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HEADER HYDROLASE 06-OCT-12 4BDS
TITLE HUMAN BUTYRYLCHOLINESTERASE IN COMPLEX WITH TACRINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CHOLINESTERASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN, RESIDUES 29-557;
COMPND 5 SYNONYM: BUTYRYLCHOLINESTERASE, ACYLCHOLINE ACYLHYDROLASE,
COMPND 6 BUTYRYLCHOLINE ESTERASE, CHOLINE ESTERASE II,
COMPND 7 PSEUDOCHOLINESTERASE;
COMPND 8 EC: 3.1.1.8;
COMPND 9 ENGINEERED: YES;
COMPND 10 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 10029;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: CHO-K1;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGS
KEYWDS HYDROLASE, NERVE TRANSMISSION, INHIBITIOR, ALPHA-BETA HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR F.NACHON,E.CARLETTI,C.RONCO,M.TROVASLET,Y.NICOLET,L.JEAN,P.-Y.RENARD
REVDAT 1 29-MAY-13 4BDS 0
JRNL AUTH F.NACHON,E.CARLETTI,C.RONCO,M.TROVASLET,Y.NICOLET,L.JEAN,
JRNL AUTH 2 P.RENARD
JRNL TITL CRYSTAL STRUCTURES OF HUMAN CHOLINESTERASES IN COMPLEX WITH
JRNL TITL 2 HUPRINE W AND TACRINE: ELEMENTS OF SPECIFICITY FOR ANTI-
JRNL TITL 3 ALZHEIMER'S DRUGS TARGETING ACETYL- AND
JRNL TITL 4 BUTYRYLCHOLINESTERASE.
JRNL REF BIOCHEM.J. 2013
JRNL REFN ESSN 1470-8728
JRNL PMID 23679855
JRNL DOI 10.1042/BJ20130013
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT 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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.100
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.904
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.36
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.79
REMARK 3 NUMBER OF REFLECTIONS : 45772
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.1765
REMARK 3 R VALUE (WORKING SET) : 0.1755
REMARK 3 FREE R VALUE : 0.2087
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.1
REMARK 3 FREE R VALUE TEST SET COUNT : 1422
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 40.9119 - 4.5224 0.99 4632 148 0.1716 0.1904
REMARK 3 2 4.5224 - 3.5903 1.00 4497 137 0.1444 0.1655
REMARK 3 3 3.5903 - 3.1366 1.00 4453 142 0.1661 0.2146
REMARK 3 4 3.1366 - 2.8499 1.00 4453 129 0.1812 0.1984
REMARK 3 5 2.8499 - 2.6457 1.00 4394 148 0.1806 0.2544
REMARK 3 6 2.6457 - 2.4897 1.00 4407 145 0.1894 0.2683
REMARK 3 7 2.4897 - 2.3651 1.00 4384 157 0.1932 0.2391
REMARK 3 8 2.3651 - 2.2621 1.00 4409 127 0.2059 0.2448
REMARK 3 9 2.2621 - 2.1750 1.00 4389 142 0.2292 0.2596
REMARK 3 10 2.1750 - 2.1000 1.00 4332 147 0.2472 0.2908
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
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) : 0.23
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.39
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 34.86
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 40.4
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 : 0.009 4548
REMARK 3 ANGLE : 1.135 6192
REMARK 3 CHIRALITY : 0.080 676
REMARK 3 PLANARITY : 0.005 778
REMARK 3 DIHEDRAL : 19.796 1694
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 6
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A AND RESSEQ 1:65
REMARK 3 ORIGIN FOR THE GROUP (A): 132.9016 127.9849 17.3185
REMARK 3 T TENSOR
REMARK 3 T11: 0.5993 T22: 0.4181
REMARK 3 T33: 0.2820 T12: -0.1051
REMARK 3 T13: -0.1446 T23: -0.0754
REMARK 3 L TENSOR
REMARK 3 L11: 2.6622 L22: 2.2135
REMARK 3 L33: 1.3772 L12: -0.5986
REMARK 3 L13: -0.2127 L23: 0.2219
REMARK 3 S TENSOR
REMARK 3 S11: -0.1346 S12: 0.6986 S13: 0.2149
REMARK 3 S21: -0.7533 S22: 0.1215 S23: 0.1332
REMARK 3 S31: -0.2378 S32: -0.2138 S33: 0.0455
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN A AND RESSEQ 66:91
REMARK 3 ORIGIN FOR THE GROUP (A): 130.2196 111.4728 32.4519
REMARK 3 T TENSOR
REMARK 3 T11: 0.3708 T22: 0.2869
REMARK 3 T33: 0.4113 T12: -0.0999
REMARK 3 T13: -0.0863 T23: -0.0810
REMARK 3 L TENSOR
REMARK 3 L11: 1.1105 L22: 0.7403
REMARK 3 L33: 2.4035 L12: 0.6579
REMARK 3 L13: -1.0400 L23: -1.1745
REMARK 3 S TENSOR
REMARK 3 S11: -0.1934 S12: 0.1231 S13: -0.3089
REMARK 3 S21: -0.2917 S22: 0.0851 S23: -0.0661
REMARK 3 S31: 0.4867 S32: -0.2820 S33: 0.0799
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN A AND RESSEQ 92:153) OR (CHAIN A AND
REMARK 3 RESSEQ 164:231)
REMARK 3 ORIGIN FOR THE GROUP (A): 137.9794 130.6719 30.9152
REMARK 3 T TENSOR
REMARK 3 T11: 0.2468 T22: 0.1603
REMARK 3 T33: 0.2050 T12: -0.0524
REMARK 3 T13: -0.0368 T23: -0.0435
REMARK 3 L TENSOR
REMARK 3 L11: 1.8228 L22: 1.9433
REMARK 3 L33: 2.0755 L12: -0.0259
REMARK 3 L13: 0.6398 L23: 0.0432
REMARK 3 S TENSOR
REMARK 3 S11: -0.0710 S12: 0.1674 S13: 0.0410
REMARK 3 S21: -0.3399 S22: 0.1076 S23: 0.0360
REMARK 3 S31: -0.2002 S32: -0.0484 S33: -0.0284
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN A AND RESSEQ 290:326) OR (CHAIN A AND
REMARK 3 RESSEQ 397:515)
REMARK 3 ORIGIN FOR THE GROUP (A): 136.1026 131.2096 47.5354
REMARK 3 T TENSOR
REMARK 3 T11: 0.1875 T22: 0.1969
REMARK 3 T33: 0.2070 T12: -0.0008
REMARK 3 T13: -0.0673 T23: -0.0575
REMARK 3 L TENSOR
REMARK 3 L11: 1.4993 L22: 1.9509
REMARK 3 L33: 2.2119 L12: 0.1511
REMARK 3 L13: 0.2608 L23: 0.1916
REMARK 3 S TENSOR
REMARK 3 S11: 0.0169 S12: -0.1681 S13: 0.0084
REMARK 3 S21: 0.0286 S22: 0.0082 S23: 0.1424
REMARK 3 S31: -0.1279 S32: -0.2212 S33: -0.0426
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: (CHAIN A AND RESSEQ 154:163) OR (CHAIN A AND
REMARK 3 RESSEQ 232:289)
REMARK 3 ORIGIN FOR THE GROUP (A): 152.3616 107.5594 28.2685
REMARK 3 T TENSOR
REMARK 3 T11: 0.4893 T22: 0.4291
REMARK 3 T33: 0.6282 T12: 0.0808
REMARK 3 T13: 0.0123 T23: -0.2027
REMARK 3 L TENSOR
REMARK 3 L11: 1.7763 L22: 3.8715
REMARK 3 L33: 5.6974 L12: 0.0893
REMARK 3 L13: -0.9645 L23: 1.5885
REMARK 3 S TENSOR
REMARK 3 S11: -0.2213 S12: 0.2033 S13: -0.6324
REMARK 3 S21: -0.1748 S22: 0.2905 S23: -0.4412
REMARK 3 S31: 0.9279 S32: 0.9187 S33: -0.0952
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: (CHAIN A AND RESSEQ 327:396) OR (CHAIN A AND
REMARK 3 RESSEQ 516:529)
REMARK 3 ORIGIN FOR THE GROUP (A): 142.2188 110.6356 58.2482
REMARK 3 T TENSOR
REMARK 3 T11: 0.3803 T22: 0.2487
REMARK 3 T33: 0.3708 T12: -0.0432
REMARK 3 T13: -0.1610 T23: 0.0248
REMARK 3 L TENSOR
REMARK 3 L11: 5.2544 L22: 3.5359
REMARK 3 L33: 3.2992 L12: 0.6090
REMARK 3 L13: 1.4110 L23: -0.6461
REMARK 3 S TENSOR
REMARK 3 S11: 0.2434 S12: -0.5473 S13: -0.4980
REMARK 3 S21: 0.3679 S22: 0.0620 S23: -0.2191
REMARK 3 S31: 0.3991 S32: -0.1686 S33: -0.2884
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 4BDS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 06-OCT-12.
REMARK 100 THE PDBE ID CODE IS EBI-54265.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-MAR-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9330
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD (QUANTUM 4)
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 45776
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.10
REMARK 200 RESOLUTION RANGE LOW (A) : 40.90
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 6.4
REMARK 200 R MERGE (I) : 0.07
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 18.40
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.40
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 6.5
REMARK 200 R MERGE FOR SHELL (I) : 0.42
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 4.80
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1P0I
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.2
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MES PH 6.5, 2.1 M
REMARK 280 AMMONIUM SULFATE, 293 K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -Y,X,Z
REMARK 290 4555 Y,-X,Z
REMARK 290 5555 -X,Y,-Z
REMARK 290 6555 X,-Y,-Z
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z
REMARK 290 9555 X+1/2,Y+1/2,Z+1/2
REMARK 290 10555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 11555 -Y+1/2,X+1/2,Z+1/2
REMARK 290 12555 Y+1/2,-X+1/2,Z+1/2
REMARK 290 13555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 14555 X+1/2,-Y+1/2,-Z+1/2
REMARK 290 15555 Y+1/2,X+1/2,-Z+1/2
REMARK 290 16555 -Y+1/2,-X+1/2,-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 0.00000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 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 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000
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 0.00000
REMARK 290 SMTRY1 9 1.000000 0.000000 0.000000 77.83000
REMARK 290 SMTRY2 9 0.000000 1.000000 0.000000 77.83000
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 63.94000
REMARK 290 SMTRY1 10 -1.000000 0.000000 0.000000 77.83000
REMARK 290 SMTRY2 10 0.000000 -1.000000 0.000000 77.83000
REMARK 290 SMTRY3 10 0.000000 0.000000 1.000000 63.94000
REMARK 290 SMTRY1 11 0.000000 -1.000000 0.000000 77.83000
REMARK 290 SMTRY2 11 1.000000 0.000000 0.000000 77.83000
REMARK 290 SMTRY3 11 0.000000 0.000000 1.000000 63.94000
REMARK 290 SMTRY1 12 0.000000 1.000000 0.000000 77.83000
REMARK 290 SMTRY2 12 -1.000000 0.000000 0.000000 77.83000
REMARK 290 SMTRY3 12 0.000000 0.000000 1.000000 63.94000
REMARK 290 SMTRY1 13 -1.000000 0.000000 0.000000 77.83000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 77.83000
REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 63.94000
REMARK 290 SMTRY1 14 1.000000 0.000000 0.000000 77.83000
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 77.83000
REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 63.94000
REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 77.83000
REMARK 290 SMTRY2 15 1.000000 0.000000 0.000000 77.83000
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 63.94000
REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 77.83000
REMARK 290 SMTRY2 16 -1.000000 0.000000 0.000000 77.83000
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 63.94000
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 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 HOH A2129 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 GLU A 1
REMARK 465 ASP A 2
REMARK 465 ASP A 3
REMARK 465 ASP A 378
REMARK 465 ASP A 379
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 GLN A 486 CG CD OE1 NE2
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 OE1 GLU A 255 O HOH A 2150 2.18
REMARK 500 O3 FU4 A 612 O HOH A 2242 2.15
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 PHE A 43 -8.36 79.70
REMARK 500 THR A 50 -115.35 -64.36
REMARK 500 LYS A 51 121.13 174.58
REMARK 500 ALA A 58 66.57 -109.92
REMARK 500 ASN A 106 54.53 -152.58
REMARK 500 PHE A 118 13.66 59.62
REMARK 500 ALA A 162 71.32 -166.29
REMARK 500 SER A 198 -121.41 57.08
REMARK 500 ASP A 297 -75.35 -132.48
REMARK 500 PHE A 398 -54.28 -130.33
REMARK 500 GLN A 455 -9.54 78.82
REMARK 500 ASN A 485 48.21 -108.79
REMARK 500 GLU A 506 -73.96 -86.50
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600 FPK IS BOUND TO THE OXYANION HOLE OF THE ENZYME, WHICH OFTEN LEADS
REMARK 600 TO THE DISTORTION OF SOME BONDS.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FU4 A 612
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AA A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 704
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 705
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 706
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FPK A 710
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE
REMARK 800 NAG A 601 BOUND TO ASN A 57
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE
REMARK 800 NAG A 611 BOUND TO ASN A 106
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF SUGAR BOUND TO
REMARK 800 ASN A 241 RESIDUES 621 TO 623
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE
REMARK 800 NAG A 631 BOUND TO ASN A 256
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF SUGAR BOUND TO
REMARK 800 ASN A 341 RESIDUES 641 TO 643
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE
REMARK 800 NAG A 651 BOUND TO ASN A 485
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1EHO RELATED DB: PDB
REMARK 900 MODEL OF (-)-COCAINE-BOUND BCHE COMPLEX.
REMARK 900 RELATED ID: 1EHQ RELATED DB: PDB
REMARK 900 MODEL OF (+)-COCAINE-BOUND BCHE COMPLEX
REMARK 900 RELATED ID: 1KCJ RELATED DB: PDB
REMARK 900 MODEL OF (-)-COCAINE-BOUND (-)-COCAINE HYDROLASE COMPLEX
REMARK 900 RELATED ID: 1P0I RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN BUTYRYL CHOLINESTERASE
REMARK 900 RELATED ID: 1P0M RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN BUTYRYL CHOLINESTERASE
REMARK 900 INCOMPLEX WITH A CHOLINE MOLECULE
REMARK 900 RELATED ID: 1P0P RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF SOMAN-AGED HUMAN
REMARK 900 BUTYRYLCHOLINESTERASE IN COMPLEX WITH THE SUBSTRATE
REMARK 900 ANALOGBUTYRYLTHIOCHOLINE
REMARK 900 RELATED ID: 1P0Q RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF SOMAN-AGED HUMAN BUTYRYL
REMARK 900 CHOLINESTERASE
REMARK 900 RELATED ID: 1XLU RELATED DB: PDB
REMARK 900 X-RAY STRUCTURE OF DI-ISOPROPYL-PHOSPHORO-FLUORIDATE (
REMARK 900 DFP)INHIBITED BUTYRYLCHOLINESTERASE AFTER AGING
REMARK 900 RELATED ID: 1XLV RELATED DB: PDB
REMARK 900 ETHYLPHOSPHORYLATED BUTYRYLCHOLINESTERASE (AGED) OBTAINEDBY
REMARK 900 REACTION WITH ECHOTHIOPHATE
REMARK 900 RELATED ID: 1XLW RELATED DB: PDB
REMARK 900 DIETHYLPHOSPHORYLATED BUTYRYLCHOLINESTERASE (NONAGED)OBTAINED
REMARK 900 BY REACTION WITH ECHOTHIOPHATE
REMARK 900 RELATED ID: 2J4C RELATED DB: PDB
REMARK 900 STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE IN COMPLEX WITH
REMARK 900 10MM HGCL2
REMARK 900 RELATED ID: 2WID RELATED DB: PDB
REMARK 900 AGED FORM OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY
REMARK 900 TABUN ANALOGUE TA1
REMARK 900 RELATED ID: 2WIF RELATED DB: PDB
REMARK 900 AGED FORM OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY
REMARK 900 TABUN ANALOGUE TA1
REMARK 900 RELATED ID: 2WIG RELATED DB: PDB
REMARK 900 NONAGED FORM OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY
REMARK 900 TABUN ANALOGUE TA4
REMARK 900 RELATED ID: 2WIJ RELATED DB: PDB
REMARK 900 NONAGED FORM OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY
REMARK 900 TABUN ANALOGUE TA5
REMARK 900 RELATED ID: 2WIK RELATED DB: PDB
REMARK 900 NONAGED FORM OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY
REMARK 900 TABUN ANALOGUE TA6
REMARK 900 RELATED ID: 2WIL RELATED DB: PDB
REMARK 900 AGED FORM OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY
REMARK 900 TABUN ANALOGUE TA5
REMARK 900 RELATED ID: 2WSL RELATED DB: PDB
REMARK 900 AGED FORM OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY
REMARK 900 TABUN ANALOGUE TA4
REMARK 900 RELATED ID: 2XMB RELATED DB: PDB
REMARK 900 G117H MUTANT OF HUMAN BUTYRYLCHOLINESTERASE IN COMPLEX
REMARK 900 WITH SULFATE
REMARK 900 RELATED ID: 2XMC RELATED DB: PDB
REMARK 900 G117H MUTANT OF HUMAN BUTYRYLCHOLINESTERASE IN COMPLEX
REMARK 900 WITH FLUORIDE ANION
REMARK 900 RELATED ID: 2XMD RELATED DB: PDB
REMARK 900 G117H MUTANT OF HUMAN BUTYRYLCHOLINESTERASE IN COMPLEX
REMARK 900 WITH ECHOTHIOPHATE
REMARK 900 RELATED ID: 2XMG RELATED DB: PDB
REMARK 900 G117H MUTANT OF HUMAN BUTYRYLCHOLINESTERASE IN COMPLEX
REMARK 900 WITH VX
REMARK 900 RELATED ID: 2XQF RELATED DB: PDB
REMARK 900 X-RAY STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED
REMARK 900 BY RACEMIC VX
REMARK 900 RELATED ID: 2XQG RELATED DB: PDB
REMARK 900 X-RAY STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED
REMARK 900 BY RACEMIC VR
REMARK 900 RELATED ID: 2XQI RELATED DB: PDB
REMARK 900 X-RAY STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED
REMARK 900 BY RACEMIC CVX
REMARK 900 RELATED ID: 2XQJ RELATED DB: PDB
REMARK 900 X-RAY STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED
REMARK 900 BY PURE ENANTIOMER VX-(R)
REMARK 900 RELATED ID: 2XQK RELATED DB: PDB
REMARK 900 X-RAY STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED
REMARK 900 BY PURE ENANTIOMER VX-(S)
REMARK 900 RELATED ID: 2Y1K RELATED DB: PDB
REMARK 900 STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY CBDP
REMARK 900 (12H SOAK): PHOSPHOSERINE ADDUCT
REMARK 900 RELATED ID: 4AQD RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF FULLY GLYCOSYLATED HUMAN
REMARK 900 BUTYRYLCHOLINESTERASE
REMARK 900 RELATED ID: 4AXB RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF SOMAN-AGED HUMAN
REMARK 900 BUTYRYLCHOLINESTERASE IN COMPLEX WITH 2-PAM
REMARK 900 RELATED ID: 4B0O RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF SOMAN-AGED HUMAN
REMARK 900 BUTYRYLCHOLINESTERASE IN COMPLEX WITH BENZYL PYRIDINIUM-4
REMARK 900 -METHYLTRICHLOROACETIMIDATE
REMARK 900 RELATED ID: 4B0P RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF SOMAN-AGED HUMAN
REMARK 900 BUTYRYLCHOLINESTERASE IN COMPLEX WITH METHYL 2-(
REMARK 900 PENTAFLUOROBENZYLOXYIMINO)PYRIDINIUM
REMARK 900 RELATED ID: 4BBZ RELATED DB: PDB
REMARK 900 STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY CBDP
REMARK 900 (2-MIN SOAK): CRESYL-PHOSPHOSERINE ADDUCT
DBREF 4BDS A 1 529 UNP P06276 CHLE_HUMAN 29 557
SEQADV 4BDS GLN A 17 UNP P06276 ASN 45 ENGINEERED MUTATION
SEQADV 4BDS GLN A 455 UNP P06276 ASN 483 ENGINEERED MUTATION
SEQADV 4BDS GLN A 481 UNP P06276 ASN 509 ENGINEERED MUTATION
SEQADV 4BDS GLN A 486 UNP P06276 ASN 514 ENGINEERED MUTATION
SEQRES 1 A 529 GLU ASP ASP ILE ILE ILE ALA THR LYS ASN GLY LYS VAL
SEQRES 2 A 529 ARG GLY MET GLN LEU THR VAL PHE GLY GLY THR VAL THR
SEQRES 3 A 529 ALA PHE LEU GLY ILE PRO TYR ALA GLN PRO PRO LEU GLY
SEQRES 4 A 529 ARG LEU ARG PHE LYS LYS PRO GLN SER LEU THR LYS TRP
SEQRES 5 A 529 SER ASP ILE TRP ASN ALA THR LYS TYR ALA ASN SER CYS
SEQRES 6 A 529 CYS GLN ASN ILE ASP GLN SER PHE PRO GLY PHE HIS GLY
SEQRES 7 A 529 SER GLU MET TRP ASN PRO ASN THR ASP LEU SER GLU ASP
SEQRES 8 A 529 CYS LEU TYR LEU ASN VAL TRP ILE PRO ALA PRO LYS PRO
SEQRES 9 A 529 LYS ASN ALA THR VAL LEU ILE TRP ILE TYR GLY GLY GLY
SEQRES 10 A 529 PHE GLN THR GLY THR SER SER LEU HIS VAL TYR ASP GLY
SEQRES 11 A 529 LYS PHE LEU ALA ARG VAL GLU ARG VAL ILE VAL VAL SER
SEQRES 12 A 529 MET ASN TYR ARG VAL GLY ALA LEU GLY PHE LEU ALA LEU
SEQRES 13 A 529 PRO GLY ASN PRO GLU ALA PRO GLY ASN MET GLY LEU PHE
SEQRES 14 A 529 ASP GLN GLN LEU ALA LEU GLN TRP VAL GLN LYS ASN ILE
SEQRES 15 A 529 ALA ALA PHE GLY GLY ASN PRO LYS SER VAL THR LEU PHE
SEQRES 16 A 529 GLY GLU SER ALA GLY ALA ALA SER VAL SER LEU HIS LEU
SEQRES 17 A 529 LEU SER PRO GLY SER HIS SER LEU PHE THR ARG ALA ILE
SEQRES 18 A 529 LEU GLN SER GLY SER PHE ASN ALA PRO TRP ALA VAL THR
SEQRES 19 A 529 SER LEU TYR GLU ALA ARG ASN ARG THR LEU ASN LEU ALA
SEQRES 20 A 529 LYS LEU THR GLY CYS SER ARG GLU ASN GLU THR GLU ILE
SEQRES 21 A 529 ILE LYS CYS LEU ARG ASN LYS ASP PRO GLN GLU ILE LEU
SEQRES 22 A 529 LEU ASN GLU ALA PHE VAL VAL PRO TYR GLY THR PRO LEU
SEQRES 23 A 529 SER VAL ASN PHE GLY PRO THR VAL ASP GLY ASP PHE LEU
SEQRES 24 A 529 THR ASP MET PRO ASP ILE LEU LEU GLU LEU GLY GLN PHE
SEQRES 25 A 529 LYS LYS THR GLN ILE LEU VAL GLY VAL ASN LYS ASP GLU
SEQRES 26 A 529 GLY THR ALA PHE LEU VAL TYR GLY ALA PRO GLY PHE SER
SEQRES 27 A 529 LYS ASP ASN ASN SER ILE ILE THR ARG LYS GLU PHE GLN
SEQRES 28 A 529 GLU GLY LEU LYS ILE PHE PHE PRO GLY VAL SER GLU PHE
SEQRES 29 A 529 GLY LYS GLU SER ILE LEU PHE HIS TYR THR ASP TRP VAL
SEQRES 30 A 529 ASP ASP GLN ARG PRO GLU ASN TYR ARG GLU ALA LEU GLY
SEQRES 31 A 529 ASP VAL VAL GLY ASP TYR ASN PHE ILE CYS PRO ALA LEU
SEQRES 32 A 529 GLU PHE THR LYS LYS PHE SER GLU TRP GLY ASN ASN ALA
SEQRES 33 A 529 PHE PHE TYR TYR PHE GLU HIS ARG SER SER LYS LEU PRO
SEQRES 34 A 529 TRP PRO GLU TRP MET GLY VAL MET HIS GLY TYR GLU ILE
SEQRES 35 A 529 GLU PHE VAL PHE GLY LEU PRO LEU GLU ARG ARG ASP GLN
SEQRES 36 A 529 TYR THR LYS ALA GLU GLU ILE LEU SER ARG SER ILE VAL
SEQRES 37 A 529 LYS ARG TRP ALA ASN PHE ALA LYS TYR GLY ASN PRO GLN
SEQRES 38 A 529 GLU THR GLN ASN GLN SER THR SER TRP PRO VAL PHE LYS
SEQRES 39 A 529 SER THR GLU GLN LYS TYR LEU THR LEU ASN THR GLU SER
SEQRES 40 A 529 THR ARG ILE MET THR LYS LEU ARG ALA GLN GLN CYS ARG
SEQRES 41 A 529 PHE TRP THR SER PHE PHE PRO LYS VAL
HET NAG A 601 14
HET NAG A 611 14
HET FU4 A 612 10
HET NAG A 621 14
HET FUL A 622 10
HET NAG A 623 14
HET NAG A 631 14
HET NAG A 641 14
HET FUL A 642 10
HET NAG A 643 14
HET NAG A 651 14
HET AA A 701 15
HET GOL A 702 6
HET SO4 A 703 5
HET SO4 A 704 5
HET CL A 705 1
HET CL A 706 1
HET FPK A 710 10
HET UNX A 711 1
HET UNX A 712 1
HET UNX A 713 1
HET UNX A 714 1
HET UNX A 715 1
HET UNX A 716 1
HET UNX A 717 1
HETNAM SO4 SULFATE ION
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM CL CHLORIDE ION
HETNAM AA 9-AMINOACRIDINE
HETNAM GOL GLYCEROL
HETNAM FU4 2,6-ANHYDRO-1-DEOXY-D-GALACTITOL
HETNAM FUL BETA-L-FUCOSE
HETNAM FPK 1-FORMYL-L-PROLINE
HETNAM UNX UNKNOWN ATOM OR ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
HETSYN FUL 6-DEOXY-BETA-L-GALACTOSE
FORMUL 2 SO4 2(O4 S 2-)
FORMUL 3 NAG 8(C8 H15 N O6)
FORMUL 4 CL 2(CL 1-)
FORMUL 5 AA C13 H11 N2 1+
FORMUL 6 GOL C3 H8 O3
FORMUL 7 FU4 C6 H12 O4
FORMUL 8 FUL 2(C6 H12 O5)
FORMUL 9 FPK C6 H9 N O3
FORMUL 10 UNX 7(X)
FORMUL 11 HOH *279(H2 O)
HELIX 1 1 LEU A 38 ARG A 42 5 5
HELIX 2 2 PHE A 76 MET A 81 1 6
HELIX 3 3 LEU A 125 ASP A 129 5 5
HELIX 4 4 GLY A 130 ARG A 138 1 9
HELIX 5 5 GLY A 149 LEU A 154 1 6
HELIX 6 6 ASN A 165 ILE A 182 1 18
HELIX 7 7 ALA A 183 PHE A 185 5 3
HELIX 8 8 SER A 198 SER A 210 1 13
HELIX 9 9 PRO A 211 PHE A 217 5 7
HELIX 10 10 SER A 235 THR A 250 1 16
HELIX 11 11 ASN A 256 ASN A 266 1 11
HELIX 12 12 ASP A 268 GLU A 276 1 9
HELIX 13 13 ALA A 277 VAL A 279 5 3
HELIX 14 14 MET A 302 LEU A 309 1 8
HELIX 15 15 GLY A 326 VAL A 331 1 6
HELIX 16 16 THR A 346 PHE A 358 1 13
HELIX 17 17 SER A 362 THR A 374 1 13
HELIX 18 18 GLU A 383 PHE A 398 1 16
HELIX 19 19 PHE A 398 GLU A 411 1 14
HELIX 20 20 PRO A 431 GLY A 435 5 5
HELIX 21 21 GLU A 441 PHE A 446 1 6
HELIX 22 22 GLY A 447 GLU A 451 5 5
HELIX 23 23 THR A 457 GLY A 478 1 22
HELIX 24 24 ARG A 515 PHE A 525 1 11
HELIX 25 25 PHE A 526 VAL A 529 5 4
SHEET 1 AA 3 ILE A 5 THR A 8 0
SHEET 2 AA 3 GLY A 11 ARG A 14 -1 O GLY A 11 N THR A 8
SHEET 3 AA 3 ILE A 55 ASN A 57 1 O TRP A 56 N ARG A 14
SHEET 1 AB11 MET A 16 VAL A 20 0
SHEET 2 AB11 GLY A 23 PRO A 32 -1 O GLY A 23 N VAL A 20
SHEET 3 AB11 TYR A 94 PRO A 100 -1 O LEU A 95 N ILE A 31
SHEET 4 AB11 ILE A 140 MET A 144 -1 O VAL A 141 N TRP A 98
SHEET 5 AB11 ALA A 107 ILE A 113 1 O THR A 108 N ILE A 140
SHEET 6 AB11 GLY A 187 GLU A 197 1 N ASN A 188 O ALA A 107
SHEET 7 AB11 ARG A 219 GLN A 223 1 O ARG A 219 N LEU A 194
SHEET 8 AB11 ILE A 317 ASN A 322 1 O LEU A 318 N LEU A 222
SHEET 9 AB11 ALA A 416 PHE A 421 1 O PHE A 417 N VAL A 319
SHEET 10 AB11 LYS A 499 LEU A 503 1 O LEU A 501 N TYR A 420
SHEET 11 AB11 ILE A 510 THR A 512 -1 O MET A 511 N TYR A 500
SHEET 1 AC 2 SER A 64 CYS A 65 0
SHEET 2 AC 2 LEU A 88 SER A 89 1 N SER A 89 O SER A 64
SSBOND 1 CYS A 65 CYS A 92 1555 1555 2.05
SSBOND 2 CYS A 252 CYS A 263 1555 1555 2.04
SSBOND 3 CYS A 400 CYS A 519 1555 1555 2.06
LINK ND2 ASN A 57 C1 NAG A 601 1555 1555 1.44
LINK ND2 ASN A 106 C1 NAG A 611 1555 1555 1.45
LINK ND2 ASN A 241 C1 NAG A 621 1555 1555 1.45
LINK ND2 ASN A 256 C1 NAG A 631 1555 1555 1.45
LINK ND2 ASN A 341 C1 NAG A 641 1555 1555 1.44
LINK ND2 ASN A 485 C1 NAG A 651 1555 1555 1.45
LINK O6 NAG A 621 C1 FUL A 622 1555 1555 1.45
LINK O4 NAG A 621 C1 NAG A 623 1555 1555 1.45
LINK O6 NAG A 641 C1 FUL A 642 1555 1555 1.44
LINK O4 NAG A 641 C1 NAG A 643 1555 1555 1.44
CISPEP 1 ALA A 101 PRO A 102 0 0.44
SITE 1 AC1 4 ASN A 188 LYS A 190 NAG A 611 HOH A2242
SITE 1 AC2 9 TRP A 82 GLU A 197 SER A 198 TYR A 332
SITE 2 AC2 9 TRP A 430 HIS A 438 FPK A 710 HOH A2056
SITE 3 AC2 9 HOH A2093
SITE 1 AC3 5 LEU A 18 TYR A 61 TRP A 98 ASP A 129
SITE 2 AC3 5 LYS A 131
SITE 1 AC4 5 GLN A 316 GLY A 413 ASN A 414 ASN A 415
SITE 2 AC4 5 HOH A2216
SITE 1 AC5 7 TRP A 231 ARG A 242 SER A 287 VAL A 288
SITE 2 AC5 7 HOH A2145 HOH A2154 HOH A2155
SITE 1 AC6 3 THR A 488 THR A 508 HOH A2240
SITE 1 AC7 2 TYR A 420 HOH A2271
SITE 1 AC8 8 GLY A 116 GLY A 117 SER A 198 ALA A 199
SITE 2 AC8 8 LEU A 286 HIS A 438 AA A 701 HOH A2092
SITE 1 AC9 2 ASN A 57 HOH A2278
SITE 1 BC1 4 ASN A 106 ASN A 188 LYS A 190 FU4 A 612
SITE 1 BC2 8 TYR A 237 ASN A 241 ASN A 245 LYS A 248
SITE 2 BC2 8 LEU A 249 PHE A 278 PRO A 281 HOH A2148
SITE 1 BC3 1 ASN A 256
SITE 1 BC4 3 SER A 338 ASN A 341 ASN A 342
SITE 1 BC5 3 ARG A 465 ASN A 485 HOH A2279
CRYST1 155.660 155.660 127.880 90.00 90.00 90.00 I 4 2 2 16
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 0.006424 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006424 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007820 0.00000
TER 4228 VAL A 529
MASTER 575 0 25 25 16 0 21 6 4698 1 195 41
END |