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HEADER HYDROXYNITRILE LYASE 10-DEC-99 1DWO
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: ACETONE 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, ACETONE COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR H.LAUBLE,S.FORSTER,B.MIEHLICH,H.WAJANT,F.EFFENBERGER
REVDAT 1 07-DEC-00 1DWO 0
JRNL AUTH H.LAUBLE,S.FORSTER,B.MIEHLICH,H.WAJANT,
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) (%) : 97.0
REMARK 3 NUMBER OF REFLECTIONS : 52853
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) : 0.192
REMARK 3 FREE R VALUE : 0.252
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.0
REMARK 3 FREE R VALUE TEST SET COUNT : 5303
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 : 4178
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 4
REMARK 3 SOLVENT ATOMS : 273
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.0
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) : 0.25
REMARK 3 ESD FROM SIGMAA (A) : 0.23
REMARK 3 LOW RESOLUTION CUTOFF (A) : 8.0
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.25
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.23
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 2.1
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 21.2
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: NULL
REMARK 4
REMARK 4 1DWO COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
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 : 52853
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 (%) : 97.1
REMARK 200 DATA REDUNDANCY : 4.2
REMARK 200 R MERGE (I) : 0.054
REMARK 200 R SYM (I) : 0.068
REMARK 200 FOR THE DATA SET : 8.6
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 (%) : 99.4
REMARK 200 DATA REDUNDANCY IN SHELL : 4.1
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.2
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 94.25000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 52.75000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 52.75000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 47.12500
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 52.75000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 52.75000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 141.37500
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 52.75000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 52.75000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 47.12500
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 52.75000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 52.75000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 141.37500
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 94.25000
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 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 1562.8 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 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 188.50000
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: 1DWQ 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
REMARK 900 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 1DWO A -4 1 PDB 1DWO 1DWO -4 1
DBREF 1DWO A 2 258 SWS P52705 HNL_MANES 1 257
DBREF 1DWO B -4 1 PDB 1DWO 1DWO -4 1
DBREF 1DWO B 2 258 SWS P52705 HNL_MANES 1 257
SEQADV 1DWO PRO A -4 PDB 1DWO CLONING ARTIFACT
SEQADV 1DWO ILE A -3 PDB 1DWO CLONING ARTIFACT
SEQADV 1DWO SER A -2 PDB 1DWO CLONING ARTIFACT
SEQADV 1DWO LYS A -1 PDB 1DWO CLONING ARTIFACT
SEQADV 1DWO MET A 1 PDB 1DWO CLONING ARTIFACT
SEQADV 1DWO PRO B -4 PDB 1DWO CLONING ARTIFACT
SEQADV 1DWO ILE B -3 PDB 1DWO CLONING ARTIFACT
SEQADV 1DWO SER B -2 PDB 1DWO CLONING ARTIFACT
SEQADV 1DWO LYS B -1 PDB 1DWO CLONING ARTIFACT
SEQADV 1DWO MET B 1 PDB 1DWO 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 CYS 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 CYS 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
HET ACN S 259 4
HETNAM ACN ACETONE
FORMUL 2 ACN C3 H6 O1
FORMUL 4 HOH *273(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 CYS A 81 VAL A 94 1 14
HELIX 7 7 SER A 115 PHE A 125 1 11
HELIX 8 8 GLY A 150 LEU A 158 1 9
HELIX 9 9 THR A 163 MET A 174 1 12
HELIX 10 10 PHE A 180 GLN A 186 1 7
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 LEU B 158 1 9
HELIX 23 23 THR B 163 MET B 174 1 12
HELIX 24 24 PHE B 180 GLN B 186 1 7
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 200 THR A 205 1 N VAL A 201 O GLY A 100
SHEET 6 AA 6 LYS A 227 VAL A 231 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 TRP B 204 1 N VAL B 201 O GLY B 100
SHEET 6 BA 6 LYS B 227 GLN B 230 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
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 105.500 105.500 188.500 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 0.009479 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009479 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005305 0.00000 |