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HEADER HYDROLASE 30-SEP-12 4BC1
TITLE STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED BY CBDP (
TITLE 2 30-MIN SOAK): CRESYL-SALIGENIN-PHOSPHOSERINE ADDUCT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYLCHOLINESTERASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN, RESIDUES 32-574;
COMPND 5 SYNONYM: ACHE;
COMPND 6 EC: 3.1.1.7;
COMPND 7 ENGINEERED: YES;
COMPND 8 OTHER_DETAILS: CRESYL-SALIGENIN-PHOSPHATE ADDUCT ON S203
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 10029;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: CHO-K1;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGS
KEYWDS HYDROLASE, BUTYRYLCHOLINESTERASE, NERVE TRANSMISSION, INHIBITOR,
KEYWDS 2 ALPHA-BETA HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR E.CARLETTI,J.-P.COLLETIER,L.M.SCHOPFER,G.SANTONI,P.MASSON,
AUTHOR 2 O.LOCKRIDGE,F.NACHON,M.WEIK
REVDAT 1 06-FEB-13 4BC1 0
JRNL AUTH E.CARLETTI,J.-P.COLLETIER,L.M.SCHOPFER,G.SANTONI,P.MASSON,
JRNL AUTH 2 O.LOCKRIDGE,F.NACHON,M.WEIK
JRNL TITL INHIBITION PATHWAYS OF THE POTENT ORGANOPHOSPHATE CBDP WITH
JRNL TITL 2 CHOLINESTERASES REVEALED BY X-RAY CRYSTALLOGRAPHIC
JRNL TITL 3 SNAPSHOTS AND MASS SPECTROMETRY
JRNL REF CHEM.RES.TOXICOL. 2013
JRNL REFN ESSN 1520-5010
JRNL PMID 23339663
JRNL DOI 10.1021/TX3004505
REMARK 2
REMARK 2 RESOLUTION. 2.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.1_1168)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.950
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.285
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.36
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.66
REMARK 3 NUMBER OF REFLECTIONS : 111450
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.1879
REMARK 3 R VALUE (WORKING SET) : 0.1863
REMARK 3 FREE R VALUE : 0.2378
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.0
REMARK 3 FREE R VALUE TEST SET COUNT : 3344
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 48.2913 - 8.4944 0.99 4765 148 0.1872 0.2008
REMARK 3 2 8.4944 - 6.7482 0.99 4599 142 0.1563 0.1991
REMARK 3 3 6.7482 - 5.8969 1.00 4581 142 0.1587 0.1911
REMARK 3 4 5.8969 - 5.3585 1.00 4547 141 0.1431 0.1888
REMARK 3 5 5.3585 - 4.9748 1.00 4548 140 0.1432 0.1946
REMARK 3 6 4.9748 - 4.6818 1.00 4520 140 0.1310 0.2069
REMARK 3 7 4.6818 - 4.4475 1.00 4544 141 0.1324 0.1851
REMARK 3 8 4.4475 - 4.2540 1.00 4504 139 0.1388 0.1875
REMARK 3 9 4.2540 - 4.0903 1.00 4515 140 0.1521 0.1975
REMARK 3 10 4.0903 - 3.9492 1.00 4495 139 0.1585 0.2264
REMARK 3 11 3.9492 - 3.8258 1.00 4523 140 0.1688 0.2252
REMARK 3 12 3.8258 - 3.7165 1.00 4489 138 0.1826 0.2466
REMARK 3 13 3.7165 - 3.6187 1.00 4481 139 0.1943 0.2733
REMARK 3 14 3.6187 - 3.5304 1.00 4486 139 0.2014 0.2493
REMARK 3 15 3.5304 - 3.4502 1.00 4464 138 0.2199 0.2797
REMARK 3 16 3.4502 - 3.3768 1.00 4481 138 0.2331 0.2892
REMARK 3 17 3.3768 - 3.3092 1.00 4441 138 0.2493 0.3000
REMARK 3 18 3.3092 - 3.2468 0.99 4477 138 0.2620 0.3264
REMARK 3 19 3.2468 - 3.1888 0.99 4456 138 0.2737 0.3262
REMARK 3 20 3.1888 - 3.1348 0.99 4456 138 0.2896 0.3721
REMARK 3 21 3.1348 - 3.0842 0.99 4402 136 0.2942 0.3627
REMARK 3 22 3.0842 - 3.0368 0.99 4470 138 0.3061 0.3756
REMARK 3 23 3.0368 - 2.9921 0.99 4434 137 0.3245 0.3940
REMARK 3 24 2.9921 - 2.9500 0.99 4428 137 0.3279 0.3706
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) : 0.44
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.00
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 63.89
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 46.8
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.009 17683
REMARK 3 ANGLE : 1.368 24190
REMARK 3 CHIRALITY : 0.085 2580
REMARK 3 PLANARITY : 0.007 3171
REMARK 3 DIHEDRAL : 16.498 6363
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A
REMARK 3 ORIGIN FOR THE GROUP (A): 5.7557 -28.8780 86.0218
REMARK 3 T TENSOR
REMARK 3 T11: 0.1548 T22: 0.1658
REMARK 3 T33: 0.1423 T12: -0.0364
REMARK 3 T13: 0.0298 T23: -0.0191
REMARK 3 L TENSOR
REMARK 3 L11: 0.9162 L22: 2.1128
REMARK 3 L33: 1.0856 L12: 0.4194
REMARK 3 L13: -0.1650 L23: -0.2406
REMARK 3 S TENSOR
REMARK 3 S11: -0.0442 S12: 0.1030 S13: -0.0033
REMARK 3 S21: 0.1079 S22: 0.0576 S23: 0.0157
REMARK 3 S31: -0.1221 S32: -0.0816 S33: 0.0173
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN B
REMARK 3 ORIGIN FOR THE GROUP (A): -8.5226 26.9534 66.2992
REMARK 3 T TENSOR
REMARK 3 T11: 0.6864 T22: 0.4258
REMARK 3 T33: 0.3489 T12: 0.4923
REMARK 3 T13: 0.2124 T23: 0.0773
REMARK 3 L TENSOR
REMARK 3 L11: 1.0905 L22: 1.2305
REMARK 3 L33: 1.1011 L12: -0.3294
REMARK 3 L13: 0.3188 L23: -0.4504
REMARK 3 S TENSOR
REMARK 3 S11: -0.1406 S12: -0.3003 S13: -0.0840
REMARK 3 S21: 0.5465 S22: 0.3940 S23: 0.3852
REMARK 3 S31: -0.6049 S32: -0.9164 S33: 0.1820
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN C
REMARK 3 ORIGIN FOR THE GROUP (A): 24.1429 12.1179 24.9778
REMARK 3 T TENSOR
REMARK 3 T11: 0.1424 T22: 0.1255
REMARK 3 T33: 0.1532 T12: 0.0244
REMARK 3 T13: 0.0850 T23: 0.0586
REMARK 3 L TENSOR
REMARK 3 L11: 0.8768 L22: 1.2883
REMARK 3 L33: 1.7093 L12: -0.0173
REMARK 3 L13: 0.2284 L23: -0.0887
REMARK 3 S TENSOR
REMARK 3 S11: -0.0958 S12: -0.0109 S13: -0.0589
REMARK 3 S21: 0.0867 S22: -0.0237 S23: -0.1211
REMARK 3 S31: -0.0723 S32: 0.2718 S33: -0.0973
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN D
REMARK 3 ORIGIN FOR THE GROUP (A): 47.6618 5.4985 80.7386
REMARK 3 T TENSOR
REMARK 3 T11: 0.1774 T22: 0.3081
REMARK 3 T33: 0.2779 T12: -0.0543
REMARK 3 T13: -0.0639 T23: 0.1119
REMARK 3 L TENSOR
REMARK 3 L11: 1.1412 L22: 1.1683
REMARK 3 L33: 2.1933 L12: -0.1253
REMARK 3 L13: 0.3234 L23: -0.2748
REMARK 3 S TENSOR
REMARK 3 S11: -0.0340 S12: 0.2116 S13: 0.1893
REMARK 3 S21: -0.0537 S22: -0.1228 S23: -0.2087
REMARK 3 S31: -0.0786 S32: 0.3692 S33: -0.1344
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 4BC1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-OCT-12.
REMARK 100 THE PDBE ID CODE IS EBI-54259.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-APR-10
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) : 0.9765
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD (QUANTUM 315R)
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 : 111473
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.95
REMARK 200 RESOLUTION RANGE LOW (A) : 48.30
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 4.5
REMARK 200 R MERGE (I) : 0.08
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 17.00
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.95
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.4
REMARK 200 DATA REDUNDANCY IN SHELL : 4.5
REMARK 200 R MERGE FOR SHELL (I) : 0.53
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.10
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 4A16
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 78
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 5.5
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS HCL BUFFER PH 7.4,
REMARK 280 1.6 M AMMONIUM SULFATE
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
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 67.77000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 112.47000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 86.62500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 112.47000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 67.77000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 86.62500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
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 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 B 1
REMARK 465 GLY B 2
REMARK 465 ARG B 3
REMARK 465 GLU B 4
REMARK 465 GLU C 1
REMARK 465 GLY C 2
REMARK 465 ARG C 3
REMARK 465 GLU D 1
REMARK 465 GLY D 2
REMARK 465 ARG D 3
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 TYR A 72 O HOH A 2052 2.02
REMARK 500 NE2 GLN A 508 O HOH A 2228 2.18
REMARK 500 O VAL B 379 OG1 THR B 383 2.15
REMARK 500 OE1 GLU B 450 O HOH B 2061 2.18
REMARK 500 NH1 ARG C 274 O HOH C 2041 2.17
REMARK 500 ND1A HIS C 387 O HOH C 2216 2.16
REMARK 500 ND1A HIS C 387 O HOH C 2215 2.19
REMARK 500 OE2 GLU D 39 O HOH D 2019 2.07
REMARK 500 O THR D 155 O HOH D 2080 2.09
REMARK 500 O GLY D 157 O HOH D 2081 2.20
REMARK 500 OG SER D 203 O2P TQV D 600 2.13
REMARK 500 CB CYS D 257 SG CYS D 272 1.67
REMARK 500 OG SER D 497 O HOH D 2169 2.07
REMARK 500 CL CL A 1544 O HOH A 2034 2.19
REMARK 500 O HOH A 2030 O HOH A 2031 2.14
REMARK 500 O HOH C 2010 O HOH C 2012 2.12
REMARK 500 O HOH C 2197 O HOH C 2199 2.19
REMARK 500 O HOH C 2199 O HOH C 2218 2.14
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 SER A 203 CB SER A 203 OG 0.079
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 PRO A 258 C - N - CA ANGL. DEV. = -14.8 DEGREES
REMARK 500 PRO C 258 C - N - CA ANGL. DEV. = -11.5 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 ALA A 62 56.18 -116.31
REMARK 500 SER A 93 143.88 -174.97
REMARK 500 CYS A 96 -1.70 -147.88
REMARK 500 ARG A 107 132.12 -36.59
REMARK 500 PRO A 111 119.41 -39.45
REMARK 500 PHE A 123 19.48 59.93
REMARK 500 SER A 203 -130.90 54.17
REMARK 500 HIS A 223 -30.85 -131.12
REMARK 500 VAL A 255 30.90 -96.51
REMARK 500 CYS A 257 46.75 -97.79
REMARK 500 ALA A 262 -143.53 -80.66
REMARK 500 ASP A 283 -18.35 -41.46
REMARK 500 ASP A 306 -76.71 -128.81
REMARK 500 VAL A 367 70.65 -104.47
REMARK 500 TYR A 449 33.32 -96.58
REMARK 500 THR A 486 23.69 -147.44
REMARK 500 SER A 495 -9.61 -146.44
REMARK 500 SER A 497 -46.90 -138.07
REMARK 500 ALA A 506 -71.58 -52.58
REMARK 500 PHE B 47 -2.05 71.43
REMARK 500 ALA B 62 51.07 -116.89
REMARK 500 CYS B 96 5.36 -157.31
REMARK 500 ALA B 109 -76.09 -56.78
REMARK 500 TYR B 133 41.23 -100.27
REMARK 500 GLN B 140 -73.84 -59.28
REMARK 500 GLU B 142 -1.93 72.97
REMARK 500 PHE B 158 17.89 -141.74
REMARK 500 ALA B 167 79.97 -151.25
REMARK 500 PRO B 194 -9.56 -58.10
REMARK 500 SER B 203 -119.80 51.64
REMARK 500 HIS B 223 -32.50 -134.29
REMARK 500 ASN B 233 -156.56 -90.04
REMARK 500 ALA B 262 -43.44 -158.61
REMARK 500 ASP B 306 -88.36 -104.68
REMARK 500 ASP B 349 -71.05 -80.43
REMARK 500 ASN B 350 -169.71 -76.85
REMARK 500 ASP B 390 105.85 -50.34
REMARK 500 VAL B 407 -51.91 -130.99
REMARK 500 SER B 495 -101.92 -66.88
REMARK 500 ASN B 514 -155.40 -156.88
REMARK 500 ARG B 525 74.67 34.08
REMARK 500 THR B 528 -62.99 70.47
REMARK 500 LYS B 538 -8.19 -55.40
REMARK 500 ALA B 542 -77.82 47.30
REMARK 500 VAL C 12 -160.00 -116.45
REMARK 500 PHE C 47 -17.42 85.82
REMARK 500 GLU C 91 127.71 -38.66
REMARK 500 CYS C 96 -9.92 -158.31
REMARK 500 SER C 110 134.19 80.92
REMARK 500 ALA C 127 133.62 171.90
REMARK 500
REMARK 500 THIS ENTRY HAS 87 RAMACHANDRAN OUTLIERS.
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 CYS D 257 PRO D 258 124.84
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH D2185 DISTANCE = 5.51 ANGSTROMS
REMARK 525 HOH D2186 DISTANCE = 5.52 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TQV A 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A1544
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1545
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1546
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1547
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1548
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1549
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1550
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A1990
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A1991
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TQV B 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B1544
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1545
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1546
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1547
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TQV C 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C1544
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C1545
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C1546
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C1547
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C1548
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C1549
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C1990
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TQV D 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D1545
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D1546
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D1547
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D1990
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D1991
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE
REMARK 800 NAG A 701 BOUND TO ASN A 265
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE
REMARK 800 NAG B 701 BOUND TO ASN B 265
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE
REMARK 800 NAG B 702 BOUND TO ASN B 350
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE
REMARK 800 NAG C 701 BOUND TO ASN C 265
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE
REMARK 800 NAG D 701 BOUND TO ASN D 265
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE
REMARK 800 NAG D 702 BOUND TO ASN D 350
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE
REMARK 800 NAG D 703 BOUND TO ASN D 464
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1C2B RELATED DB: PDB
REMARK 900 ELECTROPHORUS ELECTRICUS ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 1C2O RELATED DB: PDB
REMARK 900 ELECTROPHORUS ELECTRICUS ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 1J06 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE IN THE
REMARK 900 APOFORM
REMARK 900 RELATED ID: 1J07 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE MOUSE ACETYLCHOLINESTERASE-
REMARK 900 DECIDIUM COMPLEX
REMARK 900 RELATED ID: 1KU6 RELATED DB: PDB
REMARK 900 FASCICULIN 2-MOUSE ACETYLCHOLINESTERASE COMPLEX
REMARK 900 RELATED ID: 1MAA RELATED DB: PDB
REMARK 900 MOUSE ACETYLCHOLINESTERASE CATALYTIC DOMAIN,
REMARK 900 GLYCOSYLATEDPROTEIN
REMARK 900 RELATED ID: 1MAH RELATED DB: PDB
REMARK 900 FASCICULIN2 - MOUSE ACETYLCHOLINESTERASE COMPLEX
REMARK 900 RELATED ID: 1N5M RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE MOUSE ACETYLCHOLINESTERASE-
REMARK 900 GALLAMINE COMPLEX
REMARK 900 RELATED ID: 1N5R RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE MOUSE ACETYLCHOLINESTERASE-
REMARK 900 PROPIDIUM COMPLEX
REMARK 900 RELATED ID: 1Q83 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE MOUSE ACETYLCHOLINESTERASE-
REMARK 900 TZ2PA6SYN COMPLEX
REMARK 900 RELATED ID: 1Q84 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE MOUSE ACETYLCHOLINESTERASE-
REMARK 900 TZ2PA6ANTI COMPLEX
REMARK 900 RELATED ID: 2C0P RELATED DB: PDB
REMARK 900 AGED FORM OF MOUSE ACETYLCHOLINESTERASE INHIBITED BY
REMARK 900 TABUN
REMARK 900 RELATED ID: 2C0Q RELATED DB: PDB
REMARK 900 NON-AGED FORM OF MOUSE ACETYLCHOLINESTERASE INHIBITED BY
REMARK 900 TABUN
REMARK 900 RELATED ID: 2H9Y RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE
REMARK 900 COMPLEXEDWITH M-(N,N,N-TRIMETHYLAMMONIO)
REMARK 900 TRIFLUOROACETOPHENONE
REMARK 900 RELATED ID: 2HA0 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE
REMARK 900 COMPLEXEDWITH 4-KETOAMYLTRIMETHYLAMMONIUM
REMARK 900 RELATED ID: 2HA2 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE
REMARK 900 COMPLEXEDWITH SUCCINYLCHOLINE
REMARK 900 RELATED ID: 2HA3 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE
REMARK 900 COMPLEXEDWITH CHOLINE
REMARK 900 RELATED ID: 2HA4 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MUTANT S203A OF
REMARK 900 MOUSEACETYLCHOLINESTERASE COMPLEXED WITH ACETYLCHOLINE
REMARK 900 RELATED ID: 2HA5 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MUTANT S203A OF
REMARK 900 ACETYLCHOLINESTERASECOMPLEXED WITH ACETYLTHIOCHOLINE
REMARK 900 RELATED ID: 2HA6 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MUTANT S203A OF
REMARK 900 MOUSEACETYLCHOLINESTERASE COMPLEXED WITH SUCCINYLCHOLINE
REMARK 900 RELATED ID: 2HA7 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MUTANT S203A OF
REMARK 900 MOUSEACETYLCHOLINESTERASE COMPLEXED WITH BUTYRYLTHIOCHOLINE
REMARK 900 RELATED ID: 2JEY RELATED DB: PDB
REMARK 900 MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH HLO-7
REMARK 900 RELATED ID: 2JEZ RELATED DB: PDB
REMARK 900 MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH TABUN
REMARK 900 AND HLO-7
REMARK 900 RELATED ID: 2JF0 RELATED DB: PDB
REMARK 900 MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH TABUN
REMARK 900 AND ORTHO-7
REMARK 900 RELATED ID: 2JGE RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED
REMARK 900 BY NON-AGED METHAMIDOPHOS
REMARK 900 RELATED ID: 2JGF RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED
REMARK 900 BY NON-AGED FENAMIPHOS
REMARK 900 RELATED ID: 2JGG RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED
REMARK 900 BY NON-AGED SARIN
REMARK 900 RELATED ID: 2JGH RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED
REMARK 900 BY NON-AGED VX
REMARK 900 RELATED ID: 2JGI RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED
REMARK 900 BY NON-AGED DIISOPROPYL FLUOROPHOSPHATE (DFP)
REMARK 900 RELATED ID: 2JGJ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED
REMARK 900 BY AGED METHAMIDOPHOS
REMARK 900 RELATED ID: 2JGK RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED
REMARK 900 BY AGED FENAMIPHOS
REMARK 900 RELATED ID: 2JGL RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED
REMARK 900 BY AGED VX AND SARIN
REMARK 900 RELATED ID: 2JGM RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED
REMARK 900 BY AGED DIISOPROPYL FLUOROPHOSPHATE (DFP)
REMARK 900 RELATED ID: 2WHP RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ACETYLCHOLINESTERASE, PHOSPHONYLATED BY
REMARK 900 SARIN AND IN COMPLEX WITH HI-6
REMARK 900 RELATED ID: 2WHQ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ACETYLCHOLINESTERASE, PHOSPHONYLATED BY
REMARK 900 SARIN (AGED) IN COMPLEX WITH HI-6
REMARK 900 RELATED ID: 2WHR RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ACETYLCHOLINESTERASE IN COMPLEX WITH
REMARK 900 K027
REMARK 900 RELATED ID: 2WLS RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MUS MUSCULUS ACETYLCHOLINESTERASE IN
REMARK 900 COMPLEX WITH AMTS13
REMARK 900 RELATED ID: 2WU3 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE IN COMPLEX
REMARK 900 WITH FENAMIPHOS AND HI-6
REMARK 900 RELATED ID: 2WU4 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE IN COMPLEX
REMARK 900 WITH FENAMIPHOS AND ORTHO-7
REMARK 900 RELATED ID: 2XUD RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE Y337A MUTANT OF MOUSE
REMARK 900 ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 2XUF RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MACHE-Y337A-TZ2PA6 ANTI COMPLEX (
REMARK 900 1 MTH)
REMARK 900 RELATED ID: 2XUG RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MACHE-Y337A-TZ2PA6 ANTI COMPLEX (
REMARK 900 1 WK)
REMARK 900 RELATED ID: 2XUH RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MACHE-Y337A-TZ2PA6 ANTI COMPLEX (
REMARK 900 10 MTH)
REMARK 900 RELATED ID: 2XUI RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MACHE-Y337A-TZ2PA6 SYN COMPLEX (1
REMARK 900 WK)
REMARK 900 RELATED ID: 2XUJ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MACHE-Y337A-TZ2PA6 SYN COMPLEX (1
REMARK 900 MTH)
REMARK 900 RELATED ID: 2XUK RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MACHE-Y337A-TZ2PA6 SYN COMPLEX (
REMARK 900 10 MTH)
REMARK 900 RELATED ID: 2XUO RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MACHE-Y337A MUTANT IN COMPLEX
REMARK 900 WITH SOAKED TZ2PA6 ANTI INHIBITOR
REMARK 900 RELATED ID: 2XUP RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE MACHE-Y337A MUTANT IN COMPLEX
REMARK 900 WITH SOAKED TZ2PA6 SYN INHIBITOR
REMARK 900 RELATED ID: 2XUQ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE MACHE-Y337A MUTANT IN COMPLEX
REMARK 900 WITH SOAKED TZ2PA6 ANTI-SYN INHIBITORS
REMARK 900 RELATED ID: 4A16 RELATED DB: PDB
REMARK 900 STRUCTURE OF MOUSE ACETYLCHOLINESTERASE COMPLEX WITH
REMARK 900 HUPRINE DERIVATIVE
REMARK 900 RELATED ID: 4A23 RELATED DB: PDB
REMARK 900 MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH RACEMIC
REMARK 900 C5685
REMARK 900 RELATED ID: 4ARA RELATED DB: PDB
REMARK 900 MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH (R)-
REMARK 900 C5685 AT 2.5 A RESOLUTION.
REMARK 900 RELATED ID: 4ARB RELATED DB: PDB
REMARK 900 MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH (S)-
REMARK 900 C5685 AT 2.25 A RESOLUTION.
REMARK 900 RELATED ID: 4B7Z RELATED DB: PDB
REMARK 900 MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH N-(2-
REMARK 900 DIETHYLAMINO-ETHYL)-1-(4-METHYLPHENYL)-METHANESULFONAMIDE
REMARK 900 RELATED ID: 4B80 RELATED DB: PDB
REMARK 900 MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH N-(2-
REMARK 900 DIETHYLAMINO-ETHYL)-1-(4-FLUORO-PHENYL)-METHANESULFONAMIDE
REMARK 900 RELATED ID: 4B81 RELATED DB: PDB
REMARK 900 MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH 1-(4-
REMARK 900 CHLORO-PHENYL)-N-(2-DIETHYLAMINO-ETHYL)-METHANESULFONAMIDE
REMARK 900 RELATED ID: 4B82 RELATED DB: PDB
REMARK 900 MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH N-(2-
REMARK 900 DIETHYLAMINO-ETHYL)-2-FLUORANYL-BENZENESULFONAMIDE
REMARK 900 RELATED ID: 4B83 RELATED DB: PDB
REMARK 900 MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH N-(2-
REMARK 900 DIETHYLAMINO-ETHYL)-3-METHOXY-BENZENESULFONAMIDE
REMARK 900 RELATED ID: 4B84 RELATED DB: PDB
REMARK 900 MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH N-(2-
REMARK 900 DIETHYLAMINO-ETHYL)-3-TRIFLUOROMETHYL-BENZENESULFONAMIDE
REMARK 900 RELATED ID: 4B85 RELATED DB: PDB
REMARK 900 MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH 4-
REMARK 900 CHLORANYL-N-(2-DIETHYLAMINO-ETHYL)-BENZENESULFONAMIDE
REMARK 900 RELATED ID: 4BBZ RELATED DB: PDB
REMARK 900 STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY CBDP
REMARK 900 (2-MIN SOAK): CRESYL-PHOSPHOSERINE ADDUCT
REMARK 900 RELATED ID: 4BC0 RELATED DB: PDB
REMARK 900 STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED BY CBDP
REMARK 900 (12-H SOAK): CRESYL-PHOSPHOSERINE ADDUCT
DBREF 4BC1 A 1 543 UNP P21836 ACES_MOUSE 32 574
DBREF 4BC1 B 1 543 UNP P21836 ACES_MOUSE 32 574
DBREF 4BC1 C 1 543 UNP P21836 ACES_MOUSE 32 574
DBREF 4BC1 D 1 543 UNP P21836 ACES_MOUSE 32 574
SEQRES 1 A 543 GLU GLY ARG GLU ASP PRO GLN LEU LEU VAL ARG VAL ARG
SEQRES 2 A 543 GLY GLY GLN LEU ARG GLY ILE ARG LEU LYS ALA PRO GLY
SEQRES 3 A 543 GLY PRO VAL SER ALA PHE LEU GLY ILE PRO PHE ALA GLU
SEQRES 4 A 543 PRO PRO VAL GLY SER ARG ARG PHE MET PRO PRO GLU PRO
SEQRES 5 A 543 LYS ARG PRO TRP SER GLY VAL LEU ASP ALA THR THR PHE
SEQRES 6 A 543 GLN ASN VAL CYS TYR GLN TYR VAL ASP THR LEU TYR PRO
SEQRES 7 A 543 GLY PHE GLU GLY THR GLU MET TRP ASN PRO ASN ARG GLU
SEQRES 8 A 543 LEU SER GLU ASP CYS LEU TYR LEU ASN VAL TRP THR PRO
SEQRES 9 A 543 TYR PRO ARG PRO ALA SER PRO THR PRO VAL LEU ILE TRP
SEQRES 10 A 543 ILE TYR GLY GLY GLY PHE TYR SER GLY ALA ALA SER LEU
SEQRES 11 A 543 ASP VAL TYR ASP GLY ARG PHE LEU ALA GLN VAL GLU GLY
SEQRES 12 A 543 ALA VAL LEU VAL SER MET ASN TYR ARG VAL GLY THR PHE
SEQRES 13 A 543 GLY PHE LEU ALA LEU PRO GLY SER ARG GLU ALA PRO GLY
SEQRES 14 A 543 ASN VAL GLY LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP
SEQRES 15 A 543 VAL GLN GLU ASN ILE ALA ALA PHE GLY GLY ASP PRO MET
SEQRES 16 A 543 SER VAL THR LEU PHE GLY GLU SER ALA GLY ALA ALA SER
SEQRES 17 A 543 VAL GLY MET HIS ILE LEU SER LEU PRO SER ARG SER LEU
SEQRES 18 A 543 PHE HIS ARG ALA VAL LEU GLN SER GLY THR PRO ASN GLY
SEQRES 19 A 543 PRO TRP ALA THR VAL SER ALA GLY GLU ALA ARG ARG ARG
SEQRES 20 A 543 ALA THR LEU LEU ALA ARG LEU VAL GLY CYS PRO PRO GLY
SEQRES 21 A 543 GLY ALA GLY GLY ASN ASP THR GLU LEU ILE ALA CYS LEU
SEQRES 22 A 543 ARG THR ARG PRO ALA GLN ASP LEU VAL ASP HIS GLU TRP
SEQRES 23 A 543 HIS VAL LEU PRO GLN GLU SER ILE PHE ARG PHE SER PHE
SEQRES 24 A 543 VAL PRO VAL VAL ASP GLY ASP PHE LEU SER ASP THR PRO
SEQRES 25 A 543 GLU ALA LEU ILE ASN THR GLY ASP PHE GLN ASP LEU GLN
SEQRES 26 A 543 VAL LEU VAL GLY VAL VAL LYS ASP GLU GLY SER TYR PHE
SEQRES 27 A 543 LEU VAL TYR GLY VAL PRO GLY PHE SER LYS ASP ASN GLU
SEQRES 28 A 543 SER LEU ILE SER ARG ALA GLN PHE LEU ALA GLY VAL ARG
SEQRES 29 A 543 ILE GLY VAL PRO GLN ALA SER ASP LEU ALA ALA GLU ALA
SEQRES 30 A 543 VAL VAL LEU HIS TYR THR ASP TRP LEU HIS PRO GLU ASP
SEQRES 31 A 543 PRO THR HIS LEU ARG ASP ALA MET SER ALA VAL VAL GLY
SEQRES 32 A 543 ASP HIS ASN VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY
SEQRES 33 A 543 ARG LEU ALA ALA GLN GLY ALA ARG VAL TYR ALA TYR ILE
SEQRES 34 A 543 PHE GLU HIS ARG ALA SER THR LEU THR TRP PRO LEU TRP
SEQRES 35 A 543 MET GLY VAL PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE
SEQRES 36 A 543 GLY LEU PRO LEU ASP PRO SER LEU ASN TYR THR THR GLU
SEQRES 37 A 543 GLU ARG ILE PHE ALA GLN ARG LEU MET LYS TYR TRP THR
SEQRES 38 A 543 ASN PHE ALA ARG THR GLY ASP PRO ASN ASP PRO ARG ASP
SEQRES 39 A 543 SER LYS SER PRO GLN TRP PRO PRO TYR THR THR ALA ALA
SEQRES 40 A 543 GLN GLN TYR VAL SER LEU ASN LEU LYS PRO LEU GLU VAL
SEQRES 41 A 543 ARG ARG GLY LEU ARG ALA GLN THR CYS ALA PHE TRP ASN
SEQRES 42 A 543 ARG PHE LEU PRO LYS LEU LEU SER ALA THR
SEQRES 1 B 543 GLU GLY ARG GLU ASP PRO GLN LEU LEU VAL ARG VAL ARG
SEQRES 2 B 543 GLY GLY GLN LEU ARG GLY ILE ARG LEU LYS ALA PRO GLY
SEQRES 3 B 543 GLY PRO VAL SER ALA PHE LEU GLY ILE PRO PHE ALA GLU
SEQRES 4 B 543 PRO PRO VAL GLY SER ARG ARG PHE MET PRO PRO GLU PRO
SEQRES 5 B 543 LYS ARG PRO TRP SER GLY VAL LEU ASP ALA THR THR PHE
SEQRES 6 B 543 GLN ASN VAL CYS TYR GLN TYR VAL ASP THR LEU TYR PRO
SEQRES 7 B 543 GLY PHE GLU GLY THR GLU MET TRP ASN PRO ASN ARG GLU
SEQRES 8 B 543 LEU SER GLU ASP CYS LEU TYR LEU ASN VAL TRP THR PRO
SEQRES 9 B 543 TYR PRO ARG PRO ALA SER PRO THR PRO VAL LEU ILE TRP
SEQRES 10 B 543 ILE TYR GLY GLY GLY PHE TYR SER GLY ALA ALA SER LEU
SEQRES 11 B 543 ASP VAL TYR ASP GLY ARG PHE LEU ALA GLN VAL GLU GLY
SEQRES 12 B 543 ALA VAL LEU VAL SER MET ASN TYR ARG VAL GLY THR PHE
SEQRES 13 B 543 GLY PHE LEU ALA LEU PRO GLY SER ARG GLU ALA PRO GLY
SEQRES 14 B 543 ASN VAL GLY LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP
SEQRES 15 B 543 VAL GLN GLU ASN ILE ALA ALA PHE GLY GLY ASP PRO MET
SEQRES 16 B 543 SER VAL THR LEU PHE GLY GLU SER ALA GLY ALA ALA SER
SEQRES 17 B 543 VAL GLY MET HIS ILE LEU SER LEU PRO SER ARG SER LEU
SEQRES 18 B 543 PHE HIS ARG ALA VAL LEU GLN SER GLY THR PRO ASN GLY
SEQRES 19 B 543 PRO TRP ALA THR VAL SER ALA GLY GLU ALA ARG ARG ARG
SEQRES 20 B 543 ALA THR LEU LEU ALA ARG LEU VAL GLY CYS PRO PRO GLY
SEQRES 21 B 543 GLY ALA GLY GLY ASN ASP THR GLU LEU ILE ALA CYS LEU
SEQRES 22 B 543 ARG THR ARG PRO ALA GLN ASP LEU VAL ASP HIS GLU TRP
SEQRES 23 B 543 HIS VAL LEU PRO GLN GLU SER ILE PHE ARG PHE SER PHE
SEQRES 24 B 543 VAL PRO VAL VAL ASP GLY ASP PHE LEU SER ASP THR PRO
SEQRES 25 B 543 GLU ALA LEU ILE ASN THR GLY ASP PHE GLN ASP LEU GLN
SEQRES 26 B 543 VAL LEU VAL GLY VAL VAL LYS ASP GLU GLY SER TYR PHE
SEQRES 27 B 543 LEU VAL TYR GLY VAL PRO GLY PHE SER LYS ASP ASN GLU
SEQRES 28 B 543 SER LEU ILE SER ARG ALA GLN PHE LEU ALA GLY VAL ARG
SEQRES 29 B 543 ILE GLY VAL PRO GLN ALA SER ASP LEU ALA ALA GLU ALA
SEQRES 30 B 543 VAL VAL LEU HIS TYR THR ASP TRP LEU HIS PRO GLU ASP
SEQRES 31 B 543 PRO THR HIS LEU ARG ASP ALA MET SER ALA VAL VAL GLY
SEQRES 32 B 543 ASP HIS ASN VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY
SEQRES 33 B 543 ARG LEU ALA ALA GLN GLY ALA ARG VAL TYR ALA TYR ILE
SEQRES 34 B 543 PHE GLU HIS ARG ALA SER THR LEU THR TRP PRO LEU TRP
SEQRES 35 B 543 MET GLY VAL PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE
SEQRES 36 B 543 GLY LEU PRO LEU ASP PRO SER LEU ASN TYR THR THR GLU
SEQRES 37 B 543 GLU ARG ILE PHE ALA GLN ARG LEU MET LYS TYR TRP THR
SEQRES 38 B 543 ASN PHE ALA ARG THR GLY ASP PRO ASN ASP PRO ARG ASP
SEQRES 39 B 543 SER LYS SER PRO GLN TRP PRO PRO TYR THR THR ALA ALA
SEQRES 40 B 543 GLN GLN TYR VAL SER LEU ASN LEU LYS PRO LEU GLU VAL
SEQRES 41 B 543 ARG ARG GLY LEU ARG ALA GLN THR CYS ALA PHE TRP ASN
SEQRES 42 B 543 ARG PHE LEU PRO LYS LEU LEU SER ALA THR
SEQRES 1 C 543 GLU GLY ARG GLU ASP PRO GLN LEU LEU VAL ARG VAL ARG
SEQRES 2 C 543 GLY GLY GLN LEU ARG GLY ILE ARG LEU LYS ALA PRO GLY
SEQRES 3 C 543 GLY PRO VAL SER ALA PHE LEU GLY ILE PRO PHE ALA GLU
SEQRES 4 C 543 PRO PRO VAL GLY SER ARG ARG PHE MET PRO PRO GLU PRO
SEQRES 5 C 543 LYS ARG PRO TRP SER GLY VAL LEU ASP ALA THR THR PHE
SEQRES 6 C 543 GLN ASN VAL CYS TYR GLN TYR VAL ASP THR LEU TYR PRO
SEQRES 7 C 543 GLY PHE GLU GLY THR GLU MET TRP ASN PRO ASN ARG GLU
SEQRES 8 C 543 LEU SER GLU ASP CYS LEU TYR LEU ASN VAL TRP THR PRO
SEQRES 9 C 543 TYR PRO ARG PRO ALA SER PRO THR PRO VAL LEU ILE TRP
SEQRES 10 C 543 ILE TYR GLY GLY GLY PHE TYR SER GLY ALA ALA SER LEU
SEQRES 11 C 543 ASP VAL TYR ASP GLY ARG PHE LEU ALA GLN VAL GLU GLY
SEQRES 12 C 543 ALA VAL LEU VAL SER MET ASN TYR ARG VAL GLY THR PHE
SEQRES 13 C 543 GLY PHE LEU ALA LEU PRO GLY SER ARG GLU ALA PRO GLY
SEQRES 14 C 543 ASN VAL GLY LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP
SEQRES 15 C 543 VAL GLN GLU ASN ILE ALA ALA PHE GLY GLY ASP PRO MET
SEQRES 16 C 543 SER VAL THR LEU PHE GLY GLU SER ALA GLY ALA ALA SER
SEQRES 17 C 543 VAL GLY MET HIS ILE LEU SER LEU PRO SER ARG SER LEU
SEQRES 18 C 543 PHE HIS ARG ALA VAL LEU GLN SER GLY THR PRO ASN GLY
SEQRES 19 C 543 PRO TRP ALA THR VAL SER ALA GLY GLU ALA ARG ARG ARG
SEQRES 20 C 543 ALA THR LEU LEU ALA ARG LEU VAL GLY CYS PRO PRO GLY
SEQRES 21 C 543 GLY ALA GLY GLY ASN ASP THR GLU LEU ILE ALA CYS LEU
SEQRES 22 C 543 ARG THR ARG PRO ALA GLN ASP LEU VAL ASP HIS GLU TRP
SEQRES 23 C 543 HIS VAL LEU PRO GLN GLU SER ILE PHE ARG PHE SER PHE
SEQRES 24 C 543 VAL PRO VAL VAL ASP GLY ASP PHE LEU SER ASP THR PRO
SEQRES 25 C 543 GLU ALA LEU ILE ASN THR GLY ASP PHE GLN ASP LEU GLN
SEQRES 26 C 543 VAL LEU VAL GLY VAL VAL LYS ASP GLU GLY SER TYR PHE
SEQRES 27 C 543 LEU VAL TYR GLY VAL PRO GLY PHE SER LYS ASP ASN GLU
SEQRES 28 C 543 SER LEU ILE SER ARG ALA GLN PHE LEU ALA GLY VAL ARG
SEQRES 29 C 543 ILE GLY VAL PRO GLN ALA SER ASP LEU ALA ALA GLU ALA
SEQRES 30 C 543 VAL VAL LEU HIS TYR THR ASP TRP LEU HIS PRO GLU ASP
SEQRES 31 C 543 PRO THR HIS LEU ARG ASP ALA MET SER ALA VAL VAL GLY
SEQRES 32 C 543 ASP HIS ASN VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY
SEQRES 33 C 543 ARG LEU ALA ALA GLN GLY ALA ARG VAL TYR ALA TYR ILE
SEQRES 34 C 543 PHE GLU HIS ARG ALA SER THR LEU THR TRP PRO LEU TRP
SEQRES 35 C 543 MET GLY VAL PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE
SEQRES 36 C 543 GLY LEU PRO LEU ASP PRO SER LEU ASN TYR THR THR GLU
SEQRES 37 C 543 GLU ARG ILE PHE ALA GLN ARG LEU MET LYS TYR TRP THR
SEQRES 38 C 543 ASN PHE ALA ARG THR GLY ASP PRO ASN ASP PRO ARG ASP
SEQRES 39 C 543 SER LYS SER PRO GLN TRP PRO PRO TYR THR THR ALA ALA
SEQRES 40 C 543 GLN GLN TYR VAL SER LEU ASN LEU LYS PRO LEU GLU VAL
SEQRES 41 C 543 ARG ARG GLY LEU ARG ALA GLN THR CYS ALA PHE TRP ASN
SEQRES 42 C 543 ARG PHE LEU PRO LYS LEU LEU SER ALA THR
SEQRES 1 D 543 GLU GLY ARG GLU ASP PRO GLN LEU LEU VAL ARG VAL ARG
SEQRES 2 D 543 GLY GLY GLN LEU ARG GLY ILE ARG LEU LYS ALA PRO GLY
SEQRES 3 D 543 GLY PRO VAL SER ALA PHE LEU GLY ILE PRO PHE ALA GLU
SEQRES 4 D 543 PRO PRO VAL GLY SER ARG ARG PHE MET PRO PRO GLU PRO
SEQRES 5 D 543 LYS ARG PRO TRP SER GLY VAL LEU ASP ALA THR THR PHE
SEQRES 6 D 543 GLN ASN VAL CYS TYR GLN TYR VAL ASP THR LEU TYR PRO
SEQRES 7 D 543 GLY PHE GLU GLY THR GLU MET TRP ASN PRO ASN ARG GLU
SEQRES 8 D 543 LEU SER GLU ASP CYS LEU TYR LEU ASN VAL TRP THR PRO
SEQRES 9 D 543 TYR PRO ARG PRO ALA SER PRO THR PRO VAL LEU ILE TRP
SEQRES 10 D 543 ILE TYR GLY GLY GLY PHE TYR SER GLY ALA ALA SER LEU
SEQRES 11 D 543 ASP VAL TYR ASP GLY ARG PHE LEU ALA GLN VAL GLU GLY
SEQRES 12 D 543 ALA VAL LEU VAL SER MET ASN TYR ARG VAL GLY THR PHE
SEQRES 13 D 543 GLY PHE LEU ALA LEU PRO GLY SER ARG GLU ALA PRO GLY
SEQRES 14 D 543 ASN VAL GLY LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP
SEQRES 15 D 543 VAL GLN GLU ASN ILE ALA ALA PHE GLY GLY ASP PRO MET
SEQRES 16 D 543 SER VAL THR LEU PHE GLY GLU SER ALA GLY ALA ALA SER
SEQRES 17 D 543 VAL GLY MET HIS ILE LEU SER LEU PRO SER ARG SER LEU
SEQRES 18 D 543 PHE HIS ARG ALA VAL LEU GLN SER GLY THR PRO ASN GLY
SEQRES 19 D 543 PRO TRP ALA THR VAL SER ALA GLY GLU ALA ARG ARG ARG
SEQRES 20 D 543 ALA THR LEU LEU ALA ARG LEU VAL GLY CYS PRO PRO GLY
SEQRES 21 D 543 GLY ALA GLY GLY ASN ASP THR GLU LEU ILE ALA CYS LEU
SEQRES 22 D 543 ARG THR ARG PRO ALA GLN ASP LEU VAL ASP HIS GLU TRP
SEQRES 23 D 543 HIS VAL LEU PRO GLN GLU SER ILE PHE ARG PHE SER PHE
SEQRES 24 D 543 VAL PRO VAL VAL ASP GLY ASP PHE LEU SER ASP THR PRO
SEQRES 25 D 543 GLU ALA LEU ILE ASN THR GLY ASP PHE GLN ASP LEU GLN
SEQRES 26 D 543 VAL LEU VAL GLY VAL VAL LYS ASP GLU GLY SER TYR PHE
SEQRES 27 D 543 LEU VAL TYR GLY VAL PRO GLY PHE SER LYS ASP ASN GLU
SEQRES 28 D 543 SER LEU ILE SER ARG ALA GLN PHE LEU ALA GLY VAL ARG
SEQRES 29 D 543 ILE GLY VAL PRO GLN ALA SER ASP LEU ALA ALA GLU ALA
SEQRES 30 D 543 VAL VAL LEU HIS TYR THR ASP TRP LEU HIS PRO GLU ASP
SEQRES 31 D 543 PRO THR HIS LEU ARG ASP ALA MET SER ALA VAL VAL GLY
SEQRES 32 D 543 ASP HIS ASN VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY
SEQRES 33 D 543 ARG LEU ALA ALA GLN GLY ALA ARG VAL TYR ALA TYR ILE
SEQRES 34 D 543 PHE GLU HIS ARG ALA SER THR LEU THR TRP PRO LEU TRP
SEQRES 35 D 543 MET GLY VAL PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE
SEQRES 36 D 543 GLY LEU PRO LEU ASP PRO SER LEU ASN TYR THR THR GLU
SEQRES 37 D 543 GLU ARG ILE PHE ALA GLN ARG LEU MET LYS TYR TRP THR
SEQRES 38 D 543 ASN PHE ALA ARG THR GLY ASP PRO ASN ASP PRO ARG ASP
SEQRES 39 D 543 SER LYS SER PRO GLN TRP PRO PRO TYR THR THR ALA ALA
SEQRES 40 D 543 GLN GLN TYR VAL SER LEU ASN LEU LYS PRO LEU GLU VAL
SEQRES 41 D 543 ARG ARG GLY LEU ARG ALA GLN THR CYS ALA PHE TRP ASN
SEQRES 42 D 543 ARG PHE LEU PRO LYS LEU LEU SER ALA THR
HET TQV A 600 19
HET NAG A 701 14
HET CL A1544 1
HET SO4 A1545 5
HET SO4 A1546 5
HET SO4 A1547 5
HET SO4 A1548 5
HET SO4 A1549 5
HET SO4 A1550 5
HET CL A1990 1
HET CL A1991 1
HET TQV B 600 19
HET NAG B 701 14
HET NAG B 702 14
HET CL B1544 1
HET SO4 B1545 5
HET SO4 B1546 5
HET SO4 B1547 5
HET TQV C 600 19
HET NAG C 701 14
HET CL C1544 1
HET CL C1545 1
HET CL C1546 1
HET SO4 C1547 5
HET SO4 C1548 5
HET SO4 C1549 5
HET CL C1990 1
HET TQV D 600 19
HET NAG D 701 14
HET NAG D 702 14
HET NAG D 703 14
HET CL D1544 1
HET SO4 D1545 5
HET SO4 D1546 5
HET SO4 D1547 5
HET CL D1990 1
HET CL D1991 1
HETNAM TQV O-CRESYL-SALIGENIN PHOSPHATE
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM SO4 SULFATE ION
HETNAM CL CHLORIDE ION
FORMUL 5 TQV 4(C14 H15 O5 P)
FORMUL 6 NAG 7(C8 H15 N O6)
FORMUL 7 SO4 15(O4 S 2-)
FORMUL 8 CL 11(CL 1-)
FORMUL 9 HOH *835(H2 O)
HELIX 1 1 VAL A 42 ARG A 46 5 5
HELIX 2 2 PHE A 80 MET A 85 1 6
HELIX 3 3 LEU A 130 ASP A 134 5 5
HELIX 4 4 GLY A 135 GLY A 143 1 9
HELIX 5 5 VAL A 153 LEU A 159 1 7
HELIX 6 6 ASN A 170 ILE A 187 1 18
HELIX 7 7 ALA A 188 PHE A 190 5 3
HELIX 8 8 SER A 203 SER A 215 1 13
HELIX 9 9 SER A 215 SER A 220 1 6
HELIX 10 10 ALA A 241 VAL A 255 1 15
HELIX 11 11 ASP A 266 THR A 275 1 10
HELIX 12 12 PRO A 277 TRP A 286 1 10
HELIX 13 13 HIS A 287 LEU A 289 5 3
HELIX 14 14 THR A 311 GLY A 319 1 9
HELIX 15 15 GLY A 335 VAL A 340 1 6
HELIX 16 16 SER A 355 VAL A 367 1 13
HELIX 17 17 SER A 371 THR A 383 1 13
HELIX 18 18 ASP A 390 VAL A 407 1 18
HELIX 19 19 VAL A 407 GLN A 421 1 15
HELIX 20 20 PRO A 440 GLY A 444 5 5
HELIX 21 21 GLU A 450 PHE A 455 1 6
HELIX 22 22 GLY A 456 ASP A 460 5 5
HELIX 23 23 ASP A 460 ASN A 464 5 5
HELIX 24 24 THR A 466 GLY A 487 1 22
HELIX 25 25 ARG A 525 SER A 541 1 17
HELIX 26 26 VAL B 42 ARG B 46 5 5
HELIX 27 27 PHE B 80 MET B 85 1 6
HELIX 28 28 LEU B 130 ASP B 134 5 5
HELIX 29 29 GLY B 135 VAL B 141 1 7
HELIX 30 30 VAL B 153 LEU B 159 1 7
HELIX 31 31 ASN B 170 ILE B 187 1 18
HELIX 32 32 ALA B 188 PHE B 190 5 3
HELIX 33 33 SER B 203 SER B 215 1 13
HELIX 34 34 SER B 215 SER B 220 1 6
HELIX 35 35 SER B 240 VAL B 255 1 16
HELIX 36 36 ASN B 265 ARG B 274 1 10
HELIX 37 37 PRO B 277 GLU B 285 1 9
HELIX 38 38 TRP B 286 LEU B 289 5 4
HELIX 39 39 THR B 311 THR B 318 1 8
HELIX 40 40 GLY B 335 VAL B 340 1 6
HELIX 41 41 SER B 355 VAL B 367 1 13
HELIX 42 42 SER B 371 THR B 383 1 13
HELIX 43 43 ASP B 390 VAL B 407 1 18
HELIX 44 44 VAL B 407 GLN B 421 1 15
HELIX 45 45 GLU B 450 PHE B 455 1 6
HELIX 46 46 GLY B 456 ASP B 460 5 5
HELIX 47 47 ASP B 460 ASN B 464 5 5
HELIX 48 48 THR B 466 THR B 486 1 21
HELIX 49 49 ARG B 525 ARG B 534 1 10
HELIX 50 50 LEU B 536 SER B 541 1 6
HELIX 51 51 VAL C 42 ARG C 46 5 5
HELIX 52 52 PHE C 80 MET C 85 1 6
HELIX 53 53 LEU C 130 ASP C 134 5 5
HELIX 54 54 GLY C 135 GLY C 143 1 9
HELIX 55 55 VAL C 153 LEU C 159 1 7
HELIX 56 56 ASN C 170 ILE C 187 1 18
HELIX 57 57 ALA C 188 PHE C 190 5 3
HELIX 58 58 SER C 203 SER C 215 1 13
HELIX 59 59 SER C 215 SER C 220 1 6
HELIX 60 60 ALA C 241 VAL C 255 1 15
HELIX 61 61 ASP C 266 ARG C 276 1 11
HELIX 62 62 PRO C 277 GLU C 285 1 9
HELIX 63 63 TRP C 286 LEU C 289 5 4
HELIX 64 64 THR C 311 GLY C 319 1 9
HELIX 65 65 GLY C 335 VAL C 340 1 6
HELIX 66 66 SER C 355 VAL C 367 1 13
HELIX 67 67 SER C 371 THR C 383 1 13
HELIX 68 68 ASP C 390 VAL C 407 1 18
HELIX 69 69 VAL C 407 GLN C 421 1 15
HELIX 70 70 PRO C 440 GLY C 444 5 5
HELIX 71 71 GLU C 450 PHE C 455 1 6
HELIX 72 72 GLY C 456 ASP C 460 5 5
HELIX 73 73 ASP C 460 ASN C 464 5 5
HELIX 74 74 THR C 466 GLY C 487 1 22
HELIX 75 75 ARG C 525 PHE C 535 1 11
HELIX 76 76 PHE C 535 LEU C 540 1 6
HELIX 77 77 VAL D 42 ARG D 46 5 5
HELIX 78 78 PHE D 80 MET D 85 1 6
HELIX 79 79 LEU D 130 ASP D 134 5 5
HELIX 80 80 GLY D 135 GLY D 143 1 9
HELIX 81 81 VAL D 153 LEU D 159 1 7
HELIX 82 82 ASN D 170 ILE D 187 1 18
HELIX 83 83 ALA D 188 PHE D 190 5 3
HELIX 84 84 SER D 203 SER D 215 1 13
HELIX 85 85 LEU D 216 PHE D 222 5 7
HELIX 86 86 ALA D 241 VAL D 255 1 15
HELIX 87 87 ASN D 265 ARG D 276 1 12
HELIX 88 88 PRO D 277 GLU D 285 1 9
HELIX 89 89 TRP D 286 VAL D 288 5 3
HELIX 90 90 THR D 311 GLY D 319 1 9
HELIX 91 91 GLY D 335 VAL D 340 1 6
HELIX 92 92 SER D 355 VAL D 367 1 13
HELIX 93 93 SER D 371 THR D 383 1 13
HELIX 94 94 ASP D 390 VAL D 407 1 18
HELIX 95 95 VAL D 407 GLY D 422 1 16
HELIX 96 96 PRO D 440 GLY D 444 5 5
HELIX 97 97 GLU D 450 PHE D 455 1 6
HELIX 98 98 GLY D 456 ASP D 460 5 5
HELIX 99 99 ASP D 460 ASN D 464 5 5
HELIX 100 100 THR D 466 THR D 486 1 21
HELIX 101 101 ARG D 525 ARG D 534 1 10
HELIX 102 102 ARG D 534 ALA D 542 1 9
SHEET 1 AA 3 LEU A 9 ARG A 11 0
SHEET 2 AA 3 GLN A 16 ARG A 18 -1 O LEU A 17 N VAL A 10
SHEET 3 AA 3 VAL A 59 ASP A 61 1 O LEU A 60 N ARG A 18
SHEET 1 AB11 ILE A 20 ALA A 24 0
SHEET 2 AB11 GLY A 27 PRO A 36 -1 O GLY A 27 N ALA A 24
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 ILE A 429
SHEET 11 AB11 GLU A 519 ARG A 522 -1 O GLU A 519 N SER A 512
SHEET 1 AC 2 ALA A 38 GLU A 39 0
SHEET 2 AC 2 GLU A 51 PRO A 52 -1 O GLU A 51 N GLU A 39
SHEET 1 AD 2 VAL A 68 CYS A 69 0
SHEET 2 AD 2 LEU A 92 SER A 93 1 N SER A 93 O VAL A 68
SHEET 1 AE 2 VAL A 239 SER A 240 0
SHEET 2 AE 2 VAL A 302 VAL A 303 1 N VAL A 303 O VAL A 239
SHEET 1 BA 3 LEU B 9 ARG B 11 0
SHEET 2 BA 3 GLN B 16 ARG B 18 -1 O LEU B 17 N VAL B 10
SHEET 3 BA 3 VAL B 59 ASP B 61 1 O LEU B 60 N ARG B 18
SHEET 1 BB11 ILE B 20 LYS B 23 0
SHEET 2 BB11 PRO B 28 PRO B 36 -1 O VAL B 29 N LEU B 22
SHEET 3 BB11 TYR B 98 PRO B 104 -1 O LEU B 99 N GLY B 34
SHEET 4 BB11 VAL B 145 MET B 149 -1 O LEU B 146 N TRP B 102
SHEET 5 BB11 THR B 112 ILE B 118 1 O PRO B 113 N VAL B 145
SHEET 6 BB11 GLY B 192 GLU B 202 1 N ASP B 193 O THR B 112
SHEET 7 BB11 ARG B 224 GLN B 228 1 O ARG B 224 N LEU B 199
SHEET 8 BB11 GLN B 325 VAL B 331 1 O GLN B 325 N ALA B 225
SHEET 9 BB11 ARG B 424 PHE B 430 1 O ARG B 424 N VAL B 326
SHEET 10 BB11 GLN B 509 LEU B 513 1 O VAL B 511 N ILE B 429
SHEET 11 BB11 GLU B 519 ARG B 522 -1 O GLU B 519 N SER B 512
SHEET 1 BC 2 VAL B 68 CYS B 69 0
SHEET 2 BC 2 LEU B 92 SER B 93 1 N SER B 93 O VAL B 68
SHEET 1 CA 3 LEU C 9 ARG C 11 0
SHEET 2 CA 3 GLN C 16 ARG C 18 -1 O LEU C 17 N VAL C 10
SHEET 3 CA 3 VAL C 59 ASP C 61 1 O LEU C 60 N ARG C 18
SHEET 1 CB11 ILE C 20 ALA C 24 0
SHEET 2 CB11 GLY C 27 PRO C 36 -1 O GLY C 27 N ALA C 24
SHEET 3 CB11 TYR C 98 PRO C 104 -1 O LEU C 99 N ILE C 35
SHEET 4 CB11 VAL C 145 MET C 149 -1 O LEU C 146 N TRP C 102
SHEET 5 CB11 THR C 112 ILE C 118 1 O PRO C 113 N VAL C 145
SHEET 6 CB11 GLY C 192 GLU C 202 1 N ASP C 193 O THR C 112
SHEET 7 CB11 ARG C 224 GLN C 228 1 O ARG C 224 N LEU C 199
SHEET 8 CB11 GLN C 325 VAL C 331 1 O GLN C 325 N ALA C 225
SHEET 9 CB11 ARG C 424 PHE C 430 1 O ARG C 424 N VAL C 326
SHEET 10 CB11 GLN C 509 LEU C 513 1 O VAL C 511 N ILE C 429
SHEET 11 CB11 VAL C 520 ARG C 522 -1 O ARG C 521 N TYR C 510
SHEET 1 CC 2 VAL C 68 CYS C 69 0
SHEET 2 CC 2 LEU C 92 SER C 93 1 N SER C 93 O VAL C 68
SHEET 1 CD 2 VAL C 239 SER C 240 0
SHEET 2 CD 2 VAL C 302 VAL C 303 1 N VAL C 303 O VAL C 239
SHEET 1 DA 3 LEU D 9 VAL D 12 0
SHEET 2 DA 3 GLY D 15 ARG D 18 -1 O GLY D 15 N VAL D 12
SHEET 3 DA 3 VAL D 59 ASP D 61 1 O LEU D 60 N ARG D 18
SHEET 1 DB11 ILE D 20 ALA D 24 0
SHEET 2 DB11 GLY D 27 PRO D 36 -1 O GLY D 27 N ALA D 24
SHEET 3 DB11 TYR D 98 PRO D 104 -1 O LEU D 99 N ILE D 35
SHEET 4 DB11 VAL D 145 MET D 149 -1 O LEU D 146 N TRP D 102
SHEET 5 DB11 THR D 112 ILE D 118 1 O PRO D 113 N VAL D 145
SHEET 6 DB11 GLY D 192 GLU D 202 1 N ASP D 193 O THR D 112
SHEET 7 DB11 ARG D 224 GLN D 228 1 O ARG D 224 N LEU D 199
SHEET 8 DB11 GLN D 325 VAL D 331 1 O GLN D 325 N ALA D 225
SHEET 9 DB11 ARG D 424 PHE D 430 1 O ARG D 424 N VAL D 326
SHEET 10 DB11 GLN D 509 LEU D 513 1 O GLN D 509 N ALA D 427
SHEET 11 DB11 GLU D 519 ARG D 522 -1 O GLU D 519 N SER D 512
SHEET 1 DC 2 ALA D 38 GLU D 39 0
SHEET 2 DC 2 GLU D 51 PRO D 52 -1 O GLU D 51 N GLU D 39
SHEET 1 DD 2 VAL D 68 CYS D 69 0
SHEET 2 DD 2 LEU D 92 SER D 93 1 N SER D 93 O VAL D 68
SHEET 1 DE 2 VAL D 239 SER D 240 0
SHEET 2 DE 2 VAL D 302 VAL D 303 1 N VAL D 303 O VAL D 239
SSBOND 1 CYS A 69 CYS A 96 1555 1555 2.06
SSBOND 2 CYS A 257 CYS A 272 1555 1555 2.04
SSBOND 3 CYS A 409 CYS A 529 1555 1555 2.03
SSBOND 4 CYS B 69 CYS B 96 1555 1555 2.03
SSBOND 5 CYS B 257 CYS B 272 1555 1555 2.04
SSBOND 6 CYS B 409 CYS B 529 1555 1555 2.04
SSBOND 7 CYS C 69 CYS C 96 1555 1555 2.06
SSBOND 8 CYS C 257 CYS C 272 1555 1555 2.05
SSBOND 9 CYS C 409 CYS C 529 1555 1555 2.04
SSBOND 10 CYS D 69 CYS D 96 1555 1555 2.03
SSBOND 11 CYS D 257 CYS D 272 1555 1555 2.05
SSBOND 12 CYS D 409 CYS D 529 1555 1555 2.03
LINK ND2 ASN A 265 C1 NAG A 701 1555 1555 1.45
LINK P TQV A 600 OG SER A 203 1555 1555 1.69
LINK ND2 ASN B 265 C1 NAG B 701 1555 1555 1.45
LINK ND2 ASN B 350 C1 NAG B 702 1555 1555 1.46
LINK P TQV B 600 OG SER B 203 1555 1555 1.68
LINK ND2 ASN C 265 C1 NAG C 701 1555 1555 1.45
LINK P TQV C 600 OG SER C 203 1555 1555 1.74
LINK ND2 ASN D 265 C1 NAG D 701 1555 1555 1.45
LINK ND2 ASN D 350 C1 NAG D 702 1555 1555 1.45
LINK ND2 ASN D 464 C1 NAG D 703 1555 1555 1.46
LINK P TQV D 600 OG SER D 203 1555 1555 1.68
CISPEP 1 TYR A 105 PRO A 106 0 -1.36
CISPEP 2 PRO A 258 PRO A 259 0 3.46
CISPEP 3 SER A 497 PRO A 498 0 -11.10
CISPEP 4 TYR B 105 PRO B 106 0 5.17
CISPEP 5 CYS B 257 PRO B 258 0 -3.59
CISPEP 6 SER B 497 PRO B 498 0 -3.89
CISPEP 7 TYR C 105 PRO C 106 0 5.78
CISPEP 8 PRO C 258 PRO C 259 0 -5.93
CISPEP 9 TYR D 105 PRO D 106 0 3.62
CISPEP 10 PRO D 258 PRO D 259 0 -7.26
CISPEP 11 SER D 497 PRO D 498 0 4.50
SITE 1 AC1 12 TRP A 86 GLY A 121 GLY A 122 TYR A 124
SITE 2 AC1 12 GLU A 202 SER A 203 ALA A 204 PHE A 295
SITE 3 AC1 12 ARG A 296 PHE A 297 TYR A 337 HIS A 447
SITE 1 AC2 2 ARG A 165 HOH A2034
SITE 1 AC3 5 ARG A 525 ALA A 526 GLN A 527 THR A 528
SITE 2 AC3 5 HOH A2238
SITE 1 AC4 2 GLN A 413 ARG A 417
SITE 1 AC5 6 HIS A 381 HOH A2244 HOH A2245 LEU B 380
SITE 2 AC5 6 HIS B 381 PHE B 531
SITE 1 AC6 3 HIS A 432 LEU A 515 LYS A 516
SITE 1 AC7 1 ARG A 136
SITE 1 AC8 4 ARG A 46 PRO A 277 ALA A 278 HOH A2247
SITE 1 AC9 1 HOH A2172
SITE 1 BC1 1 ARG A 356
SITE 1 BC2 12 TRP B 86 GLY B 121 GLY B 122 TYR B 124
SITE 2 BC2 12 SER B 203 ALA B 204 PHE B 295 ARG B 296
SITE 3 BC2 12 PHE B 297 TYR B 337 HIS B 447 HOH B2042
SITE 1 BC3 1 ARG B 356
SITE 1 BC4 4 ARG B 525 ALA B 526 GLN B 527 THR B 528
SITE 1 BC5 4 HIS B 387 PRO B 388 GLU B 389 ASP B 390
SITE 1 BC6 4 GLN B 413 ARG B 417 ASN B 533 HOH B2140
SITE 1 BC7 13 TRP C 86 GLY C 121 GLY C 122 TYR C 124
SITE 2 BC7 13 GLU C 202 SER C 203 PHE C 295 PHE C 297
SITE 3 BC7 13 TYR C 337 PHE C 338 HIS C 447 HOH C2103
SITE 4 BC7 13 HOH C2233
SITE 1 BC8 1 ARG C 90
SITE 1 BC9 1 ALA C 278
SITE 1 CC1 1 ARG C 522
SITE 1 CC2 4 ARG C 525 ALA C 526 GLN C 527 THR C 528
SITE 1 CC3 6 LEU C 380 HIS C 381 HOH C2257 HOH C2258
SITE 2 CC3 6 HIS D 381 PHE D 531
SITE 1 CC4 2 GLY C 43 SER C 44
SITE 1 CC5 1 ARG C 18
SITE 1 CC6 12 TRP D 86 GLY D 121 GLY D 122 TYR D 124
SITE 2 CC6 12 SER D 203 ALA D 204 PHE D 295 ARG D 296
SITE 3 CC6 12 PHE D 297 TYR D 337 HIS D 447 HOH D2074
SITE 1 CC7 4 ARG D 525 ALA D 526 GLN D 527 THR D 528
SITE 1 CC8 5 ARG C 13 PRO C 55 VAL D 59 LEU D 60
SITE 2 CC8 5 ASP D 61
SITE 1 CC9 3 HIS D 432 ASN D 514 LEU D 515
SITE 1 DC1 1 HOH D2077
SITE 1 DC2 2 ARG A 253 HIS D 287
SITE 1 DC3 3 ASN A 265 THR A 267 GLU A 268
SITE 1 DC4 3 ASN B 265 THR B 267 GLU B 268
SITE 1 DC5 2 SER B 347 ASN B 350
SITE 1 DC6 2 ASN C 265 GLU C 268
SITE 1 DC7 2 ASN D 265 GLU D 268
SITE 1 DC8 2 SER D 347 ASN D 350
SITE 1 DC9 2 SER D 462 ASN D 464
CRYST1 135.540 173.250 224.940 90.00 90.00 90.00 P 21 21 21 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 0.007378 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005772 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004446 0.00000
TER 4225 THR A 543
TER 8428 THR B 543
TER 12659 THR C 543
TER 16903 THR D 543
MASTER 816 0 37 102 74 0 49 617994 4 284 168
END |