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HEADER HYDROLASE 23-AUG-06 2J3Q
TITLE TORPEDO ACETYLCHOLINESTERASE COMPLEXED WITH FLUOROPHORE
TITLE 2 THIOFLAVIN T
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYLCHOLINESTERASE;
COMPND 3 SYNONYM: ACHE, TORPEDO ACETYLCHOLINESTERASE;
COMPND 4 CHAIN: A;
COMPND 5 FRAGMENT: RESIDUES 22-564;
COMPND 6 EC: 3.1.1.7
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: TORPEDO CALIFORNICA;
SOURCE 3 ORGANISM_COMMON: PACIFIC ELECTRIC RAY
KEYWDS SERINE ESTERASE, ALTERNATIVE SPLICING,LIPOPROTEIN,
KEYWDS 2 GLYCOPROTEIN, TORPEDO ACHE, NEUROTRANSMITTER DEGRADATION,
KEYWDS 3 ANTICANCER PRODRUG CPT- 11, SYNAPSE, MEMBRANE, HYDROLASE,
KEYWDS 4 GPI-ANCHOR
EXPDTA X-RAY DIFFRACTION
AUTHOR M.HAREL,B.CUSACK,J.L.JOHNSON,I.SILMAN,J.L.SUSSMAN,
AUTHOR 2 T.L.ROSENBERRY
REVDAT 1 04-SEP-07 2J3Q 0
JRNL AUTH M.HAREL,B.CUSACK,J.L.JOHNSON,I.SILMAN,J.L.SUSSMAN,
JRNL AUTH 2 T.L.ROSENBERRY
JRNL TITL TORPEDO ACETYLCHOLINESTERASE COMPLEX WITH THE
JRNL TITL 2 FLUOROPHORE THIOFLAVIN T
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.8 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,
REMARK 3 GROSSE-KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,
REMARK 3 PANNU,READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMIM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.8
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 27.813
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.0
REMARK 3 OUTLIER CUTOFF HIGH (RMS(ABS(F))) : 3057165
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 19966
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.199
REMARK 3 FREE R VALUE : 0.257
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.9
REMARK 3 FREE R VALUE TEST SET COUNT : 1982
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.006
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.8
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.98
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.6
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2835
REMARK 3 BIN R VALUE (WORKING SET) : 0.282
REMARK 3 BIN FREE R VALUE : 0.337
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.0
REMARK 3 BIN FREE R VALUE SET COUNT : 315
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.019
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4250
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 64
REMARK 3 SOLVENT ATOMS : 85
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 64.3
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 37.1
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.61
REMARK 3 B22 (A**2) : 2.61
REMARK 3 B33 (A**2) : -5.21
REMARK 3 B12 (A**2) : 10.70
REMARK 3 B13 (A**2) : 0.000
REMARK 3 B23 (A**2) : 0.000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.30
REMARK 3 ESD FROM SIGMAA (A) : 0.45
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.0
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.4
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.55
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.3
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.4
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.84
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.24 ; 1.50
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.15 ; 2.00
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.70 ; 2.00
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.69 ; 2.50
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.301444
REMARK 3 BSOL : 12.7011
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3 GROUP 2 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 2 B-FACTOR (A**2) : NULL ; NULL
REMARK 3 GROUP 3 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 3 B-FACTOR (A**2) : NULL ; NULL
REMARK 3 GROUP 4 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 4 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 TOPOLOGY FILE 3 : ION.TOP
REMARK 3 PARAMETER FILE 4 : CARBOHYDRATE.PARAM
REMARK 3 TOPOLOGY FILE 4 : CARBOHYDRATE.TOP
REMARK 3 PARAMETER FILE 5 : THT_SKETCHER.PAR
REMARK 3 TOPOLOGY FILE 5 : THT_SKETCHER.TOP
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2J3Q COMPLIES WITH FORMAT V. 3.1, 01-AUG-2007
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY EBI ON 23-AUG-2006.
REMARK 100 THE EBI ID CODE IS EBI-29792.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-FEB-2005
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : MULTIWIRE
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 242941
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.80
REMARK 200 RESOLUTION RANGE LOW (A) : 30.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 200 DATA REDUNDANCY : 12.3
REMARK 200 R MERGE (I) : 0.14
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 17.90
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.5
REMARK 200 DATA REDUNDANCY IN SHELL : 12.0
REMARK 200 R MERGE FOR SHELL (I) : 0.61
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 4.93
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1U65
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.08
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 Y-X,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,1/3-Z
REMARK 290 6555 -X,Y-X,2/3-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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 47.61333
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 23.80667
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 23.80667
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 47.61333
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK ALSO PROVIDES 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 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 ASP A 1
REMARK 465 ASP A 2
REMARK 465 HIS A 3
REMARK 465 ASP A 538
REMARK 465 GLY A 539
REMARK 465 GLU A 540
REMARK 465 LEU A 541
REMARK 465 SER A 542
REMARK 465 SER A 543
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 CYS A 537 CA C O CB SG
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 NE2 HIS A 471 - O HOH A 2072 2.09
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 LYS A 11 13.56 -57.22
REMARK 500 LEU A 23 75.75 51.12
REMARK 500 SER A 25 -172.90 -175.96
REMARK 500 PRO A 39 45.02 -76.75
REMARK 500 PHE A 45 -15.12 82.74
REMARK 500 PRO A 53 131.46 -39.29
REMARK 500 ALA A 60 70.57 -105.44
REMARK 500 TYR A 63 151.80 -35.07
REMARK 500 SER A 91 148.06 -170.03
REMARK 500 SER A 108 58.45 34.11
REMARK 500 PHE A 155 -0.53 -140.60
REMARK 500 LEU A 158 70.09 -109.93
REMARK 500 ASN A 183 -26.85 -152.13
REMARK 500 PRO A 191 -6.13 -58.63
REMARK 500 SER A 200 -123.01 53.88
REMARK 500 SER A 215 -30.35 -131.69
REMARK 500 ARG A 220 -73.67 -86.71
REMARK 500 SER A 291 -73.93 -56.91
REMARK 500 GLU A 299 -81.14 -109.15
REMARK 500 ASN A 313 77.81 -67.66
REMARK 500 PHE A 314 147.03 -176.08
REMARK 500 THR A 317 -166.87 -161.01
REMARK 500 ASP A 380 52.71 -177.45
REMARK 500 VAL A 400 -66.20 -130.96
REMARK 500 THR A 412 29.97 -60.95
REMARK 500 PHE A 414 -14.41 -141.23
REMARK 500 ALA A 427 143.92 -39.75
REMARK 500 PRO A 433 175.69 -56.93
REMARK 500 HIS A 486 60.72 -175.30
REMARK 500 PRO A 493 160.15 -46.02
REMARK 500 GLU A 508 171.49 -53.07
REMARK 500 ARG A 515 76.30 53.91
REMARK 500 ARG A 517 30.87 37.91
REMARK 500 GLN A 526 -80.82 -114.63
REMARK 500 PHE A 527 -71.77 -43.00
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 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1542 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 264 NE2
REMARK 620 2 GLU A 268 OE1 74.5
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1543 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 326 OD1
REMARK 620 2 ASP A 392 OD2 71.6
REMARK 620 3 HOH A2065 O 76.1 73.3
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 SITE_DESCRIPTION: TFL BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 SITE_DESCRIPTION: NDG BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 SITE_DESCRIPTION: MG BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 SITE_DESCRIPTION: MG BINDING SITE FOR CHAIN A
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1ACJ RELATED DB: PDB
REMARK 900 ACETYLCHOLINESTERASE COMPLEXED WITH TACRINE
REMARK 900 RELATED ID: 1ACL RELATED DB: PDB
REMARK 900 ACETYLCHOLINESTERASE COMPLEXED WITH DECAMETHONIUM
REMARK 900 RELATED ID: 1AMN RELATED DB: PDB
REMARK 900 TRANSITION STATE ANALOG: ACETYLCHOLINESTERASE
REMARK 900 COMPLEXED WITH M-(N,N,N-TRIMETHYLAMMONIO)
REMARK 900 TRIFLUOROACETOPHENONE
REMARK 900 RELATED ID: 1AX9 RELATED DB: PDB
REMARK 900 ACETYLCHOLINESTERASE COMPLEXED WITH EDROPHONIUM,
REMARK 900 LAUE DATA
REMARK 900 RELATED ID: 1CFJ RELATED DB: PDB
REMARK 900 METHYLPHOSPHONYLATED ACETYLCHOLINESTERASE (AGED)
REMARK 900 OBTAINED BY REACTION WITH O-
REMARK 900 ISOPROPYLMETHYLPHOSPHONOFLUORIDATE (GB, SARIN)
REMARK 900 RELATED ID: 1DX6 RELATED DB: PDB
REMARK 900 STRUCTURE OF ACETYLCHOLINESTERASE COMPLEXED WITH
REMARK 900 (-)-GALANTHAMINE AT 2.3A RESOLUTION
REMARK 900 RELATED ID: 1E3Q RELATED DB: PDB
REMARK 900 TORPEDO CALIFORNICA ACETYLCHOLINESTERASE COMPLEXED
REMARK 900 WITH BW284C51
REMARK 900 RELATED ID: 1E66 RELATED DB: PDB
REMARK 900 STRUCTURE OF ACETYLCHOLINESTERASE COMPLEXED WITH
REMARK 900 (-)-HUPRINE X AT 2.1A RESOLUTION
REMARK 900 RELATED ID: 1EA5 RELATED DB: PDB
REMARK 900 NATIVE ACETYLCHOLINESTERASE (E.C. 3.1.1.7)
REMARK 900 FROM TORPEDO CALIFORNICA AT 1.8A
REMARK 900 RESOLUTION
REMARK 900 RELATED ID: 1EEA RELATED DB: PDB
REMARK 900 ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 1EVE RELATED DB: PDB
REMARK 900 THREE DIMENSIONAL STRUCTURE OF THE ANTI-
REMARK 900 ALZHEIMER DRUG, E2020 (ARICEPT), COMPLEXED
REMARK 900 WITH ITS TARGET ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 1FSS RELATED DB: PDB
REMARK 900 ACETYLCHOLINESTERASE COMPLEXED WITH FASCICULIN-II
REMARK 900 RELATED ID: 1GPK RELATED DB: PDB
REMARK 900 STRUCTURE OF ACETYLCHOLINESTERASE COMPLEXE WITH
REMARK 900 (+)-HUPERZINE A AT 2.1A RESOLUTION
REMARK 900 RELATED ID: 1GPN RELATED DB: PDB
REMARK 900 STRUCTURE OF ACETYLCHOLINESTERASE COMPLEXED WITH
REMARK 900 HUPERZINE B AT 2.35A RESOLUTION
REMARK 900 RELATED ID: 1GQR RELATED DB: PDB
REMARK 900 ACETYLCHOLINESTERASE (E.C. 3.1.1.7)
REMARK 900 COMPLEXED WITH RIVASTIGMINE
REMARK 900 RELATED ID: 1GQS RELATED DB: PDB
REMARK 900 ACETYLCHOLINESTERASE (E.C. 3.1.1.7)
REMARK 900 COMPLEXED WITH NAP
REMARK 900 RELATED ID: 1H22 RELATED DB: PDB
REMARK 900 STRUCTURE OF ACETYLCHOLINESTERASE (E.C. 3.1
REMARK 900 .1.7) COMPLEXED WITH (S,S)-(-)-BIS(10)-
REMARK 900 HUPERZINE A-LIKE INHIBITOR AT 2.15A
REMARK 900 RESOLUTION
REMARK 900 RELATED ID: 1H23 RELATED DB: PDB
REMARK 900 STRUCTURE OF ACETYLCHOLINESTERASE (E.C. 3.1
REMARK 900 .1.7) COMPLEXED WITH (S,S)-(-)-BIS(12)-
REMARK 900 HUPERZINE A-LIKE INHIBITOR AT 2.15A
REMARK 900 RESOLUTION
REMARK 900 RELATED ID: 1HBJ RELATED DB: PDB
REMARK 900 X-RAY CRYSTAL STRUCTURE OF COMPLEX BETWEEN
REMARK 900 TORPEDO CALIFORNICA ACHE AND A REVERSIBLE
REMARK 900 INHIBITOR, 4-AMINO-5-FLUORO-2-METHYL-3-
REMARK 900 (3-TRIFLUOROACETYLBENZYLTHIOMETHYL)QUINOLINE
REMARK 900 RELATED ID: 1JGA RELATED DB: PDB
REMARK 900 THEORETICAL MODEL OF THE DIISOPROPYLPHOSPHORYL-
REMARK 900 ACETYLCHOLINESTERASE COMPLEXED WITH 1,7-
REMARK 900 HEPTYLENE-BIS-N,N'-SYN-2-PYRIDINIUMALDOXIME
REMARK 900 RELATED ID: 1JGB RELATED DB: PDB
REMARK 900 THEORETICAL MODEL OF THE DIISOPROPYLPHOSPHORYL-
REMARK 900 ACETYLCHOLINESTERASE COMPLEXED WITH 1,3-
REMARK 900 PROPYLENE-BIS-N,N'-SYN-4-PYRIDINIUMALDOXIME
REMARK 900 RELATED ID: 1JJB RELATED DB: PDB
REMARK 900 A NEUTRAL MOLECULE IN CATION-BINDING SITE:
REMARK 900 SPECIFIC BINDINGOF PEG-SH TO
REMARK 900 ACETYLCHOLINESTERASE FROM TORPEDO CALIFORNICA
REMARK 900 RELATED ID: 1OCE RELATED DB: PDB
REMARK 900 ACETYLCHOLINESTERASE COMPLEXED WITH MF268
REMARK 900 RELATED ID: 1ODC RELATED DB: PDB
REMARK 900 STRUCTURE OF ACETYLCHOLINESTERASE (E.C. 3.1
REMARK 900 .1.7) COMPLEXED WITH N-4'-QUINOLYL-N'-9
REMARK 900 "-(1",2",3",4"-TETRAHYDROACRIDINYL)-1,8-
REMARK 900 DIAMINOOCTANE AT 2.2A RESOLUTION
REMARK 900 RELATED ID: 1QID RELATED DB: PDB
REMARK 900 SPECIFIC CHEMICAL AND STRUCTURAL DAMAGE AT
REMARK 900 NINE TIME POINTS (POINT A) CAUSED BY
REMARK 900 INTENSE SYNCHROTRON RADIATION TO TORPEDO
REMARK 900 CALIFORNICA ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 1QIE RELATED DB: PDB
REMARK 900 SPECIFIC CHEMICAL AND STRUCTURAL DAMAGE AT
REMARK 900 NINE TIME POINTS (POINT B) CAUSED BY
REMARK 900 INTENSE SYNCHROTRON RADIATION TO TORPEDO
REMARK 900 CALIFORNICA ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 1QIF RELATED DB: PDB
REMARK 900 SPECIFIC CHEMICAL AND STRUCTURAL DAMAGE AT
REMARK 900 NINE TIME POINTS (POINT C) CAUSED BY
REMARK 900 INTENSE SYNCHROTRON RADIATION TO TORPEDO
REMARK 900 CALIFORNICA ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 1QIG RELATED DB: PDB
REMARK 900 SPECIFIC CHEMICAL AND STRUCTURAL DAMAGE AT
REMARK 900 NINE TIME POINTS (POINT D) CAUSED BY
REMARK 900 INTENSE SYNCHROTRON RADIATION TO TORPEDO
REMARK 900 CALIFORNICA ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 1QIH RELATED DB: PDB
REMARK 900 SPECIFIC CHEMICAL AND STRUCTURAL DAMAGE AT
REMARK 900 NINE TIME POINTS (POINT E) CAUSED BY
REMARK 900 INTENSE SYNCHROTRON RADIATION TO TORPEDO
REMARK 900 CALIFORNICA ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 1QII RELATED DB: PDB
REMARK 900 SPECIFIC CHEMICAL AND STRUCTURAL DAMAGE AT
REMARK 900 NINE TIME POINTS (POINT F) CAUSED BY
REMARK 900 INTENSE SYNCHROTRON RADIATION TO TORPEDO
REMARK 900 CALIFORNICA ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 1QIJ RELATED DB: PDB
REMARK 900 SPECIFIC CHEMICAL AND STRUCTURAL DAMAGE AT
REMARK 900 NINE TIME POINTS (POINT G) CAUSED BY
REMARK 900 INTENSE SYNCHROTRON RADIATION TO TORPEDO
REMARK 900 CALIFORNICA ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 1QIK RELATED DB: PDB
REMARK 900 SPECIFIC CHEMICAL AND STRUCTURAL DAMAGE AT
REMARK 900 NINE TIME POINTS (POINT H) CAUSED BY
REMARK 900 INTENSE SYNCHROTRON RADIATION TO TORPEDO
REMARK 900 CALIFORNICA ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 1QIM RELATED DB: PDB
REMARK 900 SPECIFIC CHEMICAL AND STRUCTURAL DAMAGE AT
REMARK 900 NINE TIME POINTS (POINT I) CAUSED BY
REMARK 900 INTENSE SYNCHROTRON RADIATION TO TORPEDO
REMARK 900 CALIFORNICA ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 1QTI RELATED DB: PDB
REMARK 900 ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 1SOM RELATED DB: PDB
REMARK 900 TORPEDO CALIFORNICA ACETYLCHOLINESTERASE INHIBITED
REMARK 900 BY NERVE AGENT GD (SOMAN).
REMARK 900 RELATED ID: 1U65 RELATED DB: PDB
REMARK 900 ACHE W. CPT-11
REMARK 900 RELATED ID: 1UT6 RELATED DB: PDB
REMARK 900 STRUCTURE OF ACETYLCHOLINESTERASE
REMARK 900 (E.C. 3.1.1.7) COMPLEXED WITH N-9-(1',2',3',4
REMARK 900 '-TETRAHYDROACRIDINYL)-1,8- DIAMINOOCTANE AT
REMARK 900 2.4 ANGSTROMS RESOLUTION.
REMARK 900 RELATED ID: 1VOT RELATED DB: PDB
REMARK 900 ACETYLCHOLINESTERASE COMPLEXED WITH HUPERZINE A
REMARK 900 RELATED ID: 1VXO RELATED DB: PDB
REMARK 900 METHYLPHOSPHONYLATED ACETYLCHOLINESTERASE (AGED)
REMARK 900 OBTAINED BY REACTION WITH O-ETHYL-S-[2-[
REMARK 900 BIS(1-METHYLETHYL) AMINO]ETHYL]
REMARK 900 METHYLPHOSPHONOTHIOATE (VX)
REMARK 900 RELATED ID: 1VXR RELATED DB: PDB
REMARK 900 O-ETHYLMETHYLPHOSPHONYLATED ACETYLCHOLINESTERASE
REMARK 900 OBTAINED BY REACTION WITH O-ETHYL-S-[2-[
REMARK 900 BIS(1-METHYLETHYL) AMINO]ETHYL]
REMARK 900 METHYLPHOSPHONOTHIOATE (VX)
REMARK 900 RELATED ID: 1W4L RELATED DB: PDB
REMARK 900 COMPLEX OF TCACHE WITH BIS-ACTING
REMARK 900 GALANTHAMINE DERIVATIVE
REMARK 900 RELATED ID: 1W6R RELATED DB: PDB
REMARK 900 COMPLEX OF TCACHE WITH GALANTHAMINE DERIVATIVE
REMARK 900 RELATED ID: 1W75 RELATED DB: PDB
REMARK 900 NATIVE ORTHORHOMBIC FORM OF TORPEDO
REMARK 900 CALIFORNICA ACETYLCHOLINESTERASE (ACHE)
REMARK 900 RELATED ID: 1W76 RELATED DB: PDB
REMARK 900 ORTHORHOMBIC FORM OF TORPEDO CALIFORNICA
REMARK 900 ACETYLCHOLINESTERASE (ACHE) COMPLEXED WITH BIS-
REMARK 900 ACTING GALANTHAMINE DERIVATIVE
REMARK 900 RELATED ID: 1ZGB RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF TORPEDO
REMARK 900 CALIFORNICAACETYLCHOLINESTERASE IN COMPLEX WITH
REMARK 900 AN (R)-TACRINE(10)-HUPYRIDONE INHIBITOR.
REMARK 900 RELATED ID: 1ZGC RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF TORPEDO
REMARK 900 CALIFORNICAACETYLCHOLINESTERASE IN COMPLEX WITH
REMARK 900 AN (RS)-TACRINE(10)-HUPYRIDONE INHIBITOR.
REMARK 900 RELATED ID: 2ACE RELATED DB: PDB
REMARK 900 NATIVE ACETYLCHOLINESTERASE FROM TORPEDO
REMARK 900 CALIFORNICA
REMARK 900 RELATED ID: 2ACK RELATED DB: PDB
REMARK 900 ACETYLCHOLINESTERASE COMPLEXED WITH EDROPHONIUM,
REMARK 900 MONOCHROMATIC DATA
REMARK 900 RELATED ID: 2C4H RELATED DB: PDB
REMARK 900 TORPEDO CALIFORNICA ACETYLCHOLINESTERASE IN
REMARK 900 COMPLEX WITH 500MM ACETYLTHIOCHOLINE
REMARK 900 RELATED ID: 2C58 RELATED DB: PDB
REMARK 900 TORPEDO CALIFORNICA ACETYLCHOLINESTERASE IN
REMARK 900 COMPLEX WITH 20MM ACETYLTHIOCHOLINE
REMARK 900 RELATED ID: 2C5F RELATED DB: PDB
REMARK 900 TORPEDO CALIFORNICA ACETYLCHOLINESTERASE IN
REMARK 900 COMPLEX WITH A NON HYDROLYSABLE SUBSTRATE
REMARK 900 ANALOGUE, 4-OXO-N,N,N-TRIMETHYLAMMONIUM
REMARK 900 RELATED ID: 2C5G RELATED DB: PDB
REMARK 900 TORPEDO CALIFORNICA ACETYLCHOLINESTERASE IN
REMARK 900 COMPLEX WITH 20MM THIOCHOLINE
REMARK 900 RELATED ID: 2CEK RELATED DB: PDB
REMARK 900 CONFORMATIONAL FLEXIBILITY IN THE PERIPHERAL
REMARK 900 SITE OF TORPEDO CALIFORNICA ACETYLCHOLINESTERASE
REMARK 900 REVEALED BY THE COMPLEX STRUCTURE WITH A
REMARK 900 BIFUNCTIONAL INHIBITOR
REMARK 900 RELATED ID: 2CKM RELATED DB: PDB
REMARK 900 TORPEDO CALIFORNICA ACETYLCHOLINESTERASE COMPLEXED
REMARK 900 WITH ALKYLENE-LINKED BIS-TACRINE DIMER
REMARK 900 (7 CARBON LINKER)
REMARK 900 RELATED ID: 2CMF RELATED DB: PDB
REMARK 900 TORPEDO CALIFORNICA ACETYLCHOLINESTERASE COMPLEXED
REMARK 900 WITH ALKYLENE-LINKED BIS-TACRINE DIMER
REMARK 900 (5 CARBON LINKER)
REMARK 900 RELATED ID: 2DFP RELATED DB: PDB
REMARK 900 X-RAY STRUCTURE OF AGED DI-ISOPROPYL-
REMARK 900 PHOSPHORO-FLUORIDATE (DFP) BOUND TO
REMARK 900 ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 2J3D RELATED DB: PDB
REMARK 900 NATIVE MONOCLINIC FORM OF TORPEDO
REMARK 900 ACETYLCHOLINESTERASE
REMARK 900 RELATED ID: 3ACE RELATED DB: PDB
REMARK 900 THEORETICAL MODEL OF (R)-E2020 BOUND
REMARK 900 ACETYLCHOLINESTERASE COMPLEX, 3 STRUCTURES
REMARK 900 RELATED ID: 4ACE RELATED DB: PDB
REMARK 900 THEORETICAL MODEL OF (S)-E2020 BOUND
REMARK 900 ACETYLCHOLINESTERASE COMPLEX, 3 STRUCTURES
DBREF 2J3Q A 1 543 UNP P04058 ACES_TORCA 22 564
SEQRES 1 A 543 ASP ASP HIS SER GLU LEU LEU VAL ASN THR LYS SER GLY
SEQRES 2 A 543 LYS VAL MET GLY THR ARG VAL PRO VAL LEU SER SER HIS
SEQRES 3 A 543 ILE SER ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO PRO
SEQRES 4 A 543 VAL GLY ASN MET ARG PHE ARG ARG PRO GLU PRO LYS LYS
SEQRES 5 A 543 PRO TRP SER GLY VAL TRP ASN ALA SER THR TYR PRO ASN
SEQRES 6 A 543 ASN CYS GLN GLN TYR VAL ASP GLU GLN PHE PRO GLY PHE
SEQRES 7 A 543 SER GLY SER GLU MET TRP ASN PRO ASN ARG GLU MET SER
SEQRES 8 A 543 GLU ASP CYS LEU TYR LEU ASN ILE TRP VAL PRO SER PRO
SEQRES 9 A 543 ARG PRO LYS SER THR THR VAL MET VAL TRP ILE TYR GLY
SEQRES 10 A 543 GLY GLY PHE TYR SER GLY SER SER THR LEU ASP VAL TYR
SEQRES 11 A 543 ASN GLY LYS TYR LEU ALA TYR THR GLU GLU VAL VAL LEU
SEQRES 12 A 543 VAL SER LEU SER TYR ARG VAL GLY ALA PHE GLY PHE LEU
SEQRES 13 A 543 ALA LEU HIS GLY SER GLN GLU ALA PRO GLY ASN VAL GLY
SEQRES 14 A 543 LEU LEU ASP GLN ARG MET ALA LEU GLN TRP VAL HIS ASP
SEQRES 15 A 543 ASN ILE GLN PHE PHE GLY GLY ASP PRO LYS THR VAL THR
SEQRES 16 A 543 ILE PHE GLY GLU SER ALA GLY GLY ALA SER VAL GLY MET
SEQRES 17 A 543 HIS ILE LEU SER PRO GLY SER ARG ASP LEU PHE ARG ARG
SEQRES 18 A 543 ALA ILE LEU GLN SER GLY SER PRO ASN CYS PRO TRP ALA
SEQRES 19 A 543 SER VAL SER VAL ALA GLU GLY ARG ARG ARG ALA VAL GLU
SEQRES 20 A 543 LEU GLY ARG ASN LEU ASN CYS ASN LEU ASN SER ASP GLU
SEQRES 21 A 543 GLU LEU ILE HIS CYS LEU ARG GLU LYS LYS PRO GLN GLU
SEQRES 22 A 543 LEU ILE ASP VAL GLU TRP ASN VAL LEU PRO PHE ASP SER
SEQRES 23 A 543 ILE PHE ARG PHE SER PHE VAL PRO VAL ILE ASP GLY GLU
SEQRES 24 A 543 PHE PHE PRO THR SER LEU GLU SER MET LEU ASN SER GLY
SEQRES 25 A 543 ASN PHE LYS LYS THR GLN ILE LEU LEU GLY VAL ASN LYS
SEQRES 26 A 543 ASP GLU GLY SER PHE PHE LEU LEU TYR GLY ALA PRO GLY
SEQRES 27 A 543 PHE SER LYS ASP SER GLU SER LYS ILE SER ARG GLU ASP
SEQRES 28 A 543 PHE MET SER GLY VAL LYS LEU SER VAL PRO HIS ALA ASN
SEQRES 29 A 543 ASP LEU GLY LEU ASP ALA VAL THR LEU GLN TYR THR ASP
SEQRES 30 A 543 TRP MET ASP ASP ASN ASN GLY ILE LYS ASN ARG ASP GLY
SEQRES 31 A 543 LEU ASP ASP ILE VAL GLY ASP HIS ASN VAL ILE CYS PRO
SEQRES 32 A 543 LEU MET HIS PHE VAL ASN LYS TYR THR LYS PHE GLY ASN
SEQRES 33 A 543 GLY THR TYR LEU TYR PHE PHE ASN HIS ARG ALA SER ASN
SEQRES 34 A 543 LEU VAL TRP PRO GLU TRP MET GLY VAL ILE HIS GLY TYR
SEQRES 35 A 543 GLU ILE GLU PHE VAL PHE GLY LEU PRO LEU VAL LYS GLU
SEQRES 36 A 543 LEU ASN TYR THR ALA GLU GLU GLU ALA LEU SER ARG ARG
SEQRES 37 A 543 ILE MET HIS TYR TRP ALA THR PHE ALA LYS THR GLY ASN
SEQRES 38 A 543 PRO ASN GLU PRO HIS SER GLN GLU SER LYS TRP PRO LEU
SEQRES 39 A 543 PHE THR THR LYS GLU GLN LYS PHE ILE ASP LEU ASN THR
SEQRES 40 A 543 GLU PRO MET LYS VAL HIS GLN ARG LEU ARG VAL GLN MET
SEQRES 41 A 543 CYS VAL PHE TRP ASN GLN PHE LEU PRO LYS LEU LEU ASN
SEQRES 42 A 543 ALA THR ALA CYS ASP GLY GLU LEU SER SER
HET TFL A1538 20
HET NAG A1539 14
HET NAG A1540 14
HET NDG A1541 14
HET MG A1542 1
HET MG A1543 1
HETNAM TFL 2-[4-(DIMETHYLAMINO)PHENYL]-6-HYDROXY-3-
HETNAM 2 TFL METHYL-1,3-BENZOTHIAZOL-3-IUM
HETNAM MG MAGNESIUM ION
HETNAM NDG 2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETSYN NAG NAG
FORMUL 2 TFL C16 H17 N2 O S
FORMUL 3 MG 2(MG 2+)
FORMUL 4 NDG C8 H15 N O6
FORMUL 5 NAG 2(C8 H15 N O6)
FORMUL 6 HOH *85(H2 O1)
HELIX 1 1 VAL A 40 ARG A 44 5 5
HELIX 2 2 PHE A 78 MET A 83 1 6
HELIX 3 3 LEU A 127 ASN A 131 5 5
HELIX 4 4 GLY A 132 GLU A 140 1 9
HELIX 5 5 GLY A 151 LEU A 156 1 6
HELIX 6 6 ASN A 167 ASP A 182 1 16
HELIX 7 7 SER A 200 SER A 212 1 13
HELIX 8 8 SER A 212 ASP A 217 1 6
HELIX 9 9 VAL A 238 ASN A 251 1 14
HELIX 10 10 SER A 258 LYS A 269 1 12
HELIX 11 11 LYS A 270 ASP A 276 1 7
HELIX 12 12 VAL A 277 LEU A 282 5 6
HELIX 13 13 SER A 304 GLY A 312 1 9
HELIX 14 14 GLY A 328 ALA A 336 1 9
HELIX 15 15 SER A 348 VAL A 360 1 13
HELIX 16 16 ASN A 364 THR A 376 1 13
HELIX 17 17 ASN A 383 VAL A 400 1 18
HELIX 18 18 VAL A 400 THR A 412 1 13
HELIX 19 19 GLU A 443 PHE A 448 1 6
HELIX 20 20 GLY A 449 VAL A 453 5 5
HELIX 21 21 THR A 459 GLY A 480 1 22
HELIX 22 22 ARG A 517 GLN A 526 1 10
HELIX 23 23 GLN A 526 THR A 535 1 10
SHEET 1 AA 3 LEU A 7 THR A 10 0
SHEET 2 AA 3 GLY A 13 MET A 16 -1 O GLY A 13 N THR A 10
SHEET 3 AA 3 VAL A 57 ASN A 59 1 O TRP A 58 N MET A 16
SHEET 1 AB11 THR A 18 PRO A 21 0
SHEET 2 AB11 HIS A 26 PRO A 34 -1 O ILE A 27 N VAL A 20
SHEET 3 AB11 TYR A 96 VAL A 101 -1 O LEU A 97 N ILE A 33
SHEET 4 AB11 VAL A 142 SER A 145 -1 O LEU A 143 N TRP A 100
SHEET 5 AB11 THR A 109 ILE A 115 1 O THR A 110 N VAL A 142
SHEET 6 AB11 GLY A 189 GLU A 199 1 N ASP A 190 O THR A 109
SHEET 7 AB11 ARG A 221 GLN A 225 1 O ARG A 221 N ILE A 196
SHEET 8 AB11 ILE A 319 ASN A 324 1 O LEU A 320 N LEU A 224
SHEET 9 AB11 THR A 418 PHE A 423 1 O TYR A 419 N LEU A 321
SHEET 10 AB11 LYS A 501 LEU A 505 1 O ILE A 503 N PHE A 422
SHEET 11 AB11 VAL A 512 GLN A 514 -1 O HIS A 513 N PHE A 502
SHEET 1 AC 2 VAL A 236 SER A 237 0
SHEET 2 AC 2 VAL A 295 ILE A 296 1 N ILE A 296 O VAL A 236
SSBOND 1 CYS A 67 CYS A 94 1555 1555 2.03
SSBOND 2 CYS A 254 CYS A 265 1555 1555 2.02
SSBOND 3 CYS A 402 CYS A 521 1555 1555 2.05
LINK ND2 ASN A 59 C1 NAG A1539 1555 1555 1.46
LINK ND2 ASN A 416 C1 NAG A1540 1555 1555 1.45
LINK ND2 ASN A 457 C1 NDG A1541 1555 1555 1.46
LINK MG MG A1542 NE2 HIS A 264 1555 1555 2.61
LINK MG MG A1542 OE1 GLU A 268 1555 1555 2.21
LINK MG MG A1543 O HOH A2065 1555 1555 2.34
LINK MG MG A1543 OD2 ASP A 392 1555 1555 2.30
LINK MG MG A1543 OD1 ASP A 326 1555 1555 2.44
CISPEP 1 SER A 103 PRO A 104 0 0.04
SITE 1 AC1 7 TYR A 70 TYR A 121 TRP A 279 PHE A 330
SITE 2 AC1 7 TYR A 334 HOH A2014 HOH A2052
SITE 1 AC2 4 ASN A 59 SER A 61 HOH A2080 HOH A2082
SITE 1 AC3 3 ASN A 416 HOH A2083 HOH A2084
SITE 1 AC4 3 GLU A 455 ASN A 457 HOH A2085
SITE 1 AC5 3 HIS A 181 HIS A 264 GLU A 268
SITE 1 AC6 3 ASP A 326 ASP A 392 HOH A2065
CRYST1 139.440 139.440 71.420 90.00 90.00 120.00 P 32 2 1 6
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 0.007172 0.004140 0.000000 0.00000
SCALE2 0.000000 0.008281 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014002 0.00000
TER 4251 CYS A 537
MASTER 581 0 6 23 16 0 7 6 4399 1 78 42
END |