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HEADER SERINE HYDROLASE 17-MAR-99 1SOM
TITLE TORPEDO CALIFORNICA ACETYLCHOLINESTERASE INHIBITED BY NERVE
TITLE 2 AGENT GD (SOMAN).
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYLCHOLINESTERASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.1.1.7;
COMPND 5 BIOLOGICAL_UNIT: HOMODIMER;
COMPND 6 OTHER_DETAILS: NERVE AGENT GD (SOMAN) COVALENTLY BOUND TO
COMPND 7 CATALYTIC SERINE (SER200)
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: TORPEDO CALIFORNICA;
SOURCE 3 ORGANISM_COMMON: PACIFIC ELECTRIC RAY;
SOURCE 4 VARIANT: G2 FORM;
SOURCE 5 ORGAN: ELECTRIC ORGAN;
SOURCE 6 TISSUE: ELECTROPLAQUE
KEYWDS SERINE HYDROLASE, CHOLINESTERASE, NERVE AGENT,
KEYWDS 2 ORGANOPHOSPHOROUS ACID ANHYDRIDE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.M.GREENBLATT,C.B.MILLARD,J.L.SUSSMAN,I.SILMAN
REVDAT 1 25-JUN-99 1SOM 0
JRNL AUTH C.B.MILLARD,G.KRYGER,A.ORDENTLICH,H.M.GREENBLATT,
JRNL AUTH 2 M.HAREL,M.L.RAVES,Y.SEGALL,D.BARAK,A.SHAFFERMAN,
JRNL AUTH 3 I.SILMAN,J.L.SUSSMAN
JRNL TITL CRYSTAL STRUCTURES OF AGED PHOSPHONYLATED
JRNL TITL 2 ACETYLCHOLINESTERASE: NERVE AGENT REACTION
JRNL TITL 3 PRODUCTS AT THE ATOMIC LEVEL
JRNL REF BIOCHEMISTRY V. 38 7032 1999
JRNL REFN ASTM BICHAW US ISSN 0006-2960 0033
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH C.B.MILLARD,G.KRYGER,A.ORDENTLICH,M.HAREL,
REMARK 1 AUTH 2 M.L.RAVES,H.M.GREENBLAT,Y.SEGALL,D.BARAK,
REMARK 1 AUTH 3 A.SHAFFERMAN,I.SILMAN,J.L.SUSSMAN
REMARK 1 TITL CRYSTAL STRUCTURAL OF "AGED" PHOSPHORYLATED AND
REMARK 1 TITL 2 PHOSPHONYLATED TORPEDO CALIFORNICA
REMARK 1 TITL 3 ACETYLCHOLINESTERASE
REMARK 1 EDIT B. P. DOCTOR ET AL.
REMARK 1 REF STRUCTURE AND FUNCTION OF 425 1998
REMARK 1 REF 2 CHOLINESTERASES AND RELATED
REMARK 1 REF 3 PROTEINS
REMARK 1 PUBL NEW YORK : PLENUM PRESS
REMARK 1 REFN 9999
REMARK 2
REMARK 2 RESOLUTION. 2.2 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 0.5
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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.5
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 OUTLIER CUTOFF HIGH (RMS(ABS(F))) : 2163305.50000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 96.5
REMARK 3 NUMBER OF REFLECTIONS : 48792
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) : 0.210
REMARK 3 FREE R VALUE : 0.251
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2460
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) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.34
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.50
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 7455
REMARK 3 BIN R VALUE (WORKING SET) : 0.2640
REMARK 3 BIN FREE R VALUE : 0.2920
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.10
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 398
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.01
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4174
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 42
REMARK 3 SOLVENT ATOMS : 184
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 24.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.30
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 7.77000
REMARK 3 B22 (A**2) : 7.77000
REMARK 3 B33 (A**2) : -15.50000
REMARK 3 B12 (A**2) : 3.42000
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) : 0.26
REMARK 3 ESD FROM SIGMAA (A) : 0.250
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) : 0.32
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.27
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.019
REMARK 3 BOND ANGLES (DEGREES) : 1.90
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.90
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.22
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) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.37
REMARK 3 BSOL : 49.78
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 PARAMETER FILE 4 : CIS_PEPTIDE.PARAM
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : CARBOHYDRATE.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : SOMAN.TOP
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINED INITIALLY WITH REFMAC
REMARK 3 TO AN R OF 23.4 AND RFREE OF 27.9
REMARK 4
REMARK 4 1SOM COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 7
REMARK 7 CONTINUOUS ELECTRON DENSITY FEATURES IN FRONT OF THE INDOLE
REMARK 7 RINGS OF TRP84 AND TRP279 DID NOT SATISFACTORILY REFINE
REMARK 7 WITH WATER MOLECULES. THESE FEATURES WERE LEFT EMPTY DURING
REMARK 7 REFINEMENT, BUT THEIR POSITIONS ARE INDICATED IN THE MODEL
REMARK 7 BY OXYGEN ATOMS WITH ZERO OCCUPANCY (RESIDUES 1000 - 1009)
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-MAR-1999.
REMARK 100 THE RCSB ID CODE IS RCSB000673.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : DEC-1997
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 6.00
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU FR300
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NI FILTER
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE (RAXISII)
REMARK 200 DETECTOR MANUFACTURER : RIGAKU
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 49048
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.7
REMARK 200 DATA REDUNDANCY : 5.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05000
REMARK 200 FOR THE DATA SET : 15.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.28
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.1
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.29700
REMARK 200 FOR SHELL : 2.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: 2ACE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 68.0
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.80
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN WAS CRYSTALLIZED FROM
REMARK 280 35-40% W/V PEG 200 0.15M MES PH 6.0 0.05M NACL 4 DEG.
REMARK 280 CELSIUS
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,1/3+Z
REMARK 290 3555 -X+Y,-X,2/3+Z
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,2/3-Z
REMARK 290 6555 -X,-X+Y,1/3-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 45.66733
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 91.33467
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 91.33467
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 45.66733
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 1 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 APPLY THE FOLLOWING TO CHAINS: A, G, F, S
REMARK 350 BIOMT1 1 -0.500000 0.866025 0.000000 -55.78000
REMARK 350 BIOMT2 1 -0.866025 -0.500000 0.000000 96.61379
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 -45.66733
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 HIS A 486
REMARK 465 SER A 487
REMARK 465 GLN A 488
REMARK 465 GLU A 489
REMARK 465 ALA A 536
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 ASN A 42 CG OD1 ND2
REMARK 470 ARG A 46 CZ NH1 NH2
REMARK 470 ARG A 250 CZ NH1 NH2
REMARK 470 ASN A 257 CG OD1 ND2
REMARK 470 GLU A 260 OE1 OE2
REMARK 470 GLU A 268 OE1 OE2
REMARK 470 GLU A 344 OE1 OE2
REMARK 470 GLU A 350 OE1 OE2
REMARK 470 LYS A 357 NZ
REMARK 470 LYS A 413 CD CE NZ
REMARK 470 LYS A 498 CG CD CE NZ
REMARK 470 GLU A 508 CD OE1 OE2
REMARK 470 ARG A 515 CZ NH1 NH2
REMARK 470 GLN A 526 OE1 NE2
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 DUM 1008 O HOH 728 2.15
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 4*RMSD AND BY MORE THAN 0.150 ANGSTROMS (M=MODEL
REMARK 500 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 500 NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,1X,2(A4,A1,3X),12X,F5.3)
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 175 SD MET A 175 CE -0.312
REMARK 500 MET A 436 SD MET A 436 CE 0.174
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 4*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 PHE A 30 N - CA - C ANGL. DEV. = -8.2 DEGREES
REMARK 500 ASN A 66 N - CA - C ANGL. DEV. = -8.9 DEGREES
REMARK 500 ASP A 93 N - CA - C ANGL. DEV. = -9.9 DEGREES
REMARK 500 LEU A 97 CA - CB - CG ANGL. DEV. = 10.2 DEGREES
REMARK 500 THR A 126 N - CA - C ANGL. DEV. = 8.0 DEGREES
REMARK 500 VAL A 129 C - CA - CB ANGL. DEV. = -8.8 DEGREES
REMARK 500 LEU A 135 CA - CB - CG ANGL. DEV. = 7.8 DEGREES
REMARK 500 LEU A 143 CA - CB - CG ANGL. DEV. =-14.8 DEGREES
REMARK 500 SER A 147 N - CA - C ANGL. DEV. = -7.8 DEGREES
REMARK 500 PHE A 155 N - CA - C ANGL. DEV. = 8.6 DEGREES
REMARK 500 LEU A 158 N - CA - C ANGL. DEV. = -8.1 DEGREES
REMARK 500 ASN A 183 N - CA - C ANGL. DEV. = 9.3 DEGREES
REMARK 500 ARG A 216 N - CA - C ANGL. DEV. = 7.7 DEGREES
REMARK 500 PRO A 229 N - CA - C ANGL. DEV. = 8.5 DEGREES
REMARK 500 ALA A 234 N - CA - C ANGL. DEV. = 8.3 DEGREES
REMARK 500 ASN A 255 N - CA - C ANGL. DEV. =-11.4 DEGREES
REMARK 500 PRO A 283 C - N - CA ANGL. DEV. = -8.1 DEGREES
REMARK 500 ASP A 285 N - CA - C ANGL. DEV. =-13.4 DEGREES
REMARK 500 SER A 291 N - CA - C ANGL. DEV. = 8.9 DEGREES
REMARK 500 ILE A 296 N - CA - C ANGL. DEV. = -9.2 DEGREES
REMARK 500 PHE A 301 N - CA - C ANGL. DEV. = -8.4 DEGREES
REMARK 500 THR A 317 N - CA - C ANGL. DEV. = -8.9 DEGREES
REMARK 500 LEU A 320 N - CA - C ANGL. DEV. = -8.5 DEGREES
REMARK 500 LYS A 325 N - CA - C ANGL. DEV. = 7.7 DEGREES
REMARK 500 GLY A 328 N - CA - C ANGL. DEV. = 10.8 DEGREES
REMARK 500 GLY A 335 N - CA - C ANGL. DEV. = 8.7 DEGREES
REMARK 500 ASP A 342 N - CA - C ANGL. DEV. = 8.3 DEGREES
REMARK 500 LEU A 358 CA - CB - CG ANGL. DEV. = 7.5 DEGREES
REMARK 500 ALA A 363 N - CA - C ANGL. DEV. = 8.1 DEGREES
REMARK 500 ASP A 377 N - CA - C ANGL. DEV. = -9.7 DEGREES
REMARK 500 ASP A 381 N - CA - C ANGL. DEV. = 8.2 DEGREES
REMARK 500 PHE A 422 N - CA - C ANGL. DEV. = -9.9 DEGREES
REMARK 500 GLU A 443 N - CA - C ANGL. DEV. = -7.8 DEGREES
REMARK 500 GLY A 449 N - CA - C ANGL. DEV. = 8.5 DEGREES
REMARK 500 LEU A 452 CA - CB - CG ANGL. DEV. = 10.9 DEGREES
REMARK 500 ASN A 457 N - CA - C ANGL. DEV. = 9.5 DEGREES
REMARK 500 THR A 479 N - CA - C ANGL. DEV. = 7.9 DEGREES
REMARK 500 GLU A 484 N - CA - C ANGL. DEV. = -7.5 DEGREES
REMARK 500 LYS A 491 N - CA - C ANGL. DEV. = 13.5 DEGREES
REMARK 500 TRP A 492 N - CA - C ANGL. DEV. =-10.2 DEGREES
REMARK 500 LEU A 494 CA - CB - CG ANGL. DEV. = 13.0 DEGREES
REMARK 500 PHE A 495 N - CA - C ANGL. DEV. = -8.2 DEGREES
REMARK 500 ASP A 504 N - CA - C ANGL. DEV. =-10.0 DEGREES
REMARK 500 LEU A 516 CA - CB - CG ANGL. DEV. = 8.4 DEGREES
REMARK 500 ARG A 517 CB - CG - CD ANGL. DEV. = 8.4 DEGREES
REMARK 500 VAL A 518 C - CA - CB ANGL. DEV. = -9.6 DEGREES
REMARK 500 VAL A 518 CG1 - CB - CG2 ANGL. DEV. = 8.2 DEGREES
REMARK 500 THR A 535 CA - C - O ANGL. DEV. = -7.7 DEGREES
REMARK 600
REMARK 600 HETEROGEN
REMARK 600 GD (SOMAN) HAS UNDERGONE DEALKYLATION
REMARK 600 AND THE PINACOLYL GROUP IS NOT VISIBLE
REMARK 600 IN THE ELECTRON DENSITY MAPS.
REMARK 600
REMARK 600 DUMMY ATOMS NOT USED IN REFINEMENT TO SHOW
REMARK 600 LOCATION OF TWO DENSITY FEATURES NEAR THE
REMARK 600 INDOLE RINGS OF TRP84 AND TRP279
REMARK 600
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: AUTHOR-DETERMINED
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: AUTHOR-DETERMINED
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: CAT
REMARK 800 SITE_DESCRIPTION:
REMARK 800 CATALYTIC TRIAD
REMARK 800
DBREF 1SOM A 1 543 SWS 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 G 416 14
HET NAG F 59 14
HET SOM S 200 4
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM DUM DUMMY ATOMS
HETNAM SOM METHYL PHOSPHINIC ACID
HETSYN NAG NAG
FORMUL 2 NAG 2(C8 H15 N1 O6)
FORMUL 4 DUM 10()
FORMUL 14 SOM C1 H5 O2 P1
FORMUL 15 HOH *184(H2 O1)
HELIX 1 1A SER A 79 ASN A 85 1 7
HELIX 2 2A GLY A 132 GLU A 139 1 8
HELIX 3 3A VAL A 168 ASN A 183 1 16
HELIX 4 4A SER A 200 LEU A 211 1 12
HELIX 5 5A VAL A 238 LEU A 252 1 15
HELIX 6 6A ASP A 259 GLU A 268 1 10
HELIX 7 7A PRO A 271 GLU A 278 1 8
HELIX 8 8A LEU A 305 SER A 311 1 7
HELIX 9 9A SER A 329 GLY A 335 1 7
HELIX 10 10A ARG A 349 VAL A 360 1 12
HELIX 11 11A ASP A 365 THR A 376 1 12
HELIX 12 12A GLY A 384 TYR A 411 1 28
HELIX 13 13A GLU A 443 PHE A 448 1 6
HELIX 14 14A ALA A 460 THR A 479 1 20
HELIX 15 15A VAL A 518 THR A 535 1 18
SHEET 1 A 3 LEU A 6 THR A 10 0
SHEET 2 A 3 GLY A 13 MET A 16 -1 N VAL A 15 O VAL A 8
SHEET 3 A 3 VAL A 57 ALA A 60 1 N TRP A 58 O LYS A 14
SHEET 1 B11 MET A 16 PRO A 21 0
SHEET 2 B11 HIS A 26 PRO A 34 -1 O ALA A 29 N THR A 18
SHEET 3 B11 TYR A 96 PRO A 102 -1 N ILE A 99 O PHE A 30
SHEET 4 B11 VAL A 142 SER A 147 -1 N LEU A 143 O TRP A 100
SHEET 5 B11 THR A 109 TYR A 116 1 N MET A 112 O VAL A 142
SHEET 6 B11 THR A 193 GLU A 199 1 O THR A 195 N VAL A 113
SHEET 7 B11 ARG A 220 SER A 226 1 N ILE A 223 O ILE A 196
SHEET 8 B11 GLN A 318 ASN A 324 1 N GLY A 322 O LEU A 224
SHEET 9 B11 GLY A 417 PHE A 423 1 N TYR A 421 O LEU A 321
SHEET 10 B11 PHE A 502 LEU A 505 1 N ILE A 503 O LEU A 420
SHEET 11 B11 MET A 510 GLN A 514 -1 N HIS A 513 O PHE A 502
SSBOND 1 CYS A 67 CYS A 94
SSBOND 2 CYS A 254 CYS A 265
SSBOND 3 CYS A 402 CYS A 521
LINK ND2 ASN A 416 C1 NAG G 416
LINK ND2 ASN A 59 C1 NAG F 59
LINK OG SER A 200 P1 SOM S 200
CISPEP 1 SER A 103 PRO A 104 0 1.35
SITE 1 CAT 3 SER A 200 GLU A 327 HIS A 440
CRYST1 111.560 111.560 137.002 90.00 90.00 120.00 P 31 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 0.008964 0.005175 0.000000 0.00000
SCALE2 0.000000 0.010350 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007299 0.00000
END |