| content |
HEADER HYDROLASE/TOXIN 05-JUL-00 1F8U
TITLE CRYSTAL STRUCTURE OF MUTANT E202Q OF HUMAN
TITLE 2 ACETYLCHOLINESTERASE COMPLEXED WITH GREEN MAMBA VENOM
TITLE 3 PEPTIDE FASCICULIN-II
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYLCHOLINESTERASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.1.1.7;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: FASCICULIN II;
COMPND 8 CHAIN: B
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 GENE: ACHE;
SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 7 EXPRESSION_SYSTEM_CELL_LINE: HEK 293;
SOURCE 8 EXPRESSION_SYSTEM_TISSUE: KIDNEY;
SOURCE 9 EXPRESSION_SYSTEM_CELL: HUMAN EMBRYONIC KIDNEY CELLS;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: DENDROASPIS ANGUSTICEPS;
SOURCE 12 ORGANISM_COMMON: EASTERN GREEN MAMBA;
SOURCE 13 SECRETION: VENOM
KEYWDS SERINE ESTERASE, HUMAN ACETYLCHOLINESTERASE, HYDROLASE,
KEYWDS 2 SNAKE TOXIN, HYDROLASE/HYDROLASE INHIBITOR
EXPDTA X-RAY DIFFRACTION
AUTHOR G.KRYGER,M.HAREL,A.SHAFFERMAN,I.SILMAN,J.L.SUSSMAN
REVDAT 1 17-JAN-01 1F8U 0
JRNL AUTH G.KRYGER,M.HAREL,M.HAREL,A.SHAFFERMAN,I.SILMAN,
JRNL AUTH 2 J.L.SUSSMAN
JRNL TITL STRUCTURES OF RECOMBINANT NATIVE AND E202Q MUTANT
JRNL TITL 2 HUMAN ACETYLCHOLINESTERASE COMPLEXED WITH THE
JRNL TITL 3 SNAKE-VENOM TOXIN FASCICULIN-II
JRNL REF ACTA CRYSTALLOGR., SECT.D V. 56 1385 2000
JRNL REFN ASTM ABCRE6 DK ISSN 0907-4449
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.43
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 OUTLIER CUTOFF HIGH (RMS(ABS(F))) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 93.7
REMARK 3 NUMBER OF REFLECTIONS : 22803
REMARK 3
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) : 0.191
REMARK 3 FREE R VALUE : 0.227
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1134
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.007
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) : 2.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.08
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 67.70
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2578
REMARK 3 BIN R VALUE (WORKING SET) : 0.3180
REMARK 3 BIN FREE R VALUE : 0.3390
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.90
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 134
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.029
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4594
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 28
REMARK 3 SOLVENT ATOMS : 117
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 50.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 58.30
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 16.29000
REMARK 3 B22 (A**2) : 16.29000
REMARK 3 B33 (A**2) : -32.58000
REMARK 3 B12 (A**2) : 14.92000
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) : 0.33
REMARK 3 ESD FROM SIGMAA (A) : 0.580
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) : 0.40
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.59
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.40
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.20
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.95
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) : 6.42 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 9.86 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 9.65 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 13.31 ; 2.500
REMARK 3
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.35
REMARK 3 BSOL : 59.89
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_REP.PARAM
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : CARBOHYDRATE.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1F8U COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-JUL-2000.
REMARK 100 THE RCSB ID CODE IS RCSB011385.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X12C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.009
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z
REMARK 290 6555 -X,-X+Y,-Z
REMARK 290 7555 2/3+X,1/3+Y,1/3+Z
REMARK 290 8555 2/3-Y,1/3+X-Y,1/3+Z
REMARK 290 9555 2/3-X+Y,1/3-X,1/3+Z
REMARK 290 10555 2/3+Y,1/3+X,1/3-Z
REMARK 290 11555 2/3+X-Y,1/3-Y,1/3-Z
REMARK 290 12555 2/3-X,1/3-X+Y,1/3-Z
REMARK 290 13555 1/3+X,2/3+Y,2/3+Z
REMARK 290 14555 1/3-Y,2/3+X-Y,2/3+Z
REMARK 290 15555 1/3-X+Y,2/3-X,2/3+Z
REMARK 290 16555 1/3+Y,2/3+X,2/3-Z
REMARK 290 17555 1/3+X-Y,2/3-Y,2/3-Z
REMARK 290 18555 1/3-X,2/3-X+Y,2/3-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 75.55500
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 43.62170
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 82.34000
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 75.55500
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 43.62170
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 82.34000
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 75.55500
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 43.62170
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 82.34000
REMARK 290 SMTRY1 10 -0.500000 0.866025 0.000000 75.55500
REMARK 290 SMTRY2 10 0.866025 0.500000 0.000000 43.62170
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 82.34000
REMARK 290 SMTRY1 11 1.000000 0.000000 0.000000 75.55500
REMARK 290 SMTRY2 11 0.000000 -1.000000 0.000000 43.62170
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 82.34000
REMARK 290 SMTRY1 12 -0.500000 -0.866025 0.000000 75.55500
REMARK 290 SMTRY2 12 -0.866025 0.500000 0.000000 43.62170
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 82.34000
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 87.24340
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 164.68000
REMARK 290 SMTRY1 14 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 14 0.866025 -0.500000 0.000000 87.24340
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 164.68000
REMARK 290 SMTRY1 15 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 15 -0.866025 -0.500000 0.000000 87.24340
REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 164.68000
REMARK 290 SMTRY1 16 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 16 0.866025 0.500000 0.000000 87.24340
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 164.68000
REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 17 0.000000 -1.000000 0.000000 87.24340
REMARK 290 SMTRY3 17 0.000000 0.000000 -1.000000 164.68000
REMARK 290 SMTRY1 18 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 18 -0.866025 0.500000 0.000000 87.24340
REMARK 290 SMTRY3 18 0.000000 0.000000 -1.000000 164.68000
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 2 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, X
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 GLU A 1
REMARK 465 GLY A 2
REMARK 465 ARG A 3
REMARK 465 GLU A 4
REMARK 465 PRO A 259
REMARK 465 GLY A 260
REMARK 465 GLY A 261
REMARK 465 THR A 262
REMARK 465 GLY A 263
REMARK 465 GLY A 264
REMARK 465 ARG A 493
REMARK 465 ASP A 494
REMARK 465 ASP A 544
REMARK 465 THR A 545
REMARK 465 LEU A 546
REMARK 465 ASP A 547
REMARK 465 GLU A 548
REMARK 465 ALA A 549
REMARK 465 GLU A 550
REMARK 465 ARG A 551
REMARK 465 GLN A 552
REMARK 465 TRP A 553
REMARK 465 LYS A 554
REMARK 465 ALA A 555
REMARK 465 GLU A 556
REMARK 465 PHE A 557
REMARK 465 HIS A 558
REMARK 465 ARG A 559
REMARK 465 TRP A 560
REMARK 465 SER A 561
REMARK 465 SER A 562
REMARK 465 TYR A 563
REMARK 465 MET A 564
REMARK 465 VAL A 565
REMARK 465 HIS A 566
REMARK 465 TRP A 567
REMARK 465 LYS A 568
REMARK 465 ASN A 569
REMARK 465 GLN A 570
REMARK 465 PHE A 571
REMARK 465 ASP A 572
REMARK 465 HIS A 573
REMARK 465 TYR A 574
REMARK 465 SER A 575
REMARK 465 LYS A 576
REMARK 465 GLN A 577
REMARK 465 ASP A 578
REMARK 465 ARG A 579
REMARK 465 CYS A 580
REMARK 465 SER A 581
REMARK 465 ASP A 582
REMARK 465 LEU A 583
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
REMARK 500 O HOH 601 O HOH 602 2.09
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 MET A 149 CE MET A 149 SD 0.048
REMARK 500 MET A 241 CE MET A 241 SD -0.058
REMARK 500 MET A 443 CE MET A 443 SD -0.065
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 GLU A 39 N - CA - C ANGL. DEV. = -8.7 DEGREES
REMARK 500 PHE A 158 N - CA - C ANGL. DEV. = 9.0 DEGREES
REMARK 500 LEU A 161 N - CA - C ANGL. DEV. =-11.6 DEGREES
REMARK 500 ASN A 186 N - CA - C ANGL. DEV. = 9.0 DEGREES
REMARK 500 ARG A 219 N - CA - C ANGL. DEV. = 9.2 DEGREES
REMARK 500 GLN A 291 N - CA - C ANGL. DEV. = 10.3 DEGREES
REMARK 500 GLY A 335 N - CA - C ANGL. DEV. = 9.7 DEGREES
REMARK 500 ASP A 384 N - CA - C ANGL. DEV. = -8.6 DEGREES
REMARK 500 VAL A 407 N - CA - C ANGL. DEV. = 9.5 DEGREES
REMARK 500 GLY A 422 N - CA - C ANGL. DEV. = 9.5 DEGREES
REMARK 500 GLU A 491 N - CA - C ANGL. DEV. = 8.4 DEGREES
REMARK 500 ARG B 27 N - CA - C ANGL. DEV. = -8.5 DEGREES
REMARK 500 SER B 55 N - CA - C ANGL. DEV. = 9.0 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 ALA A 6 -73.48 76.80
REMARK 500 GLN A 291 168.26 62.90
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1B41 RELATED DB: PDB
REMARK 900 NATIVE HUMAN ACETYLCHOLINESTERASE COMPLEXED WITH GREEN
REMARK 900 MAMBA VENOM PEPTIDE FASCICULIN-II
DBREF 1F8U A 1 583 SWS P22303 ACES_HUMAN 32 614
DBREF 1F8U B 1 61 SWS P01403 TXF7_DENAN 1 61
SEQADV 1F8U GLN A 202 SWS P22303 GLU 233 ENGINEERED
SEQRES 1 A 583 GLU GLY ARG GLU ASP ALA GLU LEU LEU VAL THR VAL ARG
SEQRES 2 A 583 GLY GLY ARG LEU ARG GLY ILE ARG LEU LYS THR PRO GLY
SEQRES 3 A 583 GLY PRO VAL SER ALA PHE LEU GLY ILE PRO PHE ALA GLU
SEQRES 4 A 583 PRO PRO MET GLY PRO ARG ARG PHE LEU PRO PRO GLU PRO
SEQRES 5 A 583 LYS GLN PRO TRP SER GLY VAL VAL ASP ALA THR THR PHE
SEQRES 6 A 583 GLN SER VAL CYS TYR GLN TYR VAL ASP THR LEU TYR PRO
SEQRES 7 A 583 GLY PHE GLU GLY THR GLU MET TRP ASN PRO ASN ARG GLU
SEQRES 8 A 583 LEU SER GLU ASP CYS LEU TYR LEU ASN VAL TRP THR PRO
SEQRES 9 A 583 TYR PRO ARG PRO THR SER PRO THR PRO VAL LEU VAL TRP
SEQRES 10 A 583 ILE TYR GLY GLY GLY PHE TYR SER GLY ALA SER SER LEU
SEQRES 11 A 583 ASP VAL TYR ASP GLY ARG PHE LEU VAL GLN ALA GLU ARG
SEQRES 12 A 583 THR VAL LEU VAL SER MET ASN TYR ARG VAL GLY ALA PHE
SEQRES 13 A 583 GLY PHE LEU ALA LEU PRO GLY SER ARG GLU ALA PRO GLY
SEQRES 14 A 583 ASN VAL GLY LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP
SEQRES 15 A 583 VAL GLN GLU ASN VAL ALA ALA PHE GLY GLY ASP PRO THR
SEQRES 16 A 583 SER VAL THR LEU PHE GLY GLN SER ALA GLY ALA ALA SER
SEQRES 17 A 583 VAL GLY MET HIS LEU LEU SER PRO PRO SER ARG GLY LEU
SEQRES 18 A 583 PHE HIS ARG ALA VAL LEU GLN SER GLY ALA PRO ASN GLY
SEQRES 19 A 583 PRO TRP ALA THR VAL GLY MET GLY GLU ALA ARG ARG ARG
SEQRES 20 A 583 ALA THR GLN LEU ALA HIS LEU VAL GLY CYS PRO PRO GLY
SEQRES 21 A 583 GLY THR GLY GLY ASN ASP THR GLU LEU VAL ALA CYS LEU
SEQRES 22 A 583 ARG THR ARG PRO ALA GLN VAL LEU VAL ASN HIS GLU TRP
SEQRES 23 A 583 HIS VAL LEU PRO GLN GLU SER VAL PHE ARG PHE SER PHE
SEQRES 24 A 583 VAL PRO VAL VAL ASP GLY ASP PHE LEU SER ASP THR PRO
SEQRES 25 A 583 GLU ALA LEU ILE ASN ALA GLY ASP PHE HIS GLY LEU GLN
SEQRES 26 A 583 VAL LEU VAL GLY VAL VAL LYS ASP GLU GLY SER TYR PHE
SEQRES 27 A 583 LEU VAL TYR GLY ALA PRO GLY PHE SER LYS ASP ASN GLU
SEQRES 28 A 583 SER LEU ILE SER ARG ALA GLU PHE LEU ALA GLY VAL ARG
SEQRES 29 A 583 VAL GLY VAL PRO GLN VAL SER ASP LEU ALA ALA GLU ALA
SEQRES 30 A 583 VAL VAL LEU HIS TYR THR ASP TRP LEU HIS PRO GLU ASP
SEQRES 31 A 583 PRO ALA ARG LEU ARG GLU ALA LEU SER ASP VAL VAL GLY
SEQRES 32 A 583 ASP HIS ASN VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY
SEQRES 33 A 583 ARG LEU ALA ALA GLN GLY ALA ARG VAL TYR ALA TYR VAL
SEQRES 34 A 583 PHE GLU HIS ARG ALA SER THR LEU SER TRP PRO LEU TRP
SEQRES 35 A 583 MET GLY VAL PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE
SEQRES 36 A 583 GLY ILE PRO LEU ASP PRO SER ARG ASN TYR THR ALA GLU
SEQRES 37 A 583 GLU LYS ILE PHE ALA GLN ARG LEU MET ARG TYR TRP ALA
SEQRES 38 A 583 ASN PHE ALA ARG THR GLY ASP PRO ASN GLU PRO ARG ASP
SEQRES 39 A 583 PRO LYS ALA PRO GLN TRP PRO PRO TYR THR ALA GLY ALA
SEQRES 40 A 583 GLN GLN TYR VAL SER LEU ASP LEU ARG PRO LEU GLU VAL
SEQRES 41 A 583 ARG ARG GLY LEU ARG ALA GLN ALA CYS ALA PHE TRP ASN
SEQRES 42 A 583 ARG PHE LEU PRO LYS LEU LEU SER ALA THR ASP THR LEU
SEQRES 43 A 583 ASP GLU ALA GLU ARG GLN TRP LYS ALA GLU PHE HIS ARG
SEQRES 44 A 583 TRP SER SER TYR MET VAL HIS TRP LYS ASN GLN PHE ASP
SEQRES 45 A 583 HIS TYR SER LYS GLN ASP ARG CYS SER ASP LEU
SEQRES 1 B 61 THR MET CYS TYR SER HIS THR THR THR SER ARG ALA ILE
SEQRES 2 B 61 LEU THR ASN CYS GLY GLU ASN SER CYS TYR ARG LYS SER
SEQRES 3 B 61 ARG ARG HIS PRO PRO LYS MET VAL LEU GLY ARG GLY CYS
SEQRES 4 B 61 GLY CYS PRO PRO GLY ASP ASP ASN LEU GLU VAL LYS CYS
SEQRES 5 B 61 CYS THR SER PRO ASP LYS CYS ASN TYR
MODRES 1F8U ASN A 350 ASN GLYCOSYLATION SITE
HET NAG X3002 14
HET NAG X3003 14
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETSYN NAG NAG
FORMUL 3 NAG 2(C8 H15 N1 O6)
FORMUL 4 HOH *117(H2 O1)
HELIX 1 1 MET A 42 ARG A 46 5 5
HELIX 2 2 PHE A 80 MET A 85 1 6
HELIX 3 3 LEU A 130 ASP A 134 5 5
HELIX 4 4 GLY A 135 ARG A 143 1 9
HELIX 5 5 VAL A 153 LEU A 159 1 7
HELIX 6 6 ASN A 170 VAL A 187 1 18
HELIX 7 7 ALA A 188 PHE A 190 5 3
HELIX 8 8 SER A 203 SER A 215 1 13
HELIX 9 9 PRO A 216 PHE A 222 5 7
HELIX 10 10 MET A 241 VAL A 255 1 15
HELIX 11 11 ASN A 265 ARG A 274 1 10
HELIX 12 12 PRO A 277 HIS A 284 1 8
HELIX 13 13 GLU A 285 LEU A 289 5 5
HELIX 14 14 THR A 311 GLY A 319 1 9
HELIX 15 15 GLY A 335 VAL A 340 1 6
HELIX 16 16 SER A 355 VAL A 367 1 13
HELIX 17 17 SER A 371 THR A 383 1 13
HELIX 18 18 ASP A 390 VAL A 407 1 18
HELIX 19 19 VAL A 407 GLN A 421 1 15
HELIX 20 20 PRO A 440 GLY A 444 5 5
HELIX 21 21 GLU A 450 PHE A 455 1 6
HELIX 22 22 GLY A 456 ASP A 460 5 5
HELIX 23 23 THR A 466 GLY A 487 1 22
HELIX 24 24 ARG A 525 ARG A 534 1 10
HELIX 25 25 ARG A 534 ALA A 542 1 9
SHEET 1 A 3 LEU A 9 THR A 11 0
SHEET 2 A 3 ARG A 16 ARG A 18 -1 N LEU A 17 O VAL A 10
SHEET 3 A 3 VAL A 59 ASP A 61 1 N VAL A 60 O ARG A 16
SHEET 1 B11 ILE A 20 LEU A 22 0
SHEET 2 B11 VAL A 29 PRO A 36 -1 O VAL A 29 N LEU A 22
SHEET 3 B11 TYR A 98 PRO A 104 -1 N LEU A 99 O ILE A 35
SHEET 4 B11 VAL A 145 MET A 149 -1 O LEU A 146 N TRP A 102
SHEET 5 B11 THR A 112 ILE A 118 1 O PRO A 113 N VAL A 145
SHEET 6 B11 ARG A 224 GLN A 228 1 O ARG A 224 N LEU A 199
SHEET 7 B11 LEU A 324 VAL A 331 1 O GLN A 325 N ALA A 225
SHEET 8 B11 ALA A 423 PHE A 430 1 N ARG A 424 O LEU A 324
SHEET 9 B11 GLN A 509 LEU A 513 1 O VAL A 511 N VAL A 429
SHEET 10 B11 GLU A 519 ARG A 522 -1 O GLU A 519 N SER A 512
SHEET 1 C 2 ALA A 38 GLU A 39 0
SHEET 2 C 2 GLU A 51 PRO A 52 -1 O GLU A 51 N GLU A 39
SHEET 1 D 2 VAL A 68 CYS A 69 0
SHEET 2 D 2 LEU A 92 SER A 93 1 N SER A 93 O VAL A 68
SHEET 1 E 2 VAL A 239 GLY A 240 0
SHEET 2 E 2 VAL A 302 VAL A 303 1 N VAL A 303 O VAL A 239
SHEET 1 F 2 MET B 2 SER B 5 0
SHEET 2 F 2 ILE B 13 ASN B 16 -1 N ILE B 13 O SER B 5
SHEET 1 G 3 VAL B 34 CYS B 39 0
SHEET 2 G 3 CYS B 22 ARG B 27 -1 N TYR B 23 O GLY B 38
SHEET 3 G 3 LEU B 48 CYS B 53 -1 N GLU B 49 O SER B 26
SSBOND 1 CYS A 69 CYS A 96
SSBOND 2 CYS A 257 CYS A 272
SSBOND 3 CYS A 409 CYS A 529
SSBOND 4 CYS B 3 CYS B 22
SSBOND 5 CYS B 17 CYS B 39
SSBOND 6 CYS B 41 CYS B 52
SSBOND 7 CYS B 53 CYS B 59
LINK O4 NAG X3002 C1 NAG X3003
LINK C1 NAG X3002 ND2 ASN A 350
CISPEP 1 TYR A 105 PRO A 106 0 0.48
CISPEP 2 CYS A 257 PRO A 258 0 0.57
CISPEP 3 PRO B 30 PRO B 31 0 0.13
CRYST1 151.110 151.110 247.020 90.00 90.00 120.00 H 3 2 18
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 0.006618 0.003821 0.000000 0.00000
SCALE2 0.000000 0.007641 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004048 0.00000
END |