| content |
HEADER LYASE 15-MAR-99 5YAS
TITLE HYDROXYNITRILE LYASE COMPLEXED WITH HEXAFLUOROACETONE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HYDROXYNITRILE LYASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: OXYNITRILASE;
COMPND 5 EC: 4.2.1.39;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HEVEA BRASILIENSIS;
SOURCE 3 ORGANISM_COMMON: PARA RUBBER TREE;
SOURCE 4 ORGAN: LEAF;
SOURCE 5 GENE: HNL;
SOURCE 6 EXPRESSION_SYSTEM: PICHIA PASTORIS;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: BHIL-D2;
SOURCE 8 EXPRESSION_SYSTEM_GENE: HNL
KEYWDS OXYNITRILASE, CYANOGENESIS, CYANOHYDRIN FORMATION, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.ZUEGG,U.G.WAGNER,M.GUGGANIG,C.KRATKY,J.ZUEGG,U.G.WAGNER,
AUTHOR 2 M.GUGGANIG,C.KRATKY
REVDAT 1 13-OCT-99 5YAS 0
JRNL AUTH J.ZUEGG,K.GRUBER,M.GUGGANIG,U.G.WAGNER,C.KRATKY
JRNL TITL THREE-DIMENSIONAL STRUCTURES OF ENZYME-SUBSTRATE
JRNL TITL 2 COMPLEXES OF THE HYDROXYNITRILE LYASE FROM HEVEA
JRNL TITL 3 BRASILIENSIS
JRNL REF PROTEIN SCI. V. 8 1990 1999
JRNL REFN ASTM PRCIEI US ISSN 0961-8368 0795
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.HASSLACHER,C.KRATKY,H.GRIENGL,H.SCHWAB,
REMARK 1 AUTH 2 S.D.KOHLWEIN
REMARK 1 TITL HYDROXYNITRILE LYASE FROM HEVEA BRASILIENSIS:
REMARK 1 TITL 2 MOLECULAR CHARACTERIZATION AND MECHANISM OF ENZYME
REMARK 1 TITL 3 CATALYSIS
REMARK 1 REF PROTEINS: STRUCT.,FUNCT., V. 27 438 1997
REMARK 1 REF 2 GENET.
REMARK 1 REFN ASTM PSFGEY US ISSN 0887-3585 0867
REMARK 1 REFERENCE 2
REMARK 1 AUTH U.G.WAGNER,M.SCHALL,M.HAYN,M.HASSLACHER,H.SCHWAB,
REMARK 1 AUTH 2 H.GRIENGL,C.KRATKY
REMARK 1 TITL CRYSTALLIZATION OF A HYDROXYNITRILE LYASE
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.D V. 52 591 1996
REMARK 1 REFN ASTM ABCRE6 DK ISSN 0907-4449 0766
REMARK 1 REFERENCE 3
REMARK 1 AUTH U.G.WAGNER,M.HASSLACHER,H.GRIENGL,H.SCHWAB,C.KRATKY
REMARK 1 TITL MECHANISM OF CYANOGENESIS: THE CRYSTAL STRUCTURE
REMARK 1 TITL 2 OF HYDROXYNITRILE LYASE FROM HEVEA BRASILIENSIS
REMARK 1 REF STRUCTURE (LONDON) V. 4 811 1996
REMARK 1 REFN ASTM STRUE6 UK ISSN 0969-2126 2005
REMARK 2
REMARK 2 RESOLUTION. 2.2 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 16.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 10000000.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0010
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 98.9
REMARK 3 NUMBER OF REFLECTIONS : 16673
REMARK 3
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.187
REMARK 3 FREE R VALUE : 0.241
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 795
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.009
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.28
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.70
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1557
REMARK 3 BIN R VALUE (WORKING SET) : 0.2050
REMARK 3 BIN FREE R VALUE : 0.2290
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.90
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 80
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.026
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2057
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 31
REMARK 3 SOLVENT ATOMS : 342
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 5.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 9.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.21
REMARK 3 ESD FROM SIGMAA (A) : 0.160
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.28
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.19
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.012
REMARK 3 BOND ANGLES (DEGREES) : 2.60
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.20
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.90
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : OVERALL
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
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 : PARAM19X.PRO
REMARK 3 PARAMETER FILE 2 : PARAM19X.SOL
REMARK 3 TOPOLOGY FILE 1 : TOPH19X.PRO
REMARK 3 TOPOLOGY FILE 2 : TOPH19X.SOL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5YAS COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-MAR-1999.
REMARK 100 THE RCSB ID CODE IS RCSB000668.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : MAR-1997
REMARK 200 TEMPERATURE (KELVIN) : 98.0
REMARK 200 PH : 7.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG
REMARK 200 BEAMLINE : X31
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.90
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22973
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 16.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.1
REMARK 200 DATA REDUNDANCY : 3.400
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.11100
REMARK 200 FOR THE DATA SET : 6.7000
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 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR
REMARK 200 REPLACEMENT
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: 1YAS
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.9
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.73
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M NATRIUM HEPES BUFFER PH=
REMARK 280 7.5 2 % PEG 400, 2.0 M AMMONIUM SULFATE, 20 DEGREES.
REMARK 280 SOAKING CONDITIONS: 25MM HEXAFLUOROACETONE HYDRATE
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
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 3555 -X,Y,1/2-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 1/2+X,1/2+Y,Z
REMARK 290 6555 1/2-X,1/2-Y,1/2+Z
REMARK 290 7555 1/2-X,1/2+Y,1/2-Z
REMARK 290 8555 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 64.07700
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 64.07700
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 23.73050
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 53.22050
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 23.73050
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 53.22050
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 64.07700
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 23.73050
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 53.22050
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 64.07700
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 23.73050
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 53.22050
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH 510 LIES ON A SPECIAL POSITION.
REMARK 375 HOH 511 LIES ON A SPECIAL POSITION.
REMARK 375 HOH 512 LIES ON A SPECIAL POSITION.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 4*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ILE A 12 CG1 - CB - CG2 ANGL. DEV. =-10.1 DEGREES
REMARK 500 ILE A 18 N - CA - CB ANGL. DEV. = 9.3 DEGREES
REMARK 500 LYS A 23 CA - C - N ANGL. DEV. = 10.6 DEGREES
REMARK 500 LEU A 29 CA - CB - CG ANGL. DEV. = 9.4 DEGREES
REMARK 500 GLU A 59 CA - C - N ANGL. DEV. = 10.3 DEGREES
REMARK 500 SER A 80 CA - C - N ANGL. DEV. = 11.1 DEGREES
REMARK 500 GLU A 95 CA - CB - CG ANGL. DEV. = 12.5 DEGREES
REMARK 500 VAL A 117 N - CA - CB ANGL. DEV. =-10.7 DEGREES
REMARK 500 GLN A 206 CA - CB - CG ANGL. DEV. =-10.9 DEGREES
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500
REMARK 500 SER A 80 47.21 -110.83
REMARK 500 LYS A 129 48.48 -111.56
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 730 DISTANCE = 5.73 ANGSTROMS
REMARK 525 0 HOH 739 DISTANCE = 5.07 ANGSTROMS
REMARK 525 0 HOH 754 DISTANCE = 5.11 ANGSTROMS
REMARK 525 0 HOH 779 DISTANCE = 7.76 ANGSTROMS
REMARK 525 0 HOH 838 DISTANCE = 5.18 ANGSTROMS
REMARK 525 0 HOH 841 DISTANCE = 5.57 ANGSTROMS
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: DSSP AND AUTHOR-DETERMINED
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: DSSP AND AUTHOR-DETERMINED
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: CAT
REMARK 800 SITE_DESCRIPTION:
REMARK 800 ACTIVE SITE.
REMARK 800
DBREF 5YAS A 2 257 SWS P52704 HNL_HEVBR 2 257
SEQRES 1 A 257 MET ALA PHE ALA HIS PHE VAL LEU ILE HIS THR ILE CYS
SEQRES 2 A 257 HIS GLY ALA TRP ILE TRP HIS LYS LEU LYS PRO LEU LEU
SEQRES 3 A 257 GLU ALA LEU GLY HIS LYS VAL THR ALA LEU ASP LEU ALA
SEQRES 4 A 257 ALA SER GLY VAL ASP PRO ARG GLN ILE GLU GLU ILE GLY
SEQRES 5 A 257 SER PHE ASP GLU TYR SER GLU PRO LEU LEU THR PHE LEU
SEQRES 6 A 257 GLU ALA LEU PRO PRO GLY GLU LYS VAL ILE LEU VAL GLY
SEQRES 7 A 257 GLU SER CYS GLY GLY LEU ASN ILE ALA ILE ALA ALA ASP
SEQRES 8 A 257 LYS TYR CYS GLU LYS ILE ALA ALA ALA VAL PHE HIS ASN
SEQRES 9 A 257 SER VAL LEU PRO ASP THR GLU HIS CYS PRO SER TYR VAL
SEQRES 10 A 257 VAL ASP LYS LEU MET GLU VAL PHE PRO ASP TRP LYS ASP
SEQRES 11 A 257 THR THR TYR PHE THR TYR THR LYS ASP GLY LYS GLU ILE
SEQRES 12 A 257 THR GLY LEU LYS LEU GLY PHE THR LEU LEU ARG GLU ASN
SEQRES 13 A 257 LEU TYR THR LEU CYS GLY PRO GLU GLU TYR GLU LEU ALA
SEQRES 14 A 257 LYS MET LEU THR ARG LYS GLY SER LEU PHE GLN ASN ILE
SEQRES 15 A 257 LEU ALA LYS ARG PRO PHE PHE THR LYS GLU GLY TYR GLY
SEQRES 16 A 257 SER ILE LYS LYS ILE TYR VAL TRP THR ASP GLN ASP GLU
SEQRES 17 A 257 ILE PHE LEU PRO GLU PHE GLN LEU TRP GLN ILE GLU ASN
SEQRES 18 A 257 TYR LYS PRO ASP LYS VAL TYR LYS VAL GLU GLY GLY ASP
SEQRES 19 A 257 HIS LYS LEU GLN LEU THR LYS THR LYS GLU ILE ALA GLU
SEQRES 20 A 257 ILE LEU GLN GLU VAL ALA ASP THR TYR ASN
HET SO4 400 5
HET SO4 401 5
HET SO4 402 5
HET SO4 403 5
HET FAC 300 11
HETNAM SO4 SULFATE ION
HETNAM FAC 1,1,1,3,3,3-HEXAFLUOROPROPANEDIOL
HETSYN FAC HEXAFLUOROACETONE HYDRATE
FORMUL 2 SO4 4(O4 S1 2-)
FORMUL 6 FAC C3 H2 O2 F6
FORMUL 7 HOH *342(H2 O1)
HELIX 1 HA LYS A 21 ALA A 28 1 8
HELIX 2 HB SER A 53 LEU A 68 1 16
HELIX 3 HC CYS A 81 CYS A 94 1 14
HELIX 4 HD1 SER A 115 PHE A 125 1 11
HELIX 5 HD2 GLY A 149 LEU A 157 1 9
HELIX 6 HD3 GLY A 162 THR A 173 1 12
HELIX 7 HD PHE A 179 LYS A 185 1 7
HELIX 8 HE LEU A 211 TYR A 222 1 12
HELIX 9 HF LYS A 236 TYR A 256 1 21
SHEET 1 S1 6 ALA A 4 ILE A 9 0
SHEET 2 S1 6 LYS A 32 LEU A 36 1
SHEET 3 S1 6 SER A 53 LEU A 68 -1
SHEET 4 S1 6 LYS A 96 ASN A 104 -1
SHEET 5 S1 6 LYS A 198 TRP A 203 1
SHEET 6 S1 6 LYS A 226 VAL A 230 1
SHEET 1 S2 3 THR A 132 LYS A 138 0
SHEET 2 S2 3 LYS A 141 LYS A 147 -1
SHEET 3 S2 3 GLY A 176 LEU A 178 -1
SITE 1 CAT 3 SER A 80 HIS A 235 ASP A 207
CRYST1 47.461 106.441 128.154 90.00 90.00 90.00 C 2 2 21 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 0.021070 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009395 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007803 0.00000 |