| content |
HEADER LYASE 12-FEB-04 1SCQ
TITLE K236L MUTANT OF HYDROXYNITRILE LYASE FROM HEVEA
TITLE 2 BRASILIENSIS IN COMPLEX WITH ACETONECYANOHYDRIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: (S)-ACETONE-CYANOHYDRIN LYASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: HYDROXYNITRILE LYASE;
COMPND 5 EC: 4.1.2.39;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: 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,B.KRAMMER,H.SCHWAB,C.KRATKY
REVDAT 1 29-JUN-04 1SCQ 0
JRNL AUTH K.GRUBER,G.GARTLER,B.KRAMMER,H.SCHWAB,C.KRATKY
JRNL TITL REACTION MECHANISM OF HYDROXYNITRILE LYASES OF THE
JRNL TITL 2 ALPHA/BETA-HYDROLASE SUPERFAMILY: THE
JRNL TITL 3 THREE-DIMENSIONAL STRUCTURE OF THE TRANSIENT
JRNL TITL 4 ENZYME-SUBSTRATE COMPLEX CERTIFIES THE CRUCIAL
JRNL TITL 5 ROLE OF LYS236
JRNL REF J.BIOL.CHEM. V. 279 20501 2004
JRNL REFN ASTM JBCHA3 US ISSN 0021-9258
REMARK 1
REMARK 1 REFERENCE 1
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 2
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 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 V. 4 811 1996
REMARK 1 REFN ASTM STRUE6 UK ISSN 0969-2126
REMARK 2
REMARK 2 RESOLUTION. 2.90 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) : 2.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 9.98
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1297682.850
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 87.4
REMARK 3 NUMBER OF REFLECTIONS : 6445
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) : 0.215
REMARK 3 FREE R VALUE : 0.291
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.700
REMARK 3 FREE R VALUE TEST SET COUNT : 301
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.017
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) : 2.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.00
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 89.40
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 637
REMARK 3 BIN R VALUE (WORKING SET) : 0.2960
REMARK 3 BIN FREE R VALUE : 0.3880
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.60
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 31
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.070
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2056
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 26
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 25.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.00
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -3.26000
REMARK 3 B22 (A**2) : 2.93000
REMARK 3 B33 (A**2) : 0.32000
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) : 0.33
REMARK 3 ESD FROM SIGMAA (A) : 0.38
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) : 0.50
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.59
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.20
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.70
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.79
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) : 1.120 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.860 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.730 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.610 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.46
REMARK 3 BSOL : 32.91
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 : ACN.PARAM
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 : ACN.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT AGAINST MAXIMUM
REMARK 3 LIKELIHOOD TARGET FUNCTION
REMARK 4
REMARK 4 1SCQ COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 16-FEB-2004.
REMARK 100 THE RCSB ID CODE IS RCSB021599.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-MAR-2001
REMARK 200 TEMPERATURE (KELVIN) : 298.0
REMARK 200 PH : 7.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : SIEMENS
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRAPHITE
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 : 8029
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 10.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 87.7
REMARK 200 DATA REDUNDANCY : 2.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.18300
REMARK 200 FOR THE DATA SET : 7.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.79
REMARK 200 COMPLETENESS FOR SHELL (%) : 89.8
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.66800
REMARK 200 FOR SHELL : 1.900
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 (%): 55.77
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.80
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, PEG 400, HEPES,
REMARK 280 PH 7.5, VAPOR DIFFUSION, HANGING 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 64.20550
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 64.20550
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 23.77100
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 53.52750
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 23.77100
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 53.52750
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 64.20550
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 23.77100
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 53.52750
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 64.20550
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 23.77100
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 53.52750
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 107.05500
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
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 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. = -9.3 DEGREES
REMARK 500 LYS A 147 N - CA - C ANGL. DEV. = -8.5 DEGREES
REMARK 500 ASN A 156 N - CA - C ANGL. DEV. = 7.7 DEGREES
REMARK 500 LEU A 172 N - CA - C ANGL. DEV. = 7.5 DEGREES
REMARK 500 PHE A 189 N - CA - C ANGL. DEV. = -7.5 DEGREES
REMARK 500 PHE A 210 N - CA - C ANGL. DEV. = -8.3 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 -102.56 55.52
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 THE NATURAL SUBSTRATE
REMARK 900 ACETONE CYANOHYDRIN
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
DBREF 1SCQ A 1 257 SWS P52704 HNL_HEVBR 1 257
SEQADV 1SCQ LEU A 236 SWS P52704 LYS 236 ENGINEERED
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 LEU 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 CNH 300 6
HETNAM SO4 SULFATE ION
HETNAM CNH 2-HYDROXY-2-METHYLPROPANENITRILE
HETSYN CNH ACETONE CYANOHYDRIN
FORMUL 2 SO4 4(O4 S1 2-)
FORMUL 6 CNH C4 H7 N1 O1
HELIX 1 1 GLY A 15 HIS A 20 5 6
HELIX 2 2 LYS A 21 ALA A 28 1 8
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 ARG A 186 1 8
HELIX 11 11 LEU A 211 TYR A 222 1 12
HELIX 12 12 LEU A 236 LYS A 241 1 6
HELIX 13 13 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 PHE A 6 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 VAL A 202 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 47.542 107.055 128.411 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 0.021034 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009341 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007787 0.00000
TER 2057 ASN A 257
MASTER 314 0 5 13 9 0 0 6 2082 1 26 20
END |