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HEADER HYDROLASE 06-MAY-09 2WHQ
TITLE CRYSTAL STRUCTURE OF ACETYLCHOLINESTERASE, PHOSPHONYLATED
TITLE 2 BY SARIN (AGED) IN COMPLEX WITH HI-6
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYLCHOLINESTERASE;
COMPND 3 CHAIN: A, B;
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: CATALYTIC SER203 PHOSPHONYLATED BY SARIN.
COMPND 9 THE COMPLEX WAS SUBSEQUENTLY AGED
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: HUMAN EMBRYONIC KIDNEY (HEK)
SOURCE 8 293 CELLS;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PCDNA3.1
KEYWDS HI-6, SYNAPSE, MEMBRANE, SECRETED, HYDROLASE,
KEYWDS 2 NEUROTRANSMITTER DEGRADATION, CHOLINESTERASE, SERINE
KEYWDS 3 ESTERASE, ALTERNATIVE SPLICING, CELL JUNCTION, CELL
KEYWDS 4 MEMBRANE, DISULFIDE BOND, AGED SARIN, GPI-ANCHOR,
KEYWDS 5 LIPOPROTEIN, GLYCOPROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR F.EKSTROM,A.HORNBERG,E.ARTURSSON,L.G.HAMMARSTROM,
AUTHOR 2 G.SCHNEIDER,Y.P.PANG
REVDAT 1 30-JUN-09 2WHQ 0
JRNL AUTH F.EKSTROM,A.HORNBERG,E.ARTURSSON,L.G.HAMMARSTROM,
JRNL AUTH 2 G.SCHNEIDER,Y.P.PANG
JRNL TITL STRUCTURE OF HI-6*SARIN-ACETYLCHOLINESTERASE
JRNL TITL 2 DETERMINED BY X-RAY CRYSTALLOGRAPHY AND MOLECULAR
JRNL TITL 3 DYNAMICS SIMULATION: REACTIVATOR MECHANISM AND
JRNL TITL 4 DESIGN.
JRNL REF PLOS ONE V. 4 E5957 2009
JRNL REFN ISSN 1932-6203
JRNL PMID 19536291
JRNL DOI 10.1371/JOURNAL.PONE.0005957
REMARK 2
REMARK 2 RESOLUTION. 2.15 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) : 2.150
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.089
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.35
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.59
REMARK 3 NUMBER OF REFLECTIONS : 110749
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.1860
REMARK 3 R VALUE (WORKING SET) : 0.1855
REMARK 3 FREE R VALUE : 0.2119
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.0
REMARK 3 FREE R VALUE TEST SET COUNT : 2191
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 29.0921 - 5.4068 0.95 6856 137 0.1812 0.1964
REMARK 3 2 5.4068 - 4.2960 1.00 6938 137 0.1349 0.1531
REMARK 3 3 4.2960 - 3.7542 1.00 6880 134 0.1402 0.1739
REMARK 3 4 3.7542 - 3.4115 1.00 6839 146 0.1580 0.1663
REMARK 3 5 3.4115 - 3.1673 1.00 6831 125 0.1736 0.2072
REMARK 3 6 3.1673 - 2.9808 1.00 6785 148 0.1769 0.1891
REMARK 3 7 2.9808 - 2.8316 1.00 6796 137 0.1710 0.2064
REMARK 3 8 2.8316 - 2.7085 1.00 6784 133 0.1742 0.2079
REMARK 3 9 2.7085 - 2.6043 1.00 6741 151 0.1698 0.2257
REMARK 3 10 2.6043 - 2.5145 1.00 6766 147 0.1778 0.2102
REMARK 3 11 2.5145 - 2.4359 1.00 6754 115 0.1830 0.2132
REMARK 3 12 2.4359 - 2.3663 1.00 6776 131 0.2075 0.2350
REMARK 3 13 2.3663 - 2.3040 1.00 6720 147 0.2123 0.2668
REMARK 3 14 2.3040 - 2.2478 1.00 6691 139 0.2268 0.2711
REMARK 3 15 2.2478 - 2.1967 1.00 6743 141 0.2686 0.2762
REMARK 3 16 2.1967 - 2.1500 0.99 6658 123 0.3523 0.3714
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 : 0.361
REMARK 3 B_SOL : 70.001
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.35
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.38
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8334
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 152
REMARK 3 SOLVENT ATOMS : 650
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 45.78
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.8764
REMARK 3 B22 (A**2) : 0.7953
REMARK 3 B33 (A**2) : 0.0811
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 : 0.010 8737
REMARK 3 ANGLE : 1.235 11909
REMARK 3 CHIRALITY : 0.085 1280
REMARK 3 PLANARITY : 0.006 1562
REMARK 3 DIHEDRAL : 18.237 3130
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A
REMARK 3 ORIGIN FOR THE GROUP (A): 27.0729 12.3020 16.6363
REMARK 3 T TENSOR
REMARK 3 T11: 0.2717 T22: 0.2513
REMARK 3 T33: 0.2752 T12: -0.0071
REMARK 3 T13: 0.0032 T23: 0.0182
REMARK 3 L TENSOR
REMARK 3 L11: 0.6099 L22: 0.5173
REMARK 3 L33: 1.4607 L12: -0.1201
REMARK 3 L13: 0.0894 L23: -0.2302
REMARK 3 S TENSOR
REMARK 3 S11: -0.0379 S12: 0.0316 S13: -0.0027
REMARK 3 S21: 0.0209 S22: 0.0189 S23: 0.0022
REMARK 3 S31: 0.1179 S32: -0.0715 S33: 0.0183
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN B
REMARK 3 ORIGIN FOR THE GROUP (A): 7.5217 4.9684 -40.2912
REMARK 3 T TENSOR
REMARK 3 T11: 0.2751 T22: 0.2859
REMARK 3 T33: 0.2815 T12: -0.0115
REMARK 3 T13: -0.0325 T23: -0.0504
REMARK 3 L TENSOR
REMARK 3 L11: 0.5673 L22: 0.7957
REMARK 3 L33: 1.9925 L12: -0.0111
REMARK 3 L13: 0.3331 L23: 0.4133
REMARK 3 S TENSOR
REMARK 3 S11: 0.1026 S12: 0.0610 S13: -0.0450
REMARK 3 S21: 0.0504 S22: -0.0700 S23: 0.0669
REMARK 3 S31: 0.1943 S32: 0.0211 S33: -0.0265
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN W
REMARK 3 ORIGIN FOR THE GROUP (A): 21.3865 9.2199 -8.1312
REMARK 3 T TENSOR
REMARK 3 T11: 0.2948 T22: 0.2910
REMARK 3 T33: 0.2849 T12: -0.0163
REMARK 3 T13: 0.0017 T23: 0.0004
REMARK 3 L TENSOR
REMARK 3 L11: 0.1510 L22: 0.0325
REMARK 3 L33: 0.3622 L12: -0.0721
REMARK 3 L13: 0.1424 L23: -0.0457
REMARK 3 S TENSOR
REMARK 3 S11: 0.0135 S12: 0.0206 S13: -0.0581
REMARK 3 S21: -0.0086 S22: -0.0096 S23: -0.0072
REMARK 3 S31: 0.0979 S32: 0.0485 S33: -0.0045
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: RESIDUES 258-264 ARE DISORDERED
REMARK 4
REMARK 4 2WHQ COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 06-MAY-09.
REMARK 100 THE PDBE ID CODE IS EBI-39644.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-FEB-07
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) : 1.041
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 110895
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.20
REMARK 200 RESOLUTION RANGE LOW (A) : 29.20
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 5.7
REMARK 200 R MERGE (I) : 0.06
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 15.30
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.30
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 5.7
REMARK 200 R MERGE FOR SHELL (I) : 0.44
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 4.50
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: 26-30 % (V/V) PEG750MME 0.1 M
REMARK 280 HEPES PH 7.0
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 39.77500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 113.53000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 56.16000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 113.53000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 39.77500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 56.16000
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 ALA A 544
REMARK 465 THR A 545
REMARK 465 GLU A 546
REMARK 465 ALA A 547
REMARK 465 PRO A 548
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 465 THR B 545
REMARK 465 GLU B 546
REMARK 465 ALA B 547
REMARK 465 PRO B 548
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 165 CG CD NE CZ NH1 NH2
REMARK 470 TRP A 286 CG CD1 CD2 NE1 CE2 CE3 CZ2 CZ3
REMARK 470 TRP A 286 CH2
REMARK 470 LYS A 496 CG CD CE NZ
REMARK 470 GLU B 268 CG CD OE1 OE2
REMARK 470 TRP B 286 CH2
REMARK 470 TRP B 286 CG CD1 CD2 NE1 CE2 CE3 CZ2 CZ3
REMARK 470 ASP B 323 CG OD1 OD2
REMARK 470 ARG B 493 CG CD NE CZ NH1 NH2
REMARK 470 ALA B 544 CA C O CB
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 -6.43 75.85
REMARK 500 ASP A 306 -89.05 -126.27
REMARK 500 VAL A 407 -59.02 -131.54
REMARK 500 ARG A 493 43.21 -83.56
REMARK 500 ASP A 494 73.62 -175.19
REMARK 500 ARG A 525 50.50 37.28
REMARK 500 PHE B 47 -5.54 69.25
REMARK 500 ALA B 62 55.84 -119.62
REMARK 500 ASN B 170 19.67 57.47
REMARK 500 ASP B 306 -87.44 -128.67
REMARK 500 VAL B 407 -59.31 -124.27
REMARK 500 ASP B 494 98.54 111.10
REMARK 500 SER B 495 -95.94 -69.87
REMARK 500 LYS B 496 105.21 -8.48
REMARK 500 SER B 497 -158.98 -55.00
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 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 HI6 B 1545
REMARK 610 HI6 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 HI6 A1543
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HI6 B1545
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P6G A1544
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B1546
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGE B1547
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGE A1545
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGE B1548
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGE B1549
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: 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: 1C2B RELATED DB: PDB
REMARK 900 ELECTROPHORUS ELECTRICUS ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 2HA3 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE
REMARK 900 COMPLEXEDWITH CHOLINE
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: 1N5M RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE MOUSE
REMARK 900 ACETYLCHOLINESTERASE-GALLAMINE COMPLEX
REMARK 900 RELATED ID: 2HA2 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE
REMARK 900 COMPLEXEDWITH SUCCINYLCHOLINE
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: 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: 2JGF RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE
REMARK 900 INHIBITED BY NON-AGED FENAMIPHOS
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: 1C2O RELATED DB: PDB
REMARK 900 ELECTROPHORUS ELECTRICUS ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 2WHR RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ACETYLCHOLINESTERASE IN
REMARK 900 COMPLEX WITH K027
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
DBREF 2WHQ A 1 543 UNP P21836 ACES_MOUSE 32 574
DBREF 2WHQ A 544 548 PDB 2WHQ 2WHQ 544 548
DBREF 2WHQ B 1 543 UNP P21836 ACES_MOUSE 32 574
DBREF 2WHQ B 544 548 PDB 2WHQ 2WHQ 544 548
SEQRES 1 A 548 GLU GLY ARG GLU ASP PRO GLN LEU LEU VAL ARG VAL ARG
SEQRES 2 A 548 GLY GLY GLN LEU ARG GLY ILE ARG LEU LYS ALA PRO GLY
SEQRES 3 A 548 GLY PRO VAL SER ALA PHE LEU GLY ILE PRO PHE ALA GLU
SEQRES 4 A 548 PRO PRO VAL GLY SER ARG ARG PHE MET PRO PRO GLU PRO
SEQRES 5 A 548 LYS ARG PRO TRP SER GLY VAL LEU ASP ALA THR THR PHE
SEQRES 6 A 548 GLN ASN VAL CYS TYR GLN TYR VAL ASP THR LEU TYR PRO
SEQRES 7 A 548 GLY PHE GLU GLY THR GLU MET TRP ASN PRO ASN ARG GLU
SEQRES 8 A 548 LEU SER GLU ASP CYS LEU TYR LEU ASN VAL TRP THR PRO
SEQRES 9 A 548 TYR PRO ARG PRO ALA SER PRO THR PRO VAL LEU ILE TRP
SEQRES 10 A 548 ILE TYR GLY GLY GLY PHE TYR SER GLY ALA ALA SER LEU
SEQRES 11 A 548 ASP VAL TYR ASP GLY ARG PHE LEU ALA GLN VAL GLU GLY
SEQRES 12 A 548 ALA VAL LEU VAL SER MET ASN TYR ARG VAL GLY THR PHE
SEQRES 13 A 548 GLY PHE LEU ALA LEU PRO GLY SER ARG GLU ALA PRO GLY
SEQRES 14 A 548 ASN VAL GLY LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP
SEQRES 15 A 548 VAL GLN GLU ASN ILE ALA ALA PHE GLY GLY ASP PRO MET
SEQRES 16 A 548 SER VAL THR LEU PHE GLY GLU SBG ALA GLY ALA ALA SER
SEQRES 17 A 548 VAL GLY MET HIS ILE LEU SER LEU PRO SER ARG SER LEU
SEQRES 18 A 548 PHE HIS ARG ALA VAL LEU GLN SER GLY THR PRO ASN GLY
SEQRES 19 A 548 PRO TRP ALA THR VAL SER ALA GLY GLU ALA ARG ARG ARG
SEQRES 20 A 548 ALA THR LEU LEU ALA ARG LEU VAL GLY CYS PRO PRO GLY
SEQRES 21 A 548 GLY ALA GLY GLY ASN ASP THR GLU LEU ILE ALA CYS LEU
SEQRES 22 A 548 ARG THR ARG PRO ALA GLN ASP LEU VAL ASP HIS GLU TRP
SEQRES 23 A 548 HIS VAL LEU PRO GLN GLU SER ILE PHE ARG PHE SER PHE
SEQRES 24 A 548 VAL PRO VAL VAL ASP GLY ASP PHE LEU SER ASP THR PRO
SEQRES 25 A 548 GLU ALA LEU ILE ASN THR GLY ASP PHE GLN ASP LEU GLN
SEQRES 26 A 548 VAL LEU VAL GLY VAL VAL LYS ASP GLU GLY SER TYR PHE
SEQRES 27 A 548 LEU VAL TYR GLY VAL PRO GLY PHE SER LYS ASP ASN GLU
SEQRES 28 A 548 SER LEU ILE SER ARG ALA GLN PHE LEU ALA GLY VAL ARG
SEQRES 29 A 548 ILE GLY VAL PRO GLN ALA SER ASP LEU ALA ALA GLU ALA
SEQRES 30 A 548 VAL VAL LEU HIS TYR THR ASP TRP LEU HIS PRO GLU ASP
SEQRES 31 A 548 PRO THR HIS LEU ARG ASP ALA MET SER ALA VAL VAL GLY
SEQRES 32 A 548 ASP HIS ASN VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY
SEQRES 33 A 548 ARG LEU ALA ALA GLN GLY ALA ARG VAL TYR ALA TYR ILE
SEQRES 34 A 548 PHE GLU HIS ARG ALA SER THR LEU THR TRP PRO LEU TRP
SEQRES 35 A 548 MET GLY VAL PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE
SEQRES 36 A 548 GLY LEU PRO LEU ASP PRO SER LEU ASN TYR THR THR GLU
SEQRES 37 A 548 GLU ARG ILE PHE ALA GLN ARG LEU MET LYS TYR TRP THR
SEQRES 38 A 548 ASN PHE ALA ARG THR GLY ASP PRO ASN ASP PRO ARG ASP
SEQRES 39 A 548 SER LYS SER PRO GLN TRP PRO PRO TYR THR THR ALA ALA
SEQRES 40 A 548 GLN GLN TYR VAL SER LEU ASN LEU LYS PRO LEU GLU VAL
SEQRES 41 A 548 ARG ARG GLY LEU ARG ALA GLN THR CYS ALA PHE TRP ASN
SEQRES 42 A 548 ARG PHE LEU PRO LYS LEU LEU SER ALA THR ALA THR GLU
SEQRES 43 A 548 ALA PRO
SEQRES 1 B 548 GLU GLY ARG GLU ASP PRO GLN LEU LEU VAL ARG VAL ARG
SEQRES 2 B 548 GLY GLY GLN LEU ARG GLY ILE ARG LEU LYS ALA PRO GLY
SEQRES 3 B 548 GLY PRO VAL SER ALA PHE LEU GLY ILE PRO PHE ALA GLU
SEQRES 4 B 548 PRO PRO VAL GLY SER ARG ARG PHE MET PRO PRO GLU PRO
SEQRES 5 B 548 LYS ARG PRO TRP SER GLY VAL LEU ASP ALA THR THR PHE
SEQRES 6 B 548 GLN ASN VAL CYS TYR GLN TYR VAL ASP THR LEU TYR PRO
SEQRES 7 B 548 GLY PHE GLU GLY THR GLU MET TRP ASN PRO ASN ARG GLU
SEQRES 8 B 548 LEU SER GLU ASP CYS LEU TYR LEU ASN VAL TRP THR PRO
SEQRES 9 B 548 TYR PRO ARG PRO ALA SER PRO THR PRO VAL LEU ILE TRP
SEQRES 10 B 548 ILE TYR GLY GLY GLY PHE TYR SER GLY ALA ALA SER LEU
SEQRES 11 B 548 ASP VAL TYR ASP GLY ARG PHE LEU ALA GLN VAL GLU GLY
SEQRES 12 B 548 ALA VAL LEU VAL SER MET ASN TYR ARG VAL GLY THR PHE
SEQRES 13 B 548 GLY PHE LEU ALA LEU PRO GLY SER ARG GLU ALA PRO GLY
SEQRES 14 B 548 ASN VAL GLY LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP
SEQRES 15 B 548 VAL GLN GLU ASN ILE ALA ALA PHE GLY GLY ASP PRO MET
SEQRES 16 B 548 SER VAL THR LEU PHE GLY GLU SBG ALA GLY ALA ALA SER
SEQRES 17 B 548 VAL GLY MET HIS ILE LEU SER LEU PRO SER ARG SER LEU
SEQRES 18 B 548 PHE HIS ARG ALA VAL LEU GLN SER GLY THR PRO ASN GLY
SEQRES 19 B 548 PRO TRP ALA THR VAL SER ALA GLY GLU ALA ARG ARG ARG
SEQRES 20 B 548 ALA THR LEU LEU ALA ARG LEU VAL GLY CYS PRO PRO GLY
SEQRES 21 B 548 GLY ALA GLY GLY ASN ASP THR GLU LEU ILE ALA CYS LEU
SEQRES 22 B 548 ARG THR ARG PRO ALA GLN ASP LEU VAL ASP HIS GLU TRP
SEQRES 23 B 548 HIS VAL LEU PRO GLN GLU SER ILE PHE ARG PHE SER PHE
SEQRES 24 B 548 VAL PRO VAL VAL ASP GLY ASP PHE LEU SER ASP THR PRO
SEQRES 25 B 548 GLU ALA LEU ILE ASN THR GLY ASP PHE GLN ASP LEU GLN
SEQRES 26 B 548 VAL LEU VAL GLY VAL VAL LYS ASP GLU GLY SER TYR PHE
SEQRES 27 B 548 LEU VAL TYR GLY VAL PRO GLY PHE SER LYS ASP ASN GLU
SEQRES 28 B 548 SER LEU ILE SER ARG ALA GLN PHE LEU ALA GLY VAL ARG
SEQRES 29 B 548 ILE GLY VAL PRO GLN ALA SER ASP LEU ALA ALA GLU ALA
SEQRES 30 B 548 VAL VAL LEU HIS TYR THR ASP TRP LEU HIS PRO GLU ASP
SEQRES 31 B 548 PRO THR HIS LEU ARG ASP ALA MET SER ALA VAL VAL GLY
SEQRES 32 B 548 ASP HIS ASN VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY
SEQRES 33 B 548 ARG LEU ALA ALA GLN GLY ALA ARG VAL TYR ALA TYR ILE
SEQRES 34 B 548 PHE GLU HIS ARG ALA SER THR LEU THR TRP PRO LEU TRP
SEQRES 35 B 548 MET GLY VAL PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE
SEQRES 36 B 548 GLY LEU PRO LEU ASP PRO SER LEU ASN TYR THR THR GLU
SEQRES 37 B 548 GLU ARG ILE PHE ALA GLN ARG LEU MET LYS TYR TRP THR
SEQRES 38 B 548 ASN PHE ALA ARG THR GLY ASP PRO ASN ASP PRO ARG ASP
SEQRES 39 B 548 SER LYS SER PRO GLN TRP PRO PRO TYR THR THR ALA ALA
SEQRES 40 B 548 GLN GLN TYR VAL SER LEU ASN LEU LYS PRO LEU GLU VAL
SEQRES 41 B 548 ARG ARG GLY LEU ARG ALA GLN THR CYS ALA PHE TRP ASN
SEQRES 42 B 548 ARG PHE LEU PRO LYS LEU LEU SER ALA THR ALA THR GLU
SEQRES 43 B 548 ALA PRO
MODRES 2WHQ SBG A 203 SER O-[(S)-HYDROXY(METHYL)PHOSPHORYL]-L-SERINE
MODRES 2WHQ SBG B 203 SER O-[(S)-HYDROXY(METHYL)PHOSPHORYL]-L-SERINE
HET SBG A 203 10
HET NAG A 601 14
HET NAG A 701 14
HET SBG B 203 10
HET NAG B 601 14
HET HI6 A1543 12
HET HI6 B1545 12
HET P6G A1544 19
HET PEG B1546 7
HET PGE B1547 10
HET PGE A1545 10
HET PGE B1548 10
HET PGE B1549 10
HETNAM SBG O-[(S)-HYDROXY(METHYL)PHOSPHORYL]-L-SERINE
HETNAM HI6 4-(AMINOCARBONYL)-1-[({2-[(E)-(HYDROXYIMINO)
HETNAM 2 HI6 METHYL]PYRIDINIUM-1-YL}METHOXY)METHYL]
HETNAM 3 HI6 PYRIDINIUM
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM P6G HEXAETHYLENE GLYCOL
HETNAM PGE TRIETHYLENE GLYCOL
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
FORMUL 3 SBG 2(C4 H10 N O5 P)
FORMUL 4 HI6 2(C14 H16 N4 O3 2+)
FORMUL 5 P6G C12 H26 O7
FORMUL 6 PGE 4(C6 H14 O4)
FORMUL 7 NAG 3(C8 H15 N O6)
FORMUL 8 PEG C4 H10 O3
FORMUL 9 HOH *650(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 ALA A 204 SER A 215 1 12
HELIX 10 10 SER A 215 SER A 220 1 6
HELIX 11 11 SER A 240 VAL A 255 1 16
HELIX 12 12 ASN A 265 ARG A 276 1 12
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 GLY A 342 5 8
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 GLN A 421 1 15
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 ALA A 542 1 9
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 ALA B 204 LEU B 214 1 11
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 ARG B 276 1 12
HELIX 40 40 PRO B 277 TRP B 286 1 10
HELIX 41 41 HIS B 287 LEU B 289 5 3
HELIX 42 42 THR B 311 GLY B 319 1 9
HELIX 43 43 GLY B 335 VAL B 340 1 6
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 PHE B 455 1 6
HELIX 50 50 GLY B 456 ASP B 460 5 5
HELIX 51 51 ASP B 460 ASN B 464 5 5
HELIX 52 52 THR B 466 GLY B 487 1 22
HELIX 53 53 ARG B 525 ARG B 534 1 10
HELIX 54 54 ARG B 534 ALA B 542 1 9
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 GLY A 201 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 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 GLY B 201 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 2.02
SSBOND 2 CYS A 257 CYS A 272 1555 1555 2.10
SSBOND 3 CYS A 409 CYS A 529 1555 1555 2.04
SSBOND 4 CYS B 69 CYS B 96 1555 1555 2.05
SSBOND 5 CYS B 257 CYS B 272 1555 1555 2.07
SSBOND 6 CYS B 409 CYS B 529 1555 1555 2.05
LINK C GLU A 202 N SBG A 203 1555 1555 1.33
LINK C SBG A 203 N ALA A 204 1555 1555 1.33
LINK ND2 ASN A 350 C1 NAG A 601 1555 1555 1.46
LINK ND2 ASN A 464 C1 NAG A 701 1555 1555 1.44
LINK C GLU B 202 N SBG B 203 1555 1555 1.33
LINK C SBG B 203 N ALA B 204 1555 1555 1.34
LINK ND2 ASN B 350 C1 NAG B 601 1555 1555 1.45
CISPEP 1 TYR A 105 PRO A 106 0 -0.74
CISPEP 2 TYR B 105 PRO B 106 0 3.13
CISPEP 3 SER B 497 PRO B 498 0 -7.15
SITE 1 AC1 4 SER A 347 ASN A 350 HOH A2361 HOH A2362
SITE 1 AC2 1 ASN A 464
SITE 1 AC3 5 GLY B 345 SER B 347 ASN B 350 LEU B 353
SITE 2 AC3 5 HOH B2286
SITE 1 AC4 6 TRP A 86 GLY A 121 TYR A 337 HIS A 447
SITE 2 AC4 6 TYR A 449 HOH A2123
SITE 1 AC5 8 TRP B 86 GLY B 121 TYR B 124 TYR B 337
SITE 2 AC5 8 TYR B 341 HIS B 447 TYR B 449 HOH B2084
SITE 1 AC6 9 LEU A 380 HIS A 381 GLN A 527 PHE A 535
SITE 2 AC6 9 HOH A2363 LEU B 380 HIS B 381 GLN B 527
SITE 3 AC6 9 PHE B 535
SITE 1 AC7 3 LYS B 332 ASP B 396 HOH B2190
SITE 1 AC8 3 HIS B 381 TYR B 382 ASP B 384
SITE 1 AC9 5 HIS A 381 TYR A 382 HIS A 393 THR A 528
SITE 2 AC9 5 HOH A2364
SITE 1 BC1 3 ASP B 304 GLY B 305 SER B 309
SITE 1 BC2 1 GLN B 291
CRYST1 79.550 112.320 227.060 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 0.012571 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008903 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004404 0.00000
END |