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HEADER LYASE 28-AUG-23 8QD1
TITLE AYG1P FROM A. FUMIGATUS CATALYZES POLYKETIDE SHORTENING IN THE
TITLE 2 BIOSYNTHESIS OF DHN-MELANIN
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 8QD1 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) : 46.71
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.1
REMARK 3 NUMBER OF REFLECTIONS : 170348
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) : 0.168
REMARK 3 R VALUE (WORKING SET) : 0.166
REMARK 3 FREE R VALUE : 0.199
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 8937
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) : 12404
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.91
REMARK 3 BIN R VALUE (WORKING SET) : 0.1910
REMARK 3 BIN FREE R VALUE SET COUNT : 645
REMARK 3 BIN FREE R VALUE : 0.2720
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 12383
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 1743
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.76
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -12.10000
REMARK 3 B22 (A**2) : 32.10000
REMARK 3 B33 (A**2) : -20.00000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.91000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.036
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.021
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.057
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.610
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.969
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.962
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 12880 ; 0.003 ; 0.013
REMARK 3 BOND LENGTHS OTHERS (A): 11768 ; 0.001 ; 0.015
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 17621 ; 1.217 ; 1.642
REMARK 3 BOND ANGLES OTHERS (DEGREES): 27116 ; 1.183 ; 1.574
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1620 ; 6.272 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 649 ;32.873 ;21.772
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1925 ;12.201 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 77 ;11.885 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1664 ; 0.054 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 14738 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 2988 ; 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): 6414 ; 0.912 ; 1.762
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 6413 ; 0.912 ; 1.761
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 8026 ; 1.242 ; 2.646
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 8027 ; 1.241 ; 2.646
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 6466 ; 0.840 ; 1.874
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 6467 ; 0.840 ; 1.874
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 9585 ; 1.109 ; 2.771
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 15387 ; 2.190 ;22.514
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 14913 ; 1.943 ;21.675
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 24648 ; 0.466 ; 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 : 4
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 3 A 399
REMARK 3 ORIGIN FOR THE GROUP (A): 8.555 23.976 1.709
REMARK 3 T TENSOR
REMARK 3 T11: 0.0325 T22: 0.0171
REMARK 3 T33: 0.0300 T12: -0.0103
REMARK 3 T13: -0.0131 T23: 0.0006
REMARK 3 L TENSOR
REMARK 3 L11: 0.7133 L22: 0.3399
REMARK 3 L33: 1.1278 L12: -0.0741
REMARK 3 L13: 0.2169 L23: -0.0590
REMARK 3 S TENSOR
REMARK 3 S11: 0.0196 S12: -0.0777 S13: 0.0306
REMARK 3 S21: 0.0245 S22: -0.0441 S23: -0.0138
REMARK 3 S31: 0.0126 S32: -0.0275 S33: 0.0244
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 3 B 399
REMARK 3 ORIGIN FOR THE GROUP (A): -15.324 23.826 -37.665
REMARK 3 T TENSOR
REMARK 3 T11: 0.0353 T22: 0.0074
REMARK 3 T33: 0.0314 T12: 0.0031
REMARK 3 T13: -0.0081 T23: 0.0028
REMARK 3 L TENSOR
REMARK 3 L11: 0.7580 L22: 0.2347
REMARK 3 L33: 1.0430 L12: 0.0616
REMARK 3 L13: 0.1111 L23: 0.0506
REMARK 3 S TENSOR
REMARK 3 S11: -0.0011 S12: 0.0653 S13: 0.0402
REMARK 3 S21: -0.0118 S22: -0.0101 S23: -0.0115
REMARK 3 S31: -0.0061 S32: -0.0164 S33: 0.0111
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 3 C 399
REMARK 3 ORIGIN FOR THE GROUP (A): -34.176 26.923 8.375
REMARK 3 T TENSOR
REMARK 3 T11: 0.0378 T22: 0.0393
REMARK 3 T33: 0.0398 T12: 0.0081
REMARK 3 T13: 0.0066 T23: -0.0033
REMARK 3 L TENSOR
REMARK 3 L11: 0.6811 L22: 0.2074
REMARK 3 L33: 1.3369 L12: 0.0237
REMARK 3 L13: -0.1355 L23: -0.1322
REMARK 3 S TENSOR
REMARK 3 S11: 0.0063 S12: 0.0732 S13: -0.0340
REMARK 3 S21: -0.0298 S22: -0.0261 S23: -0.0056
REMARK 3 S31: -0.0108 S32: 0.0427 S33: 0.0199
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 3 D 399
REMARK 3 ORIGIN FOR THE GROUP (A): 27.814 26.964 -44.248
REMARK 3 T TENSOR
REMARK 3 T11: 0.0299 T22: 0.0080
REMARK 3 T33: 0.0316 T12: -0.0058
REMARK 3 T13: 0.0003 T23: 0.0041
REMARK 3 L TENSOR
REMARK 3 L11: 0.7427 L22: 0.3082
REMARK 3 L33: 0.9972 L12: -0.0298
REMARK 3 L13: -0.0877 L23: 0.0361
REMARK 3 S TENSOR
REMARK 3 S11: 0.0274 S12: -0.0393 S13: -0.0270
REMARK 3 S21: 0.0255 S22: -0.0406 S23: -0.0039
REMARK 3 S31: 0.0051 S32: 0.0090 S33: 0.0132
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 8QD1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 28-AUG-23.
REMARK 100 THE DEPOSITION ID IS D_1292132994.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-SEP-20
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 : 179315
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 (%) : 97.2
REMARK 200 DATA REDUNDANCY : 3.100
REMARK 200 R MERGE (I) : 0.06500
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 9.6000
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 (%) : 97.9
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.52400
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: SAD
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.44
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.25
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100-200 MM K/NA TARTRATE, 15-26% PEG
REMARK 280 3350, 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 54.24000
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 GLU A 92 CG CD OE1 OE2
REMARK 470 GLN A 131 CG CD OE1 NE2
REMARK 470 LYS A 135 CG CD CE NZ
REMARK 470 GLN A 242 CG CD OE1 NE2
REMARK 470 GLU A 319 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 GLU B 66 CG CD OE1 OE2
REMARK 470 GLN B 87 CG CD OE1 NE2
REMARK 470 HIS B 91 CG ND1 CD2 CE1 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 ARG C 3 CG CD NE CZ NH1 NH2
REMARK 470 ASP C 8 CG OD1 OD2
REMARK 470 ARG C 27 CG CD NE CZ NH1 NH2
REMARK 470 SER C 56 OG
REMARK 470 LYS C 57 CG CD CE NZ
REMARK 470 ASN C 58 CG OD1 ND2
REMARK 470 LEU C 86 CG CD1 CD2
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 LEU C 139 CG CD1 CD2
REMARK 470 ARG C 145 CG CD NE CZ NH1 NH2
REMARK 470 ASP C 173 CG OD1 OD2
REMARK 470 GLN C 174 CG CD OE1 NE2
REMARK 470 SER C 175 OG
REMARK 470 ASN C 176 CG OD1 ND2
REMARK 470 GLN C 242 CG CD OE1 NE2
REMARK 470 ASP C 272 CG OD1 OD2
REMARK 470 LYS C 316 CG CD CE NZ
REMARK 470 GLU C 319 CG CD OE1 OE2
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 GLN D 87 CG CD OE1 NE2
REMARK 470 HIS D 91 CG ND1 CD2 CE1 NE2
REMARK 470 GLU D 92 CG CD OE1 OE2
REMARK 470 GLN D 131 CG CD OE1 NE2
REMARK 470 ASP D 272 CG OD1 OD2
REMARK 470 LYS D 316 CG CD CE NZ
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 -62.46 -141.20
REMARK 500 ARG A 27 -62.21 -143.75
REMARK 500 TYR A 190 -167.85 -118.50
REMARK 500 ALA A 217 -119.99 46.15
REMARK 500 SER A 257 -112.74 57.84
REMARK 500 CYS A 284 -14.65 -149.99
REMARK 500 HIS A 285 -68.92 -155.55
REMARK 500 HIS A 299 -151.18 -105.19
REMARK 500 ASP A 338 34.90 -90.85
REMARK 500 ASP A 351 35.73 -95.70
REMARK 500 MET A 381 -19.19 87.32
REMARK 500 ASP B 11 42.73 -91.39
REMARK 500 ARG B 27 -66.00 -139.08
REMARK 500 ARG B 27 -65.40 -140.53
REMARK 500 ASP B 41 -2.21 80.65
REMARK 500 TYR B 190 -168.50 -118.06
REMARK 500 ALA B 217 -120.43 47.98
REMARK 500 SER B 257 -113.34 56.40
REMARK 500 HIS B 268 -60.67 -90.63
REMARK 500 CYS B 284 -11.25 -151.23
REMARK 500 HIS B 285 -71.04 -160.02
REMARK 500 HIS B 299 -149.76 -109.13
REMARK 500 ASP B 351 38.78 -94.63
REMARK 500 MET B 381 -24.84 87.84
REMARK 500 ASP C 11 51.59 -90.76
REMARK 500 ARG C 27 -63.78 -134.05
REMARK 500 ASP C 41 -0.09 78.91
REMARK 500 ASN C 194 26.28 -140.81
REMARK 500 ALA C 217 -120.38 46.18
REMARK 500 SER C 257 -112.08 60.76
REMARK 500 CYS C 284 -12.35 -153.02
REMARK 500 HIS C 285 -70.67 -159.39
REMARK 500 HIS C 299 -149.65 -107.92
REMARK 500 ASP C 351 36.45 -96.50
REMARK 500 MET C 381 -20.07 87.36
REMARK 500 ASP D 11 52.36 -90.75
REMARK 500 ARG D 27 -63.70 -141.66
REMARK 500 ARG D 27 -63.87 -142.06
REMARK 500 ASP D 41 -0.68 80.48
REMARK 500 TYR D 190 -168.69 -120.65
REMARK 500 ALA D 217 -119.37 48.58
REMARK 500 SER D 257 -111.33 60.62
REMARK 500 CYS D 284 -9.60 -145.84
REMARK 500 HIS D 285 -72.51 -157.33
REMARK 500 HIS D 299 -148.21 -107.56
REMARK 500 ASP D 351 36.74 -97.35
REMARK 500 MET D 381 -25.11 89.96
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH B 957 DISTANCE = 5.85 ANGSTROMS
REMARK 525 HOH B 958 DISTANCE = 6.02 ANGSTROMS
REMARK 525 HOH B 959 DISTANCE = 6.30 ANGSTROMS
REMARK 525 HOH B 960 DISTANCE = 6.46 ANGSTROMS
REMARK 525 HOH C 892 DISTANCE = 5.89 ANGSTROMS
REMARK 525 HOH C 893 DISTANCE = 6.03 ANGSTROMS
REMARK 525 HOH C 894 DISTANCE = 6.38 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6HXA RELATED DB: PDB
REMARK 900 ANTI FROM P. LUMINESCENS CATALYSES TERMINAL POLYKETIDE SHORTENING
REMARK 900 IN THE BIOSYNTHESIS OF ANTHRAQUINONES
DBREF 8QD1 A 2 406 UNP Q9UVV1 Q9UVV1_ASPFM 2 406
DBREF 8QD1 B 2 406 UNP Q9UVV1 Q9UVV1_ASPFM 2 406
DBREF 8QD1 C 2 406 UNP Q9UVV1 Q9UVV1_ASPFM 2 406
DBREF 8QD1 D 2 406 UNP Q9UVV1 Q9UVV1_ASPFM 2 406
SEQADV 8QD1 MET A -16 UNP Q9UVV1 INITIATING METHIONINE
SEQADV 8QD1 ARG A -15 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD1 GLY A -14 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD1 SER A -13 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD1 HIS A -12 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD1 HIS A -11 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD1 HIS A -10 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD1 HIS A -9 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD1 HIS A -8 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD1 HIS A -7 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD1 GLU A -6 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD1 ASN A -5 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD1 LEU A -4 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD1 TYR A -3 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD1 PHE A -2 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD1 GLN A -1 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD1 GLY A 0 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD1 SER A 1 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD1 MET B -16 UNP Q9UVV1 INITIATING METHIONINE
SEQADV 8QD1 ARG B -15 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD1 GLY B -14 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD1 SER B -13 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD1 HIS B -12 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD1 HIS B -11 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD1 HIS B -10 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD1 HIS B -9 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD1 HIS B -8 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD1 HIS B -7 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD1 GLU B -6 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD1 ASN B -5 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD1 LEU B -4 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD1 TYR B -3 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD1 PHE B -2 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD1 GLN B -1 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD1 GLY B 0 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD1 SER B 1 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD1 MET C -16 UNP Q9UVV1 INITIATING METHIONINE
SEQADV 8QD1 ARG C -15 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD1 GLY C -14 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD1 SER C -13 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD1 HIS C -12 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD1 HIS C -11 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD1 HIS C -10 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD1 HIS C -9 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD1 HIS C -8 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD1 HIS C -7 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD1 GLU C -6 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD1 ASN C -5 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD1 LEU C -4 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD1 TYR C -3 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD1 PHE C -2 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD1 GLN C -1 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD1 GLY C 0 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD1 SER C 1 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD1 MET D -16 UNP Q9UVV1 INITIATING METHIONINE
SEQADV 8QD1 ARG D -15 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD1 GLY D -14 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD1 SER D -13 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD1 HIS D -12 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD1 HIS D -11 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD1 HIS D -10 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD1 HIS D -9 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD1 HIS D -8 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD1 HIS D -7 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD1 GLU D -6 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD1 ASN D -5 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD1 LEU D -4 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD1 TYR D -3 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD1 PHE D -2 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD1 GLN D -1 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD1 GLY D 0 UNP Q9UVV1 EXPRESSION TAG
SEQADV 8QD1 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
FORMUL 5 HOH *1743(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 ALA A 70 1 7
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 TYR A 190 ASP A 193 5 4
HELIX 10 AB1 ASN A 194 ARG A 204 1 11
HELIX 11 AB2 ALA A 227 ARG A 243 1 17
HELIX 12 AB3 ALA A 258 HIS A 270 1 13
HELIX 13 AB4 ARG A 271 LEU A 274 5 4
HELIX 14 AB5 HIS A 285 LEU A 288 5 4
HELIX 15 AB6 ASP A 289 ALA A 294 1 6
HELIX 16 AB7 LYS A 295 HIS A 299 5 5
HELIX 17 AB8 ILE A 305 HIS A 313 1 9
HELIX 18 AB9 THR A 317 SER A 330 1 14
HELIX 19 AC1 ILE A 357 VAL A 362 1 6
HELIX 20 AC2 LEU A 363 HIS A 366 5 4
HELIX 21 AC3 ASN A 385 LEU A 398 1 14
HELIX 22 AC4 LEU B 6 THR B 12 5 7
HELIX 23 AC5 SER B 19 ARG B 27 1 9
HELIX 24 AC6 ARG B 27 LYS B 34 1 8
HELIX 25 AC7 SER B 43 LYS B 57 1 15
HELIX 26 AC8 SER B 64 ALA B 70 1 7
HELIX 27 AC9 PHE B 71 ALA B 88 1 18
HELIX 28 AD1 LYS B 90 ARG B 109 1 20
HELIX 29 AD2 SER B 120 SER B 138 1 19
HELIX 30 AD3 TYR B 190 ASP B 193 5 4
HELIX 31 AD4 ASN B 194 ARG B 204 1 11
HELIX 32 AD5 ALA B 227 GLN B 242 1 16
HELIX 33 AD6 ALA B 258 HIS B 270 1 13
HELIX 34 AD7 ARG B 271 LEU B 274 5 4
HELIX 35 AD8 HIS B 285 LEU B 288 5 4
HELIX 36 AD9 ASP B 289 VAL B 296 1 8
HELIX 37 AE1 ASN B 297 HIS B 299 5 3
HELIX 38 AE2 ILE B 305 HIS B 313 1 9
HELIX 39 AE3 THR B 317 SER B 330 1 14
HELIX 40 AE4 GLY B 335 GLN B 339 5 5
HELIX 41 AE5 ILE B 357 VAL B 362 1 6
HELIX 42 AE6 LEU B 363 HIS B 366 5 4
HELIX 43 AE7 ASN B 385 LEU B 398 1 14
HELIX 44 AE8 LEU C 6 PHE C 10 5 5
HELIX 45 AE9 SER C 19 ARG C 27 1 9
HELIX 46 AF1 ARG C 27 LYS C 34 1 8
HELIX 47 AF2 SER C 43 LYS C 57 1 15
HELIX 48 AF3 SER C 64 ALA C 70 1 7
HELIX 49 AF4 PHE C 71 ALA C 88 1 18
HELIX 50 AF5 LYS C 90 ARG C 109 1 20
HELIX 51 AF6 SER C 120 SER C 138 1 19
HELIX 52 AF7 ASN C 194 ARG C 204 1 11
HELIX 53 AF8 ALA C 227 GLN C 242 1 16
HELIX 54 AF9 SER C 257 HIS C 270 1 14
HELIX 55 AG1 ARG C 271 LEU C 274 5 4
HELIX 56 AG2 HIS C 285 LEU C 288 5 4
HELIX 57 AG3 ASP C 289 ALA C 294 1 6
HELIX 58 AG4 LYS C 295 HIS C 299 5 5
HELIX 59 AG5 ILE C 305 HIS C 313 1 9
HELIX 60 AG6 THR C 317 SER C 330 1 14
HELIX 61 AG7 GLY C 335 GLN C 339 5 5
HELIX 62 AG8 ILE C 357 VAL C 362 1 6
HELIX 63 AG9 LEU C 363 HIS C 366 5 4
HELIX 64 AH1 ASN C 385 LEU C 398 1 14
HELIX 65 AH2 LEU D 6 PHE D 10 5 5
HELIX 66 AH3 SER D 19 ARG D 27 1 9
HELIX 67 AH4 ARG D 27 SER D 35 1 9
HELIX 68 AH5 SER D 43 LYS D 57 1 15
HELIX 69 AH6 SER D 64 ALA D 70 1 7
HELIX 70 AH7 PHE D 71 ALA D 88 1 18
HELIX 71 AH8 LYS D 90 ARG D 109 1 20
HELIX 72 AH9 SER D 120 SER D 138 1 19
HELIX 73 AI1 TYR D 190 ASP D 193 5 4
HELIX 74 AI2 ASN D 194 ARG D 204 1 11
HELIX 75 AI3 ALA D 227 GLN D 242 1 16
HELIX 76 AI4 GLY D 259 HIS D 270 1 12
HELIX 77 AI5 ARG D 271 LEU D 274 5 4
HELIX 78 AI6 HIS D 285 LEU D 288 5 4
HELIX 79 AI7 ASP D 289 ALA D 294 1 6
HELIX 80 AI8 LYS D 295 HIS D 299 5 5
HELIX 81 AI9 ILE D 305 HIS D 313 1 9
HELIX 82 AJ1 THR D 317 SER D 330 1 14
HELIX 83 AJ2 GLY D 335 GLN D 339 5 5
HELIX 84 AJ3 ILE D 357 VAL D 362 1 6
HELIX 85 AJ4 LEU D 363 HIS D 366 5 4
HELIX 86 AJ5 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 164 N VAL A 147
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 ASN A 247 N VAL A 178
SHEET 6 AA116 GLY A 276 HIS A 280 1 O HIS A 280 N GLY A 255
SHEET 7 AA116 ARG A 343 GLY A 349 1 O LEU A 345 N ALA A 277
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 GLY B 372 N LYS A 370
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 VAL B 147 O ILE B 164
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 162 N VAL C 149
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 TRP C 254 N LEU C 182
SHEET 6 AA2 8 GLY C 276 HIS C 280 1 O HIS C 280 N GLY C 255
SHEET 7 AA2 8 ARG C 343 GLY C 349 1 O LEU C 345 N ALA C 279
SHEET 8 AA2 8 GLU C 371 TYR C 375 1 O GLU C 371 N LEU C 344
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 164 N VAL D 147
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 HIS D 280 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 1.47
CISPEP 2 PHE A 110 PRO A 111 0 -2.64
CISPEP 3 TYR A 383 PRO A 384 0 -1.12
CISPEP 4 TYR B 37 PRO B 38 0 -0.62
CISPEP 5 PHE B 110 PRO B 111 0 -2.82
CISPEP 6 TYR B 383 PRO B 384 0 -8.06
CISPEP 7 TYR C 37 PRO C 38 0 1.38
CISPEP 8 PHE C 110 PRO C 111 0 -2.78
CISPEP 9 TYR C 383 PRO C 384 0 -3.80
CISPEP 10 TYR D 37 PRO D 38 0 2.06
CISPEP 11 PHE D 110 PRO D 111 0 0.25
CISPEP 12 TYR D 383 PRO D 384 0 -3.25
CRYST1 85.830 108.480 91.890 90.00 90.03 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 0.011651 0.000000 0.000005 0.00000
SCALE2 0.000000 0.009218 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010883 0.00000
TER 3143 SER A 400
TER 6271 SER B 400
TER 9362 SER C 400
TER 12494 SER D 400
MASTER 570 0 0 86 32 0 0 614126 4 0 132
END |