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HEADER HYDROLASE 06-DEC-11 4AB1
TITLE RECOMBINANT HUMAN CARBOXYLESTERASE 1 FROM WHOLE CABBAGE
TITLE 2 LOOPERS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIVER CARBOXYLESTERASE 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 21-553;
COMPND 5 SYNONYM: ACYL-COENZYME A\:CHOLESTEROL ACYLTRANSFERASE, ACAT, BRAIN
COMPND 6 CARBOXYLESTERASE HBR1, COCAINE CARBOXYLESTERASE, EGASYN, HMSE,
COMPND 7 METHYLUMBELLIFERYL-ACETATE DEACETYLASE 1, MONOCYTE/MACROPHAGE
COMPND 8 SERINE ESTERASE, RETINYL ESTER HYDROLASE, REH, SERINE ESTERASE 1,
COMPND 9 TRIACYLGLYCEROL HYDROLASE, TGH;
COMPND 10 EC: 3.1.1.1, 3.1.1.56;
COMPND 11 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 ORGAN: LIVER;
SOURCE 6 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS
KEYWDS HYDROLASE, WHOLE INSECT EXPRESSION SYSTEMS
EXPDTA X-RAY DIFFRACTION
AUTHOR H.M.GREENBLATT,T.OTTO,D.M.CERASOLI,J.L.SUSSMAN
REVDAT 1 07-MAR-12 4AB1 0
JRNL AUTH H.M.GREENBLATT,T.OTTO,M.G.KIRKPATRICK,E.KOVALEVA,S.BROWN,
JRNL AUTH 2 G.BUCHMAN,D.M.CERASOLI,J.L.SUSSMAN
JRNL TITL STRUCTURE OF RECOMBINANT HUMAN CARBOXYLESTERASE 1 ISOLATED
JRNL TITL 2 FROM WHOLE CABBAGE LOOPER LARVAE
JRNL REF ACTA CRYSTALLOGR.,SECT.F V. F68 269 2012
JRNL REFN ISSN 1744-3091
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.88
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.80
REMARK 3 NUMBER OF REFLECTIONS : 33751
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 + TEST SET) : 0.18141
REMARK 3 R VALUE (WORKING SET) : 0.17846
REMARK 3 FREE R VALUE : 0.23578
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.2
REMARK 3 FREE R VALUE TEST SET COUNT : 1846
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.201
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.258
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2163
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.79
REMARK 3 BIN R VALUE (WORKING SET) : 0.195
REMARK 3 BIN FREE R VALUE SET COUNT : 122
REMARK 3 BIN FREE R VALUE : 0.289
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3989
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 23
REMARK 3 SOLVENT ATOMS : 241
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.008
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.85
REMARK 3 B22 (A**2) : 0.85
REMARK 3 B33 (A**2) : -1.28
REMARK 3 B12 (A**2) : 0.43
REMARK 3 B13 (A**2) : 0.00
REMARK 3 B23 (A**2) : 0.00
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.202
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.188
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.118
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.573
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.953
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.922
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4115 ; 0.020 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5603 ; 1.979 ; 1.971
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 522 ; 6.327 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 160 ;33.273 ;24.500
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 643 ;15.832 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 14 ;19.841 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 632 ; 0.142 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3107 ; 0.010 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2178 ; 0.247 ; 0.2
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2817 ; 0.316 ; 0.2
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 148 ; 0.15 ; 0.20
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 61 ; 0.258 ; 0.2
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 7 ; 0.201 ; 0.2
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS. U VALUES REFINED INDIVIDUALLY.
REMARK 4
REMARK 4 4AB1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 06-DEC-11.
REMARK 100 THE PDBE ID CODE IS EBI-50592.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-JUN-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.8726
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD (MAR225)
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 : 35646
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.20
REMARK 200 RESOLUTION RANGE LOW (A) : 50.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 16.8
REMARK 200 R MERGE (I) : 0.12
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 7.60
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.24
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 14.1
REMARK 200 R MERGE FOR SHELL (I) : 0.65
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 2HRQ
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.14
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.83
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: DROP WAS 45% PROTEIN SOLUTION
REMARK 280 (11MG/ML) OF 50 MM TRIS, PH7.6, 150 MM NACL, MIXED WITH 45%
REMARK 280 2 M AMMONIUM SULFATE, 0.1 M BIS-TRIS, PH 5.5, AND 10% 2 M
REMARK 280 NASCN.
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/2
REMARK 290 6555 X-Y,X,Z+1/2
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z
REMARK 290 10555 -Y,-X,-Z+1/2
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+1/2
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 0.00000
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 0.00000
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 88.55000
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 88.55000
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 88.55000
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 88.55000
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 88.55000
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 88.55000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
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 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 21520 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 105320 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -133.5 KCAL/MOL
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 114.84300
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 88.55000
REMARK 350 BIOMT1 3 0.500000 0.866025 0.000000 0.00000
REMARK 350 BIOMT2 3 0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 -1.000000 88.55000
REMARK 350 BIOMT1 4 -0.500000 -0.866025 0.000000 114.84300
REMARK 350 BIOMT2 4 0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 4 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 5 -0.500000 0.866025 0.000000 57.42150
REMARK 350 BIOMT2 5 -0.866025 -0.500000 0.000000 99.45696
REMARK 350 BIOMT3 5 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 6 0.500000 -0.866025 0.000000 57.42150
REMARK 350 BIOMT2 6 -0.866025 -0.500000 0.000000 99.45696
REMARK 350 BIOMT3 6 0.000000 0.000000 -1.000000 88.55000
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 A2167 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A2241 LIES ON A SPECIAL POSITION.
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 SER A 21
REMARK 465 GLU A 338
REMARK 465 ARG A 339
REMARK 465 ASN A 340
REMARK 465 PHE A 341
REMARK 465 HIS A 342
REMARK 465 SER A 369
REMARK 465 LYS A 553
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 36 CD CE NZ
REMARK 470 GLU A 41 CG CD OE1 OE2
REMARK 470 LYS A 92 CG CD CE NZ
REMARK 470 LYS A 105 CG CD CE NZ
REMARK 470 GLU A 106 CG CD OE1 OE2
REMARK 470 LYS A 111 CD CE NZ
REMARK 470 LYS A 129 CD CE NZ
REMARK 470 LYS A 237 CD CE NZ
REMARK 470 LYS A 257 CE NZ
REMARK 470 LYS A 258 CG CD CE NZ
REMARK 470 GLN A 267 CD OE1 NE2
REMARK 470 LYS A 275 CE NZ
REMARK 470 LEU A 304 CD1 CD2
REMARK 470 LEU A 308 CD1 CD2
REMARK 470 GLU A 314 CG CD OE1 OE2
REMARK 470 LYS A 330 CD CE NZ
REMARK 470 GLU A 333 CG CD OE1 OE2
REMARK 470 GLN A 336 CG CD OE1 NE2
REMARK 470 LYS A 376 CD CE NZ
REMARK 470 GLU A 394 CG CD OE1 OE2
REMARK 470 VAL A 411 CG1 CG2
REMARK 470 LYS A 414 CE NZ
REMARK 470 LYS A 462 CD CE NZ
REMARK 470 GLU A 483 CG CD OE1 OE2
REMARK 470 GLU A 512 CG CD OE1 OE2
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 NE ARG A 452 O HOH A 2193 2.13
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 TRP A 175 CD2 TRP A 175 CE2 0.076
REMARK 500 MET A 361 C LEU A 363 N 0.219
REMARK 500 TRP A 383 CD2 TRP A 383 CE2 0.075
REMARK 500
REMARK 500 REMARK: NULL
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 PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 104 NE - CZ - NH1 ANGL. DEV. = -4.5 DEGREES
REMARK 500 ARG A 186 NE - CZ - NH1 ANGL. DEV. = -4.2 DEGREES
REMARK 500 LEU A 251 CA - CB - CG ANGL. DEV. = 16.8 DEGREES
REMARK 500 MET A 361 CA - C - N ANGL. DEV. = 14.4 DEGREES
REMARK 500 MET A 361 O - C - N ANGL. DEV. = -20.2 DEGREES
REMARK 500 LEU A 420 CA - CB - CG ANGL. DEV. = 15.7 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
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 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ALA A 80 58.79 -117.90
REMARK 500 LYS A 129 49.72 -101.39
REMARK 500 SER A 185 79.65 -153.19
REMARK 500 SER A 214 80.54 -154.64
REMARK 500 SER A 221 -120.87 66.67
REMARK 500 THR A 252 0.42 58.08
REMARK 500 TRP A 357 -61.69 -162.03
REMARK 500 ASP A 409 105.77 -54.78
REMARK 500 ASN A 521 -150.35 -108.21
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 MET A 361 -11.46
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 THR A 252 23.9 L L OUTSIDE RANGE
REMARK 500 GLN A 375 23.7 L L OUTSIDE RANGE
REMARK 500 ARG A 505 20.8 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SCN A1553
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SCN A1554
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SCN A1555
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE
REMARK 800 NAG A1079 BOUND TO ASN A 79
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1MX1 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN LIVER CARBOXYLESTERASE
REMARK 900 INCOMPLEX WITH TACRINE
REMARK 900 RELATED ID: 1MX5 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN LIVER CARBOXYLESTERASE
REMARK 900 INCOMPLEXED WITH HOMATROPINE, A COCAINE ANALOGUE
REMARK 900 RELATED ID: 1MX9 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN LIVER CARBOXYLESTERASE
REMARK 900 INCOMPLEXED WITH NALOXONE METHIODIDE, A HEROIN ANALOGUE
REMARK 900 RELATED ID: 1YA4 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN LIVER CARBOXYLESTERASE 1
REMARK 900 INCOMPLEX WITH TAMOXIFEN
REMARK 900 RELATED ID: 1YA8 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN LIVER CARBOXYLESTERASE
REMARK 900 INCOMPLEX WITH CLEAVAGE PRODUCTS OF MEVASTATIN
REMARK 900 RELATED ID: 1YAH RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN LIVER CARBOXYLESTERASE
REMARK 900 COMPLEXEDTO ETYL ACETATE; A FATTY ACID ETHYL ESTER
REMARK 900 ANALOGUE
REMARK 900 RELATED ID: 1YAJ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN LIVER CARBOXYLESTERASE
REMARK 900 INCOMPLEX WITH BENZIL
DBREF 4AB1 A 21 553 UNP P23141 EST1_HUMAN 21 553
SEQRES 1 A 532 SER SER PRO PRO VAL VAL ASP THR VAL HIS GLY LYS VAL
SEQRES 2 A 532 LEU GLY LYS PHE VAL SER LEU GLU GLY PHE ALA GLN PRO
SEQRES 3 A 532 VAL ALA ILE PHE LEU GLY ILE PRO PHE ALA LYS PRO PRO
SEQRES 4 A 532 LEU GLY PRO LEU ARG PHE THR PRO PRO GLN PRO ALA GLU
SEQRES 5 A 532 PRO TRP SER PHE VAL LYS ASN ALA THR SER TYR PRO PRO
SEQRES 6 A 532 MET CYS THR GLN ASP PRO LYS ALA GLY GLN LEU LEU SER
SEQRES 7 A 532 GLU LEU PHE THR ASN ARG LYS GLU ASN ILE PRO LEU LYS
SEQRES 8 A 532 LEU SER GLU ASP CYS LEU TYR LEU ASN ILE TYR THR PRO
SEQRES 9 A 532 ALA ASP LEU THR LYS LYS ASN ARG LEU PRO VAL MET VAL
SEQRES 10 A 532 TRP ILE HIS GLY GLY GLY LEU MET VAL GLY ALA ALA SER
SEQRES 11 A 532 THR TYR ASP GLY LEU ALA LEU ALA ALA HIS GLU ASN VAL
SEQRES 12 A 532 VAL VAL VAL THR ILE GLN TYR ARG LEU GLY ILE TRP GLY
SEQRES 13 A 532 PHE PHE SER THR GLY ASP GLU HIS SER ARG GLY ASN TRP
SEQRES 14 A 532 GLY HIS LEU ASP GLN VAL ALA ALA LEU ARG TRP VAL GLN
SEQRES 15 A 532 ASP ASN ILE ALA SER PHE GLY GLY ASN PRO GLY SER VAL
SEQRES 16 A 532 THR ILE PHE GLY GLU SER ALA GLY GLY GLU SER VAL SER
SEQRES 17 A 532 VAL LEU VAL LEU SER PRO LEU ALA LYS ASN LEU PHE HIS
SEQRES 18 A 532 ARG ALA ILE SER GLU SER GLY VAL ALA LEU THR SER VAL
SEQRES 19 A 532 LEU VAL LYS LYS GLY ASP VAL LYS PRO LEU ALA GLU GLN
SEQRES 20 A 532 ILE ALA ILE THR ALA GLY CYS LYS THR THR THR SER ALA
SEQRES 21 A 532 VAL MET VAL HIS CYS LEU ARG GLN LYS THR GLU GLU GLU
SEQRES 22 A 532 LEU LEU GLU THR THR LEU LYS MET LYS PHE LEU SER LEU
SEQRES 23 A 532 ASP LEU GLN GLY ASP PRO ARG GLU SER GLN PRO LEU LEU
SEQRES 24 A 532 GLY THR VAL ILE ASP GLY MET LEU LEU LEU LYS THR PRO
SEQRES 25 A 532 GLU GLU LEU GLN ALA GLU ARG ASN PHE HIS THR VAL PRO
SEQRES 26 A 532 TYR MET VAL GLY ILE ASN LYS GLN GLU PHE GLY TRP LEU
SEQRES 27 A 532 ILE PRO MET LEU MET SER TYR PRO LEU SER GLU GLY GLN
SEQRES 28 A 532 LEU ASP GLN LYS THR ALA MET SER LEU LEU TRP LYS SER
SEQRES 29 A 532 TYR PRO LEU VAL CYS ILE ALA LYS GLU LEU ILE PRO GLU
SEQRES 30 A 532 ALA THR GLU LYS TYR LEU GLY GLY THR ASP ASP THR VAL
SEQRES 31 A 532 LYS LYS LYS ASP LEU PHE LEU ASP LEU ILE ALA ASP VAL
SEQRES 32 A 532 MET PHE GLY VAL PRO SER VAL ILE VAL ALA ARG ASN HIS
SEQRES 33 A 532 ARG ASP ALA GLY ALA PRO THR TYR MET TYR GLU PHE GLN
SEQRES 34 A 532 TYR ARG PRO SER PHE SER SER ASP MET LYS PRO LYS THR
SEQRES 35 A 532 VAL ILE GLY ASP HIS GLY ASP GLU LEU PHE SER VAL PHE
SEQRES 36 A 532 GLY ALA PRO PHE LEU LYS GLU GLY ALA SER GLU GLU GLU
SEQRES 37 A 532 ILE ARG LEU SER LYS MET VAL MET LYS PHE TRP ALA ASN
SEQRES 38 A 532 PHE ALA ARG ASN GLY ASN PRO ASN GLY GLU GLY LEU PRO
SEQRES 39 A 532 HIS TRP PRO GLU TYR ASN GLN LYS GLU GLY TYR LEU GLN
SEQRES 40 A 532 ILE GLY ALA ASN THR GLN ALA ALA GLN LYS LEU LYS ASP
SEQRES 41 A 532 LYS GLU VAL ALA PHE TRP THR ASN LEU PHE ALA LYS
HET NAG A1079 14
HET SCN A1553 3
HET SCN A1554 3
HET SCN A1555 3
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM SCN THIOCYANATE ION
FORMUL 2 NAG C8 H15 N O6
FORMUL 3 SCN 3(C N S 1-)
FORMUL 4 HOH *241(H2 O)
HELIX 1 1 LEU A 60 ARG A 64 5 5
HELIX 2 2 ASP A 90 THR A 102 1 13
HELIX 3 3 GLY A 154 ASN A 162 1 9
HELIX 4 4 LEU A 172 PHE A 178 1 7
HELIX 5 5 ASN A 188 ILE A 205 1 18
HELIX 6 6 ALA A 206 PHE A 208 5 3
HELIX 7 7 SER A 221 SER A 233 1 13
HELIX 8 8 PRO A 234 LYS A 237 5 4
HELIX 9 9 VAL A 261 ALA A 272 1 12
HELIX 10 10 THR A 278 LYS A 289 1 12
HELIX 11 11 THR A 290 LYS A 302 1 13
HELIX 12 12 THR A 331 ALA A 337 1 7
HELIX 13 13 TRP A 357 MET A 364 1 7
HELIX 14 14 ASP A 374 SER A 385 1 12
HELIX 15 15 SER A 385 CYS A 390 1 6
HELIX 16 16 LEU A 395 GLY A 405 1 11
HELIX 17 17 VAL A 411 PHE A 426 1 16
HELIX 18 18 PHE A 426 ALA A 440 1 15
HELIX 19 19 GLU A 471 PHE A 476 1 6
HELIX 20 20 GLY A 477 LEU A 481 5 5
HELIX 21 21 SER A 486 GLY A 507 1 22
HELIX 22 22 LYS A 540 ALA A 552 1 13
SHEET 1 AA 3 VAL A 25 THR A 28 0
SHEET 2 AA 3 GLY A 31 LEU A 34 -1 O GLY A 31 N THR A 28
SHEET 3 AA 3 LYS A 78 ASN A 79 1 O LYS A 78 N LEU A 34
SHEET 1 AB11 LYS A 36 VAL A 38 0
SHEET 2 AB11 VAL A 47 PRO A 54 -1 O VAL A 47 N VAL A 38
SHEET 3 AB11 TYR A 118 THR A 123 -1 O LEU A 119 N ILE A 53
SHEET 4 AB11 VAL A 164 ILE A 168 -1 O VAL A 165 N TYR A 122
SHEET 5 AB11 LEU A 133 ILE A 139 1 O PRO A 134 N VAL A 164
SHEET 6 AB11 GLY A 210 GLU A 220 1 N ASN A 211 O LEU A 133
SHEET 7 AB11 ARG A 242 GLU A 246 1 O ARG A 242 N ILE A 217
SHEET 8 AB11 TYR A 346 ASN A 351 1 O MET A 347 N SER A 245
SHEET 9 AB11 THR A 444 GLN A 450 1 O TYR A 445 N VAL A 348
SHEET 10 AB11 GLY A 525 GLY A 530 1 O LEU A 527 N GLU A 448
SHEET 11 AB11 GLN A 534 GLN A 537 -1 O GLN A 534 N GLN A 528
SHEET 1 AC 2 MET A 86 CYS A 87 0
SHEET 2 AC 2 LEU A 112 SER A 113 1 N SER A 113 O MET A 86
SHEET 1 AD 2 VAL A 256 LYS A 257 0
SHEET 2 AD 2 THR A 321 VAL A 322 1 O THR A 321 N LYS A 257
SSBOND 1 CYS A 87 CYS A 116 1555 1555 2.02
SSBOND 2 CYS A 274 CYS A 285 1555 1555 2.13
LINK ND2 ASN A 79 C1 NAG A1079 1555 1555 1.43
SITE 1 AC1 5 ALA A 250 THR A 252 THR A 331 PRO A 332
SITE 2 AC1 5 GLU A 333
SITE 1 AC2 3 GLY A 61 PRO A 62 GLN A 288
SITE 1 AC3 6 SER A 75 PHE A 76 ASP A 182 GLU A 183
SITE 2 AC3 6 ARG A 186 HOH A2153
SITE 1 AC4 2 ASN A 79 THR A 81
CRYST1 114.843 114.843 177.100 90.00 90.00 120.00 P 63 2 2 12
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 0.008708 0.005027 0.000000 0.00000
SCALE2 0.000000 0.010055 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005647 0.00000
TER 3990 ALA A 552
MASTER 494 0 4 22 18 0 6 6 4253 1 28 41
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