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HEADER LYASE 21-JUN-99 1QJ4
TITLE HYDROXYNITRILE-LYASE FROM HEVEA BRASILIENSIS AT ATOMIC
TITLE 2 RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HYDROXYNITRILE LYASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: OXYNITRILE LYASE;
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 PLASMID: BHIL-D2;
SOURCE 6 GENE: HNL;
SOURCE 7 EXPRESSION_SYSTEM: PICHIA PASTORIS;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: BHIL-D2;
SOURCE 9 EXPRESSION_SYSTEM_GENE: HNL
KEYWDS OXYNITRILASE, CYANOGENESIS, CYANHYDRIN FORMATION, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.GUGGANIG,K.GRUBER,C.KRATKY
REVDAT 1 10-OCT-99 1QJ4 0
JRNL AUTH K.GRUBER,M.GUGGANIG,U.G.WAGNER,C.KRATKY
JRNL TITL ATOMIC RESOLUTION CRYSTAL STRUCTURE OF
JRNL TITL 2 HYDROXYNITRILE LYASE FROM HEVEA BRASILIENSIS
JRNL REF BIOL.CHEM. V. 380 993 1999
JRNL REFN ASTM BICHF3 GE ISSN 1431-6730 2169
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH J.ZUEGG,K.GRUBER,M.GUGGANIG,U.G.WAGNER,C.KRATKY
REMARK 1 TITL 3D STRUCTURES OF ENZYME-SUBSTRATE COMPLEXES OF THE
REMARK 1 TITL 2 HYDROXYNITRILE LYASE FROM HEVEA BRASILIENSIS
REMARK 1 REF TO BE PUBLISHED
REMARK 1 REFN 0353
REMARK 1 REFERENCE 2
REMARK 1 AUTH U.G.WAGNER,M.HASSLACHER,H.GRIENGL,H.SCHWAB,
REMARK 1 AUTH 2 C.KRATKY
REMARK 1 TITL MECHANISM OF CYANOGENESIS: THE CRYSTAL STRUCTURE OF
REMARK 1 TITL 2 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 1 REFERENCE 3
REMARK 1 AUTH U.G.WAGNER,M.SCHALL,M.HAYN,M.HASSLACHER,H.SCHWAB,
REMARK 1 AUTH 2 H.S.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 4
REMARK 1 AUTH M.HASSLACHER,M.SCHALL,M.HAYN,H.GRIENGL,
REMARK 1 AUTH 2 S.D.KOHLWEIN,H.SCHWAB
REMARK 1 TITL MOLECULAR CLONING OF THE FULL-LENGTH CDNA OF
REMARK 1 TITL 2 (S)-HYDROXYNITRILE LYASE FROM HEVEA BRASILIENSIS.
REMARK 1 TITL 3 FUNCTIONAL EXPRESSION IN ESCHERICHIA COLI AND
REMARK 1 TITL 4 SACCHAROMYCES CEREVISIAE AND IDENTIFICATION OF AN
REMARK 1 TITL 5 ACTIVE SITE RESIDUE
REMARK 1 REF J.BIOL.CHEM. V. 271 5884 1996
REMARK 1 REFN ASTM JBCHA3 US ISSN 0021-9258 0071
REMARK 2
REMARK 2 RESOLUTION. 1.1 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : SHELXL-97
REMARK 3 AUTHORS : G.M.SHELDRICK
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.0
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.1
REMARK 3 CROSS-VALIDATION METHOD : FREE R
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (NO CUTOFF).
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : 0.1158
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.1149
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.1437
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.0
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 6192
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 123339
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : 0.1083
REMARK 3 R VALUE (WORKING SET, F>4SIG(F)) : 0.1075
REMARK 3 FREE R VALUE (F>4SIG(F)) : 0.1353
REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 5.0
REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : 5248
REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : 104710
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2155
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 32
REMARK 3 SOLVENT ATOMS : 550
REMARK 3
REMARK 3 MODEL REFINEMENT.
REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : 2629.75
REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : 2053.00
REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : 25
REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : 24572
REMARK 3 NUMBER OF RESTRAINTS : 43482
REMARK 3
REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK 3 BOND LENGTHS (A) : 0.014
REMARK 3 ANGLE DISTANCES (A) : 0.030
REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000
REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : 0.0281
REMARK 3 ZERO CHIRAL VOLUMES (A**3) : 0.086
REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : 0.095
REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : 0.109
REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : 0.005
REMARK 3 SIMILAR ADP COMPONENTS (A**2) : 0.029
REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : 0.059
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED: MOEWS & KRETSINGER, J.MOL.BIOL.91(1973)201-2
REMARK 3
REMARK 3 STEREOCHEMISTRY TARGET VALUES : ENGH AND HUBER
REMARK 3 SPECIAL CASE: NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: ANISOTROPIC REFINEMENT REDUCED
REMARK 3 FREE R (NO CUTOFF) BY 0.043.
REMARK 3 RESIDUE SER-A80 IS OBSERVED IN A RAMACHANDRAN 'FORBIDDEN'
REMARK 3 REGION. THIS CONFORMATION IS FOUND IN ALL PREVIOUS
REMARK 3 HNL-STRUCTURES. STRUCTURES OF OTHER MEMBERS OF THE
REMARK 3 ALPHA/BETA HYDROLASES FAMILY ALSO CONSISTENTLY SHOW
REMARK 3 THE EQUIVALENT RESIDUE (NUCLEOPHILE) IN SUCH A
REMARK 3 CONFORMATION.
REMARK 4
REMARK 4 1QJ4 COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY EBI ON 21-JUN-1999.
REMARK 100 THE EBI ID CODE IS EBI-2844.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-AUG-98
REMARK 200 TEMPERATURE (KELVIN) : 120
REMARK 200 PH : 7.4
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 : NONE
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.8345
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : MAR-345
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 : 123339
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.1
REMARK 200 RESOLUTION RANGE LOW (A) : 50.0
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.1
REMARK 200 DATA REDUNDANCY : 4.1
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.065
REMARK 200 FOR THE DATA SET : 20.4
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.11
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.3
REMARK 200 DATA REDUNDANCY IN SHELL : 3.8
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.364
REMARK 200 FOR SHELL : 3.0
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER
REMARK 200 SOFTWARE USED: SHELXL-97
REMARK 200 STARTING MODEL: 7YAS
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.8
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M NATRIUM HEPES BUFFER PH=7.4
REMARK 280 2 % PEG 400, 2.0 M AMMONIUM SULFATE, ROOM-TEMP.
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 64.08000
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 64.08000
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 23.64350
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 53.32750
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 23.64350
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 53.32750
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 64.08000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 23.64350
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 53.32750
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 64.08000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 23.64350
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 53.32750
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE
REMARK 300 A XRAY OBSERVED BIO-ASSEMBLY CAN BE BUILT
REMARK 300 BY SPACE GROUP SYMMETRY EXPANSION OF THE
REMARK 300 CONTENTS OF THE ASYMMETRIC UNIT
REMARK 300
REMARK 300 FOR THE HOMO-ASSEMBLY DESCRIBED BY REMARK 350
REMARK 300 THE DIFFERENCE IN ACCESSIBLE SURFACE AREA PER
REMARK 300 CHAIN BETWEEN THE ISOLATED CHAIN AND THAT FOR
REMARK 300 THE CHAIN IN THE COMPLEX IS 814.3 ANGSTROM**2
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 AN OLIGOMER OF TYPE :DIMERIC : CAN BE ASSEMBLED BY
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 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 106.65500
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 509 LIES ON A SPECIAL POSITION.
REMARK 375 HOH 596 LIES ON A SPECIAL POSITION.
REMARK 375 HOH 700 LIES ON A SPECIAL POSITION.
REMARK 375 HOH 737 LIES ON A SPECIAL POSITION.
REMARK 375 HOH 873 LIES ON A SPECIAL POSITION.
REMARK 375 HOH 990 LIES ON A SPECIAL POSITION.
REMARK 375
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: 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 DISTANCE
REMARK 500
REMARK 500 O HOH 535 O HOH 758 2.13
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 55.02 -113.35
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: DSSP
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: DSSP
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: CAT
REMARK 800 SITE_DESCRIPTION: CATALYTIC TRIAD
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1YAS RELATED DB: PDB
REMARK 900
DBREF 1QJ4 A 1 257 SWS P52704 HNL_HEVBR 1 257
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 GOL 300 6
HET SO4 400 5
HET SO4 401 5
HET SO4 402 5
HET SO4 403 5
HETNAM GOL GLYCEROL
HETNAM SO4 SULFATE ION
HETSYN GOL 1,2,3-PROPANETRIOL
FORMUL 2 GOL C3 H8 O3
FORMUL 3 SO4 4(O4 S1 2-)
FORMUL 4 HOH *550(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 ARG A 186 1 8
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 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 47.287 106.655 128.160 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 0.021147 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009376 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007803 0.00000
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