| 4BDT-pdb | HEADER HYDROLASE/INHIBITOR 06-OCT-12 4BDT
TITLE HUMAN ACETYLCHOLINESTERASE IN COMPLEX WITH HUPRINE W AND
TITLE 2 FASCICULIN 2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYLCHOLINESTERASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ACHE;
COMPND 5 EC: 3.1.1.7;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: FASCICULIN-2;
COMPND 9 CHAIN: B;
COMPND 10 SYNONYM: FAS-2, FAS2, ACETYLCHOLINESTERASE TOXIN F-VII,
COMPND 11 FASCICULIN-II, FAS-II, TOXIN TA1
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_STRAIN: CHO K1;
SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: OVARY CELLS;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PGS;
SOURCE 12 MOL_ID: 2;
SOURCE 13 ORGANISM_SCIENTIFIC: DENDROASPIS ANGUSTICEPS;
SOURCE 14 ORGANISM_COMMON: EASTERN GREEN MAMBA;
SOURCE 15 ORGANISM_TAXID: 8618
KEYWDS HYDROLASE-INHIBITOR COMPLEX, BUTYRYLCHOLINESTERASE, NERVE
KEYWDS 2 TRANSMISSION, INHIBITION, 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 4BDT 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. 3.10 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) : 3.104
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 57.934
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.35
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.27
REMARK 3 NUMBER OF REFLECTIONS : 19627
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.1621
REMARK 3 R VALUE (WORKING SET) : 0.1590
REMARK 3 FREE R VALUE : 0.2189
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.0
REMARK 3 FREE R VALUE TEST SET COUNT : 982
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 57.9440 - 5.9360 0.97 2731 144 0.1568 0.1920
REMARK 3 2 5.9360 - 4.7123 0.99 2694 141 0.1392 0.1658
REMARK 3 3 4.7123 - 4.1168 0.99 2663 140 0.1183 0.1932
REMARK 3 4 4.1168 - 3.7405 0.99 2667 141 0.1385 0.2102
REMARK 3 5 3.7405 - 3.4724 0.99 2666 140 0.1801 0.2558
REMARK 3 6 3.4724 - 3.2677 0.99 2625 139 0.2256 0.3233
REMARK 3 7 3.2677 - 3.1041 0.97 2599 137 0.2627 0.3820
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) : 0.36
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.12
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 66.43
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 48.2
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.008 5088
REMARK 3 ANGLE : 1.291 6945
REMARK 3 CHIRALITY : 0.082 738
REMARK 3 PLANARITY : 0.007 910
REMARK 3 DIHEDRAL : 18.319 1845
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A
REMARK 3 ORIGIN FOR THE GROUP (A): 0.4631 -40.5065 -58.4343
REMARK 3 T TENSOR
REMARK 3 T11: 0.2887 T22: 0.0894
REMARK 3 T33: 0.2081 T12: 0.0340
REMARK 3 T13: 0.0166 T23: 0.0542
REMARK 3 L TENSOR
REMARK 3 L11: 1.4688 L22: 1.0520
REMARK 3 L33: 1.6733 L12: -0.1864
REMARK 3 L13: 0.0954 L23: 0.0814
REMARK 3 S TENSOR
REMARK 3 S11: 0.0257 S12: -0.0342 S13: 0.0748
REMARK 3 S21: 0.0915 S22: -0.0296 S23: -0.0205
REMARK 3 S31: -0.1714 S32: -0.0290 S33: 0.0316
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN B
REMARK 3 ORIGIN FOR THE GROUP (A): -19.4319 -36.7207 -38.2366
REMARK 3 T TENSOR
REMARK 3 T11: 0.7041 T22: 0.3712
REMARK 3 T33: 0.4119 T12: 0.1027
REMARK 3 T13: 0.0665 T23: 0.0080
REMARK 3 L TENSOR
REMARK 3 L11: 1.1186 L22: 0.0157
REMARK 3 L33: 0.5367 L12: 0.0830
REMARK 3 L13: 0.7536 L23: 0.0423
REMARK 3 S TENSOR
REMARK 3 S11: 0.0930 S12: -0.6102 S13: 0.2410
REMARK 3 S21: 0.4340 S22: -0.0970 S23: 0.3343
REMARK 3 S31: -0.9828 S32: -0.3926 S33: 0.0022
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 4BDT 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-54355.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-JUN-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-4
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9790
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD (QUANTUM Q315R)
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 : 19677
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.10
REMARK 200 RESOLUTION RANGE LOW (A) : 58.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 200 DATA REDUNDANCY : 3.1
REMARK 200 R MERGE (I) : 0.09
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 16.00
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.20
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.7
REMARK 200 DATA REDUNDANCY IN SHELL : 3.1
REMARK 200 R MERGE FOR SHELL (I) : 0.66
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.00
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 2X8B
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 75
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.9
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES BUFFER PH 7.4, 1.3 M
REMARK 280 AMMONIUM SULFATE
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z
REMARK 290 6555 -X,-X+Y,-Z
REMARK 290 7555 X+2/3,Y+1/3,Z+1/3
REMARK 290 8555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 9555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 10555 Y+2/3,X+1/3,-Z+1/3
REMARK 290 11555 X-Y+2/3,-Y+1/3,-Z+1/3
REMARK 290 12555 -X+2/3,-X+Y+1/3,-Z+1/3
REMARK 290 13555 X+1/3,Y+2/3,Z+2/3
REMARK 290 14555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 15555 -X+Y+1/3,-X+2/3,Z+2/3
REMARK 290 16555 Y+1/3,X+2/3,-Z+2/3
REMARK 290 17555 X-Y+1/3,-Y+2/3,-Z+2/3
REMARK 290 18555 -X+1/3,-X+Y+2/3,-Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 75.80000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 43.76315
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 82.13333
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 75.80000
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 43.76315
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 82.13333
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 75.80000
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 43.76315
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 82.13333
REMARK 290 SMTRY1 10 -0.500000 0.866025 0.000000 75.80000
REMARK 290 SMTRY2 10 0.866025 0.500000 0.000000 43.76315
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 82.13333
REMARK 290 SMTRY1 11 1.000000 0.000000 0.000000 75.80000
REMARK 290 SMTRY2 11 0.000000 -1.000000 0.000000 43.76315
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 82.13333
REMARK 290 SMTRY1 12 -0.500000 -0.866025 0.000000 75.80000
REMARK 290 SMTRY2 12 -0.866025 0.500000 0.000000 43.76315
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 82.13333
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 87.52630
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 164.26667
REMARK 290 SMTRY1 14 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 14 0.866025 -0.500000 0.000000 87.52630
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 164.26667
REMARK 290 SMTRY1 15 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 15 -0.866025 -0.500000 0.000000 87.52630
REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 164.26667
REMARK 290 SMTRY1 16 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 16 0.866025 0.500000 0.000000 87.52630
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 164.26667
REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 17 0.000000 -1.000000 0.000000 87.52630
REMARK 290 SMTRY3 17 0.000000 0.000000 -1.000000 164.26667
REMARK 290 SMTRY1 18 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 18 -0.866025 0.500000 0.000000 87.52630
REMARK 290 SMTRY3 18 0.000000 0.000000 -1.000000 164.26667
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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 300 DETAILS: CHAINA FORMS A BIOLOGICAL DIMER WITH A SYMMETRIC
REMARK 300 MOLECULE BY INTERACTION OF 4 HELICES. THE DODECAMETRIC ASSEMBLY
REMARK 300 SHOWN IN THE ASSEMBLY INFORMATION RESULTS FROM THE ASSOCIATION
REMARK 300 OF 3 BIOLOGICAL DIMERS.
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6750 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 42860 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -155.7 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 -0.500000 0.866025 0.000000 75.80000
REMARK 350 BIOMT2 2 0.866025 0.500000 0.000000 -43.76315
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 -82.13333
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DODECAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 43490 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 129720 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -553.3 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 -0.500000 -0.866025 0.000000 -75.80000
REMARK 350 BIOMT2 2 -0.866025 0.500000 0.000000 -43.76315
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 -82.13333
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 75.80000
REMARK 350 BIOMT2 3 0.866025 0.500000 0.000000 -43.76315
REMARK 350 BIOMT3 3 0.000000 0.000000 -1.000000 -82.13333
REMARK 350 BIOMT1 4 -0.500000 -0.866025 0.000000 -75.80000
REMARK 350 BIOMT2 4 0.866025 -0.500000 0.000000 -131.28945
REMARK 350 BIOMT3 4 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 5 -0.500000 0.866025 0.000000 75.80000
REMARK 350 BIOMT2 5 -0.866025 -0.500000 0.000000 -131.28945
REMARK 350 BIOMT3 5 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 6 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 6 0.000000 -1.000000 0.000000 -175.05260
REMARK 350 BIOMT3 6 0.000000 0.000000 -1.000000 -82.13333
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4080 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24780 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -71.5 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 A2086 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 GLY A 2
REMARK 465 ARG A 3
REMARK 465 GLU A 4
REMARK 465 LYS A 568
REMARK 465 ASN A 569
REMARK 465 GLN A 570
REMARK 465 PHE A 571
REMARK 465 ASP A 572
REMARK 465 HIS A 573
REMARK 465 TYR A 574
REMARK 465 SER A 575
REMARK 465 LYS A 576
REMARK 465 GLN A 577
REMARK 465 ASP A 578
REMARK 465 ARG A 579
REMARK 465 CYS A 580
REMARK 465 SER A 581
REMARK 465 ASP A 582
REMARK 465 LEU A 583
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 GLU A 548 CD
REMARK 480 GLU A 550 CD
REMARK 480 ARG A 551 CZ
REMARK 480 GLN A 552 CD
REMARK 480 TRP A 553 CD1 CD2 CH2
REMARK 480 GLU A 556 CB CD
REMARK 480 HIS A 558 CG
REMARK 480 ARG A 559 NE
REMARK 480 TRP A 560 CD1
REMARK 480 SER A 562 OG
REMARK 480 TYR A 563 CD1
REMARK 480 VAL A 565 CB
REMARK 480 HIS A 566 ND1
REMARK 480 TRP A 567 CD2
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 O GLU A 491 O HOH A 2106 2.17
REMARK 500 O SER A 512 O HOH A 2103 2.19
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 ALA A 6 -64.42 61.89
REMARK 500 GLU A 7 67.23 -156.23
REMARK 500 PHE A 47 -11.74 73.79
REMARK 500 PRO A 88 119.32 -38.91
REMARK 500 ALA A 167 85.77 -154.55
REMARK 500 PRO A 194 7.86 -66.46
REMARK 500 SER A 203 -129.23 64.05
REMARK 500 PRO A 259 -146.71 -84.95
REMARK 500 THR A 262 78.50 -166.98
REMARK 500 PRO A 290 -70.65 -58.35
REMARK 500 ASP A 306 -91.72 -79.76
REMARK 500 SER A 352 52.17 37.38
REMARK 500 VAL A 407 -67.06 -128.04
REMARK 500 GLU A 431 55.30 -117.70
REMARK 500 HIS A 447 107.48 -27.67
REMARK 500 ASN A 464 54.82 -91.24
REMARK 500 GLU A 491 170.07 62.59
REMARK 500 ARG A 493 -156.20 -113.31
REMARK 500 PRO A 495 -144.47 -71.94
REMARK 500 ASN B 20 -153.37 -72.29
REMARK 500 ASP B 45 -156.29 -163.37
REMARK 500 THR B 54 -83.13 -128.61
REMARK 500 ASP B 57 118.33 72.56
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 HUW A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 804
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 805
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 806
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 807
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 808
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 809
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 810
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 811
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 812
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF SUGAR BOUND TO
REMARK 800 ASN A 350 RESIDUES 601 TO 603
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1B41 RELATED DB: PDB
REMARK 900 HUMAN ACETYLCHOLINESTERASE COMPLEXED WITH FASCICULIN-II,
REMARK 900 GLYCOSYLATED PROTEIN
REMARK 900 RELATED ID: 1F8U RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MUTANT E202Q OF
REMARK 900 HUMANACETYLCHOLINESTERASE COMPLEXED WITH GREEN MAMBA
REMARK 900 VENOMPEPTIDE FASCICULIN-II
REMARK 900 RELATED ID: 1FSC RELATED DB: PDB
REMARK 900 FASCICULIN 2 (SYNCHROTRON X-RAY DIFFRACTION)
REMARK 900 RELATED ID: 1FSS RELATED DB: PDB
REMARK 900 ACETYLCHOLINESTERASE COMPLEXED WITH FASCICULIN-II
REMARK 900 RELATED ID: 1KU6 RELATED DB: PDB
REMARK 900 FASCICULIN 2-MOUSE ACETYLCHOLINESTERASE COMPLEX
REMARK 900 RELATED ID: 1MAH RELATED DB: PDB
REMARK 900 FASCICULIN2 - MOUSE ACETYLCHOLINESTERASE COMPLEX
REMARK 900 RELATED ID: 1PUV RELATED DB: PDB
REMARK 900 THEORETICAL MODEL OF THE DIISOPROPYLPHOSPHORYL-
REMARK 900 ACETYLCHOLINESTERASE COMPLEXED WITH 1,7-HEPTYLENE-BIS-N
REMARK 900 ,N'-SYN-2-PYRIDINIUMALDOXIME
REMARK 900 RELATED ID: 1PUW RELATED DB: PDB
REMARK 900 THEORETICAL MODEL OF THE DIISOPROPYLPHOSPHORYL-
REMARK 900 ACETYLCHOLINESTERASE COMPLEXED WITH 1,3-PROPYLENE-BIS-N
REMARK 900 ,N'-SYN-4-PYRIDINIUMALDOXIME
REMARK 900 RELATED ID: 1VZJ RELATED DB: PDB
REMARK 900 STRUCTURE OF THE TETRAMERIZATION DOMAIN OF
REMARK 900 ACETYLCHOLINESTERASE: FOUR-FOLD INTERACTION OF A WWW
REMARK 900 MOTIF WITH A LEFT-HANDED POLYPROLINE HELIX
REMARK 900 RELATED ID: 2CLJ RELATED DB: PDB
REMARK 900 HOMOLOGY-BUILT MODEL OF HUMAN ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 2X8B RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN ACETYLCHOLINESTERASE INHIBITED
REMARK 900 BY AGED TABUN AND COMPLEXED WITH FASCICULIN-II
REMARK 900 RELATED ID: 4BDS RELATED DB: PDB
REMARK 900 HUMAN BUTYRYLCHOLINESTERASE IN COMPLEX WITH TACRINE
DBREF 4BDT A 1 583 UNP P22303 ACES_HUMAN 32 614
DBREF 4BDT B 1 61 UNP P0C1Z0 TXFA2_DENAN 1 61
SEQRES 1 A 583 GLU GLY ARG GLU ASP ALA GLU LEU LEU VAL THR VAL ARG
SEQRES 2 A 583 GLY GLY ARG LEU ARG GLY ILE ARG LEU LYS THR PRO GLY
SEQRES 3 A 583 GLY PRO VAL SER ALA PHE LEU GLY ILE PRO PHE ALA GLU
SEQRES 4 A 583 PRO PRO MET GLY PRO ARG ARG PHE LEU PRO PRO GLU PRO
SEQRES 5 A 583 LYS GLN PRO TRP SER GLY VAL VAL ASP ALA THR THR PHE
SEQRES 6 A 583 GLN SER VAL CYS TYR GLN TYR VAL ASP THR LEU TYR PRO
SEQRES 7 A 583 GLY PHE GLU GLY THR GLU MET TRP ASN PRO ASN ARG GLU
SEQRES 8 A 583 LEU SER GLU ASP CYS LEU TYR LEU ASN VAL TRP THR PRO
SEQRES 9 A 583 TYR PRO ARG PRO THR SER PRO THR PRO VAL LEU VAL TRP
SEQRES 10 A 583 ILE TYR GLY GLY GLY PHE TYR SER GLY ALA SER SER LEU
SEQRES 11 A 583 ASP VAL TYR ASP GLY ARG PHE LEU VAL GLN ALA GLU ARG
SEQRES 12 A 583 THR VAL LEU VAL SER MET ASN TYR ARG VAL GLY ALA PHE
SEQRES 13 A 583 GLY PHE LEU ALA LEU PRO GLY SER ARG GLU ALA PRO GLY
SEQRES 14 A 583 ASN VAL GLY LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP
SEQRES 15 A 583 VAL GLN GLU ASN VAL ALA ALA PHE GLY GLY ASP PRO THR
SEQRES 16 A 583 SER VAL THR LEU PHE GLY GLU SER ALA GLY ALA ALA SER
SEQRES 17 A 583 VAL GLY MET HIS LEU LEU SER PRO PRO SER ARG GLY LEU
SEQRES 18 A 583 PHE HIS ARG ALA VAL LEU GLN SER GLY ALA PRO ASN GLY
SEQRES 19 A 583 PRO TRP ALA THR VAL GLY MET GLY GLU ALA ARG ARG ARG
SEQRES 20 A 583 ALA THR GLN LEU ALA HIS LEU VAL GLY CYS PRO PRO GLY
SEQRES 21 A 583 GLY THR GLY GLY ASN ASP THR GLU LEU VAL ALA CYS LEU
SEQRES 22 A 583 ARG THR ARG PRO ALA GLN VAL LEU VAL ASN HIS GLU TRP
SEQRES 23 A 583 HIS VAL LEU PRO GLN GLU SER VAL PHE ARG PHE SER PHE
SEQRES 24 A 583 VAL PRO VAL VAL ASP GLY ASP PHE LEU SER ASP THR PRO
SEQRES 25 A 583 GLU ALA LEU ILE ASN ALA GLY ASP PHE HIS GLY LEU GLN
SEQRES 26 A 583 VAL LEU VAL GLY VAL VAL LYS ASP GLU GLY SER TYR PHE
SEQRES 27 A 583 LEU VAL TYR GLY ALA PRO GLY PHE SER LYS ASP ASN GLU
SEQRES 28 A 583 SER LEU ILE SER ARG ALA GLU PHE LEU ALA GLY VAL ARG
SEQRES 29 A 583 VAL GLY VAL PRO GLN VAL SER ASP LEU ALA ALA GLU ALA
SEQRES 30 A 583 VAL VAL LEU HIS TYR THR ASP TRP LEU HIS PRO GLU ASP
SEQRES 31 A 583 PRO ALA ARG LEU ARG GLU ALA LEU SER ASP VAL VAL GLY
SEQRES 32 A 583 ASP HIS ASN VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY
SEQRES 33 A 583 ARG LEU ALA ALA GLN GLY ALA ARG VAL TYR ALA TYR VAL
SEQRES 34 A 583 PHE GLU HIS ARG ALA SER THR LEU SER TRP PRO LEU TRP
SEQRES 35 A 583 MET GLY VAL PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE
SEQRES 36 A 583 GLY ILE PRO LEU ASP PRO SER ARG ASN TYR THR ALA GLU
SEQRES 37 A 583 GLU LYS ILE PHE ALA GLN ARG LEU MET ARG TYR TRP ALA
SEQRES 38 A 583 ASN PHE ALA ARG THR GLY ASP PRO ASN GLU PRO ARG ASP
SEQRES 39 A 583 PRO LYS ALA PRO GLN TRP PRO PRO TYR THR ALA GLY ALA
SEQRES 40 A 583 GLN GLN TYR VAL SER LEU ASP LEU ARG PRO LEU GLU VAL
SEQRES 41 A 583 ARG ARG GLY LEU ARG ALA GLN ALA CYS ALA PHE TRP ASN
SEQRES 42 A 583 ARG PHE LEU PRO LYS LEU LEU SER ALA THR ASP THR LEU
SEQRES 43 A 583 ASP GLU ALA GLU ARG GLN TRP LYS ALA GLU PHE HIS ARG
SEQRES 44 A 583 TRP SER SER TYR MET VAL HIS TRP LYS ASN GLN PHE ASP
SEQRES 45 A 583 HIS TYR SER LYS GLN ASP ARG CYS SER ASP LEU
SEQRES 1 B 61 THR MET CYS TYR SER HIS THR THR THR SER ARG ALA ILE
SEQRES 2 B 61 LEU THR ASN CYS GLY GLU ASN SER CYS TYR ARG LYS SER
SEQRES 3 B 61 ARG ARG HIS PRO PRO LYS MET VAL LEU GLY ARG GLY CYS
SEQRES 4 B 61 GLY CYS PRO PRO GLY ASP ASP ASN LEU GLU VAL LYS CYS
SEQRES 5 B 61 CYS THR SER PRO ASP LYS CYS ASN TYR
HET NAG A 601 14
HET NAG A 602 14
HET FUL A 603 10
HET HUW A 701 22
HET CL A 802 1
HET CL A 803 1
HET CL A 804 1
HET CL A 805 1
HET CL A 806 1
HET CL A 807 1
HET CL A 808 1
HET CL A 809 1
HET CL A 810 1
HET CL A 811 1
HET SO4 A 812 5
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM FUL BETA-L-FUCOSE
HETNAM HUW HUPRINE W
HETNAM CL CHLORIDE ION
HETNAM SO4 SULFATE ION
HETSYN FUL 6-DEOXY-BETA-L-GALACTOSE
FORMUL 3 NAG 2(C8 H15 N O6)
FORMUL 4 FUL C6 H12 O5
FORMUL 5 HUW C18 H19 CL N2 O
FORMUL 6 CL 10(CL 1-)
FORMUL 7 SO4 O4 S 2-
FORMUL 8 HOH *119(H2 O)
HELIX 1 1 MET A 42 ARG A 46 5 5
HELIX 2 2 LEU A 130 ASP A 134 5 5
HELIX 3 3 GLY A 135 ARG A 143 1 9
HELIX 4 4 GLY A 154 LEU A 159 1 6
HELIX 5 5 ASN A 170 VAL A 187 1 18
HELIX 6 6 ALA A 188 PHE A 190 5 3
HELIX 7 7 SER A 203 LEU A 213 1 11
HELIX 8 8 SER A 215 GLY A 220 1 6
HELIX 9 9 GLY A 240 VAL A 255 1 16
HELIX 10 10 ASP A 266 ARG A 276 1 11
HELIX 11 11 PRO A 277 HIS A 284 1 8
HELIX 12 12 GLU A 285 LEU A 289 5 5
HELIX 13 13 THR A 311 GLY A 319 1 9
HELIX 14 14 GLY A 335 GLY A 342 5 8
HELIX 15 15 SER A 355 VAL A 367 1 13
HELIX 16 16 SER A 371 THR A 383 1 13
HELIX 17 17 ASP A 390 VAL A 407 1 18
HELIX 18 18 VAL A 407 ALA A 420 1 14
HELIX 19 19 PRO A 440 GLY A 444 5 5
HELIX 20 20 GLU A 450 PHE A 455 1 6
HELIX 21 21 GLY A 456 ASP A 460 5 5
HELIX 22 22 THR A 466 GLY A 487 1 22
HELIX 23 23 ARG A 525 ARG A 534 1 10
HELIX 24 24 ARG A 534 GLU A 548 1 15
HELIX 25 25 GLU A 550 TRP A 567 1 18
SHEET 1 AA 3 LEU A 9 VAL A 12 0
SHEET 2 AA 3 GLY A 15 ARG A 18 -1 O GLY A 15 N VAL A 12
SHEET 3 AA 3 VAL A 59 ASP A 61 1 O VAL A 60 N ARG A 18
SHEET 1 AB11 ILE A 20 LYS A 23 0
SHEET 2 AB11 PRO A 28 PRO A 36 -1 O VAL A 29 N LEU A 22
SHEET 3 AB11 TYR A 98 PRO A 104 -1 O LEU A 99 N ILE A 35
SHEET 4 AB11 VAL A 145 MET A 149 -1 O LEU A 146 N TRP A 102
SHEET 5 AB11 THR A 112 ILE A 118 1 O PRO A 113 N VAL A 145
SHEET 6 AB11 GLY A 192 GLU A 202 1 N ASP A 193 O THR A 112
SHEET 7 AB11 ARG A 224 GLN A 228 1 O ARG A 224 N LEU A 199
SHEET 8 AB11 GLN A 325 VAL A 331 1 O GLN A 325 N ALA A 225
SHEET 9 AB11 ARG A 424 PHE A 430 1 O ARG A 424 N VAL A 326
SHEET 10 AB11 GLN A 509 LEU A 513 1 O VAL A 511 N VAL A 429
SHEET 11 AB11 GLU A 519 ARG A 522 -1 O GLU A 519 N SER A 512
SHEET 1 AC 2 VAL A 68 CYS A 69 0
SHEET 2 AC 2 LEU A 92 SER A 93 1 N SER A 93 O VAL A 68
SHEET 1 BA 2 MET B 2 SER B 5 0
SHEET 2 BA 2 ILE B 13 ASN B 16 -1 O ILE B 13 N SER B 5
SHEET 1 BB 3 VAL B 34 CYS B 39 0
SHEET 2 BB 3 CYS B 22 ARG B 27 -1 O TYR B 23 N GLY B 38
SHEET 3 BB 3 LEU B 48 CYS B 53 -1 O GLU B 49 N SER B 26
SSBOND 1 CYS A 69 CYS A 96 1555 1555 2.04
SSBOND 2 CYS A 257 CYS A 272 1555 1555 2.04
SSBOND 3 CYS A 409 CYS A 529 1555 1555 2.06
SSBOND 4 CYS B 3 CYS B 22 1555 1555 2.03
SSBOND 5 CYS B 17 CYS B 39 1555 1555 2.04
SSBOND 6 CYS B 41 CYS B 52 1555 1555 2.04
SSBOND 7 CYS B 53 CYS B 59 1555 1555 2.04
LINK ND2 ASN A 350 C1 NAG A 601 1555 1555 1.46
LINK O6 NAG A 601 C1 FUL A 603 1555 1555 1.45
LINK O4 NAG A 601 C1 NAG A 602 1555 1555 1.47
CISPEP 1 TYR A 105 PRO A 106 0 0.68
CISPEP 2 GLY A 264 ASN A 265 0 10.11
CISPEP 3 ASN A 265 ASP A 266 0 0.06
CISPEP 4 PRO B 30 PRO B 31 0 -3.81
SITE 1 AC1 7 TRP A 86 GLY A 121 GLY A 122 SER A 203
SITE 2 AC1 7 TYR A 337 TRP A 439 HIS A 447
SITE 1 AC2 1 ARG A 417
SITE 1 AC3 1 ARG A 356
SITE 1 AC4 1 ARG A 224
SITE 1 AC5 3 PRO A 108 ARG A 143 HOH A2033
SITE 1 AC6 1 ARG A 136
SITE 1 AC7 2 ARG A 219 ASP A 320
SITE 1 AC8 2 GLY A 58 ARG A 165
SITE 1 AC9 2 ARG A 525 GLN A 527
SITE 1 BC1 1 GLU A 376
SITE 1 BC2 3 THR A 504 GLY A 506 ALA A 507
SITE 1 BC3 4 GLY A 345 SER A 347 ASP A 349 ASN A 350
CRYST1 151.600 151.600 246.400 90.00 90.00 120.00 H 3 2 18
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 0.006596 0.003808 0.000000 0.00000
SCALE2 0.000000 0.007617 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004058 0.00000
TER 4400 TRP A 567
TER 4865 TYR B 61
MASTER 521 0 15 25 21 0 13 6 5057 2 80 50
END
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