| content |
HEADER HYDROLASE (SERINE ESTERASE) 16-NOV-95 1CUG
TITLE CUTINASE, R17E, N172K 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: R17E, N172K
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 1CUG 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 : 15049
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 : 1774
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 612
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 39.7
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) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.47
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 1CUG 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 : 15227
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 (%) : 87.0
REMARK 200 DATA REDUNDANCY : 3.3 %
REMARK 200 R MERGE (I) : 0.037
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 1HD2 ASN 27 H VAL 169 1556 1.29
REMARK 500 H VAL 169 1HD2 ASN 27 1554 1.29
REMARK 500 O HOH 502 2H HOH 808 2556 1.68
REMARK 500 2H HOH 808 O HOH 502 2546 1.68
REMARK 500 O HOH 605 1H HOH 912 1655 1.77
REMARK 500 1H HOH 912 O HOH 605 1455 1.77
REMARK 500 O VAL 210 2H HOH 542 1455 1.80
REMARK 500 2H HOH 904 O HOH 959 2556 1.80
REMARK 500 1HH2 ARG 196 OD1 ASP 132 2556 1.80
REMARK 500 OD1 ASP 132 1HH2 ARG 196 2546 1.80
REMARK 500 1H HOH 589 O HOH 551 2556 1.80
REMARK 500 O HOH 551 1H HOH 589 2546 1.80
REMARK 500 O HOH 959 2H HOH 904 2546 1.80
REMARK 500 2H HOH 542 O VAL 210 1655 1.80
REMARK 500 O ASP 139 1H HOH 540 1455 1.83
REMARK 500 OG1 THR 113 2H HOH 603 1455 1.83
REMARK 500 1H HOH 540 O ASP 139 1655 1.83
REMARK 500 2H HOH 603 OG1 THR 113 1655 1.83
REMARK 500 1H HOH 566 O ASN 25 1554 1.85
REMARK 500 OG1 THR 43 2HH2 ARG 166 1655 1.85
REMARK 500 1H HOH 518 OG1 THR 173 1556 1.85
REMARK 500 OG1 THR 173 1H HOH 518 1554 1.85
REMARK 500 2HH2 ARG 166 OG1 THR 43 1455 1.85
REMARK 500 O ASN 25 1H HOH 566 1556 1.85
REMARK 500 1H HOH 804 O HOH 548 2556 1.86
REMARK 500 O HOH 556 2H HOH 813 1556 1.86
REMARK 500 1H HOH 590 O HOH 809 2556 1.86
REMARK 500 2H HOH 813 O HOH 556 1554 1.86
REMARK 500 O HOH 809 1H HOH 590 2546 1.86
REMARK 500 O HOH 548 1H HOH 804 2546 1.86
REMARK 500 O HOH 521 H GLY 174 1556 1.87
REMARK 500 H GLY 174 O HOH 521 1554 1.87
REMARK 500 O HOH 924 1H HOH 680 1554 1.88
REMARK 500 1H HOH 680 O HOH 924 1556 1.88
REMARK 500 1H HOH 569 O HOH 806 1655 1.89
REMARK 500 O HOH 806 1H HOH 569 1455 1.89
REMARK 500 1HD2 ASN 152 O HOH 522 1554 1.91
REMARK 500 O HOH 522 1HD2 ASN 152 1556 1.91
REMARK 500 O HOH 815 2H HOH 551 2556 1.92
REMARK 500 2H HOH 551 O HOH 815 2546 1.92
REMARK 500 O ALA 209 1H HOH 539 1455 1.94
REMARK 500 1H HOH 539 O ALA 209 1655 1.94
REMARK 500 H GLY 82 OD2 ASP 139 1655 1.95
REMARK 500 OD2 ASP 139 H GLY 82 1455 1.95
REMARK 500 1H HOH 948 O HOH 644 1655 1.97
REMARK 500 O HOH 644 1H HOH 948 1455 1.97
REMARK 500 O HOH 543 2H HOH 595 1655 1.97
REMARK 500 O HOH 900 1H HOH 502 2546 1.97
REMARK 500 1H HOH 502 O HOH 900 2556 1.97
REMARK 500 2H HOH 595 O HOH 543 1455 1.97
REMARK 500 O ARG 211 2H HOH 684 1455 1.98
REMARK 500 2H HOH 684 O ARG 211 1655 1.98
REMARK 500 2H HOH 900 OD1 ASN 58 2546 1.99
REMARK 500 OD1 ASN 58 2H HOH 900 2556 1.99
REMARK 500 2H HOH 815 OG SER 92 2556 2.02
REMARK 500 OG SER 92 2H HOH 815 2546 2.02
REMARK 500 1H HOH 521 H GLY 174 1556 2.03
REMARK 500 H GLY 174 1H HOH 521 1554 2.03
REMARK 500 2H HOH 605 1H HOH 912 1655 2.06
REMARK 500 1H HOH 912 2H HOH 605 1455 2.06
REMARK 500 1H HOH 809 1H HOH 590 2546 2.06
REMARK 500 1H HOH 590 1H HOH 809 2556 2.06
REMARK 500 2HD2 ASN 27 O HOH 802 1556 2.07
REMARK 500 O HOH 802 2HD2 ASN 27 1554 2.07
REMARK 500 O GLY 157 2H HOH 524 1554 2.08
REMARK 500 N VAL 169 1HD2 ASN 27 1554 2.08
REMARK 500 1HD2 ASN 27 N VAL 169 1556 2.08
REMARK 500 2H HOH 524 O GLY 157 1556 2.08
REMARK 500 H VAL 169 ND2 ASN 27 1554 2.09
REMARK 500 ND2 ASN 27 H VAL 169 1556 2.09
REMARK 500 2H HOH 505 O HOH 579 1455 2.10
REMARK 500 1H HOH 804 1H HOH 548 2556 2.10
REMARK 500 1H HOH 548 1H HOH 804 2546 2.10
REMARK 500 2H HOH 524 2H HOH 650 1556 2.10
REMARK 500 O HOH 579 2H HOH 505 1655 2.10
REMARK 500 2H HOH 650 2H HOH 524 1554 2.10
REMARK 500 O HOH 944 1H HOH 536 1655 2.13
REMARK 500 1H HOH 518 HG1 THR 173 1556 2.13
REMARK 500 1H HOH 536 O HOH 944 1455 2.13
REMARK 500 HG1 THR 173 1H HOH 518 1554 2.13
REMARK 500 1H HOH 959 2H HOH 904 2546 2.14
REMARK 500 2H HOH 904 1H HOH 959 2556 2.14
REMARK 500 O LYS 172 2H HOH 800 1554 2.15
REMARK 500 2H HOH 800 O LYS 172 1556 2.15
REMARK 500 2H HOH 959 2H HOH 904 2546 2.15
REMARK 500 2H HOH 904 2H HOH 959 2556 2.15
REMARK 500 O HOH 804 HG SER 92 2556 2.16
REMARK 500 HG SER 92 O HOH 804 2546 2.16
REMARK 500 1H HOH 589 2H HOH 551 2556 2.19
REMARK 500 2H HOH 551 1H HOH 589 2546 2.19
REMARK 500 OE1 GLU 201 1H HOH 551 2556 2.19
REMARK 500 1H HOH 551 OE1 GLU 201 2546 2.19
REMARK 500 2H HOH 609 OD1 ASN 27 1554 2.20
REMARK 500 OD1 ASN 27 2H HOH 609 1556 2.20
REMARK 500 HG SER 92 2H HOH 815 2546 2.20
REMARK 500 2H HOH 815 HG SER 92 2556 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 1CUG SWS P00590 1 - 32 NOT IN ATOMS LIST
REMARK 999 1CUG SWS P00590 230 - 230 NOT IN ATOMS LIST
DBREF 1CUG 17 213 SWS P00590 CUTI_FUSSO 33 229
SEQADV 1CUG GLU 17 SWS P00590 ARG 33 ENGINEERED
SEQADV 1CUG ALA 32 SWS P00590 ARG 48 CONFLICT
SEQADV 1CUG LYS 172 SWS P00590 ASN 188 ENGINEERED
SEQRES 1 214 LEU PRO THR SER ASN PRO ALA GLN GLU LEU GLU ALA ARG
SEQRES 2 214 GLN LEU GLY GLU 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 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 *204(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 LYS 65 GLY 67 5 3
HELIX 5 5 LEU 81 ALA 85 5 5
HELIX 6 6 SER 92 LYS 108 1 17
HELIX 7 7 SER 120 ASP 132 5 13
HELIX 8 8 SER 135 LYS 140 1 6
HELIX 9 9 ALA 164 ARG 166 5 3
HELIX 10 10 LEU 176 THR 179 5 4
HELIX 11 11 ALA 186 LEU 189 5 4
HELIX 12 12 GLY 192 ARG 196 1 5
HELIX 13 13 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 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 |