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HEADER HYDROLASE 18-APR-25 9O9W
TITLE CRYSTAL STRUCTURE OF AN ALPHA/BETA-HYDROLASE FROM ACTINOPLANES SP.
TITLE 2 DH11
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POLY(ETHYLENE TEREPHTHALATE) HYDROLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.1.1.101;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ACTINOPLANES SP. DH11;
SOURCE 3 ORGANISM_TAXID: 2857011;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_VARIANT: C41;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PCDB179
KEYWDS PET HYDROLASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR B.NORTON-BAKER,O.STORMENT,I.I.MATHEWS,N.P.GAUTHIER,J.E.MCGEEHAN,
AUTHOR 2 G.T.BECKHAM
REVDAT 1 08-OCT-25 9O9W 0
JRNL AUTH B.NORTON-BAKER,E.KOMP,J.E.GADO,M.C.R.DENTON,I.I.MATHEWS,
JRNL AUTH 2 N.P.MURPHY,E.ERICKSON,O.O.STORMENT,R.SARANGI,N.P.GAUTHIER,
JRNL AUTH 3 J.E.MCGEEHAN,G.T.BECKHAM
JRNL TITL MACHINE LEARNING-GUIDED IDENTIFICATION OF PET HYDROLASES
JRNL TITL 2 FROM NATURAL DIVERSITY.
JRNL REF ACS CATALYSIS V. 15 16070 2025
JRNL REFN ESSN 2155-5435
JRNL PMID 40995134
JRNL DOI 10.1021/ACSCATAL.5C03460
REMARK 2
REMARK 2 RESOLUTION. 1.76 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) : 1.76
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.78
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 62371
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) : 0.163
REMARK 3 R VALUE (WORKING SET) : 0.161
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 : 3283
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) : 1.76
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.81
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4537
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.92
REMARK 3 BIN R VALUE (WORKING SET) : 0.3170
REMARK 3 BIN FREE R VALUE SET COUNT : 239
REMARK 3 BIN FREE R VALUE : 0.3300
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3852
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 14
REMARK 3 SOLVENT ATOMS : 487
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.25
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.63000
REMARK 3 B22 (A**2) : 0.63000
REMARK 3 B33 (A**2) : -2.05000
REMARK 3 B12 (A**2) : 0.32000
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): 0.090
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.094
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.077
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.995
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.975
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.959
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3979 ; 0.009 ; 0.012
REMARK 3 BOND LENGTHS OTHERS (A): 3751 ; 0.001 ; 0.016
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5443 ; 1.639 ; 1.784
REMARK 3 BOND ANGLES OTHERS (DEGREES): 8602 ; 0.560 ; 1.715
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 523 ; 6.624 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 36 ;10.980 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 564 ;10.462 ;10.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 614 ; 0.082 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4860 ; 0.008 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 952 ; 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): 2092 ; 1.833 ; 2.316
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2092 ; 1.818 ; 2.315
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2615 ; 2.239 ; 4.152
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 2616 ; 2.239 ; 4.153
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1887 ; 2.882 ; 2.566
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1888 ; 2.881 ; 2.567
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 2829 ; 4.117 ; 4.606
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 4513 ; 5.684 ;24.630
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 4396 ; 5.561 ;23.400
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 : 2
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 2 A 264
REMARK 3 ORIGIN FOR THE GROUP (A): 27.071 -17.473 -3.503
REMARK 3 T TENSOR
REMARK 3 T11: 0.1521 T22: 0.0693
REMARK 3 T33: 0.0152 T12: -0.0759
REMARK 3 T13: -0.0263 T23: 0.0075
REMARK 3 L TENSOR
REMARK 3 L11: 0.5221 L22: 0.4752
REMARK 3 L33: 0.2653 L12: 0.2308
REMARK 3 L13: 0.1379 L23: 0.1319
REMARK 3 S TENSOR
REMARK 3 S11: -0.0922 S12: -0.0464 S13: 0.0381
REMARK 3 S21: -0.1186 S22: 0.0799 S23: 0.0395
REMARK 3 S31: -0.0134 S32: -0.0021 S33: 0.0123
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 2 B 259
REMARK 3 ORIGIN FOR THE GROUP (A): 45.919 -41.895 -16.465
REMARK 3 T TENSOR
REMARK 3 T11: 0.1524 T22: 0.1449
REMARK 3 T33: 0.0200 T12: -0.0477
REMARK 3 T13: -0.0137 T23: -0.0091
REMARK 3 L TENSOR
REMARK 3 L11: 0.1539 L22: 0.2822
REMARK 3 L33: 0.5910 L12: 0.0320
REMARK 3 L13: -0.1145 L23: 0.0735
REMARK 3 S TENSOR
REMARK 3 S11: 0.1274 S12: -0.0208 S13: 0.0085
REMARK 3 S21: 0.0639 S22: -0.0527 S23: 0.0325
REMARK 3 S31: 0.0255 S32: 0.1031 S33: -0.0747
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 9O9W COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-APR-25.
REMARK 100 THE DEPOSITION ID IS D_1000294687.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-MAR-24
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
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 : 65654
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.760
REMARK 200 RESOLUTION RANGE LOW (A) : 37.780
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 13.50
REMARK 200 R MERGE (I) : 0.12300
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 13.3400
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.76
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.81
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 2.61400
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 (%): 57.82
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.92
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PRECIPITANT MIX 1, 0.06 M
REMARK 280 DIVALENTS, BUFFER SYSTEM 1 (PH 6.5) (MORPHEUS SCREEN), VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
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 99.24667
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 49.62333
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 49.62333
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 99.24667
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH B 579 LIES ON A SPECIAL POSITION.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 ALA A 1
REMARK 465 THR A 265
REMARK 465 ALA A 266
REMARK 465 ALA A 267
REMARK 465 ALA A 268
REMARK 465 GLY A 269
REMARK 465 ALA B 1
REMARK 465 THR B 260
REMARK 465 THR B 261
REMARK 465 ARG B 262
REMARK 465 ALA B 263
REMARK 465 LEU B 264
REMARK 465 THR B 265
REMARK 465 ALA B 266
REMARK 465 ALA B 267
REMARK 465 ALA B 268
REMARK 465 GLY B 269
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 NH1 ARG B 182 NH1 ARG B 182 6554 2.01
REMARK 500 O4 PGE B 301 C6 PGE B 301 6554 2.02
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 111 NE - CZ - NH2 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ARG A 141 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 ARG B 115 NE - CZ - NH1 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ARG B 182 NE - CZ - NH1 ANGL. DEV. = -6.7 DEGREES
REMARK 500 ARG B 182 NE - CZ - NH2 ANGL. DEV. = 3.3 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 129 -122.06 59.67
REMARK 500 ALA A 152 51.47 39.67
REMARK 500 SER B 129 -118.50 61.61
REMARK 500 SER B 253 31.52 -99.55
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 97 0.11 SIDE CHAIN
REMARK 500 ARG A 141 0.07 SIDE CHAIN
REMARK 500 ARG B 97 0.10 SIDE CHAIN
REMARK 500 ARG B 111 0.15 SIDE CHAIN
REMARK 500 ARG B 115 0.21 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 644 DISTANCE = 5.96 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 301 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 195 OE1
REMARK 620 2 GLU A 195 OE2 52.8
REMARK 620 3 SER A 253 O 80.0 130.7
REMARK 620 4 PRO A 255 O 95.8 87.8 83.0
REMARK 620 5 HOH A 508 O 144.7 155.2 73.3 103.3
REMARK 620 6 HOH A 561 O 80.3 90.7 95.1 175.9 79.5
REMARK 620 7 HOH A 591 O 134.7 82.7 145.3 90.0 75.3 93.6
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 302 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 195 OE1
REMARK 620 2 GLU B 195 OE2 52.1
REMARK 620 3 SER B 253 O 76.8 126.8
REMARK 620 4 PRO B 255 O 93.3 86.0 83.4
REMARK 620 5 HOH B 428 O 141.1 164.1 68.8 100.0
REMARK 620 6 HOH B 585 O 81.7 83.6 104.4 169.4 89.7
REMARK 620 7 HOH B 588 O 136.1 84.4 146.6 88.1 81.2 89.2
REMARK 620 N 1 2 3 4 5 6
DBREF 9O9W A 1 269 PDB 9O9W 9O9W 1 269
DBREF 9O9W B 1 269 PDB 9O9W 9O9W 1 269
SEQRES 1 A 269 ALA ALA ASN PRO TYR GLN ARG GLY PRO ALA PRO THR ALA
SEQRES 2 A 269 ALA SER VAL ALA ALA VAL THR GLY PRO PHE ALA THR ALA
SEQRES 3 A 269 SER VAL SER VAL PRO ARG GLY ASN GLY PHE GLY GLY GLY
SEQRES 4 A 269 VAL ILE TYR TYR PRO THR ASP THR SER GLN GLY THR PHE
SEQRES 5 A 269 GLY GLY LEU ALA ILE SER PRO GLY LEU ASN GLY THR TRP
SEQRES 6 A 269 PRO GLY ILE ALA TRP LEU GLY SER ARG LEU ALA SER GLN
SEQRES 7 A 269 GLY PHE ILE VAL PHE GLY ILE GLU THR ASN ASN LEU ASN
SEQRES 8 A 269 ASP SER PRO THR SER ARG GLY THR GLN LEU LEU ALA ALA
SEQRES 9 A 269 LEU ASP TYR LEU ALA GLN ARG SER SER VAL ARG SER ARG
SEQRES 10 A 269 LEU ASP PRO GLY ARG LEU ALA VAL ALA GLY HIS SER MET
SEQRES 11 A 269 GLY GLY GLY GLY ALA LEU ASP ALA ALA LEU ARG ARG PRO
SEQRES 12 A 269 SER LEU LYS ALA ALA ILE GLY ASN ALA PRO TYR LEU PRO
SEQRES 13 A 269 SER ASN THR LEU ALA GLY ASN ARG VAL PRO THR LEU ILE
SEQRES 14 A 269 TYR ALA MET GLN ASN ASP THR LEU VAL PRO PRO SER ARG
SEQRES 15 A 269 LEU THR SER LEU TYR ASN THR ILE PRO ALA THR THR GLU
SEQRES 16 A 269 ARG ALA TYR LEU GLU ILE THR GLY ALA GLY HIS ASN TYR
SEQRES 17 A 269 ILE GLY GLN PRO SER THR THR LEU ALA ARG THR MET ILE
SEQRES 18 A 269 PRO TRP LEU LYS ILE PHE ILE ASP ASN ASP THR ARG PHE
SEQRES 19 A 269 SER GLN PHE LEU CYS PRO LEU ALA ASP GLN SER GLY ILE
SEQRES 20 A 269 ARG GLN TYR ARG SER SER CYS PRO LEU VAL PRO ALA THR
SEQRES 21 A 269 THR ARG ALA LEU THR ALA ALA ALA GLY
SEQRES 1 B 269 ALA ALA ASN PRO TYR GLN ARG GLY PRO ALA PRO THR ALA
SEQRES 2 B 269 ALA SER VAL ALA ALA VAL THR GLY PRO PHE ALA THR ALA
SEQRES 3 B 269 SER VAL SER VAL PRO ARG GLY ASN GLY PHE GLY GLY GLY
SEQRES 4 B 269 VAL ILE TYR TYR PRO THR ASP THR SER GLN GLY THR PHE
SEQRES 5 B 269 GLY GLY LEU ALA ILE SER PRO GLY LEU ASN GLY THR TRP
SEQRES 6 B 269 PRO GLY ILE ALA TRP LEU GLY SER ARG LEU ALA SER GLN
SEQRES 7 B 269 GLY PHE ILE VAL PHE GLY ILE GLU THR ASN ASN LEU ASN
SEQRES 8 B 269 ASP SER PRO THR SER ARG GLY THR GLN LEU LEU ALA ALA
SEQRES 9 B 269 LEU ASP TYR LEU ALA GLN ARG SER SER VAL ARG SER ARG
SEQRES 10 B 269 LEU ASP PRO GLY ARG LEU ALA VAL ALA GLY HIS SER MET
SEQRES 11 B 269 GLY GLY GLY GLY ALA LEU ASP ALA ALA LEU ARG ARG PRO
SEQRES 12 B 269 SER LEU LYS ALA ALA ILE GLY ASN ALA PRO TYR LEU PRO
SEQRES 13 B 269 SER ASN THR LEU ALA GLY ASN ARG VAL PRO THR LEU ILE
SEQRES 14 B 269 TYR ALA MET GLN ASN ASP THR LEU VAL PRO PRO SER ARG
SEQRES 15 B 269 LEU THR SER LEU TYR ASN THR ILE PRO ALA THR THR GLU
SEQRES 16 B 269 ARG ALA TYR LEU GLU ILE THR GLY ALA GLY HIS ASN TYR
SEQRES 17 B 269 ILE GLY GLN PRO SER THR THR LEU ALA ARG THR MET ILE
SEQRES 18 B 269 PRO TRP LEU LYS ILE PHE ILE ASP ASN ASP THR ARG PHE
SEQRES 19 B 269 SER GLN PHE LEU CYS PRO LEU ALA ASP GLN SER GLY ILE
SEQRES 20 B 269 ARG GLN TYR ARG SER SER CYS PRO LEU VAL PRO ALA THR
SEQRES 21 B 269 THR ARG ALA LEU THR ALA ALA ALA GLY
HET CA A 301 1
HET PGE B 301 10
HET CA B 302 1
HET CL B 303 1
HET CL B 304 1
HETNAM CA CALCIUM ION
HETNAM PGE TRIETHYLENE GLYCOL
HETNAM CL CHLORIDE ION
FORMUL 3 CA 2(CA 2+)
FORMUL 4 PGE C6 H14 O4
FORMUL 6 CL 2(CL 1-)
FORMUL 8 HOH *487(H2 O)
HELIX 1 AA1 THR A 12 ALA A 18 1 7
HELIX 2 AA2 THR A 64 ALA A 69 5 6
HELIX 3 AA3 TRP A 70 SER A 77 1 8
HELIX 4 AA4 SER A 93 ARG A 111 1 19
HELIX 5 AA5 VAL A 114 SER A 116 5 3
HELIX 6 AA6 SER A 129 ARG A 142 1 14
HELIX 7 AA7 PRO A 179 THR A 189 1 11
HELIX 8 AA8 ASN A 207 GLN A 211 5 5
HELIX 9 AA9 SER A 213 ASN A 230 1 18
HELIX 10 AB1 ASP A 231 LEU A 238 5 8
HELIX 11 AB2 THR B 12 ALA B 18 1 7
HELIX 12 AB3 THR B 64 ILE B 68 5 5
HELIX 13 AB4 ALA B 69 SER B 77 1 9
HELIX 14 AB5 SER B 93 ARG B 111 1 19
HELIX 15 AB6 VAL B 114 SER B 116 5 3
HELIX 16 AB7 SER B 129 ARG B 142 1 14
HELIX 17 AB8 PRO B 179 THR B 189 1 11
HELIX 18 AB9 ASN B 207 GLN B 211 5 5
HELIX 19 AC1 SER B 213 ASN B 230 1 18
HELIX 20 AC2 ASP B 231 LEU B 238 5 8
SHEET 1 AA118 ILE A 247 SER A 252 0
SHEET 2 AA118 ARG A 196 ILE A 201 -1 N GLU A 200 O ARG A 248
SHEET 3 AA118 THR A 167 MET A 172 1 N ALA A 171 O ILE A 201
SHEET 4 AA118 ALA A 147 ASN A 151 1 N GLY A 150 O LEU A 168
SHEET 5 AA118 LEU A 118 HIS A 128 1 N GLY A 127 O ASN A 151
SHEET 6 AA118 PHE A 52 SER A 58 1 N PHE A 52 O ASP A 119
SHEET 7 AA118 ILE A 81 ILE A 85 1 O PHE A 83 N LEU A 55
SHEET 8 AA118 GLY A 39 PRO A 44 -1 N TYR A 42 O VAL A 82
SHEET 9 AA118 THR A 25 VAL A 30 -1 N VAL A 30 O GLY A 39
SHEET 10 AA118 THR B 25 VAL B 30 -1 O SER B 29 N THR A 25
SHEET 11 AA118 GLY B 39 PRO B 44 -1 O GLY B 39 N VAL B 30
SHEET 12 AA118 ILE B 81 ILE B 85 -1 O VAL B 82 N TYR B 42
SHEET 13 AA118 PHE B 52 SER B 58 1 N LEU B 55 O PHE B 83
SHEET 14 AA118 LEU B 118 HIS B 128 1 O ASP B 119 N PHE B 52
SHEET 15 AA118 ALA B 147 ASN B 151 1 O ASN B 151 N GLY B 127
SHEET 16 AA118 THR B 167 MET B 172 1 O LEU B 168 N GLY B 150
SHEET 17 AA118 ARG B 196 ILE B 201 1 O ILE B 201 N ALA B 171
SHEET 18 AA118 ILE B 247 SER B 252 -1 O ARG B 251 N TYR B 198
SSBOND 1 CYS A 239 CYS A 254 1555 1555 2.17
SSBOND 2 CYS B 239 CYS B 254 1555 1555 2.15
LINK OE1 GLU A 195 CA CA A 301 1555 1555 2.48
LINK OE2 GLU A 195 CA CA A 301 1555 1555 2.45
LINK O SER A 253 CA CA A 301 1555 1555 2.35
LINK O PRO A 255 CA CA A 301 1555 1555 2.22
LINK CA CA A 301 O HOH A 508 1555 1555 2.38
LINK CA CA A 301 O HOH A 561 1555 1555 2.16
LINK CA CA A 301 O HOH A 591 1555 1555 2.41
LINK OE1 GLU B 195 CA CA B 302 1555 1555 2.52
LINK OE2 GLU B 195 CA CA B 302 1555 1555 2.50
LINK O SER B 253 CA CA B 302 1555 1555 2.29
LINK O PRO B 255 CA CA B 302 1555 1555 2.36
LINK CA CA B 302 O HOH B 428 1555 1555 2.37
LINK CA CA B 302 O HOH B 585 1555 1555 2.38
LINK CA CA B 302 O HOH B 588 1555 1555 2.30
CISPEP 1 CYS A 239 PRO A 240 0 -3.18
CISPEP 2 CYS A 254 PRO A 255 0 0.06
CISPEP 3 CYS B 239 PRO B 240 0 2.37
CISPEP 4 CYS B 254 PRO B 255 0 1.52
CRYST1 87.250 87.250 148.870 90.00 90.00 120.00 P 32 2 1 12
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 0.011461 0.006617 0.000000 0.00000
SCALE2 0.000000 0.013234 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006717 0.00000
TER 1946 LEU A 264
TER 3874 ALA B 259
MASTER 444 0 5 20 18 0 0 6 4353 2 32 42
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