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HEADER HYDROLASE 10-APR-03 1P0I
TITLE CRYSTAL STRUCTURE OF HUMAN BUTYRYL CHOLINESTERASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CHOLINESTERASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ACYLCHOLINE ACYLHYDROLASE, CHOLINE ESTERASE II,
COMPND 5 BUTYRYLCHOLINE ESTERASE, PSEUDOCHOLINESTERASE;
COMPND 6 EC: 3.1.1.8;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 GENE: BCHE OR CHE1;
SOURCE 5 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;
SOURCE 7 EXPRESSION_SYSTEM_CELL_LINE: OVARY CELLS
KEYWDS SERINE HYDROLASE, BUTYRATE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.NICOLET,O.LOCKRIDGE,P.MASSON,J.C.FONTECILLA-CAMPS,F.NACHON
REVDAT 1 05-AUG-03 1P0I 0
JRNL AUTH Y.NICOLET,O.LOCKRIDGE,P.MASSON,
JRNL AUTH 2 J.C.FONTECILLA-CAMPS,F.NACHON
JRNL TITL CRYSTAL STRUCTURE OF HUMAN BUTYRYL CHOLINESTERASE
JRNL TITL 2 AND OF ITS COMPLEXES WITH SUBSTRATE AND PRODUCTS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH F.NACHON,Y.NICOLET,N.VIGUIE,P.MASSON,
REMARK 1 AUTH 2 J.C.FONTECILLA-CAMPS,O.LOCKRIDGE
REMARK 1 TITL ENGINEERING OF A MONOMERIC AND LOW-GLYCOSYLATED
REMARK 1 TITL 2 FORM OF HUMAN BUTYRYLCHOLINESTERASE: EXPRESSION,
REMARK 1 TITL 3 PURIFICATION, CHARACTERIZATION AND CRYSTALLIZATION
REMARK 1 REF EUR.J.BIOCHEM. V. 269 630 2002
REMARK 1 REFN ASTM EJBCAI IX ISSN 0014-2956
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 0.9
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 55.20
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 93.8
REMARK 3 NUMBER OF REFLECTIONS : 49144
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 SET) : 0.195
REMARK 3 FREE R VALUE : 0.225
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2449
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.005
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.13
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 92.50
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 7557
REMARK 3 BIN R VALUE (WORKING SET) : 0.2680
REMARK 3 BIN FREE R VALUE : 0.3250
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.10
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 402
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.016
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4199
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 148
REMARK 3 SOLVENT ATOMS : 501
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 19.80
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.50
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -3.67000
REMARK 3 B22 (A**2) : -3.67000
REMARK 3 B33 (A**2) : 7.34000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.22
REMARK 3 ESD FROM SIGMAA (A) : 0.23
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.28
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.29
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.014
REMARK 3 BOND ANGLES (DEGREES) : 1.60
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.70
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.08
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 4.210 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 4.790 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 4.770 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 5.940 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.38
REMARK 3 BSOL : 109.57
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : CARBOHYDRATE.PARAM
REMARK 3 PARAMETER FILE 3 : WATER.PARAM
REMARK 3 PARAMETER FILE 4 : ION.PARAM
REMARK 3 PARAMETER FILE 5 : LIGAND.PARAM
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : CARBOHYDRATE.TOP
REMARK 3 TOPOLOGY FILE 3 : ION.TOP
REMARK 3 TOPOLOGY FILE 4 : WATER.TOP
REMARK 3 TOPOLOGY FILE 5 : LIGAND.TOP
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1P0I COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-APR-2003.
REMARK 100 THE RCSB ID CODE IS RCSB018865.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 6.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.933
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 : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 49144
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 55.200
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 200 DATA REDUNDANCY : 7.300
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.07400
REMARK 200 FOR THE DATA SET : 6.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.11
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6
REMARK 200 DATA REDUNDANCY IN SHELL : 6.40
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.44800
REMARK 200 FOR SHELL : 1.700
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: PDB ENTRY 2ACE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.0
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.82
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, 2-(N-MORPHOLINO)-
REMARK 280 ETHANESULFONIC ACID, PH 6.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 298.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -Y,X,Z
REMARK 290 4555 Y,-X,Z
REMARK 290 5555 -X,Y,-Z
REMARK 290 6555 X,-Y,-Z
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z
REMARK 290 9555 1/2+X,1/2+Y,1/2+Z
REMARK 290 10555 1/2-X,1/2-Y,1/2+Z
REMARK 290 11555 1/2-Y,1/2+X,1/2+Z
REMARK 290 12555 1/2+Y,1/2-X,1/2+Z
REMARK 290 13555 1/2-X,1/2+Y,1/2-Z
REMARK 290 14555 1/2+X,1/2-Y,1/2-Z
REMARK 290 15555 1/2+Y,1/2+X,1/2-Z
REMARK 290 16555 1/2-Y,1/2-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 0.00000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 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 0.00000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000
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 0.00000
REMARK 290 SMTRY1 9 1.000000 0.000000 0.000000 77.33000
REMARK 290 SMTRY2 9 0.000000 1.000000 0.000000 77.33000
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 63.94500
REMARK 290 SMTRY1 10 -1.000000 0.000000 0.000000 77.33000
REMARK 290 SMTRY2 10 0.000000 -1.000000 0.000000 77.33000
REMARK 290 SMTRY3 10 0.000000 0.000000 1.000000 63.94500
REMARK 290 SMTRY1 11 0.000000 -1.000000 0.000000 77.33000
REMARK 290 SMTRY2 11 1.000000 0.000000 0.000000 77.33000
REMARK 290 SMTRY3 11 0.000000 0.000000 1.000000 63.94500
REMARK 290 SMTRY1 12 0.000000 1.000000 0.000000 77.33000
REMARK 290 SMTRY2 12 -1.000000 0.000000 0.000000 77.33000
REMARK 290 SMTRY3 12 0.000000 0.000000 1.000000 63.94500
REMARK 290 SMTRY1 13 -1.000000 0.000000 0.000000 77.33000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 77.33000
REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 63.94500
REMARK 290 SMTRY1 14 1.000000 0.000000 0.000000 77.33000
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 77.33000
REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 63.94500
REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 77.33000
REMARK 290 SMTRY2 15 1.000000 0.000000 0.000000 77.33000
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 63.94500
REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 77.33000
REMARK 290 SMTRY2 16 -1.000000 0.000000 0.000000 77.33000
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 63.94500
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, B, C
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 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 CL CL 701 LIES ON A SPECIAL POSITION.
REMARK 375 HOH 255 LIES ON A SPECIAL POSITION.
REMARK 375 HOH 450 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 GLU A 1
REMARK 465 ASP A 2
REMARK 465 ASP A 3
REMARK 465 ASP A 378
REMARK 465 ASP A 379
REMARK 465 GLN A 455
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 GLN A 486 CG CD OE1 NE2
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),F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 THR A 86 CB THR A 86 CG2 -0.084
REMARK 500 MET A 166 SD MET A 166 CE 0.114
REMARK 500 MET A 434 SD MET A 434 CE -0.132
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 ASP A 54 N - CA - C ANGL. DEV. =-14.0 DEGREES
REMARK 500 LEU A 156 N - CA - C ANGL. DEV. =-12.9 DEGREES
REMARK 500 ASN A 181 N - CA - C ANGL. DEV. = 10.5 DEGREES
REMARK 500 ALA A 232 N - CA - C ANGL. DEV. = 11.6 DEGREES
REMARK 500 VAL A 288 N - CA - C ANGL. DEV. =-10.0 DEGREES
REMARK 500 GLY A 326 N - CA - C ANGL. DEV. = 10.2 DEGREES
REMARK 500 GLY A 413 N - CA - C ANGL. DEV. = 10.5 DEGREES
REMARK 500 TYR A 420 N - CA - C ANGL. DEV. = -9.6 DEGREES
REMARK 500 GLU A 482 N - CA - C ANGL. DEV. =-14.8 DEGREES
REMARK 500 THR A 483 N - CA - C ANGL. DEV. = 10.8 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 ASP A 54 177.74 86.44
REMARK 525
REMARK 525 SOLVENT
REMARK 525 THE FOLLOWING SOLVENT MOLECULES LIE FARTHER THAN EXPECTED
REMARK 525 FROM THE PROTEIN OR NUCLEIC ACID MOLECULE AND MAY BE
REMARK 525 ASSOCIATED WITH A SYMMETRY RELATED MOLECULE (M=MODEL
REMARK 525 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH 133 DISTANCE = 5.56 ANGSTROMS
REMARK 525 HOH 180 DISTANCE = 5.77 ANGSTROMS
REMARK 525 HOH 277 DISTANCE = 6.96 ANGSTROMS
REMARK 525 HOH 338 DISTANCE = 7.41 ANGSTROMS
REMARK 525 HOH 374 DISTANCE = 5.17 ANGSTROMS
REMARK 525 HOH 409 DISTANCE = 5.02 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1POM RELATED DB: PDB
REMARK 900 COMPLEX WITH A CHOLINE MOLECULE
REMARK 900 RELATED ID: 1POP RELATED DB: PDB
REMARK 900 SOMAN-AGED BUTYRYLCHOLINESTERASE COMPLEX WITH
REMARK 900 BUTYRYLTHIOCHOLINE
REMARK 900 RELATED ID: 1POQ RELATED DB: PDB
REMARK 900 SOMAN-AGED STRUCTURE OF THE HUMAN BUTYRYLCHOLINESTERASE
DBREF 1P0I A 1 529 SWS P06276 CHLE_HUMAN 29 557
SEQADV 1P0I GLN A 17 SWS P06276 ASN 45 ENGINEERED
SEQADV 1P0I GLN A 455 SWS P06276 ASN 483 ENGINEERED
SEQADV 1P0I GLN A 481 SWS P06276 ASN 509 ENGINEERED
SEQADV 1P0I GLN A 486 SWS P06276 ASN 514 ENGINEERED
SEQRES 1 A 529 GLU ASP ASP ILE ILE ILE ALA THR LYS ASN GLY LYS VAL
SEQRES 2 A 529 ARG GLY MET GLN LEU THR VAL PHE GLY GLY THR VAL THR
SEQRES 3 A 529 ALA PHE LEU GLY ILE PRO TYR ALA GLN PRO PRO LEU GLY
SEQRES 4 A 529 ARG LEU ARG PHE LYS LYS PRO GLN SER LEU THR LYS TRP
SEQRES 5 A 529 SER ASP ILE TRP ASN ALA THR LYS TYR ALA ASN SER CYS
SEQRES 6 A 529 CYS GLN ASN ILE ASP GLN SER PHE PRO GLY PHE HIS GLY
SEQRES 7 A 529 SER GLU MET TRP ASN PRO ASN THR ASP LEU SER GLU ASP
SEQRES 8 A 529 CYS LEU TYR LEU ASN VAL TRP ILE PRO ALA PRO LYS PRO
SEQRES 9 A 529 LYS ASN ALA THR VAL LEU ILE TRP ILE TYR GLY GLY GLY
SEQRES 10 A 529 PHE GLN THR GLY THR SER SER LEU HIS VAL TYR ASP GLY
SEQRES 11 A 529 LYS PHE LEU ALA ARG VAL GLU ARG VAL ILE VAL VAL SER
SEQRES 12 A 529 MET ASN TYR ARG VAL GLY ALA LEU GLY PHE LEU ALA LEU
SEQRES 13 A 529 PRO GLY ASN PRO GLU ALA PRO GLY ASN MET GLY LEU PHE
SEQRES 14 A 529 ASP GLN GLN LEU ALA LEU GLN TRP VAL GLN LYS ASN ILE
SEQRES 15 A 529 ALA ALA PHE GLY GLY ASN PRO LYS SER VAL THR LEU PHE
SEQRES 16 A 529 GLY GLU SER ALA GLY ALA ALA SER VAL SER LEU HIS LEU
SEQRES 17 A 529 LEU SER PRO GLY SER HIS SER LEU PHE THR ARG ALA ILE
SEQRES 18 A 529 LEU GLN SER GLY SER PHE ASN ALA PRO TRP ALA VAL THR
SEQRES 19 A 529 SER LEU TYR GLU ALA ARG ASN ARG THR LEU ASN LEU ALA
SEQRES 20 A 529 LYS LEU THR GLY CYS SER ARG GLU ASN GLU THR GLU ILE
SEQRES 21 A 529 ILE LYS CYS LEU ARG ASN LYS ASP PRO GLN GLU ILE LEU
SEQRES 22 A 529 LEU ASN GLU ALA PHE VAL VAL PRO TYR GLY THR PRO LEU
SEQRES 23 A 529 SER VAL ASN PHE GLY PRO THR VAL ASP GLY ASP PHE LEU
SEQRES 24 A 529 THR ASP MET PRO ASP ILE LEU LEU GLU LEU GLY GLN PHE
SEQRES 25 A 529 LYS LYS THR GLN ILE LEU VAL GLY VAL ASN LYS ASP GLU
SEQRES 26 A 529 GLY THR ALA PHE LEU VAL TYR GLY ALA PRO GLY PHE SER
SEQRES 27 A 529 LYS ASP ASN ASN SER ILE ILE THR ARG LYS GLU PHE GLN
SEQRES 28 A 529 GLU GLY LEU LYS ILE PHE PHE PRO GLY VAL SER GLU PHE
SEQRES 29 A 529 GLY LYS GLU SER ILE LEU PHE HIS TYR THR ASP TRP VAL
SEQRES 30 A 529 ASP ASP GLN ARG PRO GLU ASN TYR ARG GLU ALA LEU GLY
SEQRES 31 A 529 ASP VAL VAL GLY ASP TYR ASN PHE ILE CYS PRO ALA LEU
SEQRES 32 A 529 GLU PHE THR LYS LYS PHE SER GLU TRP GLY ASN ASN ALA
SEQRES 33 A 529 PHE PHE TYR TYR PHE GLU HIS ARG SER SER LYS LEU PRO
SEQRES 34 A 529 TRP PRO GLU TRP MET GLY VAL MET HIS GLY TYR GLU ILE
SEQRES 35 A 529 GLU PHE VAL PHE GLY LEU PRO LEU GLU ARG ARG ASP GLN
SEQRES 36 A 529 TYR THR LYS ALA GLU GLU ILE LEU SER ARG SER ILE VAL
SEQRES 37 A 529 LYS ARG TRP ALA ASN PHE ALA LYS TYR GLY ASN PRO GLN
SEQRES 38 A 529 GLU THR GLN ASN GLN SER THR SER TRP PRO VAL PHE LYS
SEQRES 39 A 529 SER THR GLU GLN LYS TYR LEU THR LEU ASN THR GLU SER
SEQRES 40 A 529 THR ARG ILE MET THR LYS LEU ARG ALA GLN GLN CYS ARG
SEQRES 41 A 529 PHE TRP THR SER PHE PHE PRO LYS VAL
MODRES 1P0I ASN A 57 ASN GLYCOSYLATION SITE
MODRES 1P0I ASN A 106 ASN GLYCOSYLATION SITE
MODRES 1P0I ASN A 241 ASN GLYCOSYLATION SITE
MODRES 1P0I ASN A 341 ASN GLYCOSYLATION SITE
MODRES 1P0I ASN A 485 ASN GLYCOSYLATION SITE
HET NAG B 1 14
HET NAG B 2 14
HET FUC B 3 10
HET NAG C 1 14
HET NAG C 2 14
HET FUC C 3 10
HET NAG A 530 14
HET NAG A 531 14
HET NAG A 532 14
HET SUL 601 5
HET SUL 602 5
HET CL 701 1
HET CL 702 1
HET BUA A 606 6
HET MES 607 12
HET GOL 603 6
HET GOL 604 6
HET GOL 605 6
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM FUC FUCOSE
HETNAM SUL SULFATE ANION
HETNAM CL CHLORIDE ION
HETNAM BUA BUTANOIC ACID
HETNAM MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID
HETNAM GOL GLYCEROL
HETSYN NAG NAG
FORMUL 2 NAG 7(C8 H15 N1 O6)
FORMUL 2 FUC 2(C6 H12 O5)
FORMUL 7 SUL 2(O4 S1 2-)
FORMUL 9 CL 2(CL1 1-)
FORMUL 11 BUA C4 H8 O2
FORMUL 12 MES C6 H13 N1 O4 S1
FORMUL 13 GOL 3(C3 H8 O3)
FORMUL 16 HOH *483(H2 O1)
HELIX 1 1 LEU A 38 ARG A 42 5 5
HELIX 2 2 PHE A 76 MET A 81 1 6
HELIX 3 3 LEU A 125 ASP A 129 5 5
HELIX 4 4 GLY A 130 ARG A 138 1 9
HELIX 5 5 VAL A 148 LEU A 154 1 7
HELIX 6 6 ASN A 165 ILE A 182 1 18
HELIX 7 7 ALA A 183 PHE A 185 5 3
HELIX 8 8 SER A 198 SER A 210 1 13
HELIX 9 9 PRO A 211 PHE A 217 5 7
HELIX 10 10 SER A 235 THR A 250 1 16
HELIX 11 11 ASN A 256 ARG A 265 1 10
HELIX 12 12 ASP A 268 ALA A 277 1 10
HELIX 13 13 PHE A 278 VAL A 280 5 3
HELIX 14 14 MET A 302 LEU A 309 1 8
HELIX 15 15 GLY A 326 VAL A 331 1 6
HELIX 16 16 THR A 346 PHE A 358 1 13
HELIX 17 17 SER A 362 THR A 374 1 13
HELIX 18 18 GLU A 383 PHE A 398 1 16
HELIX 19 19 PHE A 398 GLU A 411 1 14
HELIX 20 20 PRO A 431 GLY A 435 5 5
HELIX 21 21 GLU A 441 PHE A 446 1 6
HELIX 22 22 GLY A 447 GLU A 451 5 5
HELIX 23 23 THR A 457 GLY A 478 1 22
HELIX 24 24 ARG A 515 SER A 524 1 10
SHEET 1 A 3 ILE A 5 THR A 8 0
SHEET 2 A 3 GLY A 11 ARG A 14 -1 O VAL A 13 N ILE A 6
SHEET 3 A 3 ILE A 55 ASN A 57 1 O TRP A 56 N LYS A 12
SHEET 1 B11 MET A 16 VAL A 20 0
SHEET 2 B11 GLY A 23 PRO A 32 -1 O VAL A 25 N LEU A 18
SHEET 3 B11 TYR A 94 PRO A 100 -1 O LEU A 95 N ILE A 31
SHEET 4 B11 ILE A 140 MET A 144 -1 O SER A 143 N ASN A 96
SHEET 5 B11 ALA A 107 ILE A 113 1 N TRP A 112 O VAL A 142
SHEET 6 B11 GLY A 187 GLU A 197 1 O ASN A 188 N ALA A 107
SHEET 7 B11 ARG A 219 GLN A 223 1 O GLN A 223 N GLY A 196
SHEET 8 B11 ILE A 317 ASN A 322 1 O LEU A 318 N LEU A 222
SHEET 9 B11 ALA A 416 PHE A 421 1 O PHE A 421 N VAL A 321
SHEET 10 B11 LYS A 499 LEU A 503 1 O LEU A 501 N TYR A 420
SHEET 11 B11 ILE A 510 THR A 512 -1 O MET A 511 N TYR A 500
SSBOND 1 CYS A 65 CYS A 92
SSBOND 2 CYS A 252 CYS A 263
SSBOND 3 CYS A 400 CYS A 519
LINK ND2 ASN A 57 C1 NAG A 531
LINK ND2 ASN A 106 C1 NAG A 530
LINK ND2 ASN A 241 C1 NAG B 1
LINK ND2 ASN A 341 C1 NAG C 1
LINK ND2 ASN A 485 C1 NAG A 532
LINK O4 NAG B 1 C1 NAG B 2
LINK O6 NAG B 1 C1 FUC B 3
LINK O4 NAG C 1 C1 NAG C 2
LINK O6 NAG C 1 C1 FUC C 3
LINK OG SER A 198 C4 BUA A 606
CISPEP 1 ALA A 101 PRO A 102 0 -0.22
CRYST1 154.660 154.660 127.890 90.00 90.00 90.00 I 4 2 2 16
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 0.006466 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006466 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007819 0.00000
TER 4200 VAL A 529
MASTER 385 0 18 24 14 0 0 6 4848 1 176 41
END |