| content |
HEADER HYDROLASE (SERINE ESTERASE) 16-NOV-95 1CUV
TITLE CUTINASE, A85F 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: A85F
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 11-JUL-96 1CUV 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. 2.01 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) : 2.01
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 : 12247
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) : 0.176
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 : 1785
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 699
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 46.9
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) : 0.010
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 1CUV 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 : 12692
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 (%) : 78.0
REMARK 200 DATA REDUNDANCY : 3.6 %
REMARK 200 R MERGE (I) : 0.112
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 (%): 54.
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: I 2 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 X,-Y,-Z
REMARK 290 4555 -X,Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 X+1/2,-Y+1/2,-Z+1/2
REMARK 290 8555 -X+1/2,Y+1/2,-Z+1/2
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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 30.50082
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 33.34890
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 58.69922
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 30.50082
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 33.34890
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 58.69922
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 30.50082
REMARK 290 SMTRY2 7 0.000000 -1.000000 0.000000 33.34890
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 58.69922
REMARK 290 SMTRY1 8 -1.000000 0.000000 0.000000 30.50082
REMARK 290 SMTRY2 8 0.000000 1.000000 0.000000 33.34890
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 58.69922
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 1HH2 ARG 196 1H HOH 665 8545 1.37
REMARK 500 1H HOH 665 1HH2 ARG 196 8555 1.37
REMARK 500 HG SER 181 H LEU 182 4656 1.42
REMARK 500 H LEU 182 HG SER 181 4656 1.42
REMARK 500 1H HOH 630 1HH2 ARG 211 7555 1.46
REMARK 500 1HH2 ARG 211 1H HOH 630 7455 1.46
REMARK 500 O HOH 565 1H HOH 651 2655 1.56
REMARK 500 1H HOH 651 O HOH 565 2655 1.56
REMARK 500 2HH2 ARG 156 2H HOH 658 4656 1.57
REMARK 500 2H HOH 658 2HH2 ARG 156 4656 1.57
REMARK 500 1H HOH 568 2H HOH 524 7555 1.61
REMARK 500 2H HOH 524 1H HOH 568 7455 1.61
REMARK 500 O HOH 570 1H HOH 563 2655 1.70
REMARK 500 1H HOH 563 O HOH 570 2655 1.70
REMARK 500 1H HOH 585 1H HOH 585 3556 1.72
REMARK 500 2HH2 ARG 211 2H HOH 568 7455 1.72
REMARK 500 2H HOH 568 2HH2 ARG 211 7555 1.72
REMARK 500 2H HOH 524 O HOH 568 7455 1.74
REMARK 500 O HOH 658 2HH2 ARG 156 4656 1.74
REMARK 500 O HOH 568 2H HOH 524 7555 1.74
REMARK 500 2HH2 ARG 156 O HOH 658 4656 1.74
REMARK 500 1H HOH 631 O HOH 604 7555 1.75
REMARK 500 O HOH 604 1H HOH 631 7455 1.75
REMARK 500 O HOH 596 1H HOH 551 7455 1.76
REMARK 500 1H HOH 551 O HOH 596 7555 1.76
REMARK 500 2H HOH 673 O HOH 568 7455 1.77
REMARK 500 O HOH 568 2H HOH 673 7555 1.77
REMARK 500 HG SER 213 1H HOH 670 7455 1.79
REMARK 500 1H HOH 670 HG SER 213 7555 1.79
REMARK 500 2H HOH 626 2H HOH 626 4656 1.79
REMARK 500 2H HOH 629 2HH2 ARG 78 7455 1.82
REMARK 500 2H HOH 686 O HOH 544 2655 1.82
REMARK 500 O HOH 544 2H HOH 686 2655 1.82
REMARK 500 2HH2 ARG 78 2H HOH 629 7555 1.82
REMARK 500 1HH2 ARG 196 O HOH 665 8545 1.85
REMARK 500 O HOH 665 1HH2 ARG 196 8555 1.85
REMARK 500 1H HOH 597 1H HOH 531 4656 1.86
REMARK 500 1H HOH 531 1H HOH 597 4656 1.86
REMARK 500 2H HOH 562 O LEU 182 2655 1.87
REMARK 500 O LEU 182 2H HOH 562 2655 1.87
REMARK 500 O HOH 605 2H HOH 526 7455 1.88
REMARK 500 2H HOH 526 O HOH 605 7555 1.88
REMARK 500 OD2 ASP 33 HE ARG 78 7455 1.89
REMARK 500 HE ARG 78 OD2 ASP 33 7555 1.89
REMARK 500 2H HOH 570 1H HOH 680 2655 1.89
REMARK 500 1H HOH 680 2H HOH 570 2655 1.89
REMARK 500 HG1 THR 19 OXT SER 213 7555 1.90
REMARK 500 OXT SER 213 HG1 THR 19 7455 1.90
REMARK 500 O VAL 184 H VAL 184 2655 1.91
REMARK 500 H VAL 184 O VAL 184 2655 1.91
REMARK 500 2H HOH 726 O HOH 676 3556 1.92
REMARK 500 O HOH 676 2H HOH 726 3556 1.92
REMARK 500 OG SER 213 1H HOH 670 7455 1.93
REMARK 500 1H HOH 653 1H HOH 581 7555 1.93
REMARK 500 1H HOH 581 1H HOH 653 7455 1.93
REMARK 500 1H HOH 670 OG SER 213 7555 1.93
REMARK 500 2H HOH 665 1HH2 ARG 196 8555 1.94
REMARK 500 1HH2 ARG 196 2H HOH 665 8545 1.94
REMARK 500 O HOH 629 2H HOH 544 7455 1.98
REMARK 500 2H HOH 544 O HOH 629 7555 1.98
REMARK 500 2H HOH 519 O GLY 212 7555 1.99
REMARK 500 2H HOH 565 O HOH 585 2655 1.99
REMARK 500 O GLY 212 2H HOH 519 7455 1.99
REMARK 500 O HOH 585 2H HOH 565 2655 1.99
REMARK 500 O HOH 694 2H HOH 564 8555 2.00
REMARK 500 2H HOH 564 O HOH 694 8545 2.00
REMARK 500 2H HOH 596 1H HOH 551 7455 2.01
REMARK 500 1H HOH 605 O TYR 77 7455 2.01
REMARK 500 2H HOH 617 1H HOH 516 7455 2.01
REMARK 500 O TYR 77 1H HOH 605 7555 2.01
REMARK 500 1H HOH 640 H ASP 66 7555 2.01
REMARK 500 H ASP 66 1H HOH 640 7455 2.01
REMARK 500 1H HOH 551 2H HOH 596 7555 2.01
REMARK 500 1H HOH 516 2H HOH 617 7555 2.01
REMARK 500 H LEU 182 OG SER 181 4656 2.02
REMARK 500 OG SER 181 H LEU 182 4656 2.02
REMARK 500 2H HOH 524 2H HOH 568 7455 2.03
REMARK 500 2H HOH 568 2H HOH 524 7555 2.03
REMARK 500 2H HOH 585 2H HOH 565 2655 2.04
REMARK 500 1H HOH 605 2H HOH 526 7455 2.04
REMARK 500 2H HOH 565 2H HOH 585 2655 2.04
REMARK 500 2H HOH 526 1H HOH 605 7555 2.04
REMARK 500 HE ARG 211 2H HOH 631 7455 2.05
REMARK 500 2H HOH 631 HE ARG 211 7555 2.05
REMARK 500 1H HOH 599 1H HOH 599 4656 2.06
REMARK 500 1H HOH 585 O HOH 585 3556 2.07
REMARK 500 1H HOH 695 2HH2 ARG 78 7455 2.07
REMARK 500 O HOH 585 1H HOH 585 3556 2.07
REMARK 500 2HH2 ARG 78 1H HOH 695 7555 2.07
REMARK 500 2H HOH 544 2H HOH 629 7555 2.08
REMARK 500 2H HOH 629 2H HOH 544 7455 2.08
REMARK 500 O SER 213 1H HOH 689 7455 2.10
REMARK 500 O HOH 568 2HH2 ARG 211 7555 2.10
REMARK 500 2HH2 ARG 211 O HOH 568 7455 2.10
REMARK 500 1H HOH 689 O SER 213 7555 2.10
REMARK 500 1H HOH 599 O HOH 599 4656 2.11
REMARK 500 1H HOH 651 2H HOH 565 2655 2.11
REMARK 500 2H HOH 565 1H HOH 651 2655 2.11
REMARK 500 O HOH 599 1H HOH 599 4656 2.11
REMARK 500 NH2 ARG 156 2H HOH 658 4656 2.14
REMARK 500 2H HOH 658 NH2 ARG 156 4656 2.14
REMARK 500 2H HOH 676 2H HOH 726 3556 2.15
REMARK 500 O HOH 630 1HH2 ARG 211 7555 2.15
REMARK 500 1HH2 ARG 211 O HOH 630 7455 2.15
REMARK 500 2H HOH 726 2H HOH 676 3556 2.15
REMARK 500 1H HOH 697 2H HOH 513 4656 2.16
REMARK 500 2H HOH 513 1H HOH 697 4656 2.16
REMARK 500 1H HOH 562 1H HOH 531 2655 2.16
REMARK 500 1H HOH 531 1H HOH 562 2655 2.16
REMARK 500 1H HOH 597 O HOH 531 4656 2.17
REMARK 500 H LEU 81 O HOH 686 2655 2.17
REMARK 500 O HOH 531 1H HOH 597 4656 2.17
REMARK 500 2H HOH 589 O HOH 633 2655 2.17
REMARK 500 O HOH 686 H LEU 81 2655 2.17
REMARK 500 O HOH 633 2H HOH 589 2655 2.17
REMARK 500 O GLY 212 1H HOH 519 7455 2.18
REMARK 500 1H HOH 519 O GLY 212 7555 2.18
REMARK 500 O HOH 697 1HZ LYS 151 4656 2.19
REMARK 500 1HZ LYS 151 O HOH 697 4656 2.19
REMARK 500 1H HOH 680 2H HOH 643 2655 2.19
REMARK 500 2H HOH 643 1H HOH 680 2655 2.19
REMARK 500 O HOH 531 1H HOH 562 2655 2.20
REMARK 500 1H HOH 562 O HOH 531 2655 2.20
REMARK 500 O HOH 599 2HE2 GLN 154 4656 2.20
REMARK 500 1H HOH 524 1H HOH 568 7455 2.20
REMARK 500 2HE2 GLN 154 O HOH 599 4656 2.20
REMARK 500 1H HOH 568 1H HOH 524 7555 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 1CUV SWS P00590 1 - 32 NOT IN ATOMS LIST
REMARK 999 1CUV SWS P00590 230 - 230 NOT IN ATOMS LIST
DBREF 1CUV 17 213 SWS P00590 CUTI_FUSSO 33 229
SEQADV 1CUV ALA 32 SWS P00590 ARG 48 CONFLICT
SEQADV 1CUV PHE 85 SWS P00590 ALA 101 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 PHE 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 *233(H2 O1)
HELIX 1 1 SER 28 SER 30 5 3
HELIX 2 2 GLY 49 PHE 63 1 15
HELIX 3 3 GLY 82 PHE 85 5 4
HELIX 4 4 SER 92 LYS 108 1 17
HELIX 5 5 GLN 121 ASP 132 1 12
HELIX 6 6 SER 135 LYS 140 1 6
HELIX 7 7 ALA 164 ARG 166 5 3
HELIX 8 8 LEU 176 THR 179 5 4
HELIX 9 9 ALA 186 LEU 189 5 4
HELIX 10 10 GLY 192 ARG 196 1 5
HELIX 11 11 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 61.000 66.700 117.400 90.00 90.00 90.00 I 2 2 2 8
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 0.016393 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014993 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008518 0.00000 |