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HEADER HYDROLASE 16-JUL-25 9PM2
TITLE CRYSTAL STRUCTURE OF AN ENGINEERED PETASE, EV3, DERIVED FROM
TITLE 2 THERMOBIFIDA FUSCA CUTINASE (TFCUT2)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POLY(ETHYLENE TEREPHTHALATE) HYDROLASE;
COMPND 3 CHAIN: A, B, C;
COMPND 4 EC: 3.1.1.101;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOBIFIDA FUSCA;
SOURCE 3 ORGANISM_TAXID: 2021;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_VARIANT: C41
KEYWDS PETASE, EVOLUTION-INFORMED DESIGN, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR I.I.MATHEWS,B.NORTON-BAKER,O.O.STORMENT,J.E.MCGEEHAN,G.T.BECKHAM,
AUTHOR 2 N.P.GAUTHIER
REVDAT 1 22-JUL-26 9PM2 0
JRNL AUTH B.NORTON-BAKER
JRNL TITL ITERATIVE COMPUTATIONAL AND RATIONAL DESIGN GENERATES
JRNL TITL 2 HUNDREDS OF DIVERSE AND ACTIVE PLASTIC-DEPOLYMERIZING
JRNL TITL 3 ENZYMES
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0430
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) : 38.46
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 117556
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) : 0.144
REMARK 3 R VALUE (WORKING SET) : 0.143
REMARK 3 FREE R VALUE : 0.167
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 6188
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) : 1.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.74
REMARK 3 REFLECTION IN BIN (WORKING SET) : 8580
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.12
REMARK 3 BIN R VALUE (WORKING SET) : 0.2600
REMARK 3 BIN FREE R VALUE SET COUNT : 452
REMARK 3 BIN FREE R VALUE : 0.2920
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5867
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 72
REMARK 3 SOLVENT ATOMS : 910
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.11000
REMARK 3 B22 (A**2) : -0.11000
REMARK 3 B33 (A**2) : 0.35000
REMARK 3 B12 (A**2) : -0.05000
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): 0.069
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.071
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.051
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.176
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.977
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.970
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6150 ; 0.011 ; 0.012
REMARK 3 BOND LENGTHS OTHERS (A): 5624 ; 0.001 ; 0.016
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8412 ; 1.855 ; 1.794
REMARK 3 BOND ANGLES OTHERS (DEGREES): 12982 ; 0.661 ; 1.727
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 791 ; 6.358 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 47 ; 8.440 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 887 ;10.841 ;10.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 946 ; 0.100 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7351 ; 0.010 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1417 ; 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): 3152 ; 1.486 ; 1.668
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 3152 ; 1.485 ; 1.668
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3947 ; 2.047 ; 2.987
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 3948 ; 2.051 ; 2.988
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2998 ; 2.880 ; 1.989
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 2995 ; 2.873 ; 1.988
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 4460 ; 4.215 ; 3.507
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 7111 ; 6.336 ;18.430
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 6832 ; 5.976 ;16.840
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
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 : 3
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 1 A 261
REMARK 3 ORIGIN FOR THE GROUP (A): -41.294 -68.837 -1.272
REMARK 3 T TENSOR
REMARK 3 T11: 0.0794 T22: 0.0228
REMARK 3 T33: 0.0560 T12: -0.0366
REMARK 3 T13: -0.0143 T23: 0.0040
REMARK 3 L TENSOR
REMARK 3 L11: 1.4862 L22: 2.4147
REMARK 3 L33: 0.4957 L12: 1.0241
REMARK 3 L13: 0.1574 L23: 0.2147
REMARK 3 S TENSOR
REMARK 3 S11: 0.0067 S12: 0.0186 S13: -0.2022
REMARK 3 S21: 0.0402 S22: 0.0913 S23: -0.1197
REMARK 3 S31: 0.0744 S32: -0.0326 S33: -0.0979
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 1 B 261
REMARK 3 ORIGIN FOR THE GROUP (A): -21.200 -35.362 0.387
REMARK 3 T TENSOR
REMARK 3 T11: 0.0345 T22: 0.0330
REMARK 3 T33: 0.0049 T12: -0.0113
REMARK 3 T13: -0.0059 T23: -0.0052
REMARK 3 L TENSOR
REMARK 3 L11: 0.9821 L22: 0.4460
REMARK 3 L33: 0.4864 L12: -0.2119
REMARK 3 L13: 0.1880 L23: -0.0059
REMARK 3 S TENSOR
REMARK 3 S11: 0.0058 S12: 0.0259 S13: 0.0097
REMARK 3 S21: 0.0082 S22: 0.0242 S23: -0.0190
REMARK 3 S31: -0.0149 S32: 0.0376 S33: -0.0300
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 1 C 261
REMARK 3 ORIGIN FOR THE GROUP (A): -55.977 -34.145 -20.660
REMARK 3 T TENSOR
REMARK 3 T11: 0.0083 T22: 0.0774
REMARK 3 T33: 0.0264 T12: -0.0111
REMARK 3 T13: -0.0029 T23: -0.0181
REMARK 3 L TENSOR
REMARK 3 L11: 0.9513 L22: 0.9412
REMARK 3 L33: 0.9404 L12: 0.0074
REMARK 3 L13: 0.1659 L23: 0.1159
REMARK 3 S TENSOR
REMARK 3 S11: 0.0415 S12: 0.0556 S13: -0.0561
REMARK 3 S21: 0.0058 S22: -0.0669 S23: 0.1414
REMARK 3 S31: 0.0527 S32: -0.1976 S33: 0.0254
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 9PM2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-JUL-25.
REMARK 100 THE DEPOSITION ID IS D_1000297863.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-MAY-24
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL12-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97946
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : RH COATED COLLIMATING MIRRORS, K
REMARK 200 -B FOCUSING MIRRORS
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 : 123744
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 38.500
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 200 DATA REDUNDANCY : 27.60
REMARK 200 R MERGE (I) : 0.20400
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 12.2300
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) : 1.74
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 2.76000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.98
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.41
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2AMMONIUM SULFATE, 0.1 TRIS(8.0),
REMARK 280 20% PEG SMEAR BROAD, PH 8.0, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 17.60667
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 35.21333
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 26.41000
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 44.01667
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 8.80333
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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 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 ASP C 246
REMARK 465 GLY C 247
REMARK 465 LEU C 248
REMARK 465 PHE C 249
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 NH2 ARG C 110 O HOH C 401 2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 27 CD GLU A 27 OE2 0.089
REMARK 500 GLU B 27 CD GLU B 27 OE2 0.162
REMARK 500 ARG C 73 NE ARG C 73 CZ -0.097
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 245 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 GLU B 27 CG - CD - OE1 ANGL. DEV. = -16.4 DEGREES
REMARK 500 ARG B 31 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ARG B 73 CD - NE - CZ ANGL. DEV. = 11.5 DEGREES
REMARK 500 ARG B 73 NE - CZ - NH1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 ARG B 73 NE - CZ - NH2 ANGL. DEV. = -6.8 DEGREES
REMARK 500 ARG B 110 NE - CZ - NH2 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ARG B 228 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 ARG C 19 NE - CZ - NH1 ANGL. DEV. = 5.0 DEGREES
REMARK 500 ARG C 19 NE - CZ - NH2 ANGL. DEV. = -5.3 DEGREES
REMARK 500 ARG C 73 CD - NE - CZ ANGL. DEV. = 10.4 DEGREES
REMARK 500 ARG C 73 NE - CZ - NH1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 ARG C 73 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 LYS C 147 CD - CE - NZ ANGL. DEV. = 14.7 DEGREES
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 SER A 130 -120.06 66.56
REMARK 500 THR A 153 56.73 38.02
REMARK 500 HIS A 184 -89.88 -121.21
REMARK 500 THR B 61 -11.67 80.07
REMARK 500 SER B 130 -121.68 68.24
REMARK 500 THR B 153 58.19 37.86
REMARK 500 HIS B 184 -91.40 -124.76
REMARK 500 THR C 61 -11.50 82.36
REMARK 500 SER C 130 -122.35 66.04
REMARK 500 THR C 153 58.04 36.88
REMARK 500 HIS C 184 -87.88 -122.37
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 96 0.09 SIDE CHAIN
REMARK 500 ARG A 118 0.09 SIDE CHAIN
REMARK 500 ARG B 96 0.09 SIDE CHAIN
REMARK 500 ARG C 96 0.10 SIDE CHAIN
REMARK 500 ARG C 118 0.09 SIDE CHAIN
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 A 678 DISTANCE = 6.03 ANGSTROMS
REMARK 525 HOH B 757 DISTANCE = 6.09 ANGSTROMS
REMARK 525 HOH B 758 DISTANCE = 6.38 ANGSTROMS
REMARK 525 HOH B 759 DISTANCE = 6.43 ANGSTROMS
REMARK 525 HOH B 760 DISTANCE = 6.52 ANGSTROMS
REMARK 525 HOH C 672 DISTANCE = 6.07 ANGSTROMS
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 PG4 A 301
DBREF 9PM2 A 1 261 PDB 9PM2 9PM2 1 261
DBREF 9PM2 B 1 261 PDB 9PM2 9PM2 1 261
DBREF 9PM2 C 1 261 PDB 9PM2 9PM2 1 261
SEQRES 1 A 261 ALA ASN PRO TYR GLU ARG GLY PRO ASN PRO THR ASP ALA
SEQRES 2 A 261 LEU LEU GLU ALA THR ARG GLY PRO PHE SER VAL SER THR
SEQRES 3 A 261 GLU THR VAL SER ARG LEU SER ALA SER GLY PHE GLY GLY
SEQRES 4 A 261 GLY THR ILE TYR TYR PRO THR SER THR GLY THR PHE GLY
SEQRES 5 A 261 ALA VAL ALA ILE SER PRO GLY TYR THR ALA THR GLN SER
SEQRES 6 A 261 SER ILE ALA TRP LEU GLY PRO ARG ILE ALA SER GLN GLY
SEQRES 7 A 261 PHE VAL VAL PHE THR ILE ASP THR ASN THR THR LEU ASP
SEQRES 8 A 261 GLY PRO ASP SER ARG GLY ARG GLN LEU LEU ALA ALA LEU
SEQRES 9 A 261 ASP TYR LEU THR ASN ARG ALA SER SER THR VAL ARG SER
SEQRES 10 A 261 ARG ILE ASP ALA SER ARG LEU ALA VAL MET GLY HIS SER
SEQRES 11 A 261 MET GLY GLY GLY GLY THR LEU GLU ALA ALA LYS ASP ARG
SEQRES 12 A 261 PRO SER LEU LYS ALA ALA ILE PRO LEU THR PRO TRP HIS
SEQRES 13 A 261 LEU ASN LYS ASN TRP SER SER VAL THR VAL PRO THR LEU
SEQRES 14 A 261 ILE ILE GLY ALA GLN ASN ASP THR ILE ALA PRO VAL ALA
SEQRES 15 A 261 THR HIS ALA GLU PRO PHE TYR ASN SER LEU PRO SER SER
SEQRES 16 A 261 LEU ASP LYS ALA TYR LEU GLU LEU CYS GLY ALA SER HIS
SEQRES 17 A 261 ILE ALA PRO ASN THR PRO ASN THR THR ILE ALA LYS TYR
SEQRES 18 A 261 SER ILE ALA TRP LEU LYS ARG PHE VAL ASP ASN ASP THR
SEQRES 19 A 261 ARG TYR GLU GLN PHE LEU CYS PRO GLY PRO ARG ASP GLY
SEQRES 20 A 261 LEU PHE GLY GLU VAL CYS GLU TYR ARG SER THR CYS PRO
SEQRES 21 A 261 PHE
SEQRES 1 B 261 ALA ASN PRO TYR GLU ARG GLY PRO ASN PRO THR ASP ALA
SEQRES 2 B 261 LEU LEU GLU ALA THR ARG GLY PRO PHE SER VAL SER THR
SEQRES 3 B 261 GLU THR VAL SER ARG LEU SER ALA SER GLY PHE GLY GLY
SEQRES 4 B 261 GLY THR ILE TYR TYR PRO THR SER THR GLY THR PHE GLY
SEQRES 5 B 261 ALA VAL ALA ILE SER PRO GLY TYR THR ALA THR GLN SER
SEQRES 6 B 261 SER ILE ALA TRP LEU GLY PRO ARG ILE ALA SER GLN GLY
SEQRES 7 B 261 PHE VAL VAL PHE THR ILE ASP THR ASN THR THR LEU ASP
SEQRES 8 B 261 GLY PRO ASP SER ARG GLY ARG GLN LEU LEU ALA ALA LEU
SEQRES 9 B 261 ASP TYR LEU THR ASN ARG ALA SER SER THR VAL ARG SER
SEQRES 10 B 261 ARG ILE ASP ALA SER ARG LEU ALA VAL MET GLY HIS SER
SEQRES 11 B 261 MET GLY GLY GLY GLY THR LEU GLU ALA ALA LYS ASP ARG
SEQRES 12 B 261 PRO SER LEU LYS ALA ALA ILE PRO LEU THR PRO TRP HIS
SEQRES 13 B 261 LEU ASN LYS ASN TRP SER SER VAL THR VAL PRO THR LEU
SEQRES 14 B 261 ILE ILE GLY ALA GLN ASN ASP THR ILE ALA PRO VAL ALA
SEQRES 15 B 261 THR HIS ALA GLU PRO PHE TYR ASN SER LEU PRO SER SER
SEQRES 16 B 261 LEU ASP LYS ALA TYR LEU GLU LEU CYS GLY ALA SER HIS
SEQRES 17 B 261 ILE ALA PRO ASN THR PRO ASN THR THR ILE ALA LYS TYR
SEQRES 18 B 261 SER ILE ALA TRP LEU LYS ARG PHE VAL ASP ASN ASP THR
SEQRES 19 B 261 ARG TYR GLU GLN PHE LEU CYS PRO GLY PRO ARG ASP GLY
SEQRES 20 B 261 LEU PHE GLY GLU VAL CYS GLU TYR ARG SER THR CYS PRO
SEQRES 21 B 261 PHE
SEQRES 1 C 261 ALA ASN PRO TYR GLU ARG GLY PRO ASN PRO THR ASP ALA
SEQRES 2 C 261 LEU LEU GLU ALA THR ARG GLY PRO PHE SER VAL SER THR
SEQRES 3 C 261 GLU THR VAL SER ARG LEU SER ALA SER GLY PHE GLY GLY
SEQRES 4 C 261 GLY THR ILE TYR TYR PRO THR SER THR GLY THR PHE GLY
SEQRES 5 C 261 ALA VAL ALA ILE SER PRO GLY TYR THR ALA THR GLN SER
SEQRES 6 C 261 SER ILE ALA TRP LEU GLY PRO ARG ILE ALA SER GLN GLY
SEQRES 7 C 261 PHE VAL VAL PHE THR ILE ASP THR ASN THR THR LEU ASP
SEQRES 8 C 261 GLY PRO ASP SER ARG GLY ARG GLN LEU LEU ALA ALA LEU
SEQRES 9 C 261 ASP TYR LEU THR ASN ARG ALA SER SER THR VAL ARG SER
SEQRES 10 C 261 ARG ILE ASP ALA SER ARG LEU ALA VAL MET GLY HIS SER
SEQRES 11 C 261 MET GLY GLY GLY GLY THR LEU GLU ALA ALA LYS ASP ARG
SEQRES 12 C 261 PRO SER LEU LYS ALA ALA ILE PRO LEU THR PRO TRP HIS
SEQRES 13 C 261 LEU ASN LYS ASN TRP SER SER VAL THR VAL PRO THR LEU
SEQRES 14 C 261 ILE ILE GLY ALA GLN ASN ASP THR ILE ALA PRO VAL ALA
SEQRES 15 C 261 THR HIS ALA GLU PRO PHE TYR ASN SER LEU PRO SER SER
SEQRES 16 C 261 LEU ASP LYS ALA TYR LEU GLU LEU CYS GLY ALA SER HIS
SEQRES 17 C 261 ILE ALA PRO ASN THR PRO ASN THR THR ILE ALA LYS TYR
SEQRES 18 C 261 SER ILE ALA TRP LEU LYS ARG PHE VAL ASP ASN ASP THR
SEQRES 19 C 261 ARG TYR GLU GLN PHE LEU CYS PRO GLY PRO ARG ASP GLY
SEQRES 20 C 261 LEU PHE GLY GLU VAL CYS GLU TYR ARG SER THR CYS PRO
SEQRES 21 C 261 PHE
HET PG4 A 301 10
HET SO4 A 302 5
HET SO4 A 303 5
HET CL A 304 1
HET CL A 305 1
HET PG4 B 301 13
HET SO4 B 302 5
HET SO4 B 303 5
HET CL B 304 1
HET CL B 305 1
HET SO4 B 306 5
HET PG4 C 301 13
HET SO4 C 302 5
HET CL C 303 1
HET CL C 304 1
HETNAM PG4 TETRAETHYLENE GLYCOL
HETNAM SO4 SULFATE ION
HETNAM CL CHLORIDE ION
FORMUL 4 PG4 3(C8 H18 O5)
FORMUL 5 SO4 6(O4 S 2-)
FORMUL 7 CL 6(CL 1-)
FORMUL 19 HOH *910(H2 O)
HELIX 1 AA1 THR A 11 ALA A 17 1 7
HELIX 2 AA2 THR A 63 ALA A 68 5 6
HELIX 3 AA3 TRP A 69 SER A 76 1 8
HELIX 4 AA4 GLY A 92 ARG A 110 1 19
HELIX 5 AA5 SER A 112 SER A 117 1 6
HELIX 6 AA6 SER A 130 ARG A 143 1 14
HELIX 7 AA7 HIS A 184 LEU A 192 1 9
HELIX 8 AA8 ILE A 209 THR A 213 5 5
HELIX 9 AA9 ASN A 215 ASP A 231 1 17
HELIX 10 AB1 ASP A 233 ARG A 235 5 3
HELIX 11 AB2 TYR A 236 CYS A 241 1 6
HELIX 12 AB3 THR B 11 ALA B 17 1 7
HELIX 13 AB4 SER B 30 ALA B 34 5 5
HELIX 14 AB5 THR B 63 ALA B 68 5 6
HELIX 15 AB6 TRP B 69 SER B 76 1 8
HELIX 16 AB7 GLY B 92 ARG B 110 1 19
HELIX 17 AB8 SER B 112 ARG B 118 1 7
HELIX 18 AB9 SER B 130 ARG B 143 1 14
HELIX 19 AC1 HIS B 184 LEU B 192 1 9
HELIX 20 AC2 ILE B 209 THR B 213 5 5
HELIX 21 AC3 ASN B 215 ASP B 231 1 17
HELIX 22 AC4 ASP B 233 ARG B 235 5 3
HELIX 23 AC5 TYR B 236 CYS B 241 1 6
HELIX 24 AC6 THR C 11 ALA C 17 1 7
HELIX 25 AC7 THR C 63 ALA C 68 5 6
HELIX 26 AC8 TRP C 69 SER C 76 1 8
HELIX 27 AC9 GLY C 92 ARG C 110 1 19
HELIX 28 AD1 SER C 112 SER C 117 1 6
HELIX 29 AD2 SER C 130 ARG C 143 1 14
HELIX 30 AD3 HIS C 184 LEU C 192 1 9
HELIX 31 AD4 ILE C 209 THR C 213 5 5
HELIX 32 AD5 ASN C 215 ASP C 231 1 17
HELIX 33 AD6 ASP C 233 ARG C 235 5 3
HELIX 34 AD7 TYR C 236 CYS C 241 1 6
SHEET 1 AA1 6 VAL A 24 VAL A 29 0
SHEET 2 AA1 6 GLY A 40 PRO A 45 -1 O GLY A 40 N VAL A 29
SHEET 3 AA1 6 VAL A 80 ILE A 84 -1 O VAL A 81 N TYR A 43
SHEET 4 AA1 6 PHE A 51 SER A 57 1 N VAL A 54 O PHE A 82
SHEET 5 AA1 6 ILE A 119 HIS A 129 1 O ASP A 120 N PHE A 51
SHEET 6 AA1 6 ALA A 148 LEU A 152 1 O LEU A 152 N GLY A 128
SHEET 1 AA2 3 THR A 168 ALA A 173 0
SHEET 2 AA2 3 LYS A 198 LEU A 203 1 O LEU A 203 N GLY A 172
SHEET 3 AA2 3 VAL A 252 SER A 257 -1 O CYS A 253 N GLU A 202
SHEET 1 AA3 6 VAL B 24 VAL B 29 0
SHEET 2 AA3 6 GLY B 40 PRO B 45 -1 O TYR B 44 N SER B 25
SHEET 3 AA3 6 VAL B 80 ILE B 84 -1 O VAL B 81 N TYR B 43
SHEET 4 AA3 6 PHE B 51 SER B 57 1 N VAL B 54 O PHE B 82
SHEET 5 AA3 6 ILE B 119 HIS B 129 1 O ASP B 120 N PHE B 51
SHEET 6 AA3 6 ALA B 148 LEU B 152 1 O LEU B 152 N GLY B 128
SHEET 1 AA4 3 THR B 168 ALA B 173 0
SHEET 2 AA4 3 LYS B 198 LEU B 203 1 O LEU B 203 N GLY B 172
SHEET 3 AA4 3 VAL B 252 SER B 257 -1 O GLU B 254 N GLU B 202
SHEET 1 AA5 6 VAL C 24 VAL C 29 0
SHEET 2 AA5 6 GLY C 40 PRO C 45 -1 O GLY C 40 N VAL C 29
SHEET 3 AA5 6 VAL C 80 ILE C 84 -1 O VAL C 81 N TYR C 43
SHEET 4 AA5 6 PHE C 51 SER C 57 1 N VAL C 54 O PHE C 82
SHEET 5 AA5 6 ILE C 119 HIS C 129 1 O ASP C 120 N PHE C 51
SHEET 6 AA5 6 ALA C 148 LEU C 152 1 O LEU C 152 N GLY C 128
SHEET 1 AA6 3 THR C 168 ALA C 173 0
SHEET 2 AA6 3 LYS C 198 LEU C 203 1 O LEU C 203 N GLY C 172
SHEET 3 AA6 3 VAL C 252 SER C 257 -1 O CYS C 253 N GLU C 202
SSBOND 1 CYS A 204 CYS A 253 1555 1555 2.10
SSBOND 2 CYS A 241 CYS A 259 1555 1555 2.12
SSBOND 3 CYS B 204 CYS B 253 1555 1555 2.15
SSBOND 4 CYS B 241 CYS B 259 1555 1555 2.18
SSBOND 5 CYS C 204 CYS C 253 1555 1555 2.08
SSBOND 6 CYS C 241 CYS C 259 1555 1555 2.13
CISPEP 1 CYS A 241 PRO A 242 0 1.55
CISPEP 2 CYS A 259 PRO A 260 0 -7.37
CISPEP 3 CYS B 241 PRO B 242 0 0.92
CISPEP 4 CYS B 259 PRO B 260 0 -7.53
CISPEP 5 CYS C 241 PRO C 242 0 8.70
CISPEP 6 CYS C 259 PRO C 260 0 -1.55
CRYST1 193.600 193.600 52.820 90.00 90.00 120.00 P 61 18
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 0.005165 0.002982 0.000000 0.00000
SCALE2 0.000000 0.005964 0.000000 0.00000
SCALE3 0.000000 0.000000 0.018932 0.00000
TER 1982 PHE A 261
TER 3972 PHE B 261
TER 5931 PHE C 261
MASTER 459 0 15 34 27 0 0 6 6849 3 78 63
END |