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HEADER HYDROLASE (SERINE ESTERASE) 15-NOV-99 1QON
TITLE ACHE FROM DROSOPHILA MELANOGASTER COMPLEX WITH TACRINE
TITLE 2 DERIVATIVE 9-(3-IODOBENZYLAMINO)-1,2,3,4-TETRAHYDROACRIDINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYLCHOLINESTERASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.1.1.7;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;
SOURCE 3 ORGANISM_COMMON: FRUIT FLY;
SOURCE 4 EXPRESSION_SYSTEM: DROSOPHILA MELANOGASTER;
SOURCE 5 EXPRESSION_SYSTEM_STRAIN: SCHNEIDER LINE 2;
SOURCE 6 EXPRESSION_SYSTEM_CELLULAR_LOCATION: SECRETED
SOURCE 7 (EXTRACELLULAR);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID DNA;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: S2-SEC 1/3;
SOURCE 10 EXPRESSION_SYSTEM_GENE: DMACHE
KEYWDS HYDROLASE (SERINE ESTERASE), HYDROLASE, SERINE ESTERASE,
KEYWDS 2 SYNAPSE, MEMBRANE, NERVE, MUSCLE, SIGNAL, NEUROTRANSMITTER
KEYWDS 3 DEGRADATION, GLYCOPROTEIN, GPI-ANCHOR, ALTERNATIVE SPLICING
EXPDTA X-RAY DIFFRACTION
AUTHOR M.HAREL,I.SILMAN,J.L.SUSSMAN
REVDAT 1 20-JUL-00 1QON 0
JRNL AUTH M.HAREL,G.KRYGER,T.L.ROSENBERRY,W.D.MALLENDER,
JRNL AUTH 2 T.LEWIS,R.J.FLETCHER,J.M.GUSS,I.SILMAN,J.L.SUSSMAN
JRNL TITL THREE-DIMENSIONAL STRUCTURES OF DROSOPHILA
JRNL TITL 2 MELANOGASTER ACETYLCHOLINESTERASE AND OF ITS
JRNL TITL 3 COMPLEXES WITH TWO POTENT INHIBITORS
JRNL REF PROTEIN SCI. V. 9 1063 2000
JRNL REFN ASTM PRCIEI US ISSN 0961-8368
REMARK 2
REMARK 2 RESOLUTION. 2.72 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 3.8
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,
REMARK 3 GROSSE-KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,
REMARK 3 PANNU,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) : 2.72
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.0
REMARK 3 OUTLIER CUTOFF HIGH (RMS(ABS(F))) : 0.0
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 96.9
REMARK 3 NUMBER OF REFLECTIONS : 19693
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) : 0.220
REMARK 3 FREE R VALUE : 0.265
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 32
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.72
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.75
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 554
REMARK 3 BIN R VALUE (WORKING SET) : 0.33
REMARK 3 BIN FREE R VALUE : 0.37
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4258
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 89
REMARK 3 SOLVENT ATOMS : 156
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 53.3
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 1.42
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE FOLLOWING RESIDUES WERE
REMARK 3 ASSIGNED PARTIAL OCCUPANCY: VAL 1, ILE 2, ASN 136,
REMARK 3 THR 137, THR 138, BMA 995, BMA 996
REMARK 4
REMARK 4 1QON COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY EBI ON 16-NOV-1999.
REMARK 100 THE EBI ID CODE IS EBI-4374.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ELETTRA BEAMLINE 5.2R
REMARK 200 BEAMLINE : 5.2R
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19982
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.72
REMARK 200 RESOLUTION RANGE LOW (A) : 30.0
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NONE
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.8
REMARK 200 DATA REDUNDANCY : 1.8
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06
REMARK 200 FOR THE DATA SET : 15.5
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.72
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.8
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.2
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.25
REMARK 200 FOR SHELL : 2.4
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CCP4
REMARK 200 STARTING MODEL: 2ACE
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: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,1/2+Z
REMARK 290 3555 1/2-Y,1/2+X,3/4+Z
REMARK 290 4555 1/2+Y,1/2-X,1/4+Z
REMARK 290 5555 1/2-X,1/2+Y,3/4-Z
REMARK 290 6555 1/2+X,1/2-Y,1/4-Z
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,1/2-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 80.01000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 47.46500
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 47.46500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 120.01500
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 47.46500
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 47.46500
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 40.00500
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 47.46500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 47.46500
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 120.01500
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 47.46500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 47.46500
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 40.00500
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 80.01000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 1 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 LYS A 103
REMARK 465 ALA A 104
REMARK 465 ARG A 105
REMARK 465 LEU A 106
REMARK 465 ARG A 107
REMARK 465 HIS A 108
REMARK 465 GLY A 109
REMARK 465 ARG A 110
REMARK 465 GLY A 111
REMARK 465 ALA A 112
REMARK 465 ASN A 113
REMARK 465 GLY A 114
REMARK 465 GLY A 115
REMARK 465 GLU A 116
REMARK 465 HIS A 117
REMARK 465 PRO A 118
REMARK 465 ASN A 119
REMARK 465 GLY A 120
REMARK 465 LYS A 121
REMARK 465 GLN A 122
REMARK 465 ALA A 123
REMARK 465 ASP A 124
REMARK 465 THR A 125
REMARK 465 ASP A 126
REMARK 465 HIS A 127
REMARK 465 LEU A 128
REMARK 465 ILE A 129
REMARK 465 HIS A 130
REMARK 465 ASN A 131
REMARK 465 GLY A 132
REMARK 465 ASN A 133
REMARK 465 PRO A 134
REMARK 465 GLN A 135
REMARK 465 ALA A 574
REMARK 465 GLY A 575
REMARK 465 THR A 576
REMARK 465 CYS A 577
REMARK 465 ASP A 578
REMARK 465 GLY A 579
REMARK 465 ASP A 580
REMARK 465 SER A 581
REMARK 465 GLY A 582
REMARK 465 SER A 583
REMARK 465 LEU A 584
REMARK 465 ALA A 585
REMARK 465 SER A 586
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 ARG A 254 CZ NH1 NH2
REMARK 470 ARG A 454 NE CZ NH1 NH2
REMARK 470 GLU A 474 CD OE1 OE2
REMARK 470 TRP A 573 CG CD1 CD2 NE1 CE2 CE3 CZ2 CZ3 CH2
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 GLY A 151 CA - C - N ANGL. DEV. = 22.0 DEGREES
REMARK 500 GLY A 151 O - C - N ANGL. DEV. = -22.9 DEGREES
REMARK 500 PHE A 152 C - N - CA ANGL. DEV. = 36.2 DEGREES
REMARK 500 PHE A 187 N - CA - C ANGL. DEV. = 10.0 DEGREES
REMARK 500 GLY A 368 N - CA - C ANGL. DEV. = 10.6 DEGREES
REMARK 500 PRO A 423 N - CA - C ANGL. DEV. = -11.2 DEGREES
REMARK 500 LEU A 479 N - CA - C ANGL. DEV. = 10.9 DEGREES
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 AND BY MORE THAN 0.150 ANGSTROMS (M=MODEL
REMARK 500 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 500 NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,1X,2(A4,A1,3X),12X,F5.3)
REMARK 500
REMARK 500 EXPECTED VALUESS: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLY A 151 C PHE A 152 N -0.298
REMARK 500 THR A 154 C GLY A 155 N 0.156
REMARK 500 MET A 349 C LYS A 350 N -0.210
REMARK 500 ALA A 352 C ASP A 353 N 0.283
REMARK 500
REMARK 500 REMARK: NULL
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
REMARK 500 ND2 ASN A 205 OD2 ASP A 337 1.81
REMARK 500 OG SER A 238 O3 SO4 A 593 1.96
REMARK 500 OD2 ASP A 337 ND2 ASN A 205 1.81
REMARK 500 O2 BMA A 994 O2 BMA A 996 2.19
REMARK 500 O2 BMA A 996 O2 BMA A 994 2.19
REMARK 500 O3 SO4 A 593 OG SER A 238 1.96
REMARK 500 O HOH 51 O HOH 77 2.04
REMARK 500 O HOH 77 O HOH 51 2.04
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 M RES CSSEQI PSI PHI
REMARK 500
REMARK 500 GLU A 40 53.14 -106.81
REMARK 500 THR A 335 54.60 129.12
REMARK 500 ASN A 422 91.82 158.00
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLY A 151 PHE A 152 238.48
REMARK 525
REMARK 525 SOLVENT
REMARK 525 SOME ATOMS COULD NOT BE ASSIGNED TO THE OLIGOMER, BY ANY
REMARK 525 SYMMETRY OPERATION TO WITHIN 5.00 ANGSTROM
REMARK 525
REMARK 525 M RES CSSEQI X Y Z SYMM-TRANS CLOSEST
REMARK 525 DIST.
REMARK 525 1 HOH 746 52.114 45.635 26.713 0 5.7
REMARK 525 1 HOH 742 -5.239 80.628 -4.407 001 555 6.3
REMARK 525 1 HOH 606 0.048 94.996 -5.122 001 555 5.3
REMARK 525 1 HOH 702 27.371 91.341 10.767 001 555 5.1
REMARK 525 1 HOH 705 7.297 84.316 37.553 001 555 5.9
REMARK 525 1 HOH 618 43.266 57.011 5.531 001 555 5.4
REMARK 525 1 HOH 727 47.436 73.740 39.800 001 555 5.3
REMARK 525 1 HOH 728 10.340 87.592 25.012 001 555 6.9
REMARK 525 1 HOH 639 33.275 31.196 -4.596 001 555 6.5
REMARK 525 1 HOH 640 49.226 42.197 21.199 001 555 6.6
REMARK 525 1 HOH 654 10.462 81.139 -17.394 001 555 5.9
REMARK 525 1 HOH 661 22.978 30.532 20.211 001 555 5.6
REMARK 525 1 HOH 689 8.125 59.509 -12.553 001 555 5.1
REMARK 525 1 HOH 666 10.432 82.227 -14.184 001 555 5.3
REMARK 525
REMARK 525 THE FOLLOWING SOLVENT MOLECULES LIE FARTHER THAN EXPECTED
REMARK 525 FROM THE PROTEIN OR NUCLEIC ACID MOLECULE AND MAY BE
REMARK 525 ASSOCIATED WITH A SYMMETRY RELATED MOLECULE (M=MODEL
REMARK 525 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 THESE MOLECULES CAN BE PLACED WITHIN 5.00 ANGSTROM OF THE
REMARK 525 OBSERVED OLIGOMER BY APPLYING THE SYMMETRY TRANSFORMATION
REMARK 525 INDICATED.
REMARK 525
REMARK 525 M RES CSSEQI ORIGINAL COORDINATES SYMMETRY TRANS. DIST.
REMARK 525 X Y Z
REMARK 525 1 HOH 674 26.169 51.716 38.040 008 665 2.66
REMARK 525 1 HOH 703 42.113 73.847 44.668 008 665 3.98
REMARK 600
REMARK 600 HETEROGEN
REMARK 600 I40: TACRINE DERIVATIVE PUTATIVE INSECTICIDE
REMARK 600
REMARK 600 GLYCOSYLATION:
REMARK 600 THE SUGAR RESIDUES ATTACHED TO ASN 493 ARE ARRANGED
REMARK 600 AS FOLLOWS:
REMARK 600
REMARK 600 ASN 493
REMARK 600 (BETA 1,N) |
REMARK 600 NAG 991
REMARK 600 (BETA 1,4) |
REMARK 600 NAG 993
REMARK 600 (BETA 1,4) |
REMARK 600 BMA 994
REMARK 600 (BETA 1,3) / \(BETA 1,6)
REMARK 600 BMA 995 BMA 996
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 RESIDUES 103-135 ARE MISSING DUE TO DISORDER.
REMARK 999
DBREF 1QON A 1 586 SWS P07140 ACES_DROME 39 624
SEQADV 1QON LEU A 584 SWS P07140 ALA 622 CONFLICT
SEQADV 1QON ALA A 585 SWS P07140 SER 623 CONFLICT
SEQADV 1QON SER A 586 SWS P07140 ILE 624 CONFLICT
SEQRES 1 A 586 VAL ILE ASP ARG LEU VAL VAL GLN THR SER SER GLY PRO
SEQRES 2 A 586 VAL ARG GLY ARG SER VAL THR VAL GLN GLY ARG GLU VAL
SEQRES 3 A 586 HIS VAL TYR THR GLY ILE PRO TYR ALA LYS PRO PRO VAL
SEQRES 4 A 586 GLU ASP LEU ARG PHE ARG LYS PRO VAL PRO ALA GLU PRO
SEQRES 5 A 586 TRP HIS GLY VAL LEU ASP ALA THR GLY LEU SER ALA THR
SEQRES 6 A 586 CYS VAL GLN GLU ARG TYR GLU TYR PHE PRO GLY PHE SER
SEQRES 7 A 586 GLY GLU GLU ILE TRP ASN PRO ASN THR ASN VAL SER GLU
SEQRES 8 A 586 ASP CYS LEU TYR ILE ASN VAL TRP ALA PRO ALA LYS ALA
SEQRES 9 A 586 ARG LEU ARG HIS GLY ARG GLY ALA ASN GLY GLY GLU HIS
SEQRES 10 A 586 PRO ASN GLY LYS GLN ALA ASP THR ASP HIS LEU ILE HIS
SEQRES 11 A 586 ASN GLY ASN PRO GLN ASN THR THR ASN GLY LEU PRO ILE
SEQRES 12 A 586 LEU ILE TRP ILE TYR GLY GLY GLY PHE MET THR GLY SER
SEQRES 13 A 586 ALA THR LEU ASP ILE TYR ASN ALA ASP ILE MET ALA ALA
SEQRES 14 A 586 VAL GLY ASN VAL ILE VAL ALA SER PHE GLN TYR ARG VAL
SEQRES 15 A 586 GLY ALA PHE GLY PHE LEU HIS LEU ALA PRO GLU MET PRO
SEQRES 16 A 586 SER GLU PHE ALA GLU GLU ALA PRO GLY ASN VAL GLY LEU
SEQRES 17 A 586 TRP ASP GLN ALA LEU ALA ILE ARG TRP LEU LYS ASP ASN
SEQRES 18 A 586 ALA HIS ALA PHE GLY GLY ASN PRO GLU TRP MET THR LEU
SEQRES 19 A 586 PHE GLY GLU SER ALA GLY SER SER SER VAL ASN ALA GLN
SEQRES 20 A 586 LEU MET SER PRO VAL THR ARG GLY LEU VAL LYS ARG GLY
SEQRES 21 A 586 MET MET GLN SER GLY THR MET ASN ALA PRO TRP SER HIS
SEQRES 22 A 586 MET THR SER GLU LYS ALA VAL GLU ILE GLY LYS ALA LEU
SEQRES 23 A 586 ILE ASN ASP CYS ASN CYS ASN ALA SER MET LEU LYS THR
SEQRES 24 A 586 ASN PRO ALA HIS VAL MET SER CYS MET ARG SER VAL ASP
SEQRES 25 A 586 ALA LYS THR ILE SER VAL GLN GLN TRP ASN SER TYR SER
SEQRES 26 A 586 GLY ILE LEU SER PHE PRO SER ALA PRO THR ILE ASP GLY
SEQRES 27 A 586 ALA PHE LEU PRO ALA ASP PRO MET THR LEU MET LYS THR
SEQRES 28 A 586 ALA ASP LEU LYS ASP TYR ASP ILE LEU MET GLY ASN VAL
SEQRES 29 A 586 ARG ASP GLU GLY THR TYR PHE LEU LEU TYR ASP PHE ILE
SEQRES 30 A 586 ASP TYR PHE ASP LYS ASP ASP ALA THR ALA LEU PRO ARG
SEQRES 31 A 586 ASP LYS TYR LEU GLU ILE MET ASN ASN ILE PHE GLY LYS
SEQRES 32 A 586 ALA THR GLN ALA GLU ARG GLU ALA ILE ILE PHE GLN TYR
SEQRES 33 A 586 THR SER TRP GLU GLY ASN PRO GLY TYR GLN ASN GLN GLN
SEQRES 34 A 586 GLN ILE GLY ARG ALA VAL GLY ASP HIS PHE PHE THR CYS
SEQRES 35 A 586 PRO THR ASN GLU TYR ALA GLN ALA LEU ALA GLU ARG GLY
SEQRES 36 A 586 ALA SER VAL HIS TYR TYR TYR PHE THR HIS ARG THR SER
SEQRES 37 A 586 THR SER LEU TRP GLY GLU TRP MET GLY VAL LEU HIS GLY
SEQRES 38 A 586 ASP GLU ILE GLU TYR PHE PHE GLY GLN PRO LEU ASN ASN
SEQRES 39 A 586 SER LEU GLN TYR ARG PRO VAL GLU ARG GLU LEU GLY LYS
SEQRES 40 A 586 ARG MET LEU SER ALA VAL ILE GLU PHE ALA LYS THR GLY
SEQRES 41 A 586 ASN PRO ALA GLN ASP GLY GLU GLU TRP PRO ASN PHE SER
SEQRES 42 A 586 LYS GLU ASP PRO VAL TYR TYR ILE PHE SER THR ASP ASP
SEQRES 43 A 586 LYS ILE GLU LYS LEU ALA ARG GLY PRO LEU ALA ALA ARG
SEQRES 44 A 586 CYS SER PHE TRP ASN ASP TYR LEU PRO LYS VAL ARG SER
SEQRES 45 A 586 TRP ALA GLY THR CYS ASP GLY ASP SER GLY SER LEU ALA
SEQRES 46 A 586 SER
HET NAG A 991 14
HET NAG A 993 14
HET BMA A 994 11
HET BMA A 995 11
HET BMA A 996 11
HET SO4 A 593 5
HET I40 A 997 23 SEE REMARK 600
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM BMA BETA-D-MANNOSE
HETNAM SO4 SULFATE ION
HETNAM I40 9-(3-IODOBENZYLAMINO)-1,2,3,4-TETRAHYDROACRIDINE
FORMUL 2 NAG 2(C8 H15 N1 O6)
FORMUL 3 BMA 3(C6 H12 O6)
FORMUL 4 SO4 O4 S1 2-
FORMUL 5 I40 C20 H19 N2 I1 1+
FORMUL 6 HOH *156(H2 O1)
HELIX 1 1 VAL A 39 ARG A 43 5 5
HELIX 2 2 PHE A 77 ILE A 82 1 6
HELIX 3 3 LEU A 159 ASN A 163 5 5
HELIX 4 4 ALA A 164 ASN A 172 1 9
HELIX 5 5 GLY A 183 LEU A 188 1 6
HELIX 6 6 LEU A 190 MET A 194 5 5
HELIX 7 7 PRO A 195 ALA A 202 5 8
HELIX 8 8 ASN A 205 ALA A 222 1 18
HELIX 9 9 HIS A 223 PHE A 225 5 3
HELIX 10 10 SER A 238 SER A 250 1 13
HELIX 11 11 THR A 275 CYS A 290 1 16
HELIX 12 12 ASN A 293 LEU A 297 5 5
HELIX 13 13 ASN A 300 ARG A 309 1 10
HELIX 14 14 ASP A 312 GLN A 320 1 9
HELIX 15 15 TRP A 321 TYR A 324 5 4
HELIX 16 16 LEU A 348 ALA A 352 5 5
HELIX 17 17 GLY A 368 PHE A 376 1 9
HELIX 18 18 PRO A 389 PHE A 401 1 13
HELIX 19 19 THR A 405 TYR A 416 1 12
HELIX 20 20 GLY A 424 PHE A 440 1 17
HELIX 21 21 PHE A 440 ARG A 454 1 15
HELIX 22 22 GLY A 473 GLY A 477 5 5
HELIX 23 23 ASP A 482 PHE A 488 1 7
HELIX 24 24 GLY A 489 ASN A 493 5 5
HELIX 25 25 ARG A 499 GLY A 520 1 22
HELIX 26 26 ARG A 553 ASP A 565 1 13
HELIX 27 27 TYR A 566 ARG A 571 1 6
SHEET 1 A 2 VAL A 6 THR A 9 0
SHEET 2 A 2 GLY A 12 ARG A 15 -1 N VAL A 14 O VAL A 7
SHEET 1 B 8 SER A 18 VAL A 21 0
SHEET 2 B 8 ARG A 24 PRO A 33 -1 N VAL A 26 O VAL A 19
SHEET 3 B 8 TYR A 95 PRO A 101 -1 N ALA A 100 O HIS A 27
SHEET 4 B 8 ILE A 174 PHE A 178 -1 N SER A 177 O ASN A 97
SHEET 5 B 8 ILE A 143 ILE A 147 1 N LEU A 144 O ILE A 174
SHEET 6 B 8 MET A 232 GLU A 237 1 N THR A 233 O ILE A 143
SHEET 7 B 8 ARG A 259 GLN A 263 1 N MET A 261 O LEU A 234
SHEET 8 B 8 ASP A 358 GLY A 362 1 N ASP A 358 O GLY A 260
SHEET 1 C 2 TYR A 460 PHE A 463 0
SHEET 2 C 2 TYR A 539 PHE A 542 1 N TYR A 540 O TYR A 460
SSBOND 1 CYS A 66 CYS A 93
SSBOND 2 CYS A 292 CYS A 307
SSBOND 3 CYS A 442 CYS A 560
LINK ND2 ASN A 493 C1 NAG A 991
LINK O4 NAG A 991 C1 NAG A 993
LINK O4 NAG A 993 C1 BMA A 994
LINK O3 BMA A 994 C1 BMA A 996
LINK O6 BMA A 994 C1 BMA A 995
CRYST1 94.930 94.930 160.020 90.00 90.00 90.00 P 43 21 2 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 0.010534 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010534 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006249 0.00000 |