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HEADER HYDROLASE (SERINE ESTERASE) 16-NOV-95 1CUC
TITLE CUTINASE, N172K, R196D MUTANT, ORTHORHOMBIC 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 II CRYSTAL (ORTHORHOMBIC)
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 1CUC 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 : 15768
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) : 0.157
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 : 561
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 33.9
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) : 1.52
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 1CUC 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 : 15984
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 (%) : 90.0
REMARK 200 DATA REDUNDANCY : 8.5 %
REMARK 200 R MERGE (I) : 0.060
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 (%): 36.
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.
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 1/2-X,-Y,1/2+Z
REMARK 290 3555 -X,1/2+Y,1/2-Z
REMARK 290 4555 1/2+X,1/2-Y,-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 18.50002
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 35.69899
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 32.10067
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 35.69899
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 18.50002
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 32.10067
REMARK 290 SMTRY3 4 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 1455 1.27
REMARK 500 H VAL 169 1HD2 ASN 27 1655 1.27
REMARK 500 2HH2 ARG 96 1H HOH 608 3655 1.58
REMARK 500 1H HOH 608 2HH2 ARG 96 3645 1.58
REMARK 500 2HH2 ARG 96 2H HOH 585 3655 1.59
REMARK 500 2H HOH 585 2HH2 ARG 96 3645 1.59
REMARK 500 1H HOH 585 2HH2 ARG 96 3645 1.60
REMARK 500 2HH2 ARG 96 1H HOH 585 3655 1.60
REMARK 500 1H HOH 585 2HH1 ARG 96 3645 1.63
REMARK 500 2HH1 ARG 96 1H HOH 585 3655 1.63
REMARK 500 O HOH 917 1H HOH 997 1655 1.70
REMARK 500 1H HOH 997 O HOH 917 1455 1.70
REMARK 500 1H HOH 605 2HH2 ARG 211 2554 1.72
REMARK 500 1H HOH 816 O HOH 610 1455 1.72
REMARK 500 O HOH 610 1H HOH 816 1655 1.72
REMARK 500 2HH2 ARG 211 1H HOH 605 2555 1.72
REMARK 500 1H HOH 979 O HOH 941 3645 1.73
REMARK 500 O HOH 941 1H HOH 979 3655 1.73
REMARK 500 O HOH 979 1H HOH 993 3645 1.74
REMARK 500 1H HOH 993 O HOH 979 3655 1.74
REMARK 500 O HOH 911 1H HOH 961 4456 1.75
REMARK 500 2HH1 ARG 96 O HOH 585 3655 1.75
REMARK 500 O HOH 585 2HH1 ARG 96 3645 1.75
REMARK 500 1H HOH 961 O HOH 911 4556 1.75
REMARK 500 HG1 THR 113 O HOH 732 4456 1.76
REMARK 500 O HOH 732 HG1 THR 113 4556 1.76
REMARK 500 O HOH 816 1H HOH 560 4456 1.77
REMARK 500 1H HOH 560 O HOH 816 4556 1.77
REMARK 500 O HOH 993 2H HOH 978 3655 1.78
REMARK 500 2H HOH 978 O HOH 993 3645 1.78
REMARK 500 1H HOH 521 O HOH 986 1455 1.79
REMARK 500 O HOH 990 2H HOH 573 3655 1.79
REMARK 500 2H HOH 573 O HOH 990 3645 1.79
REMARK 500 O HOH 986 1H HOH 521 1655 1.79
REMARK 500 2H HOH 910 O HOH 963 4456 1.81
REMARK 500 O HOH 963 2H HOH 910 4556 1.81
REMARK 500 OG1 THR 173 2H HOH 518 1655 1.82
REMARK 500 2H HOH 518 OG1 THR 173 1455 1.82
REMARK 500 H GLY 174 O HOH 521 1655 1.83
REMARK 500 O HOH 521 H GLY 174 1455 1.83
REMARK 500 O HOH 598 2H HOH 595 2654 1.84
REMARK 500 2H HOH 595 O HOH 598 2655 1.84
REMARK 500 2H HOH 976 O HOH 988 3645 1.85
REMARK 500 O PRO 193 1H HOH 550 3645 1.85
REMARK 500 2HH2 ARG 211 2H HOH 605 2555 1.85
REMARK 500 2H HOH 605 2HH2 ARG 211 2554 1.85
REMARK 500 2HH1 ARG 158 OD1 ASP 134 4556 1.85
REMARK 500 O HOH 649 1H HOH 724 4556 1.85
REMARK 500 OD1 ASP 134 2HH1 ARG 158 4456 1.85
REMARK 500 1H HOH 724 O HOH 649 4456 1.85
REMARK 500 1H HOH 550 O PRO 193 3655 1.85
REMARK 500 O HOH 988 2H HOH 976 3655 1.85
REMARK 500 O HOH 558 H GLY 46 2555 1.86
REMARK 500 H GLY 46 O HOH 558 2554 1.86
REMARK 500 2HZ LYS 140 1H HOH 994 4456 1.86
REMARK 500 O HOH 644 2H HOH 732 4456 1.86
REMARK 500 2HH2 ARG 158 OD2 ASP 134 4556 1.86
REMARK 500 2H HOH 732 O HOH 644 4556 1.86
REMARK 500 OD2 ASP 134 2HH2 ARG 158 4456 1.86
REMARK 500 1H HOH 994 2HZ LYS 140 4556 1.86
REMARK 500 2HD2 ASN 106 O HOH 727 4456 1.87
REMARK 500 H SER 92 OE1 GLU 196 3655 1.87
REMARK 500 1H HOH 526 O HOH 605 2555 1.87
REMARK 500 OE1 GLU 196 H SER 92 3645 1.87
REMARK 500 O HOH 605 1H HOH 526 2554 1.87
REMARK 500 O HOH 727 2HD2 ASN 106 4556 1.87
REMARK 500 O HOH 961 2H HOH 814 4456 1.88
REMARK 500 O ALA 209 1H HOH 598 2655 1.88
REMARK 500 2H HOH 814 O HOH 961 4556 1.88
REMARK 500 O HOH 960 1H HOH 649 4456 1.88
REMARK 500 1H HOH 649 O HOH 960 4556 1.88
REMARK 500 1H HOH 598 O ALA 209 2654 1.88
REMARK 500 O ASN 25 2H HOH 566 1455 1.89
REMARK 500 O VAL 184 2H HOH 537 2654 1.89
REMARK 500 2H HOH 566 O ASN 25 1655 1.89
REMARK 500 O ALA 190 1H HOH 553 3645 1.89
REMARK 500 1H HOH 553 O ALA 190 3655 1.89
REMARK 500 2H HOH 537 O VAL 184 2655 1.89
REMARK 500 2H HOH 709 O HOH 722 4556 1.90
REMARK 500 2HH2 ARG 96 O HOH 585 3655 1.90
REMARK 500 O HOH 722 2H HOH 709 4456 1.90
REMARK 500 O HOH 585 2HH2 ARG 96 3645 1.90
REMARK 500 1H HOH 709 O ALA 136 4556 1.92
REMARK 500 1H HOH 960 1HH1 ARG 158 4456 1.92
REMARK 500 HE ARG 211 O HOH 719 2555 1.92
REMARK 500 2H HOH 680 O HOH 987 2554 1.92
REMARK 500 O HOH 719 HE ARG 211 2554 1.92
REMARK 500 1HH1 ARG 158 1H HOH 960 4556 1.92
REMARK 500 O ALA 136 1H HOH 709 4456 1.92
REMARK 500 O HOH 987 2H HOH 680 2555 1.92
REMARK 500 O GLU 131 2H HOH 979 3655 1.93
REMARK 500 1H HOH 988 O HOH 607 3655 1.93
REMARK 500 1HD2 ASN 152 O HOH 522 1655 1.93
REMARK 500 O HOH 607 1H HOH 988 3645 1.93
REMARK 500 1H HOH 559 O HOH 978 3655 1.93
REMARK 500 O GLU 196 2H HOH 970 3645 1.93
REMARK 500 2H HOH 979 O GLU 131 3645 1.93
REMARK 500 2H HOH 970 O GLU 196 3655 1.93
REMARK 500 O HOH 978 1H HOH 559 3645 1.93
REMARK 500 O HOH 522 1HD2 ASN 152 1455 1.93
REMARK 500 O GLY 157 2H HOH 524 1655 1.94
REMARK 500 2H HOH 524 O GLY 157 1455 1.94
REMARK 500 H VAL 169 ND2 ASN 27 1655 1.95
REMARK 500 ND2 ASN 27 H VAL 169 1455 1.95
REMARK 500 1HD2 ASN 27 N VAL 169 1455 1.96
REMARK 500 N VAL 169 1HD2 ASN 27 1655 1.96
REMARK 500 2HH2 ARG 211 O HOH 605 2555 1.97
REMARK 500 O HOH 605 2HH2 ARG 211 2554 1.97
REMARK 500 O THR 107 2H HOH 707 4456 1.98
REMARK 500 2H HOH 707 O THR 107 4556 1.98
REMARK 500 O HOH 682 2H HOH 558 2554 1.99
REMARK 500 O HOH 723 1H HOH 962 4456 1.99
REMARK 500 1H HOH 962 O HOH 723 4556 1.99
REMARK 500 2H HOH 558 O HOH 682 2555 1.99
REMARK 500 O HOH 703 2H HOH 726 4456 2.00
REMARK 500 2H HOH 726 O HOH 703 4556 2.00
REMARK 500 O SER 213 2H HOH 520 2555 2.01
REMARK 500 2H HOH 520 O SER 213 2554 2.01
REMARK 500 H GLY 46 2H HOH 558 2554 2.03
REMARK 500 2H HOH 558 H GLY 46 2555 2.03
REMARK 500 OG1 THR 107 2H HOH 727 4456 2.04
REMARK 500 2H HOH 727 OG1 THR 107 4556 2.04
REMARK 500 OD1 ASN 58 1H HOH 970 3645 2.05
REMARK 500 1H HOH 925 O HOH 595 2654 2.05
REMARK 500 1H HOH 990 1HH2 ARG 17 3655 2.05
REMARK 500 O HOH 595 1H HOH 925 2655 2.05
REMARK 500 1H HOH 970 OD1 ASN 58 3655 2.05
REMARK 500 1HH2 ARG 17 1H HOH 990 3645 2.05
REMARK 500 2H HOH 980 2H HOH 816 2554 2.07
REMARK 500 2H HOH 816 2H HOH 980 2555 2.07
REMARK 500 2H HOH 986 1H HOH 521 1655 2.07
REMARK 500 1H HOH 521 2H HOH 986 1455 2.07
REMARK 500 1H HOH 582 2H HOH 951 3645 2.08
REMARK 500 2H HOH 951 1H HOH 582 3655 2.08
REMARK 500 O HOH 608 2HH2 ARG 96 3645 2.08
REMARK 500 1H HOH 605 O ASP 111 2554 2.08
REMARK 500 2HH2 ARG 96 O HOH 608 3655 2.08
REMARK 500 O ASP 111 1H HOH 605 2555 2.08
REMARK 500 2H HOH 800 O LYS 172 1455 2.09
REMARK 500 2H HOH 978 2H HOH 993 3645 2.09
REMARK 500 2H HOH 993 2H HOH 978 3655 2.09
REMARK 500 O LYS 172 2H HOH 800 1655 2.09
REMARK 500 O HOH 910 2H HOH 728 4456 2.10
REMARK 500 1H HOH 574 OXT SER 213 2554 2.10
REMARK 500 2H HOH 728 O HOH 910 4556 2.10
REMARK 500 OXT SER 213 1H HOH 574 2555 2.10
REMARK 500 2H HOH 638 O HOH 548 3645 2.11
REMARK 500 O HOH 548 2H HOH 638 3655 2.11
REMARK 500 1HD2 ASN 58 1H HOH 970 3645 2.11
REMARK 500 1H HOH 970 1HD2 ASN 58 3655 2.11
REMARK 500 2H HOH 983 O HOH 980 2555 2.12
REMARK 500 O HOH 980 2H HOH 983 2554 2.12
REMARK 500 1H HOH 983 O HOH 624 4456 2.13
REMARK 500 O HOH 624 1H HOH 983 4556 2.13
REMARK 500 2HD2 ASN 27 O HOH 802 1455 2.14
REMARK 500 2HH1 ARG 138 O HOH 703 4556 2.14
REMARK 500 O HOH 703 2HH1 ARG 138 4456 2.14
REMARK 500 2H HOH 598 2H HOH 595 2654 2.14
REMARK 500 2H HOH 595 2H HOH 598 2655 2.14
REMARK 500 H GLY 174 1H HOH 521 1655 2.14
REMARK 500 1H HOH 610 1H HOH 816 1655 2.14
REMARK 500 O HOH 802 2HD2 ASN 27 1655 2.14
REMARK 500 1H HOH 521 H GLY 174 1455 2.14
REMARK 500 1H HOH 816 1H HOH 610 1455 2.14
REMARK 500 O HOH 537 1H HOH 580 2655 2.15
REMARK 500 1H HOH 580 O HOH 537 2654 2.15
REMARK 500 1H HOH 960 1H HOH 649 4456 2.15
REMARK 500 1H HOH 649 1H HOH 960 4556 2.15
REMARK 500 O HOH 976 2H HOH 554 3645 2.16
REMARK 500 1H HOH 608 NH2 ARG 96 3645 2.16
REMARK 500 2H HOH 554 O HOH 976 3655 2.16
REMARK 500 NH2 ARG 96 1H HOH 608 3655 2.16
REMARK 500 2HH1 ARG 138 1H HOH 703 4556 2.16
REMARK 500 O HOH 993 2H HOH 977 3655 2.16
REMARK 500 1H HOH 703 2HH1 ARG 138 4456 2.16
REMARK 500 2H HOH 977 O HOH 993 3645 2.16
REMARK 500 O SER 213 1H HOH 574 2555 2.17
REMARK 500 1H HOH 574 O SER 213 2554 2.17
REMARK 500 2H HOH 979 1H HOH 993 3645 2.18
REMARK 500 1H HOH 993 2H HOH 979 3655 2.18
REMARK 500 1HH2 ARG 96 1H HOH 608 3655 2.18
REMARK 500 1H HOH 608 1HH2 ARG 96 3645 2.18
REMARK 500 1H HOH 917 2H HOH 998 1655 2.19
REMARK 500 1H HOH 727 2HD2 ASN 106 4556 2.19
REMARK 500 HG SER 28 O HOH 960 4456 2.19
REMARK 500 O HOH 960 HG SER 28 4556 2.19
REMARK 500 2HD2 ASN 106 1H HOH 727 4456 2.19
REMARK 500 2H HOH 998 1H HOH 917 1455 2.19
REMARK 500 O HOH 987 2H HOH 520 2555 2.20
REMARK 500 2H HOH 520 O HOH 987 2554 2.20
REMARK 500 1H HOH 983 1H HOH 624 4456 2.20
REMARK 500 1H HOH 624 1H HOH 983 4556 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 1CUC SWS P00590 1 - 32 NOT IN ATOMS LIST
REMARK 999 1CUC SWS P00590 230 - 230 NOT IN ATOMS LIST
DBREF 1CUC 17 213 SWS P00590 CUTI_FUSSO 33 229
SEQADV 1CUC ALA 32 SWS P00590 ARG 48 CONFLICT
SEQADV 1CUC LYS 172 SWS P00590 ASN 188 ENGINEERED
SEQADV 1CUC 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 *187(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 37.000 64.200 71.400 90.00 90.00 90.00 P 21 21 21 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 0.027027 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015576 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014006 0.00000 |