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HEADER HYDROLASE 31-JAN-20 6XYY
TITLE UPDATE OF ACHE FROM DROSOPHILA MELANOGASTER COMPLEX WITH TACRINE
TITLE 2 DERIVATIVE 9-(3-PHENYLMETHYLAMINO)-1,2,3,4-TETRAHYDROACRIDINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYLCHOLINESTERASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ACHE;
COMPND 5 EC: 3.1.1.7;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;
SOURCE 3 ORGANISM_COMMON: FRUIT FLY;
SOURCE 4 ORGANISM_TAXID: 7227;
SOURCE 5 GENE: ACE, CG17907;
SOURCE 6 EXPRESSION_SYSTEM: DROSOPHILA MELANOGASTER;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7227;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: SCHNEIDER LINE 2;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: S2-SEC 1/3
KEYWDS ACETYLCHOLINESTERASE, INSECT, INHIBITOR, COMPLEX, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR F.NACHON,J.L.SUSSMAN
REVDAT 1 18-MAR-20 6XYY 0
SPRSDE 18-MAR-20 6XYY 1DX4
JRNL AUTH F.NACHON,T.L.ROSENBERRY,I.SILMAN,J.L.SUSSMAN
JRNL TITL A SECOND LOOK AT THE CRYSTAL STRUCTURES OFDROSOPHILA
JRNL TITL 2 MELANOGASTERACETYLCHOLINESTERASE IN COMPLEX WITH TACRINE
JRNL TITL 3 DERIVATIVES PROVIDES INSIGHTS CONCERNING CATALYTIC
JRNL TITL 4 INTERMEDIATES AND THE DESIGN OF SPECIFIC INSECTICIDES.
JRNL REF MOLECULES V. 25 2020
JRNL REFN ESSN 1420-3049
JRNL PMID 32155891
JRNL DOI 10.3390/MOLECULES25051198
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.16_3549
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.78
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.1
REMARK 3 NUMBER OF REFLECTIONS : 20577
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.178
REMARK 3 R VALUE (WORKING SET) : 0.172
REMARK 3 FREE R VALUE : 0.234
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.870
REMARK 3 FREE R VALUE TEST SET COUNT : 2030
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 29.7800 - 6.6400 0.92 1324 126 0.1726 0.2252
REMARK 3 2 6.6400 - 5.2800 0.96 1274 141 0.1599 0.2089
REMARK 3 3 5.2800 - 4.6100 0.97 1256 158 0.1242 0.1764
REMARK 3 4 4.6100 - 4.1900 0.98 1262 136 0.1236 0.1500
REMARK 3 5 4.1900 - 3.8900 0.98 1253 153 0.1389 0.2079
REMARK 3 6 3.8900 - 3.6600 0.98 1276 115 0.1553 0.2325
REMARK 3 7 3.6600 - 3.4800 0.98 1251 148 0.1655 0.2493
REMARK 3 8 3.4800 - 3.3300 0.98 1251 129 0.1954 0.2475
REMARK 3 9 3.3300 - 3.2000 0.98 1261 116 0.2035 0.2920
REMARK 3 10 3.2000 - 3.0900 0.98 1234 137 0.2167 0.3036
REMARK 3 11 3.0900 - 2.9900 0.98 1232 148 0.2202 0.3139
REMARK 3 12 2.9900 - 2.9100 0.98 1253 119 0.2141 0.3369
REMARK 3 13 2.9100 - 2.8300 0.97 1218 135 0.2479 0.3097
REMARK 3 14 2.8300 - 2.7600 0.93 1167 134 0.2644 0.3291
REMARK 3 15 2.7600 - 2.7000 0.84 1035 135 0.2984 0.3878
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.354
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.901
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 50.19
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 56.87
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.008 4458
REMARK 3 ANGLE : 0.891 6069
REMARK 3 CHIRALITY : 0.057 642
REMARK 3 PLANARITY : 0.006 787
REMARK 3 DIHEDRAL : 5.440 3572
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 3 THROUGH 343 )
REMARK 3 ORIGIN FOR THE GROUP (A): 20.4339 65.3097 -0.3918
REMARK 3 T TENSOR
REMARK 3 T11: 0.2704 T22: 0.3521
REMARK 3 T33: 0.2505 T12: 0.0398
REMARK 3 T13: 0.0074 T23: 0.0036
REMARK 3 L TENSOR
REMARK 3 L11: 2.4913 L22: 2.5840
REMARK 3 L33: 3.2513 L12: -0.9986
REMARK 3 L13: 0.9226 L23: -0.6562
REMARK 3 S TENSOR
REMARK 3 S11: 0.0640 S12: 0.4144 S13: 0.0542
REMARK 3 S21: -0.3600 S22: -0.1978 S23: 0.0632
REMARK 3 S31: -0.1859 S32: 0.3883 S33: 0.1200
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 344 THROUGH 375 )
REMARK 3 ORIGIN FOR THE GROUP (A): 20.1177 61.7308 18.2561
REMARK 3 T TENSOR
REMARK 3 T11: 0.2404 T22: 0.4139
REMARK 3 T33: 0.5017 T12: 0.0210
REMARK 3 T13: 0.0456 T23: -0.0368
REMARK 3 L TENSOR
REMARK 3 L11: 1.7800 L22: 2.7227
REMARK 3 L33: 2.9743 L12: 0.4163
REMARK 3 L13: 1.8561 L23: 0.0934
REMARK 3 S TENSOR
REMARK 3 S11: -0.0395 S12: -0.1859 S13: 0.2842
REMARK 3 S21: -0.0478 S22: -0.0806 S23: 0.6991
REMARK 3 S31: -0.1635 S32: -0.2427 S33: 0.0677
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 376 THROUGH 499 )
REMARK 3 ORIGIN FOR THE GROUP (A): 33.2260 66.0916 23.1430
REMARK 3 T TENSOR
REMARK 3 T11: 0.3454 T22: 0.3740
REMARK 3 T33: 0.2863 T12: 0.0072
REMARK 3 T13: -0.0125 T23: 0.0397
REMARK 3 L TENSOR
REMARK 3 L11: 2.1856 L22: 2.6105
REMARK 3 L33: 3.5756 L12: -0.4522
REMARK 3 L13: 0.7775 L23: 0.5380
REMARK 3 S TENSOR
REMARK 3 S11: -0.2684 S12: -0.1763 S13: 0.1377
REMARK 3 S21: 0.1126 S22: 0.1181 S23: -0.3298
REMARK 3 S31: -0.5387 S32: 0.4582 S33: 0.1830
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 500 THROUGH 573 )
REMARK 3 ORIGIN FOR THE GROUP (A): 26.1374 51.9406 24.2868
REMARK 3 T TENSOR
REMARK 3 T11: 0.2996 T22: 0.2939
REMARK 3 T33: 0.3291 T12: 0.0173
REMARK 3 T13: 0.0674 T23: 0.1252
REMARK 3 L TENSOR
REMARK 3 L11: 2.4475 L22: 2.1701
REMARK 3 L33: 3.7080 L12: 0.0773
REMARK 3 L13: 1.0843 L23: -0.1765
REMARK 3 S TENSOR
REMARK 3 S11: -0.0950 S12: -0.3894 S13: -0.4287
REMARK 3 S21: 0.1798 S22: 0.0318 S23: 0.1442
REMARK 3 S31: 0.4063 S32: 0.0532 S33: -0.0231
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6XYY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-FEB-20.
REMARK 100 THE DEPOSITION ID IS D_1292106562.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JUN-99
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 : 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) : 0.98
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : BRANDEIS B4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20596
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 29.780
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.0
REMARK 200 DATA REDUNDANCY : 5.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 24.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.80
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 : 3.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 1QON
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.03
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.86
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 13% MPEG2000, 0.1 M AMMONIUM SULFATE,
REMARK 280 0.03 M LEUCINE, 0.1 M ACETATE, PH 4.6, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 292K
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,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 81.01500
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 47.90500
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 47.90500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 121.52250
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 47.90500
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 47.90500
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 40.50750
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 47.90500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 47.90500
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 121.52250
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 47.90500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 47.90500
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 40.50750
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 81.01500
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 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 S SO4 A 608 LIES ON A SPECIAL POSITION.
REMARK 375 CL CL A 609 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 741 LIES ON A SPECIAL POSITION.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 VAL A 1
REMARK 465 ILE A 2
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 ASN A 136
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 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 OG SER A 238 C1 PPI A 601 1.63
REMARK 500 O3 MAN A 605 O5 MAN A 606 1.95
REMARK 500 O4 NAG A 603 O5 NAG A 604 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O1 SO4 A 608 O4 SO4 A 608 7555 0.01
REMARK 500 O2 SO4 A 608 O3 SO4 A 608 7555 0.01
REMARK 500 S SO4 A 608 O2 SO4 A 608 7555 1.46
REMARK 500 S SO4 A 608 O3 SO4 A 608 7555 1.46
REMARK 500 S SO4 A 608 O1 SO4 A 608 7555 1.46
REMARK 500 S SO4 A 608 O4 SO4 A 608 7555 1.46
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 GLU A 40 -137.20 61.23
REMARK 500 PHE A 44 -13.42 70.43
REMARK 500 THR A 138 -26.96 118.36
REMARK 500 ASN A 139 33.72 -99.73
REMARK 500 PHE A 152 12.20 59.75
REMARK 500 ALA A 202 74.33 -157.80
REMARK 500 TRP A 231 53.44 -115.95
REMARK 500 SER A 238 -125.15 53.42
REMARK 500 ASN A 293 96.82 -59.60
REMARK 500 SER A 325 -70.32 -93.54
REMARK 500 ALA A 339 -87.11 -126.44
REMARK 500 PRO A 345 4.67 -60.80
REMARK 500 THR A 351 -73.04 -97.38
REMARK 500 PHE A 440 -68.40 -132.75
REMARK 500 SER A 572 81.50 -67.93
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PPI A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 760 A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 608
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 607 bound
REMARK 800 to ASN A 88
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A
REMARK 800 603 through MAN A 606 bound to ASN A 493
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1DX4 RELATED DB: PDB
REMARK 900 EARLIER MODEL
REMARK 900 RELATED ID: 6XYS RELATED DB: PDB
REMARK 900 NATIVE ENZYME
REMARK 900 RELATED ID: 6XYU RELATED DB: PDB
REMARK 900 SAME PROTEIN WITH SIMILAR LIGAND
DBREF 6XYY A 1 581 UNP P07140 ACES_DROME 39 619
SEQRES 1 A 581 VAL ILE ASP ARG LEU VAL VAL GLN THR SER SER GLY PRO
SEQRES 2 A 581 VAL ARG GLY ARG SER VAL THR VAL GLN GLY ARG GLU VAL
SEQRES 3 A 581 HIS VAL TYR THR GLY ILE PRO TYR ALA LYS PRO PRO VAL
SEQRES 4 A 581 GLU ASP LEU ARG PHE ARG LYS PRO VAL PRO ALA GLU PRO
SEQRES 5 A 581 TRP HIS GLY VAL LEU ASP ALA THR GLY LEU SER ALA THR
SEQRES 6 A 581 CYS VAL GLN GLU ARG TYR GLU TYR PHE PRO GLY PHE SER
SEQRES 7 A 581 GLY GLU GLU ILE TRP ASN PRO ASN THR ASN VAL SER GLU
SEQRES 8 A 581 ASP CYS LEU TYR ILE ASN VAL TRP ALA PRO ALA LYS ALA
SEQRES 9 A 581 ARG LEU ARG HIS GLY ARG GLY ALA ASN GLY GLY GLU HIS
SEQRES 10 A 581 PRO ASN GLY LYS GLN ALA ASP THR ASP HIS LEU ILE HIS
SEQRES 11 A 581 ASN GLY ASN PRO GLN ASN THR THR ASN GLY LEU PRO ILE
SEQRES 12 A 581 LEU ILE TRP ILE TYR GLY GLY GLY PHE MET THR GLY SER
SEQRES 13 A 581 ALA THR LEU ASP ILE TYR ASN ALA ASP ILE MET ALA ALA
SEQRES 14 A 581 VAL GLY ASN VAL ILE VAL ALA SER PHE GLN TYR ARG VAL
SEQRES 15 A 581 GLY ALA PHE GLY PHE LEU HIS LEU ALA PRO GLU MET PRO
SEQRES 16 A 581 SER GLU PHE ALA GLU GLU ALA PRO GLY ASN VAL GLY LEU
SEQRES 17 A 581 TRP ASP GLN ALA LEU ALA ILE ARG TRP LEU LYS ASP ASN
SEQRES 18 A 581 ALA HIS ALA PHE GLY GLY ASN PRO GLU TRP MET THR LEU
SEQRES 19 A 581 PHE GLY GLU SER ALA GLY SER SER SER VAL ASN ALA GLN
SEQRES 20 A 581 LEU MET SER PRO VAL THR ARG GLY LEU VAL LYS ARG GLY
SEQRES 21 A 581 MET MET GLN SER GLY THR MET ASN ALA PRO TRP SER HIS
SEQRES 22 A 581 MET THR SER GLU LYS ALA VAL GLU ILE GLY LYS ALA LEU
SEQRES 23 A 581 ILE ASN ASP CYS ASN CYS ASN ALA SER MET LEU LYS THR
SEQRES 24 A 581 ASN PRO ALA HIS VAL MET SER CYS MET ARG SER VAL ASP
SEQRES 25 A 581 ALA LYS THR ILE SER VAL GLN GLN TRP ASN SER TYR SER
SEQRES 26 A 581 GLY ILE LEU SER PHE PRO SER ALA PRO THR ILE ASP GLY
SEQRES 27 A 581 ALA PHE LEU PRO ALA ASP PRO MET THR LEU MET LYS THR
SEQRES 28 A 581 ALA ASP LEU LYS ASP TYR ASP ILE LEU MET GLY ASN VAL
SEQRES 29 A 581 ARG ASP GLU GLY THR TYR PHE LEU LEU TYR ASP PHE ILE
SEQRES 30 A 581 ASP TYR PHE ASP LYS ASP ASP ALA THR ALA LEU PRO ARG
SEQRES 31 A 581 ASP LYS TYR LEU GLU ILE MET ASN ASN ILE PHE GLY LYS
SEQRES 32 A 581 ALA THR GLN ALA GLU ARG GLU ALA ILE ILE PHE GLN TYR
SEQRES 33 A 581 THR SER TRP GLU GLY ASN PRO GLY TYR GLN ASN GLN GLN
SEQRES 34 A 581 GLN ILE GLY ARG ALA VAL GLY ASP HIS PHE PHE THR CYS
SEQRES 35 A 581 PRO THR ASN GLU TYR ALA GLN ALA LEU ALA GLU ARG GLY
SEQRES 36 A 581 ALA SER VAL HIS TYR TYR TYR PHE THR HIS ARG THR SER
SEQRES 37 A 581 THR SER LEU TRP GLY GLU TRP MET GLY VAL LEU HIS GLY
SEQRES 38 A 581 ASP GLU ILE GLU TYR PHE PHE GLY GLN PRO LEU ASN ASN
SEQRES 39 A 581 SER LEU GLN TYR ARG PRO VAL GLU ARG GLU LEU GLY LYS
SEQRES 40 A 581 ARG MET LEU SER ALA VAL ILE GLU PHE ALA LYS THR GLY
SEQRES 41 A 581 ASN PRO ALA GLN ASP GLY GLU GLU TRP PRO ASN PHE SER
SEQRES 42 A 581 LYS GLU ASP PRO VAL TYR TYR ILE PHE SER THR ASP ASP
SEQRES 43 A 581 LYS ILE GLU LYS LEU ALA ARG GLY PRO LEU ALA ALA ARG
SEQRES 44 A 581 CYS SER PHE TRP ASN ASP TYR LEU PRO LYS VAL ARG SER
SEQRES 45 A 581 TRP ALA GLY THR CYS ASP GLY ASP SER
HET PPI A 601 5
HET 760 A 602 22
HET NAG A 603 14
HET NAG A 604 14
HET MAN A 605 11
HET MAN A 606 11
HET NAG A 607 14
HET SO4 A 608 5
HET CL A 609 1
HETNAM PPI PROPANOIC ACID
HETNAM 760 9-(3-PHENYLMETHYLAMINO)-1,2,3,4-TETRAHYDROACRIDINE
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM MAN ALPHA-D-MANNOSE
HETNAM SO4 SULFATE ION
HETNAM CL CHLORIDE ION
HETSYN 760 9-N-PHENYLMETHYLAMINO-TACRINE
FORMUL 2 PPI C3 H6 O2
FORMUL 3 760 C20 H20 N2
FORMUL 4 NAG 3(C8 H15 N O6)
FORMUL 4 MAN 2(C6 H12 O6)
FORMUL 6 SO4 O4 S 2-
FORMUL 7 CL CL 1-
FORMUL 8 HOH *144(H2 O)
HELIX 1 AA1 VAL A 39 ARG A 43 5 5
HELIX 2 AA2 PHE A 77 ILE A 82 1 6
HELIX 3 AA3 LEU A 159 ASN A 163 5 5
HELIX 4 AA4 ALA A 164 ASN A 172 1 9
HELIX 5 AA5 GLY A 183 LEU A 188 1 6
HELIX 6 AA6 LEU A 190 MET A 194 5 5
HELIX 7 AA7 PRO A 195 ALA A 202 5 8
HELIX 8 AA8 ASN A 205 ALA A 222 1 18
HELIX 9 AA9 HIS A 223 PHE A 225 5 3
HELIX 10 AB1 SER A 238 SER A 250 1 13
HELIX 11 AB2 ALA A 269 HIS A 273 5 5
HELIX 12 AB3 THR A 275 CYS A 290 1 16
HELIX 13 AB4 ASN A 293 LYS A 298 5 6
HELIX 14 AB5 ASN A 300 ARG A 309 1 10
HELIX 15 AB6 ASP A 312 GLN A 320 1 9
HELIX 16 AB7 TRP A 321 TYR A 324 5 4
HELIX 17 AB8 GLY A 368 PHE A 376 1 9
HELIX 18 AB9 PRO A 389 PHE A 401 1 13
HELIX 19 AC1 THR A 405 TYR A 416 1 12
HELIX 20 AC2 ASN A 422 PHE A 440 1 19
HELIX 21 AC3 PHE A 440 ARG A 454 1 15
HELIX 22 AC4 GLY A 473 GLY A 477 5 5
HELIX 23 AC5 GLU A 483 PHE A 488 1 6
HELIX 24 AC6 GLY A 489 ASN A 493 5 5
HELIX 25 AC7 ARG A 499 GLY A 520 1 22
HELIX 26 AC8 ARG A 553 ASP A 565 1 13
HELIX 27 AC9 TYR A 566 SER A 572 1 7
SHEET 1 AA1 3 VAL A 6 THR A 9 0
SHEET 2 AA1 3 GLY A 12 ARG A 15 -1 O VAL A 14 N VAL A 7
SHEET 3 AA1 3 LEU A 57 ASP A 58 1 O LEU A 57 N PRO A 13
SHEET 1 AA211 ARG A 17 VAL A 21 0
SHEET 2 AA211 ARG A 24 PRO A 33 -1 O VAL A 28 N ARG A 17
SHEET 3 AA211 TYR A 95 PRO A 101 -1 O ALA A 100 N HIS A 27
SHEET 4 AA211 ILE A 174 PHE A 178 -1 O SER A 177 N ASN A 97
SHEET 5 AA211 LEU A 141 ILE A 147 1 N LEU A 144 O ILE A 174
SHEET 6 AA211 GLY A 227 GLU A 237 1 O ASN A 228 N LEU A 141
SHEET 7 AA211 ARG A 259 GLN A 263 1 O GLN A 263 N GLY A 236
SHEET 8 AA211 ASP A 358 VAL A 364 1 O ASP A 358 N GLY A 260
SHEET 9 AA211 SER A 457 PHE A 463 1 O PHE A 463 N ASN A 363
SHEET 10 AA211 TYR A 539 PHE A 542 1 O PHE A 542 N TYR A 462
SHEET 11 AA211 LEU A 551 ALA A 552 -1 O ALA A 552 N TYR A 539
SSBOND 1 CYS A 66 CYS A 93 1555 1555 2.08
SSBOND 2 CYS A 292 CYS A 307 1555 1555 2.05
SSBOND 3 CYS A 442 CYS A 560 1555 1555 2.03
LINK ND2 ASN A 88 C1 NAG A 607 1555 1555 1.45
LINK ND2 ASN A 493 C1 NAG A 603 1555 1555 1.44
LINK O4 NAG A 603 C1 NAG A 604 1555 1555 1.37
LINK O4 NAG A 604 C1 MAN A 605 1555 1555 1.37
LINK O3 MAN A 605 C1 MAN A 606 1555 1555 1.38
SITE 1 AC1 8 GLY A 150 GLY A 151 SER A 238 ALA A 239
SITE 2 AC1 8 TRP A 271 PHE A 371 HIS A 480 760 A 602
SITE 1 AC2 11 TYR A 71 TRP A 83 GLY A 150 GLY A 151
SITE 2 AC2 11 GLU A 237 TYR A 370 TRP A 472 HIS A 480
SITE 3 AC2 11 PPI A 601 HOH A 704 HOH A 749
SITE 1 AC3 2 GLN A 22 ASN A 494
SITE 1 AC4 1 ASN A 88
SITE 1 AC5 7 VAL A 21 THR A 60 GLY A 61 LEU A 62
SITE 2 AC5 7 ASN A 493 LEU A 496 HOH A 772
CRYST1 95.810 95.810 162.030 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 0.010437 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010437 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006172 0.00000
TER 4242 TRP A 573
MASTER 438 0 9 27 14 0 9 6 4472 1 104 45
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