HEADER HYDROLASE/HYDROLASE INHIBITOR 05-FEB-10 3LPG
TITLE STRUCTURE OF E. COLI BETA-GLUCURONIDASE BOUND WITH A NOVEL, POTENT
TITLE 2 INHIBITOR 3-(2-FLUOROPHENYL)-1-(2-HYDROXYETHYL)-1-((6-METHYL-2-OXO-1,
TITLE 3 2-DIHYDROQUINOLIN-3-YL)METHYL)UREA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BETA-GLUCURONIDASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: GUS, BETA-D-GLUCURONOSIDE GLUCURONOSOHYDROLASE;
COMPND 5 EC: 3.2.1.31;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 STRAIN: K-12;
SOURCE 5 GENE: B1617, GURA, GUSA, JW1609, UIDA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS ALPHA/BETA BARREL, SUGAR-BINDING DOMAIN, BETA-SANDWICH DOMAIN,
KEYWDS 2 GLYCOSYL HYDROLASE, GLYCOSIDASE, HYDROLASE, HYDROLASE-HYDROLASE
KEYWDS 3 INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR B.D.WALLACE,M.R.REDINBO
REVDAT 4 22-NOV-23 3LPG 1 REMARK
REVDAT 3 06-SEP-23 3LPG 1 REMARK SEQADV LINK
REVDAT 2 01-NOV-17 3LPG 1 REMARK
REVDAT 1 17-NOV-10 3LPG 0
JRNL AUTH B.D.WALLACE,H.WANG,K.T.LANE,J.E.SCOTT,J.ORANS,J.S.KOO,
JRNL AUTH 2 M.VENKATESH,C.JOBIN,L.A.YEH,S.MANI,M.R.REDINBO
JRNL TITL ALLEVIATING CANCER DRUG TOXICITY BY INHIBITING A BACTERIAL
JRNL TITL 2 ENZYME.
JRNL REF SCIENCE V. 330 831 2010
JRNL REFN ISSN 0036-8075
JRNL PMID 21051639
JRNL DOI 10.1126/SCIENCE.1191175
REMARK 2
REMARK 2 RESOLUTION. 2.43 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.43
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.86
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.100
REMARK 3 COMPLETENESS FOR RANGE (%) : 89.5
REMARK 3 NUMBER OF REFLECTIONS : 44902
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.206
REMARK 3 R VALUE (WORKING SET) : 0.204
REMARK 3 FREE R VALUE : 0.246
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.090
REMARK 3 FREE R VALUE TEST SET COUNT : 2287
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 30.8620 - 6.0950 0.94 2915 146 0.1630 0.1710
REMARK 3 2 6.0950 - 4.8440 0.97 2915 153 0.1610 0.1870
REMARK 3 3 4.8440 - 4.2330 0.98 2916 169 0.1480 0.1910
REMARK 3 4 4.2330 - 3.8470 0.97 2853 194 0.1610 0.2040
REMARK 3 5 3.8470 - 3.5720 0.95 2869 142 0.1810 0.2480
REMARK 3 6 3.5720 - 3.3610 0.96 2839 148 0.1990 0.2350
REMARK 3 7 3.3610 - 3.1930 0.94 2841 129 0.2130 0.2890
REMARK 3 8 3.1930 - 3.0540 0.93 2740 163 0.2300 0.3020
REMARK 3 9 3.0540 - 2.9370 0.90 2685 138 0.2380 0.3040
REMARK 3 10 2.9370 - 2.8360 0.89 2624 128 0.2560 0.3030
REMARK 3 11 2.8360 - 2.7470 0.87 2581 138 0.2630 0.3290
REMARK 3 12 2.7470 - 2.6680 0.85 2512 122 0.2790 0.3640
REMARK 3 13 2.6680 - 2.5980 0.82 2415 124 0.3050 0.4190
REMARK 3 14 2.5980 - 2.5350 0.80 2377 129 0.3160 0.3700
REMARK 3 15 2.5350 - 2.4770 0.78 2273 136 0.3060 0.3650
REMARK 3 16 2.4770 - 2.4250 0.77 2260 128 0.3200 0.3890
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : 0.27
REMARK 3 B_SOL : 33.97
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 2.410
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 70.73
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -17.76300
REMARK 3 B22 (A**2) : 21.64100
REMARK 3 B33 (A**2) : -7.91000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 2.66500
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.004 9973
REMARK 3 ANGLE : 1.023 13570
REMARK 3 CHIRALITY : 0.088 1427
REMARK 3 PLANARITY : 0.007 1772
REMARK 3 DIHEDRAL : 19.352 3522
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): -11.6434 2.3831 22.3271
REMARK 3 T TENSOR
REMARK 3 T11: 0.1479 T22: 0.2818
REMARK 3 T33: 0.1285 T12: -0.0008
REMARK 3 T13: -0.0123 T23: 0.2897
REMARK 3 L TENSOR
REMARK 3 L11: 2.4641 L22: 0.4793
REMARK 3 L33: 0.3654 L12: 0.0260
REMARK 3 L13: -0.0903 L23: -0.0165
REMARK 3 S TENSOR
REMARK 3 S11: 0.0858 S12: -1.1891 S13: -0.3878
REMARK 3 S21: 0.0376 S22: -0.0385 S23: 0.0121
REMARK 3 S31: -0.0285 S32: 0.0375 S33: -0.0205
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3LPG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-FEB-10.
REMARK 100 THE DEPOSITION ID IS D_1000057566.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-NOV-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, X-GEN
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, X-GEN
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 44902
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.425
REMARK 200 RESOLUTION RANGE LOW (A) : 30.859
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 89.5
REMARK 200 DATA REDUNDANCY : 3.900
REMARK 200 R MERGE (I) : 0.13690
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 26.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.43
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.48
REMARK 200 COMPLETENESS FOR SHELL (%) : 77.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.90
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 3K4D
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.86
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15% PEG 3350, 0.2 M MGACETATE, 0.02%
REMARK 280 SODIUM AZIDE, 5 MM 3-(2-FLUOROPHENYL)-1-(2-HYDROXYETHYL)-1-((6-
REMARK 280 METHYL-2-OXO-1,2-DIHYDROQUINOLIN-3-YL)METHYL)UREA, PH 7.4, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 83.90700
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 38.46700
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 83.90700
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 38.46700
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 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
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 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 15210 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 80750 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -92.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 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 B 700 LIES ON A SPECIAL POSITION.
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 LYS A 602
REMARK 465 GLN A 603
REMARK 465 LYS B 602
REMARK 465 GLN B 603
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 ILE A 363 CG1 CG2 CD1
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 DISTANCE
REMARK 500 O LEU B 361 OAC Z78 B 604 1.77
REMARK 500 O ALA A 90 O HOH A 650 1.78
REMARK 500 O GLU A 378 O HOH A 625 1.86
REMARK 500 O ASP A 24 OH TYR A 63 1.87
REMARK 500 O GLU B 378 O HOH B 647 1.92
REMARK 500 O ALA B 367 O HOH B 676 1.98
REMARK 500 O THR A 7 O HOH A 792 2.00
REMARK 500 O LEU A 361 OAC Z78 A 604 2.09
REMARK 500 O GLN A 108 O HOH A 666 2.10
REMARK 500 O MSE A 520 O HOH A 826 2.11
REMARK 500 O ASP B 538 O GLN B 599 2.12
REMARK 500 O ALA B 90 O HOH B 715 2.12
REMARK 500 O GLN A 195 O HOH A 669 2.17
REMARK 500 CD1 LEU A 15 OG SER A 173 2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OE1 GLU B 366 O HOH A 839 2555 1.87
REMARK 500
REMARK 500 REMARK: NULL
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 PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 PRO A 8 C - N - CD ANGL. DEV. = -13.7 DEGREES
REMARK 500 LEU A 15 N - CA - C ANGL. DEV. = -19.0 DEGREES
REMARK 500 ASP A 24 N - CA - C ANGL. DEV. = -17.2 DEGREES
REMARK 500 PRO A 48 C - N - CD ANGL. DEV. = -13.3 DEGREES
REMARK 500 ALA A 90 CB - CA - C ANGL. DEV. = 15.6 DEGREES
REMARK 500 TYR A 94 N - CA - CB ANGL. DEV. = -11.3 DEGREES
REMARK 500 ASN A 101 CB - CA - C ANGL. DEV. = -15.3 DEGREES
REMARK 500 GLN A 108 N - CA - C ANGL. DEV. = 24.2 DEGREES
REMARK 500 CYS A 197 CB - CA - C ANGL. DEV. = 14.4 DEGREES
REMARK 500 CYS A 197 N - CA - C ANGL. DEV. = -39.6 DEGREES
REMARK 500 ASN A 198 CB - CA - C ANGL. DEV. = -28.7 DEGREES
REMARK 500 ASN A 198 N - CA - CB ANGL. DEV. = -17.3 DEGREES
REMARK 500 ASN A 198 N - CA - C ANGL. DEV. = 34.8 DEGREES
REMARK 500 HIS A 199 CB - CA - C ANGL. DEV. = -16.9 DEGREES
REMARK 500 HIS A 199 N - CA - CB ANGL. DEV. = -16.4 DEGREES
REMARK 500 HIS A 199 N - CA - C ANGL. DEV. = 16.2 DEGREES
REMARK 500 ALA A 200 N - CA - CB ANGL. DEV. = -11.4 DEGREES
REMARK 500 SER A 201 N - CA - CB ANGL. DEV. = -10.0 DEGREES
REMARK 500 ASN A 209 N - CA - C ANGL. DEV. = 19.5 DEGREES
REMARK 500 THR A 230 CB - CA - C ANGL. DEV. = -34.1 DEGREES
REMARK 500 SER A 231 CB - CA - C ANGL. DEV. = 14.5 DEGREES
REMARK 500 GLY A 232 N - CA - C ANGL. DEV. = 16.8 DEGREES
REMARK 500 PHE A 357 CB - CA - C ANGL. DEV. = 12.7 DEGREES
REMARK 500 ASN A 358 N - CA - CB ANGL. DEV. = -13.0 DEGREES
REMARK 500 GLU A 366 CB - CA - C ANGL. DEV. = 14.7 DEGREES
REMARK 500 GLU A 366 N - CA - C ANGL. DEV. = -31.1 DEGREES
REMARK 500 ALA A 367 N - CA - CB ANGL. DEV. = -12.9 DEGREES
REMARK 500 GLU A 378 CB - CA - C ANGL. DEV. = 13.2 DEGREES
REMARK 500 ALA A 379 CB - CA - C ANGL. DEV. = -13.3 DEGREES
REMARK 500 ALA A 379 N - CA - C ANGL. DEV. = 30.0 DEGREES
REMARK 500 VAL A 380 N - CA - C ANGL. DEV. = -17.1 DEGREES
REMARK 500 MSE A 520 N - CA - C ANGL. DEV. = 16.4 DEGREES
REMARK 500 ASN A 550 C - N - CA ANGL. DEV. = -16.6 DEGREES
REMARK 500 PHE A 551 N - CA - CB ANGL. DEV. = -29.1 DEGREES
REMARK 500 GLN A 598 N - CA - C ANGL. DEV. = -33.7 DEGREES
REMARK 500 GLN A 599 N - CA - CB ANGL. DEV. = -23.1 DEGREES
REMARK 500 GLU B 6 CB - CA - C ANGL. DEV. = -21.9 DEGREES
REMARK 500 GLU B 6 N - CA - C ANGL. DEV. = 46.3 DEGREES
REMARK 500 THR B 7 N - CA - CB ANGL. DEV. = -17.1 DEGREES
REMARK 500 THR B 7 N - CA - C ANGL. DEV. = 31.5 DEGREES
REMARK 500 LEU B 15 CB - CA - C ANGL. DEV. = -31.4 DEGREES
REMARK 500 ASP B 16 N - CA - C ANGL. DEV. = -33.3 DEGREES
REMARK 500 LEU B 18 N - CA - C ANGL. DEV. = 30.7 DEGREES
REMARK 500 TRP B 79 N - CA - C ANGL. DEV. = -17.0 DEGREES
REMARK 500 ALA B 80 CB - CA - C ANGL. DEV. = -34.2 DEGREES
REMARK 500 ALA B 90 CB - CA - C ANGL. DEV. = 12.9 DEGREES
REMARK 500 TYR B 94 N - CA - CB ANGL. DEV. = -12.4 DEGREES
REMARK 500 CYS B 197 CB - CA - C ANGL. DEV. = 9.3 DEGREES
REMARK 500 ASN B 198 CB - CA - C ANGL. DEV. = -23.2 DEGREES
REMARK 500 HIS B 199 CB - CA - C ANGL. DEV. = -12.2 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 80 ANGLE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 HIS A 93 -126.16 51.48
REMARK 500 SER A 231 -62.03 75.10
REMARK 500 LEU A 301 -55.98 73.81
REMARK 500 PRO A 418 153.68 -47.57
REMARK 500 TRP A 471 -80.69 -120.76
REMARK 500 HIS B 93 -122.96 56.54
REMARK 500 ASN B 100 -122.31 51.96
REMARK 500 GLN B 141 30.22 -99.13
REMARK 500 PRO B 180 174.30 -59.61
REMARK 500 ASN B 198 140.33 -174.44
REMARK 500 HIS B 199 169.94 173.79
REMARK 500 LEU B 301 -55.10 75.69
REMARK 500 PHE B 357 -8.40 -52.68
REMARK 500 PRO B 371 159.63 -47.24
REMARK 500 MSE B 407 146.28 -171.36
REMARK 500 PRO B 418 178.83 -54.66
REMARK 500 TRP B 471 -80.92 -118.50
REMARK 500 TRP B 549 -162.99 -75.06
REMARK 500 GLN B 599 -54.33 74.12
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 VAL A 47 PRO A 48 101.92
REMARK 500 ILE A 143 PRO A 144 109.14
REMARK 500 VAL B 47 PRO B 48 106.70
REMARK 500 ASN B 369 LYS B 370 -138.58
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE Z78 B 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE Z78 A 604
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3K4A RELATED DB: PDB
REMARK 900 SELENOMETHIONINE SUBSTITUTED BETA-GLUCURONIDASE CRYSTAL STRUCTURE
REMARK 900 RELATED ID: 3K46 RELATED DB: PDB
REMARK 900 NATIVE CRYSTAL STRUCTURE OF FULL-LENGTH BETA-GLUCURONIDASE
REMARK 900 RELATED ID: 3K4D RELATED DB: PDB
REMARK 900 STRUCTURE OF E. COLI BETA-GLUCURONIDASE BOUND WITH GLUCARO-D-LACTAM
REMARK 900 INHIBITOR
REMARK 900 RELATED ID: 3LPF RELATED DB: PDB
REMARK 900 STRUCTURE OF E. COLI BETA-GLUCURONIDASE BOUND WITH A NOVEL, POTENT
REMARK 900 INHIBITOR 2
DBREF 3LPG A 1 603 UNP P05804 BGLR_ECOLI 1 603
DBREF 3LPG B 1 603 UNP P05804 BGLR_ECOLI 1 603
SEQADV 3LPG SER A -1 UNP P05804 EXPRESSION TAG
SEQADV 3LPG HIS A 0 UNP P05804 EXPRESSION TAG
SEQADV 3LPG SER B -1 UNP P05804 EXPRESSION TAG
SEQADV 3LPG HIS B 0 UNP P05804 EXPRESSION TAG
SEQRES 1 A 605 SER HIS MSE LEU ARG PRO VAL GLU THR PRO THR ARG GLU
SEQRES 2 A 605 ILE LYS LYS LEU ASP GLY LEU TRP ALA PHE SER LEU ASP
SEQRES 3 A 605 ARG GLU ASN CYS GLY ILE ASP GLN ARG TRP TRP GLU SER
SEQRES 4 A 605 ALA LEU GLN GLU SER ARG ALA ILE ALA VAL PRO GLY SER
SEQRES 5 A 605 PHE ASN ASP GLN PHE ALA ASP ALA ASP ILE ARG ASN TYR
SEQRES 6 A 605 ALA GLY ASN VAL TRP TYR GLN ARG GLU VAL PHE ILE PRO
SEQRES 7 A 605 LYS GLY TRP ALA GLY GLN ARG ILE VAL LEU ARG PHE ASP
SEQRES 8 A 605 ALA VAL THR HIS TYR GLY LYS VAL TRP VAL ASN ASN GLN
SEQRES 9 A 605 GLU VAL MSE GLU HIS GLN GLY GLY TYR THR PRO PHE GLU
SEQRES 10 A 605 ALA ASP VAL THR PRO TYR VAL ILE ALA GLY LYS SER VAL
SEQRES 11 A 605 ARG ILE THR VAL CYS VAL ASN ASN GLU LEU ASN TRP GLN
SEQRES 12 A 605 THR ILE PRO PRO GLY MSE VAL ILE THR ASP GLU ASN GLY
SEQRES 13 A 605 LYS LYS LYS GLN SER TYR PHE HIS ASP PHE PHE ASN TYR
SEQRES 14 A 605 ALA GLY ILE HIS ARG SER VAL MSE LEU TYR THR THR PRO
SEQRES 15 A 605 ASN THR TRP VAL ASP ASP ILE THR VAL VAL THR HIS VAL
SEQRES 16 A 605 ALA GLN ASP CYS ASN HIS ALA SER VAL ASP TRP GLN VAL
SEQRES 17 A 605 VAL ALA ASN GLY ASP VAL SER VAL GLU LEU ARG ASP ALA
SEQRES 18 A 605 ASP GLN GLN VAL VAL ALA THR GLY GLN GLY THR SER GLY
SEQRES 19 A 605 THR LEU GLN VAL VAL ASN PRO HIS LEU TRP GLN PRO GLY
SEQRES 20 A 605 GLU GLY TYR LEU TYR GLU LEU CYS VAL THR ALA LYS SER
SEQRES 21 A 605 GLN THR GLU CYS ASP ILE TYR PRO LEU ARG VAL GLY ILE
SEQRES 22 A 605 ARG SER VAL ALA VAL LYS GLY GLU GLN PHE LEU ILE ASN
SEQRES 23 A 605 HIS LYS PRO PHE TYR PHE THR GLY PHE GLY ARG HIS GLU
SEQRES 24 A 605 ASP ALA ASP LEU ARG GLY LYS GLY PHE ASP ASN VAL LEU
SEQRES 25 A 605 MSE VAL HIS ASP HIS ALA LEU MSE ASP TRP ILE GLY ALA
SEQRES 26 A 605 ASN SER TYR ARG THR SER HIS TYR PRO TYR ALA GLU GLU
SEQRES 27 A 605 MSE LEU ASP TRP ALA ASP GLU HIS GLY ILE VAL VAL ILE
SEQRES 28 A 605 ASP GLU THR ALA ALA VAL GLY PHE ASN LEU SER LEU GLY
SEQRES 29 A 605 ILE GLY PHE GLU ALA GLY ASN LYS PRO LYS GLU LEU TYR
SEQRES 30 A 605 SER GLU GLU ALA VAL ASN GLY GLU THR GLN GLN ALA HIS
SEQRES 31 A 605 LEU GLN ALA ILE LYS GLU LEU ILE ALA ARG ASP LYS ASN
SEQRES 32 A 605 HIS PRO SER VAL VAL MSE TRP SER ILE ALA ASN GLU PRO
SEQRES 33 A 605 ASP THR ARG PRO GLN GLY ALA ARG GLU TYR PHE ALA PRO
SEQRES 34 A 605 LEU ALA GLU ALA THR ARG LYS LEU ASP PRO THR ARG PRO
SEQRES 35 A 605 ILE THR CYS VAL ASN VAL MSE PHE CYS ASP ALA HIS THR
SEQRES 36 A 605 ASP THR ILE SER ASP LEU PHE ASP VAL LEU CYS LEU ASN
SEQRES 37 A 605 ARG TYR TYR GLY TRP TYR VAL GLN SER GLY ASP LEU GLU
SEQRES 38 A 605 THR ALA GLU LYS VAL LEU GLU LYS GLU LEU LEU ALA TRP
SEQRES 39 A 605 GLN GLU LYS LEU HIS GLN PRO ILE ILE ILE THR GLU TYR
SEQRES 40 A 605 GLY VAL ASP THR LEU ALA GLY LEU HIS SER MSE TYR THR
SEQRES 41 A 605 ASP MSE TRP SER GLU GLU TYR GLN CYS ALA TRP LEU ASP
SEQRES 42 A 605 MSE TYR HIS ARG VAL PHE ASP ARG VAL SER ALA VAL VAL
SEQRES 43 A 605 GLY GLU GLN VAL TRP ASN PHE ALA ASP PHE ALA THR SER
SEQRES 44 A 605 GLN GLY ILE LEU ARG VAL GLY GLY ASN LYS LYS GLY ILE
SEQRES 45 A 605 PHE THR ARG ASP ARG LYS PRO LYS SER ALA ALA PHE LEU
SEQRES 46 A 605 LEU GLN LYS ARG TRP THR GLY MSE ASN PHE GLY GLU LYS
SEQRES 47 A 605 PRO GLN GLN GLY GLY LYS GLN
SEQRES 1 B 605 SER HIS MSE LEU ARG PRO VAL GLU THR PRO THR ARG GLU
SEQRES 2 B 605 ILE LYS LYS LEU ASP GLY LEU TRP ALA PHE SER LEU ASP
SEQRES 3 B 605 ARG GLU ASN CYS GLY ILE ASP GLN ARG TRP TRP GLU SER
SEQRES 4 B 605 ALA LEU GLN GLU SER ARG ALA ILE ALA VAL PRO GLY SER
SEQRES 5 B 605 PHE ASN ASP GLN PHE ALA ASP ALA ASP ILE ARG ASN TYR
SEQRES 6 B 605 ALA GLY ASN VAL TRP TYR GLN ARG GLU VAL PHE ILE PRO
SEQRES 7 B 605 LYS GLY TRP ALA GLY GLN ARG ILE VAL LEU ARG PHE ASP
SEQRES 8 B 605 ALA VAL THR HIS TYR GLY LYS VAL TRP VAL ASN ASN GLN
SEQRES 9 B 605 GLU VAL MSE GLU HIS GLN GLY GLY TYR THR PRO PHE GLU
SEQRES 10 B 605 ALA ASP VAL THR PRO TYR VAL ILE ALA GLY LYS SER VAL
SEQRES 11 B 605 ARG ILE THR VAL CYS VAL ASN ASN GLU LEU ASN TRP GLN
SEQRES 12 B 605 THR ILE PRO PRO GLY MSE VAL ILE THR ASP GLU ASN GLY
SEQRES 13 B 605 LYS LYS LYS GLN SER TYR PHE HIS ASP PHE PHE ASN TYR
SEQRES 14 B 605 ALA GLY ILE HIS ARG SER VAL MSE LEU TYR THR THR PRO
SEQRES 15 B 605 ASN THR TRP VAL ASP ASP ILE THR VAL VAL THR HIS VAL
SEQRES 16 B 605 ALA GLN ASP CYS ASN HIS ALA SER VAL ASP TRP GLN VAL
SEQRES 17 B 605 VAL ALA ASN GLY ASP VAL SER VAL GLU LEU ARG ASP ALA
SEQRES 18 B 605 ASP GLN GLN VAL VAL ALA THR GLY GLN GLY THR SER GLY
SEQRES 19 B 605 THR LEU GLN VAL VAL ASN PRO HIS LEU TRP GLN PRO GLY
SEQRES 20 B 605 GLU GLY TYR LEU TYR GLU LEU CYS VAL THR ALA LYS SER
SEQRES 21 B 605 GLN THR GLU CYS ASP ILE TYR PRO LEU ARG VAL GLY ILE
SEQRES 22 B 605 ARG SER VAL ALA VAL LYS GLY GLU GLN PHE LEU ILE ASN
SEQRES 23 B 605 HIS LYS PRO PHE TYR PHE THR GLY PHE GLY ARG HIS GLU
SEQRES 24 B 605 ASP ALA ASP LEU ARG GLY LYS GLY PHE ASP ASN VAL LEU
SEQRES 25 B 605 MSE VAL HIS ASP HIS ALA LEU MSE ASP TRP ILE GLY ALA
SEQRES 26 B 605 ASN SER TYR ARG THR SER HIS TYR PRO TYR ALA GLU GLU
SEQRES 27 B 605 MSE LEU ASP TRP ALA ASP GLU HIS GLY ILE VAL VAL ILE
SEQRES 28 B 605 ASP GLU THR ALA ALA VAL GLY PHE ASN LEU SER LEU GLY
SEQRES 29 B 605 ILE GLY PHE GLU ALA GLY ASN LYS PRO LYS GLU LEU TYR
SEQRES 30 B 605 SER GLU GLU ALA VAL ASN GLY GLU THR GLN GLN ALA HIS
SEQRES 31 B 605 LEU GLN ALA ILE LYS GLU LEU ILE ALA ARG ASP LYS ASN
SEQRES 32 B 605 HIS PRO SER VAL VAL MSE TRP SER ILE ALA ASN GLU PRO
SEQRES 33 B 605 ASP THR ARG PRO GLN GLY ALA ARG GLU TYR PHE ALA PRO
SEQRES 34 B 605 LEU ALA GLU ALA THR ARG LYS LEU ASP PRO THR ARG PRO
SEQRES 35 B 605 ILE THR CYS VAL ASN VAL MSE PHE CYS ASP ALA HIS THR
SEQRES 36 B 605 ASP THR ILE SER ASP LEU PHE ASP VAL LEU CYS LEU ASN
SEQRES 37 B 605 ARG TYR TYR GLY TRP TYR VAL GLN SER GLY ASP LEU GLU
SEQRES 38 B 605 THR ALA GLU LYS VAL LEU GLU LYS GLU LEU LEU ALA TRP
SEQRES 39 B 605 GLN GLU LYS LEU HIS GLN PRO ILE ILE ILE THR GLU TYR
SEQRES 40 B 605 GLY VAL ASP THR LEU ALA GLY LEU HIS SER MSE TYR THR
SEQRES 41 B 605 ASP MSE TRP SER GLU GLU TYR GLN CYS ALA TRP LEU ASP
SEQRES 42 B 605 MSE TYR HIS ARG VAL PHE ASP ARG VAL SER ALA VAL VAL
SEQRES 43 B 605 GLY GLU GLN VAL TRP ASN PHE ALA ASP PHE ALA THR SER
SEQRES 44 B 605 GLN GLY ILE LEU ARG VAL GLY GLY ASN LYS LYS GLY ILE
SEQRES 45 B 605 PHE THR ARG ASP ARG LYS PRO LYS SER ALA ALA PHE LEU
SEQRES 46 B 605 LEU GLN LYS ARG TRP THR GLY MSE ASN PHE GLY GLU LYS
SEQRES 47 B 605 PRO GLN GLN GLY GLY LYS GLN
MODRES 3LPG MSE A 1 MET SELENOMETHIONINE
MODRES 3LPG MSE A 105 MET SELENOMETHIONINE
MODRES 3LPG MSE A 147 MET SELENOMETHIONINE
MODRES 3LPG MSE A 175 MET SELENOMETHIONINE
MODRES 3LPG MSE A 311 MET SELENOMETHIONINE
MODRES 3LPG MSE A 318 MET SELENOMETHIONINE
MODRES 3LPG MSE A 337 MET SELENOMETHIONINE
MODRES 3LPG MSE A 407 MET SELENOMETHIONINE
MODRES 3LPG MSE A 447 MET SELENOMETHIONINE
MODRES 3LPG MSE A 516 MET SELENOMETHIONINE
MODRES 3LPG MSE A 520 MET SELENOMETHIONINE
MODRES 3LPG MSE A 532 MET SELENOMETHIONINE
MODRES 3LPG MSE A 591 MET SELENOMETHIONINE
MODRES 3LPG MSE B 1 MET SELENOMETHIONINE
MODRES 3LPG MSE B 105 MET SELENOMETHIONINE
MODRES 3LPG MSE B 147 MET SELENOMETHIONINE
MODRES 3LPG MSE B 175 MET SELENOMETHIONINE
MODRES 3LPG MSE B 311 MET SELENOMETHIONINE
MODRES 3LPG MSE B 318 MET SELENOMETHIONINE
MODRES 3LPG MSE B 337 MET SELENOMETHIONINE
MODRES 3LPG MSE B 407 MET SELENOMETHIONINE
MODRES 3LPG MSE B 447 MET SELENOMETHIONINE
MODRES 3LPG MSE B 516 MET SELENOMETHIONINE
MODRES 3LPG MSE B 520 MET SELENOMETHIONINE
MODRES 3LPG MSE B 532 MET SELENOMETHIONINE
MODRES 3LPG MSE B 591 MET SELENOMETHIONINE
HET MSE A 1 8
HET MSE A 105 8
HET MSE A 147 8
HET MSE A 175 8
HET MSE A 311 8
HET MSE A 318 8
HET MSE A 337 8
HET MSE A 407 8
HET MSE A 447 8
HET MSE A 516 8
HET MSE A 520 8
HET MSE A 532 8
HET MSE A 591 8
HET MSE B 1 8
HET MSE B 105 8
HET MSE B 147 8
HET MSE B 175 8
HET MSE B 311 8
HET MSE B 318 8
HET MSE B 337 8
HET MSE B 407 8
HET MSE B 447 8
HET MSE B 516 8
HET MSE B 520 8
HET MSE B 532 8
HET MSE B 591 8
HET Z78 A 604 27
HET Z78 B 604 27
HETNAM MSE SELENOMETHIONINE
HETNAM Z78 3-(2-FLUOROPHENYL)-1-(2-HYDROXYETHYL)-1-[(6-METHYL-2-
HETNAM 2 Z78 OXO-1,2-DIHYDROQUINOLIN-3-YL)METHYL]UREA
FORMUL 1 MSE 26(C5 H11 N O2 SE)
FORMUL 3 Z78 2(C20 H20 F N3 O3)
FORMUL 5 HOH *358(H2 O)
HELIX 1 1 ARG A 33 SER A 37 5 5
HELIX 2 2 ASN A 52 ALA A 56 5 5
HELIX 3 3 ASP A 57 ASN A 62 1 6
HELIX 4 4 PRO A 76 ALA A 80 5 5
HELIX 5 5 THR A 119 VAL A 122 5 4
HELIX 6 6 ASP A 307 GLY A 322 1 16
HELIX 7 7 ALA A 334 GLY A 345 1 12
HELIX 8 8 ASN A 381 LYS A 400 1 20
HELIX 9 9 GLN A 419 ASP A 436 1 18
HELIX 10 10 ILE A 456 PHE A 460 5 5
HELIX 11 11 ASP A 477 HIS A 497 1 21
HELIX 12 12 SER A 522 ASP A 538 1 17
HELIX 13 13 SER A 579 MSE A 591 1 13
HELIX 14 14 ARG B 33 SER B 37 5 5
HELIX 15 15 ASP B 57 ASN B 62 1 6
HELIX 16 16 THR B 119 VAL B 122 5 4
HELIX 17 17 ASP B 307 GLY B 322 1 16
HELIX 18 18 ALA B 334 GLY B 345 1 12
HELIX 19 19 ASN B 381 LYS B 400 1 20
HELIX 20 20 GLY B 420 ASP B 436 1 17
HELIX 21 21 ILE B 456 PHE B 460 5 5
HELIX 22 22 ASP B 477 HIS B 497 1 21
HELIX 23 23 SER B 522 ASP B 538 1 17
HELIX 24 24 LYS B 578 MSE B 591 1 14
SHEET 1 A 4 GLU A 11 ILE A 12 0
SHEET 2 A 4 VAL A 174 THR A 179 -1 O LEU A 176 N ILE A 12
SHEET 3 A 4 ARG A 83 PHE A 88 -1 N VAL A 85 O TYR A 177
SHEET 4 A 4 PHE A 114 ASP A 117 -1 O PHE A 114 N PHE A 88
SHEET 1 B 6 ARG A 43 ALA A 46 0
SHEET 2 B 6 LEU A 18 ASP A 24 -1 N PHE A 21 O ARG A 43
SHEET 3 B 6 ASN A 66 PHE A 74 -1 O GLN A 70 N ALA A 20
SHEET 4 B 6 SER A 127 ASN A 135 -1 O VAL A 134 N VAL A 67
SHEET 5 B 6 TYR A 94 VAL A 99 -1 N TYR A 94 O ASN A 135
SHEET 6 B 6 GLU A 103 HIS A 107 -1 O VAL A 104 N VAL A 97
SHEET 1 C 2 GLY A 146 THR A 150 0
SHEET 2 C 2 LYS A 156 TYR A 160 -1 O LYS A 157 N ILE A 149
SHEET 1 D 3 TRP A 183 THR A 191 0
SHEET 2 D 3 SER A 201 ALA A 208 -1 O VAL A 206 N ASP A 186
SHEET 3 D 3 THR A 233 GLN A 235 -1 O THR A 233 N ASP A 203
SHEET 1 E 4 VAL A 223 GLN A 228 0
SHEET 2 E 4 ASP A 211 ARG A 217 -1 N LEU A 216 O VAL A 224
SHEET 3 E 4 TYR A 250 LYS A 257 -1 O LYS A 257 N ASP A 211
SHEET 4 E 4 CYS A 262 VAL A 269 -1 O TYR A 265 N VAL A 254
SHEET 1 F 3 VAL A 274 LYS A 277 0
SHEET 2 F 3 GLN A 280 ILE A 283 -1 O LEU A 282 N ALA A 275
SHEET 3 F 3 LYS A 286 PRO A 287 -1 O LYS A 286 N ILE A 283
SHEET 1 G 8 ILE A 441 VAL A 444 0
SHEET 2 G 8 VAL A 405 ASN A 412 1 N ILE A 410 O THR A 442
SHEET 3 G 8 VAL A 347 GLU A 351 1 N ASP A 350 O SER A 409
SHEET 4 G 8 SER A 325 ARG A 327 1 N TYR A 326 O ILE A 349
SHEET 5 G 8 PHE A 290 GLY A 294 1 N THR A 291 O SER A 325
SHEET 6 G 8 VAL A 543 VAL A 548 1 O VAL A 548 N GLY A 294
SHEET 7 G 8 ILE A 500 GLU A 504 1 N ILE A 500 O VAL A 544
SHEET 8 G 8 LEU A 463 ASN A 466 1 N LEU A 463 O ILE A 501
SHEET 1 H 2 ASN A 550 ALA A 552 0
SHEET 2 H 2 GLY A 569 PHE A 571 1 O PHE A 571 N PHE A 551
SHEET 1 I 4 GLU B 11 LYS B 13 0
SHEET 2 I 4 VAL B 174 THR B 179 -1 O LEU B 176 N ILE B 12
SHEET 3 I 4 ARG B 83 PHE B 88 -1 N ARG B 83 O THR B 179
SHEET 4 I 4 PHE B 114 ASP B 117 -1 O PHE B 114 N PHE B 88
SHEET 1 J 6 ARG B 43 ILE B 45 0
SHEET 2 J 6 TRP B 19 LEU B 23 -1 N PHE B 21 O ARG B 43
SHEET 3 J 6 ASN B 66 PHE B 74 -1 O GLN B 70 N ALA B 20
SHEET 4 J 6 SER B 127 ASN B 135 -1 O ILE B 130 N ARG B 71
SHEET 5 J 6 TYR B 94 VAL B 99 -1 N LYS B 96 O CYS B 133
SHEET 6 J 6 GLN B 102 HIS B 107 -1 O GLN B 102 N VAL B 99
SHEET 1 K 2 GLY B 146 THR B 150 0
SHEET 2 K 2 LYS B 156 TYR B 160 -1 O SER B 159 N MSE B 147
SHEET 1 L 2 VAL B 184 THR B 191 0
SHEET 2 L 2 SER B 201 VAL B 207 -1 O TRP B 204 N THR B 188
SHEET 1 M 4 VAL B 223 THR B 226 0
SHEET 2 M 4 ASP B 211 ARG B 217 -1 N LEU B 216 O VAL B 224
SHEET 3 M 4 TYR B 250 LYS B 257 -1 O CYS B 253 N GLU B 215
SHEET 4 M 4 CYS B 262 VAL B 269 -1 O TYR B 265 N VAL B 254
SHEET 1 N 2 VAL B 274 VAL B 276 0
SHEET 2 N 2 PHE B 281 ILE B 283 -1 O LEU B 282 N ALA B 275
SHEET 1 O 5 GLY B 292 GLY B 294 0
SHEET 2 O 5 SER B 325 ARG B 327 1 O ARG B 327 N PHE B 293
SHEET 3 O 5 VAL B 347 GLU B 351 1 O ILE B 349 N TYR B 326
SHEET 4 O 5 VAL B 405 ASN B 412 1 O SER B 409 N ASP B 350
SHEET 5 O 5 ILE B 441 VAL B 444 1 O THR B 442 N ILE B 410
SHEET 1 P 3 LEU B 463 ASN B 466 0
SHEET 2 P 3 ILE B 500 GLU B 504 1 O ILE B 501 N LEU B 463
SHEET 3 P 3 VAL B 543 GLU B 546 1 O GLY B 545 N ILE B 502
LINK C HIS A 0 N MSE A 1 1555 1555 1.33
LINK C MSE A 1 N LEU A 2 1555 1555 1.33
LINK C VAL A 104 N MSE A 105 1555 1555 1.33
LINK C MSE A 105 N GLU A 106 1555 1555 1.32
LINK C GLY A 146 N MSE A 147 1555 1555 1.32
LINK C MSE A 147 N VAL A 148 1555 1555 1.32
LINK C VAL A 174 N MSE A 175 1555 1555 1.33
LINK C MSE A 175 N LEU A 176 1555 1555 1.33
LINK C LEU A 310 N MSE A 311 1555 1555 1.33
LINK C MSE A 311 N VAL A 312 1555 1555 1.33
LINK C LEU A 317 N MSE A 318 1555 1555 1.33
LINK C MSE A 318 N ASP A 319 1555 1555 1.33
LINK C GLU A 336 N MSE A 337 1555 1555 1.33
LINK C MSE A 337 N LEU A 338 1555 1555 1.33
LINK C VAL A 406 N MSE A 407 1555 1555 1.33
LINK C MSE A 407 N TRP A 408 1555 1555 1.33
LINK C VAL A 446 N MSE A 447 1555 1555 1.33
LINK C MSE A 447 N PHE A 448 1555 1555 1.33
LINK C SER A 515 N MSE A 516 1555 1555 1.33
LINK C MSE A 516 N TYR A 517 1555 1555 1.33
LINK C ASP A 519 N MSE A 520 1555 1555 1.33
LINK C MSE A 520 N TRP A 521 1555 1555 1.33
LINK C ASP A 531 N MSE A 532 1555 1555 1.33
LINK C MSE A 532 N TYR A 533 1555 1555 1.33
LINK C GLY A 590 N MSE A 591 1555 1555 1.33
LINK C MSE A 591 N ASN A 592 1555 1555 1.33
LINK C HIS B 0 N MSE B 1 1555 1555 1.33
LINK C MSE B 1 N LEU B 2 1555 1555 1.33
LINK C VAL B 104 N MSE B 105 1555 1555 1.33
LINK C MSE B 105 N GLU B 106 1555 1555 1.33
LINK C GLY B 146 N MSE B 147 1555 1555 1.33
LINK C MSE B 147 N VAL B 148 1555 1555 1.33
LINK C VAL B 174 N MSE B 175 1555 1555 1.33
LINK C MSE B 175 N LEU B 176 1555 1555 1.33
LINK C LEU B 310 N MSE B 311 1555 1555 1.33
LINK C MSE B 311 N VAL B 312 1555 1555 1.33
LINK C LEU B 317 N MSE B 318 1555 1555 1.33
LINK C MSE B 318 N ASP B 319 1555 1555 1.33
LINK C GLU B 336 N MSE B 337 1555 1555 1.33
LINK C MSE B 337 N LEU B 338 1555 1555 1.33
LINK C VAL B 406 N MSE B 407 1555 1555 1.33
LINK C MSE B 407 N TRP B 408 1555 1555 1.33
LINK C VAL B 446 N MSE B 447 1555 1555 1.33
LINK C MSE B 447 N PHE B 448 1555 1555 1.33
LINK C SER B 515 N MSE B 516 1555 1555 1.33
LINK C MSE B 516 N TYR B 517 1555 1555 1.33
LINK C ASP B 519 N MSE B 520 1555 1555 1.33
LINK C MSE B 520 N TRP B 521 1555 1555 1.34
LINK C ASP B 531 N MSE B 532 1555 1555 1.33
LINK C MSE B 532 N TYR B 533 1555 1555 1.33
LINK C GLY B 590 N MSE B 591 1555 1555 1.33
LINK C MSE B 591 N ASN B 592 1555 1555 1.33
SITE 1 AC1 11 PHE A 365 ASP B 163 LEU B 361 GLY B 362
SITE 2 AC1 11 GLU B 413 PHE B 448 TYR B 468 TYR B 472
SITE 3 AC1 11 LEU B 561 HOH B 654 HOH B 718
SITE 1 AC2 10 LEU A 361 GLY A 362 ILE A 363 GLU A 413
SITE 2 AC2 10 PHE A 448 TYR A 472 LEU A 561 HOH A 667
SITE 3 AC2 10 HOH A 677 PHE B 365
CRYST1 167.814 76.934 125.810 90.00 124.75 90.00 C 1 2 1 8
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 0.005959 0.000000 0.004133 0.00000
SCALE2 0.000000 0.012998 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009673 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
