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HEADER HYDROLASE (SERINE ESTERASE) 16-NOV-95 1CUJ
TITLE CUTINASE, S120C MUTANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CUTINASE;
COMPND 3 CHAIN: NULL;
COMPND 4 EC: 3.1.1.3;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: S120C
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: FUSARIUM SOLANI PISI;
SOURCE 3 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 4 EXPRESSION_SYSTEM_PLASMID: PUC19
KEYWDS HYDROLASE, SERINE ESTERASE, GLYCOPROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR C.MARTINEZ,C.CAMBILLAU
REVDAT 1 11-JUL-96 1CUJ 0
JRNL AUTH S.LONGHI,A.NICOLAS,L.CREVELD,M.EGMOND,C.T.VERRIPS,
JRNL AUTH 2 J.DE VLIEG,C.MARTINEZ,C.CAMBILLAU
JRNL TITL DYNAMICS OF FUSARIUM SOLANI CUTINASE INVESTIGATED
JRNL TITL 2 THROUGH STRUCTURAL COMPARISON AMONG DIFFERENT
JRNL TITL 3 CRYSTAL FORMS OF ITS VARIANTS
JRNL REF TO BE PUBLISHED REF NOW ASSIGNED AS
JRNL REFN 0353
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH A.NICOLAS,M.EGMOND,C.T.VERRIPS,J.DE VLIEG,S.LONGHI,
REMARK 1 AUTH 2 C.CAMBILLAU,C.MARTINEZ
REMARK 1 TITL CONTRIBUTION OF CUTINASE SER 42 SIDE-CHAIN TO THE
REMARK 1 TITL 2 STABILIZATION OF THE OXYANION TRANSITION STATE
REMARK 1 REF TO BE PUBLISHED REF NOW ASSIGNED AS
REMARK 1 REFN 0353
REMARK 1 REFERENCE 2
REMARK 1 AUTH C.MARTINEZ,A.NICOLAS,H.VAN TILBEURGH,M.P.EGLOFF,
REMARK 1 AUTH 2 C.CUDREY,R.VERGER,C.CAMBILLAU
REMARK 1 TITL CUTINASE, A LIPOLYTIC ENZYME WITH A PREFORMED
REMARK 1 TITL 2 OXYANION HOLE
REMARK 1 REF BIOCHEMISTRY V. 33 83 1994
REMARK 1 REFN ASTM BICHAW US ISSN 0006-2960 0033
REMARK 1 REFERENCE 3
REMARK 1 AUTH C.MARTINEZ,P.DE GEUS,P.STANSSENS,M.LAUWEREYS,
REMARK 1 AUTH 2 C.CAMBILLAU
REMARK 1 TITL ENGINEERING CYSTEINE MUTANTS TO OBTAIN
REMARK 1 TITL 2 CRYSTALLOGRAPHIC PHASES WITH A CUTINASE FROM
REMARK 1 TITL 3 FUSARIUM SOLANI PISI
REMARK 1 REF PROTEIN ENG. V. 6 157 1993
REMARK 1 REFN ASTM PRENE9 UK ISSN 0269-2139 0859
REMARK 1 REFERENCE 4
REMARK 1 AUTH C.MARTINEZ,P.DE GEUS,M.LAUWEREYS,G.MATTHYSSENS,
REMARK 1 AUTH 2 C.CAMBILLAU
REMARK 1 TITL FUSARIUM SOLANI CUTINASE IS A LIPOLYTIC ENZYME
REMARK 1 TITL 2 WITH A CATALYTIC SERINE ACCESSIBLE TO SOLVENT
REMARK 1 REF NATURE V. 356 615 1992
REMARK 1 REFN ASTM NATUAS UK ISSN 0028-0836 0006
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 6.0
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 20014
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.156
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 COMPLETENESS IN THIS BIN (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1778
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 639
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 44.0
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.022
REMARK 3 BOND ANGLES (DEGREES) : 2.27
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 0 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 0 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 PARAMETER FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1CUJ COMPLIES WITH FORMAT V. 2.0, 16-FEB-1996
REMARK 6
REMARK 6 SER 120:
REMARK 6 THE "EPSILON" CONFORMATION OF THE CATALYTIC SERINE IS A
REMARK 6 TYPICAL FEATURE OF THE ALPHA/BETA HYDROLASE FAMILY, WHICH
REMARK 6 CUTINASE BELONGS TO.
REMARK 7
REMARK 7 THE FIRST 16 N-TERMINAL RESIDUES AND LAST C-TERMINAL
REMARK 7 RESIDUE ARE NOT OBSERVED IN THE ELECTRON DENSITY. THEY
REMARK 7 ARE NOT INCLUDED IN THIS ENTRY.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 293
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU200 ROTATING
REMARK 200 ANODE
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRAPHITE CRYSTAL
REMARK 200 OPTICS : COLLIMATOR
REMARK 200
REMARK 200 DETECTOR TYPE : X100A
REMARK 200 DETECTOR MANUFACTURER : SIEMENS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21942
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 83.0
REMARK 200 DATA REDUNDANCY : 2.8 %
REMARK 200 R MERGE (I) : 0.044
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 37.
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 33.67910
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 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. SOME OF THESE MAY BE ATOMS
REMARK 500 LOCATED ON SPECIAL POSITIONS IN THE CELL.
REMARK 500
REMARK 500 DISTANCE CUTOFF: 2.2 ANGSTROMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 1HD2 ASN 27 H VAL 169 1556 1.45
REMARK 500 H VAL 169 1HD2 ASN 27 1554 1.45
REMARK 500 1H HOH 616 2HH2 ARG 196 2546 1.57
REMARK 500 2HH2 ARG 196 1H HOH 616 2556 1.57
REMARK 500 1HH2 ARG 96 1H HOH 650 2547 1.72
REMARK 500 1H HOH 650 1HH2 ARG 96 2557 1.72
REMARK 500 O HOH 698 2H HOH 640 1556 1.83
REMARK 500 2H HOH 640 O HOH 698 1554 1.83
REMARK 500 O HOH 510 1H HOH 523 1554 1.83
REMARK 500 O HOH 597 2H HOH 651 1554 1.83
REMARK 500 2H HOH 651 O HOH 597 1556 1.83
REMARK 500 1H HOH 523 O HOH 510 1556 1.83
REMARK 500 2HH2 ARG 166 OG1 THR 43 1455 1.85
REMARK 500 OG1 THR 43 2HH2 ARG 166 1655 1.85
REMARK 500 1H HOH 546 O HOH 605 1655 1.86
REMARK 500 H GLY 174 O HOH 523 1554 1.86
REMARK 500 O HOH 605 1H HOH 546 1455 1.86
REMARK 500 O HOH 572 2H HOH 583 1554 1.86
REMARK 500 O HOH 523 H GLY 174 1556 1.86
REMARK 500 2H HOH 583 O HOH 572 1556 1.86
REMARK 500 2H HOH 520 OG1 THR 173 1556 1.87
REMARK 500 O VAL 210 1H HOH 545 1455 1.87
REMARK 500 O HOH 525 1H HOH 670 1556 1.87
REMARK 500 O HOH 701 2H HOH 599 2546 1.87
REMARK 500 O ASP 139 1H HOH 543 1455 1.87
REMARK 500 2H HOH 663 O HOH 542 1455 1.87
REMARK 500 OG1 THR 173 2H HOH 520 1554 1.87
REMARK 500 O HOH 542 2H HOH 663 1655 1.87
REMARK 500 1H HOH 670 O HOH 525 1554 1.87
REMARK 500 1H HOH 666 2H HOH 532 1455 1.87
REMARK 500 2H HOH 532 1H HOH 666 1655 1.87
REMARK 500 1H HOH 543 O ASP 139 1655 1.87
REMARK 500 2H HOH 599 O HOH 701 2556 1.87
REMARK 500 1H HOH 545 O VAL 210 1655 1.87
REMARK 500 1H HOH 665 O HOH 611 1455 1.88
REMARK 500 3HZ LYS 206 1H HOH 589 1455 1.88
REMARK 500 O HOH 611 1H HOH 665 1655 1.88
REMARK 500 1H HOH 589 3HZ LYS 206 1655 1.88
REMARK 500 O HOH 583 1H HOH 636 1556 1.89
REMARK 500 1H HOH 705 O HOH 577 2546 1.89
REMARK 500 1H HOH 697 O HOH 564 1655 1.89
REMARK 500 O HOH 577 1H HOH 705 2556 1.89
REMARK 500 O HOH 663 1H HOH 611 1455 1.89
REMARK 500 O HOH 564 1H HOH 697 1455 1.89
REMARK 500 2HH1 ARG 196 1H HOH 616 2556 1.89
REMARK 500 1H HOH 636 O HOH 583 1554 1.89
REMARK 500 1H HOH 611 O HOH 663 1655 1.89
REMARK 500 1H HOH 616 2HH1 ARG 196 2546 1.89
REMARK 500 1HH1 ARG 196 2H HOH 692 2556 1.90
REMARK 500 O HOH 577 1H HOH 616 2556 1.90
REMARK 500 OD1 ASN 25 1H HOH 510 1556 1.90
REMARK 500 2H HOH 619 O ASP 165 1556 1.90
REMARK 500 1H HOH 616 O HOH 577 2546 1.90
REMARK 500 1H HOH 510 OD1 ASN 25 1554 1.90
REMARK 500 2H HOH 692 1HH1 ARG 196 2546 1.90
REMARK 500 O HOH 666 2H HOH 586 1455 1.90
REMARK 500 2H HOH 586 O HOH 666 1655 1.90
REMARK 500 O ASP 165 2H HOH 619 1554 1.90
REMARK 500 1H HOH 602 O ALA 85 2556 1.90
REMARK 500 O ALA 85 1H HOH 602 2546 1.90
REMARK 500 HG1 THR 173 O HOH 679 1554 1.91
REMARK 500 O ASN 25 2H HOH 573 1556 1.91
REMARK 500 O HOH 679 HG1 THR 173 1556 1.91
REMARK 500 2H HOH 573 O ASN 25 1554 1.91
REMARK 500 1H HOH 659 3HZ LYS 168 1556 1.92
REMARK 500 2HH1 ARG 196 O HOH 616 2556 1.92
REMARK 500 1HH2 ARG 196 OD1 ASP 132 2556 1.92
REMARK 500 1H HOH 681 O HOH 670 1556 1.92
REMARK 500 2H HOH 554 O HOH 653 2547 1.92
REMARK 500 OD1 ASP 132 1HH2 ARG 196 2546 1.92
REMARK 500 2H HOH 589 O HOH 569 1655 1.92
REMARK 500 O HOH 569 2H HOH 589 1455 1.92
REMARK 500 3HZ LYS 168 1H HOH 659 1554 1.92
REMARK 500 O HOH 670 1H HOH 681 1554 1.92
REMARK 500 O HOH 653 2H HOH 554 2557 1.92
REMARK 500 O HOH 616 2HH1 ARG 196 2546 1.92
REMARK 500 O ALA 136 1H HOH 551 1455 1.93
REMARK 500 O HOH 665 2H HOH 532 1455 1.93
REMARK 500 1H HOH 551 O ALA 136 1655 1.93
REMARK 500 2H HOH 532 O HOH 665 1655 1.93
REMARK 500 HG1 THR 19 2H HOH 677 1556 1.94
REMARK 500 2H HOH 621 OG1 THR 113 1655 1.94
REMARK 500 OG1 THR 113 2H HOH 621 1455 1.94
REMARK 500 2H HOH 677 HG1 THR 19 1554 1.94
REMARK 500 2H HOH 692 O HOH 592 2546 1.94
REMARK 500 O HOH 592 2H HOH 692 2556 1.94
REMARK 500 O HOH 581 1H HOH 640 1556 1.94
REMARK 500 1H HOH 640 O HOH 581 1554 1.94
REMARK 500 2H HOH 620 O HOH 576 1456 1.94
REMARK 500 O HOH 576 2H HOH 620 1654 1.94
REMARK 500 2H HOH 721 O HOH 638 1655 1.95
REMARK 500 O HOH 638 2H HOH 721 1455 1.95
REMARK 500 O ALA 209 2H HOH 542 1455 1.95
REMARK 500 2H HOH 542 O ALA 209 1655 1.95
REMARK 500 O HOH 636 2H HOH 659 1554 1.96
REMARK 500 2H HOH 659 O HOH 636 1556 1.96
REMARK 500 1H HOH 715 O HOH 639 1556 1.97
REMARK 500 O HOH 639 1H HOH 715 1554 1.97
REMARK 500 O HOH 657 1H HOH 644 1556 1.97
REMARK 500 1H HOH 644 O HOH 657 1554 1.97
REMARK 500 1H HOH 624 O HOH 672 1556 1.98
REMARK 500 O HOH 672 1H HOH 624 1554 1.98
REMARK 500 2H HOH 577 1H HOH 705 2556 1.99
REMARK 500 O SER 61 2H HOH 716 2556 1.99
REMARK 500 1H HOH 705 2H HOH 577 2546 1.99
REMARK 500 2H HOH 555 O HOH 599 2546 1.99
REMARK 500 O HOH 599 2H HOH 555 2556 1.99
REMARK 500 2H HOH 716 O SER 61 2546 1.99
REMARK 500 2H HOH 629 O PRO 87 2556 2.00
REMARK 500 OH TYR 119 1H HOH 663 1655 2.00
REMARK 500 1H HOH 587 O HOH 507 1655 2.00
REMARK 500 O HOH 507 1H HOH 587 1455 2.00
REMARK 500 1H HOH 663 OH TYR 119 1455 2.00
REMARK 500 N VAL 169 1HD2 ASN 27 1554 2.00
REMARK 500 O PRO 87 2H HOH 629 2546 2.00
REMARK 500 1HD2 ASN 27 N VAL 169 1556 2.00
REMARK 500 1H HOH 623 O SER 213 1655 2.01
REMARK 500 1HD2 ASN 152 O HOH 524 1554 2.01
REMARK 500 O SER 213 1H HOH 623 1455 2.01
REMARK 500 O HOH 524 1HD2 ASN 152 1556 2.01
REMARK 500 1H HOH 581 1H HOH 640 1556 2.02
REMARK 500 1H HOH 640 1H HOH 581 1554 2.02
REMARK 500 1H HOH 670 2H HOH 525 1554 2.02
REMARK 500 O HOH 677 1H HOH 624 1554 2.02
REMARK 500 1H HOH 624 O HOH 677 1556 2.02
REMARK 500 2H HOH 525 1H HOH 670 1556 2.02
REMARK 500 2H HOH 658 O HOH 603 1556 2.03
REMARK 500 2H HOH 677 1H HOH 624 1554 2.03
REMARK 500 1H HOH 624 2H HOH 677 1556 2.03
REMARK 500 O HOH 603 2H HOH 658 1554 2.03
REMARK 500 O HOH 623 2H HOH 565 1655 2.04
REMARK 500 O HOH 666 2H HOH 532 1455 2.04
REMARK 500 O HOH 575 1H HOH 620 1654 2.04
REMARK 500 1H HOH 620 O HOH 575 1456 2.04
REMARK 500 2H HOH 565 O HOH 623 1455 2.04
REMARK 500 2H HOH 532 O HOH 666 1655 2.04
REMARK 500 1H HOH 714 O HOH 615 2556 2.05
REMARK 500 OD2 ASP 139 H GLY 82 1455 2.05
REMARK 500 H GLY 82 OD2 ASP 139 1655 2.05
REMARK 500 1H HOH 727 O ARG 156 1556 2.05
REMARK 500 O ARG 156 1H HOH 727 1554 2.05
REMARK 500 O HOH 615 1H HOH 714 2546 2.05
REMARK 500 1H HOH 629 O HOH 690 2556 2.06
REMARK 500 O HOH 690 1H HOH 629 2546 2.06
REMARK 500 2H HOH 614 OG SER 57 2546 2.06
REMARK 500 OG SER 57 2H HOH 614 2556 2.06
REMARK 500 1H HOH 715 1H HOH 639 1556 2.07
REMARK 500 1H HOH 624 1H HOH 677 1556 2.07
REMARK 500 O ALA 164 2H HOH 525 1554 2.07
REMARK 500 1H HOH 677 1H HOH 624 1554 2.07
REMARK 500 2H HOH 525 O ALA 164 1556 2.07
REMARK 500 1H HOH 639 1H HOH 715 1554 2.07
REMARK 500 2H HOH 589 1H HOH 569 1655 2.08
REMARK 500 1H HOH 569 2H HOH 589 1455 2.08
REMARK 500 O SER 61 1H HOH 686 2556 2.08
REMARK 500 1H HOH 686 O SER 61 2546 2.08
REMARK 500 2H HOH 595 O HOH 651 1554 2.09
REMARK 500 2H HOH 677 OG1 THR 19 1554 2.09
REMARK 500 1H HOH 681 2H HOH 670 1556 2.09
REMARK 500 OG1 THR 19 2H HOH 677 1556 2.09
REMARK 500 2H HOH 670 1H HOH 681 1554 2.09
REMARK 500 O HOH 651 2H HOH 595 1556 2.09
REMARK 500 HH TYR 119 1H HOH 663 1655 2.10
REMARK 500 O HOH 558 2H HOH 654 2547 2.10
REMARK 500 2H HOH 503 O HOH 636 1556 2.10
REMARK 500 1H HOH 663 HH TYR 119 1455 2.10
REMARK 500 2H HOH 654 O HOH 558 2557 2.10
REMARK 500 O HOH 629 1H HOH 689 2556 2.10
REMARK 500 1H HOH 689 O HOH 629 2546 2.10
REMARK 500 O HOH 636 2H HOH 503 1554 2.10
REMARK 500 OG SER 54 1H HOH 691 2556 2.11
REMARK 500 1H HOH 691 OG SER 54 2546 2.11
REMARK 500 2H HOH 557 O HOH 653 2547 2.13
REMARK 500 O HOH 653 2H HOH 557 2557 2.13
REMARK 500 1H HOH 524 1HD2 ASN 152 1556 2.15
REMARK 500 2H HOH 588 OD1 ASP 165 1655 2.15
REMARK 500 OD1 ASP 165 2H HOH 588 1455 2.15
REMARK 500 1HD2 ASN 152 1H HOH 524 1554 2.15
REMARK 500 1H HOH 603 2H HOH 658 1554 2.17
REMARK 500 2H HOH 658 1H HOH 603 1556 2.17
REMARK 500 O THR 167 1H HOH 525 1554 2.17
REMARK 500 1H HOH 611 2H HOH 663 1655 2.17
REMARK 500 2H HOH 663 1H HOH 611 1455 2.17
REMARK 500 1H HOH 525 O THR 167 1556 2.17
REMARK 500 O HOH 649 2H HOH 596 1556 2.18
REMARK 500 1H HOH 564 1H HOH 697 1455 2.18
REMARK 500 2H HOH 565 2H HOH 623 1455 2.18
REMARK 500 1H HOH 697 1H HOH 564 1655 2.18
REMARK 500 2H HOH 596 O HOH 649 1554 2.18
REMARK 500 2H HOH 623 2H HOH 565 1655 2.18
REMARK 500 2H HOH 679 HG1 THR 173 1556 2.19
REMARK 500 2H HOH 696 2H HOH 564 1655 2.19
REMARK 500 HG1 THR 173 2H HOH 679 1554 2.19
REMARK 500 2H HOH 564 2H HOH 696 1455 2.19
REMARK 500 1H HOH 583 H CYS 171 1556 2.20
REMARK 500 H CYS 171 1H HOH 583 1554 2.20
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: CAT
REMARK 800 SITE_DESCRIPTION: CATALYTIC TRIAD. IN THE S120C
REMARK 800 STRUCTURE, SER 120 HAS BEEN SUBSTITUTED BY CYS.
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 1CUJ SWS P00590 1 - 32 NOT IN ATOMS LIST
REMARK 999 1CUJ SWS P00590 230 - 230 NOT IN ATOMS LIST
DBREF 1CUJ 17 213 SWS P00590 CUTI_FUSSO 33 229
SEQADV 1CUJ ALA 32 SWS P00590 ARG 48 CONFLICT
SEQADV 1CUJ CYS 120 SWS P00590 SER 136 ENGINEERED
SEQRES 1 214 LEU PRO THR SER ASN PRO ALA GLN GLU LEU GLU ALA ARG
SEQRES 2 214 GLN LEU GLY ARG THR THR ARG ASP ASP LEU ILE ASN GLY
SEQRES 3 214 ASN SER ALA SER CYS ALA ASP VAL ILE PHE ILE TYR ALA
SEQRES 4 214 ARG GLY SER THR GLU THR GLY ASN LEU GLY THR LEU GLY
SEQRES 5 214 PRO SER ILE ALA SER ASN LEU GLU SER ALA PHE GLY LYS
SEQRES 6 214 ASP GLY VAL TRP ILE GLN GLY VAL GLY GLY ALA TYR ARG
SEQRES 7 214 ALA THR LEU GLY ASP ASN ALA LEU PRO ARG GLY THR SER
SEQRES 8 214 SER ALA ALA ILE ARG GLU MET LEU GLY LEU PHE GLN GLN
SEQRES 9 214 ALA ASN THR LYS CYS PRO ASP ALA THR LEU ILE ALA GLY
SEQRES 10 214 GLY TYR CYS GLN GLY ALA ALA LEU ALA ALA ALA SER ILE
SEQRES 11 214 GLU ASP LEU ASP SER ALA ILE ARG ASP LYS ILE ALA GLY
SEQRES 12 214 THR VAL LEU PHE GLY TYR THR LYS ASN LEU GLN ASN ARG
SEQRES 13 214 GLY ARG ILE PRO ASN TYR PRO ALA ASP ARG THR LYS VAL
SEQRES 14 214 PHE CYS ASN THR GLY ASP LEU VAL CYS THR GLY SER LEU
SEQRES 15 214 ILE VAL ALA ALA PRO HIS LEU ALA TYR GLY PRO ASP ALA
SEQRES 16 214 ARG GLY PRO ALA PRO GLU PHE LEU ILE GLU LYS VAL ARG
SEQRES 17 214 ALA VAL ARG GLY SER ALA
FORMUL 2 HOH *213(H2 O1)
HELIX 1 1 ASP 22 ASN 25 1 4
HELIX 2 2 SER 28 SER 30 5 3
HELIX 3 3 GLY 49 PHE 63 1 15
HELIX 4 4 LYS 65 GLY 67 5 3
HELIX 5 5 LEU 81 ALA 85 5 5
HELIX 6 6 SER 92 LYS 108 1 17
HELIX 7 7 CYS 120 ASP 132 5 13
HELIX 8 8 SER 135 LYS 140 1 6
HELIX 9 9 ALA 164 ARG 166 5 3
HELIX 10 10 LEU 176 THR 179 5 4
HELIX 11 11 ALA 186 LEU 189 5 4
HELIX 12 12 GLY 192 ARG 196 1 5
HELIX 13 13 PRO 198 VAL 210 1 13
SHEET 1 A 5 VAL 68 GLY 72 0
SHEET 2 A 5 VAL 34 ALA 39 1 N VAL 34 O TRP 69
SHEET 3 A 5 THR 113 TYR 119 1 N THR 113 O ILE 35
SHEET 4 A 5 THR 144 PHE 147 1 N VAL 145 O ALA 116
SHEET 5 A 5 THR 167 PHE 170 1 N LYS 168 O THR 144
SSBOND 1 CYS 31 CYS 109
SSBOND 2 CYS 171 CYS 178
SITE 1 CAT 3 CYS 120 HIS 188 ASP 175
CRYST1 35.120 67.360 37.050 90.00 93.90 90.00 P 1 21 1 2
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 0.028474 0.000000 0.001941 0.00000
SCALE2 0.000000 0.014846 0.000000 0.00000
SCALE3 0.000000 0.000000 0.027053 0.00000 |