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HEADER HYDROLASE (SERINE ESTERASE) 16-NOV-95 1CUW
TITLE CUTINASE, G82A, A85F, V184I, A185L, L189F MUTANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CUTINASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.1.1.3;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: G82A, A85F, V184I, A185L, L189F
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 1CUW 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. 2.70 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) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 6.0
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.5
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 7796
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) : 0.142
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 : 3586
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 1242
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) : 1.40
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:
REMARK 3
REMARK 3 RMSD BOND DISTANCE MOLECULE A : 0.008 ANGSTROMS
REMARK 3 RMSD BOND DISTANCE MOLECULE B : 0.007 ANGSTROMS
REMARK 3 RMSD ANGLE DISTANCE MOLECULE A : 1.40 DEGREES
REMARK 3 RMSD ANGLE DISTANCE MOLECULE B : 1.39 DEGREES
REMARK 3
REMARK 3 MEAN B (ANGSTROMS**2) MOLECULE A : MAIN : 18.2
REMARK 3 MEAN B (ANGSTROMS**2) MOLECULE A : SIDE : 26.3
REMARK 3 MEAN B (ANGSTROMS**2) MOLECULE A : SOLV : 48.4
REMARK 3
REMARK 3 MEAN B (ANGSTROMS**2) MOLECULE B : MAIN : 20.0
REMARK 3 MEAN B (ANGSTROMS**2) MOLECULE B : SIDE : 28.3
REMARK 3 MEAN B (ANGSTROMS**2) MOLECULE B : SOLV : 49.1
REMARK 4
REMARK 4 1CUW 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 : 9151
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 (%) : 94.0
REMARK 200 DATA REDUNDANCY : 2.5 %
REMARK 200 R MERGE (I) : 0.158
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 (%): 51.
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: C 1 2 1
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 1/2+X,1/2+Y,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 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 65.19755
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 27.34931
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 65.19755
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 27.34931
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 295
REMARK 295 NON-CRYSTALLOGRAPHIC SYMMETRY
REMARK 295 THE TRANSFORMATIONS PRESENTED ON THE MTRIX RECORDS BELOW
REMARK 295 DESCRIBE NON-CRYSTALLOGRAPHIC RELATIONSHIPS AMONG ATOMS
REMARK 295 IN THIS ENTRY. APPLYING THE APPROPRIATE MTRIX
REMARK 295 TRANSFORMATION TO THE RESIDUES LISTED FIRST WILL YIELD
REMARK 295 APPROXIMATE COORDINATES FOR THE RESIDUES LISTED SECOND.
REMARK 295 CHAIN IDENTIFIERS GIVEN AS "?" REFER TO CHAINS FOR WHICH
REMARK 295 ATOMS ARE NOT FOUND IN THIS ENTRY.
REMARK 295
REMARK 295 APPLIED TO TRANSFORMED TO
REMARK 295 TRANSFORM CHAIN RESIDUES CHAIN RESIDUES RMSD
REMARK 295 SSS
REMARK 295 M 1 B 17 .. 213 A 17 .. 213 0.921
REMARK 295
REMARK 295 WHERE SSS -> COLUMNS 8-10 OF MTRIX RECORDS
REMARK 295
REMARK 295 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 2HH2 ARG B 138 2H HOH A 695 2656 1.22
REMARK 500 2H HOH A 695 2HH2 ARG B 138 2656 1.22
REMARK 500 HE ARG A 166 2H HOH B 505 3455 1.24
REMARK 500 2H HOH B 505 HE ARG A 166 3545 1.24
REMARK 500 1H HOH A 804 1HH1 ARG B 196 2657 1.30
REMARK 500 1HH1 ARG B 196 1H HOH A 804 2657 1.30
REMARK 500 2H HOH A 804 1HH1 ARG B 196 2657 1.33
REMARK 500 1HH1 ARG B 196 2H HOH A 804 2657 1.33
REMARK 500 1H HOH A 663 H ASN A 25 4556 1.42
REMARK 500 H ASN A 25 1H HOH A 663 4546 1.42
REMARK 500 2H HOH B 953 2HH1 ARG A 96 2656 1.46
REMARK 500 2HH1 ARG A 96 2H HOH B 953 2656 1.46
REMARK 500 2HH2 ARG B 96 1HZ LYS A 65 3555 1.51
REMARK 500 1HZ LYS A 65 2HH2 ARG B 96 3445 1.51
REMARK 500 O HOH B 630 2H HOH B 601 4647 1.56
REMARK 500 1H HOH B 505 1H HOH A 946 3545 1.56
REMARK 500 1H HOH A 946 1H HOH B 505 3455 1.56
REMARK 500 2H HOH B 601 O HOH B 630 4657 1.56
REMARK 500 1H HOH B 505 1H HOH A 505 3545 1.57
REMARK 500 1H HOH A 505 1H HOH B 505 3455 1.57
REMARK 500 1H HOH B 589 HE ARG B 20 4647 1.58
REMARK 500 HE ARG B 20 1H HOH B 589 4657 1.58
REMARK 500 O HOH B 518 2H HOH B 804 4657 1.61
REMARK 500 2H HOH B 804 O HOH B 518 4647 1.61
REMARK 500 O HOH A 555 1H HOH B 663 2656 1.62
REMARK 500 1H HOH B 663 O HOH A 555 2656 1.62
REMARK 500 HE ARG B 20 2H HOH B 589 4657 1.63
REMARK 500 2H HOH B 589 HE ARG B 20 4647 1.63
REMARK 500 O HOH A 693 1H HOH B 621 2656 1.65
REMARK 500 1H HOH B 621 O HOH A 693 2656 1.65
REMARK 500 1H HOH A 946 O HOH B 505 3455 1.66
REMARK 500 O HOH B 505 1H HOH A 946 3545 1.66
REMARK 500 1HH1 ARG B 196 O HOH A 804 2657 1.69
REMARK 500 O HOH A 804 1HH1 ARG B 196 2657 1.69
REMARK 500 1HH1 ARG A 196 O HOH B 677 3445 1.70
REMARK 500 2H HOH B 646 HE ARG A 96 2656 1.70
REMARK 500 1HH2 ARG A 166 2H HOH B 505 3455 1.70
REMARK 500 O HOH A 638 1H HOH B 677 3445 1.70
REMARK 500 2H HOH B 505 1HH2 ARG A 166 3545 1.70
REMARK 500 O HOH B 677 1HH1 ARG A 196 3555 1.70
REMARK 500 HE ARG A 96 2H HOH B 646 2656 1.70
REMARK 500 1H HOH B 677 O HOH A 638 3555 1.70
REMARK 500 O HOH A 595 1H HOH B 917 3455 1.71
REMARK 500 1H HOH B 917 O HOH A 595 3545 1.71
REMARK 500 O HOH A 553 2H HOH B 624 2656 1.72
REMARK 500 1H HOH B 631 O HOH A 642 2656 1.72
REMARK 500 2H HOH B 624 O HOH A 553 2656 1.72
REMARK 500 O HOH A 642 1H HOH B 631 2656 1.72
REMARK 500 1H HOH B 941 O HOH A 940 2656 1.73
REMARK 500 O HOH A 940 1H HOH B 941 2656 1.73
REMARK 500 2H HOH B 518 2H HOH B 804 4657 1.73
REMARK 500 2H HOH B 804 2H HOH B 518 4647 1.73
REMARK 500 1H HOH A 555 2H HOH B 560 2656 1.74
REMARK 500 2HH2 ARG B 138 2H HOH A 694 2656 1.74
REMARK 500 2H HOH B 560 1H HOH A 555 2656 1.74
REMARK 500 2H HOH A 694 2HH2 ARG B 138 2656 1.74
REMARK 500 1HD2 ASN B 161 1H HOH A 693 2656 1.75
REMARK 500 1H HOH A 693 1HD2 ASN B 161 2656 1.75
REMARK 500 2HH2 ARG A 78 1H HOH B 600 2656 1.77
REMARK 500 O HOH B 584 1H HOH A 804 2657 1.77
REMARK 500 1H HOH B 600 2HH2 ARG A 78 2656 1.77
REMARK 500 1H HOH A 804 O HOH B 584 2657 1.77
REMARK 500 1H HOH A 951 O HOH B 953 2656 1.78
REMARK 500 O HOH A 694 2HH2 ARG B 138 2656 1.78
REMARK 500 O SER A 92 1H HOH B 645 2656 1.78
REMARK 500 1H HOH A 694 O HOH B 560 2656 1.78
REMARK 500 1H HOH B 645 O SER A 92 2656 1.78
REMARK 500 2HH2 ARG B 138 O HOH A 694 2656 1.78
REMARK 500 O HOH B 953 1H HOH A 951 2656 1.78
REMARK 500 O HOH B 560 1H HOH A 694 2656 1.78
REMARK 500 O ALA A 93 2H HOH B 663 2656 1.79
REMARK 500 2H HOH A 631 O HOH B 624 2656 1.79
REMARK 500 O HOH B 624 2H HOH A 631 2656 1.79
REMARK 500 O HOH B 952 2HH2 ARG A 96 2656 1.79
REMARK 500 2HH2 ARG A 96 O HOH B 952 2656 1.79
REMARK 500 2H HOH B 663 O ALA A 93 2656 1.79
REMARK 500 O HOH B 560 1H HOH A 555 2656 1.80
REMARK 500 1H HOH A 555 O HOH B 560 2656 1.80
REMARK 500 2H HOH B 643 2H HOH A 501 3555 1.82
REMARK 500 2H HOH A 501 2H HOH B 643 3445 1.82
REMARK 500 1H HOH B 806 2H HOH A 806 3545 1.82
REMARK 500 2H HOH A 806 1H HOH B 806 3455 1.82
REMARK 500 O HOH A 663 H ASN A 25 4556 1.82
REMARK 500 H ASN A 25 O HOH A 663 4546 1.82
REMARK 500 2H HOH B 643 OG SER A 57 3555 1.83
REMARK 500 OG SER A 57 2H HOH B 643 3445 1.83
REMARK 500 HE ARG A 96 O HOH B 645 2656 1.83
REMARK 500 O HOH B 645 HE ARG A 96 2656 1.83
REMARK 500 2H HOH A 709 2H HOH A 504 4556 1.83
REMARK 500 2H HOH B 600 2HH2 ARG A 78 2656 1.83
REMARK 500 2H HOH A 504 2H HOH A 709 4546 1.83
REMARK 500 2HH2 ARG A 78 2H HOH B 600 2656 1.83
REMARK 500 2HD2 ASN B 161 2H HOH A 694 2656 1.84
REMARK 500 1H HOH B 554 1H HOH A 642 2656 1.84
REMARK 500 1H HOH A 642 1H HOH B 554 2656 1.84
REMARK 500 2H HOH A 694 2HD2 ASN B 161 2656 1.84
REMARK 500 2H HOH B 630 2H HOH B 601 4647 1.85
REMARK 500 O HOH A 695 2H HOH B 707 2656 1.85
REMARK 500 2H HOH B 601 2H HOH B 630 4657 1.85
REMARK 500 2H HOH B 707 O HOH A 695 2656 1.85
REMARK 500 2HH2 ARG A 138 OD1 ASN A 25 4556 1.86
REMARK 500 2H HOH A 621 1H HOH A 522 4556 1.86
REMARK 500 OD1 ASN A 25 2HH2 ARG A 138 4546 1.86
REMARK 500 1H HOH A 522 2H HOH A 621 4546 1.86
REMARK 500 1H HOH B 707 O HOH A 700 2656 1.87
REMARK 500 O HOH A 700 1H HOH B 707 2656 1.87
REMARK 500 HE ARG A 96 1H HOH B 645 2656 1.87
REMARK 500 1H HOH B 645 HE ARG A 96 2656 1.87
REMARK 500 2H HOH A 707 OD1 ASN A 25 4556 1.87
REMARK 500 OD1 ASN A 25 2H HOH A 707 4546 1.87
REMARK 500 2HH1 ARG B 138 1H HOH A 695 2656 1.88
REMARK 500 1H HOH A 695 2HH1 ARG B 138 2656 1.88
REMARK 500 O HOH A 630 HG SER B 57 2657 1.88
REMARK 500 HG SER B 57 O HOH A 630 2657 1.88
REMARK 500 O ALA A 76 2H HOH B 621 2656 1.89
REMARK 500 2HH2 ARG B 138 O HOH A 695 2656 1.89
REMARK 500 2HH2 ARG B 138 1H HOH A 695 2656 1.89
REMARK 500 1H HOH A 695 2HH2 ARG B 138 2656 1.89
REMARK 500 O HOH A 695 2HH2 ARG B 138 2656 1.89
REMARK 500 2H HOH B 621 O ALA A 76 2656 1.89
REMARK 500 O HOH B 643 2H HOH A 501 3555 1.89
REMARK 500 2H HOH A 501 O HOH B 643 3445 1.89
REMARK 500 O ASP A 21 2H HOH A 560 4546 1.91
REMARK 500 2H HOH A 560 O ASP A 21 4556 1.91
REMARK 500 O THR B 19 1H HOH B 630 4657 1.92
REMARK 500 1H HOH B 630 O THR B 19 4647 1.92
REMARK 500 HE ARG A 166 O HOH B 505 3455 1.92
REMARK 500 O HOH B 505 HE ARG A 166 3545 1.92
REMARK 500 2H HOH A 518 O HOH A 645 4546 1.93
REMARK 500 2H HOH A 504 O HOH A 709 4546 1.93
REMARK 500 O HOH A 709 2H HOH A 504 4556 1.93
REMARK 500 2HH2 ARG B 17 OE2 GLU A 205 2657 1.93
REMARK 500 O HOH A 645 2H HOH A 518 4556 1.93
REMARK 500 OE2 GLU A 205 2HH2 ARG B 17 2657 1.93
REMARK 500 2H HOH A 904 1H HOH B 640 3445 1.95
REMARK 500 1H HOH B 640 2H HOH A 904 3555 1.95
REMARK 500 O LEU A 133 1HD2 ASN A 25 4556 1.96
REMARK 500 1HD2 ASN A 25 O LEU A 133 4546 1.96
REMARK 500 1H HOH A 640 O HOH B 941 2656 1.96
REMARK 500 O HOH B 941 1H HOH A 640 2656 1.96
REMARK 500 1H HOH B 518 1H HOH B 815 4657 1.97
REMARK 500 2H HOH A 951 OE1 GLN B 103 2656 1.97
REMARK 500 O HOH A 621 1H HOH A 522 4556 1.97
REMARK 500 1H HOH B 815 1H HOH B 518 4647 1.97
REMARK 500 1H HOH A 522 O HOH A 621 4546 1.97
REMARK 500 OE1 GLN B 103 2H HOH A 951 2656 1.97
REMARK 500 O HOH A 806 1H HOH B 806 3455 1.98
REMARK 500 1H HOH A 560 O ASP A 22 4556 1.98
REMARK 500 1H HOH B 806 O HOH A 806 3545 1.98
REMARK 500 2HH2 ARG A 78 O HOH B 600 2656 1.98
REMARK 500 O HOH B 589 HE ARG B 20 4647 1.98
REMARK 500 O HOH A 505 1H HOH B 505 3455 1.98
REMARK 500 O HOH B 600 2HH2 ARG A 78 2656 1.98
REMARK 500 O ASP A 22 1H HOH A 560 4546 1.98
REMARK 500 HE ARG B 20 O HOH B 589 4657 1.98
REMARK 500 1H HOH B 505 O HOH A 505 3545 1.98
REMARK 500 2H HOH A 695 NH2 ARG B 138 2656 1.99
REMARK 500 1H HOH B 584 1H HOH A 804 2657 1.99
REMARK 500 1H HOH A 804 1H HOH B 584 2657 1.99
REMARK 500 NH2 ARG B 138 2H HOH A 695 2656 1.99
REMARK 500 2H HOH A 694 NH2 ARG B 138 2656 2.00
REMARK 500 NH2 ARG B 138 2H HOH A 694 2656 2.00
REMARK 500 OD1 ASP A 165 1HH2 ARG B 166 3455 2.00
REMARK 500 1HH2 ARG B 166 OD1 ASP A 165 3545 2.00
REMARK 500 2H HOH B 645 2H HOH A 553 2656 2.00
REMARK 500 2H HOH A 553 2H HOH B 645 2656 2.00
REMARK 500 1H HOH B 621 2H HOH A 693 2656 2.01
REMARK 500 H ASP A 66 O HOH B 695 3445 2.01
REMARK 500 O HOH B 695 H ASP A 66 3555 2.01
REMARK 500 2H ARG B 17 O HOH B 669 4657 2.01
REMARK 500 2H HOH A 693 1H HOH B 621 2656 2.01
REMARK 500 2H HOH A 518 2H HOH A 645 4546 2.01
REMARK 500 2H HOH A 621 O ASN A 25 4556 2.01
REMARK 500 O ASN A 25 2H HOH A 621 4546 2.01
REMARK 500 2H HOH A 645 2H HOH A 518 4556 2.01
REMARK 500 O HOH B 669 2H ARG B 17 4647 2.01
REMARK 500 O HOH B 666 2H HOH A 589 2657 2.02
REMARK 500 2H HOH A 589 O HOH B 666 2657 2.02
REMARK 500 2H HOH B 505 1H HOH A 505 3545 2.02
REMARK 500 2H HOH B 953 1H HOH A 951 2656 2.02
REMARK 500 1H HOH A 951 2H HOH B 953 2656 2.02
REMARK 500 1H HOH A 505 2H HOH B 505 3455 2.02
REMARK 500 1H HOH A 642 2H HOH B 552 2656 2.02
REMARK 500 2H HOH B 552 1H HOH A 642 2656 2.02
REMARK 500 2H HOH B 552 O HOH A 642 2656 2.03
REMARK 500 O HOH B 573 1H HOH A 589 2657 2.03
REMARK 500 1H HOH A 694 1H HOH B 560 2656 2.03
REMARK 500 2H HOH A 700 OD1 ASP B 134 2656 2.03
REMARK 500 1H HOH A 589 O HOH B 573 2657 2.03
REMARK 500 O HOH A 642 2H HOH B 552 2656 2.03
REMARK 500 1H HOH B 560 1H HOH A 694 2656 2.03
REMARK 500 OD1 ASP B 134 2H HOH A 700 2656 2.03
REMARK 500 1H HOH A 505 O HOH B 505 3455 2.03
REMARK 500 O HOH B 505 1H HOH A 505 3545 2.03
REMARK 500 1H HOH A 640 1H HOH B 941 2656 2.04
REMARK 500 2H HOH B 663 H GLU A 97 2656 2.04
REMARK 500 H GLU A 97 2H HOH B 663 2656 2.04
REMARK 500 O HOH B 554 1H HOH A 642 2656 2.04
REMARK 500 1H HOH B 941 1H HOH A 640 2656 2.04
REMARK 500 1H HOH A 642 O HOH B 554 2656 2.04
REMARK 500 2HH2 ARG A 96 2H HOH B 952 2656 2.05
REMARK 500 2H HOH B 952 2HH2 ARG A 96 2656 2.05
REMARK 500 2H HOH B 946 HE ARG A 166 3545 2.05
REMARK 500 2H HOH B 554 1H HOH A 553 2656 2.05
REMARK 500 HE ARG A 166 2H HOH B 946 3455 2.05
REMARK 500 1H HOH A 553 2H HOH B 554 2656 2.05
REMARK 500 CA ASP A 22 2H HOH A 560 4546 2.06
REMARK 500 HG SER A 135 O HOH A 905 4556 2.06
REMARK 500 1H HOH A 693 1H HOH B 621 2656 2.06
REMARK 500 1H HOH B 621 1H HOH A 693 2656 2.06
REMARK 500 1H HOH B 557 1H HOH A 953 2656 2.06
REMARK 500 2H HOH A 550 OD1 ASP B 132 2656 2.06
REMARK 500 OD1 ASP B 132 2H HOH A 550 2656 2.06
REMARK 500 O HOH A 905 HG SER A 135 4546 2.06
REMARK 500 2H HOH A 560 CA ASP A 22 4556 2.06
REMARK 500 1H HOH A 953 1H HOH B 557 2656 2.06
REMARK 500 2H HOH A 653 2H HOH A 645 4546 2.07
REMARK 500 2H HOH A 645 2H HOH A 653 4556 2.07
REMARK 500 O HOH B 653 1H HOH B 804 4657 2.07
REMARK 500 2HH1 ARG B 96 2H HOH A 691 3555 2.07
REMARK 500 1H HOH A 555 1H HOH B 663 2656 2.07
REMARK 500 1H HOH B 804 O HOH B 653 4647 2.07
REMARK 500 1H HOH B 663 1H HOH A 555 2656 2.07
REMARK 500 2H HOH A 691 2HH1 ARG B 96 3445 2.07
REMARK 500 NE ARG A 166 2H HOH B 505 3455 2.08
REMARK 500 2H HOH A 804 NH1 ARG B 196 2657 2.08
REMARK 500 2H HOH B 505 NE ARG A 166 3545 2.08
REMARK 500 2H HOH A 638 1H HOH B 677 3445 2.08
REMARK 500 1H HOH B 630 2H HOH B 601 4647 2.08
REMARK 500 2H HOH B 512 1H HOH A 686 3555 2.08
REMARK 500 2H HOH B 601 1H HOH B 630 4657 2.08
REMARK 500 1H HOH B 946 1H HOH A 505 3545 2.08
REMARK 500 NH1 ARG B 196 2H HOH A 804 2657 2.08
REMARK 500 1H HOH A 505 1H HOH B 946 3455 2.08
REMARK 500 1H HOH B 677 2H HOH A 638 3555 2.08
REMARK 500 1H HOH A 686 2H HOH B 512 3445 2.08
REMARK 500 1H HOH B 677 1HH1 ARG A 196 3555 2.09
REMARK 500 NH2 ARG B 96 1HZ LYS A 65 3555 2.09
REMARK 500 1HH1 ARG A 196 1H HOH B 677 3445 2.09
REMARK 500 1H HOH A 815 O HOH B 607 2657 2.09
REMARK 500 1HZ LYS A 65 NH2 ARG B 96 3445 2.09
REMARK 500 O HOH B 607 1H HOH A 815 2657 2.09
REMARK 500 1H HOH A 537 2HH1 ARG B 17 2657 2.10
REMARK 500 O ASP A 21 2H HOH A 663 4546 2.10
REMARK 500 2HH1 ARG B 17 1H HOH A 537 2657 2.10
REMARK 500 O HOH A 806 2H HOH B 806 3455 2.10
REMARK 500 2H HOH A 663 O ASP A 21 4556 2.10
REMARK 500 2H HOH B 806 O HOH A 806 3545 2.10
REMARK 500 O GLU B 131 2H HOH A 694 2656 2.11
REMARK 500 H ASN A 25 2H HOH A 663 4546 2.11
REMARK 500 1H HOH B 631 1H HOH A 642 2656 2.11
REMARK 500 O HOH B 815 1H HOH B 518 4647 2.11
REMARK 500 2H HOH B 953 2HH2 ARG A 96 2656 2.11
REMARK 500 2H HOH A 663 H ASN A 25 4556 2.11
REMARK 500 2HH2 ARG A 96 2H HOH B 953 2656 2.11
REMARK 500 1H HOH B 518 O HOH B 815 4657 2.11
REMARK 500 2H HOH A 694 O GLU B 131 2656 2.11
REMARK 500 2H HOH A 553 2H HOH B 646 2656 2.11
REMARK 500 2H HOH B 646 2H HOH A 553 2656 2.11
REMARK 500 1H HOH A 642 1H HOH B 631 2656 2.11
REMARK 500 O LEU B 133 2H HOH A 695 2656 2.12
REMARK 500 1H HOH B 517 O HOH B 594 4657 2.12
REMARK 500 H GLY A 26 1H HOH A 560 4546 2.12
REMARK 500 1HE2 GLN B 103 1H HOH A 572 3555 2.12
REMARK 500 1H HOH A 572 1HE2 GLN B 103 3445 2.12
REMARK 500 NH2 ARG A 78 1H HOH B 600 2656 2.12
REMARK 500 1H HOH B 600 NH2 ARG A 78 2656 2.12
REMARK 500 2H HOH A 695 O LEU B 133 2656 2.12
REMARK 500 1H HOH A 560 H GLY A 26 4556 2.12
REMARK 500 O HOH B 594 1H HOH B 517 4647 2.12
REMARK 500 2H HOH B 621 O HOH A 597 2656 2.13
REMARK 500 1H HOH A 685 1H HOH B 556 3445 2.13
REMARK 500 O HOH A 686 2H HOH B 512 3445 2.13
REMARK 500 O HOH A 597 2H HOH B 621 2656 2.13
REMARK 500 2H HOH A 693 O GLU B 131 2656 2.13
REMARK 500 1H HOH A 904 O HOH B 512 3445 2.13
REMARK 500 2H HOH B 512 O HOH A 686 3555 2.13
REMARK 500 O HOH B 512 1H HOH A 904 3555 2.13
REMARK 500 1H HOH B 556 1H HOH A 685 3555 2.13
REMARK 500 O GLU B 131 2H HOH A 693 2656 2.13
REMARK 500 1H HOH B 707 2H HOH A 700 2656 2.14
REMARK 500 O HOH A 695 H SER B 135 2656 2.14
REMARK 500 1HE2 GLN B 104 1H HOH A 687 3555 2.14
REMARK 500 1H HOH A 687 1HE2 GLN B 104 3445 2.14
REMARK 500 1H HOH B 589 NE ARG B 20 4647 2.14
REMARK 500 2HD2 ASN B 161 O HOH A 694 2656 2.14
REMARK 500 NE ARG B 20 1H HOH B 589 4657 2.14
REMARK 500 O HOH A 694 2HD2 ASN B 161 2656 2.14
REMARK 500 2H HOH A 700 1H HOH B 707 2656 2.14
REMARK 500 OE2 GLU A 201 1H HOH B 638 2657 2.14
REMARK 500 H SER B 135 O HOH A 695 2656 2.14
REMARK 500 1H HOH B 638 OE2 GLU A 201 2657 2.14
REMARK 500 N GLY A 26 1H HOH A 560 4546 2.15
REMARK 500 O HOH A 645 2HD2 ASN A 25 4556 2.15
REMARK 500 1H HOH A 560 N GLY A 26 4556 2.15
REMARK 500 O HOH A 572 1HE2 GLN B 103 3445 2.15
REMARK 500 1HE2 GLN B 103 O HOH A 572 3555 2.15
REMARK 500 2HD2 ASN A 25 O HOH A 645 4546 2.15
REMARK 500 1H HOH B 600 1HH2 ARG A 78 2656 2.16
REMARK 500 1H HOH B 518 2H HOH B 589 4657 2.16
REMARK 500 OE2 GLU B 205 1HH1 ARG B 17 4647 2.16
REMARK 500 2H HOH B 560 O HOH A 555 2656 2.16
REMARK 500 1HH1 ARG B 17 OE2 GLU B 205 4657 2.16
REMARK 500 O HOH A 560 H ASN A 25 4556 2.16
REMARK 500 2H HOH B 589 1H HOH B 518 4647 2.16
REMARK 500 1HH2 ARG A 78 1H HOH B 600 2656 2.16
REMARK 500 H ASN A 25 O HOH A 560 4546 2.16
REMARK 500 O HOH A 555 2H HOH B 560 2656 2.16
REMARK 500 O HOH B 518 1H HOH B 815 4657 2.17
REMARK 500 O HOH A 693 1HD2 ASN B 161 2656 2.17
REMARK 500 1H HOH A 946 OD1 ASP B 165 3455 2.17
REMARK 500 O SER A 61 2H HOH B 940 3445 2.17
REMARK 500 2H HOH A 562 OD2 ASP B 165 3455 2.17
REMARK 500 1HD2 ASN B 161 O HOH A 693 2656 2.17
REMARK 500 2H HOH B 560 1H HOH A 694 2656 2.17
REMARK 500 1H HOH B 815 O HOH B 518 4647 2.17
REMARK 500 OD2 ASP B 165 2H HOH A 562 3545 2.17
REMARK 500 1H HOH A 694 2H HOH B 560 2656 2.17
REMARK 500 OD1 ASP B 165 1H HOH A 946 3545 2.17
REMARK 500 1H HOH A 953 O HOH B 557 2656 2.17
REMARK 500 1H HOH A 553 O HOH B 554 2656 2.17
REMARK 500 O HOH B 557 1H HOH A 953 2656 2.17
REMARK 500 2H HOH B 940 O SER A 61 3555 2.17
REMARK 500 O HOH B 554 1H HOH A 553 2656 2.17
REMARK 500 HG SER B 57 1H HOH A 630 2657 2.18
REMARK 500 H ALA A 136 1H HOH A 520 4556 2.18
REMARK 500 1H HOH A 630 HG SER B 57 2657 2.18
REMARK 500 1H HOH A 520 H ALA A 136 4546 2.18
REMARK 500 1HH2 ARG B 166 1H HOH A 814 3545 2.19
REMARK 500 1H HOH A 814 1HH2 ARG B 166 3455 2.19
REMARK 500 1H HOH B 695 H LYS A 65 3555 2.19
REMARK 500 OD1 ASP B 165 1HH2 ARG A 166 3545 2.19
REMARK 500 1HH2 ARG A 166 OD1 ASP B 165 3455 2.19
REMARK 500 1H HOH A 560 O HOH A 575 4556 2.19
REMARK 500 H LYS A 65 1H HOH B 695 3445 2.19
REMARK 500 O HOH A 575 1H HOH A 560 4546 2.19
REMARK 500 2H HOH A 693 1HD2 ASN B 161 2656 2.20
REMARK 500 1H HOH B 677 1H HOH A 638 3555 2.20
REMARK 500 1H HOH A 800 O HOH A 707 4546 2.20
REMARK 500 1H HOH A 638 1H HOH B 677 3445 2.20
REMARK 500 O HOH A 707 1H HOH A 800 4556 2.20
REMARK 500 1HD2 ASN B 161 2H HOH A 693 2656 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 1CUW A SWS P00590 1 - 32 NOT IN ATOMS LIST
REMARK 999 1CUW A SWS P00590 230 - 230 NOT IN ATOMS LIST
REMARK 999 1CUW B SWS P00590 1 - 32 NOT IN ATOMS LIST
REMARK 999 1CUW B SWS P00590 230 - 230 NOT IN ATOMS LIST
DBREF 1CUW A 17 213 SWS P00590 CUTI_FUSSO 33 229
DBREF 1CUW B 17 213 SWS P00590 CUTI_FUSSO 33 229
SEQADV 1CUW ALA A 32 SWS P00590 ARG 48 CONFLICT
SEQADV 1CUW ALA A 82 SWS P00590 GLY 98 ENGINEERED
SEQADV 1CUW PHE A 85 SWS P00590 ALA 101 ENGINEERED
SEQADV 1CUW ILE A 184 SWS P00590 VAL 200 ENGINEERED
SEQADV 1CUW LEU A 185 SWS P00590 ALA 201 ENGINEERED
SEQADV 1CUW PHE A 189 SWS P00590 LEU 205 ENGINEERED
SEQADV 1CUW ALA B 32 SWS P00590 ARG 48 CONFLICT
SEQADV 1CUW ALA B 82 SWS P00590 GLY 98 ENGINEERED
SEQADV 1CUW PHE B 85 SWS P00590 ALA 101 ENGINEERED
SEQADV 1CUW ILE B 184 SWS P00590 VAL 200 ENGINEERED
SEQADV 1CUW LEU B 185 SWS P00590 ALA 201 ENGINEERED
SEQADV 1CUW PHE B 189 SWS P00590 LEU 205 ENGINEERED
SEQRES 1 A 214 LEU PRO THR SER ASN PRO ALA GLN GLU LEU GLU ALA ARG
SEQRES 2 A 214 GLN LEU GLY ARG THR THR ARG ASP ASP LEU ILE ASN GLY
SEQRES 3 A 214 ASN SER ALA SER CYS ALA ASP VAL ILE PHE ILE TYR ALA
SEQRES 4 A 214 ARG GLY SER THR GLU THR GLY ASN LEU GLY THR LEU GLY
SEQRES 5 A 214 PRO SER ILE ALA SER ASN LEU GLU SER ALA PHE GLY LYS
SEQRES 6 A 214 ASP GLY VAL TRP ILE GLN GLY VAL GLY GLY ALA TYR ARG
SEQRES 7 A 214 ALA THR LEU ALA ASP ASN PHE LEU PRO ARG GLY THR SER
SEQRES 8 A 214 SER ALA ALA ILE ARG GLU MET LEU GLY LEU PHE GLN GLN
SEQRES 9 A 214 ALA ASN THR LYS CYS PRO ASP ALA THR LEU ILE ALA GLY
SEQRES 10 A 214 GLY TYR SER GLN GLY ALA ALA LEU ALA ALA ALA SER ILE
SEQRES 11 A 214 GLU ASP LEU ASP SER ALA ILE ARG ASP LYS ILE ALA GLY
SEQRES 12 A 214 THR VAL LEU PHE GLY TYR THR LYS ASN LEU GLN ASN ARG
SEQRES 13 A 214 GLY ARG ILE PRO ASN TYR PRO ALA ASP ARG THR LYS VAL
SEQRES 14 A 214 PHE CYS ASN THR GLY ASP LEU VAL CYS THR GLY SER LEU
SEQRES 15 A 214 ILE ILE LEU ALA PRO HIS PHE ALA TYR GLY PRO ASP ALA
SEQRES 16 A 214 ARG GLY PRO ALA PRO GLU PHE LEU ILE GLU LYS VAL ARG
SEQRES 17 A 214 ALA VAL ARG GLY SER ALA
SEQRES 1 B 214 LEU PRO THR SER ASN PRO ALA GLN GLU LEU GLU ALA ARG
SEQRES 2 B 214 GLN LEU GLY ARG THR THR ARG ASP ASP LEU ILE ASN GLY
SEQRES 3 B 214 ASN SER ALA SER CYS ALA ASP VAL ILE PHE ILE TYR ALA
SEQRES 4 B 214 ARG GLY SER THR GLU THR GLY ASN LEU GLY THR LEU GLY
SEQRES 5 B 214 PRO SER ILE ALA SER ASN LEU GLU SER ALA PHE GLY LYS
SEQRES 6 B 214 ASP GLY VAL TRP ILE GLN GLY VAL GLY GLY ALA TYR ARG
SEQRES 7 B 214 ALA THR LEU ALA ASP ASN PHE LEU PRO ARG GLY THR SER
SEQRES 8 B 214 SER ALA ALA ILE ARG GLU MET LEU GLY LEU PHE GLN GLN
SEQRES 9 B 214 ALA ASN THR LYS CYS PRO ASP ALA THR LEU ILE ALA GLY
SEQRES 10 B 214 GLY TYR SER GLN GLY ALA ALA LEU ALA ALA ALA SER ILE
SEQRES 11 B 214 GLU ASP LEU ASP SER ALA ILE ARG ASP LYS ILE ALA GLY
SEQRES 12 B 214 THR VAL LEU PHE GLY TYR THR LYS ASN LEU GLN ASN ARG
SEQRES 13 B 214 GLY ARG ILE PRO ASN TYR PRO ALA ASP ARG THR LYS VAL
SEQRES 14 B 214 PHE CYS ASN THR GLY ASP LEU VAL CYS THR GLY SER LEU
SEQRES 15 B 214 ILE ILE LEU ALA PRO HIS PHE ALA TYR GLY PRO ASP ALA
SEQRES 16 B 214 ARG GLY PRO ALA PRO GLU PHE LEU ILE GLU LYS VAL ARG
SEQRES 17 B 214 ALA VAL ARG GLY SER ALA
FORMUL 3 HOH *414(H2 O1)
HELIX 1 1 SER A 28 SER A 30 5 3
HELIX 2 2 GLY A 49 PHE A 63 1 15
HELIX 3 3 LYS A 65 GLY A 67 5 3
HELIX 4 4 ALA A 82 PHE A 85 5 4
HELIX 5 5 SER A 92 LYS A 108 1 17
HELIX 6 6 SER A 120 GLU A 131 5 12
HELIX 7 7 SER A 135 LYS A 140 1 6
HELIX 8 8 ALA A 164 ARG A 166 5 3
HELIX 9 9 LEU A 176 THR A 179 1 4
HELIX 10 10 ALA A 186 PHE A 189 5 4
HELIX 11 11 GLY A 192 ARG A 196 1 5
HELIX 12 12 PRO A 198 ARG A 211 1 14
HELIX 13 13 ASP B 22 ASN B 25 1 4
HELIX 14 14 GLY B 49 PHE B 63 1 15
HELIX 15 15 LYS B 65 GLY B 67 5 3
HELIX 16 16 ALA B 82 PHE B 85 5 4
HELIX 17 17 SER B 92 LYS B 108 1 17
HELIX 18 18 SER B 120 ASP B 132 5 13
HELIX 19 19 SER B 135 LYS B 140 1 6
HELIX 20 20 ALA B 164 ARG B 166 5 3
HELIX 21 21 LEU B 176 CYS B 178 5 3
HELIX 22 22 ALA B 186 PHE B 189 5 4
HELIX 23 23 GLY B 192 ARG B 196 1 5
HELIX 24 24 PRO B 198 VAL B 210 1 13
SHEET 1 A 5 VAL A 68 GLY A 72 0
SHEET 2 A 5 VAL A 34 ALA A 39 1 N VAL A 34 O TRP A 69
SHEET 3 A 5 THR A 113 TYR A 119 1 N THR A 113 O ILE A 35
SHEET 4 A 5 ILE A 141 PHE A 147 1 N ALA A 142 O LEU A 114
SHEET 5 A 5 THR A 167 PHE A 170 1 N LYS A 168 O THR A 144
SHEET 1 B 5 VAL B 68 GLY B 72 0
SHEET 2 B 5 VAL B 34 ALA B 39 1 N VAL B 34 O TRP B 69
SHEET 3 B 5 THR B 113 TYR B 119 1 N THR B 113 O ILE B 35
SHEET 4 B 5 ILE B 141 PHE B 147 1 N ALA B 142 O LEU B 114
SHEET 5 B 5 THR B 167 PHE B 170 1 N LYS B 168 O THR B 144
SSBOND 1 CYS A 31 CYS A 109
SSBOND 2 CYS A 171 CYS A 178
SSBOND 3 CYS B 31 CYS B 109
SSBOND 4 CYS B 171 CYS B 178
SITE 1 CAA 3 SER A 120 HIS A 188 ASP A 175
SITE 1 CAB 3 SER B 120 HIS B 188 ASP B 175
CRYST1 130.400 54.700 69.840 90.00 116.10 90.00 C 1 2 1 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 0.007669 0.000000 0.003757 0.00000
SCALE2 0.000000 0.018282 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015944 0.00000
MTRIX1 1 -0.869619 0.243789 -0.429335 91.69283 1
MTRIX2 1 0.253527 -0.525687 -0.812021 66.51099 1
MTRIX3 1 -0.423657 -0.814997 0.395340 71.64167 1 |