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HEADER CHOLINESTERASE 19-MAR-99 1CFJ
TITLE METHYLPHOSPHONYLATED ACETYLCHOLINESTERASE (AGED) OBTAINED
TITLE 2 BY REACTION WITH O-ISOPROPYLMETHYLPHOSPHONOFLUORIDATE (GB,
TITLE 3 SARIN)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYLCHOLINESTERASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.1.1.7;
COMPND 5 OTHER_DETAILS: COMPLEXED WITH METHYLPHOSPHONIC ACID ESTER
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: TORPEDO CALIFORNICA;
SOURCE 3 ORGANISM_COMMON: PACIFIC ELECTRIC RAY;
SOURCE 4 ORGAN: ELECTRIC ORGAN;
SOURCE 5 TISSUE: ELECTROPLAQUE;
SOURCE 6 CELLULAR_LOCATION: MEMBRANE BOUND BY GPI ANCHOR
KEYWDS CHOLINESTERASE, ORGANOPHOSPHATE, SERINE HYDROLASE,
KEYWDS 2 CHEMICAL-WARFARE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.B.MILLARD,I.SILMAN,J.L.SUSSMAN
REVDAT 1 01-APR-99 1CFJ 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 PHOSPHONYLATED
JRNL TITL 2 ACETYLCHOLINESTERASE: NERVE AGENT REACTION
JRNL TITL 3 PRODUCTS AT THE ATOMIC LEVEL
JRNL REF TO BE PUBLISHED
JRNL REFN 0353
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH C.B.MILLARD,ET AL.
REMARK 1 TITL CRYSTAL STRUCTURES OF "AGED" PHOSPHORYLATED AND
REMARK 1 TITL 2 PHOSPHONYLATED ACETYLCHOLINESTERASE: A PRELIMINARY
REMARK 1 TITL 3 REPORT
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. 2.60 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) : 2.6
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.0
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.0
REMARK 3 OUTLIER CUTOFF HIGH (RMS(ABS(F))) : 3132443.55
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 93.2
REMARK 3 NUMBER OF REFLECTIONS : 28531
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) : 0.186
REMARK 3 FREE R VALUE : 0.247
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.2
REMARK 3 FREE R VALUE TEST SET COUNT : 1497
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) : 2.6
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.76
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.0
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 4624
REMARK 3 BIN R VALUE (WORKING SET) : 0.224
REMARK 3 BIN FREE R VALUE : 0.29
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.9
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 288
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.02
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 : 32
REMARK 3 SOLVENT ATOMS : 220
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 40.2
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.5
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 8.48
REMARK 3 B22 (A**2) : 8.48
REMARK 3 B33 (A**2) : -16.9
REMARK 3 B12 (A**2) : 8.97
REMARK 3 B13 (A**2) : 0.0
REMARK 3 B23 (A**2) : 0.0
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.26
REMARK 3 ESD FROM SIGMAA (A) : 0.26
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) : 0.36
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.33
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.019
REMARK 3 BOND ANGLES (DEGREES) : 2.0
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.2
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.29
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) : 2.27 ; 1.5
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 3.4 ; 2.0
REMARK 3 SIDE-CHAIN BOND (A**2) : 4.01 ; 2.0
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 5.34 ; 2.5
REMARK 3
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.35
REMARK 3 BSOL : 38.55
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 : GB.PAR
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 : GB.TOP
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1CFJ COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 7
REMARK 7 CONTINUOUS POSITIVE DIFFERENCE DENSITY IN (FO-FC) MAPS
REMARK 7 OCCURS IN FRONT OF THE INDOLE RINGS OF W84 AND W279. THIS
REMARK 7 DENSITY IS PRESENTLY MODELLED WITH WATERS 1007/1008/1009
REMARK 7 (W84) AND WATERS 1003/1004/1005 (W279)
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-MAR-1999.
REMARK 100 THE RCSB ID CODE IS RCSB000683.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JUL-1997
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 6.0
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) : 1.1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : 4X4 CCD
REMARK 200 DETECTOR MANUFACTURER : BRANDEIS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 30011
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.6
REMARK 200 RESOLUTION RANGE LOW (A) : 30.0
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.4
REMARK 200 DATA REDUNDANCY : 6.7
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.09
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.3
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.6
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.69
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.3
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.17
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.2
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR
REMARK 200 REPLACEMENT
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): 3.8
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 35-40% (W/V) PEG-200 0.15 M
REMARK 280 MES BUFFER PH 6, 0.05 M NACL, 4 DEG C
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 45.54100
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 91.08200
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 91.08200
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 45.54100
REMARK 290
REMARK 290 REMARK: NULL
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 1
REMARK 465 ASP 2
REMARK 465 HIS 3
REMARK 465 ALA 536
REMARK 465 CYS 537
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 -0.182
REMARK 500 MET A 379 SD MET A 379 CE 0.190
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 MET A 16 CB - CG - SD ANGL. DEV. = 8.5 DEGREES
REMARK 500 MET A 43 CB - CG - SD ANGL. DEV. = -8.8 DEGREES
REMARK 500 LEU A 97 CA - CB - CG ANGL. DEV. = 9.4 DEGREES
REMARK 500 TRP A 100 N - CA - C ANGL. DEV. = -8.4 DEGREES
REMARK 500 VAL A 129 C - CA - CB ANGL. DEV. = -9.0 DEGREES
REMARK 500 VAL A 141 N - CA - C ANGL. DEV. = -9.5 DEGREES
REMARK 500 SER A 147 N - CA - C ANGL. DEV. = -8.1 DEGREES
REMARK 500 PHE A 155 N - CA - C ANGL. DEV. = 11.0 DEGREES
REMARK 500 ASN A 183 N - CA - C ANGL. DEV. = 9.9 DEGREES
REMARK 500 ARG A 216 N - CA - C ANGL. DEV. = 10.1 DEGREES
REMARK 500 LEU A 218 N - CA - C ANGL. DEV. = 8.3 DEGREES
REMARK 500 PRO A 229 N - CA - C ANGL. DEV. = 8.2 DEGREES
REMARK 500 ALA A 234 N - CA - C ANGL. DEV. = 8.1 DEGREES
REMARK 500 LEU A 252 CA - CB - CG ANGL. DEV. =-14.6 DEGREES
REMARK 500 ASN A 255 N - CA - C ANGL. DEV. = -8.1 DEGREES
REMARK 500 ASP A 285 N - CA - C ANGL. DEV. =-13.4 DEGREES
REMARK 500 ILE A 287 C - CA - CB ANGL. DEV. = 9.4 DEGREES
REMARK 500 ILE A 287 N - CA - C ANGL. DEV. = -9.6 DEGREES
REMARK 500 SER A 291 N - CA - C ANGL. DEV. = 10.9 DEGREES
REMARK 500 ILE A 296 N - CA - C ANGL. DEV. = -8.8 DEGREES
REMARK 500 ASP A 297 N - CA - C ANGL. DEV. = 8.0 DEGREES
REMARK 500 LEU A 320 N - CA - C ANGL. DEV. = -8.2 DEGREES
REMARK 500 GLY A 328 N - CA - C ANGL. DEV. = 8.7 DEGREES
REMARK 500 GLY A 335 N - CA - C ANGL. DEV. = 7.9 DEGREES
REMARK 500 ASP A 342 N - CA - C ANGL. DEV. = 8.3 DEGREES
REMARK 500 LEU A 358 CA - CB - CG ANGL. DEV. = 8.0 DEGREES
REMARK 500 VAL A 360 N - CA - C ANGL. DEV. = -8.5 DEGREES
REMARK 500 LEU A 366 CA - CB - CG ANGL. DEV. =-11.4 DEGREES
REMARK 500 ASP A 377 N - CA - C ANGL. DEV. = -9.9 DEGREES
REMARK 500 ILE A 401 CG1 - CB - CG2 ANGL. DEV. = -9.5 DEGREES
REMARK 500 PRO A 403 C - N - CA ANGL. DEV. = -8.3 DEGREES
REMARK 500 PHE A 422 N - CA - C ANGL. DEV. =-10.6 DEGREES
REMARK 500 ILE A 439 N - CA - C ANGL. DEV. = 9.0 DEGREES
REMARK 500 GLU A 443 N - CA - C ANGL. DEV. = -8.2 DEGREES
REMARK 500 GLY A 449 N - CA - C ANGL. DEV. = 10.6 DEGREES
REMARK 500 ASN A 457 N - CA - C ANGL. DEV. = 8.5 DEGREES
REMARK 500 TYR A 458 N - CA - C ANGL. DEV. = -8.7 DEGREES
REMARK 500 THR A 479 N - CA - C ANGL. DEV. = 9.4 DEGREES
REMARK 500 TRP A 492 N - CA - C ANGL. DEV. = -9.9 DEGREES
REMARK 500 PRO A 493 C - N - CA ANGL. DEV. = -9.0 DEGREES
REMARK 500 LEU A 494 CA - CB - CG ANGL. DEV. = 12.6 DEGREES
REMARK 500 ASP A 504 N - CA - C ANGL. DEV. = -9.4 DEGREES
REMARK 500 LEU A 531 CA - CB - CG ANGL. DEV. = 8.1 DEGREES
REMARK 600
REMARK 600 ANIONIC METHYLPHOSPHONATE ADDUCT COVALENTLY BOUND TO S200
REMARK 600
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: MULTIPLE SEQUENCE ALIGNMENT
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: MULTIPLE SEQUENCE ALIGNMENT
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: CAT
REMARK 800 SITE_DESCRIPTION:
REMARK 800 CATALYTIC TRIAD
REMARK 800
REMARK 800 SITE_IDENTIFIER: OXY
REMARK 800 SITE_DESCRIPTION:
REMARK 800 CATALYTIC OXYANION HOLE
REMARK 800
DBREF 1CFJ 1 537 SWS P04058 ACES_TORCA 22 558
SEQRES 1 A 537 ASP ASP HIS SER GLU LEU LEU VAL ASN THR LYS SER GLY
SEQRES 2 A 537 LYS VAL MET GLY THR ARG VAL PRO VAL LEU SER SER HIS
SEQRES 3 A 537 ILE SER ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO PRO
SEQRES 4 A 537 VAL GLY ASN MET ARG PHE ARG ARG PRO GLU PRO LYS LYS
SEQRES 5 A 537 PRO TRP SER GLY VAL TRP ASN ALA SER THR TYR PRO ASN
SEQRES 6 A 537 ASN CYS GLN GLN TYR VAL ASP GLU GLN PHE PRO GLY PHE
SEQRES 7 A 537 SER GLY SER GLU MET TRP ASN PRO ASN ARG GLU MET SER
SEQRES 8 A 537 GLU ASP CYS LEU TYR LEU ASN ILE TRP VAL PRO SER PRO
SEQRES 9 A 537 ARG PRO LYS SER THR THR VAL MET VAL TRP ILE TYR GLY
SEQRES 10 A 537 GLY GLY PHE TYR SER GLY SER SER THR LEU ASP VAL TYR
SEQRES 11 A 537 ASN GLY LYS TYR LEU ALA TYR THR GLU GLU VAL VAL LEU
SEQRES 12 A 537 VAL SER LEU SER TYR ARG VAL GLY ALA PHE GLY PHE LEU
SEQRES 13 A 537 ALA LEU HIS GLY SER GLN GLU ALA PRO GLY ASN VAL GLY
SEQRES 14 A 537 LEU LEU ASP GLN ARG MET ALA LEU GLN TRP VAL HIS ASP
SEQRES 15 A 537 ASN ILE GLN PHE PHE GLY GLY ASP PRO LYS THR VAL THR
SEQRES 16 A 537 ILE PHE GLY GLU SER ALA GLY GLY ALA SER VAL GLY MET
SEQRES 17 A 537 HIS ILE LEU SER PRO GLY SER ARG ASP LEU PHE ARG ARG
SEQRES 18 A 537 ALA ILE LEU GLN SER GLY SER PRO ASN CYS PRO TRP ALA
SEQRES 19 A 537 SER VAL SER VAL ALA GLU GLY ARG ARG ARG ALA VAL GLU
SEQRES 20 A 537 LEU GLY ARG ASN LEU ASN CYS ASN LEU ASN SER ASP GLU
SEQRES 21 A 537 GLU LEU ILE HIS CYS LEU ARG GLU LYS LYS PRO GLN GLU
SEQRES 22 A 537 LEU ILE ASP VAL GLU TRP ASN VAL LEU PRO PHE ASP SER
SEQRES 23 A 537 ILE PHE ARG PHE SER PHE VAL PRO VAL ILE ASP GLY GLU
SEQRES 24 A 537 PHE PHE PRO THR SER LEU GLU SER MET LEU ASN SER GLY
SEQRES 25 A 537 ASN PHE LYS LYS THR GLN ILE LEU LEU GLY VAL ASN LYS
SEQRES 26 A 537 ASP GLU GLY SER PHE PHE LEU LEU TYR GLY ALA PRO GLY
SEQRES 27 A 537 PHE SER LYS ASP SER GLU SER LYS ILE SER ARG GLU ASP
SEQRES 28 A 537 PHE MET SER GLY VAL LYS LEU SER VAL PRO HIS ALA ASN
SEQRES 29 A 537 ASP LEU GLY LEU ASP ALA VAL THR LEU GLN TYR THR ASP
SEQRES 30 A 537 TRP MET ASP ASP ASN ASN GLY ILE LYS ASN ARG ASP GLY
SEQRES 31 A 537 LEU ASP ASP ILE VAL GLY ASP HIS ASN VAL ILE CYS PRO
SEQRES 32 A 537 LEU MET HIS PHE VAL ASN LYS TYR THR LYS PHE GLY ASN
SEQRES 33 A 537 GLY THR TYR LEU TYR PHE PHE ASN HIS ARG ALA SER ASN
SEQRES 34 A 537 LEU VAL TRP PRO GLU TRP MET GLY VAL ILE HIS GLY TYR
SEQRES 35 A 537 GLU ILE GLU PHE VAL PHE GLY LEU PRO LEU VAL LYS GLU
SEQRES 36 A 537 LEU ASN TYR THR ALA GLU GLU GLU ALA LEU SER ARG ARG
SEQRES 37 A 537 ILE MET HIS TYR TRP ALA THR PHE ALA LYS THR GLY ASN
SEQRES 38 A 537 PRO ASN GLU PRO HIS SER GLN GLU SER LYS TRP PRO LEU
SEQRES 39 A 537 PHE THR THR LYS GLU GLN LYS PHE ILE ASP LEU ASN THR
SEQRES 40 A 537 GLU PRO MET LYS VAL HIS GLN ARG LEU ARG VAL GLN MET
SEQRES 41 A 537 CYS VAL PHE TRP ASN GLN PHE LEU PRO LYS LEU LEU ASN
SEQRES 42 A 537 ALA THR ALA CYS
HET NAG A9416 14
HET NAG A9059 14
HET GB A 999 4
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM GB METHYLPHOSPHONIC ACID ESTER
HETSYN NAG NAG
FORMUL 2 NAG 2(C8 H15 N1 O6)
FORMUL 4 GB C1 H3 O2 P1
FORMUL 5 HOH *220(H2 O1)
HELIX 1 1A SER A 79 ASN A 85 1
HELIX 2 2A GLY A 132 GLU A 139 1
HELIX 3 3A VAL A 168 ASN A 183 1
HELIX 4 4A SER A 200 LEU A 211 1
HELIX 5 5A VAL A 238 LEU A 252 1
HELIX 6 6A ASP A 259 GLU A 268 1
HELIX 7 7A PRO A 271 GLU A 278 1
HELIX 8 8A LEU A 305 SER A 311 1
HELIX 9 9A SER A 329 GLY A 335 1
HELIX 10 10A ARG A 349 VAL A 360 1
HELIX 11 11A ASP A 365 THR A 376 1
HELIX 12 12A GLY A 384 TYR A 411 1
HELIX 13 13A GLU A 443 PHE A 448 1
HELIX 14 14A ALA A 460 THR A 479 1
HELIX 15 15A VAL A 518 THR A 535 1
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 OG SER A 200 P1 GB A 999
LINK ND2 ASN A 59 C1 NAG A9059
LINK ND2 ASN A 416 C1 NAG A9416
CISPEP 1 SER A 103 PRO A 104 0 0.39
SITE 1 CAT 3 SER A 200 HIS A 440 GLU A 327
SITE 1 OXY 3 GLY A 118 GLY A 119 ALA A 201
CRYST1 111.395 111.395 136.623 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 0.008977 0.005183 0.000000 0.00000
SCALE2 0.000000 0.010366 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007319 0.00000 |