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HEADER HYDROLASE 31-JAN-20 6XYS
TITLE UPDATE OF NATIVE ACETYLCHOLINESTERASE FROM DROSOPHILA MELANOGASTER
CAVEAT 6XYS NAG A 602 HAS WRONG CHIRALITY AT ATOM C1 BMA A 604 HAS WRONG
CAVEAT 2 6XYS CHIRALITY AT ATOM C1
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_COMMON: FRUIT FLY;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7227;
SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: SCHNEIDER LINE 2;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID DNA;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: S2-SEC 1/3
KEYWDS ACETYLCHOLINESTERASE, INSECT, CATALYTIC, INTERMEDIATES, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR F.NACHON,J.L.SUSSMAN
REVDAT 1 18-MAR-20 6XYS 0
SPRSDE 18-MAR-20 6XYS 1QO9
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 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.HAREL,G.KRYGER,T.L.ROSENBERRY,W.D.MALLENDER,T.LEWIS,
REMARK 1 AUTH 2 R.J.FLETCHER,J.M.GUSS,I.SILMAN,J.L.SUSSMAN
REMARK 1 TITL THREE-DIMENSIONAL STRUCTURES OF DROSOPHILA MELANOGASTER
REMARK 1 TITL 2 ACETYLCHOLINESTERASE AND OF ITS COMPLEXES WITH TWO POTENT
REMARK 1 TITL 3 INHIBITORS.
REMARK 1 REF PROTEIN SCI. V. 9 1063 2000
REMARK 1 REFN ISSN 0961-8368
REMARK 1 PMID 10892800
REMARK 1 DOI 10.1110/PS.9.6.1063
REMARK 2
REMARK 2 RESOLUTION. 2.46 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) : 2.46
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.18
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 3 NUMBER OF REFLECTIONS : 26738
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.233
REMARK 3 R VALUE (WORKING SET) : 0.229
REMARK 3 FREE R VALUE : 0.296
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1338
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 34.1800 - 5.2800 0.97 2694 142 0.1736 0.1928
REMARK 3 2 5.2800 - 4.2000 0.99 2588 136 0.1646 0.2317
REMARK 3 3 4.2000 - 3.6700 0.99 2576 136 0.1971 0.2727
REMARK 3 4 3.6700 - 3.3300 0.99 2551 134 0.2469 0.3641
REMARK 3 5 3.3300 - 3.0900 1.00 2547 135 0.2885 0.3737
REMARK 3 6 3.0900 - 2.9100 1.00 2521 132 0.3123 0.3960
REMARK 3 7 2.9100 - 2.7600 0.99 2520 134 0.3161 0.3719
REMARK 3 8 2.7600 - 2.6400 0.99 2496 131 0.3357 0.4093
REMARK 3 9 2.6400 - 2.5400 0.99 2504 132 0.3526 0.4409
REMARK 3 10 2.5400 - 2.4600 0.95 2403 126 0.3994 0.5233
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) : 0.442
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 38.130
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 51.47
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 79.57
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 4427
REMARK 3 ANGLE : 1.044 6026
REMARK 3 CHIRALITY : 0.056 638
REMARK 3 PLANARITY : 0.007 783
REMARK 3 DIHEDRAL : 7.681 3561
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 5
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 3 THROUGH 94 )
REMARK 3 ORIGIN FOR THE GROUP (A): 26.6830 61.2624 -7.5890
REMARK 3 T TENSOR
REMARK 3 T11: 0.7632 T22: 0.8266
REMARK 3 T33: 0.5430 T12: -0.2579
REMARK 3 T13: 0.1959 T23: -0.0706
REMARK 3 L TENSOR
REMARK 3 L11: 2.6415 L22: 2.3309
REMARK 3 L33: 3.6014 L12: -0.6662
REMARK 3 L13: -0.2308 L23: 0.7659
REMARK 3 S TENSOR
REMARK 3 S11: 0.4753 S12: 0.3436 S13: 0.1676
REMARK 3 S21: -1.0063 S22: -0.0360 S23: -0.3271
REMARK 3 S31: -0.7755 S32: 1.3245 S33: -0.1818
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 95 THROUGH 289 )
REMARK 3 ORIGIN FOR THE GROUP (A): 17.7086 61.6307 2.9363
REMARK 3 T TENSOR
REMARK 3 T11: 0.5204 T22: 0.4012
REMARK 3 T33: 0.4651 T12: -0.1633
REMARK 3 T13: 0.0539 T23: -0.0885
REMARK 3 L TENSOR
REMARK 3 L11: 2.0066 L22: 3.1076
REMARK 3 L33: 4.5143 L12: -1.1492
REMARK 3 L13: -0.2085 L23: 0.5012
REMARK 3 S TENSOR
REMARK 3 S11: 0.1669 S12: -0.0664 S13: 0.1285
REMARK 3 S21: -0.5914 S22: 0.0984 S23: 0.0465
REMARK 3 S31: -0.8202 S32: 0.8442 S33: -0.1299
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 290 THROUGH 375 )
REMARK 3 ORIGIN FOR THE GROUP (A): 17.9854 73.0646 8.2711
REMARK 3 T TENSOR
REMARK 3 T11: 1.0431 T22: 0.4697
REMARK 3 T33: 0.6005 T12: -0.3067
REMARK 3 T13: 0.1213 T23: -0.0827
REMARK 3 L TENSOR
REMARK 3 L11: 1.9121 L22: 1.9024
REMARK 3 L33: 3.2924 L12: -0.7358
REMARK 3 L13: 0.1496 L23: -0.0034
REMARK 3 S TENSOR
REMARK 3 S11: -0.0455 S12: -0.1075 S13: 0.4771
REMARK 3 S21: -0.3384 S22: 0.1423 S23: -0.2176
REMARK 3 S31: -1.5201 S32: 0.8372 S33: -0.0840
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 376 THROUGH 499 )
REMARK 3 ORIGIN FOR THE GROUP (A): 32.8334 65.2159 22.7449
REMARK 3 T TENSOR
REMARK 3 T11: 0.6375 T22: 1.1942
REMARK 3 T33: 0.6610 T12: -0.2145
REMARK 3 T13: 0.0603 T23: -0.2331
REMARK 3 L TENSOR
REMARK 3 L11: 1.2650 L22: 1.8506
REMARK 3 L33: 2.1336 L12: -0.6171
REMARK 3 L13: 0.1477 L23: 0.5357
REMARK 3 S TENSOR
REMARK 3 S11: -0.1498 S12: -0.1289 S13: 0.2926
REMARK 3 S21: 0.0407 S22: 0.5146 S23: -0.5664
REMARK 3 S31: -0.6561 S32: 1.1918 S33: -0.2971
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 500 THROUGH 573 )
REMARK 3 ORIGIN FOR THE GROUP (A): 25.8591 51.3858 23.6718
REMARK 3 T TENSOR
REMARK 3 T11: 0.3681 T22: 0.9799
REMARK 3 T33: 0.5214 T12: 0.1549
REMARK 3 T13: 0.0325 T23: -0.0235
REMARK 3 L TENSOR
REMARK 3 L11: 1.6718 L22: 1.1280
REMARK 3 L33: 3.7980 L12: 0.1691
REMARK 3 L13: -0.1107 L23: 0.3134
REMARK 3 S TENSOR
REMARK 3 S11: -0.2620 S12: -0.3513 S13: -0.1927
REMARK 3 S21: 0.1224 S22: 0.3462 S23: -0.2167
REMARK 3 S31: 0.3685 S32: 1.1307 S33: -0.2148
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 6XYS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 31-JAN-20.
REMARK 100 THE DEPOSITION ID IS D_1292106538.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-JAN-98
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
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 : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26803
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.455
REMARK 200 RESOLUTION RANGE LOW (A) : 34.180
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 200 DATA REDUNDANCY : 6.000
REMARK 200 R MERGE (I) : 0.04870
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 20.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.46
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.54
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.33500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.300
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: 1QO9
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.83
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.72
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 79.50500
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 47.31000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 47.31000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 119.25750
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 47.31000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 47.31000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 39.75250
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 47.31000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 47.31000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 119.25750
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 47.31000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 47.31000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 39.75250
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 79.50500
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1550 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20720 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 13.0 KCAL/MOL
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 CL CL A 606 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 708 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 THR A 137
REMARK 465 THR A 138
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 O3 MAN A 603 O5 BMA A 604 1.93
REMARK 500 OD2 ASP A 482 O HOH A 701 2.07
REMARK 500 OH TYR A 461 O HOH A 702 2.07
REMARK 500 O GLU A 72 O HOH A 703 2.11
REMARK 500 OD1 ASP A 92 OH TYR A 95 2.11
REMARK 500 NH1 ARG A 254 O HOH A 704 2.12
REMARK 500 OD1 ASP A 378 O HOH A 705 2.13
REMARK 500 O PHE A 380 O HOH A 706 2.14
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 N HIS A 303 NZ LYS A 547 3554 1.89
REMARK 500 OD1 ASN A 300 CE LYS A 547 3554 2.08
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 -109.41 57.73
REMARK 500 PHE A 44 -3.65 76.22
REMARK 500 ALA A 59 54.82 -106.02
REMARK 500 GLU A 72 54.16 -141.18
REMARK 500 PHE A 77 105.41 -37.89
REMARK 500 ASP A 92 90.31 -62.54
REMARK 500 CYS A 93 -9.80 -151.05
REMARK 500 MET A 153 -9.21 -150.59
REMARK 500 PHE A 178 143.71 -173.71
REMARK 500 ALA A 202 67.44 -152.27
REMARK 500 TRP A 231 40.83 -86.72
REMARK 500 SER A 238 -126.90 63.33
REMARK 500 ASN A 288 -19.19 -144.18
REMARK 500 ASN A 293 -65.06 80.36
REMARK 500 ALA A 294 -20.04 69.46
REMARK 500 LEU A 297 -13.73 -45.52
REMARK 500 ASN A 300 78.65 -156.90
REMARK 500 PRO A 301 -89.76 -63.91
REMARK 500 ALA A 302 7.64 -55.15
REMARK 500 ALA A 339 -92.05 -139.89
REMARK 500 LEU A 354 34.07 -95.42
REMARK 500 GLU A 367 -69.21 -28.37
REMARK 500 ALA A 387 96.26 -69.98
REMARK 500 PRO A 389 -170.73 -69.62
REMARK 500 LYS A 403 2.21 -66.67
REMARK 500 ASN A 422 109.10 -50.94
REMARK 500 PHE A 440 -68.73 -130.05
REMARK 500 TRP A 529 80.62 -161.41
REMARK 500
REMARK 500 REMARK: NULL
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 ASN A 288 ASP A 289 147.91
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 ACT A 607
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A
REMARK 800 601 through MAN A 605 bound to ASN A 493
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1QO9 RELATED DB: PDB
REMARK 900 EARLIER MODEL
DBREF 6XYS 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 NAG A 601 14
HET NAG A 602 14
HET MAN A 603 11
HET BMA A 604 11
HET MAN A 605 11
HET CL A 606 1
HET ACT A 607 3
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM MAN ALPHA-D-MANNOSE
HETNAM BMA BETA-D-MANNOSE
HETNAM CL CHLORIDE ION
HETNAM ACT ACETATE ION
FORMUL 2 NAG 2(C8 H15 N O6)
FORMUL 2 MAN 2(C6 H12 O6)
FORMUL 2 BMA C6 H12 O6
FORMUL 3 CL CL 1-
FORMUL 4 ACT C2 H3 O2 1-
FORMUL 5 HOH *94(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 ASN A 221 1 17
HELIX 9 AA9 ALA A 222 PHE A 225 5 4
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 ALA A 302 SER A 310 1 9
HELIX 14 AB5 ASP A 312 GLN A 320 1 9
HELIX 15 AB6 TRP A 321 TYR A 324 5 4
HELIX 16 AB7 ASP A 344 ALA A 352 1 9
HELIX 17 AB8 GLY A 368 PHE A 376 1 9
HELIX 18 AB9 ARG A 390 PHE A 401 1 12
HELIX 19 AC1 THR A 405 TYR A 416 1 12
HELIX 20 AC2 GLY A 424 PHE A 440 1 17
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 ASP A 565 ARG A 571 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 GLY A 12 N THR A 9
SHEET 3 AA1 3 LEU A 57 ASP A 58 1 O LEU A 57 N ARG A 15
SHEET 1 AA211 ARG A 17 VAL A 21 0
SHEET 2 AA211 ARG A 24 PRO A 33 -1 O VAL A 26 N VAL A 19
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 VAL A 175 N TRP A 99
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 TYR A 540 N TYR A 460
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 2.07
SSBOND 2 CYS A 292 CYS A 307 1555 1555 2.05
SSBOND 3 CYS A 442 CYS A 560 1555 1555 2.01
LINK OG SER A 238 C ACT A 607 1555 1555 1.43
LINK ND2 ASN A 493 C1 NAG A 601 1555 1555 1.43
LINK O4 NAG A 601 C1 NAG A 602 1555 1555 1.37
LINK O4 NAG A 602 C1 MAN A 603 1555 1555 1.38
LINK O3 MAN A 603 C1 BMA A 604 1555 1555 1.37
LINK O3 BMA A 604 C1 MAN A 605 1555 1555 1.38
SITE 1 AC1 5 GLY A 150 GLY A 151 SER A 238 ALA A 239
SITE 2 AC1 5 HIS A 480
SITE 1 AC2 7 ARG A 17 VAL A 21 THR A 60 GLY A 61
SITE 2 AC2 7 LEU A 62 ILE A 166 ASN A 493
CRYST1 94.620 94.620 159.010 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 0.010569 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010569 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006289 0.00000
TER 4240 TRP A 573
MASTER 474 0 7 27 14 0 4 6 4376 1 72 45
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