| content |
HEADER HYDROLASE 24-NOV-25 9XUH
TITLE INACTIVE MUTANT S168A OF DSPETASE05 IN COMPLEX WITH TEREPHTHALIC ACID
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA/BETA HYDROLASE;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONADOTA BACTERIUM;
SOURCE 3 ORGANISM_TAXID: 1977087;
SOURCE 4 GENE: BXT89_15940;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS HYDROLASE, PET HYDROLASE, PET DEGRADATION ENZYME
EXPDTA X-RAY DIFFRACTION
AUTHOR X.LI,M.Z.ZHANG,S.Q.HUANG,C.ZENG,J.-W.HUANG,C.-C.CHEN,R.-T.GUO
REVDAT 1 23-SEP-26 9XUH 0
JRNL AUTH X.LI,M.Z.ZHANG,S.Q.HUANG,C.ZENG,J.-W.HUANG,C.-C.CHEN,
JRNL AUTH 2 R.-T.GUO
JRNL TITL INACTIVE MUTANT S168A OF DSPETASE05 IN COMPLEX WITH
JRNL TITL 2 TEREPHTHALIC ACID
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.49 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0238
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) : 1.49
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 23.53
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 54904
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) : 0.108
REMARK 3 R VALUE (WORKING SET) : 0.107
REMARK 3 FREE R VALUE : 0.132
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2975
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) : 1.49
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.53
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4001
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.1340
REMARK 3 BIN FREE R VALUE SET COUNT : 239
REMARK 3 BIN FREE R VALUE : 0.1700
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1889
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 28
REMARK 3 SOLVENT ATOMS : 442
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.42
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.044
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.042
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.021
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.227
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.982
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.977
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2056 ; 0.013 ; 0.013
REMARK 3 BOND LENGTHS OTHERS (A): 1747 ; 0.002 ; 0.017
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2824 ; 1.827 ; 1.647
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4080 ; 1.663 ; 1.574
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 286 ; 6.999 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 100 ;34.594 ;22.800
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 283 ; 8.810 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 10 ;11.968 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 275 ; 0.102 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2444 ; 0.010 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 450 ; 0.002 ; 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): 1067 ; 1.611 ; 1.309
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1063 ; 1.428 ; 1.300
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1337 ; 1.745 ; 1.968
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1338 ; 1.746 ; 1.971
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 989 ; 2.694 ; 1.547
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 990 ; 2.693 ; 1.549
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 1474 ; 2.976 ; 2.250
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 2507 ; 6.148 ;19.294
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 2367 ; 5.331 ;17.320
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 3803 ; 3.029 ; 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 9XUH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 28-NOV-25.
REMARK 100 THE DEPOSITION ID IS D_1300066363.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-DEC-23
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 : NSRRC
REMARK 200 BEAMLINE : TPS 05A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9998
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 X 9M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 57879
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.490
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 9.600
REMARK 200 R MERGE (I) : 0.06500
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 10.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.49
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.54
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 9.60
REMARK 200 R MERGE FOR SHELL (I) : 0.52900
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: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.90
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.32
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 4.0 M POTASSIUM FORMATE, 0.1 M BIS
REMARK 280 -TRIS PROPANE 9.0, 2% W/V POLYETHYLENE GLYCOL MONOMETHYL ETHER 2,
REMARK 280 000, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 21 3
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290 5555 Z,X,Y
REMARK 290 6555 Z+1/2,-X+1/2,-Y
REMARK 290 7555 -Z+1/2,-X,Y+1/2
REMARK 290 8555 -Z,X+1/2,-Y+1/2
REMARK 290 9555 Y,Z,X
REMARK 290 10555 -Y,Z+1/2,-X+1/2
REMARK 290 11555 Y+1/2,-Z+1/2,-X
REMARK 290 12555 -Y+1/2,-Z,X+1/2
REMARK 290 13555 X+1/2,Y+1/2,Z+1/2
REMARK 290 14555 -X,-Y+1/2,Z
REMARK 290 15555 -X+1/2,Y,-Z
REMARK 290 16555 X,-Y,-Z+1/2
REMARK 290 17555 Z+1/2,X+1/2,Y+1/2
REMARK 290 18555 Z,-X,-Y+1/2
REMARK 290 19555 -Z,-X+1/2,Y
REMARK 290 20555 -Z+1/2,X,-Y
REMARK 290 21555 Y+1/2,Z+1/2,X+1/2
REMARK 290 22555 -Y+1/2,Z,-X
REMARK 290 23555 Y,-Z,-X+1/2
REMARK 290 24555 -Y,-Z+1/2,X
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 64.40350
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 64.40350
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 64.40350
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 64.40350
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 64.40350
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 64.40350
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 6 0.000000 0.000000 1.000000 64.40350
REMARK 290 SMTRY2 6 -1.000000 0.000000 0.000000 64.40350
REMARK 290 SMTRY3 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 0.000000 -1.000000 64.40350
REMARK 290 SMTRY2 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 1.000000 0.000000 64.40350
REMARK 290 SMTRY1 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 8 1.000000 0.000000 0.000000 64.40350
REMARK 290 SMTRY3 8 0.000000 -1.000000 0.000000 64.40350
REMARK 290 SMTRY1 9 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 9 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 9 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 10 0.000000 0.000000 1.000000 64.40350
REMARK 290 SMTRY3 10 -1.000000 0.000000 0.000000 64.40350
REMARK 290 SMTRY1 11 0.000000 1.000000 0.000000 64.40350
REMARK 290 SMTRY2 11 0.000000 0.000000 -1.000000 64.40350
REMARK 290 SMTRY3 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 12 0.000000 -1.000000 0.000000 64.40350
REMARK 290 SMTRY2 12 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 12 1.000000 0.000000 0.000000 64.40350
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 64.40350
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 64.40350
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 64.40350
REMARK 290 SMTRY1 14 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 64.40350
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 15 -1.000000 0.000000 0.000000 64.40350
REMARK 290 SMTRY2 15 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 16 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 16 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 64.40350
REMARK 290 SMTRY1 17 0.000000 0.000000 1.000000 64.40350
REMARK 290 SMTRY2 17 1.000000 0.000000 0.000000 64.40350
REMARK 290 SMTRY3 17 0.000000 1.000000 0.000000 64.40350
REMARK 290 SMTRY1 18 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 18 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 18 0.000000 -1.000000 0.000000 64.40350
REMARK 290 SMTRY1 19 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 19 -1.000000 0.000000 0.000000 64.40350
REMARK 290 SMTRY3 19 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 20 0.000000 0.000000 -1.000000 64.40350
REMARK 290 SMTRY2 20 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 20 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 21 0.000000 1.000000 0.000000 64.40350
REMARK 290 SMTRY2 21 0.000000 0.000000 1.000000 64.40350
REMARK 290 SMTRY3 21 1.000000 0.000000 0.000000 64.40350
REMARK 290 SMTRY1 22 0.000000 -1.000000 0.000000 64.40350
REMARK 290 SMTRY2 22 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 22 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 23 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 23 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 23 -1.000000 0.000000 0.000000 64.40350
REMARK 290 SMTRY1 24 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 24 0.000000 0.000000 -1.000000 64.40350
REMARK 290 SMTRY3 24 1.000000 0.000000 0.000000 0.00000
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 200 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9850 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -1.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1810 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19010 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 -64.40350
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 744 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 842 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 939 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 940 LIES ON A SPECIAL POSITION.
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 O HOH A 610 O HOH A 756 1.84
REMARK 500 O HOH A 771 O HOH A 886 1.85
REMARK 500 O HOH A 561 O HOH A 732 1.95
REMARK 500 ND2 ASN A 199 O HOH A 501 1.98
REMARK 500 O HOH A 513 O HOH A 650 2.10
REMARK 500
REMARK 500 REMARK: NULL
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 CG2 THR A 101 O HOH A 517 16554 2.09
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 THR A 101 OG1 - CB - CG2 ANGL. DEV. = -14.6 DEGREES
REMARK 500 ALA A 102 C - N - CA ANGL. DEV. = 19.5 DEGREES
REMARK 500 ARG A 161 NE - CZ - NH2 ANGL. DEV. = -3.2 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 THR A 101 -13.83 80.07
REMARK 500 THR A 101 44.03 35.84
REMARK 500 ALA A 168 -123.03 63.82
REMARK 500 ALA A 221 72.23 -110.73
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 941 DISTANCE = 5.83 ANGSTROMS
REMARK 525 HOH A 942 DISTANCE = 6.08 ANGSTROMS
DBREF1 9XUH A 46 301 UNP A0A1S8DDV9_9GAMM
DBREF2 9XUH A A0A1S8DDV9 34 289
SEQADV 9XUH ALA A 168 UNP A0A1S8DDV SER 156 ENGINEERED MUTATION
SEQRES 1 A 256 ASN PRO ASP THR GLY THR GLY PHE PRO GLY VAL SER SER
SEQRES 2 A 256 PHE SER ALA ASP GLY SER PHE ALA THR THR SER GLY SER
SEQRES 3 A 256 ALA GLY LEU SER CYS THR VAL PHE ARG PRO SER THR LEU
SEQRES 4 A 256 GLY ALA ASN GLY LEU LYS HIS PRO ILE ILE VAL TRP GLY
SEQRES 5 A 256 ASN GLY THR THR ALA SER PRO SER THR TYR SER GLY ILE
SEQRES 6 A 256 LEU GLU HIS TRP ALA SER HIS GLY PHE VAL VAL ILE ALA
SEQRES 7 A 256 ALA ASN THR SER ASN ALA GLY THR GLY GLN ASP MET LEU
SEQRES 8 A 256 ASN CYS VAL ASP TYR LEU THR THR GLN ASN ASN ARG SER
SEQRES 9 A 256 THR GLY THR TYR ALA ASN LYS LEU ASP LEU ASN ARG ILE
SEQRES 10 A 256 GLY ALA ALA GLY HIS ALA GLN GLY GLY GLY GLY THR ILE
SEQRES 11 A 256 MET ALA GLY GLN ASP TYR ARG ILE LYS VAL THR ALA PRO
SEQRES 12 A 256 PHE GLN PRO TYR THR ILE GLY LEU GLY HIS ASN SER SER
SEQRES 13 A 256 SER GLN SER ASN GLN ASN GLY PRO MET PHE LEU MET THR
SEQRES 14 A 256 GLY SER ALA ASP THR ILE ALA SER PRO THR LEU ASN ALA
SEQRES 15 A 256 LEU PRO VAL TYR ASN ARG ALA ASN VAL PRO VAL PHE TRP
SEQRES 16 A 256 GLY GLU LEU SER GLY ALA SER HIS PHE GLU PRO VAL GLY
SEQRES 17 A 256 SER ALA GLY ASP PHE ARG GLY PRO SER THR ALA TRP PHE
SEQRES 18 A 256 ARG TYR HIS LEU MET ASP ASP ALA SER ALA GLU ASP THR
SEQRES 19 A 256 PHE TYR GLY SER ASN CYS ASP LEU CYS THR ASP ASN ASP
SEQRES 20 A 256 TRP ASP VAL ARG ARG LYS GLY ILE ASN
HET UB7 A 401 12
HET EDO A 402 4
HET ACT A 403 4
HET ACT A 404 4
HET ACT A 405 4
HETNAM UB7 TEREPHTHALIC ACID
HETNAM EDO 1,2-ETHANEDIOL
HETNAM ACT ACETATE ION
HETSYN UB7 BENZENE-1,4-DICARBOXYLIC ACID
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 UB7 C8 H6 O4
FORMUL 3 EDO C2 H6 O2
FORMUL 4 ACT 3(C2 H3 O2 1-)
FORMUL 7 HOH *442(H2 O)
HELIX 1 AA1 GLY A 85 LEU A 89 5 5
HELIX 2 AA2 SER A 103 THR A 106 5 4
HELIX 3 AA3 TYR A 107 HIS A 117 1 11
HELIX 4 AA4 GLY A 132 ARG A 148 1 17
HELIX 5 AA5 ALA A 168 GLY A 178 1 11
HELIX 6 AA6 ASN A 199 ASN A 205 5 7
HELIX 7 AA7 SER A 222 ALA A 227 1 6
HELIX 8 AA8 ALA A 227 ALA A 234 1 8
HELIX 9 AA9 ALA A 255 ASP A 257 5 3
HELIX 10 AB1 PHE A 258 ASP A 272 1 15
HELIX 11 AB2 ASP A 273 PHE A 280 5 8
HELIX 12 AB3 CYS A 285 ASP A 290 1 6
SHEET 1 AA1 6 THR A 67 SER A 71 0
SHEET 2 AA1 6 CYS A 76 PRO A 81 -1 O ARG A 80 N THR A 68
SHEET 3 AA1 6 VAL A 120 ALA A 124 -1 O ALA A 123 N THR A 77
SHEET 4 AA1 6 HIS A 91 GLY A 97 1 N PRO A 92 O VAL A 120
SHEET 5 AA1 6 LEU A 157 HIS A 167 1 O ASP A 158 N HIS A 91
SHEET 6 AA1 6 VAL A 185 PHE A 189 1 O PHE A 189 N GLY A 166
SHEET 1 AA2 3 MET A 210 GLY A 215 0
SHEET 2 AA2 3 VAL A 238 LEU A 243 1 O LEU A 243 N THR A 214
SHEET 3 AA2 3 TRP A 293 LYS A 298 -1 O ARG A 296 N TRP A 240
SSBOND 1 CYS A 76 CYS A 138 1555 1555 2.28
SSBOND 2 CYS A 285 CYS A 288 1555 1555 2.09
CRYST1 128.807 128.807 128.807 90.00 90.00 90.00 I 21 3 24
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 0.007764 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007764 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007764 0.00000
TER 1967 ASN A 301
MASTER 434 0 5 12 9 0 0 6 2359 1 32 20
END |