| content |
HEADER HYDROLASE 08-JAN-07 2OGS
TITLE CRYSTAL STRUCTURE OF THE GEOBACILLUS STEAROTHERMOPHILUS
TITLE 2 CARBOXYLESTERASE EST55 AT PH 6.2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THERMOSTABLE CARBOXYLESTERASE EST50;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.1.1.1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS STEAROTHERMOPHILUS;
SOURCE 3 ORGANISM_COMMON: BACTERIA;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_COMMON: BACTERIA;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: TOP10
KEYWDS CARBOXYLESTERASE, ALPHA/BETA HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.LIU,H.E.EWIS,P.C.TAI,C.D.LU,I.T.WEBER
REVDAT 1 13-FEB-07 2OGS 0
JRNL AUTH P.LIU,H.E.EWIS,P.C.TAI,C.D.LU,I.T.WEBER
JRNL TITL CRYSTAL STRUCTURE OF THE GEOBACILLUS
JRNL TITL 2 STEAROTHERMOPHILUS CARBOXYLESTERASE EST55 AND ITS
JRNL TITL 3 ACTIVATION OF PRODRUG CPT-11.
JRNL REF J.MOL.BIOL. 2006
JRNL REFN ASTM JMOBAK UK ESSN 1089-8638
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.02 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
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) : 2.02
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.77
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1769127.620
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 33883
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) : 0.204
REMARK 3 FREE R VALUE : 0.236
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3410
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.004
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) : 2.02
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.15
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.00
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 4945
REMARK 3 BIN R VALUE (WORKING SET) : 0.2310
REMARK 3 BIN FREE R VALUE : 0.2660
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.80
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 600
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.011
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3865
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 3
REMARK 3 SOLVENT ATOMS : 151
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 20.80
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 37.30
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.46000
REMARK 3 B22 (A**2) : -0.72000
REMARK 3 B33 (A**2) : 2.17000
REMARK 3 B12 (A**2) : 0.00000
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) : 0.23
REMARK 3 ESD FROM SIGMAA (A) : 0.15
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) : 0.28
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.21
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.20
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.90
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.96
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) : 2.080 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 3.360 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.440 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.800 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.39
REMARK 3 BSOL : 49.34
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 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : ION.TOP
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2OGS COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-JAN-2007.
REMARK 100 THE RCSB ID CODE IS RCSB041116.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-NOV-2004
REMARK 200 TEMPERATURE (KELVIN) : 95.0
REMARK 200 PH : 6.20
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SER-CAT22
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : SI
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 300
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MARCCD
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 33952
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.020
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 7.300
REMARK 200 R MERGE (I) : 0.08500
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 17.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.02
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.09
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.30
REMARK 200 R MERGE FOR SHELL (I) : 0.31100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 11.230
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CCP4
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.52
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG3350, AMMONIUM IODINE, PH 6.2,
REMARK 280 VAPOR DIFFUSION, HANGING DROP
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 1/2-X,-Y,1/2+Z
REMARK 290 3555 -X,1/2+Y,1/2-Z
REMARK 290 4555 1/2+X,1/2-Y,-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 34.76500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 49.51500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 36.74500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 49.51500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 34.76500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 36.74500
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 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 BIOMOLECULE: 1
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 MET A 1
REMARK 465 GLU A 2
REMARK 465 ASP A 66
REMARK 465 PRO A 67
REMARK 465 ILE A 68
REMARK 465 PHE A 69
REMARK 465 SER A 70
REMARK 465 GLY A 71
REMARK 465 LEU A 72
REMARK 465 LEU A 73
REMARK 465 GLY A 74
REMARK 465 ARG A 75
REMARK 465 MET A 76
REMARK 465 PHE A 401
REMARK 465 GLY A 402
REMARK 465 GLY A 403
REMARK 465 GLN A 404
REMARK 465 GLY A 497
REMARK 465 ARG A 498
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 SER A 65 OG
REMARK 470 SER A 77 OG
REMARK 470 LYS A 327 CG CD CE NZ
REMARK 470 ARG A 335 CG CD NE CZ NH1 NH2
REMARK 470 SER A 355 OG
REMARK 470 VAL A 400 CG1 CG2
REMARK 470 LEU A 405 CG CD1 CD2
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 140 SD MET A 140 CE -0.041
REMARK 500 MET A 217 SD MET A 217 CE 0.045
REMARK 500 PRO A 301 CD PRO A 301 N -0.069
REMARK 500 HIS A 443 CB HIS A 443 CG 0.040
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 87 CA - CB - CG ANGL. DEV. = 8.1 DEGREES
REMARK 500 TRP A 119 CA - CB - CG ANGL. DEV. = 8.0 DEGREES
REMARK 500 ASN A 137 N - CA - C ANGL. DEV. = -8.2 DEGREES
REMARK 500 ASN A 177 N - CA - C ANGL. DEV. = 8.2 DEGREES
REMARK 500 VAL A 279 N - CA - C ANGL. DEV. = -9.0 DEGREES
REMARK 500 LEU A 303 N - CA - C ANGL. DEV. = -9.0 DEGREES
REMARK 500 PHE A 371 N - CA - C ANGL. DEV. = 8.8 DEGREES
REMARK 500 ARG A 393 N - CA - C ANGL. DEV. = -8.4 DEGREES
REMARK 500 HIS A 409 N - CA - C ANGL. DEV. = 8.6 DEGREES
REMARK 500 LEU A 413 N - CA - C ANGL. DEV. = 9.7 DEGREES
REMARK 500 ASN A 456 N - CA - C ANGL. DEV. = 7.7 DEGREES
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2OGT RELATED DB: PDB
DBREF 2OGS A 1 498 UNP Q8GCC7 Q8GCC7_BACST 1 498
SEQADV 2OGS 0CS A 408 UNP Q8GCC7 CYS 408 MODIFIED RESIDUE
SEQRES 1 A 498 MET GLU ARG THR VAL VAL GLU THR ARG TYR GLY ARG LEU
SEQRES 2 A 498 ARG GLY GLU MET ASN GLU GLY VAL PHE VAL TRP LYS GLY
SEQRES 3 A 498 ILE PRO TYR ALA LYS ALA PRO VAL GLY GLU ARG ARG PHE
SEQRES 4 A 498 LEU PRO PRO GLU PRO PRO ASP ALA TRP ASP GLY VAL ARG
SEQRES 5 A 498 GLU ALA THR SER PHE GLY PRO VAL VAL MET GLN PRO SER
SEQRES 6 A 498 ASP PRO ILE PHE SER GLY LEU LEU GLY ARG MET SER GLU
SEQRES 7 A 498 ALA PRO SER GLU ASP GLY LEU TYR LEU ASN ILE TRP SER
SEQRES 8 A 498 PRO ALA ALA ASP GLY LYS LYS ARG PRO VAL LEU PHE TRP
SEQRES 9 A 498 ILE HIS GLY GLY ALA PHE LEU PHE GLY SER GLY SER SER
SEQRES 10 A 498 PRO TRP TYR ASP GLY THR ALA PHE ALA LYS HIS GLY ASP
SEQRES 11 A 498 VAL VAL VAL VAL THR ILE ASN TYR ARG MET ASN VAL PHE
SEQRES 12 A 498 GLY PHE LEU HIS LEU GLY ASP SER PHE GLY GLU ALA TYR
SEQRES 13 A 498 ALA GLN ALA GLY ASN LEU GLY ILE LEU ASP GLN VAL ALA
SEQRES 14 A 498 ALA LEU ARG TRP VAL LYS GLU ASN ILE ALA ALA PHE GLY
SEQRES 15 A 498 GLY ASP PRO ASP ASN ILE THR ILE PHE GLY GLU SER ALA
SEQRES 16 A 498 GLY ALA ALA SER VAL GLY VAL LEU LEU SER LEU PRO GLU
SEQRES 17 A 498 ALA SER GLY LEU PHE ARG ARG ALA MET LEU GLN SER GLY
SEQRES 18 A 498 SER GLY SER LEU LEU LEU ARG SER PRO GLU THR ALA MET
SEQRES 19 A 498 ALA MET THR GLU ARG ILE LEU ASP LYS ALA GLY ILE ARG
SEQRES 20 A 498 PRO GLY ASP ARG GLU ARG LEU LEU SER ILE PRO ALA GLU
SEQRES 21 A 498 GLU LEU LEU ARG ALA ALA LEU SER LEU GLY PRO GLY VAL
SEQRES 22 A 498 MET TYR GLY PRO VAL VAL ASP GLY ARG VAL LEU ARG ARG
SEQRES 23 A 498 HIS PRO ILE GLU ALA LEU ARG TYR GLY ALA ALA SER GLY
SEQRES 24 A 498 ILE PRO ILE LEU ILE GLY VAL THR LYS ASP GLU TYR ASN
SEQRES 25 A 498 LEU PHE THR LEU THR ASP PRO SER TRP THR LYS LEU GLY
SEQRES 26 A 498 GLU LYS GLU LEU LEU ASP ARG ILE ASN ARG GLU VAL GLY
SEQRES 27 A 498 PRO VAL PRO GLU GLU ALA ILE ARG TYR TYR LYS GLU THR
SEQRES 28 A 498 ALA GLU PRO SER ALA PRO THR TRP GLN THR TRP LEU ARG
SEQRES 29 A 498 ILE MET THR TYR ARG VAL PHE VAL GLU GLY MET LEU ARG
SEQRES 30 A 498 THR ALA ASP ALA GLN ALA ALA GLN GLY ALA ASP VAL TYR
SEQRES 31 A 498 MET TYR ARG PHE ASP TYR GLU THR PRO VAL PHE GLY GLY
SEQRES 32 A 498 GLN LEU LYS ALA 0CS HIS ALA LEU GLU LEU PRO PHE VAL
SEQRES 33 A 498 PHE HIS ASN LEU HIS GLN PRO GLY VAL ALA ASN PHE VAL
SEQRES 34 A 498 GLY ASN ARG PRO GLU ARG GLU ALA ILE ALA ASN GLU MET
SEQRES 35 A 498 HIS TYR ALA TRP LEU SER PHE ALA ARG THR GLY ASP PRO
SEQRES 36 A 498 ASN GLY ALA HIS LEU PRO GLU ALA TRP PRO ALA TYR THR
SEQRES 37 A 498 ASN GLU ARG LYS ALA ALA PHE VAL PHE SER ALA ALA SER
SEQRES 38 A 498 HIS VAL GLU ASP ASP PRO PHE GLY ARG GLU ARG ALA ALA
SEQRES 39 A 498 TRP GLN GLY ARG
MODRES 2OGS 0CS A 408 ALA 3-[(S)-HYDROPEROXYSULFINYL]-L-ALANINE
HET 0CS A 408 9
HET IOD 501 1
HET IOD 502 1
HET IOD 503 1
HETNAM 0CS 3-[(S)-HYDROPEROXYSULFINYL]-L-ALANINE
HETNAM IOD IODIDE ION
FORMUL 1 0CS C3 H7 N1 O5 S1
FORMUL 2 IOD 3(I1 1-)
FORMUL 5 HOH *151(H2 O1)
HELIX 1 1 VAL A 34 ARG A 38 5 5
HELIX 2 2 SER A 117 ASP A 121 5 5
HELIX 3 3 GLY A 122 ASP A 130 1 9
HELIX 4 4 MET A 140 PHE A 145 1 6
HELIX 5 5 GLY A 153 ALA A 157 5 5
HELIX 6 6 GLN A 158 GLY A 160 5 3
HELIX 7 7 ASN A 161 ILE A 178 1 18
HELIX 8 8 ALA A 179 PHE A 181 5 3
HELIX 9 9 SER A 194 LEU A 206 1 13
HELIX 10 10 PRO A 207 SER A 210 5 4
HELIX 11 11 SER A 229 GLY A 245 1 17
HELIX 12 12 ASP A 250 ILE A 257 1 8
HELIX 13 13 PRO A 258 SER A 268 1 11
HELIX 14 14 LEU A 269 VAL A 273 5 5
HELIX 15 15 HIS A 287 TYR A 294 1 8
HELIX 16 16 ASP A 309 THR A 317 5 9
HELIX 17 17 ASP A 318 LEU A 324 5 7
HELIX 18 18 GLY A 325 GLY A 338 1 14
HELIX 19 19 PRO A 341 ALA A 352 1 12
HELIX 20 20 PRO A 357 PHE A 371 1 15
HELIX 21 21 PHE A 371 GLN A 385 1 15
HELIX 22 22 GLU A 412 HIS A 418 1 7
HELIX 23 23 ASN A 431 GLY A 453 1 23
HELIX 24 24 PHE A 488 GLN A 496 1 9
SHEET 1 A 3 VAL A 5 THR A 8 0
SHEET 2 A 3 GLY A 11 ARG A 14 -1 O LEU A 13 N VAL A 6
SHEET 3 A 3 VAL A 51 GLU A 53 1 O ARG A 52 N ARG A 12
SHEET 1 B11 GLU A 16 ASN A 18 0
SHEET 2 B11 VAL A 21 PRO A 28 -1 O VAL A 21 N ASN A 18
SHEET 3 B11 TYR A 86 SER A 91 -1 O SER A 91 N PHE A 22
SHEET 4 B11 VAL A 132 ILE A 136 -1 O VAL A 133 N TRP A 90
SHEET 5 B11 ARG A 99 ILE A 105 1 N TRP A 104 O VAL A 134
SHEET 6 B11 GLY A 183 GLU A 193 1 O THR A 189 N VAL A 101
SHEET 7 B11 ARG A 215 GLN A 219 1 O GLN A 219 N GLY A 192
SHEET 8 B11 ILE A 302 THR A 307 1 O LEU A 303 N LEU A 218
SHEET 9 B11 VAL A 389 PHE A 394 1 O PHE A 394 N VAL A 306
SHEET 10 B11 ALA A 473 PHE A 477 1 O PHE A 475 N MET A 391
SHEET 11 B11 HIS A 482 ASP A 485 -1 O HIS A 482 N VAL A 476
CISPEP 1 GLY A 338 PRO A 339 0 -0.24
CRYST1 69.530 73.490 99.030 90.00 90.00 90.00 P 21 21 21 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 0.014382 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013607 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010098 0.00000
TER 3866 GLN A 496
MASTER 300 0 4 24 14 0 0 6 4019 1 9 39
END |