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HEADER HYDROLASE 27-JUL-10 2XMC
TITLE G117H MUTANT OF HUMAN BUTYRYLCHOLINESTERASE IN COMPLEX WITH
TITLE 2 FLUORIDE ANION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CHOLINESTERASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 29-557;
COMPND 5 SYNONYM: ACYLCHOLINE ACYLHYDROLASE, CHOLINE ESTERASE II,
COMPND 6 BUTYRYLCHOLINESTERASE, PSEUDOCHOLINESTERASE;
COMPND 7 EC: 3.1.1.8;
COMPND 8 ENGINEERED: YES;
COMPND 9 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
KEYWDS HYDROLASE, GLYCOPROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR F.NACHON,E.CARLETTI,M.WANDHAMMER,Y.NICOLET,L.M.SCHOPFER,P.MASSON,
AUTHOR 2 O.LOCKRIDGE
REVDAT 1 01-DEC-10 2XMC 0
JRNL AUTH F.NACHON,E.CARLETTI,M.WANDHAMMER,Y.NICOLET,L.M.SCHOPFER,
JRNL AUTH 2 P.MASSON,O.LOCKRIDGE
JRNL TITL X-RAY CRYSTALLOGRAPHIC SNAPSHOTS OF REACTION INTERMEDIATES
JRNL TITL 2 IN THE G117H MUTANT OF HUMAN BUTYRYLCHOLINESTERASE, A NERVE
JRNL TITL 3 AGENT TARGET ENGINEERED INTO A CATALYTIC BIOSCAVENGE
JRNL REF BIOCHEM.J. 2010
JRNL REFN ESSN 1470-8728
JRNL DOI 10.1042/BJ20101648
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0102
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 109.76
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.70
REMARK 3 NUMBER OF REFLECTIONS : 28951
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 + TEST SET) : 0.19373
REMARK 3 R VALUE (WORKING SET) : 0.19183
REMARK 3 FREE R VALUE : 0.25250
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.2
REMARK 3 FREE R VALUE TEST SET COUNT : 945
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.400
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.462
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2095
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.69
REMARK 3 BIN R VALUE (WORKING SET) : 0.295
REMARK 3 BIN FREE R VALUE SET COUNT : 66
REMARK 3 BIN FREE R VALUE : 0.415
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4216
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 171
REMARK 3 SOLVENT ATOMS : 229
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 46.084
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.44
REMARK 3 B22 (A**2) : -0.44
REMARK 3 B33 (A**2) : 0.87
REMARK 3 B12 (A**2) : 0.00
REMARK 3 B13 (A**2) : 0.00
REMARK 3 B23 (A**2) : -0.00
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.312
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.247
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.196
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 19.015
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.956
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.926
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4498 ; 0.021 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6126 ; 2.009 ; 1.981
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 528 ; 8.462 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 205 ;36.806 ;24.049
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 705 ;18.671 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 22 ;21.721 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 673 ; 0.140 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3429 ; 0.009 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 2626 ; 0.924 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4243 ; 1.708 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1872 ; 3.079 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1882 ; 4.886 ; 4.500
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 6
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 3 A 64
REMARK 3 ORIGIN FOR THE GROUP (A): 27.6420 -23.4140 -46.9260
REMARK 3 T TENSOR
REMARK 3 T11: 0.2521 T22: 0.3820
REMARK 3 T33: 0.2901 T12: 0.0691
REMARK 3 T13: 0.0344 T23: -0.1604
REMARK 3 L TENSOR
REMARK 3 L11: 2.7690 L22: 2.9962
REMARK 3 L33: 1.3605 L12: 0.5148
REMARK 3 L13: -0.4047 L23: 0.7372
REMARK 3 S TENSOR
REMARK 3 S11: 0.0033 S12: 0.7861 S13: -0.1602
REMARK 3 S21: -0.6543 S22: -0.1311 S23: 0.0769
REMARK 3 S31: 0.0811 S32: -0.2047 S33: 0.1278
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 65 A 92
REMARK 3 ORIGIN FOR THE GROUP (A): 43.8130 -25.5360 -31.9170
REMARK 3 T TENSOR
REMARK 3 T11: 0.1348 T22: 0.2120
REMARK 3 T33: 0.4645 T12: 0.0870
REMARK 3 T13: 0.0781 T23: -0.0932
REMARK 3 L TENSOR
REMARK 3 L11: 0.8459 L22: 1.1614
REMARK 3 L33: 1.4837 L12: -0.9863
REMARK 3 L13: -0.1888 L23: 0.2580
REMARK 3 S TENSOR
REMARK 3 S11: 0.1469 S12: 0.2191 S13: -0.0204
REMARK 3 S21: -0.0926 S22: -0.1292 S23: -0.2537
REMARK 3 S31: 0.2085 S32: 0.3450 S33: -0.0177
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 93 A 230
REMARK 3 ORIGIN FOR THE GROUP (A): 25.9070 -16.8250 -33.6750
REMARK 3 T TENSOR
REMARK 3 T11: 0.0805 T22: 0.1568
REMARK 3 T33: 0.2990 T12: 0.0494
REMARK 3 T13: 0.0387 T23: -0.0600
REMARK 3 L TENSOR
REMARK 3 L11: 1.6450 L22: 1.5271
REMARK 3 L33: 1.3725 L12: -0.1092
REMARK 3 L13: -0.0581 L23: 0.2869
REMARK 3 S TENSOR
REMARK 3 S11: 0.0685 S12: 0.3474 S13: -0.0302
REMARK 3 S21: -0.2226 S22: -0.0470 S23: -0.0257
REMARK 3 S31: 0.0228 S32: -0.1035 S33: -0.0215
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 231 A 289
REMARK 3 ORIGIN FOR THE GROUP (A): 49.0430 -4.5310 -34.6590
REMARK 3 T TENSOR
REMARK 3 T11: 0.1149 T22: 0.3192
REMARK 3 T33: 0.5585 T12: -0.1072
REMARK 3 T13: 0.1797 T23: 0.0049
REMARK 3 L TENSOR
REMARK 3 L11: 2.8577 L22: 4.0758
REMARK 3 L33: 8.0362 L12: 0.7430
REMARK 3 L13: -2.9208 L23: -2.0129
REMARK 3 S TENSOR
REMARK 3 S11: 0.2703 S12: 0.0851 S13: 0.4371
REMARK 3 S21: -0.0758 S22: -0.2361 S23: -0.7299
REMARK 3 S31: -0.7627 S32: 1.0398 S33: -0.0342
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 290 A 332
REMARK 3 ORIGIN FOR THE GROUP (A): 30.0970 -7.8830 -22.0060
REMARK 3 T TENSOR
REMARK 3 T11: 0.0961 T22: 0.0586
REMARK 3 T33: 0.3302 T12: 0.0120
REMARK 3 T13: 0.0615 T23: -0.0649
REMARK 3 L TENSOR
REMARK 3 L11: 1.6763 L22: 1.3802
REMARK 3 L33: 1.5269 L12: -0.6200
REMARK 3 L13: 0.0908 L23: 0.0600
REMARK 3 S TENSOR
REMARK 3 S11: 0.0693 S12: 0.0027 S13: 0.2467
REMARK 3 S21: -0.0499 S22: 0.0704 S23: -0.1466
REMARK 3 S31: -0.1332 S32: -0.0070 S33: -0.1397
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 333 A 529
REMARK 3 ORIGIN FOR THE GROUP (A): 31.7710 -19.6760 -10.8110
REMARK 3 T TENSOR
REMARK 3 T11: 0.1349 T22: 0.0911
REMARK 3 T33: 0.2894 T12: 0.0233
REMARK 3 T13: 0.0252 T23: -0.0522
REMARK 3 L TENSOR
REMARK 3 L11: 2.1227 L22: 1.1803
REMARK 3 L33: 1.5463 L12: -0.1205
REMARK 3 L13: 0.2447 L23: 0.6264
REMARK 3 S TENSOR
REMARK 3 S11: 0.0320 S12: -0.1570 S13: -0.0613
REMARK 3 S21: 0.2365 S22: 0.0887 S23: -0.1028
REMARK 3 S31: 0.2063 S32: 0.0742 S33: -0.1208
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS.
REMARK 3 ATOM RECORD CONTAINS SUM OF TLS AND RESIDUAL B FACTORS.
REMARK 3 ANISOU RECORD CONTAINS SUM OF TLS AND RESIDUAL U FACTORS.
REMARK 4
REMARK 4 2XMC COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 27-JUL-10.
REMARK 100 THE PDBE ID CODE IS EBI-44795.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-JAN-08
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 : ID14-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.934
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
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 : 29897
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.40
REMARK 200 RESOLUTION RANGE LOW (A) : 41.10
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.7
REMARK 200 DATA REDUNDANCY : 5.1
REMARK 200 R MERGE (I) : 0.06
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 28.00
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.50
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.2
REMARK 200 DATA REDUNDANCY IN SHELL : 7.1
REMARK 200 R MERGE FOR SHELL (I) : 0.51
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.60
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 (%): 56
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.8
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE 2.1 M,
REMARK 280 2-(N-MORPHOLINO)-ETHANESULFONIC ACID 0.1 M, PH 6.5, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 298.0K
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 77.79500
REMARK 290 SMTRY2 9 0.000000 1.000000 0.000000 77.79500
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 63.99500
REMARK 290 SMTRY1 10 -1.000000 0.000000 0.000000 77.79500
REMARK 290 SMTRY2 10 0.000000 -1.000000 0.000000 77.79500
REMARK 290 SMTRY3 10 0.000000 0.000000 1.000000 63.99500
REMARK 290 SMTRY1 11 0.000000 -1.000000 0.000000 77.79500
REMARK 290 SMTRY2 11 1.000000 0.000000 0.000000 77.79500
REMARK 290 SMTRY3 11 0.000000 0.000000 1.000000 63.99500
REMARK 290 SMTRY1 12 0.000000 1.000000 0.000000 77.79500
REMARK 290 SMTRY2 12 -1.000000 0.000000 0.000000 77.79500
REMARK 290 SMTRY3 12 0.000000 0.000000 1.000000 63.99500
REMARK 290 SMTRY1 13 -1.000000 0.000000 0.000000 77.79500
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 77.79500
REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 63.99500
REMARK 290 SMTRY1 14 1.000000 0.000000 0.000000 77.79500
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 77.79500
REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 63.99500
REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 77.79500
REMARK 290 SMTRY2 15 1.000000 0.000000 0.000000 77.79500
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 63.99500
REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 77.79500
REMARK 290 SMTRY2 16 -1.000000 0.000000 0.000000 77.79500
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 63.99500
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: OCTAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 48780 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 157700 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -170.8 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 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 3 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 4 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT1 5 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT2 5 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 5 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 6 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 6 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 6 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 7 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 7 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 400
REMARK 400 COMPOUND
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, ASN 45 TO GLN
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, GLY 145 TO HIS
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, ASN 483 TO GLN
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, ASN 509 TO GLN
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, ASN 514 TO GLN
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 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 UNK UNX A 1531 UNK UNX A 1532 1.54
REMARK 500 UNK UNX A 1536 UNK UNX A 1537 1.61
REMARK 500 UNK UNX A 1540 UNK UNX A 1541 1.72
REMARK 500 UNK UNX A 1541 UNK UNX A 1542 1.91
REMARK 500 UNK UNX A 1544 UNK UNX A 1547 1.96
REMARK 500 UNK UNX A 1541 UNK UNX A 1543 2.00
REMARK 500 UNK UNX A 1537 UNK UNX A 1538 2.03
REMARK 500 UNK UNX A 1532 UNK UNX A 1534 2.04
REMARK 500 UNK UNX A 1532 UNK UNX A 1533 2.07
REMARK 500 O PRO A 157 O HOH A 2090 2.12
REMARK 500
REMARK 500 REMARK: NULL
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 PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 42 NE - CZ - NH2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 ARG A 465 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
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 21 58.09 37.82
REMARK 500 PHE A 43 -8.45 85.89
REMARK 500 ASP A 54 146.77 145.41
REMARK 500 MET A 81 -9.85 -58.86
REMARK 500 SER A 89 145.79 -177.98
REMARK 500 CYS A 92 14.25 -141.31
REMARK 500 ASN A 106 56.85 -157.99
REMARK 500 PHE A 118 9.57 59.48
REMARK 500 PRO A 160 1.05 -69.24
REMARK 500 ALA A 162 72.85 -156.58
REMARK 500 SER A 198 -121.49 61.26
REMARK 500 ARG A 254 -130.24 -136.11
REMARK 500 GLU A 255 39.80 159.37
REMARK 500 GLU A 257 -26.17 -39.94
REMARK 500 ASP A 297 -77.18 -129.83
REMARK 500 GLN A 311 79.70 -100.38
REMARK 500 VAL A 361 101.53 17.58
REMARK 500 ASP A 378 -61.64 -148.44
REMARK 500 ASP A 379 -31.52 -21.93
REMARK 500 GLN A 380 71.42 58.03
REMARK 500 ARG A 381 72.76 49.10
REMARK 500 PHE A 398 -55.36 -132.01
REMARK 500 GLN A 455 -20.73 93.57
REMARK 500 ASN A 485 40.62 -106.06
REMARK 500 GLN A 486 64.17 39.55
REMARK 500 THR A 496 -92.70 94.98
REMARK 500 GLU A 506 -88.48 -88.17
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 SER A 53 ASP A 54 -148.05
REMARK 500 ARG A 254 GLU A 255 147.54
REMARK 500 GLU A 255 ASN A 256 144.29
REMARK 500 GLY A 360 VAL A 361 63.29
REMARK 500 GLN A 380 ARG A 381 39.56
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 VAL A 361 10.7 L L OUTSIDE RANGE
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 F A1530
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1548
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A1549
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A1550
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A1552
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A1553
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A1565
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1559
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1560
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1561
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF
REMARK 800 SUGAR BOUND TO ASN A 106 RESIDUES 1557 TO 1558
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF
REMARK 800 SUGAR BOUND TO ASN A 241 RESIDUES 1562 TO 1564
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF
REMARK 800 SUGAR BOUND TO ASN A 341 RESIDUES 1554 TO 1556
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2WSL RELATED DB: PDB
REMARK 900 AGED FORM OF HUMAN BUTYRYLCHOLINESTERASE
REMARK 900 INHIBITED BY TABUN ANALOGUE TA4
REMARK 900 RELATED ID: 2J4C RELATED DB: PDB
REMARK 900 STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE IN
REMARK 900 COMPLEX WITH 10MM HGCL2
REMARK 900 RELATED ID: 2WIK RELATED DB: PDB
REMARK 900 NONAGED FORM OF HUMAN BUTYRYLCHOLINESTERASE
REMARK 900 INHIBITED BY TABUN ANALOGUE TA6
REMARK 900 RELATED ID: 1KCJ RELATED DB: PDB
REMARK 900 MODEL OF (-)-COCAINE-BOUND (-)-COCAINE
REMARK 900 HYDROLASE COMPLEX
REMARK 900 RELATED ID: 1P0P RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF SOMAN-AGED HUMAN
REMARK 900 BUTYRYLCHOLINESTERASE IN COMPLEX WITH THE
REMARK 900 SUBSTRATE ANALOGBUTYRYLTHIOCHOLINE
REMARK 900 RELATED ID: 1XLU RELATED DB: PDB
REMARK 900 X-RAY STRUCTURE OF DI-ISOPROPYL-PHOSPHORO-
REMARK 900 FLUORIDATE (DFP)INHIBITED BUTYRYLCHOLINESTERASE
REMARK 900 AFTER AGING
REMARK 900 RELATED ID: 2WIJ RELATED DB: PDB
REMARK 900 NONAGED FORM OF HUMAN BUTYRYLCHOLINESTERASE
REMARK 900 INHIBITED BY TABUN ANALOGUE TA5
REMARK 900 RELATED ID: 1XLV RELATED DB: PDB
REMARK 900 ETHYLPHOSPHORYLATED BUTYRYLCHOLINESTERASE (AGED)
REMARK 900 OBTAINEDBY REACTION WITH ECHOTHIOPHATE
REMARK 900 RELATED ID: 1EHO RELATED DB: PDB
REMARK 900 MODEL OF (-)-COCAINE-BOUND BCHE COMPLEX.
REMARK 900 RELATED ID: 1P0M RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN BUTYRYL
REMARK 900 CHOLINESTERASE INCOMPLEX WITH A CHOLINE
REMARK 900 MOLECULE
REMARK 900 RELATED ID: 1XLW RELATED DB: PDB
REMARK 900 DIETHYLPHOSPHORYLATED BUTYRYLCHOLINESTERASE (NONAGED
REMARK 900 )OBTAINED BY REACTION WITH ECHOTHIOPHATE
REMARK 900 RELATED ID: 1EHQ RELATED DB: PDB
REMARK 900 MODEL OF (+)-COCAINE-BOUND BCHE COMPLEX
REMARK 900 RELATED ID: 1P0Q RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF SOMAN-AGED HUMAN
REMARK 900 BUTYRYL CHOLINESTERASE
REMARK 900 RELATED ID: 2WID RELATED DB: PDB
REMARK 900 AGED FORM OF HUMAN BUTYRYLCHOLINESTERASE
REMARK 900 INHIBITED BY TABUN ANALOGUE TA1
REMARK 900 RELATED ID: 2WIL RELATED DB: PDB
REMARK 900 AGED FORM OF HUMAN BUTYRYLCHOLINESTERASE
REMARK 900 INHIBITED BY TABUN ANALOGUE TA5
REMARK 900 RELATED ID: 2WIF RELATED DB: PDB
REMARK 900 AGED FORM OF HUMAN BUTYRYLCHOLINESTERASE
REMARK 900 INHIBITED BY TABUN ANALOGUE TA1
REMARK 900 RELATED ID: 1P0I RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN BUTYRYL
REMARK 900 CHOLINESTERASE
REMARK 900 RELATED ID: 2WIG RELATED DB: PDB
REMARK 900 NONAGED FORM OF HUMAN BUTYRYLCHOLINESTERASE
REMARK 900 INHIBITED BY TABUN ANALOGUE TA4
REMARK 900 RELATED ID: 2XMD RELATED DB: PDB
REMARK 900 G117H MUTANT OF HUMAN BUTYRYLCHOLINESTERASE IN
REMARK 900 COMPLEX WITH ECHOTHIOPHATE
REMARK 900 RELATED ID: 2XMB RELATED DB: PDB
REMARK 900 G117H MUTANT OF HUMAN BUTYRYLCHOLINESTERASE IN
REMARK 900 COMPLEX WITH SULFATE
REMARK 900 RELATED ID: 2XMG RELATED DB: PDB
REMARK 900 G117H MUTANT OF HUMAN BUTYRYLCHOLINESTERASE IN
REMARK 900 COMPLEX WITH VX
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 5 MUTATIONS, N17Q, G117H, N455Q, N481Q, N486Q
DBREF 2XMC A 1 529 UNP P06276 CHLE_HUMAN 29 557
SEQADV 2XMC GLN A 17 UNP P06276 ASN 45 ENGINEERED MUTATION
SEQADV 2XMC HIS A 117 UNP P06276 GLY 145 ENGINEERED MUTATION
SEQADV 2XMC GLN A 455 UNP P06276 ASN 483 ENGINEERED MUTATION
SEQADV 2XMC GLN A 481 UNP P06276 ASN 509 ENGINEERED MUTATION
SEQADV 2XMC 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 HIS
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 F A1530 1
HET SO4 A1548 5
HET CL A1549 1
HET CL A1550 1
HET CL A1551 1
HET CL A1552 1
HET K A1553 1
HET CL A1565 1
HET NAG A1554 14
HET NAG A1555 14
HET FUC A1556 10
HET NAG A1557 14
HET FUC A1558 10
HET NAG A1559 14
HET NAG A1560 14
HET NAG A1561 14
HET NAG A1562 14
HET NAG A1563 14
HET FUC A1564 10
HET UNX A1531 1
HET UNX A1532 1
HET UNX A1533 1
HET UNX A1534 1
HET UNX A1535 1
HET UNX A1536 1
HET UNX A1537 1
HET UNX A1538 1
HET UNX A1539 1
HET UNX A1540 1
HET UNX A1541 1
HET UNX A1542 1
HET UNX A1543 1
HET UNX A1544 1
HET UNX A1545 1
HET UNX A1546 1
HET UNX A1547 1
HETNAM K POTASSIUM ION
HETNAM SO4 SULFATE ION
HETNAM CL CHLORIDE ION
HETNAM F FLUORIDE ION
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM FUC ALPHA-L-FUCOSE
HETNAM UNX UNKNOWN ATOM OR ION
FORMUL 2 SO4 O4 S 2-
FORMUL 3 CL 5(CL 1-)
FORMUL 4 FUC 3(C6 H12 O5)
FORMUL 5 NAG 8(C8 H15 N O6)
FORMUL 6 UNX 17(X)
FORMUL 7 HOH *229(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 VAL A 148 LEU A 154 1 7
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 LYS A 267 1 12
HELIX 12 12 ASP A 268 GLU A 276 1 9
HELIX 13 13 ALA A 277 VAL A 280 5 4
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 GLU A 451 GLN A 455 5 5
HELIX 24 24 THR A 457 GLY A 478 1 22
HELIX 25 25 ARG A 515 PHE A 525 1 11
HELIX 26 26 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 ALA A 101 -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
SSBOND 1 CYS A 65 CYS A 92 1555 1555 2.09
SSBOND 2 CYS A 252 CYS A 263 1555 1555 2.08
SSBOND 3 CYS A 400 CYS A 519 1555 1555 2.07
LINK ND2 ASN A 57 C1 NAG A1559 1555 1555 1.46
LINK ND2 ASN A 106 C1 NAG A1557 1555 1555 1.46
LINK ND2 ASN A 241 C1 NAG A1562 1555 1555 1.45
LINK ND2 ASN A 256 C1 NAG A1561 1555 1555 1.44
LINK ND2 ASN A 341 C1 NAG A1554 1555 1555 1.45
LINK ND2 ASN A 485 C1 NAG A1560 1555 1555 1.45
LINK K K A1553 O HOH A2212 1555 1555 2.93
LINK O4 NAG A1554 C1 NAG A1555 1555 1555 1.44
LINK O6 NAG A1554 C1 FUC A1556 1555 1555 1.44
LINK O6 NAG A1557 C1 FUC A1558 1555 1555 1.45
LINK O6 NAG A1562 C1 FUC A1564 1555 1555 1.45
LINK O4 NAG A1562 C1 NAG A1563 1555 1555 1.47
CISPEP 1 ALA A 101 PRO A 102 0 4.86
CISPEP 2 VAL A 377 ASP A 378 0 -24.19
SITE 1 AC1 5 GLY A 116 HIS A 117 SER A 198 ALA A 199
SITE 2 AC1 5 HOH A2101
SITE 1 AC2 4 GLN A 316 GLY A 413 ASN A 414 ASN A 415
SITE 1 AC3 3 PHE A 21 GLU A 451 ARG A 453
SITE 1 AC4 3 THR A 488 THR A 508 HOH A2187
SITE 1 AC5 2 TYR A 420 HOH A2212
SITE 1 AC6 2 ARG A 515 HOH A2212
SITE 1 AC7 1 THR A 512
SITE 1 AC8 2 ASN A 57 HOH A2225
SITE 1 AC9 4 ARG A 465 GLU A 482 ASN A 485 HOH A2226
SITE 1 BC1 2 ASN A 256 THR A 258
SITE 1 BC2 6 ASN A 106 ASN A 188 LYS A 190 SER A 191
SITE 2 BC2 6 HOH A2222 HOH A2223
SITE 1 BC3 6 ASN A 241 ASN A 245 PHE A 278 VAL A 279
SITE 2 BC3 6 HOH A2228 HOH A2229
SITE 1 BC4 3 SER A 338 ASN A 341 ASN A 342
CRYST1 155.590 155.590 127.990 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 0.006427 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006427 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007813 0.00000
TER 4217 VAL A 529
MASTER 671 0 36 26 14 0 16 6 4616 1 161 41
END |