| content |
HEADER HYDROLASE (SERINE ESTERASE) 28-NOV-95 1XZI
TITLE FUSARIUM SOLANI CUTINASE MUTANT WITH THR 119 REPLACED BY HIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CUTINASE;
COMPND 3 CHAIN: NULL;
COMPND 4 EC: 3.1.1.-;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: T119H
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 A.NICOLAS,C.CAMBILLAU
REVDAT 1 14-OCT-96 1XZI 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 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. 1.69 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) : 1.69
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 : 17873
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) : 0.148
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 : 1778
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 609
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) : 0.017
REMARK 3 BOND ANGLES (DEGREES) : 2.43
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 0.093 ANGSTROMS
REMARK 3 MEAN B (A**2) MAIN : 9.7
REMARK 3 MEAN B (A**2) SIDE : 19.1
REMARK 3 MEAN B (A**2) SOLVENT : 39.6
REMARK 4
REMARK 4 1XZI 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 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 : NULL
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 : XDS
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18097
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 (%) : 95.0
REMARK 200 DATA REDUNDANCY : 3.1
REMARK 200 R MERGE (I) : 0.056
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: 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 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 2HH2 ARG 166 HG1 THR 43 1455 1.21
REMARK 500 HG1 THR 43 2HH2 ARG 166 1655 1.21
REMARK 500 1HD2 ASN 27 H VAL 169 1556 1.26
REMARK 500 H VAL 169 1HD2 ASN 27 1554 1.26
REMARK 500 2HH1 ARG 196 1H HOH 663 2556 1.43
REMARK 500 1H HOH 663 2HH1 ARG 196 2546 1.43
REMARK 500 O HOH 565 1H HOH 576 1554 1.62
REMARK 500 1H HOH 576 O HOH 565 1556 1.62
REMARK 500 O HOH 674 2H HOH 634 1655 1.65
REMARK 500 2H HOH 634 O HOH 674 1455 1.65
REMARK 500 2H HOH 595 1H HOH 543 1455 1.69
REMARK 500 1H HOH 543 2H HOH 595 1655 1.69
REMARK 500 O HOH 603 HG1 THR 113 1655 1.78
REMARK 500 HG1 THR 113 O HOH 603 1455 1.78
REMARK 500 H GLY 174 1H HOH 521 1554 1.79
REMARK 500 1H HOH 521 H GLY 174 1556 1.79
REMARK 500 1H HOH 547 O ALA 136 1655 1.82
REMARK 500 2H HOH 521 O HOH 508 1556 1.82
REMARK 500 O HOH 508 2H HOH 521 1554 1.82
REMARK 500 O ALA 136 1H HOH 547 1455 1.82
REMARK 500 2HH2 ARG 166 OG1 THR 43 1455 1.83
REMARK 500 OG1 THR 43 2HH2 ARG 166 1655 1.83
REMARK 500 1H HOH 713 O HOH 653 1554 1.85
REMARK 500 1HH2 ARG 196 OD1 ASP 132 2556 1.85
REMARK 500 O HOH 653 1H HOH 713 1556 1.85
REMARK 500 OD1 ASP 132 1HH2 ARG 196 2546 1.85
REMARK 500 O HOH 521 H GLY 174 1556 1.86
REMARK 500 H GLY 174 O HOH 521 1554 1.86
REMARK 500 O HOH 635 1H HOH 568 1456 1.88
REMARK 500 1H HOH 568 O HOH 635 1654 1.88
REMARK 500 HG1 THR 173 1H HOH 518 1554 1.88
REMARK 500 1H HOH 518 HG1 THR 173 1556 1.88
REMARK 500 O ASP 139 2H HOH 540 1455 1.88
REMARK 500 2H HOH 540 O ASP 139 1655 1.88
REMARK 500 1HD2 ASN 25 2H HOH 508 1556 1.89
REMARK 500 2H HOH 508 1HD2 ASN 25 1554 1.89
REMARK 500 1H HOH 659 O HOH 688 2546 1.91
REMARK 500 O HOH 688 1H HOH 659 2556 1.91
REMARK 500 2H HOH 634 1H HOH 674 1455 1.91
REMARK 500 1H HOH 674 2H HOH 634 1655 1.91
REMARK 500 O VAL 210 2H HOH 542 1455 1.93
REMARK 500 2H HOH 542 O VAL 210 1655 1.93
REMARK 500 O GLY 157 2H HOH 524 1554 1.93
REMARK 500 2H HOH 524 O GLY 157 1556 1.93
REMARK 500 1H HOH 568 1H HOH 635 1654 1.94
REMARK 500 1HD2 ASN 152 O ILE 24 1554 1.94
REMARK 500 1H HOH 635 1H HOH 568 1456 1.94
REMARK 500 O ILE 24 1HD2 ASN 152 1556 1.94
REMARK 500 O LYS 140 1H HOH 736 1455 1.97
REMARK 500 1H HOH 736 O LYS 140 1655 1.97
REMARK 500 2H HOH 628 O HOH 595 1655 1.97
REMARK 500 1HD2 ASN 27 N VAL 169 1556 1.97
REMARK 500 O HOH 595 2H HOH 628 1455 1.97
REMARK 500 N VAL 169 1HD2 ASN 27 1554 1.97
REMARK 500 1HZ LYS 206 2H HOH 581 1455 1.98
REMARK 500 1H HOH 505 O HOH 579 1455 1.98
REMARK 500 2HH1 ARG 196 O HOH 663 2556 1.98
REMARK 500 O HOH 627 H ASP 165 1655 1.98
REMARK 500 OD2 ASP 139 H GLY 82 1455 1.98
REMARK 500 2H HOH 581 1HZ LYS 206 1655 1.98
REMARK 500 O HOH 579 1H HOH 505 1655 1.98
REMARK 500 O HOH 663 2HH1 ARG 196 2546 1.98
REMARK 500 H ASP 165 O HOH 627 1455 1.98
REMARK 500 H GLY 82 OD2 ASP 139 1655 1.98
REMARK 500 1H HOH 520 2H HOH 615 1556 1.99
REMARK 500 1H HOH 522 OD1 ASN 152 1556 1.99
REMARK 500 OD1 ASN 152 1H HOH 522 1554 1.99
REMARK 500 2H HOH 615 1H HOH 520 1554 1.99
REMARK 500 O HOH 644 1H HOH 729 1455 2.01
REMARK 500 1H HOH 729 O HOH 644 1655 2.01
REMARK 500 O HOH 518 HG1 THR 173 1556 2.02
REMARK 500 HG1 THR 173 O HOH 518 1554 2.02
REMARK 500 2H HOH 521 H GLY 174 1556 2.03
REMARK 500 H GLY 174 2H HOH 521 1554 2.03
REMARK 500 O HOH 713 2HD2 ASN 25 1554 2.03
REMARK 500 2HD2 ASN 25 O HOH 713 1556 2.03
REMARK 500 O HOH 543 2H HOH 595 1655 2.04
REMARK 500 2H HOH 595 O HOH 543 1455 2.04
REMARK 500 H VAL 169 ND2 ASN 27 1554 2.07
REMARK 500 ND2 ASN 27 H VAL 169 1556 2.07
REMARK 500 O HOH 508 1HD2 ASN 25 1554 2.08
REMARK 500 1HD2 ASN 25 O HOH 508 1556 2.08
REMARK 500 1H HOH 603 HG1 THR 113 1655 2.10
REMARK 500 HG1 THR 113 1H HOH 603 1455 2.10
REMARK 500 1H HOH 665 O HOH 576 1554 2.11
REMARK 500 O HOH 576 1H HOH 665 1556 2.11
REMARK 500 O HOH 610 2H HOH 627 1455 2.12
REMARK 500 2H HOH 627 O HOH 610 1655 2.12
REMARK 500 1H HOH 670 O HOH 569 1456 2.12
REMARK 500 NH2 ARG 166 HG1 THR 43 1455 2.12
REMARK 500 1H HOH 713 1H HOH 653 1554 2.12
REMARK 500 O HOH 569 1H HOH 670 1654 2.12
REMARK 500 1H HOH 653 1H HOH 713 1556 2.12
REMARK 500 HG1 THR 43 NH2 ARG 166 1655 2.12
REMARK 500 2H HOH 634 2H HOH 674 1455 2.14
REMARK 500 O HOH 523 1H HOH 650 1556 2.14
REMARK 500 2H HOH 674 2H HOH 634 1655 2.14
REMARK 500 1H HOH 650 O HOH 523 1554 2.14
REMARK 500 O THR 167 1H HOH 523 1554 2.14
REMARK 500 1H HOH 523 O THR 167 1556 2.14
REMARK 500 O HOH 581 1HZ LYS 206 1655 2.15
REMARK 500 1HZ LYS 206 O HOH 581 1455 2.15
REMARK 500 2HH1 ARG 166 HG1 THR 43 1455 2.15
REMARK 500 HG1 THR 43 2HH1 ARG 166 1655 2.15
REMARK 500 1H HOH 638 1H HOH 559 2556 2.16
REMARK 500 1H HOH 559 1H HOH 638 2546 2.16
REMARK 500 OD1 ASP 165 2H HOH 580 1455 2.17
REMARK 500 2H HOH 580 OD1 ASP 165 1655 2.17
REMARK 500 O HOH 611 1H HOH 574 1554 2.18
REMARK 500 1H HOH 581 OD2 ASP 165 1655 2.18
REMARK 500 2H HOH 565 1H HOH 576 1554 2.18
REMARK 500 OD2 ASP 165 1H HOH 581 1455 2.18
REMARK 500 1H HOH 576 2H HOH 565 1556 2.18
REMARK 500 1H HOH 574 O HOH 611 1556 2.18
REMARK 500 1H HOH 544 1H HOH 659 2556 2.19
REMARK 500 1H HOH 659 1H HOH 544 2546 2.19
REMARK 525
REMARK 525 SOLVENT
REMARK 525 THE FOLLOWING SOLVENT MOLECULES LIE FARTHER THAN EXPECTED
REMARK 525 FROM THE PROTEIN OR NUCLEIC ACID MOLECULE AND MAY BE
REMARK 525 ASSOCIATED WITH A SYMMETRY RELATED MOLECULE (M=MODEL
REMARK 525 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 0 HOH 635 DISTANCE = 5.26 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: CAT
REMARK 800 SITE_DESCRIPTION: CATALYTIC TRIAD.
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 1XZI SWS P00590 1 - 32 NOT IN ATOMS LIST
REMARK 999 1XZI SWS P00590 230 - 230 NOT IN ATOMS LIST
DBREF 1XZI 17 213 SWS P00590 CUTI_FUSSO 33 229
SEQADV 1XZI ALA 32 SWS P00590 ARG 48 CLONING ARTIFACT
SEQADV 1XZI HIS 119 SWS P00590 TYR 135 ENGINEERED
SEQRES 1 214 LEU PRO THR SER ASN PRO ALA GLN GLU LEU GLU ALA ARG
SEQRES 2 214 GLN LEU GLU 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 HIS 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 *203(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 ARG 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 HIS 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 |