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HEADER HYDROLASE (SERINE ESTERASE) 28-NOV-95 1XZJ
TITLE FUSARIUM SOLANI CUTINASE MUTANT WITH THR 38 REPLACED BY PHE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CUTINASE;
COMPND 3 CHAIN: NULL;
COMPND 4 EC: 3.1.1.-;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: T38F
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: FUSARIUM SOLANI PISI;
SOURCE 3 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;
SOURCE 4 EXPRESSION_SYSTEM_PLASMID: MIRY;
KEYWDS HYDROLASE, SERINE ESTERASE, GLYCOPROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR S.LONGHI,C.CAMBILLAU
REVDAT 1 14-OCT-96 1XZJ 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,
REMARK 1 AUTH 2 S.LONGHI,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. 1.69 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) : 1.69
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 : 16800
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) : 0.153
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 : 1777
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 672
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 1.46
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 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 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:
REMARK 3 FINAL RMS COORD. SHIFT 0.079 ANGSTROMS
REMARK 3 MEAN B (A**2) MAIN : 9.6
REMARK 3 MEAN B (A**2) SIDE : 19.1
REMARK 3 MEAN B (A**2) SOLVENT : 37.8
REMARK 4
REMARK 4 1XZJ COMPLIES WITH FORMAT V. 2.0, 16-FEB-1996
REMARK 6
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 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : 18 CM IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16961
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 88.0
REMARK 200 DATA REDUNDANCY : 2.9
REMARK 200 R MERGE (I) : 0.020
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 1.30
REMARK 500 H VAL 169 1HD2 ASN 27 1554 1.30
REMARK 500 2HH2 ARG 208 1H HOH 601 2556 1.50
REMARK 500 1H HOH 601 2HH2 ARG 208 2546 1.50
REMARK 500 O HOH 659 2H HOH 502 2546 1.64
REMARK 500 2H HOH 502 O HOH 659 2556 1.64
REMARK 500 2H HOH 548 1H HOH 665 2546 1.68
REMARK 500 1H HOH 598 O HOH 721 1455 1.68
REMARK 500 O HOH 721 1H HOH 598 1655 1.68
REMARK 500 1H HOH 665 2H HOH 548 2556 1.68
REMARK 500 O HOH 635 1H HOH 673 1655 1.70
REMARK 500 1H HOH 673 O HOH 635 1455 1.70
REMARK 500 1H HOH 664 O HOH 666 1554 1.73
REMARK 500 O HOH 626 2H HOH 619 1554 1.73
REMARK 500 2H HOH 619 O HOH 626 1556 1.73
REMARK 500 O HOH 666 1H HOH 664 1556 1.73
REMARK 500 1H HOH 702 O HOH 638 2546 1.74
REMARK 500 O HOH 638 1H HOH 702 2556 1.74
REMARK 500 HG1 THR 173 O HOH 517 1554 1.74
REMARK 500 1H HOH 695 O HOH 563 1456 1.74
REMARK 500 O HOH 563 1H HOH 695 1654 1.74
REMARK 500 O HOH 517 HG1 THR 173 1556 1.74
REMARK 500 1H HOH 665 O HOH 548 2556 1.75
REMARK 500 O HOH 548 1H HOH 665 2546 1.75
REMARK 500 O HOH 556 1H HOH 565 2546 1.77
REMARK 500 1H HOH 565 O HOH 556 2556 1.77
REMARK 500 2H HOH 686 O HOH 588 1556 1.80
REMARK 500 O HOH 690 1H HOH 628 2546 1.80
REMARK 500 1H HOH 628 O HOH 690 2556 1.80
REMARK 500 O HOH 588 2H HOH 686 1554 1.80
REMARK 500 2H HOH 665 O HOH 606 2556 1.81
REMARK 500 O HOH 662 1H HOH 519 1554 1.81
REMARK 500 1H HOH 519 O HOH 662 1556 1.81
REMARK 500 O HOH 606 2H HOH 665 2546 1.81
REMARK 500 1H HOH 594 O HOH 673 1655 1.82
REMARK 500 O HOH 649 2H HOH 721 1455 1.82
REMARK 500 1H HOH 695 2H HOH 563 1456 1.82
REMARK 500 2H HOH 721 O HOH 649 1655 1.82
REMARK 500 2H HOH 563 1H HOH 695 1654 1.82
REMARK 500 O HOH 673 1H HOH 594 1455 1.82
REMARK 500 O HOH 656 2H HOH 545 2556 1.83
REMARK 500 2H HOH 545 O HOH 656 2546 1.83
REMARK 500 1H HOH 679 2H HOH 686 1554 1.84
REMARK 500 2H HOH 686 1H HOH 679 1556 1.84
REMARK 500 O HOH 592 HG1 THR 113 1655 1.84
REMARK 500 HG1 THR 113 O HOH 592 1455 1.84
REMARK 500 O HOH 661 2H HOH 702 2555 1.85
REMARK 500 O HOH 520 H GLY 174 1556 1.85
REMARK 500 H GLY 174 O HOH 520 1554 1.85
REMARK 500 2H ARG 17 O HOH 651 1556 1.86
REMARK 500 O HOH 651 2H ARG 17 1554 1.86
REMARK 500 2HH2 ARG 166 OG1 THR 43 1455 1.86
REMARK 500 OG1 THR 43 2HH2 ARG 166 1655 1.86
REMARK 500 2H HOH 540 O VAL 210 1655 1.86
REMARK 500 O VAL 210 2H HOH 540 1455 1.86
REMARK 500 O ALA 136 1H HOH 544 1455 1.87
REMARK 500 O HOH 567 2H HOH 676 1556 1.87
REMARK 500 2H HOH 676 O HOH 567 1554 1.87
REMARK 500 1H HOH 544 O ALA 136 1655 1.87
REMARK 500 HG1 THR 43 2HH2 ARG 166 1655 1.88
REMARK 500 2HH2 ARG 166 HG1 THR 43 1455 1.88
REMARK 500 O HOH 658 1H HOH 564 1455 1.89
REMARK 500 O HOH 563 2H HOH 666 1654 1.89
REMARK 500 1H HOH 564 O HOH 658 1655 1.89
REMARK 500 2H HOH 666 O HOH 563 1456 1.89
REMARK 500 1HH2 ARG 196 OD1 ASP 132 2556 1.90
REMARK 500 O HOH 502 1H HOH 667 2556 1.90
REMARK 500 OD1 ASP 132 1HH2 ARG 196 2546 1.90
REMARK 500 1H HOH 667 O HOH 502 2546 1.90
REMARK 500 O HOH 573 2H HOH 664 1655 1.90
REMARK 500 O ALA 209 1H HOH 537 1455 1.90
REMARK 500 2H HOH 664 O HOH 573 1455 1.90
REMARK 500 H CYS 31 O HOH 680 1456 1.90
REMARK 500 1H HOH 537 O ALA 209 1655 1.90
REMARK 500 O HOH 680 H CYS 31 1654 1.90
REMARK 500 1H HOH 505 O HOH 572 1455 1.91
REMARK 500 OD2 ASP 139 H GLY 82 1455 1.91
REMARK 500 O HOH 572 1H HOH 505 1655 1.91
REMARK 500 H GLY 82 OD2 ASP 139 1655 1.91
REMARK 500 1H HOH 704 O ARG 211 2446 1.92
REMARK 500 O ARG 211 1H HOH 704 2456 1.92
REMARK 500 1H HOH 585 O HOH 541 1455 1.93
REMARK 500 1H HOH 547 O HOH 581 2546 1.93
REMARK 500 O HOH 541 1H HOH 585 1655 1.93
REMARK 500 O HOH 581 1H HOH 547 2556 1.93
REMARK 500 1HH2 ARG 211 2H HOH 706 2456 1.94
REMARK 500 2H HOH 522 O GLY 157 1556 1.95
REMARK 500 O HOH 686 2H HOH 678 1556 1.95
REMARK 500 2H HOH 661 3HZ LYS 65 1554 1.95
REMARK 500 1H HOH 567 O HOH 681 1556 1.95
REMARK 500 3HZ LYS 65 2H HOH 661 1556 1.95
REMARK 500 O HOH 681 1H HOH 567 1554 1.95
REMARK 500 2H HOH 678 O HOH 686 1554 1.95
REMARK 500 O GLY 157 2H HOH 522 1554 1.95
REMARK 500 HE ARG 211 1H HOH 706 2456 1.96
REMARK 500 HG1 THR 173 2H HOH 517 1554 1.96
REMARK 500 2H HOH 517 HG1 THR 173 1556 1.96
REMARK 500 2H HOH 700 OD1 ASN 58 2546 1.96
REMARK 500 OD1 ASN 58 2H HOH 700 2556 1.96
REMARK 500 O HOH 639 3HZ LYS 151 2556 1.97
REMARK 500 1H HOH 594 1H HOH 673 1655 1.97
REMARK 500 1H HOH 673 1H HOH 594 1455 1.97
REMARK 500 3HZ LYS 151 O HOH 639 2546 1.97
REMARK 500 1H HOH 592 1H HOH 554 1655 1.98
REMARK 500 1H HOH 606 2H HOH 665 2546 1.98
REMARK 500 1H HOH 554 1H HOH 592 1455 1.98
REMARK 500 2H HOH 665 1H HOH 606 2556 1.98
REMARK 500 1H HOH 619 O HOH 676 1556 1.99
REMARK 500 HG1 THR 173 1H HOH 517 1554 1.99
REMARK 500 1H HOH 517 HG1 THR 173 1556 1.99
REMARK 500 O HOH 676 1H HOH 619 1554 1.99
REMARK 500 HE ARG 211 O HOH 706 2456 1.99
REMARK 500 1HD2 ASN 152 O HOH 521 1554 2.00
REMARK 500 O HOH 521 1HD2 ASN 152 1556 2.00
REMARK 500 2H HOH 673 1H HOH 594 1455 2.00
REMARK 500 O HOH 702 3H ARG 17 2546 2.00
REMARK 500 3H ARG 17 O HOH 702 2556 2.00
REMARK 500 1H HOH 594 2H HOH 673 1655 2.00
REMARK 500 2HH1 ARG 208 1H HOH 601 2556 2.01
REMARK 500 HG1 THR 18 O HOH 703 2556 2.01
REMARK 500 O HOH 601 2HH1 ARG 208 2546 2.01
REMARK 500 2HH1 ARG 208 O HOH 601 2556 2.01
REMARK 500 1H HOH 601 2HH1 ARG 208 2546 2.01
REMARK 500 1H HOH 678 2H HOH 686 1554 2.02
REMARK 500 2H HOH 686 1H HOH 678 1556 2.02
REMARK 500 N VAL 169 1HD2 ASN 27 1554 2.02
REMARK 500 1HD2 ASN 27 N VAL 169 1556 2.02
REMARK 500 2H HOH 561 O ASN 25 1554 2.02
REMARK 500 1H HOH 538 O ASP 139 1655 2.02
REMARK 500 O ASN 25 2H HOH 561 1556 2.02
REMARK 500 1HH2 ARG 211 O HOH 706 2456 2.02
REMARK 500 O ASP 139 1H HOH 538 1455 2.02
REMARK 500 OD1 ASP 165 1H HOH 573 1455 2.03
REMARK 500 1H HOH 520 H GLY 174 1556 2.03
REMARK 500 1H HOH 679 O HOH 686 1554 2.03
REMARK 500 1H HOH 573 OD1 ASP 165 1655 2.03
REMARK 500 H GLY 174 1H HOH 520 1554 2.03
REMARK 500 O HOH 686 1H HOH 679 1556 2.03
REMARK 500 O HOH 614 2H HOH 565 2546 2.04
REMARK 500 2H HOH 565 O HOH 614 2556 2.04
REMARK 500 H VAL 169 ND2 ASN 27 1554 2.06
REMARK 500 ND2 ASN 27 H VAL 169 1556 2.06
REMARK 500 O HOH 692 2H HOH 653 2546 2.07
REMARK 500 2H HOH 653 O HOH 692 2556 2.07
REMARK 500 O HOH 702 1H ARG 17 2546 2.08
REMARK 500 1H ARG 17 O HOH 702 2556 2.08
REMARK 500 2H HOH 562 O HOH 695 1654 2.09
REMARK 500 2H HOH 585 O HOH 685 1455 2.09
REMARK 500 O HOH 695 2H HOH 562 1456 2.09
REMARK 500 2HD2 ASN 27 O HOH 655 1556 2.09
REMARK 500 O HOH 685 2H HOH 585 1655 2.09
REMARK 500 O HOH 655 2HD2 ASN 27 1554 2.09
REMARK 500 1H HOH 660 O HOH 582 2546 2.10
REMARK 500 O HOH 582 1H HOH 660 2556 2.10
REMARK 500 1H HOH 519 1H HOH 662 1556 2.11
REMARK 500 1H HOH 666 1H HOH 664 1556 2.11
REMARK 500 1H HOH 662 1H HOH 519 1554 2.11
REMARK 500 1H HOH 664 1H HOH 666 1554 2.11
REMARK 500 2H HOH 646 1HD2 ASN 58 2546 2.12
REMARK 500 1HD2 ASN 58 2H HOH 646 2556 2.12
REMARK 500 2H HOH 585 2H HOH 685 1455 2.14
REMARK 500 2H HOH 649 2H HOH 721 1455 2.14
REMARK 500 O HOH 601 2HH2 ARG 208 2546 2.14
REMARK 500 2H HOH 685 2H HOH 585 1655 2.14
REMARK 500 2H HOH 721 2H HOH 649 1655 2.14
REMARK 500 2HH2 ARG 208 O HOH 601 2556 2.14
REMARK 500 1HD2 ASN 152 1H HOH 521 1554 2.15
REMARK 500 1H HOH 521 1HD2 ASN 152 1556 2.15
REMARK 500 OG SER 92 2H HOH 656 2546 2.16
REMARK 500 O SER 213 1H HOH 707 2456 2.16
REMARK 500 1H HOH 707 O SER 213 2446 2.16
REMARK 500 HG SER 92 2H HOH 656 2546 2.16
REMARK 500 2H HOH 656 OG SER 92 2556 2.16
REMARK 500 2H HOH 563 2H HOH 666 1654 2.16
REMARK 500 2H HOH 666 2H HOH 563 1456 2.16
REMARK 500 2H HOH 656 HG SER 92 2556 2.16
REMARK 500 2H HOH 678 2H HOH 686 1554 2.17
REMARK 500 2H HOH 686 2H HOH 678 1556 2.17
REMARK 500 O HOH 665 2H HOH 611 2556 2.17
REMARK 500 2H HOH 611 O HOH 665 2546 2.17
REMARK 500 1H HOH 573 2H HOH 664 1655 2.18
REMARK 500 1H HOH 609 1H HOH 616 2556 2.18
REMARK 500 1H HOH 616 1H HOH 609 2546 2.18
REMARK 500 2H HOH 664 1H HOH 573 1455 2.18
REMARK 500 2HZ LYS 65 2H HOH 661 1556 2.19
REMARK 500 HG SER 135 O HOH 629 1455 2.19
REMARK 500 2H HOH 535 O HOH 684 1455 2.19
REMARK 500 2H HOH 661 2HZ LYS 65 1554 2.19
REMARK 500 O HOH 629 HG SER 135 1655 2.19
REMARK 500 O HOH 684 2H HOH 535 1655 2.19
REMARK 525
REMARK 525 SOLVENT
REMARK 525 THE FOLLOWING SOLVENT MOLECULES LIE FARTHER THAN EXPECTED
REMARK 525 FROM THE PROTEIN OR NUCLEIC ACID MOLECULE AND MAY BE
REMARK 525 ASSOCIATED WITH A SYMMETRY RELATED MOLECULE (M=MODEL
REMARK 525 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 0 HOH 620 DISTANCE = 7.39 ANGSTROMS
REMARK 525 0 HOH 680 DISTANCE = 5.63 ANGSTROMS
REMARK 525 0 HOH 701 DISTANCE = 6.79 ANGSTROMS
REMARK 525 0 HOH 702 DISTANCE = 6.79 ANGSTROMS
REMARK 525 0 HOH 714 DISTANCE = 6.10 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: CAT
REMARK 800 SITE_DESCRIPTION: CATALYTIC TRIAD.
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 1XZJ SWS P00590 1 - 32 NOT IN ATOMS LIST
REMARK 999 1XZJ SWS P00590 230 - 230 NOT IN ATOMS LIST
DBREF 1XZJ 17 213 SWS P00590 CUTI_FUSSO 33 229
SEQADV 1XZJ ALA 32 SWS P00590 ARG 48 CLONING ARTIFACT
SEQADV 1XZJ PHE 38 SWS P00590 TYR 54 ENGINEERED
SEQRES 1 214 LEU PRO THR SER ASN PRO ALA GLN GLU LEU GLU ALA ARG
SEQRES 2 214 GLN LEU GLU ARG THR THR ARG ASP ASP LEU ILE ASN GLY
SEQRES 3 214 ASN SER ALA SER CYS ALA ASP VAL ILE PHE ILE PHE 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 SER 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 *224(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 LEU 81 ALA 85 5 5
HELIX 5 5 SER 92 LYS 108 1 17
HELIX 6 6 SER 120 ASP 132 5 13
HELIX 7 7 SER 135 LYS 140 1 6
HELIX 8 8 ALA 164 ARG 166 5 3
HELIX 9 9 LEU 176 THR 179 5 4
HELIX 10 10 ALA 186 LEU 189 5 4
HELIX 11 11 GLY 192 ARG 196 1 5
HELIX 12 12 PRO 198 ARG 211 1 14
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 ILE 141 PHE 147 1 N ALA 142 O LEU 114
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 SER 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 |