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HEADER HYDROLASE/TOXIN 05-JAN-99 1B41
TITLE HUMAN ACETYLCHOLINESTERASE COMPLEXED WITH FASCICULIN-II,
TITLE 2 GLYCOSYLATED PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYLCHOLINESTERASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SINGLE DOMAIN;
COMPND 5 SYNONYM: HUACHE H-SUBUNIT;
COMPND 6 EC: 3.1.1.7;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: FASCICULIN-2;
COMPND 11 CHAIN: B;
COMPND 12 FRAGMENT: SINGLE DOMAIN;
COMPND 13 SYNONYM: ACETYLCHOLINESTERASE TOXIN F-VII;
COMPND 14 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 GENE: ACHE;
SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 7 EXPRESSION_SYSTEM_CELL_LINE: HEK 293;
SOURCE 8 EXPRESSION_SYSTEM_TISSUE: KIDNEY;
SOURCE 9 EXPRESSION_SYSTEM_CELL: HUMAN EMBRYONIC KIDNEY CELLS;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: DENDROASPIS ANGUSTICEPS;
SOURCE 12 ORGANISM_COMMON: EASTERN GREEN MAMBA;
SOURCE 13 TISSUE: VENOM
KEYWDS SERINE ESTERASE, HUMAN-ACETYLCHOLINESTERASE, HYDROLASE,
KEYWDS 2 SNAKE TOXIN
EXPDTA X-RAY DIFFRACTION
AUTHOR G.KRYGER,M.HAREL,A.SHAFFERMAN,I.SILMAN,J.L.SUSSMAN
REVDAT 1 17-JAN-01 1B41 0
JRNL AUTH G.KRYGER,M.HAREL,K.GILES,L.TOKER,B.VELAN,A.LAZAR,
JRNL AUTH 2 C.KRONMAN,D.BARAK,N.ARIEL,A.SHAFFERMAN,I.SILMAN,
JRNL AUTH 3 J.L.SUSSMAN
JRNL TITL STRUCTURES OF RECOMBINANT NATIVE AND E202Q MUTANT
JRNL TITL 2 HUMAN ACETYLCHOLINESTERASE COMPLEXED WITH THE
JRNL TITL 3 SNAKE-VENOM TOXIN FASCICULIN-II
JRNL REF ACTA CRYSTALLOGR., SECT.D V. 56 1385 2000
JRNL REFN ASTM ABCRE6 DK ISSN 0907-4449
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH G.KRYGER,K.GILES,L.TOKER,B.VELAN,A.LAZAR,C.KRONMAN,
REMARK 1 AUTH 2 D.BARAK,N.ARIEL,A.SHAFFERMAN,W.MALLENDER,
REMARK 1 AUTH 3 T.ROSENBERRY,I.SILMAN,J.L.SUSSMAN,M.HAREL
REMARK 1 TITL STRUCTURAL STUDIES ON HUMAN AND INSECT
REMARK 1 TITL 2 ACETYLCHOLINESTERASE
REMARK 1 EDIT B.P.DOCTOR, P.TAYLOR, D.M.QUINN, R.L.ROTUNDO,
REMARK 1 EDIT 2 M.K.GENTRY
REMARK 1 REF STRUCTURE AND FUNCTION OF 14 1998
REMARK 1 REF 2 CHOLINESTERASES AND RELATED
REMARK 1 REF 3 PROTEINS. PROCEEDINGS OF
REMARK 1 REF 4 THE SIXTH INTERNATIONAL
REMARK 1 REF 5 MEETING ON CHOLINESTERASES
REMARK 1 REF 6 HELD IN LA JOLLA,
REMARK 1 REF 7 CALIFORNIA, MARCH 20-24,
REMARK 1 REF 8 1998
REMARK 1 PUBL NEW YORK : PLENUM PRESS
REMARK 1 REFN US ISSN 0-306-46050-5
REMARK 2
REMARK 2 RESOLUTION. 2.76 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK 3 : 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) : 2.76
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.74
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 OUTLIER CUTOFF HIGH (RMS(ABS(F))) : 3998639.10000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 98.9
REMARK 3 NUMBER OF REFLECTIONS : 26128
REMARK 3
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) : 0.219
REMARK 3 FREE R VALUE : 0.265
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.700
REMARK 3 FREE R VALUE TEST SET COUNT : 2016
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) : 2.76
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.93
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 76.80
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3189
REMARK 3 BIN R VALUE (WORKING SET) : 0.3620
REMARK 3 BIN FREE R VALUE : 0.4120
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 7.70
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 266
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.025
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4642
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 52
REMARK 3 SOLVENT ATOMS : 194
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 42.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 49.90
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 12.47000
REMARK 3 B22 (A**2) : 12.47000
REMARK 3 B33 (A**2) : -24.94000
REMARK 3 B12 (A**2) : 11.28000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.36
REMARK 3 ESD FROM SIGMAA (A) : 0.600
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.45
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.70
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.40
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.40
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.07
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) : 1.27 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.21 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.83 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 4.12 ; 2.500
REMARK 3
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.33
REMARK 3 BSOL : 48.85
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
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : CARBOHYDRATE.PARAM
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : CARBOHYDRATE.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE FOLLOWING SIDE CHAINS WERE
REMARK 3 MODELED IN TWO CONFORMATIONS: A13, A91, A166, A246, A253,
REMARK 3 B11
REMARK 4
REMARK 4 1B41 COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 6
REMARK 6 FOR CHAIN A, BOTH THE N-TERMINAL AND C-TERMINAL
REMARK 6 RESIDUES WERE NOT SEEN IN THE DENSITY MAPS
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-AUG-1999.
REMARK 100 THE RCSB ID CODE IS RCSB001291.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.20
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X12C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.009
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26128
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 4.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.08100
REMARK 200 FOR THE DATA SET : 15.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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
REMARK 200 REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1FSS
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z
REMARK 290 6555 -X,-X+Y,-Z
REMARK 290 7555 2/3+X,1/3+Y,1/3+Z
REMARK 290 8555 2/3-Y,1/3+X-Y,1/3+Z
REMARK 290 9555 2/3-X+Y,1/3-X,1/3+Z
REMARK 290 10555 2/3+Y,1/3+X,1/3-Z
REMARK 290 11555 2/3+X-Y,1/3-Y,1/3-Z
REMARK 290 12555 2/3-X,1/3-X+Y,1/3-Z
REMARK 290 13555 1/3+X,2/3+Y,2/3+Z
REMARK 290 14555 1/3-Y,2/3+X-Y,2/3+Z
REMARK 290 15555 1/3-X+Y,2/3-X,2/3+Z
REMARK 290 16555 1/3+Y,2/3+X,2/3-Z
REMARK 290 17555 1/3+X-Y,2/3-Y,2/3-Z
REMARK 290 18555 1/3-X,2/3-X+Y,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 0.00000
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 0.00000
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 0.00000
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 0.00000
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 74.49500
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 43.00971
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 82.33667
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 74.49500
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 43.00971
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 82.33667
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 74.49500
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 43.00971
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 82.33667
REMARK 290 SMTRY1 10 -0.500000 0.866025 0.000000 74.49500
REMARK 290 SMTRY2 10 0.866025 0.500000 0.000000 43.00971
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 82.33667
REMARK 290 SMTRY1 11 1.000000 0.000000 0.000000 74.49500
REMARK 290 SMTRY2 11 0.000000 -1.000000 0.000000 43.00971
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 82.33667
REMARK 290 SMTRY1 12 -0.500000 -0.866025 0.000000 74.49500
REMARK 290 SMTRY2 12 -0.866025 0.500000 0.000000 43.00971
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 82.33667
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 86.01942
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 164.67333
REMARK 290 SMTRY1 14 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 14 0.866025 -0.500000 0.000000 86.01942
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 164.67333
REMARK 290 SMTRY1 15 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 15 -0.866025 -0.500000 0.000000 86.01942
REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 164.67333
REMARK 290 SMTRY1 16 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 16 0.866025 0.500000 0.000000 86.01942
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 164.67333
REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 17 0.000000 -1.000000 0.000000 86.01942
REMARK 290 SMTRY3 17 0.000000 0.000000 -1.000000 164.67333
REMARK 290 SMTRY1 18 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 18 -0.866025 0.500000 0.000000 86.01942
REMARK 290 SMTRY3 18 0.000000 0.000000 -1.000000 164.67333
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 2 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
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 APPLY THE FOLLOWING TO CHAINS: A, B, X
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH 697 LIES ON A SPECIAL POSITION.
REMARK 375 HOH 696 LIES ON A SPECIAL POSITION.
REMARK 375 HOH 676 LIES ON A SPECIAL POSITION.
REMARK 400
REMARK 400 COMPOUND
REMARK 400 VERTEBRATE ACHE OCCURS AS AN ARRAY OF MOLECULAR FORMS,
REMARK 400 BY MEANS OF ALTERNATIVE SPLICING, WHICH DIFFER IN THE
REMARK 400 NUMBER OF SUBUNITS WHICH THEY CONTAIN AND IN THEIR
REMARK 400 QUATERNARY STRUCTURE.
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 259
REMARK 465 GLY A 260
REMARK 465 GLY A 261
REMARK 465 THR A 262
REMARK 465 GLY A 263
REMARK 465 GLY A 264
REMARK 465 ARG A 493
REMARK 465 ASP A 494
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 A 268 CG CD OE1 OE2
REMARK 470 GLN A 291 CD OE1 NE2
REMARK 470 GLN A 369 CD OE1 NE2
REMARK 470 ARG A 522 CZ NH1 NH2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI
REMARK 500 O HOH 601 O HOH 602 2.19
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),F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 MET A 211 SD MET A 211 CG -0.042
REMARK 500 MET A 443 CE MET A 443 SD -0.048
REMARK 500 PRO A 492 CG PRO A 492 CB 0.051
REMARK 500 PRO A 495 CD PRO A 495 CG 0.048
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, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 LEU A 146 CA - CB - CG ANGL. DEV. = 9.1 DEGREES
REMARK 500 PHE A 158 N - CA - C ANGL. DEV. = 11.1 DEGREES
REMARK 500 LEU A 161 N - CA - C ANGL. DEV. =-10.9 DEGREES
REMARK 500 ASN A 186 N - CA - C ANGL. DEV. = 10.7 DEGREES
REMARK 500 GLN A 291 N - CA - C ANGL. DEV. = 13.5 DEGREES
REMARK 500 VAL A 294 N - CA - C ANGL. DEV. = -8.7 DEGREES
REMARK 500 GLY A 335 N - CA - C ANGL. DEV. = 9.8 DEGREES
REMARK 500 ASP A 384 N - CA - C ANGL. DEV. =-10.2 DEGREES
REMARK 500 GLU A 491 N - CA - C ANGL. DEV. = 16.2 DEGREES
REMARK 500 PRO A 495 N - CA - C ANGL. DEV. = 10.3 DEGREES
REMARK 500 ARG B 27 N - CA - C ANGL. DEV. = -9.1 DEGREES
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: CAT
REMARK 800 SITE_DESCRIPTION:
REMARK 800 CATALYTIC TRIAD
DBREF 1B41 A 5 543 SWS P22303 ACES_HUMAN 36 574
DBREF 1B41 B 1 61 SWS P01403 TXF7_DENAN 1 61
SEQADV 1B41 ASN B 47 SWS P01403 TYR 47 ENGINEERED
SEQRES 1 A 539 ASP ALA GLU LEU LEU VAL THR VAL ARG GLY GLY ARG LEU
SEQRES 2 A 539 ARG GLY ILE ARG LEU LYS THR PRO GLY GLY PRO VAL SER
SEQRES 3 A 539 ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO PRO MET GLY
SEQRES 4 A 539 PRO ARG ARG PHE LEU PRO PRO GLU PRO LYS GLN PRO TRP
SEQRES 5 A 539 SER GLY VAL VAL ASP ALA THR THR PHE GLN SER VAL CYS
SEQRES 6 A 539 TYR GLN TYR VAL ASP THR LEU TYR PRO GLY PHE GLU GLY
SEQRES 7 A 539 THR GLU MET TRP ASN PRO ASN ARG GLU LEU SER GLU ASP
SEQRES 8 A 539 CYS LEU TYR LEU ASN VAL TRP THR PRO TYR PRO ARG PRO
SEQRES 9 A 539 THR SER PRO THR PRO VAL LEU VAL TRP ILE TYR GLY GLY
SEQRES 10 A 539 GLY PHE TYR SER GLY ALA SER SER LEU ASP VAL TYR ASP
SEQRES 11 A 539 GLY ARG PHE LEU VAL GLN ALA GLU ARG THR VAL LEU VAL
SEQRES 12 A 539 SER MET ASN TYR ARG VAL GLY ALA PHE GLY PHE LEU ALA
SEQRES 13 A 539 LEU PRO GLY SER ARG GLU ALA PRO GLY ASN VAL GLY LEU
SEQRES 14 A 539 LEU ASP GLN ARG LEU ALA LEU GLN TRP VAL GLN GLU ASN
SEQRES 15 A 539 VAL ALA ALA PHE GLY GLY ASP PRO THR SER VAL THR LEU
SEQRES 16 A 539 PHE GLY GLU SER ALA GLY ALA ALA SER VAL GLY MET HIS
SEQRES 17 A 539 LEU LEU SER PRO PRO SER ARG GLY LEU PHE HIS ARG ALA
SEQRES 18 A 539 VAL LEU GLN SER GLY ALA PRO ASN GLY PRO TRP ALA THR
SEQRES 19 A 539 VAL GLY MET GLY GLU ALA ARG ARG ARG ALA THR GLN LEU
SEQRES 20 A 539 ALA HIS LEU VAL GLY CYS PRO PRO GLY GLY THR GLY GLY
SEQRES 21 A 539 ASN ASP THR GLU LEU VAL ALA CYS LEU ARG THR ARG PRO
SEQRES 22 A 539 ALA GLN VAL LEU VAL ASN HIS GLU TRP HIS VAL LEU PRO
SEQRES 23 A 539 GLN GLU SER VAL PHE ARG PHE SER PHE VAL PRO VAL VAL
SEQRES 24 A 539 ASP GLY ASP PHE LEU SER ASP THR PRO GLU ALA LEU ILE
SEQRES 25 A 539 ASN ALA GLY ASP PHE HIS GLY LEU GLN VAL LEU VAL GLY
SEQRES 26 A 539 VAL VAL LYS ASP GLU GLY SER TYR PHE LEU VAL TYR GLY
SEQRES 27 A 539 ALA PRO GLY PHE SER LYS ASP ASN GLU SER LEU ILE SER
SEQRES 28 A 539 ARG ALA GLU PHE LEU ALA GLY VAL ARG VAL GLY VAL PRO
SEQRES 29 A 539 GLN VAL SER ASP LEU ALA ALA GLU ALA VAL VAL LEU HIS
SEQRES 30 A 539 TYR THR ASP TRP LEU HIS PRO GLU ASP PRO ALA ARG LEU
SEQRES 31 A 539 ARG GLU ALA LEU SER ASP VAL VAL GLY ASP HIS ASN VAL
SEQRES 32 A 539 VAL CYS PRO VAL ALA GLN LEU ALA GLY ARG LEU ALA ALA
SEQRES 33 A 539 GLN GLY ALA ARG VAL TYR ALA TYR VAL PHE GLU HIS ARG
SEQRES 34 A 539 ALA SER THR LEU SER TRP PRO LEU TRP MET GLY VAL PRO
SEQRES 35 A 539 HIS GLY TYR GLU ILE GLU PHE ILE PHE GLY ILE PRO LEU
SEQRES 36 A 539 ASP PRO SER ARG ASN TYR THR ALA GLU GLU LYS ILE PHE
SEQRES 37 A 539 ALA GLN ARG LEU MET ARG TYR TRP ALA ASN PHE ALA ARG
SEQRES 38 A 539 THR GLY ASP PRO ASN GLU PRO ARG ASP PRO LYS ALA PRO
SEQRES 39 A 539 GLN TRP PRO PRO TYR THR ALA GLY ALA GLN GLN TYR VAL
SEQRES 40 A 539 SER LEU ASP LEU ARG PRO LEU GLU VAL ARG ARG GLY LEU
SEQRES 41 A 539 ARG ALA GLN ALA CYS ALA PHE TRP ASN ARG PHE LEU PRO
SEQRES 42 A 539 LYS LEU LEU SER ALA THR
SEQRES 1 B 61 THR MET CYS TYR SER HIS THR THR THR SER ARG ALA ILE
SEQRES 2 B 61 LEU THR ASN CYS GLY GLU ASN SER CYS TYR ARG LYS SER
SEQRES 3 B 61 ARG ARG HIS PRO PRO LYS MET VAL LEU GLY ARG GLY CYS
SEQRES 4 B 61 GLY CYS PRO PRO GLY ASP ASP ASN LEU GLU VAL LYS CYS
SEQRES 5 B 61 CYS THR SER PRO ASP LYS CYS ASN TYR
MODRES 1B41 ASN A 350 ASN GLYCOSYLATION SITE
MODRES 1B41 ASN A 464 ASN GLYCOSYLATION SITE
HET FUC X3001 10
HET NAG X3002 14
HET NAG X3003 14
HET NAG A3004 14
HETNAM FUC FUCOSE
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETSYN NAG NAG
FORMUL 3 FUC C6 H12 O5
FORMUL 3 NAG 3(C8 H15 N1 O6)
FORMUL 5 HOH *194(H2 O1)
HELIX 1 1 MET A 42 ARG A 46 5 5
HELIX 2 2 PHE A 80 MET A 85 1 6
HELIX 3 3 LEU A 130 ASP A 134 5 5
HELIX 4 4 GLY A 135 ARG A 143 1 9
HELIX 5 5 VAL A 153 LEU A 159 1 7
HELIX 6 6 ASN A 170 VAL A 187 1 18
HELIX 7 7 ALA A 188 PHE A 190 5 3
HELIX 8 8 SER A 203 LEU A 214 1 12
HELIX 9 9 SER A 215 PHE A 222 5 8
HELIX 10 10 MET A 241 VAL A 255 1 15
HELIX 11 11 ASN A 265 ARG A 274 1 10
HELIX 12 12 PRO A 277 GLU A 285 1 9
HELIX 13 13 THR A 311 GLY A 319 1 9
HELIX 14 14 GLY A 335 VAL A 340 1 6
HELIX 15 15 SER A 355 VAL A 367 1 13
HELIX 16 16 SER A 371 TYR A 382 1 12
HELIX 17 17 ASP A 390 VAL A 407 1 18
HELIX 18 18 VAL A 407 GLN A 421 1 15
HELIX 19 19 PRO A 440 GLY A 444 5 5
HELIX 20 20 GLU A 450 PHE A 455 1 6
HELIX 21 21 GLY A 456 ASP A 460 5 5
HELIX 22 22 THR A 466 GLY A 487 1 22
HELIX 23 23 ARG A 525 ARG A 534 1 10
HELIX 24 24 ARG A 534 ALA A 542 1 9
SHEET 1 A 3 LEU A 9 VAL A 12 0
SHEET 2 A 3 GLY A 15 ARG A 18 -1 O GLY A 15 N VAL A 12
SHEET 3 A 3 VAL A 59 ASP A 61 1 N VAL A 60 O ARG A 16
SHEET 1 B11 ILE A 20 LEU A 22 0
SHEET 2 B11 VAL A 29 PRO A 36 -1 O VAL A 29 N LEU A 22
SHEET 3 B11 TYR A 98 THR A 103 -1 O LEU A 99 N ILE A 35
SHEET 4 B11 VAL A 145 MET A 149 -1 O LEU A 146 N TRP A 102
SHEET 5 B11 THR A 112 ILE A 118 1 O PRO A 113 N VAL A 145
SHEET 6 B11 GLY A 192 GLU A 202 1 N ASP A 193 O THR A 112
SHEET 7 B11 ARG A 224 GLN A 228 1 O ARG A 224 N LEU A 199
SHEET 8 B11 GLN A 325 VAL A 331 1 O GLN A 325 N ALA A 225
SHEET 9 B11 ARG A 424 PHE A 430 1 O ARG A 424 N VAL A 326
SHEET 10 B11 GLN A 509 LEU A 513 1 O VAL A 511 N VAL A 429
SHEET 11 B11 GLU A 519 ARG A 522 -1 O GLU A 519 N SER A 512
SHEET 1 C 2 VAL A 68 CYS A 69 0
SHEET 2 C 2 LEU A 92 SER A 93 1 N SER A 93 O VAL A 68
SHEET 1 D 2 VAL A 239 GLY A 240 0
SHEET 2 D 2 VAL A 302 VAL A 303 1 N VAL A 303 O VAL A 239
SHEET 1 E 2 MET B 2 SER B 5 0
SHEET 2 E 2 ILE B 13 ASN B 16 -1 N ILE B 13 O SER B 5
SHEET 1 F 3 VAL B 34 CYS B 39 0
SHEET 2 F 3 CYS B 22 ARG B 27 -1 N TYR B 23 O GLY B 38
SHEET 3 F 3 LEU B 48 CYS B 53 -1 N GLU B 49 O SER B 26
SSBOND 1 CYS A 69 CYS A 96
SSBOND 2 CYS A 257 CYS A 272
SSBOND 3 CYS A 409 CYS A 529
SSBOND 4 CYS B 3 CYS B 22
SSBOND 5 CYS B 17 CYS B 39
SSBOND 6 CYS B 41 CYS B 52
SSBOND 7 CYS B 53 CYS B 59
LINK O4 NAG X3002 C1 NAG X3003
LINK C1 FUC X3001 O6 NAG X3002
LINK C1 NAG X3002 ND2 ASN A 350
LINK ND2 ASN A 464 C1 NAG A3004
CISPEP 1 TYR A 105 PRO A 106 0 0.19
CISPEP 2 CYS A 257 PRO A 258 0 -0.02
CISPEP 3 PRO B 30 PRO B 31 0 0.05
CRYST1 148.990 148.990 247.010 90.00 90.00 120.00 H 3 2 18
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 0.006712 0.003875 0.000000 0.00000
SCALE2 0.000000 0.007750 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004048 0.00000
END |