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HEADER HYDROLASE 12-MAY-09 2WIL
TITLE AGED FORM OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY TABUN
TITLE 2 ANALOGUE TA5
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CHOLINESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RESIDUES 29-557;
COMPND 5 SYNONYM: ACYLCHOLINE ACYLHYDROLASE, BUTYRYLCHOLINE
COMPND 6 ESTERASE, CHOLINE ESTERASE II, PSEUDOCHOLINESTERASE;
COMPND 7 EC: 3.1.1.8;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES;
COMPND 10 OTHER_DETAILS: S198 IS PHOSPHORAMIDYLATED
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 10029;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: CHO-K1;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: OVARY CELLS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGS
KEYWDS TABUN, AGING, HYDROLASE, INHIBITION, POLYMORPHISM,
KEYWDS 2 GLYCOPROTEIN, DISULFIDE BOND, SERINE ESTERASE, DISEASE
KEYWDS 3 MUTATION, BUTYRYLCHOLINESTERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR E.CARLETTI,N.AURBEK,E.GILLON,M.LOIODICE,Y.NICOLET,
AUTHOR 2 J.FONTECILLA,P.MASSON,H.THIERMANN,F.NACHON,F.WOREK
REVDAT 2 02-JUN-09 2WIL 1 REVDAT
REVDAT 1 26-MAY-09 2WIL 0
JRNL AUTH E.CARLETTI,N.AURBEK,E.GILLON,M.LOIODICE,Y.NICOLET,
JRNL AUTH 2 J.FONTECILLA,P.MASSON,H.THIERMANN,F.NACHON,F.WOREK
JRNL TITL STRUCTURE-ACTIVITY ANALYSIS OF AGING AND
JRNL TITL 2 REACTIVATION OF HUMAN BUTYRYLCHOLINESTERASE
JRNL TITL 3 INHIBITED BY ANALOGUES OF TABUN
JRNL REF BIOCHEM.J. 2009
JRNL REFN ESSN 1470-8728
JRNL PMID 19368529
JRNL DOI 10.1042/BJ20090091
REMARK 2
REMARK 2 RESOLUTION. 3.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.4.0069
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) : 3.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.39
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.25
REMARK 3 NUMBER OF REFLECTIONS : 28167
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) : 0.22120
REMARK 3 R VALUE (WORKING SET) : 0.22016
REMARK 3 FREE R VALUE : 0.25281
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.2
REMARK 3 FREE R VALUE TEST SET COUNT : 937
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) : 3.100
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.180
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2026
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.08
REMARK 3 BIN R VALUE (WORKING SET) : 0.352
REMARK 3 BIN FREE R VALUE SET COUNT : 64
REMARK 3 BIN FREE R VALUE : 0.416
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8397
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 264
REMARK 3 SOLVENT ATOMS : 137
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 73.731
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.02
REMARK 3 B22 (A**2) : -0.02
REMARK 3 B33 (A**2) : 0.05
REMARK 3 B12 (A**2) : 0.00
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.445
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.336
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 19.693
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.931
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.913
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8916 ; 0.012 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 12142 ; 1.415 ; 1.976
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1056 ; 5.988 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 403 ;35.627 ;24.020
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1400 ;19.034 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 44 ;17.531 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1327 ; 0.087 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6734 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): 5247 ; 0.598 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 8475 ; 1.146 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3669 ; 1.358 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3664 ; 2.480 ; 4.500
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 : 2
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 1531 A 1542 1
REMARK 3 1 B 1531 B 1539 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 118 ; 0.03 ; 0.05
REMARK 3 TIGHT THERMAL 1 A (A**2): 118 ; 0.35 ; 0.50
REMARK 3 TIGHT POSITIONAL 1 B (A): 118 ; 0.03 ; 0.05
REMARK 3 TIGHT THERMAL 1 B (A**2): 118 ; 0.35 ; 0.50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 2 A 529 1
REMARK 3 1 B 4 B 529 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 2 A (A): 4185 ; 0.04 ; 0.05
REMARK 3 TIGHT THERMAL 2 A (A**2): 4185 ; 0.11 ; 0.50
REMARK 3 TIGHT POSITIONAL 2 B (A): 4185 ; 0.04 ; 0.05
REMARK 3 TIGHT THERMAL 2 B (A**2): 4185 ; 0.11 ; 0.50
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH 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
REMARK 3 RIDING POSITIONS.
REMARK 4
REMARK 4 2WIL COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-MAY-09.
REMARK 100 THE PDBE ID CODE IS EBI-39791.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-SEP-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-4
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9395
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28167
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.10
REMARK 200 RESOLUTION RANGE LOW (A) : 48.40
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 200 DATA REDUNDANCY : 5.7
REMARK 200 R MERGE (I) : 0.10
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 29.20
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.20
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.2
REMARK 200 DATA REDUNDANCY IN SHELL : 5.9
REMARK 200 R MERGE FOR SHELL (I) : 0.30
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 8.60
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: XDS
REMARK 200 STARTING MODEL: PDB ENTRY 1P0I
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.7
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.3
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.1 M AMMONIUM SULFATE, 100 MM
REMARK 280 MES PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 4 21 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+1/2,X+1/2,Z
REMARK 290 4555 Y+1/2,-X+1/2,Z
REMARK 290 5555 -X+1/2,Y+1/2,-Z
REMARK 290 6555 X+1/2,-Y+1/2,-Z
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-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 75.17500
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 75.17500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 75.17500
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 75.17500
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 75.17500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 75.17500
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 75.17500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 75.17500
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
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 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 AUTHOR DETERMINED BIOLOGICAL UNIT: OCTAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 34890 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 158820 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -56.61 KCAL/MOL
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 -1.000000 0.000000 0.000000 -150.35000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 0.000000 1.000000 0.000000 -75.17500
REMARK 350 BIOMT2 3 -1.000000 0.000000 0.000000 -75.17500
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 4 0.000000 -1.000000 0.000000 -75.17500
REMARK 350 BIOMT2 4 1.000000 0.000000 0.000000 75.17500
REMARK 350 BIOMT3 4 0.000000 0.000000 1.000000 0.00000
REMARK 400
REMARK 400 COMPOUND
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, ASN 45 TO GLN
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, ASN 509 TO GLN
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, ASN 45 TO GLN
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, ASN 509 TO GLN
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 378
REMARK 465 ASP A 379
REMARK 465 GLU B 1
REMARK 465 ASP B 2
REMARK 465 ASP B 3
REMARK 465 ASP B 378
REMARK 465 ASP B 379
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 ASN A 486 CG OD1 ND2
REMARK 470 ASN B 486 CG OD1 ND2
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER;
REMARK 480 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 480 I=INSERTION CODE):
REMARK 480 M RES CSSEQI ATOMS
REMARK 480 TYR A 282 CG CD1 CD2 CE1 CE2 CZ OH
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 OE1 GLN A 380 - O HOH A 2041 2.15
REMARK 500 O LYS B 355 - O HOH B 2047 2.18
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 TYR A 282 CB TYR A 282 CG -0.171
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 TYR A 282 CB - CG - CD1 ANGL. DEV. = -7.5 DEGREES
REMARK 500 TYR A 282 CB - CG - CD2 ANGL. DEV. = 7.4 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 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 ASP A 3 104.71 37.68
REMARK 500 LYS A 9 5.21 -59.47
REMARK 500 ASP A 54 -167.35 98.86
REMARK 500 ALA A 58 72.72 -104.26
REMARK 500 GLN A 67 161.25 178.13
REMARK 500 CYS A 92 12.32 -146.90
REMARK 500 LYS A 103 124.72 -35.36
REMARK 500 PHE A 118 10.51 57.93
REMARK 500 PHE A 153 16.89 -141.32
REMARK 500 SER A 198 -120.62 44.36
REMARK 500 SER A 224 68.70 37.54
REMARK 500 SER A 226 147.43 -171.59
REMARK 500 ASN A 228 4.90 -68.89
REMARK 500 GLU A 255 -63.92 -107.14
REMARK 500 ASP A 297 -82.80 -113.30
REMARK 500 ASP A 301 159.10 173.86
REMARK 500 GLN A 311 66.06 -103.17
REMARK 500 ASN A 342 22.30 -74.21
REMARK 500 SER A 362 153.11 -34.43
REMARK 500 THR A 374 44.03 -106.22
REMARK 500 ASP A 375 79.53 -101.21
REMARK 500 PHE A 398 -69.00 -135.20
REMARK 500 VAL A 436 89.28 -63.77
REMARK 500 PRO A 449 0.12 -66.20
REMARK 500 ARG A 453 70.83 -64.54
REMARK 500 ASP A 454 -16.60 -152.48
REMARK 500 PRO A 480 43.92 -89.35
REMARK 500 ASN A 485 49.83 -98.43
REMARK 500 GLU A 506 -107.25 -73.93
REMARK 500 LYS B 9 6.01 -59.74
REMARK 500 PHE B 28 79.42 -110.86
REMARK 500 ASP B 54 -167.48 99.05
REMARK 500 ALA B 58 73.38 -103.95
REMARK 500 GLN B 67 157.59 176.04
REMARK 500 MET B 81 -17.95 -49.37
REMARK 500 LYS B 103 125.47 -33.54
REMARK 500 SER B 198 -124.57 39.89
REMARK 500 SER B 224 77.53 26.93
REMARK 500 SER B 226 146.06 -171.84
REMARK 500 GLU B 255 -67.15 -108.19
REMARK 500 PRO B 285 -17.02 -47.69
REMARK 500 ASP B 297 -77.14 -114.69
REMARK 500 ASP B 301 160.07 170.19
REMARK 500 GLN B 311 66.96 -106.26
REMARK 500 ASN B 342 22.60 -74.98
REMARK 500 SER B 362 154.34 -37.37
REMARK 500 THR B 374 46.63 -106.23
REMARK 500 ASP B 375 78.36 -102.93
REMARK 500 PHE B 398 -66.52 -132.58
REMARK 500 VAL B 436 87.53 -62.03
REMARK 500 PRO B 449 1.88 -69.86
REMARK 500 ARG B 453 71.01 -60.18
REMARK 500 ASP B 454 -15.74 -154.69
REMARK 500 PRO B 480 41.40 -83.42
REMARK 500 ASN B 485 46.72 -96.37
REMARK 500 GLU B 506 -106.69 -75.97
REMARK 500 ARG B 515 55.76 37.62
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TCX A 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TCX B 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1531
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1532
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FUC A1533
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1534
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1535
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FUC A1536
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1537
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1538
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1539
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B1531
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B1532
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FUC B1533
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B1534
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B1535
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FUC B1536
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B1537
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B1538
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B1539
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1540
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1541
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1540
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A1542
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1EHQ RELATED DB: PDB
REMARK 900 MODEL OF (+)-COCAINE-BOUND BCHE COMPLEX
REMARK 900 RELATED ID: 2J4C RELATED DB: PDB
REMARK 900 STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE IN
REMARK 900 COMPLEX WITH 10MM HGCL2
REMARK 900 RELATED ID: 1P0Q RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF SOMAN-AGED HUMAN
REMARK 900 BUTYRYL CHOLINESTERASE
REMARK 900 RELATED ID: 2WIK RELATED DB: PDB
REMARK 900 NONAGED FORM OF HUMAN BUTYRYLCHOLINESTERASE
REMARK 900 INHIBITED BY TABUN ANALOGUE TA6
REMARK 900 RELATED ID: 1KCJ RELATED DB: PDB
REMARK 900 MODEL OF (-)-COCAINE-BOUND (-)-COCAINE
REMARK 900 HYDROLASE COMPLEX
REMARK 900 RELATED ID: 1P0P RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF SOMAN-AGED HUMAN
REMARK 900 BUTYRYLCHOLINESTERASE IN COMPLEX WITH THE
REMARK 900 SUBSTRATE ANALOGBUTYRYLTHIOCHOLINE
REMARK 900 RELATED ID: 2WID RELATED DB: PDB
REMARK 900 AGED FORM OF HUMAN BUTYRYLCHOLINESTERASE
REMARK 900 INHIBITED BY TABUN ANALOGUE TA1
REMARK 900 RELATED ID: 1XLU RELATED DB: PDB
REMARK 900 X-RAY STRUCTURE OF DI-ISOPROPYL-PHOSPHORO-
REMARK 900 FLUORIDATE (DFP)INHIBITED BUTYRYLCHOLINESTERASE
REMARK 900 AFTER AGING
REMARK 900 RELATED ID: 2WIJ RELATED DB: PDB
REMARK 900 NONAGED FORM OF HUMAN BUTYRYLCHOLINESTERASE
REMARK 900 INHIBITED BY TABUN ANALOGUE TA5
REMARK 900 RELATED ID: 1XLV RELATED DB: PDB
REMARK 900 ETHYLPHOSPHORYLATED BUTYRYLCHOLINESTERASE (AGED)
REMARK 900 OBTAINEDBY REACTION WITH ECHOTHIOPHATE
REMARK 900 RELATED ID: 1EHO RELATED DB: PDB
REMARK 900 MODEL OF (-)-COCAINE-BOUND BCHE COMPLEX.
REMARK 900 RELATED ID: 2WIF RELATED DB: PDB
REMARK 900 AGED FORM OF HUMAN BUTYRYLCHOLINESTERASE
REMARK 900 INHIBITED BY TABUN ANALOGUE TA1
REMARK 900 RELATED ID: 1P0M RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN BUTYRYL
REMARK 900 CHOLINESTERASE INCOMPLEX WITH A CHOLINE
REMARK 900 MOLECULE
REMARK 900 RELATED ID: 1XLW RELATED DB: PDB
REMARK 900 DIETHYLPHOSPHORYLATED BUTYRYLCHOLINESTERASE (NONAGED
REMARK 900 )OBTAINED BY REACTION WITH ECHOTHIOPHATE
REMARK 900 RELATED ID: 1P0I RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN BUTYRYL
REMARK 900 CHOLINESTERASE
REMARK 900 RELATED ID: 2WIG RELATED DB: PDB
REMARK 900 NONAGED FORM OF HUMAN BUTYRYLCHOLINESTERASE
REMARK 900 INHIBITED BY TABUN ANALOGUE TA4
DBREF 2WIL A 1 529 UNP P06276 CHLE_HUMAN 29 557
DBREF 2WIL B 1 529 UNP P06276 CHLE_HUMAN 29 557
SEQADV 2WIL GLN A 17 UNP P06276 ASN 45 ENGINEERED MUTATION
SEQADV 2WIL GLN A 481 UNP P06276 ASN 509 ENGINEERED MUTATION
SEQADV 2WIL GLN B 17 UNP P06276 ASN 45 ENGINEERED MUTATION
SEQADV 2WIL GLN B 481 UNP P06276 ASN 509 ENGINEERED MUTATION
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 ASN
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 ASN 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
SEQRES 1 B 529 GLU ASP ASP ILE ILE ILE ALA THR LYS ASN GLY LYS VAL
SEQRES 2 B 529 ARG GLY MET GLN LEU THR VAL PHE GLY GLY THR VAL THR
SEQRES 3 B 529 ALA PHE LEU GLY ILE PRO TYR ALA GLN PRO PRO LEU GLY
SEQRES 4 B 529 ARG LEU ARG PHE LYS LYS PRO GLN SER LEU THR LYS TRP
SEQRES 5 B 529 SER ASP ILE TRP ASN ALA THR LYS TYR ALA ASN SER CYS
SEQRES 6 B 529 CYS GLN ASN ILE ASP GLN SER PHE PRO GLY PHE HIS GLY
SEQRES 7 B 529 SER GLU MET TRP ASN PRO ASN THR ASP LEU SER GLU ASP
SEQRES 8 B 529 CYS LEU TYR LEU ASN VAL TRP ILE PRO ALA PRO LYS PRO
SEQRES 9 B 529 LYS ASN ALA THR VAL LEU ILE TRP ILE TYR GLY GLY GLY
SEQRES 10 B 529 PHE GLN THR GLY THR SER SER LEU HIS VAL TYR ASP GLY
SEQRES 11 B 529 LYS PHE LEU ALA ARG VAL GLU ARG VAL ILE VAL VAL SER
SEQRES 12 B 529 MET ASN TYR ARG VAL GLY ALA LEU GLY PHE LEU ALA LEU
SEQRES 13 B 529 PRO GLY ASN PRO GLU ALA PRO GLY ASN MET GLY LEU PHE
SEQRES 14 B 529 ASP GLN GLN LEU ALA LEU GLN TRP VAL GLN LYS ASN ILE
SEQRES 15 B 529 ALA ALA PHE GLY GLY ASN PRO LYS SER VAL THR LEU PHE
SEQRES 16 B 529 GLY GLU SER ALA GLY ALA ALA SER VAL SER LEU HIS LEU
SEQRES 17 B 529 LEU SER PRO GLY SER HIS SER LEU PHE THR ARG ALA ILE
SEQRES 18 B 529 LEU GLN SER GLY SER PHE ASN ALA PRO TRP ALA VAL THR
SEQRES 19 B 529 SER LEU TYR GLU ALA ARG ASN ARG THR LEU ASN LEU ALA
SEQRES 20 B 529 LYS LEU THR GLY CYS SER ARG GLU ASN GLU THR GLU ILE
SEQRES 21 B 529 ILE LYS CYS LEU ARG ASN LYS ASP PRO GLN GLU ILE LEU
SEQRES 22 B 529 LEU ASN GLU ALA PHE VAL VAL PRO TYR GLY THR PRO LEU
SEQRES 23 B 529 SER VAL ASN PHE GLY PRO THR VAL ASP GLY ASP PHE LEU
SEQRES 24 B 529 THR ASP MET PRO ASP ILE LEU LEU GLU LEU GLY GLN PHE
SEQRES 25 B 529 LYS LYS THR GLN ILE LEU VAL GLY VAL ASN LYS ASP GLU
SEQRES 26 B 529 GLY THR ALA PHE LEU VAL TYR GLY ALA PRO GLY PHE SER
SEQRES 27 B 529 LYS ASP ASN ASN SER ILE ILE THR ARG LYS GLU PHE GLN
SEQRES 28 B 529 GLU GLY LEU LYS ILE PHE PHE PRO GLY VAL SER GLU PHE
SEQRES 29 B 529 GLY LYS GLU SER ILE LEU PHE HIS TYR THR ASP TRP VAL
SEQRES 30 B 529 ASP ASP GLN ARG PRO GLU ASN TYR ARG GLU ALA LEU GLY
SEQRES 31 B 529 ASP VAL VAL GLY ASP TYR ASN PHE ILE CYS PRO ALA LEU
SEQRES 32 B 529 GLU PHE THR LYS LYS PHE SER GLU TRP GLY ASN ASN ALA
SEQRES 33 B 529 PHE PHE TYR TYR PHE GLU HIS ARG SER SER LYS LEU PRO
SEQRES 34 B 529 TRP PRO GLU TRP MET GLY VAL MET HIS GLY TYR GLU ILE
SEQRES 35 B 529 GLU PHE VAL PHE GLY LEU PRO LEU GLU ARG ARG ASP ASN
SEQRES 36 B 529 TYR THR LYS ALA GLU GLU ILE LEU SER ARG SER ILE VAL
SEQRES 37 B 529 LYS ARG TRP ALA ASN PHE ALA LYS TYR GLY ASN PRO GLN
SEQRES 38 B 529 GLU THR GLN ASN ASN SER THR SER TRP PRO VAL PHE LYS
SEQRES 39 B 529 SER THR GLU GLN LYS TYR LEU THR LEU ASN THR GLU SER
SEQRES 40 B 529 THR ARG ILE MET THR LYS LEU ARG ALA GLN GLN CYS ARG
SEQRES 41 B 529 PHE TRP THR SER PHE PHE PRO LYS VAL
HET TCX A 600 6
HET TCX B 600 6
HET NAG A1531 14
HET NAG A1532 14
HET FUC A1533 10
HET NAG A1534 14
HET NAG A1535 14
HET FUC A1536 10
HET NAG A1537 14
HET NAG A1538 14
HET NAG A1539 14
HET NAG B1531 14
HET NAG B1532 14
HET FUC B1533 10
HET NAG B1534 14
HET NAG B1535 14
HET FUC B1536 10
HET NAG B1537 14
HET NAG B1538 14
HET NAG B1539 14
HET SO4 A1540 5
HET SO4 A1541 5
HET SO4 B1540 5
HET CL A1542 1
HETNAM SO4 SULFATE ION
HETNAM CL CHLORIDE ION
HETNAM TCX ETHYLPHOSPHORAMIDIC ACID
HETNAM FUC ALPHA-L-FUCOSE
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
FORMUL 3 SO4 3(O4 S 2-)
FORMUL 4 CL CL 1-
FORMUL 5 TCX 2(C2 H8 N1 O3 P1)
FORMUL 6 FUC 4(C6 H12 O5)
FORMUL 7 NAG 14(C8 H15 N O6)
FORMUL 8 HOH *137(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 SER A 210 SER A 215 1 6
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 MET A 302 LEU A 309 1 8
HELIX 14 14 GLY A 326 VAL A 331 1 6
HELIX 15 15 THR A 346 PHE A 358 1 13
HELIX 16 16 SER A 362 THR A 374 1 13
HELIX 17 17 GLU A 383 PHE A 398 1 16
HELIX 18 18 PHE A 398 GLU A 411 1 14
HELIX 19 19 PRO A 431 GLY A 435 5 5
HELIX 20 20 GLU A 441 PHE A 446 1 6
HELIX 21 21 GLY A 447 GLU A 451 5 5
HELIX 22 22 THR A 457 GLY A 478 1 22
HELIX 23 23 ARG A 515 SER A 524 1 10
HELIX 24 24 PHE A 525 VAL A 529 5 5
HELIX 25 25 LEU B 38 ARG B 42 5 5
HELIX 26 26 PHE B 76 MET B 81 1 6
HELIX 27 27 LEU B 125 ASP B 129 5 5
HELIX 28 28 GLY B 130 ARG B 138 1 9
HELIX 29 29 VAL B 148 LEU B 154 1 7
HELIX 30 30 ASN B 165 ILE B 182 1 18
HELIX 31 31 ALA B 183 PHE B 185 5 3
HELIX 32 32 SER B 198 SER B 210 1 13
HELIX 33 33 PRO B 211 PHE B 217 5 7
HELIX 34 34 SER B 235 THR B 250 1 16
HELIX 35 35 ASN B 256 ARG B 265 1 10
HELIX 36 36 ASP B 268 ALA B 277 1 10
HELIX 37 37 MET B 302 LEU B 309 1 8
HELIX 38 38 GLY B 326 VAL B 331 1 6
HELIX 39 39 THR B 346 PHE B 358 1 13
HELIX 40 40 SER B 362 THR B 374 1 13
HELIX 41 41 GLU B 383 PHE B 398 1 16
HELIX 42 42 PHE B 398 GLU B 411 1 14
HELIX 43 43 PRO B 431 GLY B 435 5 5
HELIX 44 44 GLU B 441 PHE B 446 1 6
HELIX 45 45 GLY B 447 GLU B 451 5 5
HELIX 46 46 THR B 457 GLY B 478 1 22
HELIX 47 47 ARG B 515 PHE B 525 1 11
HELIX 48 48 PHE B 526 VAL B 529 5 4
SHEET 1 AA 3 ILE A 5 THR A 8 0
SHEET 2 AA 3 GLY A 11 ARG A 14 -1 O GLY A 11 N THR A 8
SHEET 3 AA 3 ILE A 55 ASN A 57 1 O TRP A 56 N ARG A 14
SHEET 1 AB11 GLN A 17 THR A 19 0
SHEET 2 AB11 THR A 24 PRO A 32 -1 O VAL A 25 N LEU A 18
SHEET 3 AB11 TYR A 94 PRO A 100 -1 O LEU A 95 N ILE A 31
SHEET 4 AB11 ILE A 140 MET A 144 -1 O VAL A 141 N TRP A 98
SHEET 5 AB11 ALA A 107 ILE A 113 1 O THR A 108 N ILE A 140
SHEET 6 AB11 GLY A 187 GLU A 197 1 N ASN A 188 O ALA A 107
SHEET 7 AB11 ARG A 219 GLN A 223 1 O ARG A 219 N LEU A 194
SHEET 8 AB11 ILE A 317 ASN A 322 1 O LEU A 318 N LEU A 222
SHEET 9 AB11 ALA A 416 PHE A 421 1 O PHE A 417 N VAL A 319
SHEET 10 AB11 LYS A 499 LEU A 503 1 O LEU A 501 N TYR A 420
SHEET 11 AB11 ILE A 510 THR A 512 -1 O MET A 511 N TYR A 500
SHEET 1 BA 3 ILE B 5 THR B 8 0
SHEET 2 BA 3 GLY B 11 ARG B 14 -1 O GLY B 11 N THR B 8
SHEET 3 BA 3 ILE B 55 ASN B 57 1 O TRP B 56 N ARG B 14
SHEET 1 BB11 GLN B 17 THR B 19 0
SHEET 2 BB11 THR B 24 PRO B 32 -1 O VAL B 25 N LEU B 18
SHEET 3 BB11 TYR B 94 ALA B 101 -1 O LEU B 95 N ILE B 31
SHEET 4 BB11 ILE B 140 MET B 144 -1 O VAL B 141 N TRP B 98
SHEET 5 BB11 ALA B 107 ILE B 113 1 O THR B 108 N ILE B 140
SHEET 6 BB11 GLY B 187 GLU B 197 1 N ASN B 188 O ALA B 107
SHEET 7 BB11 ARG B 219 GLN B 223 1 O ARG B 219 N LEU B 194
SHEET 8 BB11 ILE B 317 ASN B 322 1 O LEU B 318 N LEU B 222
SHEET 9 BB11 ALA B 416 PHE B 421 1 O PHE B 417 N VAL B 319
SHEET 10 BB11 LYS B 499 LEU B 503 1 O LEU B 501 N TYR B 420
SHEET 11 BB11 ILE B 510 THR B 512 -1 O MET B 511 N TYR B 500
SSBOND 1 CYS A 65 CYS A 92 1555 1555 2.02
SSBOND 2 CYS A 252 CYS A 263 1555 1555 2.04
SSBOND 3 CYS A 400 CYS A 519 1555 1555 2.05
SSBOND 4 CYS B 65 CYS B 92 1555 1555 2.05
SSBOND 5 CYS B 252 CYS B 263 1555 1555 2.04
SSBOND 6 CYS B 400 CYS B 519 1555 1555 2.06
LINK ND2 ASN A 57 C1 NAG A1538 1555 1555 1.48
LINK ND2 ASN A 106 C1 NAG A1537 1555 1555 1.46
LINK OG SER A 198 P TCX A 600 1555 1555 1.61
LINK ND2 ASN A 241 C1 NAG A1531 1555 1555 1.46
LINK ND2 ASN A 341 C1 NAG A1534 1555 1555 1.44
LINK ND2 ASN A 485 C1 NAG A1539 1555 1555 1.45
LINK O6 NAG A1531 C1 FUC A1533 1555 1555 1.46
LINK O4 NAG A1531 C1 NAG A1532 1555 1555 1.46
LINK O6 NAG A1534 C1 FUC A1536 1555 1555 1.45
LINK O4 NAG A1534 C1 NAG A1535 1555 1555 1.45
LINK ND2 ASN B 57 C1 NAG B1538 1555 1555 1.47
LINK ND2 ASN B 106 C1 NAG B1537 1555 1555 1.45
LINK OG SER B 198 P TCX B 600 1555 1555 1.61
LINK ND2 ASN B 241 C1 NAG B1531 1555 1555 1.46
LINK ND2 ASN B 341 C1 NAG B1534 1555 1555 1.46
LINK ND2 ASN B 485 C1 NAG B1539 1555 1555 1.45
LINK O4 NAG B1531 C1 NAG B1532 1555 1555 1.46
LINK O6 NAG B1531 C1 FUC B1533 1555 1555 1.45
LINK O4 NAG B1534 C1 NAG B1535 1555 1555 1.45
LINK O6 NAG B1534 C1 FUC B1536 1555 1555 1.44
CISPEP 1 ASP A 2 ASP A 3 0 11.34
CISPEP 2 ALA A 101 PRO A 102 0 9.15
CISPEP 3 ALA B 101 PRO B 102 0 9.03
SITE 1 AC1 7 GLY A 116 GLY A 117 SER A 198 ALA A 199
SITE 2 AC1 7 TRP A 231 LEU A 286 HIS A 438
SITE 1 AC2 8 GLY B 116 GLY B 117 SER B 198 ALA B 199
SITE 2 AC2 8 TRP B 231 LEU B 286 PHE B 398 HIS B 438
SITE 1 AC3 5 TYR A 237 ASN A 241 ASN A 245 NAG A1532
SITE 2 AC3 5 FUC A1533
SITE 1 AC4 3 NAG A1531 FUC A1533 HOH A2061
SITE 1 AC5 3 PHE A 278 NAG A1531 NAG A1532
SITE 1 AC6 5 SER A 338 ASN A 341 NAG A1535 FUC A1536
SITE 2 AC6 5 HOH A2062
SITE 1 AC7 3 NAG A1534 HOH A2062 HOH A2063
SITE 1 AC8 2 NAG A1534 HOH A2035
SITE 1 AC9 3 ASN A 106 ASN A 188 HOH A2064
SITE 1 BC1 3 ARG A 14 ASN A 57 HOH A2065
SITE 1 BC2 3 ARG A 465 GLU A 482 ASN A 485
SITE 1 BC3 6 TYR B 237 ASN B 241 ASN B 245 NAG B1532
SITE 2 BC3 6 FUC B1533 HOH B2070
SITE 1 BC4 2 NAG B1531 FUC B1533
SITE 1 BC5 4 ASN B 245 PHE B 278 NAG B1531 NAG B1532
SITE 1 BC6 4 SER B 338 ASN B 341 NAG B1535 FUC B1536
SITE 1 BC7 1 NAG B1534
SITE 1 BC8 1 NAG B1534
SITE 1 BC9 3 ASN B 106 ASN B 188 HOH B2071
SITE 1 CC1 2 ARG B 14 ASN B 57
SITE 1 CC2 4 ARG B 465 GLU B 482 ASN B 485 HOH B2072
SITE 1 CC3 3 GLN A 316 ASN A 414 ASN A 415
SITE 1 CC4 4 LEU A 514 ARG A 515 GLN A 518 ARG B 509
SITE 1 CC5 3 GLN B 316 ASN B 414 ASN B 415
SITE 1 CC6 1 TYR A 420
CRYST1 150.350 150.350 139.430 90.00 90.00 90.00 P 4 21 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 0.006651 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006651 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007172 0.00000
TER 4206 VAL A 529
TER 8399 VAL B 529
MASTER 603 0 24 48 28 0 29 6 8798 2 287 82
END |