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HEADER HYDROLASE (SERINE ESTERASE) 28-NOV-95 1XZL
TITLE FUSARIUM SOLANI CUTINASE COMPLEX WITH N-HEXYLPHOSPHONATE
TITLE 2 ETHYL ESTER
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CUTINASE;
COMPND 3 CHAIN: NULL;
COMPND 4 EC: 3.1.1.-;
COMPND 5 ENGINEERED: YES;
COMPND 6 OTHER_DETAILS: COMPLEX WITH N-HEXYLPHOSPHONATE ETHYL ESTER
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: FUSARIUM SOLANI PISI;
SOURCE 3 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 4 EXPRESSION_SYSTEM_PLASMID: PUC 19;
KEYWDS HYDROLASE, SERINE ESTERASE, GLYCOPROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR S.LONGHI,C.CAMBILLAU
REVDAT 1 30-NOV-96 1XZL 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.C.LAU,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 : 16898
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) : 0.141
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 : 11
REMARK 3 SOLVENT ATOMS : 723
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) : 1.49
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 (A): 0.010
REMARK 3 MEAN B (A**2) MAIN : 9.4
REMARK 3 MEAN B (A**2) SIDE : 20.6
REMARK 3 MEAN B (A**2) SOLVENT : 43.1
REMARK 4
REMARK 4 1XZL 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 7
REMARK 7 THERE IS A COVALENT BOND BETWEEN OG OF RESIDUE SER 120 AND
REMARK 7 THE PHOSPHATE OF THE N-HEXYLPHOSPHONATE ETHYL ESTER
REMARK 7 INHIBITOR.
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 : NULL
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 : 17053
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 : 3.7
REMARK 200 R MERGE (I) : 0.026
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 2H HOH 710 2HH2 ARG 208 2546 1.22
REMARK 500 2HH2 ARG 208 2H HOH 710 2556 1.22
REMARK 500 1HD2 ASN 27 H VAL 169 1556 1.25
REMARK 500 H VAL 169 1HD2 ASN 27 1554 1.25
REMARK 500 2HH2 ARG 166 HG1 THR 43 1455 1.31
REMARK 500 HG1 THR 43 2HH2 ARG 166 1655 1.31
REMARK 500 2HH1 ARG 196 2H HOH 722 2556 1.50
REMARK 500 2H HOH 722 2HH1 ARG 196 2546 1.50
REMARK 500 O HOH 570 1H HOH 695 1655 1.63
REMARK 500 1H HOH 695 O HOH 570 1455 1.63
REMARK 500 O HOH 656 2H ARG 17 1554 1.68
REMARK 500 1H HOH 694 2HH2 ARG 211 1655 1.68
REMARK 500 2HH2 ARG 211 1H HOH 694 1455 1.68
REMARK 500 2H ARG 17 O HOH 656 1556 1.68
REMARK 500 1H HOH 722 O HOH 564 2546 1.71
REMARK 500 O HOH 564 1H HOH 722 2556 1.71
REMARK 500 O HOH 617 1H HOH 739 1554 1.72
REMARK 500 1H HOH 739 O HOH 617 1556 1.72
REMARK 500 O HOH 735 1H HOH 692 2646 1.76
REMARK 500 O HOH 690 1H HOH 571 1455 1.79
REMARK 500 O HOH 707 2H HOH 589 1554 1.79
REMARK 500 O HOH 583 2H HOH 540 1455 1.79
REMARK 500 2H HOH 540 O HOH 583 1655 1.79
REMARK 500 1H HOH 571 O HOH 690 1655 1.79
REMARK 500 2H HOH 589 O HOH 707 1556 1.79
REMARK 500 1H HOH 539 O VAL 210 1655 1.81
REMARK 500 O VAL 210 1H HOH 539 1455 1.81
REMARK 500 1H HOH 694 2HH1 ARG 211 1655 1.83
REMARK 500 O HOH 664 2H HOH 502 2546 1.83
REMARK 500 2H HOH 502 O HOH 664 2556 1.83
REMARK 500 2HH1 ARG 211 1H HOH 694 1455 1.83
REMARK 500 O HOH 745 2H HOH 666 1556 1.84
REMARK 500 1HE2 GLN 104 O HOH 718 1556 1.84
REMARK 500 2H HOH 590 OG1 THR 113 1655 1.84
REMARK 500 OG1 THR 113 2H HOH 590 1455 1.84
REMARK 500 O HOH 718 1HE2 GLN 104 1554 1.84
REMARK 500 2H HOH 666 O HOH 745 1554 1.84
REMARK 500 1H HOH 735 1H HOH 692 2646 1.85
REMARK 500 2H HOH 721 O HOH 593 2546 1.86
REMARK 500 1H HOH 551 O HOH 673 2547 1.86
REMARK 500 O HOH 593 2H HOH 721 2556 1.86
REMARK 500 O HOH 673 1H HOH 551 2557 1.86
REMARK 500 O HOH 599 2H HOH 596 1556 1.87
REMARK 500 O HOH 697 1H HOH 612 1655 1.87
REMARK 500 1H HOH 612 O HOH 697 1455 1.87
REMARK 500 2H HOH 596 O HOH 599 1554 1.87
REMARK 500 1H HOH 718 O HOH 511 1554 1.88
REMARK 500 2H HOH 537 O ASP 139 1655 1.88
REMARK 500 O HOH 712 HG SER 135 1655 1.88
REMARK 500 O HOH 511 1H HOH 718 1556 1.88
REMARK 500 HG SER 135 O HOH 712 1455 1.88
REMARK 500 O ASP 139 2H HOH 537 1455 1.88
REMARK 500 2H HOH 610 O HOH 688 2546 1.89
REMARK 500 O HOH 688 2H HOH 610 2556 1.89
REMARK 500 2HH2 ARG 166 OG1 THR 43 1455 1.89
REMARK 500 OG1 THR 43 2HH2 ARG 166 1655 1.89
REMARK 500 O HOH 520 H GLY 174 1556 1.90
REMARK 500 OG1 THR 173 2H HOH 517 1554 1.90
REMARK 500 H GLY 174 O HOH 520 1554 1.90
REMARK 500 1HH2 ARG 196 OD1 ASP 132 2556 1.90
REMARK 500 2H HOH 517 OG1 THR 173 1556 1.90
REMARK 500 OD1 ASP 132 1HH2 ARG 196 2546 1.90
REMARK 500 O HOH 694 2HH2 ARG 211 1655 1.91
REMARK 500 O HOH 546 2H HOH 579 2546 1.91
REMARK 500 O ASN 25 2H HOH 560 1556 1.91
REMARK 500 O HOH 521 1HD2 ASN 152 1556 1.91
REMARK 500 1HD2 ASN 152 O HOH 521 1554 1.91
REMARK 500 2H HOH 579 O HOH 546 2556 1.91
REMARK 500 2HH2 ARG 211 O HOH 694 1455 1.91
REMARK 500 2H HOH 560 O ASN 25 1554 1.91
REMARK 500 O HOH 722 2HH1 ARG 196 2546 1.92
REMARK 500 2HH1 ARG 196 O HOH 722 2556 1.92
REMARK 500 O HOH 667 1H HOH 519 1554 1.94
REMARK 500 2H HOH 502 1H HOH 664 2556 1.94
REMARK 500 1H HOH 664 2H HOH 502 2546 1.94
REMARK 500 1H HOH 519 O HOH 667 1556 1.94
REMARK 500 O ALA 209 1H HOH 536 1455 1.95
REMARK 500 1H HOH 536 O ALA 209 1655 1.95
REMARK 500 2H HOH 555 O HOH 564 2546 1.97
REMARK 500 O HOH 564 2H HOH 555 2556 1.97
REMARK 500 OD2 ASP 139 H GLY 82 1455 1.98
REMARK 500 H GLY 82 OD2 ASP 139 1655 1.98
REMARK 500 O HOH 502 1H HOH 672 2556 1.99
REMARK 500 1H HOH 672 O HOH 502 2546 1.99
REMARK 500 1H HOH 745 2H HOH 666 1556 2.00
REMARK 500 ND2 ASN 27 H VAL 169 1556 2.00
REMARK 500 H VAL 169 ND2 ASN 27 1554 2.00
REMARK 500 2H HOH 666 1H HOH 745 1554 2.00
REMARK 500 O HOH 678 2H HOH 562 1456 2.00
REMARK 500 2H HOH 562 O HOH 678 1654 2.00
REMARK 500 O HOH 553 1H HOH 592 1455 2.01
REMARK 500 O HOH 747 2H HOH 520 1554 2.01
REMARK 500 N VAL 169 1HD2 ASN 27 1554 2.01
REMARK 500 1HD2 ASN 27 N VAL 169 1556 2.01
REMARK 500 2H HOH 520 O HOH 747 1556 2.01
REMARK 500 1H HOH 592 O HOH 553 1655 2.01
REMARK 500 O HOH 586 2H HOH 703 1654 2.02
REMARK 500 1HE2 GLN 104 1H HOH 718 1556 2.02
REMARK 500 2H HOH 703 O HOH 586 1456 2.02
REMARK 500 2H HOH 588 O GLY 212 1655 2.02
REMARK 500 O GLY 212 2H HOH 588 1455 2.02
REMARK 500 1H HOH 718 1HE2 GLN 104 1554 2.02
REMARK 500 O ALA 136 2H HOH 714 1455 2.03
REMARK 500 2H HOH 714 O ALA 136 1655 2.03
REMARK 500 1H HOH 656 O THR 19 1554 2.04
REMARK 500 O THR 19 1H HOH 656 1556 2.04
REMARK 500 O HOH 616 1H HOH 671 1554 2.04
REMARK 500 1H HOH 671 O HOH 616 1556 2.04
REMARK 500 O HOH 710 2HH2 ARG 208 2546 2.05
REMARK 500 1H HOH 721 1HH1 ARG 196 2546 2.05
REMARK 500 2HH2 ARG 208 O HOH 710 2556 2.05
REMARK 500 1HH1 ARG 196 1H HOH 721 2556 2.05
REMARK 500 1H HOH 663 O HOH 563 1455 2.07
REMARK 500 O HOH 563 1H HOH 663 1655 2.07
REMARK 500 2H HOH 617 1H HOH 739 1554 2.07
REMARK 500 1H HOH 665 O HOH 580 2546 2.07
REMARK 500 O HOH 580 1H HOH 665 2556 2.07
REMARK 500 1H HOH 739 2H HOH 617 1556 2.07
REMARK 500 1H HOH 566 2H HOH 666 1556 2.08
REMARK 500 2H HOH 666 1H HOH 566 1554 2.08
REMARK 500 O ALA 29 1H HOH 685 1456 2.09
REMARK 500 OD1 ASN 155 2H HOH 729 2546 2.09
REMARK 500 2H HOH 729 OD1 ASN 155 2556 2.09
REMARK 500 1H HOH 685 O ALA 29 1654 2.09
REMARK 500 O HOH 615 1HD2 ASN 58 2546 2.10
REMARK 500 O HOH 719 1H HOH 673 2546 2.10
REMARK 500 2H HOH 659 O ASN 172 1556 2.10
REMARK 500 1H HOH 607 O HOH 586 1456 2.10
REMARK 500 O HOH 586 1H HOH 607 1654 2.10
REMARK 500 O ASN 172 2H HOH 659 1554 2.10
REMARK 500 1H HOH 673 O HOH 719 2556 2.10
REMARK 500 1HD2 ASN 58 O HOH 615 2556 2.10
REMARK 500 2H HOH 667 1H HOH 519 1554 2.14
REMARK 500 O ALA 136 1H HOH 543 1455 2.14
REMARK 500 2H HOH 589 2H HOH 707 1556 2.14
REMARK 500 1H HOH 519 2H HOH 667 1556 2.14
REMARK 500 1H HOH 722 2HH2 ARG 196 2546 2.14
REMARK 500 1H HOH 543 O ALA 136 1655 2.14
REMARK 500 2HH2 ARG 196 1H HOH 722 2556 2.14
REMARK 500 2H HOH 707 2H HOH 589 1554 2.14
REMARK 500 2H HOH 540 2H HOH 583 1655 2.15
REMARK 500 1H HOH 722 2H HOH 564 2546 2.15
REMARK 500 O HOH 673 2HE2 GLN 104 2557 2.15
REMARK 500 HG1 THR 43 NH2 ARG 166 1655 2.15
REMARK 500 2H HOH 583 2H HOH 540 1455 2.15
REMARK 500 2H HOH 564 1H HOH 722 2556 2.15
REMARK 500 2HE2 GLN 104 O HOH 673 2547 2.15
REMARK 500 NH2 ARG 166 HG1 THR 43 1455 2.15
REMARK 500 OD1 ASN 58 1H HOH 649 2556 2.16
REMARK 500 1H HOH 649 OD1 ASN 58 2546 2.16
REMARK 500 1HD2 ASN 152 2H HOH 521 1554 2.16
REMARK 500 2H HOH 521 1HD2 ASN 152 1556 2.16
REMARK 500 O HOH 693 2H HOH 534 1655 2.17
REMARK 500 2H HOH 534 O HOH 693 1455 2.17
REMARK 500 2HH1 ARG 156 2H HOH 623 1554 2.17
REMARK 500 2H HOH 623 2HH1 ARG 156 1556 2.17
REMARK 500 2H HOH 562 H HOH 678 1654 2.18
REMARK 500 2H HOH 710 NH2 ARG 208 2546 2.18
REMARK 500 H HOH 678 2H HOH 562 1456 2.18
REMARK 500 NH2 ARG 208 2H HOH 710 2556 2.18
REMARK 500 2H HOH 574 O HOH 721 2556 2.19
REMARK 500 2H HOH 571 OD1 ASP 165 1655 2.19
REMARK 500 O HOH 721 2H HOH 574 2546 2.19
REMARK 500 HG SER 135 1H HOH 712 1455 2.19
REMARK 500 1H HOH 712 HG SER 135 1655 2.19
REMARK 500 O HOH 599 H ASP 165 1556 2.19
REMARK 500 OD1 ASP 165 2H HOH 571 1455 2.19
REMARK 500 H ASP 165 O HOH 599 1554 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 588 DISTANCE = 7.35 ANGSTROMS
REMARK 525 0 HOH 623 DISTANCE = 6.95 ANGSTROMS
REMARK 525 0 HOH 657 DISTANCE = 5.94 ANGSTROMS
REMARK 525 0 HOH 673 DISTANCE = 10.98 ANGSTROMS
REMARK 525 0 HOH 679 DISTANCE = 7.92 ANGSTROMS
REMARK 525 0 HOH 691 DISTANCE = 5.82 ANGSTROMS
REMARK 525 0 HOH 692 DISTANCE = 12.32 ANGSTROMS
REMARK 525 0 HOH 698 DISTANCE = 5.99 ANGSTROMS
REMARK 525 0 HOH 701 DISTANCE = 6.03 ANGSTROMS
REMARK 525 0 HOH 706 DISTANCE = 5.10 ANGSTROMS
REMARK 525 0 HOH 742 DISTANCE = 6.27 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: CAT
REMARK 800 SITE_DESCRIPTION: CATALYTIC TRIAD
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 1XZL SWS P00590 1 - 32 NOT IN ATOMS LIST
REMARK 999 1XZL SWS P00590 230 - 230 NOT IN ATOMS LIST
DBREF 1XZL 17 213 SWS P00590 CUTI_FUSSO 33 229
SEQADV 1XZL ALA 32 SWS P00590 ARG 48 CLONING ARTIFACT
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 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 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
HET HEE 901 11
HETNAM HEE N-HEXYLPHOSPHONATE ETHYL ESTER
FORMUL 2 HEE C8 H18 O2 P1
FORMUL 3 HOH *239(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
LINK P HEE 901 OG SER 120
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 |