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HEADER HYDROLASE 28-SEP-09 2WU3
TITLE CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE IN COMPLEX
TITLE 2 WITH FENAMIPHOS AND 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 EC: 3.1.1.7;
COMPND 6 ENGINEERED: YES;
COMPND 7 OTHER_DETAILS: FENAMIPHOS COVALENTLY BOUND TO SER203
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_VECTOR: PCDNA3.1
KEYWDS ACETYLCHOLINESTERASE, ALTERNATIVE SPLICING, FENAMIPHOS,
KEYWDS 2 GLYCOPROTEIN, HYDROLASE, MEMBRANE, NEUROTRANSMITTER
KEYWDS 3 DEGRADATION, SERINE ESTERASE, SYNAPSE, HI-6
EXPDTA X-RAY DIFFRACTION
AUTHOR A.HORNBERG,E.ARTURSSON,R.WARME,Y.-P.PANG,F.EKSTROM
REVDAT 1 20-OCT-09 2WU3 0
JRNL AUTH A.HORNBERG,E.ARTURSSON,R.WARME,Y.-P.PANG,F.EKSTROM
JRNL TITL CRYSTAL STRUCTURES OF OXIME-BOUND FENAMIPHOS-
JRNL TITL 2 ACETYLCHOLINESTERASES: REACTIVATION INVOLVING
JRNL TITL 3 FLIPPING OF THE HIS447 RING TO FORM A REACTIVE
JRNL TITL 4 GLU334-HIS447-OXIME TRIAD.
JRNL REF BIOCHEM.PHARM. 2009
JRNL REFN ESSN 1873-2968
JRNL PMID 19732756
JRNL DOI 10.1016/J.BCP.2009.08.027
REMARK 2
REMARK 2 RESOLUTION. 2.70 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) : 2.700
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.024
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.91
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.99
REMARK 3 NUMBER OF REFLECTIONS : 55778
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.1723
REMARK 3 R VALUE (WORKING SET) : 0.1712
REMARK 3 FREE R VALUE : 0.2260
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.0
REMARK 3 FREE R VALUE TEST SET COUNT : 1098
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 29.0254 - 5.3899 1.00 7153 141 0.1579 0.1877
REMARK 3 2 5.3899 - 4.2825 1.00 6886 133 0.1255 0.1717
REMARK 3 3 4.2825 - 3.7425 1.00 6821 133 0.1375 0.2065
REMARK 3 4 3.7425 - 3.4009 1.00 6798 148 0.1570 0.2108
REMARK 3 5 3.4009 - 3.1574 1.00 6788 116 0.1807 0.2277
REMARK 3 6 3.1574 - 2.9715 1.00 6766 157 0.1998 0.2861
REMARK 3 7 2.9715 - 2.8228 1.00 6715 136 0.2255 0.2923
REMARK 3 8 2.8228 - 2.7000 1.00 6753 134 0.2619 0.3379
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 : 0.307
REMARK 3 B_SOL : 45.342
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.35
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.86
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 52.16
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 53.21
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.9782
REMARK 3 B22 (A**2) : -0.4190
REMARK 3 B33 (A**2) : 1.3972
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 : 0.011 8770
REMARK 3 ANGLE : 1.395 11967
REMARK 3 CHIRALITY : 0.209 1285
REMARK 3 PLANARITY : 0.007 1572
REMARK 3 DIHEDRAL : 19.703 3104
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A
REMARK 3 ORIGIN FOR THE GROUP (A): 27.0899 11.9506 16.4087
REMARK 3 T TENSOR
REMARK 3 T11: 0.1411 T22: 0.1136
REMARK 3 T33: 0.1497 T12: -0.0143
REMARK 3 T13: 0.0025 T23: 0.0243
REMARK 3 L TENSOR
REMARK 3 L11: 0.5119 L22: 0.6943
REMARK 3 L33: 1.3268 L12: -0.0894
REMARK 3 L13: 0.1404 L23: -0.2203
REMARK 3 S TENSOR
REMARK 3 S11: -0.0420 S12: 0.0080 S13: 0.0144
REMARK 3 S21: 0.0282 S22: 0.0337 S23: -0.0164
REMARK 3 S31: 0.1219 S32: -0.0322 S33: 0.0028
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN B
REMARK 3 ORIGIN FOR THE GROUP (A): 7.6714 4.7588 -40.5758
REMARK 3 T TENSOR
REMARK 3 T11: 0.1537 T22: 0.1421
REMARK 3 T33: 0.1515 T12: -0.0070
REMARK 3 T13: -0.0496 T23: -0.0514
REMARK 3 L TENSOR
REMARK 3 L11: 0.4161 L22: 0.6305
REMARK 3 L33: 1.8289 L12: 0.0584
REMARK 3 L13: 0.2470 L23: 0.1268
REMARK 3 S TENSOR
REMARK 3 S11: 0.1346 S12: 0.0633 S13: -0.0386
REMARK 3 S21: 0.0263 S22: -0.0813 S23: 0.0545
REMARK 3 S31: 0.2281 S32: 0.0385 S33: -0.0549
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 2WU3 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 29-SEP-09.
REMARK 100 THE PDBE ID CODE IS EBI-41273.
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 : I911-5
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.90736
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
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 : 55859
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.70
REMARK 200 RESOLUTION RANGE LOW (A) : 29.79
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 7.4
REMARK 200 R MERGE (I) : 0.08
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.85
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.5
REMARK 200 R MERGE FOR SHELL (I) : 0.44
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CCP4
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): 3.8
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 28% PEG750MME, 0.1M HEPES PH7.0
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 39.38000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 113.85000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 55.61500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 113.85000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 39.38000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 55.61500
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: 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 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 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 ALA B 544
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 GLU B 268 CG CD OE1 OE2
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 ALA B 542 N ASP B 544 2.13
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 CYS A 96 CB CYS A 96 SG -0.141
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: 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 CYS A 96 N - CA - CB ANGL. DEV. = -9.2 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 GLU A 4 177.51 -46.05
REMARK 500 PHE A 47 -15.60 75.77
REMARK 500 SER A 93 146.39 -175.45
REMARK 500 CYS A 96 -27.81 -151.81
REMARK 500 ALA A 167 67.92 -159.66
REMARK 500 ASN A 170 15.64 58.52
REMARK 500 VAL A 303 91.16 -69.03
REMARK 500 ASP A 306 -83.40 -143.93
REMARK 500 THR A 318 -52.57 -129.58
REMARK 500 ASP A 333 69.30 -107.89
REMARK 500 ARG A 493 -78.41 -62.73
REMARK 500 ASP A 494 84.77 -68.43
REMARK 500 SER A 541 52.08 143.19
REMARK 500 ALA A 544 -23.02 174.04
REMARK 500 THR A 545 -119.19 -72.72
REMARK 500 ALA B 62 64.00 -119.18
REMARK 500 CYS B 96 13.81 -144.64
REMARK 500 ASP B 306 -79.67 -119.11
REMARK 500 ASP B 323 50.09 -96.46
REMARK 500 ASN B 350 -138.80 -91.70
REMARK 500 VAL B 367 61.50 -117.05
REMARK 500 VAL B 407 -66.58 -122.14
REMARK 500 HIS B 447 121.79 -37.17
REMARK 500 ASP B 494 99.69 137.24
REMARK 500 SER B 495 -170.77 -69.39
REMARK 500 LYS B 496 106.54 38.07
REMARK 500 SER B 497 -56.72 -125.51
REMARK 500 LEU B 518 129.55 -34.98
REMARK 500 ARG B 525 63.11 35.99
REMARK 500 SER B 541 43.20 -67.32
REMARK 500 ALA B 542 46.41 177.26
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 ASP A 95 CYS A 96 -133.74
REMARK 500 LEU A 540 SER A 541 -115.68
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 O-{(S)-ETHOXY[(1-METHYLETHYL)AMINO] PHOSPHORYL}-L-SERINE
REMARK 600 (SXE): MODIFIED SER203
REMARK 600 N-ACETYL-D-GLUCOSAMINE (NAG): COVALENTLY BOUND TO ASN
REMARK 600 RESIDUES
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 A 601
REMARK 610 HI6 B 601
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HI6 A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HI6 B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P6G C 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO3 D 951
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO3 D 952
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: 1Q83 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE MOUSE
REMARK 900 ACETYLCHOLINESTERASE-TZ2PA6SYN COMPLEX
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: 2WLS RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MUS MUSCULUS
REMARK 900 ACETYLCHOLINESTERASE IN COMPLEX WITH AMTS13
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: 2C0P RELATED DB: PDB
REMARK 900 AGED FORM OF MOUSE ACETYLCHOLINESTERASE
REMARK 900 INHIBITED BY TABUN
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: 2WHR RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ACETYLCHOLINESTERASE IN
REMARK 900 COMPLEX WITH K027
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: 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: 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: 2WU4 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE
REMARK 900 IN COMPLEX WITH FENAMIPHOS AND ORTHO-7
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 STRUCTURE STARTS AT RESIDUE 32 AND ENDS AT RESIDUE 574
DBREF 2WU3 A 1 543 UNP P21836 ACES_MOUSE 32 574
DBREF 2WU3 A 544 548 PDB 2WU3 2WU3 544 548
DBREF 2WU3 B 1 543 UNP P21836 ACES_MOUSE 32 574
DBREF 2WU3 B 544 548 PDB 2WU3 2WU3 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 SXE 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 SXE 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 2WU3 SXE A 203 SER MODIFIED SERINE
MODRES 2WU3 SXE B 203 SER MODIFIED SERINE
HET SXE A 203 30
HET HI6 A 601 18
HET SXE B 203 30
HET HI6 B 601 18
HET NAG C 601 14
HET NAG C 701 14
HET P6G C 901 19
HET CO3 D 951 4
HET CO3 D 952 4
HETNAM HI6 4-(AMINOCARBONYL)-1-[({2-[(E)-(HYDROXYIMINO)
HETNAM 2 HI6 METHYL]PYRIDINIUM-1-YL}METHOXY)METHYL]
HETNAM 3 HI6 PYRIDINIUM
HETNAM P6G HEXAETHYLENE GLYCOL
HETNAM CO3 CARBONATE ION
HETNAM SXE O-{(S)-ETHOXY[(1-METHYLETHYL)AMINO]
HETNAM 2 SXE PHOSPHORYL}-L-SERINE
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETSYN HI6 1-(2-HYDROXY-IMINOMETHYLPYRIDINIUM)-1-(4-
HETSYN 2 HI6 CARBOXYAMINO)-PYRIDINIUM DIMETHYLETHER
HETSYN P6G POLYETHYLENE GLYCOL PEG400
HETSYN NAG NAG
FORMUL 3 HI6 2(C14 H16 N4 O3 2+)
FORMUL 4 P6G C12 H26 O7
FORMUL 5 CO3 2(C O3 2-)
FORMUL 6 SXE 2(C8 H19 N2 O5 P)
FORMUL 7 NAG 2(C8 H15 N O6)
FORMUL 8 HOH *291(H2 O)
HELIX 1 1 ASP A 5 LEU A 9 5 5
HELIX 2 2 THR A 83 ASN A 87 5 5
HELIX 3 3 LEU A 130 ASP A 134 5 5
HELIX 4 4 ARG A 136 GLU A 142 1 7
HELIX 5 5 LEU A 173 ILE A 187 1 15
HELIX 6 6 ALA A 188 PHE A 190 5 3
HELIX 7 7 SER A 215 SER A 220 1 6
HELIX 8 8 GLU A 243 VAL A 255 1 13
HELIX 9 9 ASN A 265 ARG A 276 1 12
HELIX 10 10 PRO A 277 TRP A 286 1 10
HELIX 11 11 HIS A 287 LEU A 289 5 3
HELIX 12 12 THR A 311 ASN A 317 1 7
HELIX 13 13 SER A 355 ALA A 361 1 7
HELIX 14 14 SER A 371 THR A 383 1 13
HELIX 15 15 ASP A 390 VAL A 402 1 13
HELIX 16 16 VAL A 407 ALA A 415 1 9
HELIX 17 17 GLU A 450 PHE A 455 1 6
HELIX 18 18 ASP A 460 ASN A 464 5 5
HELIX 19 19 THR A 466 THR A 486 1 21
HELIX 20 20 ARG A 525 ARG A 534 1 10
HELIX 21 21 ARG A 534 LEU A 539 1 6
HELIX 22 22 THR B 83 ASN B 87 5 5
HELIX 23 23 LEU B 130 ASP B 134 5 5
HELIX 24 24 ARG B 136 GLU B 142 1 7
HELIX 25 25 LEU B 173 ILE B 187 1 15
HELIX 26 26 ALA B 188 PHE B 190 5 3
HELIX 27 27 SER B 215 SER B 220 1 6
HELIX 28 28 GLU B 243 VAL B 255 1 13
HELIX 29 29 ASN B 265 ARG B 276 1 12
HELIX 30 30 PRO B 277 TRP B 286 1 10
HELIX 31 31 HIS B 287 LEU B 289 5 3
HELIX 32 32 THR B 311 THR B 318 1 8
HELIX 33 33 SER B 355 ALA B 361 1 7
HELIX 34 34 SER B 371 THR B 383 1 13
HELIX 35 35 ASP B 390 VAL B 402 1 13
HELIX 36 36 VAL B 407 ALA B 415 1 9
HELIX 37 37 GLU B 450 PHE B 455 1 6
HELIX 38 38 ASP B 460 ASN B 464 5 5
HELIX 39 39 THR B 466 THR B 486 1 21
HELIX 40 40 ARG B 525 ARG B 534 1 10
HELIX 41 41 ARG B 534 SER B 541 1 8
SHEET 1 AA 2 LEU A 17 ARG A 18 0
SHEET 2 AA 2 LEU A 60 ASP A 61 1 O LEU A 60 N ARG A 18
SHEET 1 AB11 ARG A 21 LEU A 22 0
SHEET 2 AB11 VAL A 29 PHE A 32 -1 O VAL A 29 N LEU A 22
SHEET 3 AB11 LEU A 99 PRO A 104 -1 O VAL A 101 N PHE A 32
SHEET 4 AB11 VAL A 145 MET A 149 -1 O LEU A 146 N TRP A 102
SHEET 5 AB11 VAL A 114 TRP A 117 1 O LEU A 115 N VAL A 147
SHEET 6 AB11 VAL A 197 PHE A 200 1 O THR A 198 N ILE A 116
SHEET 7 AB11 ARG A 224 VAL A 226 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 TYR A 510 LEU A 513 1 O VAL A 511 N ILE A 429
SHEET 11 AB11 GLU A 519 ARG A 521 -1 O GLU A 519 N SER A 512
SHEET 1 AC 2 VAL A 68 CYS A 69 0
SHEET 2 AC 2 LEU A 92 SER A 93 1 N SER A 93 O VAL A 68
SHEET 1 BA 2 LEU B 17 ARG B 18 0
SHEET 2 BA 2 LEU B 60 ASP B 61 1 O LEU B 60 N ARG B 18
SHEET 1 BB11 ARG B 21 LEU B 22 0
SHEET 2 BB11 VAL B 29 PHE B 32 -1 O VAL B 29 N LEU B 22
SHEET 3 BB11 LEU B 99 PRO B 104 -1 O VAL B 101 N PHE B 32
SHEET 4 BB11 VAL B 145 MET B 149 -1 O LEU B 146 N TRP B 102
SHEET 5 BB11 VAL B 114 TRP B 117 1 O LEU B 115 N VAL B 147
SHEET 6 BB11 VAL B 197 PHE B 200 1 O THR B 198 N ILE B 116
SHEET 7 BB11 ARG B 224 VAL B 226 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 TYR B 510 LEU B 513 1 O VAL B 511 N ILE B 429
SHEET 11 BB11 GLU B 519 ARG B 521 -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
SSBOND 1 CYS A 69 CYS A 96 1555 1555 1.99
SSBOND 2 CYS A 257 CYS A 272 1555 1555 2.07
SSBOND 3 CYS A 409 CYS A 529 1555 1555 2.04
SSBOND 4 CYS B 69 CYS B 96 1555 1555 2.03
SSBOND 5 CYS B 257 CYS B 272 1555 1555 2.05
SSBOND 6 CYS B 409 CYS B 529 1555 1555 2.04
LINK C GLU A 202 N ASXE A 203 1555 1555 1.34
LINK C GLU A 202 N BSXE A 203 1555 1555 1.34
LINK C ASXE A 203 N ALA A 204 1555 1555 1.33
LINK C BSXE A 203 N ALA A 204 1555 1555 1.33
LINK C GLU B 202 N BSXE B 203 1555 1555 1.34
LINK C GLU B 202 N ASXE B 203 1555 1555 1.34
LINK C BSXE B 203 N ALA B 204 1555 1555 1.33
LINK C ASXE B 203 N ALA B 204 1555 1555 1.33
LINK C1 NAG C 701 ND2 ASN A 464 1555 1555 1.48
CISPEP 1 TYR A 105 PRO A 106 0 0.66
CISPEP 2 TYR B 105 PRO B 106 0 7.07
CISPEP 3 SER B 497 PRO B 498 0 -8.03
SITE 1 AC1 10 ASP A 74 TYR A 124 SXE A 203 GLU A 285
SITE 2 AC1 10 TRP A 286 ARG A 296 PHE A 297 SER A 298
SITE 3 AC1 10 TYR A 337 TYR A 341
SITE 1 AC2 9 TYR B 124 SXE B 203 GLU B 285 TRP B 286
SITE 2 AC2 9 PHE B 297 SER B 298 TYR B 337 TYR B 341
SITE 3 AC2 9 HOH B2068
SITE 1 AC3 4 ASN A 350 LEU A 353 HOH C2001 HOH C2002
SITE 1 AC4 1 ASN A 464
SITE 1 AC5 11 LEU A 380 HIS A 381 GLN A 527 PHE A 535
SITE 2 AC5 11 ALA B 377 LEU B 380 HIS B 381 GLN B 527
SITE 3 AC5 11 PHE B 535 HOH C2003 HOH C2004
SITE 1 AC6 1 TRP A 286
SITE 1 AC7 2 TRP B 286 HIS B 287
CRYST1 78.760 111.230 227.700 90.00 90.00 90.00 P 21 21 21 1
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 0.012697 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008990 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004392 0.00000
END |