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HEADER LYASE 20-DEC-04 1YB6
TITLE HYDROXYNITRILE LYASE FROM HEVEA BRASILIENSIS IN COMPLEX
TITLE 2 WITH MANDELONITRILE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: (S)-ACETONE-CYANOHYDRIN LYASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: (S)-HYDROXYNITRILE LYASE; (S)-HYDROXYNITRILASE;
COMPND 5 OXYNITRILASE;
COMPND 6 EC: 4.1.2.39;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HEVEA BRASILIENSIS;
SOURCE 3 ORGANISM_COMMON: PARA RUBBER TREE;
SOURCE 4 TISSUE: LEAF;
SOURCE 5 GENE: HNL;
SOURCE 6 EXPRESSION_SYSTEM: PICHIA PASTORIS;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FUNGI;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: BHIL-D2
KEYWDS ALPHA-BETA HYDROLASE FOLD; SUBSTRATE COMPLEX; CATALYTIC
KEYWDS 2 TRIAD
EXPDTA X-RAY DIFFRACTION
AUTHOR K.GRUBER,G.GARTLER,C.KRATKY
REVDAT 1 20-DEC-05 1YB6 0
JRNL AUTH G.GARTLER,C.KRATKY,K.GRUBER
JRNL TITL STRUCTURAL DETERMINANTS OF THE ENANTIOSELECTIVITY
JRNL TITL 2 OF THE HYDROXYNITRILE LYASE FROM HEVEA BRASILIENSIS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH K.GRUBER,G.GARTLER,B.KRAMMER,H.SCHWAB,C.KRATKY
REMARK 1 TITL REACTION MECHANISM OF HYDROXYNITRILE LYASES OF THE
REMARK 1 TITL 2 ALPHA/BETA-HYDROLASE SUPERFAMILY: THE
REMARK 1 TITL 3 THREE-DIMENSIONAL STRUCTURE OF THE TRANSIENT
REMARK 1 TITL 4 ENZYME-SUBSTRATE COMPLEX CERTIFIES THE CRUCIAL
REMARK 1 TITL 5 ROLE OF LYS236
REMARK 1 REF J.BIOL.CHEM. V. 279 20501 2004
REMARK 1 REFN ASTM JBCHA3 US ISSN 0021-9258
REMARK 1 REFERENCE 2
REMARK 1 AUTH K.GRUBER,M.GUGGANIG,U.G.WAGNER,C.KRATKY
REMARK 1 TITL ATOMIC RESOLUTION CRYSTAL STRUCTURE OF
REMARK 1 TITL 2 HYDROXYNITRILE LYASE FROM HEVEA BRASILIENSIS
REMARK 1 REF BIOL.CHEM. V. 380 993 1999
REMARK 1 REFN GE ISSN 1431-6730
REMARK 1 REFERENCE 3
REMARK 1 AUTH J.ZUEGG,K.GRUBER,M.GUGGANIG,U.G.WAGNER,C.KRATKY
REMARK 1 TITL THREE-DIMENSIONAL STRUCTURES OF ENZYME-SUBSTRATE
REMARK 1 TITL 2 COMPLEXES OF THE HYDROXYNITRILE LYASE FROM HEVEA
REMARK 1 TITL 3 BRASILIENSIS
REMARK 1 REF PROTEIN SCI. V. 8 1990 1999
REMARK 1 REFN ASTM PRCIEI US ISSN 0961-8368
REMARK 1 REFERENCE 4
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 V. 4 811 1996
REMARK 1 REFN ASTM STRUE6 UK ISSN 0969-2126
REMARK 2
REMARK 2 RESOLUTION. 1.54 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.54
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 23.68
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1782074.180
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 95.9
REMARK 3 NUMBER OF REFLECTIONS : 46514
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) : 0.167
REMARK 3 FREE R VALUE : 0.182
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2365
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.004
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 15
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.54
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.58
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.30
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3015
REMARK 3 BIN R VALUE (WORKING SET) : 0.1710
REMARK 3 BIN FREE R VALUE : 0.1880
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.80
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 151
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.015
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2149
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 20
REMARK 3 SOLVENT ATOMS : 286
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 13.80
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 14.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.49000
REMARK 3 B22 (A**2) : 0.53000
REMARK 3 B33 (A**2) : -0.04000
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) : 0.14
REMARK 3 ESD FROM SIGMAA (A) : 0.02
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) : 0.15
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.05
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.004
REMARK 3 BOND ANGLES (DEGREES) : 1.30
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.70
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.77
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 0.830 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.210 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.710 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.470 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.38
REMARK 3 BSOL : 50.78
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : MN.PAR
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : ION.TOP
REMARK 3 TOPOLOGY FILE 4 : MN.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1YB6 COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PRAGUE ON 19-JAN-2005.
REMARK 100 THE RCSB ID CODE IS RCSB031332.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-JUN-2001
REMARK 200 TEMPERATURE (KELVIN) : 100.0
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 : BW7B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.8426
REMARK 200 MONOCHROMATOR : UNKNOWN
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MAR
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 46599
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.540
REMARK 200 RESOLUTION RANGE LOW (A) : 23.680
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.8
REMARK 200 DATA REDUNDANCY : 4.900
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.02300
REMARK 200 FOR THE DATA SET : 28.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.54
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.58
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.09800
REMARK 200 FOR SHELL : 7.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: 2YAS
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.80
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.78
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, PEG 400, PH 7.50,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K
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 64.17550
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 64.17550
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 23.68100
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 53.27650
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 23.68100
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 53.27650
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 64.17550
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 23.68100
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 53.27650
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 64.17550
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 23.68100
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 53.27650
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 1 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 106.55300
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
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 512 LIES ON A SPECIAL POSITION.
REMARK 375 HOH 769 LIES ON A SPECIAL POSITION.
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI
REMARK 500 NE2 GLN A 206 O HOH 593 0.56
REMARK 500 C8 MNN 300 O HOH 768 0.96
REMARK 500 N9 MNN 300 O HOH 768 0.97
REMARK 500 CD GLN A 206 O HOH 593 1.80
REMARK 500 C7 MNN 300 O HOH 768 2.19
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 6*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 LYS A 32 N - CA - C ANGL. DEV. = -8.5 DEGREES
REMARK 500 LYS A 32 N - CA - C ANGL. DEV. = -8.7 DEGREES
REMARK 500 ASP A 37 N - CA - C ANGL. DEV. =-10.5 DEGREES
REMARK 500 ASN A 156 N - CA - C ANGL. DEV. = 7.5 DEGREES
REMARK 500 LEU A 172 N - CA - C ANGL. DEV. = 10.1 DEGREES
REMARK 500 PHE A 210 N - CA - C ANGL. DEV. =-10.4 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
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 SER A 80 -106.68 52.41
REMARK 500 LYS A 129 -118.70 51.14
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1QJ4 RELATED DB: PDB
REMARK 900 RELATED ID: 1YAS RELATED DB: PDB
REMARK 900 RELATED ID: 2YAS RELATED DB: PDB
REMARK 900 RELATED ID: 3YAS RELATED DB: PDB
REMARK 900 RELATED ID: 4YAS RELATED DB: PDB
REMARK 900 RELATED ID: 5YAS RELATED DB: PDB
REMARK 900 RELATED ID: 6YAS RELATED DB: PDB
REMARK 900 RELATED ID: 7YAS RELATED DB: PDB
REMARK 900 RELATED ID: 1SC9 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN, COMPLEXED WITH ACETONECYANOHYDRIN
REMARK 900 RELATED ID: 1SCI RELATED DB: PDB
REMARK 900 THE SAME PROTEIN, K236L MUTANT
REMARK 900 RELATED ID: 1SCK RELATED DB: PDB
REMARK 900 THE SAME PROTEIN, K236L MUTANT COMPLEXED WITH ACETONE
REMARK 900 RELATED ID: 1SCQ RELATED DB: PDB
REMARK 900 THE SAME PROTEIN, K236L MUTANT COMPLEXED WITH
REMARK 900 ACETONECYANOHYDRIN
REMARK 900 RELATED ID: 1YB7 RELATED DB: PDB
DBREF 1YB6 A 2 257 SWS P52704 HNL_HEVBR 2 257
SEQRES 1 A 256 ALA PHE ALA HIS PHE VAL LEU ILE HIS THR ILE CYS HIS
SEQRES 2 A 256 GLY ALA TRP ILE TRP HIS LYS LEU LYS PRO LEU LEU GLU
SEQRES 3 A 256 ALA LEU GLY HIS LYS VAL THR ALA LEU ASP LEU ALA ALA
SEQRES 4 A 256 SER GLY VAL ASP PRO ARG GLN ILE GLU GLU ILE GLY SER
SEQRES 5 A 256 PHE ASP GLU TYR SER GLU PRO LEU LEU THR PHE LEU GLU
SEQRES 6 A 256 ALA LEU PRO PRO GLY GLU LYS VAL ILE LEU VAL GLY GLU
SEQRES 7 A 256 SER CYS GLY GLY LEU ASN ILE ALA ILE ALA ALA ASP LYS
SEQRES 8 A 256 TYR CYS GLU LYS ILE ALA ALA ALA VAL PHE HIS ASN SER
SEQRES 9 A 256 VAL LEU PRO ASP THR GLU HIS CYS PRO SER TYR VAL VAL
SEQRES 10 A 256 ASP LYS LEU MET GLU VAL PHE PRO ASP TRP LYS ASP THR
SEQRES 11 A 256 THR TYR PHE THR TYR THR LYS ASP GLY LYS GLU ILE THR
SEQRES 12 A 256 GLY LEU LYS LEU GLY PHE THR LEU LEU ARG GLU ASN LEU
SEQRES 13 A 256 TYR THR LEU CYS GLY PRO GLU GLU TYR GLU LEU ALA LYS
SEQRES 14 A 256 MET LEU THR ARG LYS GLY SER LEU PHE GLN ASN ILE LEU
SEQRES 15 A 256 ALA LYS ARG PRO PHE PHE THR LYS GLU GLY TYR GLY SER
SEQRES 16 A 256 ILE LYS LYS ILE TYR VAL TRP THR ASP GLN ASP GLU ILE
SEQRES 17 A 256 PHE LEU PRO GLU PHE GLN LEU TRP GLN ILE GLU ASN TYR
SEQRES 18 A 256 LYS PRO ASP LYS VAL TYR LYS VAL GLU GLY GLY ASP HIS
SEQRES 19 A 256 LYS LEU GLN LEU THR LYS THR LYS GLU ILE ALA GLU ILE
SEQRES 20 A 256 LEU GLN GLU VAL ALA ASP THR TYR ASN
HET SO4 400 5
HET SO4 401 5
HET MNN 300 10
HETNAM SO4 SULFATE ION
HETNAM MNN (S)-MANDELIC ACID NITRILE
HETSYN MNN (S)-HYDROXY(PHENYL)ACETONITRILE
FORMUL 2 SO4 2(O4 S1 2-)
FORMUL 4 MNN C8 H7 N1 O1
FORMUL 5 HOH *286(H2 O1)
HELIX 1 1 GLY A 15 HIS A 20 5 6
HELIX 2 2 LYS A 21 LEU A 29 1 9
HELIX 3 3 GLN A 47 ILE A 51 5 5
HELIX 4 4 SER A 53 SER A 58 1 6
HELIX 5 5 SER A 58 ALA A 67 1 10
HELIX 6 6 CYS A 81 CYS A 94 1 14
HELIX 7 7 SER A 115 PHE A 125 1 11
HELIX 8 8 GLY A 149 LEU A 157 1 9
HELIX 9 9 GLY A 162 THR A 173 1 12
HELIX 10 10 PHE A 179 LYS A 185 1 7
HELIX 11 11 GLY A 193 ILE A 197 5 5
HELIX 12 12 LEU A 211 TYR A 222 1 12
HELIX 13 13 LYS A 236 LYS A 241 1 6
HELIX 14 14 LYS A 241 TYR A 256 1 16
SHEET 1 A 6 LYS A 32 LEU A 36 0
SHEET 2 A 6 HIS A 5 ILE A 9 1 N LEU A 8 O THR A 34
SHEET 3 A 6 VAL A 74 GLU A 79 1 O VAL A 77 N ILE A 9
SHEET 4 A 6 ILE A 97 HIS A 103 1 O VAL A 101 N LEU A 76
SHEET 5 A 6 LYS A 199 TRP A 203 1 O ILE A 200 N PHE A 102
SHEET 6 A 6 LYS A 226 LYS A 229 1 O TYR A 228 N TYR A 201
SHEET 1 B 3 THR A 132 LYS A 138 0
SHEET 2 B 3 LYS A 141 LYS A 147 -1 O ILE A 143 N TYR A 136
SHEET 3 B 3 GLY A 176 SER A 177 -1 O GLY A 176 N LEU A 146
CRYST1 47.362 106.553 128.351 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 0.021114 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009385 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007791 0.00000
TER 2150 ASN A 257
MASTER 339 0 3 14 9 0 0 6 2455 1 20 20
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