| content |
HEADER HYDROLASE 28-JUN-10 2XI4
TITLE TORPEDO CALIFORNICA ACETYLCHOLINESTERASE IN COMPLEX WITH AFLATOXIN
TITLE 2 B1 (ORTHORHOMBIC SPACE GROUP)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYLCHOLINESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RESIDUES 22-558;
COMPND 5 SYNONYM: ACHE;
COMPND 6 EC: 3.1.1.7
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: TORPEDO CALIFORNICA;
SOURCE 3 ORGANISM_COMMON: PACIFIC ELECTRIC RAY;
SOURCE 4 ORGANISM_TAXID: 7787;
SOURCE 5 VARIANT: G2 FORM;
SOURCE 6 ORGAN: ELECTRIC ORGAN;
SOURCE 7 TISSUE: ELECTROPLAQUE
KEYWDS ACETYLCHOLINESTERASE BACKDOOR, MYCOTOXIN, ALZHEIMER DISEASE, CELL
KEYWDS 2 JUNCTION, GPI-ANCHOR, HYDROLASE, NEUROTRANSMITTER CLEAVAGE,
KEYWDS 3 NEUROTRANSMITTER DEGRADATION, SERINE ESTERASE, SYNAPSE
EXPDTA X-RAY DIFFRACTION
AUTHOR B.SANSON,J.P.COLLETIER,Y.XU,P.T.LANG,H.JIANG,I.SILMAN,J.L.SUSSMAN,
AUTHOR 2 M.WEIK
REVDAT 1 23-MAR-11 2XI4 0
JRNL AUTH B.SANSON,J.P.COLLETIER,I.SILMAN,J.L.SUSSMAN,M.WEIK
JRNL TITL OPEN BACKDOOR IN THE STRUCTURE OF ACETYLCHOLINESTERASE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
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) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.22
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.00
REMARK 3 NUMBER OF REFLECTIONS : 62177
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) : 0.18244
REMARK 3 R VALUE (WORKING SET) : 0.17988
REMARK 3 FREE R VALUE : 0.23366
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.8
REMARK 3 FREE R VALUE TEST SET COUNT : 3156
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) : 2.300
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.360
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4612
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.00
REMARK 3 BIN R VALUE (WORKING SET) : 0.207
REMARK 3 BIN FREE R VALUE SET COUNT : 242
REMARK 3 BIN FREE R VALUE : 0.291
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8569
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 183
REMARK 3 SOLVENT ATOMS : 744
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 38.486
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 37.284
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.42
REMARK 3 B22 (A**2) : 3.85
REMARK 3 B33 (A**2) : -2.43
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): 0.264
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.214
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.148
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.367
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.959
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.932
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 9024 ; 0.014 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 12273 ; 1.491 ; 1.966
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1103 ; 6.435 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 429 ;33.086 ;24.009
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1443 ;15.569 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 51 ;17.754 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1285 ; 0.104 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6997 ; 0.007 ; 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): 5349 ; 0.664 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 8668 ; 1.225 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3675 ; 2.199 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3583 ; 3.439 ; 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 : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 4 A 316
REMARK 3 ORIGIN FOR THE GROUP (A): 83.7940 57.3740 13.2100
REMARK 3 T TENSOR
REMARK 3 T11: 0.0489 T22: 0.0258
REMARK 3 T33: 0.0665 T12: 0.0048
REMARK 3 T13: -0.0043 T23: 0.0357
REMARK 3 L TENSOR
REMARK 3 L11: 1.9739 L22: 1.4855
REMARK 3 L33: 1.9991 L12: 0.2953
REMARK 3 L13: 0.4956 L23: -0.1421
REMARK 3 S TENSOR
REMARK 3 S11: -0.0206 S12: 0.1528 S13: 0.1164
REMARK 3 S21: -0.1773 S22: 0.0360 S23: 0.0757
REMARK 3 S31: -0.0572 S32: -0.0269 S33: -0.0153
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 317 A 535
REMARK 3 ORIGIN FOR THE GROUP (A): 88.3410 44.3470 33.2010
REMARK 3 T TENSOR
REMARK 3 T11: 0.1113 T22: 0.0432
REMARK 3 T33: 0.1008 T12: 0.0166
REMARK 3 T13: 0.0137 T23: 0.0547
REMARK 3 L TENSOR
REMARK 3 L11: 1.6826 L22: 0.6666
REMARK 3 L33: 3.0309 L12: 0.0326
REMARK 3 L13: 0.8779 L23: 0.1108
REMARK 3 S TENSOR
REMARK 3 S11: 0.0633 S12: -0.1823 S13: -0.2298
REMARK 3 S21: 0.0261 S22: 0.0331 S23: 0.0158
REMARK 3 S31: 0.2926 S32: 0.0734 S33: -0.0965
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 4 B 327
REMARK 3 ORIGIN FOR THE GROUP (A): 99.7260 55.6500 89.8060
REMARK 3 T TENSOR
REMARK 3 T11: 0.0569 T22: 0.0582
REMARK 3 T33: 0.0612 T12: -0.0160
REMARK 3 T13: 0.0014 T23: -0.0391
REMARK 3 L TENSOR
REMARK 3 L11: 2.0271 L22: 1.2911
REMARK 3 L33: 1.7975 L12: -0.2701
REMARK 3 L13: 0.2260 L23: 0.1285
REMARK 3 S TENSOR
REMARK 3 S11: -0.0075 S12: -0.2883 S13: 0.1571
REMARK 3 S21: 0.1464 S22: 0.0560 S23: -0.0054
REMARK 3 S31: -0.0933 S32: -0.0053 S33: -0.0485
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 328 B 535
REMARK 3 ORIGIN FOR THE GROUP (A): 95.1610 43.2220 70.0340
REMARK 3 T TENSOR
REMARK 3 T11: 0.0943 T22: 0.0338
REMARK 3 T33: 0.0843 T12: -0.0196
REMARK 3 T13: 0.0008 T23: -0.0417
REMARK 3 L TENSOR
REMARK 3 L11: 1.9842 L22: 0.7380
REMARK 3 L33: 2.2853 L12: -0.1239
REMARK 3 L13: 0.7727 L23: -0.1942
REMARK 3 S TENSOR
REMARK 3 S11: 0.0588 S12: 0.1099 S13: -0.2271
REMARK 3 S21: -0.0253 S22: 0.0517 S23: 0.0253
REMARK 3 S31: 0.1487 S32: -0.0704 S33: -0.1105
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 : 1.40
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 2XI4 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 28-JUN-10.
REMARK 100 THE PDBE ID CODE IS EBI-44354.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-SEP-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.8
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
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 65334
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.30
REMARK 200 RESOLUTION RANGE LOW (A) : 46.22
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 200 DATA REDUNDANCY : 6.05
REMARK 200 R MERGE (I) : 0.06
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 23.07
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.35
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.94
REMARK 200 R MERGE FOR SHELL (I) : 0.42
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 4.57
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: REFMAC5
REMARK 200 STARTING MODEL: PDB ENTRY 1W75
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.2
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.1
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: ACHE WAS CRYSTALLIZED IN 34%
REMARK 280 PEG200, 150 MM MES, PH 6, 4 DEG. C. THE CRYSTAL WAS SOAKED
REMARK 280 FOR 15 H IN 100 MICROMOLAR AFLATOXIN B1, 10% ETOH, 36% PEG200,
REMARK 280 150MM MES, PH 5.8, 4 DEG C.
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+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 45.86500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 75.36500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 53.51500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 75.36500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 45.86500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 53.51500
REMARK 290 SMTRY3 4 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 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5660 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 39340 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 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 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 ASP A 1
REMARK 465 ASP A 2
REMARK 465 HIS A 3
REMARK 465 GLN A 488
REMARK 465 GLU A 489
REMARK 465 ALA A 536
REMARK 465 CYS A 537
REMARK 465 ASP B 1
REMARK 465 ASP B 2
REMARK 465 HIS B 3
REMARK 465 ALA B 536
REMARK 465 CYS B 537
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 413 CD CE NZ
REMARK 470 LYS A 454 CE NZ
REMARK 470 HIS A 486 ND1 CD2 CE1 NE2
REMARK 470 LYS A 511 CE NZ
REMARK 470 ARG B 46 NE CZ NH1 NH2
REMARK 470 LYS B 413 CD CE NZ
REMARK 470 LYS B 454 CE NZ
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 221 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ARG B 221 NE - CZ - NH2 ANGL. DEV. = -4.3 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 LEU A 23 60.97 32.42
REMARK 500 SER A 25 -169.21 -161.04
REMARK 500 PHE A 45 -13.59 79.87
REMARK 500 SER A 108 74.24 -154.67
REMARK 500 SER A 200 -116.81 61.64
REMARK 500 GLU A 299 -72.19 -131.47
REMARK 500 ASP A 380 51.10 -157.60
REMARK 500 VAL A 400 -59.58 -125.69
REMARK 500 ALA A 427 147.48 -39.34
REMARK 500 ASN A 429 90.55 -68.87
REMARK 500 HIS A 440 122.15 -23.08
REMARK 500 HIS A 486 151.56 94.63
REMARK 500 ARG A 515 68.98 60.17
REMARK 500 GLN A 526 -55.53 -120.80
REMARK 500 LEU B 23 52.51 36.47
REMARK 500 PHE B 45 -13.22 83.57
REMARK 500 SER B 108 68.93 -152.09
REMARK 500 SER B 200 -117.78 58.44
REMARK 500 GLU B 299 -71.07 -123.17
REMARK 500 THR B 317 -159.52 -158.47
REMARK 500 ASP B 380 47.50 -148.06
REMARK 500 VAL B 400 -57.43 -130.15
REMARK 500 HIS B 486 -10.44 70.91
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K A1010 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 508 OE1
REMARK 620 2 GLU B 508 OE2 56.9
REMARK 620 3 GLU A 163 OE1 70.6 113.0
REMARK 620 4 GLU A 260 OE1 132.0 166.0 81.0
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A1010
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AFT A1000
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AFT B1000
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B1003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGE B1004
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A1003
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A1004
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B1005
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A1005
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGE A1006
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B1006
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1007
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1008
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B1008
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B1009
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1009
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1ZGB RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF TORPEDO CALIFORNICAACETYLCHOLINESTERASE
REMARK 900 IN COMPLEX WITH AN (R)-TACRINE(10)-HUPYRIDONE
REMARK 900 INHIBITOR.
REMARK 900 RELATED ID: 1AMN RELATED DB: PDB
REMARK 900 TRANSITION STATE ANALOG: ACETYLCHOLINESTERASE COMPLEXED WITH
REMARK 900 M-(N,N,N-TRIMETHYLAMMONIO)TRIFLUOROACETOPHENONE
REMARK 900 RELATED ID: 1QTI RELATED DB: PDB
REMARK 900 ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 1E66 RELATED DB: PDB
REMARK 900 STRUCTURE OF ACETYLCHOLINESTERASE COMPLEXED WITH (-)-HUPRINE
REMARK 900 X AT 2.1A RESOLUTION
REMARK 900 RELATED ID: 2J3D RELATED DB: PDB
REMARK 900 NATIVE MONOCLINIC FORM OF TORPEDO ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 2VQ6 RELATED DB: PDB
REMARK 900 TORPEDO CALIFORNICA ACETYLCHOLINESTERASE COMPLEXED WITH 2-
REMARK 900 PAM
REMARK 900 RELATED ID: 2ACK RELATED DB: PDB
REMARK 900 ACETYLCHOLINESTERASE COMPLEXED WITH EDROPHONIUM, MONOCHROMATIC
REMARK 900 DATA
REMARK 900 RELATED ID: 1QII RELATED DB: PDB
REMARK 900 SPECIFIC CHEMICAL AND STRUCTURAL DAMAGE AT NINE TIME
REMARK 900 POINTS (POINT F) CAUSED BY INTENSE SYNCHROTRON RADIATION
REMARK 900 TO TORPEDO CALIFORNICA ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 2CKM RELATED DB: PDB
REMARK 900 TORPEDO CALIFORNICA ACETYLCHOLINESTERASE COMPLEXED WITH
REMARK 900 ALKYLENE-LINKED BIS-TACRINE DIMER (7 CARBON LINKER)
REMARK 900 RELATED ID: 1DX6 RELATED DB: PDB
REMARK 900 STRUCTURE OF ACETYLCHOLINESTERASE COMPLEXED WITH (-)-
REMARK 900 GALANTHAMINE AT 2.3A RESOLUTION
REMARK 900 RELATED ID: 1QIE RELATED DB: PDB
REMARK 900 SPECIFIC CHEMICAL AND STRUCTURAL DAMAGE AT NINE TIME
REMARK 900 POINTS (POINT B) CAUSED BY INTENSE SYNCHROTRON RADIATION
REMARK 900 TO TORPEDO CALIFORNICA ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 1QIJ RELATED DB: PDB
REMARK 900 SPECIFIC CHEMICAL AND STRUCTURAL DAMAGE AT NINE TIME
REMARK 900 POINTS (POINT G) CAUSED BY INTENSE SYNCHROTRON RADIATION
REMARK 900 TO TORPEDO CALIFORNICA ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 1ACL RELATED DB: PDB
REMARK 900 ACETYLCHOLINESTERASE COMPLEXED WITH DECAMETHONIUM
REMARK 900 RELATED ID: 1W4L RELATED DB: PDB
REMARK 900 COMPLEX OF TCACHE WITH BIS-ACTING GALANTHAMINE
REMARK 900 DERIVATIVE
REMARK 900 RELATED ID: 1ODC RELATED DB: PDB
REMARK 900 STRUCTURE OF ACETYLCHOLINESTERASE (E.C. 3.1.1.7)
REMARK 900 COMPLEXED WITH N-4'-QUINOLYL-N'-9"-(1",2",3",4"-
REMARK 900 TETRAHYDROACRIDINYL)-1,8- DIAMINOOCTANE AT 2.2A
REMARK 900 RESOLUTION
REMARK 900 RELATED ID: 2CMF RELATED DB: PDB
REMARK 900 TORPEDO CALIFORNICA ACETYLCHOLINESTERASE COMPLEXED WITH
REMARK 900 ALKYLENE-LINKED BIS-TACRINE DIMER (5 CARBON LINKER)
REMARK 900 RELATED ID: 2WG0 RELATED DB: PDB
REMARK 900 AGED CONJUGATE OF TORPEDO CALIFORNICA ACETYLCHOLINESTERASE
REMARK 900 WITH SOMAN (OBTAINED BY IN CRYSTALLO AGING)
REMARK 900 RELATED ID: 1GQS RELATED DB: PDB
REMARK 900 ACETYLCHOLINESTERASE (E.C. 3.1.1.7) COMPLEXED WITH
REMARK 900 NAP
REMARK 900 RELATED ID: 2J3Q RELATED DB: PDB
REMARK 900 TORPEDO ACETYLCHOLINESTERASE COMPLEXED WITH FLUOROPHORE
REMARK 900 THIOFLAVIN T
REMARK 900 RELATED ID: 1E3Q RELATED DB: PDB
REMARK 900 TORPEDO CALIFORNICA ACETYLCHOLINESTERASE COMPLEXED WITH
REMARK 900 BW284C51
REMARK 900 RELATED ID: 2J4F RELATED DB: PDB
REMARK 900 TORPEDO ACETYLCHOLINESTERASE - HG HEAVY-ATOM DERIVATIVE
REMARK 900 RELATED ID: 1QIK RELATED DB: PDB
REMARK 900 SPECIFIC CHEMICAL AND STRUCTURAL DAMAGE AT NINE TIME
REMARK 900 POINTS (POINT H) CAUSED BY INTENSE SYNCHROTRON RADIATION
REMARK 900 TO TORPEDO CALIFORNICA ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 2DFP RELATED DB: PDB
REMARK 900 X-RAY STRUCTURE OF AGED DI-ISOPROPYL-PHOSPHORO-
REMARK 900 FLUORIDATE (DFP) BOUND TO ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 2C5F RELATED DB: PDB
REMARK 900 TORPEDO CALIFORNICA ACETYLCHOLINESTERASE IN COMPLEX WITH A
REMARK 900 NON HYDROLYSABLE SUBSTRATE ANALOGUE, 4-OXO-N,N,N-
REMARK 900 TRIMETHYLAMMONIUM
REMARK 900 RELATED ID: 1EA5 RELATED DB: PDB
REMARK 900 NATIVE ACETYLCHOLINESTERASE (E.C. 3.1.1.7) FROM
REMARK 900 TORPEDO CALIFORNICA AT 1.8A RESOLUTION
REMARK 900 RELATED ID: 1EEA RELATED DB: PDB
REMARK 900 ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 2VJC RELATED DB: PDB
REMARK 900 TORPEDO CALIFORNICA ACETYLCHOLINESTERASE IN COMPLEX WITH A
REMARK 900 NON HYDROLYSABLE SUBSTRATE ANALOGUE, 4-OXO-N,N,N-
REMARK 900 TRIMETHYLPENTANAMINIUM - ORTHORHOMBIC SPACE GROUP - DATASET
REMARK 900 A AT 150K
REMARK 900 RELATED ID: 1QIF RELATED DB: PDB
REMARK 900 SPECIFIC CHEMICAL AND STRUCTURAL DAMAGE AT NINE TIME
REMARK 900 POINTS (POINT C) CAUSED BY INTENSE SYNCHROTRON RADIATION
REMARK 900 TO TORPEDO CALIFORNICA ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 2VJB RELATED DB: PDB
REMARK 900 TORPEDO CALIFORNICA ACETYLCHOLINESTERASE IN COMPLEX WITH A
REMARK 900 NON HYDROLYSABLE SUBSTRATE ANALOGUE, 4-OXO-N,N,N-
REMARK 900 TRIMETHYLPENTANAMINIUM - ORTHORHOMBIC SPACE GROUP - DATASET
REMARK 900 D AT 100K
REMARK 900 RELATED ID: 1QIG RELATED DB: PDB
REMARK 900 SPECIFIC CHEMICAL AND STRUCTURAL DAMAGE AT NINE TIME
REMARK 900 POINTS (POINT D) CAUSED BY INTENSE SYNCHROTRON RADIATION
REMARK 900 TO TORPEDO CALIFORNICA ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 1ZGC RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF TORPEDO CALIFORNICAACETYLCHOLINESTERASE
REMARK 900 IN COMPLEX WITH AN (RS)-TACRINE(10)-HUPYRIDONE
REMARK 900 INHIBITOR.
REMARK 900 RELATED ID: 1QID RELATED DB: PDB
REMARK 900 SPECIFIC CHEMICAL AND STRUCTURAL DAMAGE AT NINE TIME
REMARK 900 POINTS (POINT A) CAUSED BY INTENSE SYNCHROTRON RADIATION
REMARK 900 TO TORPEDO CALIFORNICA ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 2WFZ RELATED DB: PDB
REMARK 900 NON-AGED CONJUGATE OF TORPEDO CALIFORNICA
REMARK 900 ACETYLCHOLINESTERASE WITH SOMAN
REMARK 900 RELATED ID: 1JJB RELATED DB: PDB
REMARK 900 A NEUTRAL MOLECULE IN CATION-BINDING SITE: SPECIFIC
REMARK 900 BINDINGOF PEG-SH TO ACETYLCHOLINESTERASE FROM TORPEDO
REMARK 900 CALIFORNICA
REMARK 900 RELATED ID: 2VJD RELATED DB: PDB
REMARK 900 TORPEDO CALIFORNICA ACETYLCHOLINESTERASE IN COMPLEX WITH A
REMARK 900 NON HYDROLYSABLE SUBSTRATE ANALOGUE, 4-OXO-N,N,N-
REMARK 900 TRIMETHYLPENTANAMINIUM - ORTHORHOMBIC SPACE GROUP - DATASET
REMARK 900 C AT 150K
REMARK 900 RELATED ID: 1UT6 RELATED DB: PDB
REMARK 900 STRUCTURE OF ACETYLCHOLINESTERASE (E.C. 3.1.1.7)
REMARK 900 COMPLEXED WITH N-9-(1',2',3',4'-TETRAHYDROACRIDINYL)-
REMARK 900 1,8- DIAMINOOCTANE AT 2.4 ANGSTROMS RESOLUTION.
REMARK 900 RELATED ID: 2WG1 RELATED DB: PDB
REMARK 900 TERNARY COMPLEX OF THE AGED CONJUGATE OF TORPEDO
REMARK 900 CALIFORNICA ACEYLCHOLINESTERASE WITH SOMAN AND 2-PAM
REMARK 900 RELATED ID: 2VT6 RELATED DB: PDB
REMARK 900 NATIVE TORPEDO CALIFORNICA ACETYLCHOLINESTERASE COLLECTED
REMARK 900 WITH A CUMULATED DOSE OF 9400000 GY
REMARK 900 RELATED ID: 2W9I RELATED DB: PDB
REMARK 900 ACHE IN COMPLEX WITH METHYLENE BLUE
REMARK 900 RELATED ID: 2WG2 RELATED DB: PDB
REMARK 900 NON-AGED CONJUGATE OF TORPEDO CALIFORNICA
REMARK 900 ACETYLCHOLINESTERASE WITH SOMAN (ALTERNATIVE REFINEMENT)
REMARK 900 RELATED ID: 2VT7 RELATED DB: PDB
REMARK 900 NATIVE TORPEDO CALIFORNICA ACETYLCHOLINESTERASE COLLECTED
REMARK 900 WITH A CUMULATED DOSE OF 800000 GY
REMARK 900 RELATED ID: 2CEK RELATED DB: PDB
REMARK 900 CONFORMATIONAL FLEXIBILITY IN THE PERIPHERAL SITE OF
REMARK 900 TORPEDO CALIFORNICA ACETYLCHOLINESTERASE REVEALED BY THE
REMARK 900 COMPLEX STRUCTURE WITH A BIFUNCTIONAL INHIBITOR
REMARK 900 RELATED ID: 1QIM RELATED DB: PDB
REMARK 900 SPECIFIC CHEMICAL AND STRUCTURAL DAMAGE AT NINE TIME
REMARK 900 POINTS (POINT I) CAUSED BY INTENSE SYNCHROTRON RADIATION
REMARK 900 TO TORPEDO CALIFORNICA ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 1GPK RELATED DB: PDB
REMARK 900 STRUCTURE OF ACETYLCHOLINESTERASE COMPLEXE WITH (+)-
REMARK 900 HUPERZINE A AT 2.1A RESOLUTION
REMARK 900 RELATED ID: 1JGA RELATED DB: PDB
REMARK 900 THEORETICAL MODEL OF THE DIISOPROPYLPHOSPHORYL-
REMARK 900 ACETYLCHOLINESTERASE COMPLEXED WITH 1,7-HEPTYLENE-BIS-N
REMARK 900 ,N'-SYN-2-PYRIDINIUMALDOXIME
REMARK 900 RELATED ID: 3ACE RELATED DB: PDB
REMARK 900 THEORETICAL MODEL OF (R)-E2020 BOUND ACETYLCHOLINESTERASE
REMARK 900 COMPLEX, 3 STRUCTURES
REMARK 900 RELATED ID: 1OCE RELATED DB: PDB
REMARK 900 ACETYLCHOLINESTERASE COMPLEXED WITH MF268
REMARK 900 RELATED ID: 1W6R RELATED DB: PDB
REMARK 900 COMPLEX OF TCACHE WITH GALANTHAMINE DERIVATIVE
REMARK 900 RELATED ID: 1SOM RELATED DB: PDB
REMARK 900 TORPEDO CALIFORNICA ACETYLCHOLINESTERASE INHIBITED BY NERVE
REMARK 900 AGENT GD (SOMAN).
REMARK 900 RELATED ID: 1VXO RELATED DB: PDB
REMARK 900 METHYLPHOSPHONYLATED ACETYLCHOLINESTERASE (AGED) OBTAINED BY
REMARK 900 REACTION WITH O-ETHYL-S-[2-[BIS(1-METHYLETHYL) AMINO
REMARK 900 ]ETHYL] METHYLPHOSPHONOTHIOATE (VX)
REMARK 900 RELATED ID: 2W6C RELATED DB: PDB
REMARK 900 ACHE IN COMPLEX WITH A BIS-(-)-NOR-MEPTAZINOL
REMARK 900 DERIVATIVE
REMARK 900 RELATED ID: 2VJA RELATED DB: PDB
REMARK 900 TORPEDO CALIFORNICA ACETYLCHOLINESTERASE IN COMPLEX WITH A
REMARK 900 NON HYDROLYSABLE SUBSTRATE ANALOGUE, 4-OXO-N,N,N-
REMARK 900 TRIMETHYLPENTANAMINIUM - ORTHORHOMBIC SPACE GROUP - DATASET
REMARK 900 A AT 100K
REMARK 900 RELATED ID: 1CFJ RELATED DB: PDB
REMARK 900 METHYLPHOSPHONYLATED ACETYLCHOLINESTERASE (AGED) OBTAINED BY
REMARK 900 REACTION WITH O-ISOPROPYLMETHYLPHOSPHONOFLUORIDATE (GB,
REMARK 900 SARIN)
REMARK 900 RELATED ID: 2V96 RELATED DB: PDB
REMARK 900 STRUCTURE OF THE UNPHOTOLYSED COMPLEX OF TCACHE WITH 1
REMARK 900 -(2-NITROPHENYL)-2,2,2-TRIFLUOROETHYL-ARSENOCHOLINE AT
REMARK 900 100K
REMARK 900 RELATED ID: 1U65 RELATED DB: PDB
REMARK 900 ACHE W. CPT-11
REMARK 900 RELATED ID: 1AX9 RELATED DB: PDB
REMARK 900 ACETYLCHOLINESTERASE COMPLEXED WITH EDROPHONIUM, LAUE DATA
REMARK 900 RELATED ID: 1W76 RELATED DB: PDB
REMARK 900 ORTHORHOMBIC FORM OF TORPEDO CALIFORNICA
REMARK 900 ACETYLCHOLINESTERASE (ACHE) COMPLEXED WITH BIS-ACTING
REMARK 900 GALANTHAMINE DERIVATIVE
REMARK 900 RELATED ID: 1H22 RELATED DB: PDB
REMARK 900 STRUCTURE OF ACETYLCHOLINESTERASE (E.C. 3.1.1.7)
REMARK 900 COMPLEXED WITH (S,S)-(-)-BIS(10)-HUPERZINE A-LIKE
REMARK 900 INHIBITOR AT 2.15A RESOLUTION
REMARK 900 RELATED ID: 1EVE RELATED DB: PDB
REMARK 900 THREE DIMENSIONAL STRUCTURE OF THE ANTI-ALZHEIMER DRUG
REMARK 900 , E2020 (ARICEPT), COMPLEXED WITH ITS TARGET
REMARK 900 ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 2C4H RELATED DB: PDB
REMARK 900 TORPEDO CALIFORNICA ACETYLCHOLINESTERASE IN COMPLEX WITH
REMARK 900 500MM ACETYLTHIOCHOLINE
REMARK 900 RELATED ID: 1GQR RELATED DB: PDB
REMARK 900 ACETYLCHOLINESTERASE (E.C. 3.1.1.7) COMPLEXED WITH
REMARK 900 RIVASTIGMINE
REMARK 900 RELATED ID: 2VA9 RELATED DB: PDB
REMARK 900 STRUCTURE OF NATIVE TCACHE AFTER A 9 SECONDS ANNEALING
REMARK 900 TO ROOM TEMPERATURE DURING THE FIRST 5 SECONDS OF
REMARK 900 WHICH LASER IRRADIATION AT 266NM TOOK PLACE
REMARK 900 RELATED ID: 2ACE RELATED DB: PDB
REMARK 900 NATIVE ACETYLCHOLINESTERASE FROM TORPEDO CALIFORNICA
REMARK 900 RELATED ID: 1VXR RELATED DB: PDB
REMARK 900 O-ETHYLMETHYLPHOSPHONYLATED ACETYLCHOLINESTERASE OBTAINED BY
REMARK 900 REACTION WITH O-ETHYL-S-[2-[BIS(1-METHYLETHYL) AMINO
REMARK 900 ]ETHYL] METHYLPHOSPHONOTHIOATE (VX)
REMARK 900 RELATED ID: 4ACE RELATED DB: PDB
REMARK 900 THEORETICAL MODEL OF (S)-E2020 BOUND ACETYLCHOLINESTERASE
REMARK 900 COMPLEX, 3 STRUCTURES
REMARK 900 RELATED ID: 2C58 RELATED DB: PDB
REMARK 900 TORPEDO CALIFORNICA ACETYLCHOLINESTERASE IN COMPLEX WITH
REMARK 900 20MM ACETYLTHIOCHOLINE
REMARK 900 RELATED ID: 1HBJ RELATED DB: PDB
REMARK 900 X-RAY CRYSTAL STRUCTURE OF COMPLEX BETWEEN TORPEDO
REMARK 900 CALIFORNICA ACHE AND A REVERSIBLE INHIBITOR, 4-AMINO-5
REMARK 900 -FLUORO-2-METHYL-3-(3-TRIFLUOROACETYLBENZYLTHIOMETHYL)
REMARK 900 QUINOLINE
REMARK 900 RELATED ID: 1VOT RELATED DB: PDB
REMARK 900 ACETYLCHOLINESTERASE COMPLEXED WITH HUPERZINE A
REMARK 900 RELATED ID: 1W75 RELATED DB: PDB
REMARK 900 NATIVE ORTHORHOMBIC FORM OF TORPEDO CALIFORNICA
REMARK 900 ACETYLCHOLINESTERASE (ACHE)
REMARK 900 RELATED ID: 2C5G RELATED DB: PDB
REMARK 900 TORPEDO CALIFORNICA ACETYLCHOLINESTERASE IN COMPLEX WITH
REMARK 900 20MM THIOCHOLINE
REMARK 900 RELATED ID: 1JGB RELATED DB: PDB
REMARK 900 THEORETICAL MODEL OF THE DIISOPROPYLPHOSPHORYL-
REMARK 900 ACETYLCHOLINESTERASE COMPLEXED WITH 1,3-PROPYLENE-BIS-N
REMARK 900 ,N'-SYN-4-PYRIDINIUMALDOXIME
REMARK 900 RELATED ID: 2V98 RELATED DB: PDB
REMARK 900 STRUCTURE OF THE COMPLEX OF TCACHE WITH 1-(2-
REMARK 900 NITROPHENYL)-2,2,2-TRIFLUOROETHYL-ARSENOCHOLINE AFTER A
REMARK 900 9 SECONDS ANNEALING TO ROOM TEMPERATURE, DURING HTE
REMARK 900 FIRST 5 SECONDS OF WHICH LASER IRRADIATION AT 266NM
REMARK 900 TOOK PLACE
REMARK 900 RELATED ID: 1GPN RELATED DB: PDB
REMARK 900 STRUCTURE OF ACETYLCHOLINESTERASE COMPLEXED WITH HUPERZINE
REMARK 900 B AT 2.35A RESOLUTION
REMARK 900 RELATED ID: 1QIH RELATED DB: PDB
REMARK 900 SPECIFIC CHEMICAL AND STRUCTURAL DAMAGE AT NINE TIME
REMARK 900 POINTS (POINT E) CAUSED BY INTENSE SYNCHROTRON RADIATION
REMARK 900 TO TORPEDO CALIFORNICA ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 2VB4 RELATED DB: PDB
REMARK 900 TORPEDO CALIFORNICA ACETYLCHOLINESTERASE COMPLEXED WITH 2-
REMARK 900 PAM
REMARK 900 RELATED ID: 1H23 RELATED DB: PDB
REMARK 900 STRUCTURE OF ACETYLCHOLINESTERASE (E.C. 3.1.1.7)
REMARK 900 COMPLEXED WITH (S,S)-(-)-BIS(12)-HUPERZINE A-LIKE
REMARK 900 INHIBITOR AT 2.15A RESOLUTION
REMARK 900 RELATED ID: 1ACJ RELATED DB: PDB
REMARK 900 ACETYLCHOLINESTERASE COMPLEXED WITH TACRINE
REMARK 900 RELATED ID: 1FSS RELATED DB: PDB
REMARK 900 ACETYLCHOLINESTERASE COMPLEXED WITH FASCICULIN-II
REMARK 900 RELATED ID: 2V97 RELATED DB: PDB
REMARK 900 STRUCTURE OF THE UNPHOTOLYSED COMPLEX OF TCACHE WITH 1
REMARK 900 -(2-NITROPHENYL)-2,2,2-TRIFLUOROETHYL-ARSENOCHOLINE
REMARK 900 AFTER A 9 SECONDS ANNEALING TO ROOM TEMPERATURE
DBREF 2XI4 A 1 537 UNP P04058 ACES_TORCA 22 558
DBREF 2XI4 B 1 537 UNP P04058 ACES_TORCA 22 558
SEQRES 1 A 537 ASP ASP HIS SER GLU LEU LEU VAL ASN THR LYS SER GLY
SEQRES 2 A 537 LYS VAL MET GLY THR ARG VAL PRO VAL LEU SER SER HIS
SEQRES 3 A 537 ILE SER ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO PRO
SEQRES 4 A 537 VAL GLY ASN MET ARG PHE ARG ARG PRO GLU PRO LYS LYS
SEQRES 5 A 537 PRO TRP SER GLY VAL TRP ASN ALA SER THR TYR PRO ASN
SEQRES 6 A 537 ASN CYS GLN GLN TYR VAL ASP GLU GLN PHE PRO GLY PHE
SEQRES 7 A 537 SER GLY SER GLU MET TRP ASN PRO ASN ARG GLU MET SER
SEQRES 8 A 537 GLU ASP CYS LEU TYR LEU ASN ILE TRP VAL PRO SER PRO
SEQRES 9 A 537 ARG PRO LYS SER THR THR VAL MET VAL TRP ILE TYR GLY
SEQRES 10 A 537 GLY GLY PHE TYR SER GLY SER SER THR LEU ASP VAL TYR
SEQRES 11 A 537 ASN GLY LYS TYR LEU ALA TYR THR GLU GLU VAL VAL LEU
SEQRES 12 A 537 VAL SER LEU SER TYR ARG VAL GLY ALA PHE GLY PHE LEU
SEQRES 13 A 537 ALA LEU HIS GLY SER GLN GLU ALA PRO GLY ASN VAL GLY
SEQRES 14 A 537 LEU LEU ASP GLN ARG MET ALA LEU GLN TRP VAL HIS ASP
SEQRES 15 A 537 ASN ILE GLN PHE PHE GLY GLY ASP PRO LYS THR VAL THR
SEQRES 16 A 537 ILE PHE GLY GLU SER ALA GLY GLY ALA SER VAL GLY MET
SEQRES 17 A 537 HIS ILE LEU SER PRO GLY SER ARG ASP LEU PHE ARG ARG
SEQRES 18 A 537 ALA ILE LEU GLN SER GLY SER PRO ASN CYS PRO TRP ALA
SEQRES 19 A 537 SER VAL SER VAL ALA GLU GLY ARG ARG ARG ALA VAL GLU
SEQRES 20 A 537 LEU GLY ARG ASN LEU ASN CYS ASN LEU ASN SER ASP GLU
SEQRES 21 A 537 GLU LEU ILE HIS CYS LEU ARG GLU LYS LYS PRO GLN GLU
SEQRES 22 A 537 LEU ILE ASP VAL GLU TRP ASN VAL LEU PRO PHE ASP SER
SEQRES 23 A 537 ILE PHE ARG PHE SER PHE VAL PRO VAL ILE ASP GLY GLU
SEQRES 24 A 537 PHE PHE PRO THR SER LEU GLU SER MET LEU ASN SER GLY
SEQRES 25 A 537 ASN PHE LYS LYS THR GLN ILE LEU LEU GLY VAL ASN LYS
SEQRES 26 A 537 ASP GLU GLY SER PHE PHE LEU LEU TYR GLY ALA PRO GLY
SEQRES 27 A 537 PHE SER LYS ASP SER GLU SER LYS ILE SER ARG GLU ASP
SEQRES 28 A 537 PHE MET SER GLY VAL LYS LEU SER VAL PRO HIS ALA ASN
SEQRES 29 A 537 ASP LEU GLY LEU ASP ALA VAL THR LEU GLN TYR THR ASP
SEQRES 30 A 537 TRP MET ASP ASP ASN ASN GLY ILE LYS ASN ARG ASP GLY
SEQRES 31 A 537 LEU ASP ASP ILE VAL GLY ASP HIS ASN VAL ILE CYS PRO
SEQRES 32 A 537 LEU MET HIS PHE VAL ASN LYS TYR THR LYS PHE GLY ASN
SEQRES 33 A 537 GLY THR TYR LEU TYR PHE PHE ASN HIS ARG ALA SER ASN
SEQRES 34 A 537 LEU VAL TRP PRO GLU TRP MET GLY VAL ILE HIS GLY TYR
SEQRES 35 A 537 GLU ILE GLU PHE VAL PHE GLY LEU PRO LEU VAL LYS GLU
SEQRES 36 A 537 LEU ASN TYR THR ALA GLU GLU GLU ALA LEU SER ARG ARG
SEQRES 37 A 537 ILE MET HIS TYR TRP ALA THR PHE ALA LYS THR GLY ASN
SEQRES 38 A 537 PRO ASN GLU PRO HIS SER GLN GLU SER LYS TRP PRO LEU
SEQRES 39 A 537 PHE THR THR LYS GLU GLN LYS PHE ILE ASP LEU ASN THR
SEQRES 40 A 537 GLU PRO MET LYS VAL HIS GLN ARG LEU ARG VAL GLN MET
SEQRES 41 A 537 CYS VAL PHE TRP ASN GLN PHE LEU PRO LYS LEU LEU ASN
SEQRES 42 A 537 ALA THR ALA CYS
SEQRES 1 B 537 ASP ASP HIS SER GLU LEU LEU VAL ASN THR LYS SER GLY
SEQRES 2 B 537 LYS VAL MET GLY THR ARG VAL PRO VAL LEU SER SER HIS
SEQRES 3 B 537 ILE SER ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO PRO
SEQRES 4 B 537 VAL GLY ASN MET ARG PHE ARG ARG PRO GLU PRO LYS LYS
SEQRES 5 B 537 PRO TRP SER GLY VAL TRP ASN ALA SER THR TYR PRO ASN
SEQRES 6 B 537 ASN CYS GLN GLN TYR VAL ASP GLU GLN PHE PRO GLY PHE
SEQRES 7 B 537 SER GLY SER GLU MET TRP ASN PRO ASN ARG GLU MET SER
SEQRES 8 B 537 GLU ASP CYS LEU TYR LEU ASN ILE TRP VAL PRO SER PRO
SEQRES 9 B 537 ARG PRO LYS SER THR THR VAL MET VAL TRP ILE TYR GLY
SEQRES 10 B 537 GLY GLY PHE TYR SER GLY SER SER THR LEU ASP VAL TYR
SEQRES 11 B 537 ASN GLY LYS TYR LEU ALA TYR THR GLU GLU VAL VAL LEU
SEQRES 12 B 537 VAL SER LEU SER TYR ARG VAL GLY ALA PHE GLY PHE LEU
SEQRES 13 B 537 ALA LEU HIS GLY SER GLN GLU ALA PRO GLY ASN VAL GLY
SEQRES 14 B 537 LEU LEU ASP GLN ARG MET ALA LEU GLN TRP VAL HIS ASP
SEQRES 15 B 537 ASN ILE GLN PHE PHE GLY GLY ASP PRO LYS THR VAL THR
SEQRES 16 B 537 ILE PHE GLY GLU SER ALA GLY GLY ALA SER VAL GLY MET
SEQRES 17 B 537 HIS ILE LEU SER PRO GLY SER ARG ASP LEU PHE ARG ARG
SEQRES 18 B 537 ALA ILE LEU GLN SER GLY SER PRO ASN CYS PRO TRP ALA
SEQRES 19 B 537 SER VAL SER VAL ALA GLU GLY ARG ARG ARG ALA VAL GLU
SEQRES 20 B 537 LEU GLY ARG ASN LEU ASN CYS ASN LEU ASN SER ASP GLU
SEQRES 21 B 537 GLU LEU ILE HIS CYS LEU ARG GLU LYS LYS PRO GLN GLU
SEQRES 22 B 537 LEU ILE ASP VAL GLU TRP ASN VAL LEU PRO PHE ASP SER
SEQRES 23 B 537 ILE PHE ARG PHE SER PHE VAL PRO VAL ILE ASP GLY GLU
SEQRES 24 B 537 PHE PHE PRO THR SER LEU GLU SER MET LEU ASN SER GLY
SEQRES 25 B 537 ASN PHE LYS LYS THR GLN ILE LEU LEU GLY VAL ASN LYS
SEQRES 26 B 537 ASP GLU GLY SER PHE PHE LEU LEU TYR GLY ALA PRO GLY
SEQRES 27 B 537 PHE SER LYS ASP SER GLU SER LYS ILE SER ARG GLU ASP
SEQRES 28 B 537 PHE MET SER GLY VAL LYS LEU SER VAL PRO HIS ALA ASN
SEQRES 29 B 537 ASP LEU GLY LEU ASP ALA VAL THR LEU GLN TYR THR ASP
SEQRES 30 B 537 TRP MET ASP ASP ASN ASN GLY ILE LYS ASN ARG ASP GLY
SEQRES 31 B 537 LEU ASP ASP ILE VAL GLY ASP HIS ASN VAL ILE CYS PRO
SEQRES 32 B 537 LEU MET HIS PHE VAL ASN LYS TYR THR LYS PHE GLY ASN
SEQRES 33 B 537 GLY THR TYR LEU TYR PHE PHE ASN HIS ARG ALA SER ASN
SEQRES 34 B 537 LEU VAL TRP PRO GLU TRP MET GLY VAL ILE HIS GLY TYR
SEQRES 35 B 537 GLU ILE GLU PHE VAL PHE GLY LEU PRO LEU VAL LYS GLU
SEQRES 36 B 537 LEU ASN TYR THR ALA GLU GLU GLU ALA LEU SER ARG ARG
SEQRES 37 B 537 ILE MET HIS TYR TRP ALA THR PHE ALA LYS THR GLY ASN
SEQRES 38 B 537 PRO ASN GLU PRO HIS SER GLN GLU SER LYS TRP PRO LEU
SEQRES 39 B 537 PHE THR THR LYS GLU GLN LYS PHE ILE ASP LEU ASN THR
SEQRES 40 B 537 GLU PRO MET LYS VAL HIS GLN ARG LEU ARG VAL GLN MET
SEQRES 41 B 537 CYS VAL PHE TRP ASN GLN PHE LEU PRO LYS LEU LEU ASN
SEQRES 42 B 537 ALA THR ALA CYS
HET AFT A1000 23
HET CL A1001 1
HET CL A1002 1
HET PEG A1003 7
HET PEG A1004 7
HET PEG A1005 7
HET PGE A1006 10
HET NAG A1007 14
HET NAG A1008 14
HET NAG A1009 14
HET K A1010 1
HET AFT B1000 23
HET CL B1001 1
HET CL B1002 1
HET PEG B1003 7
HET PGE B1004 10
HET PEG B1005 7
HET PEG B1006 7
HET NAG B1008 14
HET NAG B1009 14
HETNAM CL CHLORIDE ION
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM PGE TRIETHYLENE GLYCOL
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM K POTASSIUM ION
FORMUL 3 AFT AFLATOXIN B1
FORMUL 4 CL 4(CL 1-)
FORMUL 5 PEG 6(C4 H10 O3)
FORMUL 6 PGE 2(C6 H14 O4)
FORMUL 7 NAG 5(C8 H15 N O6)
FORMUL 8 K K 1+
FORMUL 9 HOH *744(H2 O)
HELIX 1 1 VAL A 40 ARG A 44 5 5
HELIX 2 2 PHE A 78 MET A 83 1 6
HELIX 3 3 LEU A 127 ASN A 131 5 5
HELIX 4 4 GLY A 132 GLU A 140 1 9
HELIX 5 5 VAL A 150 LEU A 156 1 7
HELIX 6 6 ASN A 167 ILE A 184 1 18
HELIX 7 7 GLN A 185 PHE A 187 5 3
HELIX 8 8 SER A 200 SER A 212 1 13
HELIX 9 9 PRO A 213 PHE A 219 5 7
HELIX 10 10 VAL A 238 LEU A 252 1 15
HELIX 11 11 SER A 258 LYS A 269 1 12
HELIX 12 12 LYS A 270 GLU A 278 1 9
HELIX 13 13 TRP A 279 LEU A 282 5 4
HELIX 14 14 SER A 304 GLY A 312 1 9
HELIX 15 15 GLY A 328 ALA A 336 1 9
HELIX 16 16 SER A 348 VAL A 360 1 13
HELIX 17 17 ASN A 364 THR A 376 1 13
HELIX 18 18 ASN A 383 VAL A 400 1 18
HELIX 19 19 VAL A 400 LYS A 413 1 14
HELIX 20 20 PRO A 433 GLY A 437 5 5
HELIX 21 21 TYR A 442 PHE A 448 1 7
HELIX 22 22 GLY A 449 VAL A 453 5 5
HELIX 23 23 VAL A 453 ASN A 457 5 5
HELIX 24 24 THR A 459 GLY A 480 1 22
HELIX 25 25 ARG A 517 GLN A 526 1 10
HELIX 26 26 GLN A 526 THR A 535 1 10
HELIX 27 27 VAL B 40 ARG B 44 5 5
HELIX 28 28 PHE B 78 MET B 83 1 6
HELIX 29 29 LEU B 127 ASN B 131 5 5
HELIX 30 30 GLY B 132 GLU B 140 1 9
HELIX 31 31 VAL B 150 LEU B 156 1 7
HELIX 32 32 ASN B 167 ILE B 184 1 18
HELIX 33 33 GLN B 185 PHE B 187 5 3
HELIX 34 34 SER B 200 SER B 212 1 13
HELIX 35 35 SER B 215 PHE B 219 5 5
HELIX 36 36 VAL B 238 LEU B 252 1 15
HELIX 37 37 SER B 258 GLU B 268 1 11
HELIX 38 38 LYS B 270 GLU B 278 1 9
HELIX 39 39 TRP B 279 LEU B 282 5 4
HELIX 40 40 SER B 304 GLY B 312 1 9
HELIX 41 41 GLY B 328 ALA B 336 1 9
HELIX 42 42 SER B 348 VAL B 360 1 13
HELIX 43 43 ASN B 364 TYR B 375 1 12
HELIX 44 44 ASN B 383 VAL B 400 1 18
HELIX 45 45 VAL B 400 LYS B 413 1 14
HELIX 46 46 PRO B 433 GLY B 437 5 5
HELIX 47 47 GLU B 443 PHE B 448 1 6
HELIX 48 48 GLY B 449 VAL B 453 5 5
HELIX 49 49 VAL B 453 ASN B 457 5 5
HELIX 50 50 THR B 459 GLY B 480 1 22
HELIX 51 51 ARG B 517 GLN B 526 1 10
HELIX 52 52 GLN B 526 ASN B 533 1 8
SHEET 1 AA 3 LEU A 7 THR A 10 0
SHEET 2 AA 3 GLY A 13 MET A 16 -1 O GLY A 13 N THR A 10
SHEET 3 AA 3 VAL A 57 ASN A 59 1 O TRP A 58 N MET A 16
SHEET 1 AB11 THR A 18 VAL A 22 0
SHEET 2 AB11 SER A 25 PRO A 34 -1 O SER A 25 N VAL A 22
SHEET 3 AB11 TYR A 96 VAL A 101 -1 O LEU A 97 N ILE A 33
SHEET 4 AB11 VAL A 142 SER A 145 -1 O LEU A 143 N TRP A 100
SHEET 5 AB11 THR A 109 ILE A 115 1 O THR A 110 N VAL A 142
SHEET 6 AB11 GLY A 189 GLU A 199 1 N ASP A 190 O THR A 109
SHEET 7 AB11 ARG A 221 GLN A 225 1 O ARG A 221 N ILE A 196
SHEET 8 AB11 ILE A 319 ASN A 324 1 O LEU A 320 N LEU A 224
SHEET 9 AB11 THR A 418 PHE A 423 1 O TYR A 419 N LEU A 321
SHEET 10 AB11 LYS A 501 LEU A 505 1 O ILE A 503 N PHE A 422
SHEET 11 AB11 VAL A 512 GLN A 514 -1 O HIS A 513 N PHE A 502
SHEET 1 AC 2 VAL A 236 SER A 237 0
SHEET 2 AC 2 VAL A 295 ILE A 296 1 N ILE A 296 O VAL A 236
SHEET 1 BA 3 LEU B 7 THR B 10 0
SHEET 2 BA 3 GLY B 13 MET B 16 -1 O GLY B 13 N THR B 10
SHEET 3 BA 3 VAL B 57 ASN B 59 1 O TRP B 58 N MET B 16
SHEET 1 BB11 THR B 18 VAL B 22 0
SHEET 2 BB11 SER B 25 PRO B 34 -1 O SER B 25 N VAL B 22
SHEET 3 BB11 TYR B 96 PRO B 102 -1 O LEU B 97 N ILE B 33
SHEET 4 BB11 VAL B 142 SER B 145 -1 O LEU B 143 N TRP B 100
SHEET 5 BB11 THR B 109 ILE B 115 1 O THR B 110 N VAL B 142
SHEET 6 BB11 GLY B 189 GLU B 199 1 N ASP B 190 O THR B 109
SHEET 7 BB11 ARG B 221 GLN B 225 1 O ARG B 221 N ILE B 196
SHEET 8 BB11 GLN B 318 ASN B 324 1 O GLN B 318 N ALA B 222
SHEET 9 BB11 GLY B 417 PHE B 423 1 O GLY B 417 N ILE B 319
SHEET 10 BB11 LYS B 501 LEU B 505 1 O ILE B 503 N PHE B 422
SHEET 11 BB11 VAL B 512 GLN B 514 -1 O HIS B 513 N PHE B 502
SHEET 1 BC 2 VAL B 236 SER B 237 0
SHEET 2 BC 2 VAL B 295 ILE B 296 1 N ILE B 296 O VAL B 236
SSBOND 1 CYS A 67 CYS A 94 1555 1555 2.05
SSBOND 2 CYS A 254 CYS A 265 1555 1555 2.06
SSBOND 3 CYS A 402 CYS A 521 1555 1555 2.04
SSBOND 4 CYS B 67 CYS B 94 1555 1555 2.08
SSBOND 5 CYS B 254 CYS B 265 1555 1555 2.05
SSBOND 6 CYS B 402 CYS B 521 1555 1555 2.01
LINK ND2 ASN A 59 C1 NAG A1007 1555 1555 1.44
LINK ND2 ASN A 416 C1 NAG A1008 1555 1555 1.45
LINK ND2 ASN A 457 C1 NAG A1009 1555 1555 1.45
LINK K K A1010 OE1 GLU A 260 1555 1555 2.29
LINK K K A1010 OE1 GLU B 508 1555 3755 2.27
LINK K K A1010 OE2 GLU B 508 1555 3755 2.26
LINK K K A1010 OE1 GLU A 163 1555 1555 2.73
LINK ND2 ASN B 59 C1 NAG B1008 1555 1555 1.45
LINK ND2 ASN B 416 C1 NAG B1009 1555 1555 1.43
CISPEP 1 SER A 103 PRO A 104 0 8.25
CISPEP 2 SER B 103 PRO B 104 0 2.12
SITE 1 AC1 1 THR B 497
SITE 1 AC2 1 TYR B 134
SITE 1 AC3 1 LEU A 23
SITE 1 AC4 4 GLU A 163 GLU A 260 HIS A 264 GLU B 508
SITE 1 AC5 12 TYR A 70 TYR A 121 TRP A 279 SER A 286
SITE 2 AC5 12 ILE A 287 PHE A 288 ARG A 289 PHE A 290
SITE 3 AC5 12 PHE A 330 TYR A 334 HOH A2001 HOH A2002
SITE 1 AC6 15 TYR B 70 TYR B 121 TRP B 279 SER B 286
SITE 2 AC6 15 ILE B 287 PHE B 288 ARG B 289 PHE B 290
SITE 3 AC6 15 PHE B 330 TYR B 334 HOH B2001 HOH B2002
SITE 4 AC6 15 HOH B2003 HOH B2004 HOH B2005
SITE 1 AC7 3 TRP B 100 ASN B 131 HOH B2374
SITE 1 AC8 6 GLY B 118 TYR B 121 GLU B 199 PHE B 330
SITE 2 AC8 6 HIS B 440 HOH B2376
SITE 1 AC9 3 SER A 55 VAL A 57 HOH A2340
SITE 1 BC1 9 GLY A 80 MET A 83 TRP A 84 TRP A 432
SITE 2 BC1 9 HIS A 440 GLY A 441 TYR A 442 GLU A 445
SITE 3 BC1 9 HOH A2341
SITE 1 BC2 9 MET B 405 HIS B 406 ASN B 409 LEU B 516
SITE 2 BC2 9 VAL B 518 CYS B 521 ASN B 525 HOH B2349
SITE 3 BC2 9 HOH B2377
SITE 1 BC3 7 HIS A 406 ASN A 409 CYS A 521 VAL A 522
SITE 2 BC3 7 ASN A 525 GLN A 526 HOH A2342
SITE 1 BC4 9 TRP A 84 GLY A 118 TYR A 121 GLU A 199
SITE 2 BC4 9 PHE A 331 HIS A 440 HOH A2095 HOH A2148
SITE 3 BC4 9 HOH A2343
SITE 1 BC5 1 ASN B 483
SITE 1 BC6 4 ASN A 59 SER A 61 HOH A2345 HOH A2346
SITE 1 BC7 5 ASN A 416 HOH A2347 HOH A2348 HOH A2350
SITE 2 BC7 5 HOH A2351
SITE 1 BC8 7 ASN B 59 SER B 61 THR B 62 HOH B2382
SITE 2 BC8 7 HOH B2383 HOH B2384 HOH B2385
SITE 1 BC9 7 ASN B 416 HOH B2387 HOH B2389 HOH B2390
SITE 2 BC9 7 HOH B2391 HOH B2392 HOH B2393
SITE 1 CC1 1 ASN A 457
CRYST1 91.730 107.030 150.730 90.00 90.00 90.00 P 21 21 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.010902 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009343 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006634 0.00000
TER 4275 THR A 535
TER 8571 THR B 535
MASTER 755 0 20 52 32 0 35 6 9496 2 198 84
END |