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HEADER HYDROLASE (SERINE ESTERASE) 28-NOV-95 1XZK
TITLE FUSARIUM SOLANI CUTINASE COMPLEX WITH DI(ISOPROPYL)PHOSPHATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CUTINASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.1.1.-;
COMPND 5 ENGINEERED: YES;
COMPND 6 OTHER_DETAILS: COMPLEX WITH DI(ISOPROPYL)PHOSPHATE
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 C.MARTINEZ,C.CAMBILLAU
REVDAT 1 30-NOV-96 1XZK 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.CAMBILLAU,C.MARTINEZ
REMARK 1 TITL CONTRIBUTION OF CUTINASE SERINE 42 SIDE CHAIN TO
REMARK 1 TITL 2 THE STABILIZATION OF THE OXYANION TRANSITION STATE
REMARK 1 REF BIOCHEMISTRY V. 35 398 1996
REMARK 1 REFN ASTM BICHAW US ISSN 0006-2960 0033
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,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 : 21537
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) : 0.161
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 : 3556
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 20
REMARK 3 SOLVENT ATOMS : 263
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) : 0.012
REMARK 3 BOND ANGLES (DEGREES) : 1.85
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 0.01 ANGSTROMS
REMARK 3 MOLECULE A
REMARK 3 MEAN B (A**2) MAIN : 20.3
REMARK 3 MEAN B (A**2) SIDE : 24.3
REMARK 3 MOLECULE B
REMARK 3 MEAN B (A**2) MAIN : 15.1
REMARK 3 MEAN B (A**2) SIDE : 20.1
REMARK 3 SOLVENT
REMARK 3 MEAN B (A**2) SOLVENT : 41.5
REMARK 3
REMARK 3 DISTANCE RESTRAINTS (A).
REMARK 3 RMSD BOND DISTANCE MOLECULE A : 0.011 A
REMARK 3 RMSD BOND DISTANCE MOLECULE B : 0.012 A
REMARK 3
REMARK 3 RMSD ANGLE DISTANCE MOLECULE A : 1.78 DEG
REMARK 3 RMSD ANGLE DISTANCE MOLECULE B : 1.85 DEG
REMARK 4
REMARK 4 1XZK 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 DI(ISOPROPYL)PHOSPHATE 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 : 1
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 : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22117
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 (%) : 90.0
REMARK 200 DATA REDUNDANCY : 2.66
REMARK 200 R MERGE (I) : 0.046
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 (%): 43.
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 47.39785
REMARK 290 SMTRY3 2 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 0.500
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 2H HOH 237 1HE2 GLN A 103 1554 1.22
REMARK 500 1HE2 GLN A 103 2H HOH 237 1556 1.22
REMARK 500 2HH2 ARG A 96 2H HOH 117 1556 1.28
REMARK 500 2H HOH 117 2HH2 ARG A 96 1554 1.28
REMARK 500 2H HOH 35 1HE2 GLN B 103 1556 1.53
REMARK 500 1HE2 GLN B 103 2H HOH 35 1554 1.53
REMARK 500 2HE2 GLN B 104 1HH1 ARG B 156 1655 1.59
REMARK 500 1HH1 ARG B 156 2HE2 GLN B 104 1455 1.59
REMARK 500 2HH2 ARG A 17 OD1 ASP B 111 2655 1.64
REMARK 500 OD1 ASP B 111 2HH2 ARG A 17 2645 1.64
REMARK 500 1H HOH 96 1HH1 ARG A 96 1554 1.74
REMARK 500 2H HOH 118 H ALA B 29 1455 1.74
REMARK 500 2H HOH 123 1H HOH 155 2655 1.74
REMARK 500 1H HOH 155 2H HOH 123 2645 1.74
REMARK 500 1HH1 ARG A 96 1H HOH 96 1556 1.74
REMARK 500 H ALA B 29 2H HOH 118 1655 1.74
REMARK 500 1HD2 ASN B 106 1H HOH 125 2645 1.78
REMARK 500 1H HOH 125 1HD2 ASN B 106 2655 1.78
REMARK 500 1H HOH 117 HG SER A 92 1554 1.81
REMARK 500 HG SER A 92 1H HOH 117 1556 1.81
REMARK 500 2HH1 ARG B 196 O ALA A 29 2646 1.82
REMARK 500 O ALA A 29 2HH1 ARG B 196 2656 1.82
REMARK 500 1H HOH 212 1H HOH 57 1455 1.83
REMARK 500 1H HOH 79 O HOH 69 1655 1.83
REMARK 500 1H HOH 57 1H HOH 212 1655 1.83
REMARK 500 O HOH 69 1H HOH 79 1455 1.83
REMARK 500 1HH1 ARG B 196 O SER A 28 2646 1.84
REMARK 500 O SER A 28 1HH1 ARG B 196 2656 1.84
REMARK 500 2H HOH 198 2H HOH 96 1556 1.85
REMARK 500 2H HOH 96 2H HOH 198 1554 1.85
REMARK 500 H GLY B 174 O HOH 79 1455 1.86
REMARK 500 2H HOH 32 O HOH 117 1556 1.86
REMARK 500 O HOH 117 2H HOH 32 1554 1.86
REMARK 500 O HOH 79 H GLY B 174 1655 1.86
REMARK 500 1HH1 ARG A 96 2H HOH 96 1556 1.88
REMARK 500 2H HOH 96 1HH1 ARG A 96 1554 1.88
REMARK 500 1H HOH 117 2HH1 ARG A 96 1554 1.89
REMARK 500 2HH1 ARG A 96 1H HOH 117 1556 1.89
REMARK 500 O HOH 249 2HD2 ASN B 25 1455 1.89
REMARK 500 2HD2 ASN B 25 O HOH 249 1655 1.89
REMARK 500 1HE2 GLN A 103 O HOH 237 1556 1.92
REMARK 500 O HOH 237 1HE2 GLN A 103 1554 1.92
REMARK 500 O HOH 160 1HD2 ASN B 27 1455 1.94
REMARK 500 1HD2 ASN B 27 O HOH 160 1655 1.94
REMARK 500 2HZ LYS A 140 O HOH 230 2656 1.95
REMARK 500 2HD2 ASN B 25 2H HOH 249 1655 1.95
REMARK 500 2H HOH 249 2HD2 ASN B 25 1455 1.95
REMARK 500 O HOH 230 2HZ LYS A 140 2646 1.95
REMARK 500 H VAL B 169 OD1 ASN B 27 1455 1.96
REMARK 500 OD1 ASN B 27 H VAL B 169 1655 1.96
REMARK 500 OG1 THR B 173 2H HOH 77 1455 1.98
REMARK 500 2H HOH 77 OG1 THR B 173 1655 1.98
REMARK 500 OG SER B 92 2H HOH 63 1554 1.98
REMARK 500 2H HOH 63 OG SER B 92 1556 1.98
REMARK 500 1H HOH 117 2HH2 ARG A 96 1554 1.98
REMARK 500 2HH2 ARG A 96 1H HOH 117 1556 1.98
REMARK 500 O HOH 117 2HH2 ARG A 96 1554 2.01
REMARK 500 1HE2 GLN B 103 O HOH 35 1554 2.01
REMARK 500 O HOH 35 1HE2 GLN B 103 1556 2.01
REMARK 500 2HH2 ARG A 96 O HOH 117 1556 2.01
REMARK 500 1HE2 GLN A 103 1H HOH 237 1556 2.03
REMARK 500 1H HOH 237 1HE2 GLN A 103 1554 2.03
REMARK 500 2H ARG A 17 1H HOH 176 2655 2.07
REMARK 500 2H HOH 117 2H HOH 32 1554 2.07
REMARK 500 2H HOH 32 2H HOH 117 1556 2.07
REMARK 500 1H HOH 176 2H ARG A 17 2645 2.07
REMARK 500 1HH1 ARG A 96 O HOH 96 1556 2.08
REMARK 500 O HOH 96 1HH1 ARG A 96 1554 2.08
REMARK 500 1HH1 ARG B 156 NE2 GLN B 104 1455 2.09
REMARK 500 NE2 GLN B 104 1HH1 ARG B 156 1655 2.09
REMARK 500 2H HOH 35 NE2 GLN B 103 1556 2.10
REMARK 500 NE2 GLN B 103 2H HOH 35 1554 2.10
REMARK 500 H ALA B 29 O HOH 118 1655 2.12
REMARK 500 2H HOH 77 HG1 THR B 173 1655 2.12
REMARK 500 O HOH 118 H ALA B 29 1455 2.12
REMARK 500 HG1 THR B 173 2H HOH 77 1455 2.12
REMARK 500 1HH1 ARG A 196 O HOH 223 2655 2.13
REMARK 500 2HZ LYS A 140 2H HOH 230 2656 2.13
REMARK 500 2H HOH 230 2HZ LYS A 140 2646 2.13
REMARK 500 O HOH 223 1HH1 ARG A 196 2645 2.13
REMARK 500 1HH1 ARG A 196 2H HOH 223 2655 2.14
REMARK 500 2H HOH 223 1HH1 ARG A 196 2645 2.14
REMARK 500 2HE2 GLN B 104 2HH1 ARG B 156 1655 2.15
REMARK 500 2HE2 GLN B 104 NH1 ARG B 156 1655 2.15
REMARK 500 2HH1 ARG B 156 2HE2 GLN B 104 1455 2.15
REMARK 500 NH1 ARG B 156 2HE2 GLN B 104 1455 2.15
REMARK 500 2H HOH 96 O HOH 198 1554 2.16
REMARK 500 1H HOH 79 H GLY B 174 1655 2.16
REMARK 500 1H HOH 249 2HD2 ASN B 25 1455 2.16
REMARK 500 2HD2 ASN B 25 1H HOH 249 1655 2.16
REMARK 500 H GLY B 174 1H HOH 79 1455 2.16
REMARK 500 O HOH 198 2H HOH 96 1556 2.16
REMARK 500 NE2 GLN A 103 2H HOH 237 1556 2.17
REMARK 500 2H HOH 237 NE2 GLN A 103 1554 2.17
REMARK 500 1HD2 ASN B 27 2H HOH 160 1655 2.19
REMARK 500 2H HOH 160 1HD2 ASN B 27 1455 2.19
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: CTA
REMARK 800 SITE_DESCRIPTION: CATALYTIC TRIAD IN MOLECULE A
REMARK 800
REMARK 800 SITE_IDENTIFIER: CTB
REMARK 800 SITE_DESCRIPTION: CATALYTIC TRIAD IN MOLECULE B
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 1XZK A SWS P00590 1 - 32 NOT IN ATOMS LIST
REMARK 999 1XZK A SWS P00590 230 - 230 NOT IN ATOMS LIST
REMARK 999 1XZK B SWS P00590 1 - 32 NOT IN ATOMS LIST
REMARK 999 1XZK B SWS P00590 230 - 230 NOT IN ATOMS LIST
DBREF 1XZK A 17 213 SWS P00590 CUTI_FUSSO 33 229
DBREF 1XZK B 17 213 SWS P00590 CUTI_FUSSO 33 229
SEQADV 1XZK ALA A 32 SWS P00590 ARG 48 CLONING ARTIFACT
SEQADV 1XZK ALA B 32 SWS P00590 ARG 48 CLONING ARTIFACT
SEQRES 1 A 214 LEU PRO THR SER ASN PRO ALA GLN GLU LEU GLU ALA ARG
SEQRES 2 A 214 GLN LEU GLU 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 GLY ASP ASN ALA 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 VAL ALA ALA PRO HIS LEU 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 GLU 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 GLY ASP ASN ALA 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 VAL ALA ALA PRO HIS LEU 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
HET DFP A 401 10
HET DFP B 401 10
HETNAM DFP DI(ISOPROPYL)PHOSPHATE
FORMUL 3 DFP 2(C6 H14 O3 P1)
FORMUL 4 HOH *263(H2 O1)
HELIX 1 1 SER A 28 SER A 30 5 3
HELIX 2 2 GLY A 49 ALA A 62 1 14
HELIX 3 3 LYS A 65 GLY A 67 5 3
HELIX 4 4 GLY A 82 ALA A 85 5 4
HELIX 5 5 SER A 92 LYS A 108 1 17
HELIX 6 6 SER A 120 ASP A 132 5 13
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 5 4
HELIX 10 10 ALA A 186 LEU 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 SER B 28 SER B 30 5 3
HELIX 15 15 GLY B 49 PHE B 63 1 15
HELIX 16 16 GLY B 82 ALA B 85 5 4
HELIX 17 17 SER B 92 LYS B 108 1 17
HELIX 18 18 GLN B 121 ASP B 132 1 12
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 ALA B 186 LEU B 189 5 4
HELIX 22 22 GLY B 192 ARG B 196 1 5
HELIX 23 23 PRO B 198 ARG B 211 1 14
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
LINK P DFP A 401 CB SER A 120
LINK P DFP A 401 OG SER A 120
LINK P DFP B 401 CB SER B 120
LINK P DFP B 401 OG SER B 120
SITE 1 CTA 3 SER A 120 HIS A 188 ASP A 175
SITE 1 CTB 3 SER B 120 HIS B 188 ASP B 175
CRYST1 37.200 94.800 55.000 90.00 101.30 90.00 P 1 21 1 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 0.026882 0.000000 0.005371 0.00000
SCALE2 0.000000 0.010549 0.000000 0.00000
SCALE3 0.000000 0.000000 0.018541 0.00000
MTRIX1 1 0.897880 0.086340 0.431690 -5.05890 1
MTRIX2 1 0.082080 -0.996220 0.028520 9.33670 1
MTRIX3 1 0.432510 0.009820 -0.901570 18.70270 1 |