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HEADER HYDROLASE 04-APR-24 9EWR
TITLE CRYSTAL STRUCTURE OF AN INVERSE CHARGED CUTINASE MUTANT FROM
TITLE 2 SACCHAROPOLYSPORA FLAVA (611)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CUTINASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.1.1.74;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROPOLYSPORA FLAVA;
SOURCE 3 ORGANISM_TAXID: 95161;
SOURCE 4 GENE: SAMN05660874_00127;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI B;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 37762
KEYWDS CUTINASE, PLASTIC, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.ZAHN,K.GREEN,L.OLIVEIRA,B.R.LICHTENSTEIN
REVDAT 1 16-APR-25 9EWR 0
JRNL AUTH L.OLIVEIRA-PESSOA,B.R.LICHTENSTEIN
JRNL TITL REDESIGNING SURFACE CHARGE TO CONTROL SUBSTRATE MORPHOLOGY
JRNL TITL 2 PREFERENCE OF A PET-HYDROLASE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.17 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0425
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.17
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 122.27
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 63.7
REMARK 3 NUMBER OF REFLECTIONS : 98972
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : FREE R-VALUE
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.186
REMARK 3 FREE R VALUE : 0.204
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.953
REMARK 3 FREE R VALUE TEST SET COUNT : 4902
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) : 1.17
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.20
REMARK 3 REFLECTION IN BIN (WORKING SET) : 171
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 1.58
REMARK 3 BIN R VALUE (WORKING SET) : 0.2550
REMARK 3 BIN FREE R VALUE SET COUNT : 9
REMARK 3 BIN FREE R VALUE : 0.3110
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3994
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 462
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.71
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.12400
REMARK 3 B22 (A**2) : -0.27000
REMARK 3 B33 (A**2) : 0.07200
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.20100
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.063
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.062
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.040
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.860
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.953
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.941
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4143 ; 0.010 ; 0.012
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5638 ; 1.976 ; 1.826
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 527 ; 6.567 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 32 ;14.567 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 685 ;11.051 ;10.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 619 ; 0.123 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3168 ; 0.012 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2036 ; 0.214 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2863 ; 0.316 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 399 ; 0.239 ; 0.200
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): 2075 ; 0.971 ; 0.820
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2592 ; 1.501 ; 1.472
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2068 ; 1.847 ; 1.039
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3039 ; 2.765 ; 1.800
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
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 : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 6 A 261 NULL
REMARK 3 1 A 6 A 261 NULL
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
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 : Ap 3 Ap 262
REMARK 3 ORIGIN FOR THE GROUP (A): 16.0826 -0.1611 14.6587
REMARK 3 T TENSOR
REMARK 3 T11: 0.0153 T22: 0.0078
REMARK 3 T33: 0.0015 T12: -0.0067
REMARK 3 T13: 0.0001 T23: 0.0016
REMARK 3 L TENSOR
REMARK 3 L11: 0.9322 L22: 0.6597
REMARK 3 L33: 0.8507 L12: -0.0477
REMARK 3 L13: 0.1786 L23: 0.0941
REMARK 3 S TENSOR
REMARK 3 S11: -0.0017 S12: 0.0442 S13: -0.0046
REMARK 3 S21: -0.0356 S22: 0.0038 S23: -0.0175
REMARK 3 S31: 0.0264 S32: -0.0065 S33: -0.0021
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 0
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 ORIGIN FOR THE GROUP (A): -3.5804 4.5942 45.8899
REMARK 3 T TENSOR
REMARK 3 T11: 0.0321 T22: 0.0471
REMARK 3 T33: 0.0133 T12: 0.0165
REMARK 3 T13: -0.0076 T23: -0.0189
REMARK 3 L TENSOR
REMARK 3 L11: 0.9198 L22: 0.5032
REMARK 3 L33: 0.8145 L12: 0.1233
REMARK 3 L13: 0.0733 L23: -0.0677
REMARK 3 S TENSOR
REMARK 3 S11: -0.0034 S12: -0.1010 S13: -0.0040
REMARK 3 S21: 0.0600 S22: 0.0129 S23: 0.0022
REMARK 3 S31: 0.0161 S32: 0.0235 S33: -0.0095
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK BULK SOLVENT
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 NOT BEEN USED
REMARK 4
REMARK 4 9EWR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 04-APR-24.
REMARK 100 THE DEPOSITION ID IS D_1292137698.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-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 : DIAMOND
REMARK 200 BEAMLINE : I03
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9763
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 XE 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : AUTOPROC
REMARK 200 DATA SCALING SOFTWARE : STARANISO
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 98981
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.166
REMARK 200 RESOLUTION RANGE LOW (A) : 122.272
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.5
REMARK 200 DATA REDUNDANCY : 6.200
REMARK 200 R MERGE (I) : 0.08100
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 7.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.17
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.32
REMARK 200 COMPLETENESS FOR SHELL (%) : 62.3
REMARK 200 DATA REDUNDANCY IN SHELL : 3.40
REMARK 200 R MERGE FOR SHELL (I) : 0.76500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.800
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 (%): 37.30
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.96
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 3.5 M SODIUM FORMATE, 0.1 M TRIS PH
REMARK 280 8.5, VAPOR DIFFUSION, SITTING 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 20.65800
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 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 1
REMARK 465 ALA A 2
REMARK 465 ASN A 49
REMARK 465 THR A 50
REMARK 465 THR A 51
REMARK 465 GLU A 263
REMARK 465 HIS A 264
REMARK 465 HIS A 265
REMARK 465 HIS A 266
REMARK 465 HIS A 267
REMARK 465 HIS A 268
REMARK 465 HIS A 269
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 GLU B 3
REMARK 465 PRO B 4
REMARK 465 ALA B 5
REMARK 465 HIS B 265
REMARK 465 HIS B 266
REMARK 465 HIS B 267
REMARK 465 HIS B 268
REMARK 465 HIS B 269
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 B 399 O HOH B 467 1.61
REMARK 500 O HOH A 379 O HOH A 414 1.89
REMARK 500 O HOH A 345 O HOH A 530 1.94
REMARK 500 O HOH A 517 O HOH B 458 1.95
REMARK 500 OD1 ASP A 144 O HOH A 301 2.09
REMARK 500 NH1 ARG A 77 OD1 ASP A 216 2.11
REMARK 500 O HOH A 304 O HOH A 366 2.11
REMARK 500 O HOH A 426 O HOH A 490 2.14
REMARK 500 O HOH B 355 O HOH B 401 2.18
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 O HOH A 543 O HOH B 483 1655 1.98
REMARK 500 O HOH B 471 O HOH B 499 1455 2.10
REMARK 500 O HOH B 309 O HOH B 426 2556 2.15
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 33 CG - CD - NE ANGL. DEV. = -15.8 DEGREES
REMARK 500 ARG A 167 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 ARG A 230 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 ARG A 230 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ARG B 33 CG - CD - NE ANGL. DEV. = -14.8 DEGREES
REMARK 500 ARG B 33 NE - CZ - NH2 ANGL. DEV. = -3.4 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 132 -123.12 66.86
REMARK 500 THR A 155 54.47 38.62
REMARK 500 HIS A 186 -83.72 -130.20
REMARK 500 ASP A 216 123.32 -38.57
REMARK 500 ASP A 216 123.36 -38.52
REMARK 500 ASP B 52 -131.09 -98.89
REMARK 500 SER B 132 -125.13 69.65
REMARK 500 THR B 155 57.23 36.11
REMARK 500 HIS B 186 -84.97 -131.42
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 33 0.11 SIDE CHAIN
REMARK 500 ARG A 100 0.11 SIDE CHAIN
REMARK 500 ARG A 164 0.13 SIDE CHAIN
REMARK 500 ARG A 167 0.15 SIDE CHAIN
REMARK 500 ARG B 21 0.09 SIDE CHAIN
REMARK 500 ARG B 33 0.19 SIDE CHAIN
REMARK 500 ARG B 100 0.10 SIDE CHAIN
REMARK 500 ARG B 164 0.11 SIDE CHAIN
REMARK 500 ARG B 167 0.14 SIDE CHAIN
REMARK 500 ARG B 237 0.09 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 7QJP RELATED DB: PDB
REMARK 900 ORIGINAL ENZYME
DBREF1 9EWR A 2 261 UNP A0A1I6NU60_9PSEU
DBREF2 9EWR A A0A1I6NU60 34 293
DBREF1 9EWR B 2 261 UNP A0A1I6NU60_9PSEU
DBREF2 9EWR B A0A1I6NU60 34 293
SEQADV 9EWR MET A 1 UNP A0A1I6NU6 INITIATING METHIONINE
SEQADV 9EWR LYS A 6 UNP A0A1I6NU6 ASP 38 ENGINEERED MUTATION
SEQADV 9EWR LYS A 11 UNP A0A1I6NU6 ASP 43 ENGINEERED MUTATION
SEQADV 9EWR LYS A 19 UNP A0A1I6NU6 ALA 51 ENGINEERED MUTATION
SEQADV 9EWR ASN A 27 UNP A0A1I6NU6 ASP 59 ENGINEERED MUTATION
SEQADV 9EWR ARG A 28 UNP A0A1I6NU6 GLU 60 ENGINEERED MUTATION
SEQADV 9EWR ARG A 29 UNP A0A1I6NU6 GLU 61 ENGINEERED MUTATION
SEQADV 9EWR LYS A 35 UNP A0A1I6NU6 SER 67 ENGINEERED MUTATION
SEQADV 9EWR LYS A 37 UNP A0A1I6NU6 SER 69 ENGINEERED MUTATION
SEQADV 9EWR ASN A 49 UNP A0A1I6NU6 ASP 81 ENGINEERED MUTATION
SEQADV 9EWR LYS A 109 UNP A0A1I6NU6 ASP 141 ENGINEERED MUTATION
SEQADV 9EWR LYS A 114 UNP A0A1I6NU6 ASP 146 ENGINEERED MUTATION
SEQADV 9EWR LYS A 116 UNP A0A1I6NU6 ASP 148 ENGINEERED MUTATION
SEQADV 9EWR LYS A 147 UNP A0A1I6NU6 ALA 179 ENGINEERED MUTATION
SEQADV 9EWR ARG A 164 UNP A0A1I6NU6 SER 196 ENGINEERED MUTATION
SEQADV 9EWR ARG A 167 UNP A0A1I6NU6 GLN 199 ENGINEERED MUTATION
SEQADV 9EWR GLU A 188 UNP A0A1I6NU6 LYS 220 ENGINEERED MUTATION
SEQADV 9EWR LYS A 192 UNP A0A1I6NU6 GLU 224 ENGINEERED MUTATION
SEQADV 9EWR LYS A 197 UNP A0A1I6NU6 ASP 229 ENGINEERED MUTATION
SEQADV 9EWR ARG A 240 UNP A0A1I6NU6 GLN 272 ENGINEERED MUTATION
SEQADV 9EWR ARG A 247 UNP A0A1I6NU6 GLU 279 ENGINEERED MUTATION
SEQADV 9EWR ASN A 249 UNP A0A1I6NU6 ASP 281 ENGINEERED MUTATION
SEQADV 9EWR LYS A 250 UNP A0A1I6NU6 ASP 282 ENGINEERED MUTATION
SEQADV 9EWR ARG A 256 UNP A0A1I6NU6 GLN 288 ENGINEERED MUTATION
SEQADV 9EWR LYS A 262 UNP A0A1I6NU6 EXPRESSION TAG
SEQADV 9EWR GLU A 263 UNP A0A1I6NU6 EXPRESSION TAG
SEQADV 9EWR HIS A 264 UNP A0A1I6NU6 EXPRESSION TAG
SEQADV 9EWR HIS A 265 UNP A0A1I6NU6 EXPRESSION TAG
SEQADV 9EWR HIS A 266 UNP A0A1I6NU6 EXPRESSION TAG
SEQADV 9EWR HIS A 267 UNP A0A1I6NU6 EXPRESSION TAG
SEQADV 9EWR HIS A 268 UNP A0A1I6NU6 EXPRESSION TAG
SEQADV 9EWR HIS A 269 UNP A0A1I6NU6 EXPRESSION TAG
SEQADV 9EWR MET B 1 UNP A0A1I6NU6 INITIATING METHIONINE
SEQADV 9EWR LYS B 6 UNP A0A1I6NU6 ASP 38 ENGINEERED MUTATION
SEQADV 9EWR LYS B 11 UNP A0A1I6NU6 ASP 43 ENGINEERED MUTATION
SEQADV 9EWR LYS B 19 UNP A0A1I6NU6 ALA 51 ENGINEERED MUTATION
SEQADV 9EWR ASN B 27 UNP A0A1I6NU6 ASP 59 ENGINEERED MUTATION
SEQADV 9EWR ARG B 28 UNP A0A1I6NU6 GLU 60 ENGINEERED MUTATION
SEQADV 9EWR ARG B 29 UNP A0A1I6NU6 GLU 61 ENGINEERED MUTATION
SEQADV 9EWR LYS B 35 UNP A0A1I6NU6 SER 67 ENGINEERED MUTATION
SEQADV 9EWR LYS B 37 UNP A0A1I6NU6 SER 69 ENGINEERED MUTATION
SEQADV 9EWR ASN B 49 UNP A0A1I6NU6 ASP 81 ENGINEERED MUTATION
SEQADV 9EWR LYS B 109 UNP A0A1I6NU6 ASP 141 ENGINEERED MUTATION
SEQADV 9EWR LYS B 114 UNP A0A1I6NU6 ASP 146 ENGINEERED MUTATION
SEQADV 9EWR LYS B 116 UNP A0A1I6NU6 ASP 148 ENGINEERED MUTATION
SEQADV 9EWR LYS B 147 UNP A0A1I6NU6 ALA 179 ENGINEERED MUTATION
SEQADV 9EWR ARG B 164 UNP A0A1I6NU6 SER 196 ENGINEERED MUTATION
SEQADV 9EWR ARG B 167 UNP A0A1I6NU6 GLN 199 ENGINEERED MUTATION
SEQADV 9EWR GLU B 188 UNP A0A1I6NU6 LYS 220 ENGINEERED MUTATION
SEQADV 9EWR LYS B 192 UNP A0A1I6NU6 GLU 224 ENGINEERED MUTATION
SEQADV 9EWR LYS B 197 UNP A0A1I6NU6 ASP 229 ENGINEERED MUTATION
SEQADV 9EWR ARG B 240 UNP A0A1I6NU6 GLN 272 ENGINEERED MUTATION
SEQADV 9EWR ARG B 247 UNP A0A1I6NU6 GLU 279 ENGINEERED MUTATION
SEQADV 9EWR ASN B 249 UNP A0A1I6NU6 ASP 281 ENGINEERED MUTATION
SEQADV 9EWR LYS B 250 UNP A0A1I6NU6 ASP 282 ENGINEERED MUTATION
SEQADV 9EWR ARG B 256 UNP A0A1I6NU6 GLN 288 ENGINEERED MUTATION
SEQADV 9EWR LYS B 262 UNP A0A1I6NU6 EXPRESSION TAG
SEQADV 9EWR GLU B 263 UNP A0A1I6NU6 EXPRESSION TAG
SEQADV 9EWR HIS B 264 UNP A0A1I6NU6 EXPRESSION TAG
SEQADV 9EWR HIS B 265 UNP A0A1I6NU6 EXPRESSION TAG
SEQADV 9EWR HIS B 266 UNP A0A1I6NU6 EXPRESSION TAG
SEQADV 9EWR HIS B 267 UNP A0A1I6NU6 EXPRESSION TAG
SEQADV 9EWR HIS B 268 UNP A0A1I6NU6 EXPRESSION TAG
SEQADV 9EWR HIS B 269 UNP A0A1I6NU6 EXPRESSION TAG
SEQRES 1 A 269 MET ALA GLU PRO ALA LYS VAL HIS GLY PRO LYS PRO THR
SEQRES 2 A 269 GLU GLU SER ILE THR LYS PRO ARG GLY PRO PHE GLU VAL
SEQRES 3 A 269 ASN ARG ARG SER VAL SER ARG LEU LYS VAL LYS GLY PHE
SEQRES 4 A 269 GLY GLY GLY THR ILE TYR TYR PRO THR ASN THR THR ASP
SEQRES 5 A 269 GLY LEU PHE SER ALA VAL SER ILE SER PRO GLY PHE THR
SEQRES 6 A 269 GLY THR GLN GLU THR MET ALA TRP TYR GLY PRO ARG LEU
SEQRES 7 A 269 ALA SER GLN GLY PHE VAL VAL PHE THR ILE ASP THR ILE
SEQRES 8 A 269 THR THR THR ASP GLN PRO ASP SER ARG ALA ARG GLN LEU
SEQRES 9 A 269 GLN ALA SER LEU LYS TYR LEU VAL ASN LYS SER LYS VAL
SEQRES 10 A 269 LYS ASP ILE ILE ASP PRO ALA ARG LEU GLY VAL MET GLY
SEQRES 11 A 269 HIS SER MET GLY GLY GLY GLY SER LEU LYS ALA ALA LEU
SEQRES 12 A 269 ASP ASN PRO LYS LEU LYS ALA ALA ILE PRO LEU THR PRO
SEQRES 13 A 269 TRP HIS THR THR LYS ASP PHE ARG GLY VAL ARG THR PRO
SEQRES 14 A 269 THR LEU ILE ILE GLY ALA GLN ASN ASP THR VAL ALA PRO
SEQRES 15 A 269 VAL SER GLN HIS ALA GLU PRO PHE TYR LYS SER LEU PRO
SEQRES 16 A 269 ASP LYS PRO GLY LYS ALA TYR LEU GLU LEU ALA GLY ALA
SEQRES 17 A 269 SER HIS LEU ALA PRO ASN THR ASP ASN THR THR ILE ALA
SEQRES 18 A 269 LYS PHE SER ILE ALA TRP LEU LYS ARG PHE LEU ASP ASP
SEQRES 19 A 269 ASP THR ARG TYR ASP ARG PHE LEU CYS PRO PRO PRO ARG
SEQRES 20 A 269 ASN ASN LYS SER ILE SER ASP TYR ARG SER THR CYS PRO
SEQRES 21 A 269 TYR LYS GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 269 MET ALA GLU PRO ALA LYS VAL HIS GLY PRO LYS PRO THR
SEQRES 2 B 269 GLU GLU SER ILE THR LYS PRO ARG GLY PRO PHE GLU VAL
SEQRES 3 B 269 ASN ARG ARG SER VAL SER ARG LEU LYS VAL LYS GLY PHE
SEQRES 4 B 269 GLY GLY GLY THR ILE TYR TYR PRO THR ASN THR THR ASP
SEQRES 5 B 269 GLY LEU PHE SER ALA VAL SER ILE SER PRO GLY PHE THR
SEQRES 6 B 269 GLY THR GLN GLU THR MET ALA TRP TYR GLY PRO ARG LEU
SEQRES 7 B 269 ALA SER GLN GLY PHE VAL VAL PHE THR ILE ASP THR ILE
SEQRES 8 B 269 THR THR THR ASP GLN PRO ASP SER ARG ALA ARG GLN LEU
SEQRES 9 B 269 GLN ALA SER LEU LYS TYR LEU VAL ASN LYS SER LYS VAL
SEQRES 10 B 269 LYS ASP ILE ILE ASP PRO ALA ARG LEU GLY VAL MET GLY
SEQRES 11 B 269 HIS SER MET GLY GLY GLY GLY SER LEU LYS ALA ALA LEU
SEQRES 12 B 269 ASP ASN PRO LYS LEU LYS ALA ALA ILE PRO LEU THR PRO
SEQRES 13 B 269 TRP HIS THR THR LYS ASP PHE ARG GLY VAL ARG THR PRO
SEQRES 14 B 269 THR LEU ILE ILE GLY ALA GLN ASN ASP THR VAL ALA PRO
SEQRES 15 B 269 VAL SER GLN HIS ALA GLU PRO PHE TYR LYS SER LEU PRO
SEQRES 16 B 269 ASP LYS PRO GLY LYS ALA TYR LEU GLU LEU ALA GLY ALA
SEQRES 17 B 269 SER HIS LEU ALA PRO ASN THR ASP ASN THR THR ILE ALA
SEQRES 18 B 269 LYS PHE SER ILE ALA TRP LEU LYS ARG PHE LEU ASP ASP
SEQRES 19 B 269 ASP THR ARG TYR ASP ARG PHE LEU CYS PRO PRO PRO ARG
SEQRES 20 B 269 ASN ASN LYS SER ILE SER ASP TYR ARG SER THR CYS PRO
SEQRES 21 B 269 TYR LYS GLU HIS HIS HIS HIS HIS HIS
FORMUL 3 HOH *462(H2 O)
HELIX 1 AA1 THR A 13 LYS A 19 1 7
HELIX 2 AA2 SER A 32 VAL A 36 5 5
HELIX 3 AA3 THR A 67 ALA A 72 5 6
HELIX 4 AA4 TRP A 73 SER A 80 1 8
HELIX 5 AA5 GLN A 96 LYS A 114 1 19
HELIX 6 AA6 VAL A 117 ASP A 119 5 3
HELIX 7 AA7 SER A 132 ASN A 145 1 14
HELIX 8 AA8 HIS A 186 LEU A 194 1 9
HELIX 9 AA9 LEU A 211 THR A 215 5 5
HELIX 10 AB1 ASN A 217 LEU A 232 1 16
HELIX 11 AB2 ASP A 235 LEU A 242 5 8
HELIX 12 AB3 THR B 13 LYS B 19 1 7
HELIX 13 AB4 SER B 32 VAL B 36 5 5
HELIX 14 AB5 THR B 67 ALA B 72 5 6
HELIX 15 AB6 TRP B 73 SER B 80 1 8
HELIX 16 AB7 GLN B 96 LYS B 114 1 19
HELIX 17 AB8 VAL B 117 ASP B 119 5 3
HELIX 18 AB9 SER B 132 ASN B 145 1 14
HELIX 19 AC1 HIS B 186 LEU B 194 1 9
HELIX 20 AC2 LEU B 211 THR B 215 5 5
HELIX 21 AC3 ASN B 217 LEU B 232 1 16
HELIX 22 AC4 ASP B 235 ARG B 237 5 3
HELIX 23 AC5 TYR B 238 CYS B 243 1 6
SHEET 1 AA1 6 VAL A 26 VAL A 31 0
SHEET 2 AA1 6 GLY A 42 PRO A 47 -1 O ILE A 44 N ARG A 29
SHEET 3 AA1 6 VAL A 84 ILE A 88 -1 O VAL A 85 N TYR A 45
SHEET 4 AA1 6 PHE A 55 SER A 61 1 N ILE A 60 O PHE A 86
SHEET 5 AA1 6 ILE A 121 HIS A 131 1 O ASP A 122 N PHE A 55
SHEET 6 AA1 6 ALA A 150 LEU A 154 1 O LEU A 154 N GLY A 130
SHEET 1 AA2 3 THR A 170 ALA A 175 0
SHEET 2 AA2 3 LYS A 200 LEU A 205 1 O LEU A 205 N GLY A 174
SHEET 3 AA2 3 ILE A 252 SER A 257 -1 O ASP A 254 N GLU A 204
SHEET 1 AA3 6 VAL B 26 VAL B 31 0
SHEET 2 AA3 6 GLY B 42 PRO B 47 -1 O ILE B 44 N ARG B 29
SHEET 3 AA3 6 PHE B 83 ILE B 88 -1 O VAL B 85 N TYR B 45
SHEET 4 AA3 6 PHE B 55 SER B 61 1 N ILE B 60 O PHE B 86
SHEET 5 AA3 6 ILE B 121 HIS B 131 1 O ASP B 122 N PHE B 55
SHEET 6 AA3 6 ALA B 150 LEU B 154 1 O LEU B 154 N GLY B 130
SHEET 1 AA4 3 THR B 170 ALA B 175 0
SHEET 2 AA4 3 LYS B 200 LEU B 205 1 O LEU B 205 N GLY B 174
SHEET 3 AA4 3 ILE B 252 SER B 257 -1 O ASP B 254 N GLU B 204
SSBOND 1 CYS A 243 CYS A 259 1555 1555 2.08
SSBOND 2 CYS B 243 CYS B 259 1555 1555 2.06
CISPEP 1 LYS A 197 PRO A 198 0 13.25
CISPEP 2 CYS A 243 PRO A 244 0 -6.57
CISPEP 3 CYS A 259 PRO A 260 0 -3.16
CISPEP 4 LYS B 197 PRO B 198 0 12.64
CISPEP 5 CYS B 243 PRO B 244 0 -2.08
CISPEP 6 CYS B 259 PRO B 260 0 -9.86
CRYST1 46.084 41.316 124.088 90.00 99.82 90.00 P 1 21 1 4
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 0.021700 0.000000 0.003754 0.00000
SCALE2 0.000000 0.024204 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008179 0.00000
TER 2014 LYS A 262
TER 4033 HIS B 264
MASTER 417 0 0 23 18 0 0 6 4456 2 4 42
END |