| 1CUB-pdb | HEADER HYDROLASE (SERINE ESTERASE) 16-NOV-95 1CUB
TITLE CUTINASE, N172K, R196D MUTANT, MONOCLINIC CRYSTAL FORM
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: N172K, R196E;
COMPND 7 OTHER_DETAILS: FORM I CRYSTAL (MONOCLINIC)
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 S.LONGHI,C.CAMBILLAU
REVDAT 1 11-JUL-96 1CUB 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. 1.75 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) : 1.75
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 : 15472
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) : 0.147
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 : 1774
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 603
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 37.5
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) : 0.012
REMARK 3 BOND ANGLES (DEGREES) : 1.58
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 1CUB 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 : IMAGE PLATE (18CM)
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MAR XDS
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15523
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 (%) : 89.0
REMARK 200 DATA REDUNDANCY : 4.1 %
REMARK 200 R MERGE (I) : 0.038
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:
REMARK 280 CRYSTAL FORMS OF THIS MUTANT. THE THREE FORMS ARE
REMARK 280 REFERRED TO AS N172K,R196E_I, N172K,R196E_II,
REMARK 280 N172K,R196E_III BY THE AUTHORS. FORM I CRYSTALLIZES
REMARK 280 IN THE SAME SPACE GROUP OF THE NATIVE ENZYME.
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 1H HOH 756 1HH2 ARG 78 1655 1.25
REMARK 500 1HH2 ARG 78 1H HOH 756 1455 1.25
REMARK 500 H VAL 169 1HD2 ASN 27 1556 1.27
REMARK 500 1HD2 ASN 27 H VAL 169 1554 1.27
REMARK 500 HG1 THR 43 2HH2 ARG 166 1455 1.43
REMARK 500 2HH2 ARG 166 HG1 THR 43 1655 1.43
REMARK 500 2H HOH 740 HE ARG 211 2646 1.47
REMARK 500 HE ARG 211 2H HOH 740 2656 1.47
REMARK 500 2HH2 ARG 211 2H HOH 605 1655 1.59
REMARK 500 2H HOH 605 2HH2 ARG 211 1455 1.59
REMARK 500 1H HOH 505 O HOH 768 1655 1.67
REMARK 500 O HOH 768 1H HOH 505 1455 1.67
REMARK 500 1H HOH 710 O HOH 744 1655 1.69
REMARK 500 O HOH 744 1H HOH 710 1455 1.69
REMARK 500 2HH1 ARG 208 1H HOH 560 2656 1.70
REMARK 500 1H HOH 560 2HH1 ARG 208 2646 1.70
REMARK 500 2HH2 ARG 211 1H HOH 605 1655 1.71
REMARK 500 1H HOH 605 2HH2 ARG 211 1455 1.71
REMARK 500 2H HOH 610 O HOH 770 1655 1.72
REMARK 500 O HOH 770 2H HOH 610 1455 1.72
REMARK 500 O HOH 807 1H HOH 520 1556 1.73
REMARK 500 O HOH 505 1H HOH 796 1655 1.73
REMARK 500 1H HOH 520 O HOH 807 1554 1.73
REMARK 500 1H HOH 796 O HOH 505 1455 1.73
REMARK 500 O HOH 546 1H HOH 790 1554 1.75
REMARK 500 2H HOH 791 O HOH 697 2556 1.75
REMARK 500 O HOH 697 2H HOH 791 2546 1.75
REMARK 500 1H HOH 790 O HOH 546 1556 1.75
REMARK 500 O HOH 759 2H HOH 520 1655 1.76
REMARK 500 2H HOH 520 O HOH 759 1455 1.76
REMARK 500 1H HOH 716 O HOH 677 1556 1.78
REMARK 500 O HOH 677 1H HOH 716 1554 1.78
REMARK 500 1H HOH 697 O HOH 589 2546 1.79
REMARK 500 O HOH 791 1H HOH 722 2656 1.79
REMARK 500 1H HOH 722 O HOH 791 2646 1.79
REMARK 500 O HOH 589 1H HOH 697 2556 1.79
REMARK 500 1H HOH 791 O HOH 731 2556 1.80
REMARK 500 O HOH 731 1H HOH 791 2546 1.80
REMARK 500 2H HOH 762 O HOH 561 1455 1.81
REMARK 500 2H HOH 512 O HOH 788 1554 1.81
REMARK 500 O HOH 561 2H HOH 762 1655 1.81
REMARK 500 O HOH 788 2H HOH 512 1556 1.81
REMARK 500 O HOH 744 1H HOH 737 1455 1.82
REMARK 500 O HOH 752 HG1 THR 113 1455 1.82
REMARK 500 1H HOH 737 O HOH 744 1655 1.82
REMARK 500 HG1 THR 113 O HOH 752 1655 1.82
REMARK 500 O HOH 787 2HE2 GLN 104 1556 1.83
REMARK 500 1H HOH 567 O HOH 723 1456 1.83
REMARK 500 1H HOH 542 O VAL 210 1455 1.83
REMARK 500 2HE2 GLN 104 O HOH 787 1554 1.83
REMARK 500 O VAL 210 1H HOH 542 1655 1.83
REMARK 500 O HOH 723 1H HOH 567 1654 1.83
REMARK 500 O CYS 171 1H HOH 803 1556 1.84
REMARK 500 2H HOH 680 2H HOH 759 1455 1.84
REMARK 500 2H HOH 524 O HOH 709 1554 1.84
REMARK 500 O HOH 709 2H HOH 524 1556 1.84
REMARK 500 2H HOH 759 2H HOH 680 1655 1.84
REMARK 500 1H HOH 803 O CYS 171 1554 1.84
REMARK 500 O HOH 806 2H HOH 521 1556 1.86
REMARK 500 2HH2 ARG 166 OG1 THR 43 1655 1.86
REMARK 500 OG1 THR 43 2HH2 ARG 166 1455 1.86
REMARK 500 O HOH 771 1H HOH 779 1456 1.86
REMARK 500 2H HOH 521 O HOH 806 1554 1.86
REMARK 500 O HOH 521 H GLY 174 1554 1.87
REMARK 500 H GLY 174 O HOH 521 1556 1.87
REMARK 500 O HOH 759 2H HOH 680 1655 1.88
REMARK 500 2H HOH 680 O HOH 759 1455 1.88
REMARK 500 2H HOH 756 HE ARG 78 1655 1.88
REMARK 500 O HOH 595 2H HOH 782 1655 1.88
REMARK 500 2H HOH 782 O HOH 595 1455 1.88
REMARK 500 HE ARG 78 2H HOH 756 1455 1.88
REMARK 500 1H HOH 744 1H HOH 737 1455 1.89
REMARK 500 HG SER 213 1H HOH 783 1655 1.89
REMARK 500 1H HOH 783 HG SER 213 1455 1.89
REMARK 500 1H HOH 737 1H HOH 744 1655 1.89
REMARK 500 1H HOH 789 O HOH 512 1556 1.89
REMARK 500 O HOH 512 1H HOH 789 1554 1.89
REMARK 500 1H HOH 518 OG1 THR 173 1554 1.89
REMARK 500 OG1 THR 173 1H HOH 518 1556 1.89
REMARK 500 O HOH 774 1H HOH 783 1655 1.90
REMARK 500 1H HOH 605 2HH1 ARG 211 1455 1.90
REMARK 500 1H HOH 783 O HOH 774 1455 1.90
REMARK 500 2HH1 ARG 211 1H HOH 605 1655 1.90
REMARK 500 2H HOH 502 O HOH 745 2556 1.91
REMARK 500 2H HOH 783 HG SER 213 1455 1.91
REMARK 500 O HOH 644 1H HOH 752 1655 1.91
REMARK 500 1H HOH 752 O HOH 644 1455 1.91
REMARK 500 O HOH 803 1H HOH 738 1554 1.91
REMARK 500 HG SER 213 2H HOH 783 1655 1.91
REMARK 500 1H HOH 738 O HOH 803 1556 1.91
REMARK 500 O HOH 745 2H HOH 502 2546 1.91
REMARK 500 O HOH 522 1HD2 ASN 152 1554 1.92
REMARK 500 2H HOH 677 2H HOH 709 1554 1.92
REMARK 500 1HD2 ASN 152 O HOH 522 1556 1.92
REMARK 500 2H HOH 709 2H HOH 677 1556 1.92
REMARK 500 H SER 213 2H HOH 786 1655 1.93
REMARK 500 1H HOH 808 O GLU 196 2646 1.93
REMARK 500 2H HOH 786 H SER 213 1455 1.93
REMARK 500 O GLU 196 1H HOH 808 2656 1.93
REMARK 500 O SER 213 2H HOH 786 1655 1.94
REMARK 500 1H HOH 589 O HOH 808 2656 1.94
REMARK 500 O HOH 808 1H HOH 589 2646 1.94
REMARK 500 2H HOH 786 O SER 213 1455 1.94
REMARK 500 HG1 THR 80 O HOH 791 2546 1.95
REMARK 500 O PRO 193 1H HOH 550 2556 1.95
REMARK 500 1H HOH 550 O PRO 193 2546 1.95
REMARK 500 O HOH 791 HG1 THR 80 2556 1.95
REMARK 500 O HOH 714 H CYS 31 1456 1.96
REMARK 500 2H HOH 750 O ALA 136 1455 1.96
REMARK 500 H CYS 31 O HOH 714 1654 1.96
REMARK 500 O ALA 136 2H HOH 750 1655 1.96
REMARK 500 O HOH 730 H SER 42 1655 1.97
REMARK 500 H SER 42 O HOH 730 1455 1.97
REMARK 500 2H HOH 769 O HOH 737 1455 1.97
REMARK 500 O HOH 737 2H HOH 769 1655 1.97
REMARK 500 2H HOH 757 O TYR 77 1655 1.98
REMARK 500 O TYR 77 2H HOH 757 1455 1.98
REMARK 500 O HOH 783 HG SER 213 1455 1.98
REMARK 500 HG SER 213 O HOH 783 1655 1.98
REMARK 500 O ALA 85 2H HOH 779 1456 1.98
REMARK 500 O HOH 796 1HH2 ARG 166 1455 1.99
REMARK 500 1HH2 ARG 166 O HOH 796 1655 1.99
REMARK 500 O HOH 792 H ALA 93 2556 2.00
REMARK 500 O GLU 60 2H HOH 780 2655 2.00
REMARK 500 H ALA 93 O HOH 792 2546 2.00
REMARK 500 ND2 ASN 27 H VAL 169 1554 2.01
REMARK 500 O ASN 25 2H HOH 566 1554 2.01
REMARK 500 O HOH 722 1H HOH 733 1655 2.01
REMARK 500 2H HOH 566 O ASN 25 1556 2.01
REMARK 500 H VAL 169 ND2 ASN 27 1556 2.01
REMARK 500 N VAL 169 1HD2 ASN 27 1556 2.01
REMARK 500 1HD2 ASN 27 N VAL 169 1554 2.01
REMARK 500 1H HOH 733 O HOH 722 1455 2.01
REMARK 500 1H HOH 677 O GLY 157 1554 2.02
REMARK 500 2H HOH 728 O HOH 502 2646 2.02
REMARK 500 1H HOH 756 HE ARG 78 1655 2.02
REMARK 500 O HOH 502 2H HOH 728 2656 2.02
REMARK 500 HE ARG 78 1H HOH 756 1455 2.02
REMARK 500 O GLY 157 1H HOH 677 1556 2.02
REMARK 500 2H HOH 709 O HOH 677 1556 2.02
REMARK 500 O HOH 677 2H HOH 709 1554 2.02
REMARK 500 O HOH 730 1H HOH 742 1655 2.03
REMARK 500 2H HOH 714 O SER 28 1456 2.03
REMARK 500 O SER 28 2H HOH 714 1654 2.03
REMARK 500 O HOH 605 1H HOH 526 1455 2.03
REMARK 500 O HOH 605 2HH2 ARG 211 1455 2.03
REMARK 500 O HOH 720 2H HOH 805 1554 2.03
REMARK 500 2HD2 ASN 27 O HOH 716 1554 2.03
REMARK 500 1H HOH 742 O HOH 730 1455 2.03
REMARK 500 2H HOH 805 O HOH 720 1556 2.03
REMARK 500 1H HOH 526 O HOH 605 1655 2.03
REMARK 500 O HOH 716 2HD2 ASN 27 1556 2.03
REMARK 500 2HH2 ARG 211 O HOH 605 1655 2.03
REMARK 500 2H HOH 739 1H HOH 589 2546 2.04
REMARK 500 1H HOH 589 2H HOH 739 2556 2.04
REMARK 500 O HOH 785 2H HOH 552 2556 2.05
REMARK 500 O ARG 78 1H HOH 755 1455 2.05
REMARK 500 2H HOH 806 2H HOH 521 1556 2.05
REMARK 500 2H HOH 521 2H HOH 806 1554 2.05
REMARK 500 H GLY 82 OD2 ASP 139 1455 2.05
REMARK 500 1H HOH 755 O ARG 78 1655 2.05
REMARK 500 OD2 ASP 139 H GLY 82 1655 2.05
REMARK 500 2H HOH 731 1H HOH 791 2546 2.05
REMARK 500 2H HOH 552 O HOH 785 2546 2.05
REMARK 500 1H HOH 791 2H HOH 731 2556 2.05
REMARK 500 O HOH 798 1H HOH 792 2546 2.06
REMARK 500 O HOH 757 1HH2 ARG 78 1655 2.06
REMARK 500 O SER 213 2H HOH 783 1655 2.06
REMARK 500 1HH2 ARG 78 O HOH 757 1455 2.06
REMARK 500 1H HOH 796 HE ARG 166 1455 2.06
REMARK 500 1H HOH 792 O HOH 798 2556 2.06
REMARK 500 2H HOH 783 O SER 213 1455 2.06
REMARK 500 HE ARG 166 1H HOH 796 1655 2.06
REMARK 500 O HOH 682 1H HOH 758 1455 2.07
REMARK 500 H SER 92 OE2 GLU 196 2546 2.07
REMARK 500 OE2 GLU 196 H SER 92 2556 2.07
REMARK 500 O HOH 728 2H HOH 674 1655 2.07
REMARK 500 1H HOH 760 O HOH 784 1655 2.07
REMARK 500 O HOH 756 1HH2 ARG 78 1655 2.07
REMARK 500 2H HOH 674 O HOH 728 1455 2.07
REMARK 500 1H HOH 758 O HOH 682 1655 2.07
REMARK 500 O HOH 784 1H HOH 760 1455 2.07
REMARK 500 1HH2 ARG 78 O HOH 756 1455 2.07
REMARK 500 OD1 ASN 58 2H HOH 808 2656 2.08
REMARK 500 2H HOH 808 OD1 ASN 58 2646 2.08
REMARK 500 1H HOH 697 1H HOH 589 2546 2.08
REMARK 500 O HOH 773 1H HOH 732 2656 2.08
REMARK 500 1H HOH 505 1H HOH 768 1655 2.08
REMARK 500 1H HOH 768 1H HOH 505 1455 2.08
REMARK 500 1H HOH 732 O HOH 773 2646 2.08
REMARK 500 1H HOH 589 1H HOH 697 2556 2.08
REMARK 500 1H HOH 808 1H HOH 589 2646 2.09
REMARK 500 1H HOH 589 1H HOH 808 2656 2.09
REMARK 500 2H HOH 582 O HOH 765 2556 2.10
REMARK 500 O HOH 676 1H HOH 578 1655 2.10
REMARK 500 O HOH 765 2H HOH 582 2546 2.10
REMARK 500 1H HOH 578 O HOH 676 1455 2.10
REMARK 500 1H HOH 785 2H HOH 552 2556 2.11
REMARK 500 2H HOH 552 1H HOH 785 2546 2.11
REMARK 500 1H HOH 580 O HOH 719 1455 2.11
REMARK 500 O HOH 719 1H HOH 580 1655 2.11
REMARK 500 2H HOH 709 2H HOH 524 1556 2.12
REMARK 500 1H HOH 746 2H HOH 737 1455 2.12
REMARK 500 2H HOH 737 1H HOH 746 1655 2.12
REMARK 500 2H HOH 521 1H HOH 806 1554 2.12
REMARK 500 1H HOH 806 2H HOH 521 1556 2.12
REMARK 500 2H HOH 524 2H HOH 709 1554 2.12
REMARK 500 O HOH 732 2H HOH 537 2646 2.13
REMARK 500 2H HOH 512 1H HOH 788 1554 2.13
REMARK 500 1H HOH 788 2H HOH 512 1556 2.13
REMARK 500 2H HOH 739 O HOH 589 2546 2.13
REMARK 500 2H HOH 537 O HOH 732 2656 2.13
REMARK 500 O HOH 589 2H HOH 739 2556 2.13
REMARK 500 O HOH 794 1H HOH 730 1455 2.14
REMARK 500 1H HOH 716 2H HOH 677 1556 2.14
REMARK 500 O HOH 690 3HZ LYS 206 1455 2.14
REMARK 500 2H HOH 677 1H HOH 716 1554 2.14
REMARK 500 3HZ LYS 206 O HOH 690 1655 2.14
REMARK 500 1H HOH 730 O HOH 794 1655 2.14
REMARK 500 2H HOH 753 O HOH 733 1655 2.15
REMARK 500 2H HOH 744 1H HOH 710 1455 2.15
REMARK 500 O HOH 733 2H HOH 753 1455 2.15
REMARK 500 1H HOH 710 2H HOH 744 1655 2.15
REMARK 500 O HOH 740 HE ARG 211 2646 2.16
REMARK 500 2H HOH 794 1H HOH 730 1455 2.16
REMARK 500 2HE2 GLN 104 2H HOH 787 1554 2.16
REMARK 500 2H HOH 787 2HE2 GLN 104 1556 2.16
REMARK 500 HE ARG 211 O HOH 740 2656 2.16
REMARK 500 HG SER 61 1H HOH 781 2655 2.16
REMARK 500 1H HOH 730 2H HOH 794 1655 2.16
REMARK 500 1H HOH 756 NH2 ARG 78 1655 2.17
REMARK 500 NH2 ARG 78 1H HOH 756 1455 2.17
REMARK 500 2H HOH 717 O HOH 779 1456 2.17
REMARK 500 1H HOH 733 1H HOH 722 1455 2.18
REMARK 500 OG SER 61 2H HOH 781 2655 2.18
REMARK 500 1H HOH 757 1HH2 ARG 78 1655 2.18
REMARK 500 1H HOH 722 1H HOH 733 1655 2.18
REMARK 500 1HH2 ARG 78 1H HOH 757 1455 2.18
REMARK 500 1H HOH 518 HG1 THR 173 1554 2.19
REMARK 500 HG1 THR 173 1H HOH 518 1556 2.19
REMARK 500 1H HOH 714 O ALA 29 1456 2.19
REMARK 500 O ALA 29 1H HOH 714 1654 2.19
REMARK 500 1H HOH 731 1H HOH 791 2546 2.20
REMARK 500 1H HOH 697 2H HOH 791 2546 2.20
REMARK 500 1H HOH 791 1H HOH 731 2556 2.20
REMARK 500 2H HOH 791 1H HOH 697 2556 2.20
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: CAT
REMARK 800 SITE_DESCRIPTION: CATALYTIC TRIAD
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 1CUB SWS P00590 1 - 32 NOT IN ATOMS LIST
REMARK 999 1CUB SWS P00590 230 - 230 NOT IN ATOMS LIST
DBREF 1CUB 17 213 SWS P00590 CUTI_FUSSO 33 229
SEQADV 1CUB ALA 32 SWS P00590 ARG 48 CONFLICT
SEQADV 1CUB LYS 172 SWS P00590 ASN 188 ENGINEERED
SEQADV 1CUB GLU 196 SWS P00590 ARG 212 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 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 LYS 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 GLU GLY PRO ALA PRO GLU PHE LEU ILE GLU LYS VAL ARG
SEQRES 17 214 ALA VAL ARG GLY SER ALA
FORMUL 2 HOH *201(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 GLU 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
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