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HEADER HYDROXYNITRILE LYASE 10-DEC-99 1DWQ
TITLE CRYSTAL STRUCTURE OF HYDROXYNITRILE LYASE FROM MANIHOT
TITLE 2 ESCULENTA IN COMPLEX WITH SUBSTRATES ACETONE AND
TITLE 3 CHLOROACETONE:IMPLICATIONS FOR THE MECHANISM OF
TITLE 4 CYANOGENESIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HYDROXYNITRILE LYASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES;
COMPND 5 SYNONYM: (S)-ACETONE-CYANOHYDRIN LYASE, (S)-HYDROXYNITRILASE;
COMPND 6 EC: 4.2.1.37;
COMPND 7 OTHER_DETAILS: CHLOROACETONE COMPLEX
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MANIHOT ESCULENTA;
SOURCE 3 ORGANISM_COMMON: CASSAVA;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 OTHER_DETAILS: RECOMBINANT PROTEIN
KEYWDS HYDROXYNITRILE LYASE, CHLOROACETONE COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR H.LAUBLE,S.FORSTER,B.MIELICH,H.WAJANT,F.EFFENBERGER
REVDAT 1 07-DEC-00 1DWQ 0
JRNL AUTH H.LAUBL,B.MIEHLICH,H.WAJANT,S.FORSTER,
JRNL AUTH 2 F.EFFENBERGER
JRNL TITL THE CRYSTAL STRUCTURE OF HYDROXYNITRILE LYASE FROM
JRNL TITL 2 MANIHOT ESCULENTA IN COMPLEX WITH SUBSTRATES
JRNL TITL 3 ACETONE AND CHLOROACETONE: IMPLICATIONS FOR THE
JRNL TITL 4 MECHANISM OF CYANOGENESIS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.2 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.8
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.2
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.0
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.0
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 10000000.00
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.001
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 97.4
REMARK 3 NUMBER OF REFLECTIONS : 51519
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NONE
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.207
REMARK 3 FREE R VALUE : 0.244
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.0
REMARK 3 FREE R VALUE TEST SET COUNT : 5419
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 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 : 4166
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 25
REMARK 3 SOLVENT ATOMS : 211
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 33.0
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 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.019
REMARK 3 BOND ANGLES (DEGREES) : 2.9
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.6
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : 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 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 : NULL
REMARK 3 TOPOLOGY FILE 1 : TOPH19X.PRO
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: CHLOROACETONE COMPLEX
REMARK 4
REMARK 4 1DWQ COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY EBI ON 12-DEC-1999.
REMARK 100 THE EBI ID CODE IS EBI-4457.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG BEAMLINE X11
REMARK 200 BEAMLINE : X11
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.905
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 : 54130
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.2
REMARK 200 RESOLUTION RANGE LOW (A) : 20.0
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NONE
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.7
REMARK 200 DATA REDUNDANCY : 3.8
REMARK 200 R MERGE (I) : 0.055
REMARK 200 R SYM (I) : 0.074
REMARK 200 FOR THE DATA SET : 7.5
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.2
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.3
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.2
REMARK 200 DATA REDUNDANCY IN SHELL : 3.8
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.1
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 71
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.3
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M NACITRAT, PH 5.4,
REMARK 280 6% PEG8000, 28% MPD
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
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 1/2-Y,1/2+X,1/4+Z
REMARK 290 4555 1/2+Y,1/2-X,3/4+Z
REMARK 290 5555 1/2-X,1/2+Y,1/4-Z
REMARK 290 6555 1/2+X,1/2-Y,3/4-Z
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 94.65000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 52.25000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 52.25000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 47.32500
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 52.25000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 52.25000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 141.97500
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 52.25000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 52.25000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 47.32500
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 52.25000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 52.25000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 141.97500
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 94.65000
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 2 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 300
REMARK 300 BIOLOGICAL_UNIT: TETRAMER
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, B
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 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 189.30000
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 PRO B -4
REMARK 465 ILE B -3
REMARK 465 SER B -2
REMARK 465 LYS B -1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: ASA
REMARK 800 SITE_DESCRIPTION: CATALYTIC TRIAD ACTIVE SITE
REMARK 800
REMARK 800 SITE_IDENTIFIER: ASB
REMARK 800 SITE_DESCRIPTION: CATALYTIC TRIAD ACTIVE SITE
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1DWP RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HYDROXYNITRILE LYASE FROM MANIHOT
REMARK 900 ESCULENTA AT 2.2 ANGSTROM RESOLUTION
REMARK 900 RELATED ID: 1DWO RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HYDROXYNITRILE LYASE FROM MANIHOT
REMARK 900 ESCULENTA IN COMPLEX WITH SUBSTRATES ACETONE AND
REMARK 900 CHLOROACETONE:IMPLICATIONS FOR THE MECHANISM OF CYANOGENESIS
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE SWISSPROT ENTRY P52705 REPORTS THIS ENZYME TO BE EC 4.2.1.39,
REMARK 999 AND TO HAVE A HOMOTRIMERIC SUBUNIT STRUCTURE. THE CORRECT
REMARK 999 EC NUMBER IS 4.2.1.37 AND THE MOLECULE IS A TETRAMER.
REMARK 999
DBREF 1DWQ A -4 1 PDB 1DWQ 1DWQ -4 1
DBREF 1DWQ A 2 258 SWS P52705 HNL_MANES 1 257
DBREF 1DWQ B -4 1 PDB 1DWQ 1DWQ -4 1
DBREF 1DWQ B 2 258 SWS P52705 HNL_MANES 1 257
SEQADV 1DWQ PRO A -4 PDB 1DWQ CLONING ARTIFACT
SEQADV 1DWQ ILE A -3 PDB 1DWQ CLONING ARTIFACT
SEQADV 1DWQ SER A -2 PDB 1DWQ CLONING ARTIFACT
SEQADV 1DWQ LYS A -1 PDB 1DWQ CLONING ARTIFACT
SEQADV 1DWQ MET A 1 PDB 1DWQ CLONING ARTIFACT
SEQADV 1DWQ PRO B -4 PDB 1DWQ CLONING ARTIFACT
SEQADV 1DWQ ILE B -3 PDB 1DWQ CLONING ARTIFACT
SEQADV 1DWQ SER B -2 PDB 1DWQ CLONING ARTIFACT
SEQADV 1DWQ LYS B -1 PDB 1DWQ CLONING ARTIFACT
SEQADV 1DWQ MET B 1 PDB 1DWQ CLONING ARTIFACT
SEQRES 1 A 262 PRO ILE SER LYS MET VAL THR ALA HIS PHE VAL LEU ILE
SEQRES 2 A 262 HIS THR ILE CYS HIS GLY ALA TRP ILE TRP HIS LYS LEU
SEQRES 3 A 262 LYS PRO ALA LEU GLU ARG ALA GLY HIS LYS VAL THR ALA
SEQRES 4 A 262 LEU ASP MET ALA ALA SER GLY ILE ASP PRO ARG GLN ILE
SEQRES 5 A 262 GLU GLN ILE ASN SER PHE ASP GLU TYR SER GLU PRO LEU
SEQRES 6 A 262 LEU THR PHE LEU GLU LYS LEU PRO GLN GLY GLU LYS VAL
SEQRES 7 A 262 ILE ILE VAL GLY GLU SER CSA ALA GLY LEU ASN ILE ALA
SEQRES 8 A 262 ILE ALA ALA ASP ARG TYR VAL ASP LYS ILE ALA ALA GLY
SEQRES 9 A 262 VAL PHE HIS ASN SER LEU LEU PRO ASP THR VAL HIS SER
SEQRES 10 A 262 PRO SER TYR THR VAL GLU LYS LEU LEU GLU SER PHE PRO
SEQRES 11 A 262 ASP TRP ARG ASP THR GLU TYR PHE THR PHE THR ASN ILE
SEQRES 12 A 262 THR GLY GLU THR ILE THR THR MET LYS LEU GLY PHE VAL
SEQRES 13 A 262 LEU LEU ARG GLU ASN LEU PHE THR LYS CYS THR ASP GLY
SEQRES 14 A 262 GLU TYR GLU LEU ALA LYS MET VAL MET ARG LYS GLY SER
SEQRES 15 A 262 LEU PHE GLN ASN VAL LEU ALA GLN ARG PRO LYS PHE THR
SEQRES 16 A 262 GLU LYS GLY TYR GLY SER ILE LYS LYS VAL TYR ILE TRP
SEQRES 17 A 262 THR ASP GLN ASP LYS ILE PHE LEU PRO ASP PHE GLN ARG
SEQRES 18 A 262 TRP GLN ILE ALA ASN TYR LYS PRO ASP LYS VAL TYR GLN
SEQRES 19 A 262 VAL GLN GLY GLY ASP HIS LYS LEU GLN LEU THR LYS THR
SEQRES 20 A 262 GLU GLU VAL ALA HIS ILE LEU GLN GLU VAL ALA ASP ALA
SEQRES 21 A 262 TYR ALA
SEQRES 1 B 262 PRO ILE SER LYS MET VAL THR ALA HIS PHE VAL LEU ILE
SEQRES 2 B 262 HIS THR ILE CYS HIS GLY ALA TRP ILE TRP HIS LYS LEU
SEQRES 3 B 262 LYS PRO ALA LEU GLU ARG ALA GLY HIS LYS VAL THR ALA
SEQRES 4 B 262 LEU ASP MET ALA ALA SER GLY ILE ASP PRO ARG GLN ILE
SEQRES 5 B 262 GLU GLN ILE ASN SER PHE ASP GLU TYR SER GLU PRO LEU
SEQRES 6 B 262 LEU THR PHE LEU GLU LYS LEU PRO GLN GLY GLU LYS VAL
SEQRES 7 B 262 ILE ILE VAL GLY GLU SER CSA ALA GLY LEU ASN ILE ALA
SEQRES 8 B 262 ILE ALA ALA ASP ARG TYR VAL ASP LYS ILE ALA ALA GLY
SEQRES 9 B 262 VAL PHE HIS ASN SER LEU LEU PRO ASP THR VAL HIS SER
SEQRES 10 B 262 PRO SER TYR THR VAL GLU LYS LEU LEU GLU SER PHE PRO
SEQRES 11 B 262 ASP TRP ARG ASP THR GLU TYR PHE THR PHE THR ASN ILE
SEQRES 12 B 262 THR GLY GLU THR ILE THR THR MET LYS LEU GLY PHE VAL
SEQRES 13 B 262 LEU LEU ARG GLU ASN LEU PHE THR LYS CYS THR ASP GLY
SEQRES 14 B 262 GLU TYR GLU LEU ALA LYS MET VAL MET ARG LYS GLY SER
SEQRES 15 B 262 LEU PHE GLN ASN VAL LEU ALA GLN ARG PRO LYS PHE THR
SEQRES 16 B 262 GLU LYS GLY TYR GLY SER ILE LYS LYS VAL TYR ILE TRP
SEQRES 17 B 262 THR ASP GLN ASP LYS ILE PHE LEU PRO ASP PHE GLN ARG
SEQRES 18 B 262 TRP GLN ILE ALA ASN TYR LYS PRO ASP LYS VAL TYR GLN
SEQRES 19 B 262 VAL GLN GLY GLY ASP HIS LYS LEU GLN LEU THR LYS THR
SEQRES 20 B 262 GLU GLU VAL ALA HIS ILE LEU GLN GLU VAL ALA ASP ALA
SEQRES 21 B 262 TYR ALA
MODRES 1DWQ CSA A 81 CYS S-ACETONYLCYSTEIN
MODRES 1DWQ CSA B 81 CYS S-ACETONYLCYSTEIN
HET CSA A 81 10
HET CSA B 81 10
HET ATO 259 5
HETNAM CSA S-ACETONYLCYSTEINE
HETNAM ATO CHLOROACETONE
HETSYN CSA S-(2-OXOPROPYL)-L-CYSTEINE
FORMUL 1 CSA 2(C6 H11 N1 O3 S1)
FORMUL 2 ATO C3 H5 O1 CL1
FORMUL 3 HOH *211(H2 O1)
HELIX 1 1 GLY A 15 HIS A 20 5 6
HELIX 2 2 LYS A 21 ALA 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 LEU A 68 1 11
HELIX 6 6 ALA A 82 VAL A 94 1 13
HELIX 7 7 SER A 115 PHE A 125 1 11
HELIX 8 8 GLY A 150 ASN A 157 1 8
HELIX 9 9 THR A 163 MET A 174 1 12
HELIX 10 10 PHE A 180 ARG A 187 1 8
HELIX 11 11 GLY A 194 ILE A 198 5 5
HELIX 12 12 LEU A 212 TYR A 223 1 12
HELIX 13 13 LYS A 237 LYS A 242 1 6
HELIX 14 14 LYS A 242 ALA A 258 1 17
HELIX 15 15 GLY B 15 HIS B 20 5 6
HELIX 16 16 LYS B 21 ALA B 29 1 9
HELIX 17 17 GLN B 47 ILE B 51 5 5
HELIX 18 18 SER B 53 SER B 58 1 6
HELIX 19 19 SER B 58 LEU B 68 1 11
HELIX 20 20 ALA B 82 VAL B 94 1 13
HELIX 21 21 SER B 115 PHE B 125 1 11
HELIX 22 22 GLY B 150 ASN B 157 1 8
HELIX 23 23 THR B 163 MET B 174 1 12
HELIX 24 24 PHE B 180 ARG B 187 1 8
HELIX 25 25 GLY B 194 ILE B 198 5 5
HELIX 26 26 LEU B 212 TYR B 223 1 12
HELIX 27 27 LYS B 237 LYS B 242 1 6
HELIX 28 28 LYS B 242 ALA B 258 1 17
SHEET 1 AA 6 LYS A 32 LEU A 36 0
SHEET 2 AA 6 HIS A 5 ILE A 9 1 N PHE A 6 O LYS A 32
SHEET 3 AA 6 VAL A 74 GLU A 79 1 N ILE A 75 O VAL A 7
SHEET 4 AA 6 ILE A 97 HIS A 103 1 N ALA A 98 O VAL A 74
SHEET 5 AA 6 LYS A 199 TRP A 204 1 N LYS A 199 O GLY A 100
SHEET 6 AA 6 LYS A 227 GLN A 230 1 N LYS A 227 O TYR A 202
SHEET 1 AB 2 GLU A 132 THR A 137 0
SHEET 2 AB 2 THR A 143 LYS A 148 -1 N LYS A 148 O GLU A 132
SHEET 1 BA 6 LYS B 32 LEU B 36 0
SHEET 2 BA 6 HIS B 5 ILE B 9 1 N PHE B 6 O LYS B 32
SHEET 3 BA 6 VAL B 74 GLU B 79 1 N ILE B 75 O VAL B 7
SHEET 4 BA 6 ILE B 97 HIS B 103 1 N ALA B 98 O VAL B 74
SHEET 5 BA 6 LYS B 200 THR B 205 1 N VAL B 201 O GLY B 100
SHEET 6 BA 6 LYS B 227 VAL B 231 1 N LYS B 227 O TYR B 202
SHEET 1 BB 2 GLU B 132 THR B 137 0
SHEET 2 BB 2 THR B 143 LYS B 148 -1 N LYS B 148 O GLU B 132
LINK C SER A 80 N CSA A 81 1555 1555
LINK C CSA A 81 N ALA A 82 1555 1555
LINK C SER B 80 N CSA B 81 1555 1555
LINK C CSA B 81 N ALA B 82 1555 1555
SITE 1 ASA 3 SER A 80 ASP A 208 HIS A 236
SITE 1 ASB 3 SER B 80 ASP B 208 HIS B 236
CRYST1 104.500 104.500 189.300 90.00 90.00 90.00 P 41 21 2 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 0.009569 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009569 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005283 0.00000
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