2J3D-pdb | HEADER HYDROLASE 20-AUG-06 2J3D
TITLE NATIVE MONOCLINIC FORM OF TORPEDO ACETYLCHOLINESTERASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYLCHOLINESTERASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 22-564;
COMPND 5 SYNONYM: ACHE;
COMPND 6 EC: 3.1.1.7
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 ORGANISM_SCIENTIFIC: TORPEDO CALIFORNICA;
SOURCE 4 ORGANISM_COMMON: PACIFIC ELECTRIC RAY
KEYWDS HYDROLASE, ALZHEIMER'S DISEASE, ALTERNATIVE SPLICING,
KEYWDS 2 NERVE, MUSCLE, NEUROTRANSMITTER DEGRADATION,
KEYWDS 3 CHOLINESTERASE, SYNAPSE, GPI-ANCHOR, LIPOPROTEIN,
KEYWDS 4 GLYCOPROTEIN, SERINE HYDROLASE, SERINE ESTERASE, MEMBRANE,
KEYWDS 5 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.HAREL,J.L.SUSSMAN
REVDAT 1 24-JUN-08 2J3D 0
JRNL AUTH M.HAREL,J.L.SUSSMAN
JRNL TITL NATIVE MONOCLINIC FORM OF TORPEDO
JRNL TITL 2 ACETYLCHOLINESTERASE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.6 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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.6
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.8
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.0
REMARK 3 OUTLIER CUTOFF HIGH (RMS(ABS(F))) : 4121275
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 3 NUMBER OF REFLECTIONS : 27514
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) : 0.2170
REMARK 3 FREE R VALUE : 0.2606
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.0
REMARK 3 FREE R VALUE TEST SET COUNT : 2752
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.005
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) : 2.6
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.76
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.0
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3958
REMARK 3 BIN R VALUE (WORKING SET) : 0.315
REMARK 3 BIN FREE R VALUE : 0.354
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.0
REMARK 3 BIN FREE R VALUE SET COUNT : 440
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.017
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4245
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 47
REMARK 3 SOLVENT ATOMS : 98
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 23.8
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.9
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.92
REMARK 3 B22 (A**2) : 2.77
REMARK 3 B33 (A**2) : -5.69
REMARK 3 B12 (A**2) : 0.000
REMARK 3 B13 (A**2) : -0.81
REMARK 3 B23 (A**2) : 0.000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.32
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) : 0.39
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.52
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) : 22.6
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.88
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NONE
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.21 ; 1.5
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.04 ; 2.0
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.76 ; 2.0
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.72 ; 2.5
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.336285
REMARK 3 BSOL : 18.4348
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
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2J3D COMPLIES WITH FORMAT V. 3.1, 01-AUG-2007
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY EBI ON 21-AUG-2006.
REMARK 100 THE EBI ID CODE IS EBI-29743.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-JUL-2006
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
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 : 27043
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.60
REMARK 200 RESOLUTION RANGE LOW (A) : 33.80
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.4
REMARK 200 DATA REDUNDANCY : 3.1
REMARK 200 R MERGE (I) : 0.13
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 8.90
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.70
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.1
REMARK 200 R MERGE FOR SHELL (I) : 0.44
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.60
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 1EA5
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 64.7
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.5
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 64.37000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 52.74500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 64.37000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 52.74500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
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 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 CYS A 537
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 ALA A 536 CA C O CB
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500
REMARK 500 CG2 THR A 535 CG2 THR A 535 2555 2.20
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 PRO A 38 108.06 -51.18
REMARK 500 PRO A 39 55.28 -67.16
REMARK 500 ASN A 42 -8.60 -54.84
REMARK 500 PHE A 45 -21.49 81.47
REMARK 500 ALA A 60 62.19 -114.68
REMARK 500 SER A 108 78.63 -151.91
REMARK 500 GLU A 140 60.81 34.59
REMARK 500 LEU A 158 79.87 -117.32
REMARK 500 ALA A 164 68.68 -163.92
REMARK 500 THR A 193 57.05 -147.34
REMARK 500 SER A 200 -122.50 52.88
REMARK 500 THR A 317 -159.37 -148.20
REMARK 500 ASP A 326 63.95 -117.96
REMARK 500 ASP A 380 56.67 -146.99
REMARK 500 VAL A 400 -64.31 -121.67
REMARK 500 ASN A 424 26.66 -141.08
REMARK 500 HIS A 486 -6.84 51.37
REMARK 500 SER A 487 159.21 -41.85
REMARK 500 ARG A 515 74.31 33.41
REMARK 500 LEU A 516 107.78 -56.67
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 A1539 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 264 ND1
REMARK 620 2 GLU A 261 OE1 94.3
REMARK 620 3 GLU A 261 OE2 89.1 51.8
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1540 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 139 OE2
REMARK 620 2 HIS A 471 ND1 98.0
REMARK 620 3 MG A1543 MG 52.6 75.6
REMARK 620 4 GLU A 139 OE1 57.6 81.7 100.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1541 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 392 OD2
REMARK 620 2 ASP A 326 OD1 69.4
REMARK 620 3 HOH A2078 O 57.1 63.0
REMARK 620 N 1 2
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 GLU A 139 OE2
REMARK 620 2 HIS A 471 ND1 93.5
REMARK 620 3 MG A1540 MG 68.7 53.0
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 1536
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 1537
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 1538
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1539
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1540
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1541
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1542
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1543
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-
REMARK 900 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 (E.C. 3.1
REMARK 900 .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 (7
REMARK 900 CARBON LINKER)
REMARK 900 RELATED ID: 2CMF RELATED DB: PDB
REMARK 900 TORPEDO CALIFORNICA ACETYLCHOLINESTERASE COMPLEXED
REMARK 900 WITH ALKYLENE-LINKED BIS-TACRINE DIMER (5
REMARK 900 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: 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 2J3D 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 NAG A1536 14
HET NAG A1537 14
HET NAG A1538 14
HET MG A1539 1
HET MG A1540 1
HET MG A1541 1
HET MG A1542 1
HET MG A1543 1
HETNAM MG MAGNESIUM ION
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETSYN NAG NAG
FORMUL 3 MG 5(MG 2+)
FORMUL 4 NAG 3(C8 H15 N O6)
FORMUL 5 HOH *98(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 139 1 8
HELIX 5 5 VAL A 150 LEU A 156 1 7
HELIX 6 6 ASN A 167 ILE A 184 1 18
HELIX 7 7 GLN A 185 PHE A 187 5 3
HELIX 8 8 SER A 200 SER A 212 1 13
HELIX 9 9 SER A 215 PHE A 219 5 5
HELIX 10 10 SER A 237 LEU A 252 1 16
HELIX 11 11 SER A 258 ARG A 267 1 10
HELIX 12 12 LYS A 270 VAL A 277 1 8
HELIX 13 13 GLU A 278 LEU A 282 5 5
HELIX 14 14 SER A 304 SER A 311 1 8
HELIX 15 15 GLY A 328 ALA A 336 1 9
HELIX 16 16 SER A 348 VAL A 360 1 13
HELIX 17 17 ASN A 364 TYR A 375 1 12
HELIX 18 18 ASN A 383 VAL A 400 1 18
HELIX 19 19 VAL A 400 LYS A 413 1 14
HELIX 20 20 PRO A 433 GLY A 437 5 5
HELIX 21 21 GLU A 443 PHE A 448 1 6
HELIX 22 22 GLY A 449 VAL A 453 5 5
HELIX 23 23 VAL A 453 ASN A 457 5 5
HELIX 24 24 THR A 459 GLY A 480 1 22
HELIX 25 25 ARG A 517 GLN A 526 1 10
HELIX 26 26 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
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 2.04
LINK ND2 ASN A 59 C1 NAG A1538 1555 1555 1.46
LINK ND2 ASN A 416 C1 NAG A1537 1555 1555 1.45
LINK ND2 ASN A 457 C1 NAG A1536 1555 1555 1.46
LINK MG MG A1539 ND1 HIS A 264 1555 1555 2.10
LINK MG MG A1539 OE2 GLU A 261 1555 1555 1.95
LINK MG MG A1539 OE1 GLU A 261 1555 1555 2.78
LINK MG MG A1540 OE1 GLU A 139 1555 1555 2.17
LINK MG MG A1540 ND1 HIS A 471 1555 1555 2.22
LINK MG MG A1540 MG MG A1543 1555 1555 2.18
LINK MG MG A1540 OE2 GLU A 139 1555 1555 2.37
LINK MG MG A1541 O HOH A2078 1555 1555 2.43
LINK MG MG A1541 OD1 ASP A 326 1555 1555 2.47
LINK MG MG A1541 OD2 ASP A 392 1555 1555 2.49
LINK MG MG A1543 ND1 HIS A 471 1555 1555 2.70
LINK MG MG A1543 OE2 GLU A 139 1555 1555 2.03
CISPEP 1 SER A 103 PRO A 104 0 0.08
SITE 1 AC1 2 GLU A 455 ASN A 457
SITE 1 AC2 5 ASN A 416 GLY A 417 LEU A 494 HOH A2082
SITE 2 AC2 5 HOH A2098
SITE 1 AC3 2 ASN A 59 SER A 61
SITE 1 AC4 2 GLU A 261 HIS A 264
SITE 1 AC5 3 GLU A 139 GLU A 260 HIS A 471
SITE 1 AC6 4 ASP A 326 ASP A 389 ASP A 392 HOH A2078
SITE 1 AC7 3 GLU A 260 GLU A 261 HIS A 264
SITE 1 AC8 2 GLU A 139 HIS A 471
CRYST1 128.740 105.490 70.600 90.00 106.62 90.00 C 1 2 1 4
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 0.007768 0.000000 0.002319 0.00000
SCALE2 0.000000 0.009480 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014782 0.00000
TER 4246 ALA A 536
MASTER 589 0 8 26 14 0 9 6 4390 1 64 42
END
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