2WLS-pdb | HEADER HYDROLASE 25-JUN-09 2WLS
TITLE CRYSTAL STRUCTURE OF MUS MUSCULUS ACETYLCHOLINESTERASE IN
TITLE 2 COMPLEX WITH AMTS13
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYLCHOLINESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN, RESIDUES 32-574;
COMPND 5 EC: 3.1.1.7;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 7 EXPRESSION_SYSTEM_CELL_LINE: HEK293F;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PCDNA3.1
KEYWDS SERINE ESTERASE, ALTERNATIVE SPLICING, AMTS13, SYNAPSE,
KEYWDS 2 MEMBRANE, HYDROLASE, CELL MEMBRANE, CHOLINESTERASE,
KEYWDS 3 ACETYLCHOLINESTERASE, NEUROTRANSMITTER DEGRADATION,
KEYWDS 4 GPI-ANCHOR, LIPOPROTEIN, GLYCOPROTEIN, CELL JUNCTION
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.P.PANG,F.EKSTROM,G.A.POLSINELLI,Y.GAO,S.RANA,D.H.HUA,
AUTHOR 2 B.ANDERSSON,P.O.ANDERSSON,L.PENG,S.K.SINGH,R.K.MISHRA,
AUTHOR 3 K.Y.ZHU,A.M.FALLON,D.W.RAGSDALE,S.BRIMIJOIN
REVDAT 1 08-SEP-09 2WLS 0
JRNL AUTH Y.P.PANG,F.EKSTROM,G.A.POLSINELLI,Y.GAO,S.RANA,
JRNL AUTH 2 D.H.HUA,B.ANDERSSON,P.O.ANDERSSON,L.PENG,S.K.SINGH,
JRNL AUTH 3 R.K.MISHRA,K.Y.ZHU,A.M.FALLON,D.W.RAGSDALE,
JRNL AUTH 4 S.BRIMIJOIN
JRNL TITL SELECTIVE AND IRREVERSIBLE INHIBITORS OF MOSQUITO
JRNL TITL 2 ACETYLCHOLINESTERASES FOR CONTROLLING MALARIA AND
JRNL TITL 3 OTHER MOSQUITO-BORNE DISEASES.
JRNL REF PLOS ONE V. 4 E6851 2009
JRNL REFN ISSN 1932-6203
JRNL PMID 19714254
JRNL DOI 10.1371/JOURNAL.PONE.0006851
REMARK 2
REMARK 2 RESOLUTION. 2.60 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-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.600
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.037
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.36
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.45
REMARK 3 NUMBER OF REFLECTIONS : 61249
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.1859
REMARK 3 R VALUE (WORKING SET) : 0.1851
REMARK 3 FREE R VALUE : 0.2261
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.0
REMARK 3 FREE R VALUE TEST SET COUNT : 1220
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 29.0386 - 5.3980 0.99 6952 137 0.1723 0.1876
REMARK 3 2 5.3980 - 4.2890 0.99 6736 133 0.1454 0.1799
REMARK 3 3 4.2890 - 3.7481 0.99 6616 125 0.1591 0.2035
REMARK 3 4 3.7481 - 3.4060 1.00 6641 143 0.1789 0.2185
REMARK 3 5 3.4060 - 3.1622 1.00 6671 116 0.1955 0.2075
REMARK 3 6 3.1622 - 2.9759 1.00 6608 155 0.2256 0.2956
REMARK 3 7 2.9759 - 2.8270 1.00 6615 130 0.2297 0.3095
REMARK 3 8 2.8270 - 2.7041 1.00 6573 135 0.2408 0.3194
REMARK 3 9 2.7041 - 2.6000 1.00 6617 146 0.2509 0.3073
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 : 0.332
REMARK 3 B_SOL : 69.005
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.35
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.53
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 60.66
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.8455
REMARK 3 B22 (A**2) : 2.0636
REMARK 3 B33 (A**2) : -2.9091
REMARK 3 B12 (A**2) : 0.0000
REMARK 3 B13 (A**2) : -0.0000
REMARK 3 B23 (A**2) : -0.0000
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 8703
REMARK 3 ANGLE : 1.133 11873
REMARK 3 CHIRALITY : 0.075 1281
REMARK 3 PLANARITY : 0.006 1557
REMARK 3 DIHEDRAL : 18.461 3116
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 3 THE SO2CH3 GROUP OF AMTS13 IS UNDEFINED
REMARK 4
REMARK 4 2WLS COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 25-JUN-09.
REMARK 100 THE PDBE ID CODE IS EBI-40229.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-JAN-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : MAX II
REMARK 200 BEAMLINE : I911-3
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.948
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : MAR MOSAIC 225
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 61580
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.60
REMARK 200 RESOLUTION RANGE LOW (A) : 29.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 7.3
REMARK 200 R MERGE (I) : 0.08
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 17.20
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.74
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.3
REMARK 200 R MERGE FOR SHELL (I) : 0.52
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 4.40
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: REFMAC
REMARK 200 STARTING MODEL: PDB ENTRY 1J06
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 70
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.1
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 39.24000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 113.80200
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 55.15250
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 113.80200
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 39.24000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 55.15250
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
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 GENERATING THE BIOMOLECULE
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: PQS
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: PQS
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 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 PRO A 258
REMARK 465 PRO A 259
REMARK 465 GLY A 260
REMARK 465 GLY A 261
REMARK 465 ALA A 262
REMARK 465 GLY A 263
REMARK 465 GLY A 264
REMARK 465 THR A 543
REMARK 465 GLU B 1
REMARK 465 GLY B 2
REMARK 465 ARG B 3
REMARK 465 PRO B 258
REMARK 465 PRO B 259
REMARK 465 GLY B 260
REMARK 465 GLY B 261
REMARK 465 ALA B 262
REMARK 465 GLY B 263
REMARK 465 GLY B 264
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ARG A 3 CG CD NE CZ NH1 NH2
REMARK 470 ASP A 323 CG OD1 OD2
REMARK 470 ARG A 493 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 496 CG CD CE NZ
REMARK 470 ARG B 493 CG CD NE CZ NH1 NH2
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 ND2 ASN B 350 - C2 NAG B 601 2.10
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 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 47 -11.37 71.00
REMARK 500 CYS A 96 1.47 -152.35
REMARK 500 PHE A 158 -4.26 -142.68
REMARK 500 ALA A 167 69.49 -161.55
REMARK 500 SER A 203 -124.68 58.94
REMARK 500 ASP A 306 -89.77 -140.35
REMARK 500 TYR A 341 56.91 -94.76
REMARK 500 SER A 371 174.11 -56.58
REMARK 500 VAL A 407 -66.52 -128.24
REMARK 500 GLN A 421 31.52 -140.88
REMARK 500 SER A 462 7.77 -68.35
REMARK 500 ASN A 464 14.97 83.16
REMARK 500 PHE B 47 -0.87 75.76
REMARK 500 PRO B 55 153.34 -45.09
REMARK 500 ALA B 62 56.64 -117.95
REMARK 500 ALA B 167 71.96 -161.93
REMARK 500 SER B 203 -124.29 50.27
REMARK 500 ASP B 306 -83.79 -121.43
REMARK 500 GLN B 322 -74.34 -39.57
REMARK 500 ASP B 323 39.17 -90.90
REMARK 500 TYR B 341 59.55 -91.95
REMARK 500 VAL B 367 65.15 -119.14
REMARK 500 HIS B 387 58.31 -146.99
REMARK 500 VAL B 407 -66.07 -128.16
REMARK 500 ASN B 464 40.22 70.20
REMARK 500 ASP B 491 107.79 -58.52
REMARK 500 ASP B 494 114.42 175.53
REMARK 500 LYS B 496 123.32 65.97
REMARK 500 SER B 497 -30.55 -148.95
REMARK 500 PRO B 498 -165.96 -75.82
REMARK 500 ALA B 506 -75.51 -64.19
REMARK 500 SER B 541 47.29 -79.56
REMARK 500 ALA B 542 24.19 179.48
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 600
REMARK 600 HETEROGEN
REMARK 600 N,N,N-TRIMETHYL-13-(METHYLSULFONYLTHIO)TRIDECAN-1-AMINIUM
REMARK 600 BROMIDE (A13): COMPUND REPORTED IN PANG Y-P, SINGH SK, GAO
REMARK 600 Y, LASSITER TL, MISHRA RK, ET AL.2009 SELECTIVE AND
REMARK 600 IRREVERSIBLE INHIBITORS OF APHID ACETYLCHOLINESTERASES
REMARK 600 STEPS TOWARD HUMAN-SAFE INSECTICIDES. PLOS ONE 4 E4349.
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 X13 B 1544
REMARK 610 X13 A 1543
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE X13 A1543
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE X13 B1544
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B1545
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P6G B1546
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2JGH RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE
REMARK 900 INHIBITED BY NON-AGED VX
REMARK 900 RELATED ID: 2WHQ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ACETYLCHOLINESTERASE,
REMARK 900 PHOSPHONYLATED BY SARIN (AGED) IN COMPLEX
REMARK 900 WITH HI-6
REMARK 900 RELATED ID: 1MAH RELATED DB: PDB
REMARK 900 FASCICULIN2 - MOUSE ACETYLCHOLINESTERASE COMPLEX
REMARK 900 RELATED ID: 2HA6 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MUTANT S203A OF
REMARK 900 MOUSEACETYLCHOLINESTERASE COMPLEXED WITH
REMARK 900 SUCCINYLCHOLINE
REMARK 900 RELATED ID: 1MAA RELATED DB: PDB
REMARK 900 MOUSE ACETYLCHOLINESTERASE CATALYTIC DOMAIN,
REMARK 900 GLYCOSYLATEDPROTEIN
REMARK 900 RELATED ID: 2C0Q RELATED DB: PDB
REMARK 900 NON-AGED FORM OF MOUSE ACETYLCHOLINESTERASE
REMARK 900 INHIBITED BY TABUN
REMARK 900 RELATED ID: 2JGG RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE
REMARK 900 INHIBITED BY NON-AGED SARIN
REMARK 900 RELATED ID: 2JGL RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE
REMARK 900 INHIBITED BY AGED VX AND SARIN
REMARK 900 RELATED ID: 1Q84 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE MOUSE
REMARK 900 ACETYLCHOLINESTERASE-TZ2PA6ANTI COMPLEX
REMARK 900 RELATED ID: 2JGM RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE
REMARK 900 INHIBITED BY AGED DIISOPROPYL FLUOROPHOSPHATE
REMARK 900 (DFP)
REMARK 900 RELATED ID: 2JGE RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE
REMARK 900 INHIBITED BY NON-AGED METHAMIDOPHOS
REMARK 900 RELATED ID: 1Q83 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE MOUSE
REMARK 900 ACETYLCHOLINESTERASE-TZ2PA6SYN COMPLEX
REMARK 900 RELATED ID: 2HA3 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE
REMARK 900 COMPLEXEDWITH CHOLINE
REMARK 900 RELATED ID: 1C2B RELATED DB: PDB
REMARK 900 ELECTROPHORUS ELECTRICUS ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 2HA0 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE
REMARK 900 COMPLEXEDWITH 4-KETOAMYLTRIMETHYLAMMONIUM
REMARK 900 RELATED ID: 2JEY RELATED DB: PDB
REMARK 900 MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX
REMARK 900 WITH HLO-7
REMARK 900 RELATED ID: 2JGI RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE
REMARK 900 INHIBITED BY NON-AGED DIISOPROPYL
REMARK 900 FLUOROPHOSPHATE (DFP)
REMARK 900 RELATED ID: 1N5R RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE MOUSE
REMARK 900 ACETYLCHOLINESTERASE-PROPIDIUM COMPLEX
REMARK 900 RELATED ID: 2JGJ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE
REMARK 900 INHIBITED BY AGED METHAMIDOPHOS
REMARK 900 RELATED ID: 1J06 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE
REMARK 900 IN THE APOFORM
REMARK 900 RELATED ID: 2JF0 RELATED DB: PDB
REMARK 900 MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX
REMARK 900 WITH TABUN AND ORTHO-7
REMARK 900 RELATED ID: 2C0P RELATED DB: PDB
REMARK 900 AGED FORM OF MOUSE ACETYLCHOLINESTERASE
REMARK 900 INHIBITED BY 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: 2WHR RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ACETYLCHOLINESTERASE IN
REMARK 900 COMPLEX WITH K027
REMARK 900 RELATED ID: 1N5M RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE MOUSE
REMARK 900 ACETYLCHOLINESTERASE-GALLAMINE COMPLEX
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: 2HA2 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE
REMARK 900 COMPLEXEDWITH SUCCINYLCHOLINE
REMARK 900 RELATED ID: 2WHP RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ACETYLCHOLINESTERASE,
REMARK 900 PHOSPHONYLATED BY SARIN AND IN COMPLEX WITH
REMARK 900 HI-6
REMARK 900 RELATED ID: 2JEZ RELATED DB: PDB
REMARK 900 MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX
REMARK 900 WITH TABUN AND HLO-7
REMARK 900 RELATED ID: 2JGK RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE
REMARK 900 INHIBITED BY AGED FENAMIPHOS
REMARK 900 RELATED ID: 1KU6 RELATED DB: PDB
REMARK 900 FASCICULIN 2-MOUSE ACETYLCHOLINESTERASE COMPLEX
REMARK 900 RELATED ID: 2HA4 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MUTANT S203A OF
REMARK 900 MOUSEACETYLCHOLINESTERASE COMPLEXED WITH
REMARK 900 ACETYLCHOLINE
REMARK 900 RELATED ID: 1J07 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE MOUSE
REMARK 900 ACETYLCHOLINESTERASE-DECIDIUM COMPLEX
REMARK 900 RELATED ID: 2HA7 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MUTANT S203A OF
REMARK 900 MOUSEACETYLCHOLINESTERASE COMPLEXED WITH
REMARK 900 BUTYRYLTHIOCHOLINE
REMARK 900 RELATED ID: 2JGF RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE
REMARK 900 INHIBITED BY NON-AGED FENAMIPHOS
REMARK 900 RELATED ID: 1C2O RELATED DB: PDB
REMARK 900 ELECTROPHORUS ELECTRICUS ACETYLCHOLINESTERASE
DBREF 2WLS A 1 543 UNP P21836 ACES_MOUSE 32 574
DBREF 2WLS B 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
HET NAG A 601 14
HET NAG A 701 14
HET X13 A1543 18
HET X13 B1544 18
HET PEG B1545 7
HET P6G B1546 19
HETNAM P6G HEXAETHYLENE GLYCOL
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM X13 N,N,N-TRIMETHYL-13-[(METHYLSULFONYL)SULFANYL]
HETNAM 2 X13 TRIDECAN-1-AMINIUM
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
FORMUL 3 P6G C12 H26 O7
FORMUL 4 PEG C4 H10 O3
FORMUL 5 X13 2(C17 H38 N1 O2 S2)
FORMUL 6 NAG 2(C8 H15 N O6)
FORMUL 7 HOH *349(H2 O1)
HELIX 1 1 ASP A 5 GLN A 7 5 3
HELIX 2 2 VAL A 42 ARG A 46 5 5
HELIX 3 3 PHE A 80 MET A 85 1 6
HELIX 4 4 LEU A 130 ASP A 134 5 5
HELIX 5 5 GLY A 135 GLY A 143 1 9
HELIX 6 6 VAL A 153 LEU A 159 1 7
HELIX 7 7 ASN A 170 ILE A 187 1 18
HELIX 8 8 ALA A 188 PHE A 190 5 3
HELIX 9 9 SER A 203 LEU A 214 1 12
HELIX 10 10 SER A 215 SER A 220 1 6
HELIX 11 11 ALA A 241 GLY A 256 1 16
HELIX 12 12 ASN A 265 ARG A 274 1 10
HELIX 13 13 PRO A 277 GLU A 285 1 9
HELIX 14 14 TRP A 286 LEU A 289 5 4
HELIX 15 15 THR A 311 GLY A 319 1 9
HELIX 16 16 GLY A 335 VAL A 340 1 6
HELIX 17 17 SER A 355 VAL A 367 1 13
HELIX 18 18 SER A 371 THR A 383 1 13
HELIX 19 19 ASP A 390 VAL A 407 1 18
HELIX 20 20 VAL A 407 ALA A 420 1 14
HELIX 21 21 PRO A 440 GLY A 444 5 5
HELIX 22 22 GLU A 450 PHE A 455 1 6
HELIX 23 23 GLY A 456 ASP A 460 5 5
HELIX 24 24 ASP A 460 ASN A 464 5 5
HELIX 25 25 THR A 466 GLY A 487 1 22
HELIX 26 26 ARG A 525 ARG A 534 1 10
HELIX 27 27 ARG A 534 LEU A 540 1 7
HELIX 28 28 ASP B 5 GLN B 7 5 3
HELIX 29 29 VAL B 42 ARG B 46 5 5
HELIX 30 30 PHE B 80 MET B 85 1 6
HELIX 31 31 LEU B 130 ASP B 134 5 5
HELIX 32 32 GLY B 135 GLY B 143 1 9
HELIX 33 33 VAL B 153 LEU B 159 1 7
HELIX 34 34 ASN B 170 ILE B 187 1 18
HELIX 35 35 ALA B 188 PHE B 190 5 3
HELIX 36 36 SER B 203 LEU B 214 1 12
HELIX 37 37 SER B 215 SER B 220 1 6
HELIX 38 38 ALA B 241 VAL B 255 1 15
HELIX 39 39 ASN B 265 THR B 275 1 11
HELIX 40 40 PRO B 277 GLU B 285 1 9
HELIX 41 41 TRP B 286 VAL B 288 5 3
HELIX 42 42 THR B 311 GLY B 319 1 9
HELIX 43 43 GLY B 335 LEU B 339 5 5
HELIX 44 44 SER B 355 VAL B 367 1 13
HELIX 45 45 SER B 371 THR B 383 1 13
HELIX 46 46 ASP B 390 VAL B 407 1 18
HELIX 47 47 VAL B 407 GLN B 421 1 15
HELIX 48 48 PRO B 440 GLY B 444 5 5
HELIX 49 49 GLU B 450 GLY B 456 1 7
HELIX 50 50 LEU B 457 ASN B 464 5 8
HELIX 51 51 THR B 466 GLY B 487 1 22
HELIX 52 52 ARG B 525 SER B 541 1 17
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 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 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 AD 2 VAL A 239 SER A 240 0
SHEET 2 AD 2 VAL A 302 VAL A 303 1 N VAL A 303 O VAL A 239
SHEET 1 BA 3 LEU B 9 VAL B 12 0
SHEET 2 BA 3 GLY B 15 ARG B 18 -1 O GLY B 15 N VAL B 12
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 ALA B 24 0
SHEET 2 BB11 GLY B 27 PRO B 36 -1 O GLY B 27 N ALA B 24
SHEET 3 BB11 TYR B 98 PRO B 104 -1 O LEU B 99 N ILE B 35
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 BD 2 VAL B 239 SER B 240 0
SHEET 2 BD 2 VAL B 302 VAL B 303 1 N VAL B 303 O VAL B 239
SSBOND 1 CYS A 69 CYS A 96 1555 1555 2.06
SSBOND 2 CYS A 257 CYS A 272 1555 1555 2.06
SSBOND 3 CYS A 409 CYS A 529 1555 1555 2.06
SSBOND 4 CYS B 69 CYS B 96 1555 1555 2.06
SSBOND 5 CYS B 257 CYS B 272 1555 1555 2.06
SSBOND 6 CYS B 409 CYS B 529 1555 1555 2.06
LINK ND2 ASN A 350 C1 NAG A 601 1555 1555 1.45
LINK ND2 ASN A 464 C1 NAG A 701 1555 1555 1.45
CISPEP 1 TYR A 105 PRO A 106 0 -0.49
CISPEP 2 TYR B 105 PRO B 106 0 9.64
CISPEP 3 SER B 497 PRO B 498 0 -9.54
SITE 1 AC1 6 GLY A 345 SER A 347 ASN A 350 HOH A2107
SITE 2 AC1 6 HOH A2182 HOH A2183
SITE 1 AC2 1 ASN A 464
SITE 1 AC3 7 GLY B 345 SER B 347 ASN B 350 LEU B 353
SITE 2 AC3 7 HOH B2162 HOH B2163 HOH B2164
SITE 1 AC4 8 TYR A 72 TRP A 86 GLY A 121 TYR A 124
SITE 2 AC4 8 GLU A 202 TRP A 286 PHE A 338 HIS A 447
SITE 1 AC5 7 TYR B 72 TRP B 86 GLU B 202 TRP B 286
SITE 2 AC5 7 PHE B 338 TYR B 341 HIS B 447
SITE 1 AC6 3 GLY B 305 SER B 309 ASP B 310
SITE 1 AC7 10 LEU A 380 HIS A 381 GLN A 527 PHE A 535
SITE 2 AC7 10 LEU B 380 HIS B 381 GLN B 527 PHE B 535
SITE 3 AC7 10 HOH B2165 HOH B2166
CRYST1 78.480 110.305 227.604 90.00 90.00 90.00 P 21 21 21 8
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 0.012742 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009066 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004394 0.00000
TER 4186 ALA A 542
TER 8346 THR B 543
MASTER 471 0 6 52 36 0 13 6 8783 2 104 84
END
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