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HEADER HYDROLASE 21-APR-99 1VXO
TITLE METHYLPHOSPHONYLATED ACETYLCHOLINESTERASE (AGED) OBTAINED
TITLE 2 BY REACTION WITH O-ETHYL-S-[2-[BIS(1-METHYLETHYL)
TITLE 3 AMINO]ETHYL] METHYLPHOSPHONOTHIOATE (VX)
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 THE NERVE AGENT VX (AGED)
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, CHEMICAL-
KEYWDS 2 WARFARE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.B.MILLARD,I.SILMAN,J.L.SUSSMAN
REVDAT 1 15-NOV-99 1VXO 0
JRNL AUTH C.B.MILLARD,G.KOELLNER,A.ORDENTLICH,A.SHAFFERMAN,
JRNL AUTH 2 I.SILMAN,J.L.SUSSMAN
JRNL TITL REACTION PRODUCTS OF ACETYLCHOLINESTERASE AND VX
JRNL TITL 2 REVEAL A MOBILE HISTIDINE IN THE CATALYTIC TRIAD
JRNL REF J.AM.CHEM.SOC. V. 121 9883 1999
JRNL REFN ASTM JACSAT US ISSN 0002-7863 0004
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.40 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) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 OUTLIER CUTOFF HIGH (RMS(ABS(F))) : 1956322.52000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 97.0
REMARK 3 NUMBER OF REFLECTIONS : 38787
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) : 0.194
REMARK 3 FREE R VALUE : 0.234
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1923
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) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.55
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 83.70
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 5213
REMARK 3 BIN R VALUE (WORKING SET) : 0.2380
REMARK 3 BIN FREE R VALUE : 0.2760
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.20
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 286
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.020
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 : 216
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 29.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 37.40
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 7.26000
REMARK 3 B22 (A**2) : 7.26000
REMARK 3 B33 (A**2) : -14.50000
REMARK 3 B12 (A**2) : 4.46000
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) : 0.27
REMARK 3 ESD FROM SIGMAA (A) : 0.240
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) : 0.34
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.29
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.024
REMARK 3 BOND ANGLES (DEGREES) : 2.10
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.00
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.38
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) : 1.08 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.75 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.82 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.70 ; 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 : 36.82
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 : VXA.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 : VXA.TOP
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: USED COMPOSITE-OMIT MAP METHOD
REMARK 4
REMARK 4 1VXO COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 7
REMARK 7 ACHE WAS PHOSPHONYLATED WITH VX, THE CONJUGATE WAS
REMARK 7 CRYSTALLIZED, AND SUBSEQUENTLY ALLOWED TO UNDERGO
REMARK 7 COMPLETE AGING (DEALKYLATION OF THE OP ETHYL GROUP). THE
REMARK 7 STRUCTURE OF THE OP-ACHE CONJUGATE BEFORE AGING ALSO WAS
REMARK 7 SOLVED BY X-RAY DIFFRACTION, AND IS DEPOSITED UNDER A
REMARK 7 SEPARATE PDB ACCESSION CODE.
REMARK 8
REMARK 8 CONTINUOUS POSITIVE DIFFERENCE DENSITY IN (FO-FC) MAPS
REMARK 8 OCCURS IN FRONT OF THE INDOLE RINGS OF W84 AND W279. THIS
REMARK 8 DENSITY IS PRESENTLY MODELED WITH WATERS 1074/1075/1077
REMARK 8 (W84) AND WATERS 1079/1087/1127/1107 (W279).
REMARK 9
REMARK 9 RESIDUES 536 AND 537 WERE NOT RESOLVED.
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-APR-1999.
REMARK 100 THE RCSB ID CODE IS RCSB000907.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-MAR-1999
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) : 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) : 0.98
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : 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 : 38823
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
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 (%) : 97.2
REMARK 200 DATA REDUNDANCY : 10.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06000
REMARK 200 FOR THE DATA SET : 14.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.49
REMARK 200 COMPLETENESS FOR SHELL (%) : 80.5
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.24000
REMARK 200 FOR SHELL : 4.000
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): 3.80
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
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 45.98500
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 91.97000
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 91.97000
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 45.98500
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 A 1
REMARK 465 ASP A 2
REMARK 465 HIS A 3
REMARK 465 ALA A 536
REMARK 465 CYS A 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,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 LEU A 333 CG LEU A 333 CD1 0.168
REMARK 500 MET A 405 SD MET A 405 CE 0.158
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. =-10.2 DEGREES
REMARK 500 ASN A 66 N - CA - C ANGL. DEV. = -9.1 DEGREES
REMARK 500 MET A 83 CG - SD - CE ANGL. DEV. = 8.9 DEGREES
REMARK 500 ASP A 93 N - CA - C ANGL. DEV. = -9.4 DEGREES
REMARK 500 TRP A 100 N - CA - C ANGL. DEV. = -9.4 DEGREES
REMARK 500 THR A 109 N - CA - C ANGL. DEV. = 8.3 DEGREES
REMARK 500 THR A 126 N - CA - C ANGL. DEV. = 8.6 DEGREES
REMARK 500 GLY A 132 N - CA - C ANGL. DEV. = 8.9 DEGREES
REMARK 500 LEU A 158 N - CA - C ANGL. DEV. = -8.3 DEGREES
REMARK 500 ASN A 183 N - CA - C ANGL. DEV. = 8.5 DEGREES
REMARK 500 ARG A 216 N - CA - C ANGL. DEV. = 9.4 DEGREES
REMARK 500 PRO A 229 N - CA - C ANGL. DEV. = 9.1 DEGREES
REMARK 500 ARG A 243 CG - CD - NE ANGL. DEV. =-13.0 DEGREES
REMARK 500 LEU A 252 CA - CB - CG ANGL. DEV. = -9.0 DEGREES
REMARK 500 ASP A 285 N - CA - C ANGL. DEV. =-14.3 DEGREES
REMARK 500 SER A 291 N - CA - C ANGL. DEV. = 9.0 DEGREES
REMARK 500 PHE A 301 N - CA - C ANGL. DEV. = -9.3 DEGREES
REMARK 500 GLY A 335 N - CA - C ANGL. DEV. = 10.4 DEGREES
REMARK 500 LEU A 358 CA - CB - CG ANGL. DEV. = 12.7 DEGREES
REMARK 500 ASP A 377 N - CA - C ANGL. DEV. = -8.7 DEGREES
REMARK 500 ASP A 381 N - CA - C ANGL. DEV. = 8.6 DEGREES
REMARK 500 PRO A 403 C - N - CA ANGL. DEV. = -9.5 DEGREES
REMARK 500 PHE A 422 N - CA - C ANGL. DEV. =-10.1 DEGREES
REMARK 500 ILE A 439 N - CA - C ANGL. DEV. = 9.7 DEGREES
REMARK 500 GLY A 441 N - CA - C ANGL. DEV. = 9.7 DEGREES
REMARK 500 GLU A 443 N - CA - C ANGL. DEV. = -9.3 DEGREES
REMARK 500 GLY A 449 N - CA - C ANGL. DEV. = 10.1 DEGREES
REMARK 500 LEU A 452 CA - CB - CG ANGL. DEV. = 11.4 DEGREES
REMARK 500 THR A 479 N - CA - C ANGL. DEV. = 13.7 DEGREES
REMARK 500 TRP A 492 N - CA - C ANGL. DEV. =-13.4 DEGREES
REMARK 500 LEU A 494 CA - CB - CG ANGL. DEV. = 13.8 DEGREES
REMARK 500 MET A 510 CG - SD - CE ANGL. DEV. = 9.1 DEGREES
REMARK 600
REMARK 600 HETEROGEN
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 1VXO A 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 VXA A 999 4
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM VXA METHYLPHOSPHONIC ACID ESTER GROUP
HETSYN NAG NAG
FORMUL 2 NAG 2(C8 H15 N1 O6)
FORMUL 4 VXA C1 H3 O2 P1 1-
FORMUL 5 HOH *216(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 OG SER A 200 P1 VXA 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 0.42
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 112.509 112.509 137.955 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 0.008888 0.005131 0.000000 0.00000
SCALE2 0.000000 0.010263 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007249 0.00000 |