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HEADER HYDROLASE 27-JUL-10 2XMG
TITLE G117H MUTANT OF HUMAN BUTYRYLCHOLINESTERASE IN COMPLEX WITH
TITLE 2 VX
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 GLYCOPROTEIN, HYDROLASE
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 2XMG 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. 2.70 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) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 110.43
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.29
REMARK 3 NUMBER OF REFLECTIONS : 20059
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) : 0.17916
REMARK 3 R VALUE (WORKING SET) : 0.17623
REMARK 3 FREE R VALUE : 0.25047
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.2
REMARK 3 FREE R VALUE TEST SET COUNT : 880
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) : 2.700
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.770
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1475
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.97
REMARK 3 BIN R VALUE (WORKING SET) : 0.275
REMARK 3 BIN FREE R VALUE SET COUNT : 54
REMARK 3 BIN FREE R VALUE : 0.357
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4226
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 167
REMARK 3 SOLVENT ATOMS : 151
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 56.147
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.18
REMARK 3 B22 (A**2) : -1.18
REMARK 3 B33 (A**2) : 2.36
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): 0.765
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.333
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.239
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 25.354
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.955
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.907
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4516 ; 0.018 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6152 ; 1.933 ; 1.981
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 530 ; 7.342 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 206 ;36.159 ;24.029
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 706 ;19.289 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 22 ;21.545 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 675 ; 0.128 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3443 ; 0.008 ; 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): 2632 ; 0.675 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4254 ; 1.313 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1884 ; 2.349 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1897 ; 3.958 ; 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: 0.2993 T22: 0.4820
REMARK 3 T33: 0.1277 T12: 0.0642
REMARK 3 T13: 0.0806 T23: -0.1789
REMARK 3 L TENSOR
REMARK 3 L11: 3.8991 L22: 4.8661
REMARK 3 L33: 1.7496 L12: 1.6458
REMARK 3 L13: -0.8329 L23: 0.6040
REMARK 3 S TENSOR
REMARK 3 S11: -0.1636 S12: 1.2809 S13: -0.2888
REMARK 3 S21: -1.3057 S22: 0.0654 S23: 0.0019
REMARK 3 S31: 0.3232 S32: -0.2801 S33: 0.0981
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: 0.1058 T22: 0.1519
REMARK 3 T33: 0.3898 T12: 0.0967
REMARK 3 T13: 0.1390 T23: -0.0937
REMARK 3 L TENSOR
REMARK 3 L11: 1.2198 L22: 1.5511
REMARK 3 L33: 5.7121 L12: -0.7230
REMARK 3 L13: 0.7826 L23: -1.8913
REMARK 3 S TENSOR
REMARK 3 S11: 0.1292 S12: 0.2531 S13: -0.1061
REMARK 3 S21: -0.0697 S22: -0.3369 S23: -0.6249
REMARK 3 S31: 0.3637 S32: 0.5974 S33: 0.2077
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: -0.0139 T22: 0.0475
REMARK 3 T33: 0.1079 T12: 0.0869
REMARK 3 T13: 0.0746 T23: -0.0482
REMARK 3 L TENSOR
REMARK 3 L11: 3.3860 L22: 2.7054
REMARK 3 L33: 2.5862 L12: 0.7579
REMARK 3 L13: -0.1607 L23: 1.1379
REMARK 3 S TENSOR
REMARK 3 S11: 0.1015 S12: 0.3754 S13: 0.0635
REMARK 3 S21: -0.2462 S22: -0.0652 S23: -0.0428
REMARK 3 S31: 0.1067 S32: -0.1165 S33: -0.0364
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: 0.2458 T22: 0.4350
REMARK 3 T33: 0.5466 T12: -0.1654
REMARK 3 T13: 0.2126 T23: 0.0013
REMARK 3 L TENSOR
REMARK 3 L11: 5.9461 L22: 3.2439
REMARK 3 L33: 13.1047 L12: 1.2106
REMARK 3 L13: -7.6653 L23: -2.6491
REMARK 3 S TENSOR
REMARK 3 S11: 0.3483 S12: -0.4482 S13: 0.3656
REMARK 3 S21: 0.0387 S22: -0.3487 S23: -0.9626
REMARK 3 S31: -1.2595 S32: 1.7806 S33: 0.0004
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: 0.0310 T22: -0.0182
REMARK 3 T33: 0.2392 T12: 0.0128
REMARK 3 T13: 0.0594 T23: -0.0696
REMARK 3 L TENSOR
REMARK 3 L11: 1.8182 L22: 1.5625
REMARK 3 L33: 2.0707 L12: -1.1236
REMARK 3 L13: -0.7769 L23: -0.0844
REMARK 3 S TENSOR
REMARK 3 S11: 0.0988 S12: 0.1110 S13: 0.2832
REMARK 3 S21: 0.0987 S22: 0.1148 S23: -0.2676
REMARK 3 S31: -0.2777 S32: 0.1067 S33: -0.2136
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: 0.0940 T22: -0.0016
REMARK 3 T33: 0.1241 T12: 0.0323
REMARK 3 T13: 0.0271 T23: -0.0417
REMARK 3 L TENSOR
REMARK 3 L11: 4.3467 L22: 1.6289
REMARK 3 L33: 2.3100 L12: 0.2598
REMARK 3 L13: 0.6664 L23: 0.8767
REMARK 3 S TENSOR
REMARK 3 S11: 0.0903 S12: -0.2195 S13: -0.2016
REMARK 3 S21: 0.4551 S22: 0.1131 S23: -0.1982
REMARK 3 S31: 0.2382 S32: 0.1050 S33: -0.2034
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 RIDING
REMARK 3 POSITIONS. ATOM RECORD CONTAINS SUM OF TLS AND RESIDUAL B
REMARK 3 FACTORS. ANISOU RECORD CONTAINS SUM OF TLS AND RESIDUAL U FACTORS.
REMARK 4
REMARK 4 2XMG 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-44800.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-NOV-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.8726
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20940
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.70
REMARK 200 RESOLUTION RANGE LOW (A) : 110.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.3
REMARK 200 DATA REDUNDANCY : 8.0
REMARK 200 R MERGE (I) : 0.07
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 23.70
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.80
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.4
REMARK 200 R MERGE FOR SHELL (I) : 0.60
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.80
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 (%): 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 78.28500
REMARK 290 SMTRY2 9 0.000000 1.000000 0.000000 78.28500
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 64.19500
REMARK 290 SMTRY1 10 -1.000000 0.000000 0.000000 78.28500
REMARK 290 SMTRY2 10 0.000000 -1.000000 0.000000 78.28500
REMARK 290 SMTRY3 10 0.000000 0.000000 1.000000 64.19500
REMARK 290 SMTRY1 11 0.000000 -1.000000 0.000000 78.28500
REMARK 290 SMTRY2 11 1.000000 0.000000 0.000000 78.28500
REMARK 290 SMTRY3 11 0.000000 0.000000 1.000000 64.19500
REMARK 290 SMTRY1 12 0.000000 1.000000 0.000000 78.28500
REMARK 290 SMTRY2 12 -1.000000 0.000000 0.000000 78.28500
REMARK 290 SMTRY3 12 0.000000 0.000000 1.000000 64.19500
REMARK 290 SMTRY1 13 -1.000000 0.000000 0.000000 78.28500
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 78.28500
REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 64.19500
REMARK 290 SMTRY1 14 1.000000 0.000000 0.000000 78.28500
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 78.28500
REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 64.19500
REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 78.28500
REMARK 290 SMTRY2 15 1.000000 0.000000 0.000000 78.28500
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 64.19500
REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 78.28500
REMARK 290 SMTRY2 16 -1.000000 0.000000 0.000000 78.28500
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 64.19500
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: 51160 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 161200 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -81.2 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 1537 UNK UNX A 1542 2.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 404 CG GLU A 404 CD 0.091
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 58.68 37.89
REMARK 500 PHE A 43 -12.31 71.69
REMARK 500 LYS A 51 144.30 96.79
REMARK 500 ASP A 54 165.16 72.11
REMARK 500 ASN A 63 125.79 -27.55
REMARK 500 ASP A 87 145.68 -35.95
REMARK 500 ASN A 106 58.90 -156.25
REMARK 500 PHE A 118 9.61 59.86
REMARK 500 ASN A 159 107.89 -49.49
REMARK 500 ALA A 162 81.98 -158.69
REMARK 500 SER A 198 -120.98 58.11
REMARK 500 SER A 253 107.60 -55.70
REMARK 500 ARG A 254 -162.99 -107.95
REMARK 500 GLU A 255 -59.92 -122.34
REMARK 500 GLU A 276 -44.60 -29.89
REMARK 500 ASP A 297 -77.41 -120.87
REMARK 500 TYR A 332 35.15 -94.50
REMARK 500 VAL A 361 102.37 30.68
REMARK 500 ASP A 378 -47.47 -162.01
REMARK 500 ASP A 379 -43.60 -17.82
REMARK 500 GLN A 380 63.68 63.27
REMARK 500 ARG A 381 71.80 62.53
REMARK 500 PHE A 398 -61.26 -128.05
REMARK 500 PRO A 480 57.09 -91.37
REMARK 500 THR A 496 -80.80 77.99
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 GLY A 360 VAL A 361 48.00
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 16.3 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 VX A1530
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1531
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A1532
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A1533
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A1534
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A1535
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NH4 A1543
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1549
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1550
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1551
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A1555
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 106 RESIDUES 1547 TO 1548
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 241 RESIDUES 1552 TO 1554
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF
REMARK 800 SUGAR BOUND TO ASN A 341 RESIDUES 1544 TO 1546
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: 2XMB RELATED DB: PDB
REMARK 900 G117H MUTANT OF HUMAN BUTYRYLCHOLINESTERASE IN
REMARK 900 COMPLEX WITH SULFATE
REMARK 900 RELATED ID: 1KCJ RELATED DB: PDB
REMARK 900 MODEL OF (-)-COCAINE-BOUND (-)-COCAINE
REMARK 900 HYDROLASE COMPLEX
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: 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: 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: 2WIJ RELATED DB: PDB
REMARK 900 NONAGED FORM OF HUMAN BUTYRYLCHOLINESTERASE
REMARK 900 INHIBITED BY TABUN ANALOGUE TA5
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: 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: 2XMC RELATED DB: PDB
REMARK 900 G117H MUTANT OF HUMAN BUTYRYLCHOLINESTERASE IN
REMARK 900 COMPLEX WITH FLUORIDE ANION
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 FIVE MUTATIONS, N17Q, G117H, N455Q, N481Q, N486Q
DBREF 2XMG A 1 529 UNP P06276 CHLE_HUMAN 29 557
SEQADV 2XMG GLN A 17 UNP P06276 ASN 45 ENGINEERED MUTATION
SEQADV 2XMG HIS A 117 UNP P06276 GLY 145 ENGINEERED MUTATION
SEQADV 2XMG GLN A 455 UNP P06276 ASN 483 ENGINEERED MUTATION
SEQADV 2XMG GLN A 481 UNP P06276 ASN 509 ENGINEERED MUTATION
SEQADV 2XMG 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 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 VX A1530 6
HET SO4 A1531 5
HET CL A1532 1
HET CL A1533 1
HET CL A1534 1
HET CL A1535 1
HET NH4 A1543 1
HET NAG A1544 14
HET NAG A1545 14
HET FUL A1546 10
HET NAG A1547 14
HET FUL A1548 10
HET NAG A1549 14
HET NAG A1550 14
HET NAG A1551 14
HET NAG A1552 14
HET NAG A1553 14
HET FUL A1554 10
HET CL A1555 1
HET NH4 A1556 1
HETNAM UNX UNKNOWN ATOM OR ION
HETNAM VX O-ETHYLMETHYLPHOSPHONIC ACID ESTER GROUP
HETNAM SO4 SULFATE ION
HETNAM CL CHLORIDE ION
HETNAM NH4 AMMONIUM ION
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM FUL BETA-L-FUCOSE
HETSYN FUL 6-DEOXY-BETA-L-GALACTOSE
FORMUL 2 UNX 7(X)
FORMUL 3 VX C3 H9 O3 P
FORMUL 4 SO4 O4 S 2-
FORMUL 5 CL 5(CL 1-)
FORMUL 6 NH4 2(H4 N 1+)
FORMUL 7 NAG 8(C8 H15 N O6)
FORMUL 8 FUL 3(C6 H12 O5)
FORMUL 9 HOH *151(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 SER A 198 LEU A 208 1 11
HELIX 8 8 SER A 210 PHE A 217 5 8
HELIX 9 9 SER A 235 THR A 250 1 16
HELIX 10 10 ASN A 256 ARG A 265 1 10
HELIX 11 11 ASP A 268 ALA A 277 1 10
HELIX 12 12 MET A 302 LEU A 309 1 8
HELIX 13 13 GLU A 325 GLY A 333 5 9
HELIX 14 14 THR A 346 PHE A 358 1 13
HELIX 15 15 SER A 362 THR A 374 1 13
HELIX 16 16 GLU A 383 PHE A 398 1 16
HELIX 17 17 PHE A 398 GLU A 411 1 14
HELIX 18 18 PRO A 431 GLY A 435 5 5
HELIX 19 19 GLU A 441 GLY A 447 1 7
HELIX 20 20 LEU A 448 GLN A 455 5 8
HELIX 21 21 THR A 457 GLY A 478 1 22
HELIX 22 22 ARG A 515 PHE A 525 1 11
HELIX 23 23 PHE A 526 VAL A 529 5 4
SHEET 1 AA 3 ILE A 5 ALA A 7 0
SHEET 2 AA 3 LYS A 12 ARG A 14 -1 O VAL A 13 N ILE A 6
SHEET 3 AA 3 TRP A 56 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
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 2.06
SSBOND 2 CYS A 252 CYS A 263 1555 1555 2.08
SSBOND 3 CYS A 400 CYS A 519 1555 1555 2.08
LINK ND2 ASN A 57 C1 NAG A1549 1555 1555 1.47
LINK ND2 ASN A 106 C1 NAG A1547 1555 1555 1.47
LINK OG SER A 198 P1 VX A1530 1555 1555 1.67
LINK ND2 ASN A 241 C1 NAG A1552 1555 1555 1.47
LINK ND2 ASN A 256 C1 NAG A1551 1555 1555 1.46
LINK ND2 ASN A 341 C1 NAG A1544 1555 1555 1.44
LINK ND2 ASN A 485 C1 NAG A1550 1555 1555 1.46
LINK O6 NAG A1544 C1 FUL A1546 1555 1555 1.44
LINK O4 NAG A1544 C1 NAG A1545 1555 1555 1.44
LINK O6 NAG A1547 C1 FUL A1548 1555 1555 1.45
LINK O4 NAG A1552 C1 NAG A1553 1555 1555 1.46
LINK O6 NAG A1552 C1 FUL A1554 1555 1555 1.45
CISPEP 1 ALA A 101 PRO A 102 0 1.71
CISPEP 2 VAL A 377 ASP A 378 0 -2.51
CISPEP 3 GLN A 380 ARG A 381 0 28.43
SITE 1 AC1 5 GLY A 116 HIS A 117 SER A 198 ALA A 199
SITE 2 AC1 5 HIS A 438
SITE 1 AC2 4 GLN A 316 GLY A 413 ASN A 414 ASN A 415
SITE 1 AC3 3 LYS A 323 TYR A 420 HOH A2144
SITE 1 AC4 1 ARG A 347
SITE 1 AC5 1 ARG A 515
SITE 1 AC6 1 THR A 508
SITE 1 AC7 3 GLU A 443 HOH A2146 HOH A2147
SITE 1 AC8 3 ARG A 14 ASN A 57 HOH A2150
SITE 1 AC9 3 ARG A 465 ASN A 485 HOH A2151
SITE 1 BC1 2 ASN A 256 HOH A2061
SITE 1 BC2 1 THR A 512
SITE 1 BC3 4 ASN A 106 ASN A 188 LYS A 190 HOH A2149
SITE 1 BC4 5 ASN A 241 ASN A 245 LEU A 249 PHE A 278
SITE 2 BC4 5 PRO A 281
SITE 1 BC5 4 GLY A 336 SER A 338 ASN A 341 HOH A2148
CRYST1 156.570 156.570 128.390 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 0.006387 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006387 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007789 0.00000
TER 4227 VAL A 529
MASTER 658 0 27 23 16 0 16 6 4544 1 166 41
END |