAL ASP ASP GLY VAL VAL PRO ILE GLU ASP CYS
SEQRES 30 A 423 LEU VAL LEU PHE GLU HIS GLY SER PRO LYS GLU GLY ARG
SEQRES 31 A 423 PHE TYR LYS GLY LEU PRO HIS MET GLY TYR PRO ASN SER
SEQRES 32 A 423 LEU PRO VAL SER TYR GLU TRP LEU GLU GLN VAL LEU ALA
SEQRES 33 A 423 SER PRO SER LYS THR LYS ASN
SEQRES 1 B 423 MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLU ASN LEU
SEQRES 2 B 423 TYR PHE GLN GLY SER PRO ARG TRP ILE LEU GLY ASP LYS
SEQRES 3 B 423 PHE ASP THR VAL PHE PRO HIS LYS GLY SER LEU LYS VAL
SEQRES 4 B 423 LEU TRP GLU SER ARG TRP LYS PHE ALA CYS SER LYS SER
SEQRES 5 B 423 VAL TYR PRO PHE HIS ASP GLY SER ILE GLU ASP PHE GLU
SEQRES 6 B 423 PRO ILE PHE ASN HIS LEU ILE SER LYS ASN ILE ASN ASP
SEQRES 7 B 423 ALA ALA SER ASP GLU TYR THR GLN ALA PHE LEU PRO THR
SEQRES 8 B 423 ALA SER ALA LEU GLU GLU LYS ALA ALA GLN ALA LEU GLN
SEQRES 9 B 423 ALA GLY LYS HIS GLU GLU ALA SER ASN LEU LEU CYS ARG
SEQRES 10 B 423 ALA ALA VAL VAL TYR ARG ILE SER ARG PHE PRO TYR VAL
SEQRES 11 B 423 ASP ILE THR LYS PRO ASN SER ILE LYS ARG VAL ALA PHE
SEQRES 12 B 423 GLU ARG GLN LYS GLN ALA TYR LEU LYS ALA THR SER LEU
SEQRES 13 B 423 TRP THR GLN PRO ILE ARG GLU VAL THR VAL PRO HIS THR
SEQRES 14 B 423 TYR ARG THR GLY ASN ASP GLY ALA HIS ILE PRO ILE TYR
SEQRES 15 B 423 ILE ARG THR PRO ALA GLY ALA ASP GLN SER ASN PRO VAL
SEQRES 16 B 423 PRO ILE VAL LEU ILE MET THR GLY LEU ASP GLY TYR ARG
SEQRES 17 B 423 PRO ASP ASN SER GLN ARG THR HIS GLU ILE LEU ALA ARG
SEQRES 18 B 423 GLY TRP ALA ALA VAL VAL ALA GLU ILE PRO GLY THR ALA
SEQRES 19 B 423 ASP CYS PRO ALA ASP PRO ALA ASP PRO ALA SER PRO ASP
SEQRES 20 B 423 ARG LEU TRP ASP SER VAL LEU SER TYR LEU ASP GLN ARG
SEQRES 21 B 423 PRO GLU LEU ASN THR ALA LYS MET VAL VAL TRP GLY LEU
SEQRES 22 B 423 SER ALA GLY GLY TYR TYR ALA ILE ARG ALA ALA HIS THR
SEQRES 23 B 423 HIS ARG ASP ARG LEU LEU GLY ALA ILE ALA HIS GLY PRO
SEQRES 24 B 423 GLY CYS HIS TYR TYR LEU ASP PRO GLU TRP LEU ALA LYS
SEQRES 25 B 423 VAL ASN ASP HIS GLU TYR PRO PHE GLU ILE THR ALA ALA
SEQRES 26 B 423 TRP ALA THR LYS HIS GLY TYR LYS THR VAL GLU GLU PHE
SEQRES 27 B 423 VAL ALA GLY ALA GLN LYS LYS PHE SER LEU VAL GLU THR
SEQRES 28 B 423 GLY ILE VAL ASP GLN PRO SER CYS ARG LEU LEU LEU LEU
SEQRES 29 B 423 ASN GLY VAL ASP ASP GLY VAL VAL PRO ILE GLU ASP CYS
SEQRES 30 B 423 LEU VAL LEU PHE GLU HIS GLY SER PRO LYS GLU GLY ARG
SEQRES 31 B 423 PHE TYR LYS GLY LEU PRO HIS MET GLY TYR PRO ASN SER
SEQRES 32 B 423 LEU PRO VAL SER TYR GLU TRP LEU GLU GLN VAL LEU ALA
SEQRES 33 B 423 SER PRO SER LYS THR LYS ASN
SEQRES 1 C 423 MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLU ASN LEU
SEQRES 2 C 423 TYR PHE GLN GLY SER PRO ARG TRP ILE LEU GLY ASP LYS
SEQRES 3 C 423 PHE ASP THR VAL PHE PRO HIS LYS GLY SER LEU LYS VAL
SEQRES 4 C 423 LEU TRP GLU SER ARG TRP LYS PHE ALA CYS SER LYS SER
SEQRES 5 C 423 VAL TYR PRO PHE HIS ASP GLY SER ILE GLU ASP PHE GLU
SEQRES 6 C 423 PRO ILE PHE ASN HIS LEU ILE SER LYS ASN ILE ASN ASP
SEQRES 7 C 423 ALA ALA SER ASP GLU TYR THR GLN ALA PHE LEU PRO THR
SEQRES 8 C 423 ALA SER ALA LEU GLU GLU LYS ALA ALA GLN ALA LEU GLN
SEQRES 9 C 423 ALA GLY LYS HIS GLU GLU ALA SER ASN LEU LEU CYS ARG
SEQRES 10 C 423 ALA ALA VAL VAL TYR ARG ILE SER ARG PHE PRO TYR VAL
SEQRES 11 C 423 ASP ILE THR LYS PRO ASN SER ILE LYS ARG VAL ALA PHE
SEQRES 12 C 423 GLU ARG GLN LYS GLN ALA TYR LEU LYS ALA THR SER LEU
SEQRES 13 C 423 TRP THR GLN PRO ILE ARG GLU VAL THR VAL PRO HIS THR
SEQRES 14 C 423 TYR ARG THR GLY ASN ASP GLY ALA HIS ILE PRO ILE TYR
SEQRES 15 C 423 ILE ARG THR PRO ALA GLY ALA ASP GLN SER ASN PRO VAL
SEQRES 16 C 423 PRO ILE VAL LEU ILE MET THR GLY LEU ASP GLY TYR ARG
SEQRES 17 C 423 PRO ASP ASN SER GLN ARG THR HIS GLU ILE LEU ALA ARG
SEQRES 18 C 423 GLY TRP ALA ALA VAL VAL ALA GLU ILE PRO GLY THR ALA
SEQRES 19 C 423 ASP CYS PRO ALA ASP PRO ALA ASP PRO ALA SER PRO ASP
SEQRES 20 C 423 ARG LEU TRP ASP SER VAL LEU SER TYR LEU ASP GLN ARG
SEQRES 21 C 423 PRO GLU LEU ASN THR ALA LYS MET VAL VAL TRP GLY LEU
SEQRES 22 C 423 SER ALA GLY GLY TYR TYR ALA ILE ARG ALA ALA HIS THR
SEQRES 23 C 423 HIS ARG ASP ARG LEU LEU GLY ALA ILE ALA HIS GLY PRO
SEQRES 24 C 423 GLY CYS HIS TYR TYR LEU ASP PRO GLU TRP LEU ALA LYS
SEQRES 25 C 423 VAL ASN ASP HIS GLU TYR PRO PHE GLU ILE THR ALA ALA
SEQRES 26 C 423 TRP ALA THR LYS HIS GLY TYR LYS THR VAL GLU GLU PHE
SEQRES 27 C 423 VAL ALA GLY ALA GLN LYS LYS PHE SER LEU VAL GLU THR
SEQRES 28 C 423 GLY ILE VAL ASP GLN PRO SER CYS ARG LEU LEU LEU LEU
SEQRES 29 C 423 ASN GLY VAL ASP ASP GLY VAL VAL PRO ILE GLU ASP CYS
SEQRES 30 C 423 LEU VAL LEU PHE GLU HIS GLY SER PRO LYS GLU GLY ARG
SEQRES 31 C 423 PHE TYR LYS GLY LEU PRO HIS MET GLY TYR PRO ASN SER
SEQRES 32 C 423 LEU PRO VAL SER TYR GLU TRP LEU GLU GLN VAL LEU ALA
SEQRES 33 C 423 SER PRO SER LYS THR LYS ASN
SEQRES 1 D 423 MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLU ASN LEU
SEQRES 2 D 423 TYR PHE GLN GLY SER PRO ARG TRP ILE LEU GLY ASP LYS
SEQRES 3 D 423 PHE ASP THR VAL PHE PRO HIS LYS GLY SER LEU LYS VAL
SEQRES 4 D 423 LEU TRP GLU SER ARG TRP LYS PHE ALA CYS SER LYS SER
SEQRES 5 D 423 VAL TYR PRO PHE HIS ASP GLY SER ILE GLU ASP PHE GLU
SEQRES 6 D 423 PRO ILE PHE ASN HIS LEU ILE SER LYS ASN ILE ASN ASP
SEQRES 7 D 423 ALA ALA SER ASP GLU TYR THR GLN ALA PHE LEU PRO THR
SEQRES 8 D 423 ALA SER ALA LEU GLU GLU LYS ALA ALA GLN ALA LEU GLN
SEQRES 9 D 423 ALA GLY LYS HIS GLU GLU ALA SER ASN LEU LEU CYS ARG
SEQRES 10 D 423 ALA ALA VAL VAL TYR ARG ILE SER ARG PHE PRO TYR VAL
SEQRES 11 D 423 ASP ILE THR LYS PRO ASN SER ILE LYS ARG VAL ALA PHE
SEQRES 12 D 423 GLU ARG GLN LYS GLN ALA TYR LEU LYS ALA THR SER LEU
SEQRES 13 D 423 TRP THR GLN PRO ILE ARG GLU VAL THR VAL PRO HIS THR
SEQRES 14 D 423 TYR ARG THR GLY ASN ASP GLY ALA HIS ILE PRO ILE TYR
SEQRES 15 D 423 ILE ARG THR PRO ALA GLY ALA ASP GLN SER ASN PRO VAL
SEQRES 16 D 423 PRO ILE VAL LEU ILE MET THR GLY LEU ASP GLY TYR ARG
SEQRES 17 D 423 PRO ASP ASN SER GLN ARG THR HIS GLU ILE LEU ALA ARG
SEQRES 18 D 423 GLY TRP ALA ALA VAL VAL ALA GLU ILE PRO GLY THR ALA
SEQRES 19 D 423 ASP CYS PRO ALA ASP PRO ALA ASP PRO ALA SER PRO ASP
SEQRES 20 D 423 ARG LEU TRP ASP SER VAL LEU SER TYR LEU ASP GLN ARG
SEQRES 21 D 423 PRO GLU LEU ASN THR ALA LYS MET VAL VAL TRP GLY LEU
SEQRES 22 D 423 SER ALA GLY GLY TYR TYR ALA ILE ARG ALA ALA HIS THR
SEQRES 23 D 423 HIS ARG ASP ARG LEU LEU GLY ALA ILE ALA HIS GLY PRO
SEQRES 24 D 423 GLY CYS HIS TYR TYR LEU ASP PRO GLU TRP LEU ALA LYS
SEQRES 25 D 423 VAL ASN ASP HIS GLU TYR PRO PHE GLU ILE THR ALA ALA
SEQRES 26 D 423 TRP ALA THR LYS HIS GLY TYR LYS THR VAL GLU GLU PHE
SEQRES 27 D 423 VAL ALA GLY ALA GLN LYS LYS PHE SER LEU VAL GLU THR
SEQRES 28 D 423 GLY ILE VAL ASP GLN PRO SER CYS ARG LEU LEU LEU LEU
SEQRES 29 D 423 ASN GLY VAL ASP ASP GLY VAL VAL PRO ILE GLU ASP CYS
SEQRES 30 D 423 LEU VAL LEU PHE GLU HIS GLY SER PRO LYS GLU GLY ARG
SEQRES 31 D 423 PHE TYR LYS GLY LEU PRO HIS MET GLY TYR PRO ASN SER
SEQRES 32 D 423 LEU PRO VAL SER TYR GLU TRP LEU GLU GLN VAL LEU ALA
SEQRES 33 D 423 SER PRO SER LYS THR LYS ASN
HET QW8 A1001 14
HET PGE A1002 10
HET FLV A1003 15
HET FLV A1004 15
HET QW8 B1001 14
HET EDO B1002 4
HET FLV B1003 15
HET FLV B1004 15
HET QW8 C1001 14
HET PGE C1002 10
HET EDO C1003 4
HET FLV C1004 15
HET FLV C1005 15
HET QW8 D1001 14
HET FLV D1002 15
HET FLV D1003 15
HETNAM QW8 NAPHTHALENE-1,3,6,8-TETROL
HETNAM PGE TRIETHYLENE GLYCOL
HETNAM FLV FLAVIOLIN
HETNAM EDO 1,2-ETHANEDIOL
HETSYN QW8 1,3,6,8-TETRAHYDROXYNAPHTHALENE
HETSYN FLV 2,5,7-TRIHYDROXYNAPHTHOQUINONE
HETSYN EDO ETHYLENE GLYCOL
FORMUL 5 QW8 4(C10 H8 O4)
FORMUL 6 PGE 2(C6 H14 O4)
FORMUL 7 FLV 8(C10 H6 O5)
FORMUL 10 EDO 2(C2 H6 O2)
FORMUL 21 HOH *1027(H2 O)
HELIX 1 AA1 LEU A 6 THR A 12 5 7
HELIX 2 AA2 SER A 19 ARG A 27 1 9
HELIX 3 AA3 ARG A 27 LYS A 34 1 8
HELIX 4 AA4 SER A 43 LYS A 57 1 15
HELIX 5 AA5 SER A 64 GLN A 69 1 6
HELIX 6 AA6 PHE A 71 ALA A 88 1 18
HELIX 7 AA7 LYS A 90 ARG A 109 1 20
HELIX 8 AA8 SER A 120 SER A 138 1 19
HELIX 9 AA9 ASN A 194 ARG A 204 1 11
HELIX 10 AB1 ALA A 227 ARG A 243 1 17
HELIX 11 AB2 ALA A 258 HIS A 270 1 13
HELIX 12 AB3 ARG A 271 LEU A 274 5 4
HELIX 13 AB4 HIS A 285 LEU A 288 5 4
HELIX 14 AB5 ASP A 289 ALA A 294 1 6
HELIX 15 AB6 LYS A 295 HIS A 299 5 5
HELIX 16 AB7 ILE A 305 HIS A 313 1 9
HELIX 17 AB8 THR A 317 SER A 330 1 14
HELIX 18 AB9 ILE A 357 VAL A 362 1 6
HELIX 19 AC1 LEU A 363 HIS A 366 5 4
HELIX 20 AC2 ASN A 385 LEU A 398 1 14
HELIX 21 AC3 LEU B 6 THR B 12 5 7
HELIX 22 AC4 SER B 19 ARG B 27 1 9
HELIX 23 AC5 ARG B 27 SER B 35 1 9
HELIX 24 AC6 SER B 43 LYS B 57 1 15
HELIX 25 AC7 SER B 64 ALA B 70 1 7
HELIX 26 AC8 PHE B 71 ALA B 88 1 18
HELIX 27 AC9 LYS B 90 ARG B 109 1 20
HELIX 28 AD1 SER B 120 SER B 138 1 19
HELIX 29 AD2 ASN B 194 ARG B 204 1 11
HELIX 30 AD3 ALA B 227 ARG B 243 1 17
HELIX 31 AD4 ALA B 258 HIS B 270 1 13
HELIX 32 AD5 ARG B 271 LEU B 274 5 4
HELIX 33 AD6 HIS B 285 LEU B 288 5 4
HELIX 34 AD7 ASP B 289 ALA B 294 1 6
HELIX 35 AD8 LYS B 295 HIS B 299 5 5
HELIX 36 AD9 ILE B 305 HIS B 313 1 9
HELIX 37 AE1 THR B 317 SER B 330 1 14
HELIX 38 AE2 ILE B 357 VAL B 362 1 6
HELIX 39 AE3 LEU B 363 HIS B 366 5 4
HELIX 40 AE4 ASN B 385 LEU B 398 1 14
HELIX 41 AE5 LEU C 6 THR C 12 5 7
HELIX 42 AE6 SER C 19 ARG C 27 1 9
HELIX 43 AE7 ARG C 27 LYS C 34 1 8
HELIX 44 AE8 SER C 43 ASN C 58 1 16
HELIX 45 AE9 SER C 64 GLN C 69 1 6
HELIX 46 AF1 PHE C 71 ALA C 88 1 18
HELIX 47 AF2 LYS C 90 ARG C 109 1 20
HELIX 48 AF3 SER C 120 SER C 138 1 19
HELIX 49 AF4 TYR C 190 ASP C 193 5 4
HELIX 50 AF5 ASN C 194 ARG C 204 1 11
HELIX 51 AF6 ALA C 227 ARG C 243 1 17
HELIX 52 AF7 ALA C 258 HIS C 270 1 13
HELIX 53 AF8 ARG C 271 LEU C 274 5 4
HELIX 54 AF9 HIS C 285 LEU C 288 5 4
HELIX 55 AG1 ASP C 289 VAL C 296 1 8
HELIX 56 AG2 ASN C 297 HIS C 299 5 3
HELIX 57 AG3 ILE C 305 HIS C 313 1 9
HELIX 58 AG4 THR C 317 SER C 330 1 14
HELIX 59 AG5 GLY C 335 GLN C 339 5 5
HELIX 60 AG6 ILE C 357 VAL C 362 1 6
HELIX 61 AG7 LEU C 363 HIS C 366 5 4
HELIX 62 AG8 LEU C 387 LEU C 398 1 12
HELIX 63 AG9 LEU D 6 THR D 12 5 7
HELIX 64 AH1 SER D 19 ARG D 27 1 9
HELIX 65 AH2 ARG D 27 LYS D 34 1 8
HELIX 66 AH3 SER D 43 LYS D 57 1 15
HELIX 67 AH4 SER D 64 ALA D 70 1 7
HELIX 68 AH5 PHE D 71 ALA D 88 1 18
HELIX 69 AH6 LYS D 90 ARG D 109 1 20
HELIX 70 AH7 SER D 120 LEU D 139 1 20
HELIX 71 AH8 ASN D 194 ARG D 204 1 11
HELIX 72 AH9 ALA D 227 ARG D 243 1 17
HELIX 73 AI1 GLY D 259 HIS D 270 1 12
HELIX 74 AI2 ARG D 271 LEU D 274 5 4
HELIX 75 AI3 HIS D 285 LEU D 288 5 4
HELIX 76 AI4 ASP D 289 ALA D 294 1 6
HELIX 77 AI5 LYS D 295 HIS D 299 5 5
HELIX 78 AI6 ILE D 305 HIS D 313 1 9
HELIX 79 AI7 THR D 317 SER D 330 1 14
HELIX 80 AI8 ILE D 357 VAL D 362 1 6
HELIX 81 AI9 LEU D 363 HIS D 366 5 4
HELIX 82 AJ1 ASN D 385 LEU D 398 1 14
SHEET 1 AA116 ARG A 145 PRO A 150 0
SHEET 2 AA116 HIS A 161 ARG A 167 -1 O ILE A 166 N ARG A 145
SHEET 3 AA116 ALA A 207 ALA A 211 -1 O ALA A 208 N ARG A 167
SHEET 4 AA116 VAL A 178 MET A 184 1 N ILE A 183 O VAL A 209
SHEET 5 AA116 LEU A 246 LEU A 256 1 O LEU A 256 N MET A 184
SHEET 6 AA116 GLY A 276 HIS A 280 1 O ILE A 278 N GLY A 255
SHEET 7 AA116 ARG A 343 GLY A 349 1 O LEU A 345 N ALA A 279
SHEET 8 AA116 LYS A 370 TYR A 375 1 O GLU A 371 N LEU A 344
SHEET 9 AA116 LYS B 370 TYR B 375 -1 O LYS B 370 N GLY A 372
SHEET 10 AA116 ARG B 343 GLY B 349 1 N LEU B 344 O GLU B 371
SHEET 11 AA116 GLY B 276 HIS B 280 1 N ALA B 279 O LEU B 345
SHEET 12 AA116 LEU B 246 LEU B 256 1 N GLY B 255 O HIS B 280
SHEET 13 AA116 VAL B 178 MET B 184 1 N VAL B 178 O ASN B 247
SHEET 14 AA116 ALA B 207 ALA B 211 1 O VAL B 209 N ILE B 183
SHEET 15 AA116 HIS B 161 ARG B 167 -1 N ARG B 167 O ALA B 208
SHEET 16 AA116 ARG B 145 PRO B 150 -1 N ARG B 145 O ILE B 166
SHEET 1 AA2 8 ARG C 145 PRO C 150 0
SHEET 2 AA2 8 HIS C 161 ARG C 167 -1 O ILE C 164 N VAL C 147
SHEET 3 AA2 8 ALA C 207 ALA C 211 -1 O ALA C 208 N ARG C 167
SHEET 4 AA2 8 VAL C 178 MET C 184 1 N ILE C 183 O VAL C 209
SHEET 5 AA2 8 LEU C 246 LEU C 256 1 O ASN C 247 N VAL C 178
SHEET 6 AA2 8 GLY C 276 HIS C 280 1 O ILE C 278 N GLY C 255
SHEET 7 AA2 8 ARG C 343 GLY C 349 1 O LEU C 345 N ALA C 277
SHEET 8 AA2 8 GLU C 371 TYR C 375 1 O GLU C 371 N LEU C 346
SHEET 1 AA3 8 ARG D 145 PRO D 150 0
SHEET 2 AA3 8 HIS D 161 ARG D 167 -1 O ILE D 166 N ARG D 145
SHEET 3 AA3 8 ALA D 207 ALA D 211 -1 O VAL D 210 N TYR D 165
SHEET 4 AA3 8 VAL D 178 MET D 184 1 N ILE D 183 O VAL D 209
SHEET 5 AA3 8 LEU D 246 LEU D 256 1 O ASN D 247 N VAL D 178
SHEET 6 AA3 8 GLY D 276 HIS D 280 1 O ILE D 278 N GLY D 255
SHEET 7 AA3 8 ARG D 343 GLY D 349 1 O LEU D 345 N ALA D 279
SHEET 8 AA3 8 GLU D 371 TYR D 375 1 O GLU D 371 N LEU D 344
CISPEP 1 TYR A 37 PRO A 38 0 1.17
CISPEP 2 PHE A 110 PRO A 111 0 -3.26
CISPEP 3 TYR A 383 PRO A 384 0 -5.36
CISPEP 4 TYR B 37 PRO B 38 0 0.59
CISPEP 5 PHE B 110 PRO B 111 0 -4.88
CISPEP 6 TYR B 383 PRO B 384 0 -2.31
CISPEP 7 TYR C 37 PRO C 38 0 1.23
CISPEP 8 PHE C 110 PRO C 111 0 -2.37
CISPEP 9 TYR C 383 PRO C 384 0 -8.03
CISPEP 10 TYR D 37 PRO D 38 0 -0.12
CISPEP 11 PHE D 110 PRO D 111 0 -2.52
CISPEP 12 TYR D 383 PRO D 384 0 -2.37
CRYST1 85.480 107.440 92.720 90.00 90.16 90.00 P 1 21 1 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 0.011699 0.000000 0.000032 0.00000
SCALE2 0.000000 0.009308 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010785 0.00000
TER 3139 SER A 400
TER 6269 SER B 400
TER 9368 SER C 400
TER 12491 SER D 400
MASTER 482 0 16 82 32 0 0 613617 4 204 132
END |