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HEADER HYDROLASE 10-JUN-02 1LZL
TITLE BACTERIAL HEROIN ESTERASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HEROIN ESTERASE;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RHODOCOCCUS SP.;
SOURCE 3 ORGANISM_COMMON: BACTERIA;
SOURCE 4 STRAIN: H1;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: BACTERIA;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21-GOLD(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET28A(+)
KEYWDS ALPHA/BETA HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR X.ZHU,N.A.LARSEN,A.BASRAN,N.C.BRUCE,I.A.WILSON
REVDAT 1 28-JAN-03 1LZL 0
JRNL AUTH X.ZHU,N.A.LARSEN,A.BASRAN,N.C.BRUCE,I.A.WILSON
JRNL TITL OBSERVATION OF AN ARSENIC ADDUCT IN AN ACETYL
JRNL TITL 2 ESTERASE CRYSTAL STRUCTURE
JRNL REF J.BIOL.CHEM. V. 278 2008 2003
JRNL REFN ASTM JBCHA3 US ISSN 0021-9258
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.30 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) : 1.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 26.70
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
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) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.153
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.213
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 3700
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 68788
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : NULL
REMARK 3 R VALUE (WORKING SET, F>4SIG(F)) : 0.143
REMARK 3 FREE R VALUE (F>4SIG(F)) : 0.200
REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : 3037
REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : 56844
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2386
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 313
REMARK 3
REMARK 3 MODEL REFINEMENT.
REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : NULL
REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : NULL
REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : 6
REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : NULL
REMARK 3 NUMBER OF RESTRAINTS : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK 3 BOND LENGTHS (A) : 0.011
REMARK 3 ANGLE DISTANCES (A) : 0.029
REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000
REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : 0.027
REMARK 3 ZERO CHIRAL VOLUMES (A**3) : 0.063
REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : 0.069
REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : 0.019
REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : 0.006
REMARK 3 SIMILAR ADP COMPONENTS (A**2) : 0.049
REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : 0.072
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED: AS DESCRIBED IN J.MOL.BIOL. 91(1973) 201-228
REMARK 3
REMARK 3 STEREOCHEMISTRY TARGET VALUES : ENGH & HUBER
REMARK 3 SPECIAL CASE: NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1LZL COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-JUN-2002.
REMARK 100 THE RCSB ID CODE IS RCSB016418.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-MAR-2002
REMARK 200 TEMPERATURE (KELVIN) : 95.5
REMARK 200 PH : 6.40
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : 9-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.94641
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 76984
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.300
REMARK 200 RESOLUTION RANGE LOW (A) : 26.700
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 4.000
REMARK 200 R MERGE (I) : 0.04200
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 35.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.32
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.5
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.58500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1LZK
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, SODIUM CHLORIDE,
REMARK 280 BES, PH 6.4, EVAPORATION, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,2/3+Z
REMARK 290 3555 -X+Y,-X,1/3+Z
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,1/3-Z
REMARK 290 6555 -X,-X+Y,2/3-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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 70.45000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 35.22500
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 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 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 35.22500
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 70.45000
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 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 465 LEU A 319
REMARK 465 SER A 320
REMARK 465 PRO A 321
REMARK 465 VAL A 322
REMARK 465 SER A 323
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 ARG A 272 CD - NE - CZ ANGL. DEV. = 27.3 DEGREES
REMARK 500 ARG A 314 CD - NE - CZ ANGL. DEV. = 27.2 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 LEU A 208 -52.89 65.33
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1LZK RELATED DB: PDB
REMARK 900 THE SAME PROTEIN
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 AUTHORS STATE THAT GENBANK REFERENCE SEQUENCE
REMARK 999 IS INCORRECT FOR RESIDUES 159, 299, 301, 307-313
REMARK 999 AND 315-322. AUTHORS MAINTAIN THAT THEIR SEQUENCE
REMARK 999 IS CORRECT AND HAS AN ADDITIONAL RESIDUE 323. THIS
REMARK 999 SEQUENCE HAS NOT YET BEEN DEPOSITED IN ANY SEQUENCE
REMARK 999 REFERENCE DATABASE.
DBREF 1LZL A 1 323 GB 2088525 AAC45283 1 322
SEQADV 1LZL GLN A 159 GB 2088525 GLU 159 SEE REMARK 999
SEQADV 1LZL ALA A 299 GB 2088525 GLY 299 SEE REMARK 999
SEQADV 1LZL SER A 301 GB 2088525 ARG 301 SEE REMARK 999
SEQADV 1LZL GLU A 307 GB 2088525 LYS 307 SEE REMARK 999
SEQADV 1LZL ALA A 308 GB 2088525 PRO 308 SEE REMARK 999
SEQADV 1LZL LEU A 309 GB 2088525 HIS 309 SEE REMARK 999
SEQADV 1LZL THR A 310 GB 2088525 CYS 310 SEE REMARK 999
SEQADV 1LZL ALA A 311 GB 2088525 ASP 311 SEE REMARK 999
SEQADV 1LZL ILE A 312 GB 2088525 PRO 312 SEE REMARK 999
SEQADV 1LZL ARG A 313 GB 2088525 GLU 313 SEE REMARK 999
SEQADV 1LZL GLY A 315 GB 2088525 VAL 315 SEE REMARK 999
SEQADV 1LZL LEU A 316 GB 2088525 ALA 316 SEE REMARK 999
SEQADV 1LZL ARG A 317 GB 2088525 PHE 317 SEE REMARK 999
SEQADV 1LZL SER A 318 GB 2088525 ALA 318 SEE REMARK 999
SEQADV 1LZL LEU A 319 GB 2088525 VAL 319 SEE REMARK 999
SEQADV 1LZL SER A 320 GB 2088525 ALA 320 SEE REMARK 999
SEQADV 1LZL PRO A 321 GB 2088525 VAL 321 SEE REMARK 999
SEQADV 1LZL VAL A 322 GB 2088525 SER 322 SEE REMARK 999
SEQADV 1LZL SER A 323 GB 2088525 323 SEE REMARK 999
SEQRES 1 A 323 MET THR THR PHE PRO THR LEU ASP PRO GLU LEU ALA ALA
SEQRES 2 A 323 ALA LEU THR MET LEU PRO LYS VAL ASP PHE ALA ASP LEU
SEQRES 3 A 323 PRO ASN ALA ARG ALA THR TYR ASP ALA LEU ILE GLY ALA
SEQRES 4 A 323 MET LEU ALA ASP LEU SER PHE ASP GLY VAL SER LEU ARG
SEQRES 5 A 323 GLU LEU SER ALA PRO GLY LEU ASP GLY ASP PRO GLU VAL
SEQRES 6 A 323 LYS ILE ARG PHE VAL THR PRO ASP ASN THR ALA GLY PRO
SEQRES 7 A 323 VAL PRO VAL LEU LEU TRP ILE HIS GLY GLY GLY PHE ALA
SEQRES 8 A 323 ILE GLY THR ALA GLU SER SER ASP PRO PHE CYS VAL GLU
SEQRES 9 A 323 VAL ALA ARG GLU LEU GLY PHE ALA VAL ALA ASN VAL GLU
SEQRES 10 A 323 TYR ARG LEU ALA PRO GLU THR THR PHE PRO GLY PRO VAL
SEQRES 11 A 323 ASN ASP CYS TYR ALA ALA LEU LEU TYR ILE HIS ALA HIS
SEQRES 12 A 323 ALA GLU GLU LEU GLY ILE ASP PRO SER ARG ILE ALA VAL
SEQRES 13 A 323 GLY GLY GLN SER ALA GLY GLY GLY LEU ALA ALA GLY THR
SEQRES 14 A 323 VAL LEU LYS ALA ARG ASP GLU GLY VAL VAL PRO VAL ALA
SEQRES 15 A 323 PHE GLN PHE LEU GLU ILE PRO GLU LEU ASP ASP ARG LEU
SEQRES 16 A 323 GLU THR VAL SER MET THR ASN PHE VAL ASP THR PRO LEU
SEQRES 17 A 323 TRP HIS ARG PRO ASN ALA ILE LEU SER TRP LYS TYR TYR
SEQRES 18 A 323 LEU GLY GLU SER TYR SER GLY PRO GLU ASP PRO ASP VAL
SEQRES 19 A 323 SER ILE TYR ALA ALA PRO SER ARG ALA THR ASP LEU THR
SEQRES 20 A 323 GLY LEU PRO PRO THR TYR LEU SER THR MET GLU LEU ASP
SEQRES 21 A 323 PRO LEU ARG ASP GLU GLY ILE GLU TYR ALA LEU ARG LEU
SEQRES 22 A 323 LEU GLN ALA GLY VAL SER VAL GLU LEU HIS SER PHE PRO
SEQRES 23 A 323 GLY THR PHE HIS GLY SER ALA LEU VAL ALA THR ALA ALA
SEQRES 24 A 323 VAL SER GLU ARG GLY ALA ALA GLU ALA LEU THR ALA ILE
SEQRES 25 A 323 ARG ARG GLY LEU ARG SER LEU SER PRO VAL SER
FORMUL 2 HOH *313(H2 O1)
HELIX 1 1 ASP A 8 LEU A 15 1 8
HELIX 2 2 ASP A 25 ALA A 42 1 18
HELIX 3 3 THR A 94 SER A 97 5 4
HELIX 4 4 SER A 98 GLY A 110 1 13
HELIX 5 5 PRO A 127 HIS A 143 1 17
HELIX 6 6 HIS A 143 GLY A 148 1 6
HELIX 7 7 SER A 160 GLY A 177 1 18
HELIX 8 8 THR A 197 PHE A 203 1 7
HELIX 9 9 HIS A 210 GLY A 223 1 14
HELIX 10 10 ALA A 239 ALA A 243 5 5
HELIX 11 11 LEU A 262 ALA A 276 1 15
HELIX 12 12 GLY A 291 VAL A 295 5 5
HELIX 13 13 ALA A 298 LEU A 316 1 19
SHEET 1 A 8 VAL A 49 ALA A 56 0
SHEET 2 A 8 VAL A 65 PRO A 72 -1 O THR A 71 N SER A 50
SHEET 3 A 8 ALA A 112 VAL A 116 -1 O ASN A 115 N ARG A 68
SHEET 4 A 8 VAL A 79 ILE A 85 1 N TRP A 84 O VAL A 116
SHEET 5 A 8 PHE A 183 GLU A 187 1 O GLU A 187 N GLY A 158
SHEET 6 A 8 THR A 252 MET A 257 1 O TYR A 253 N LEU A 186
SHEET 7 A 8 VAL A 280 PHE A 285 1 O GLU A 281 N LEU A 254
CISPEP 1 GLY A 77 PRO A 78 0 16.45
CISPEP 2 ALA A 121 PRO A 122 0 -0.68
CISPEP 3 PHE A 126 PRO A 127 0 8.81
CRYST1 71.431 71.431 105.675 90.00 90.00 120.00 P 32 2 1 6
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 0.014000 0.008083 0.000000 0.00000
SCALE2 0.000000 0.016165 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009463 0.00000
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