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HEADER HYDROLASE 13-MAY-16 5JYC
TITLE CRYSTAL STRUCTURE OF THE E153Q MUTANT OF THE CFTR INHIBITORY FACTOR
TITLE 2 CIF CONTAINING THE ADDUCTED 14,15-EET HYDROLYSIS INTERMEDIATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CFTR INHIBITORY FACTOR;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA (STRAIN UCBPP-PA14);
SOURCE 3 ORGANISM_TAXID: 208963;
SOURCE 4 STRAIN: UCBPP-PA14;
SOURCE 5 GENE: PA14_26090;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: TOP10
KEYWDS EPOXIDE HYDROLASE, HYDROXYALKYL-ENZYME INTERMEDIATE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.L.HVORECNY,D.R.MADDEN
REVDAT 1 11-JAN-17 5JYC 0
JRNL AUTH B.A.FLITTER,K.L.HVORECNY,E.ONO,T.EDDENS,J.YANG,D.H.KWAK,
JRNL AUTH 2 C.D.BAHL,T.H.HAMPTON,C.MORISSEAU,B.D.HAMMOCK,X.LIU,J.S.LEE,
JRNL AUTH 3 J.K.KOLLS,B.D.LEVY,D.R.MADDEN,J.M.BOMBERGER
JRNL TITL PSEUDOMONAS AERUGINOSA SABOTAGES THE GENERATION OF HOST
JRNL TITL 2 PRORESOLVING LIPID MEDIATORS.
JRNL REF PROC. NATL. ACAD. SCI. 2016
JRNL REF 2 U.S.A.
JRNL REFN ESSN 1091-6490
JRNL PMID 27980032
JRNL DOI 10.1073/PNAS.1610242114
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.10_2155: 000)
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.41
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.990
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 82560
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.155
REMARK 3 R VALUE (WORKING SET) : 0.153
REMARK 3 FREE R VALUE : 0.191
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 4138
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 35.4151 - 6.2037 1.00 2646 207 0.1539 0.1686
REMARK 3 2 6.2037 - 4.9283 1.00 2778 0 0.1472 0.0000
REMARK 3 3 4.9283 - 4.3065 1.00 2577 207 0.1151 0.1363
REMARK 3 4 4.3065 - 3.9133 1.00 2552 207 0.1273 0.1610
REMARK 3 5 3.9133 - 3.6332 1.00 2767 0 0.1399 0.0000
REMARK 3 6 3.6332 - 3.4191 1.00 2550 207 0.1432 0.1513
REMARK 3 7 3.4191 - 3.2480 1.00 2543 207 0.1527 0.1691
REMARK 3 8 3.2480 - 3.1067 1.00 2770 0 0.1614 0.0000
REMARK 3 9 3.1067 - 2.9872 1.00 2525 207 0.1698 0.2252
REMARK 3 10 2.9872 - 2.8842 1.00 2558 206 0.1716 0.2048
REMARK 3 11 2.8842 - 2.7940 1.00 2744 0 0.1576 0.0000
REMARK 3 12 2.7940 - 2.7142 1.00 2553 207 0.1609 0.2183
REMARK 3 13 2.7142 - 2.6427 1.00 2535 207 0.1570 0.2134
REMARK 3 14 2.6427 - 2.5783 1.00 2780 0 0.1618 0.0000
REMARK 3 15 2.5783 - 2.5197 1.00 2526 207 0.1607 0.2106
REMARK 3 16 2.5197 - 2.4661 1.00 2510 206 0.1635 0.2289
REMARK 3 17 2.4661 - 2.4168 1.00 2744 0 0.1644 0.0000
REMARK 3 18 2.4168 - 2.3712 1.00 2563 207 0.1602 0.2019
REMARK 3 19 2.3712 - 2.3288 1.00 2524 207 0.1514 0.2246
REMARK 3 20 2.3288 - 2.2894 1.00 2705 0 0.1590 0.0000
REMARK 3 21 2.2894 - 2.2524 1.00 2572 207 0.1673 0.2263
REMARK 3 22 2.2524 - 2.2178 1.00 2544 207 0.1541 0.1956
REMARK 3 23 2.2178 - 2.1852 1.00 2698 0 0.1568 0.0000
REMARK 3 24 2.1852 - 2.1544 1.00 2554 207 0.1660 0.2201
REMARK 3 25 2.1544 - 2.1253 1.00 2543 207 0.1551 0.2004
REMARK 3 26 2.1253 - 2.0977 1.00 2726 0 0.1635 0.0000
REMARK 3 27 2.0977 - 2.0715 1.00 2544 207 0.1683 0.2067
REMARK 3 28 2.0715 - 2.0465 1.00 2488 207 0.1715 0.2523
REMARK 3 29 2.0465 - 2.0227 1.00 2770 0 0.1721 0.0000
REMARK 3 30 2.0227 - 2.0000 1.00 2533 207 0.1801 0.2461
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.180
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.600
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
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 : 0.006 9980
REMARK 3 ANGLE : 0.829 13546
REMARK 3 CHIRALITY : 0.051 1384
REMARK 3 PLANARITY : 0.006 1775
REMARK 3 DIHEDRAL : 16.119 5904
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ( CHAIN A AND ( RESID 25:321 OR RESID 401:401 ) )
REMARK 3 ORIGIN FOR THE GROUP (A): 21.9695 12.1975 -27.4820
REMARK 3 T TENSOR
REMARK 3 T11: 0.0964 T22: 0.1063
REMARK 3 T33: 0.0887 T12: -0.0026
REMARK 3 T13: -0.0036 T23: -0.0157
REMARK 3 L TENSOR
REMARK 3 L11: 0.6128 L22: 0.5674
REMARK 3 L33: 0.5522 L12: -0.0229
REMARK 3 L13: 0.0377 L23: -0.0512
REMARK 3 S TENSOR
REMARK 3 S11: 0.0028 S12: 0.0586 S13: -0.0579
REMARK 3 S21: -0.0379 S22: -0.0028 S23: -0.0216
REMARK 3 S31: 0.0929 S32: 0.0405 S33: 0.0000
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: ( CHAIN B AND ( RESID 25:321 OR RESID 401:401 ) )
REMARK 3 ORIGIN FOR THE GROUP (A): 31.0633 51.7550 -15.6217
REMARK 3 T TENSOR
REMARK 3 T11: 0.1070 T22: 0.0984
REMARK 3 T33: 0.1461 T12: -0.0260
REMARK 3 T13: -0.0183 T23: -0.0030
REMARK 3 L TENSOR
REMARK 3 L11: 0.6927 L22: 0.6907
REMARK 3 L33: 0.4889 L12: 0.2267
REMARK 3 L13: 0.0187 L23: 0.1209
REMARK 3 S TENSOR
REMARK 3 S11: -0.0202 S12: -0.0188 S13: 0.1196
REMARK 3 S21: 0.0270 S22: 0.0227 S23: -0.0316
REMARK 3 S31: -0.0851 S32: 0.0029 S33: 0.0010
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: ( CHAIN C AND ( RESID 25:321 OR RESID 401:401 ) )
REMARK 3 ORIGIN FOR THE GROUP (A): -5.8220 44.9818 -27.2580
REMARK 3 T TENSOR
REMARK 3 T11: 0.1004 T22: 0.0941
REMARK 3 T33: 0.1315 T12: -0.0057
REMARK 3 T13: -0.0013 T23: 0.0101
REMARK 3 L TENSOR
REMARK 3 L11: 0.6533 L22: 0.6362
REMARK 3 L33: 0.5751 L12: -0.0853
REMARK 3 L13: -0.0500 L23: 0.0098
REMARK 3 S TENSOR
REMARK 3 S11: 0.0156 S12: 0.0456 S13: 0.1216
REMARK 3 S21: -0.0539 S22: -0.0147 S23: 0.0504
REMARK 3 S31: -0.0841 S32: -0.0158 S33: -0.0082
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: ( CHAIN D AND ( RESID 25:321 OR RESID 401:401 ) )
REMARK 3 ORIGIN FOR THE GROUP (A): -15.0329 5.4048 -15.6676
REMARK 3 T TENSOR
REMARK 3 T11: 0.1016 T22: 0.1084
REMARK 3 T33: 0.0830 T12: -0.0273
REMARK 3 T13: 0.0048 T23: 0.0032
REMARK 3 L TENSOR
REMARK 3 L11: 0.6471 L22: 0.5795
REMARK 3 L33: 0.3991 L12: 0.1057
REMARK 3 L13: -0.1059 L23: -0.1478
REMARK 3 S TENSOR
REMARK 3 S11: -0.0039 S12: -0.0497 S13: -0.0586
REMARK 3 S21: 0.0157 S22: -0.0067 S23: 0.0714
REMARK 3 S31: 0.0439 S32: 0.0061 S33: 0.0080
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 5JYC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-MAY-16.
REMARK 100 THE DEPOSITION ID IS D_1000220316.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-APR-11
REMARK 200 TEMPERATURE (KELVIN) : 80
REMARK 200 PH : 5.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL14-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 270
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS DEC 6TH, 2010
REMARK 200 DATA SCALING SOFTWARE : XDS DEC 6TH, 2010
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 82560
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 35.410
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 6.240
REMARK 200 R MERGE (I) : 0.10600
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 14.2700
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.05
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 6.16
REMARK 200 R MERGE FOR SHELL (I) : 0.45000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 4.440
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX (1.7_650: ???)
REMARK 200 STARTING MODEL: 3KD2
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.26
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.25
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8K, CALCIUM CHLORIDE, SODIUM
REMARK 280 ACETATE, PH 5.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K
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 84.46500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 41.80100
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 84.46500
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 41.80100
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2810 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20810 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2790 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20900 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
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 HIS A 322
REMARK 465 HIS A 323
REMARK 465 HIS A 324
REMARK 465 HIS A 325
REMARK 465 HIS B 322
REMARK 465 HIS B 323
REMARK 465 HIS B 324
REMARK 465 HIS B 325
REMARK 465 HIS C 322
REMARK 465 HIS C 323
REMARK 465 HIS C 324
REMARK 465 HIS C 325
REMARK 465 HIS D 322
REMARK 465 HIS D 323
REMARK 465 HIS D 324
REMARK 465 HIS D 325
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 GLN A 65 -166.82 -129.97
REMARK 500 ASP A 129 -129.83 57.77
REMARK 500 ALA A 154 144.34 -170.61
REMARK 500 ASN A 210 78.21 -100.26
REMARK 500 ASP B 129 -129.84 62.07
REMARK 500 ALA B 154 145.05 -176.16
REMARK 500 ASP B 185 18.26 59.32
REMARK 500 ASP C 129 -131.87 59.06
REMARK 500 ASN C 210 76.69 -100.29
REMARK 500 THR D 99 -61.26 -91.20
REMARK 500 ASP D 129 -132.24 59.71
REMARK 500 ALA D 154 145.56 -175.74
REMARK 500 ARG D 319 92.27 -68.71
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH D 715 DISTANCE = 5.85 ANGSTROMS
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 THE LIGAND EET AS A SUBSTRATE IS AN EPOXIDE, WHICH IS CONVERTED
REMARK 600 INTO A DIOL VIA A TWO-STEP REACTION WHICH INCLUDES A COVALENT
REMARK 600 INTERMEDIATE. THE PROTEIN PLUS ADDUCT (C15 ATOM OF EET COVALENTLY
REMARK 600 LINKED TO OD2 ATOM OF ASP 129) IS THE RESULT OF THE FIRST STEP IN
REMARK 600 THE REACTION.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EET A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide EET B 401 and ASP B
REMARK 800 129
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide EET C 401 and ASP C
REMARK 800 129
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide EET D 401 and ASP D
REMARK 800 129
DBREF1 5JYC A 25 325 UNP A0A0M3KL26_PSEAB
DBREF2 5JYC A A0A0M3KL26 1 301
DBREF1 5JYC B 25 325 UNP A0A0M3KL26_PSEAB
DBREF2 5JYC B A0A0M3KL26 1 301
DBREF1 5JYC C 25 325 UNP A0A0M3KL26_PSEAB
DBREF2 5JYC C A0A0M3KL26 1 301
DBREF1 5JYC D 25 325 UNP A0A0M3KL26_PSEAB
DBREF2 5JYC D A0A0M3KL26 1 301
SEQADV 5JYC GLN A 153 UNP A0A0M3KL2 GLU 129 ENGINEERED MUTATION
SEQADV 5JYC GLN B 153 UNP A0A0M3KL2 GLU 129 ENGINEERED MUTATION
SEQADV 5JYC GLN C 153 UNP A0A0M3KL2 GLU 129 ENGINEERED MUTATION
SEQADV 5JYC GLN D 153 UNP A0A0M3KL2 GLU 129 ENGINEERED MUTATION
SEQRES 1 A 301 ALA GLU GLU PHE PRO VAL PRO ASN GLY PHE GLU SER ALA
SEQRES 2 A 301 TYR ARG GLU VAL ASP GLY VAL LYS LEU HIS TYR VAL LYS
SEQRES 3 A 301 GLY GLY GLN GLY PRO LEU VAL MET LEU VAL HIS GLY PHE
SEQRES 4 A 301 GLY GLN THR TRP TYR GLU TRP HIS GLN LEU MET PRO GLU
SEQRES 5 A 301 LEU ALA LYS ARG PHE THR VAL ILE ALA PRO ASP LEU PRO
SEQRES 6 A 301 GLY LEU GLY GLN SER GLU PRO PRO LYS THR GLY TYR SER
SEQRES 7 A 301 GLY GLU GLN VAL ALA VAL TYR LEU HIS LYS LEU ALA ARG
SEQRES 8 A 301 GLN PHE SER PRO ASP ARG PRO PHE ASP LEU VAL ALA HIS
SEQRES 9 A 301 ASP ILE GLY ILE TRP ASN THR TYR PRO MET VAL VAL LYS
SEQRES 10 A 301 ASN GLN ALA ASP ILE ALA ARG LEU VAL TYR MET GLN ALA
SEQRES 11 A 301 PRO ILE PRO ASP ALA ARG ILE TYR ARG PHE PRO ALA PHE
SEQRES 12 A 301 THR ALA GLN GLY GLU SER LEU VAL TRP HIS PHE SER PHE
SEQRES 13 A 301 PHE ALA ALA ASP ASP ARG LEU ALA GLU THR LEU ILE ALA
SEQRES 14 A 301 GLY LYS GLU ARG PHE PHE LEU GLU HIS PHE ILE LYS SER
SEQRES 15 A 301 HIS ALA SER ASN THR GLU VAL PHE SER GLU ARG LEU LEU
SEQRES 16 A 301 ASP LEU TYR ALA ARG SER TYR ALA LYS PRO HIS SER LEU
SEQRES 17 A 301 ASN ALA SER PHE GLU TYR TYR ARG ALA LEU ASN GLU SER
SEQRES 18 A 301 VAL ARG GLN ASN ALA GLU LEU ALA LYS THR ARG LEU GLN
SEQRES 19 A 301 MET PRO THR MET THR LEU ALA GLY GLY GLY HIS GLY GLY
SEQRES 20 A 301 MET GLY THR PHE GLN LEU GLU GLN MET LYS ALA TYR ALA
SEQRES 21 A 301 GLU ASP VAL GLU GLY HIS VAL LEU PRO GLY CYS GLY HIS
SEQRES 22 A 301 TRP LEU PRO GLU GLU CYS ALA ALA PRO MET ASN ARG LEU
SEQRES 23 A 301 VAL ILE ASP PHE LEU SER ARG GLY ARG HIS HIS HIS HIS
SEQRES 24 A 301 HIS HIS
SEQRES 1 B 301 ALA GLU GLU PHE PRO VAL PRO ASN GLY PHE GLU SER ALA
SEQRES 2 B 301 TYR ARG GLU VAL ASP GLY VAL LYS LEU HIS TYR VAL LYS
SEQRES 3 B 301 GLY GLY GLN GLY PRO LEU VAL MET LEU VAL HIS GLY PHE
SEQRES 4 B 301 GLY GLN THR TRP TYR GLU TRP HIS GLN LEU MET PRO GLU
SEQRES 5 B 301 LEU ALA LYS ARG PHE THR VAL ILE ALA PRO ASP LEU PRO
SEQRES 6 B 301 GLY LEU GLY GLN SER GLU PRO PRO LYS THR GLY TYR SER
SEQRES 7 B 301 GLY GLU GLN VAL ALA VAL TYR LEU HIS LYS LEU ALA ARG
SEQRES 8 B 301 GLN PHE SER PRO ASP ARG PRO PHE ASP LEU VAL ALA HIS
SEQRES 9 B 301 ASP ILE GLY ILE TRP ASN THR TYR PRO MET VAL VAL LYS
SEQRES 10 B 301 ASN GLN ALA ASP ILE ALA ARG LEU VAL TYR MET GLN ALA
SEQRES 11 B 301 PRO ILE PRO ASP ALA ARG ILE TYR ARG PHE PRO ALA PHE
SEQRES 12 B 301 THR ALA GLN GLY GLU SER LEU VAL TRP HIS PHE SER PHE
SEQRES 13 B 301 PHE ALA ALA ASP ASP ARG LEU ALA GLU THR LEU ILE ALA
SEQRES 14 B 301 GLY LYS GLU ARG PHE PHE LEU GLU HIS PHE ILE LYS SER
SEQRES 15 B 301 HIS ALA SER ASN THR GLU VAL PHE SER GLU ARG LEU LEU
SEQRES 16 B 301 ASP LEU TYR ALA ARG SER TYR ALA LYS PRO HIS SER LEU
SEQRES 17 B 301 ASN ALA SER PHE GLU TYR TYR ARG ALA LEU ASN GLU SER
SEQRES 18 B 301 VAL ARG GLN ASN ALA GLU LEU ALA LYS THR ARG LEU GLN
SEQRES 19 B 301 MET PRO THR MET THR LEU ALA GLY GLY GLY HIS GLY GLY
SEQRES 20 B 301 MET GLY THR PHE GLN LEU GLU GLN MET LYS ALA TYR ALA
SEQRES 21 B 301 GLU ASP VAL GLU GLY HIS VAL LEU PRO GLY CYS GLY HIS
SEQRES 22 B 301 TRP LEU PRO GLU GLU CYS ALA ALA PRO MET ASN ARG LEU
SEQRES 23 B 301 VAL ILE ASP PHE LEU SER ARG GLY ARG HIS HIS HIS HIS
SEQRES 24 B 301 HIS HIS
SEQRES 1 C 301 ALA GLU GLU PHE PRO VAL PRO ASN GLY PHE GLU SER ALA
SEQRES 2 C 301 TYR ARG GLU VAL ASP GLY VAL LYS LEU HIS TYR VAL LYS
SEQRES 3 C 301 GLY GLY GLN GLY PRO LEU VAL MET LEU VAL HIS GLY PHE
SEQRES 4 C 301 GLY GLN THR TRP TYR GLU TRP HIS GLN LEU MET PRO GLU
SEQRES 5 C 301 LEU ALA LYS ARG PHE THR VAL ILE ALA PRO ASP LEU PRO
SEQRES 6 C 301 GLY LEU GLY GLN SER GLU PRO PRO LYS THR GLY TYR SER
SEQRES 7 C 301 GLY GLU GLN VAL ALA VAL TYR LEU HIS LYS LEU ALA ARG
SEQRES 8 C 301 GLN PHE SER PRO ASP ARG PRO PHE ASP LEU VAL ALA HIS
SEQRES 9 C 301 ASP ILE GLY ILE TRP ASN THR TYR PRO MET VAL VAL LYS
SEQRES 10 C 301 ASN GLN ALA ASP ILE ALA ARG LEU VAL TYR MET GLN ALA
SEQRES 11 C 301 PRO ILE PRO ASP ALA ARG ILE TYR ARG PHE PRO ALA PHE
SEQRES 12 C 301 THR ALA GLN GLY GLU SER LEU VAL TRP HIS PHE SER PHE
SEQRES 13 C 301 PHE ALA ALA ASP ASP ARG LEU ALA GLU THR LEU ILE ALA
SEQRES 14 C 301 GLY LYS GLU ARG PHE PHE LEU GLU HIS PHE ILE LYS SER
SEQRES 15 C 301 HIS ALA SER ASN THR GLU VAL PHE SER GLU ARG LEU LEU
SEQRES 16 C 301 ASP LEU TYR ALA ARG SER TYR ALA LYS PRO HIS SER LEU
SEQRES 17 C 301 ASN ALA SER PHE GLU TYR TYR ARG ALA LEU ASN GLU SER
SEQRES 18 C 301 VAL ARG GLN ASN ALA GLU LEU ALA LYS THR ARG LEU GLN
SEQRES 19 C 301 MET PRO THR MET THR LEU ALA GLY GLY GLY HIS GLY GLY
SEQRES 20 C 301 MET GLY THR PHE GLN LEU GLU GLN MET LYS ALA TYR ALA
SEQRES 21 C 301 GLU ASP VAL GLU GLY HIS VAL LEU PRO GLY CYS GLY HIS
SEQRES 22 C 301 TRP LEU PRO GLU GLU CYS ALA ALA PRO MET ASN ARG LEU
SEQRES 23 C 301 VAL ILE ASP PHE LEU SER ARG GLY ARG HIS HIS HIS HIS
SEQRES 24 C 301 HIS HIS
SEQRES 1 D 301 ALA GLU GLU PHE PRO VAL PRO ASN GLY PHE GLU SER ALA
SEQRES 2 D 301 TYR ARG GLU VAL ASP GLY VAL LYS LEU HIS TYR VAL LYS
SEQRES 3 D 301 GLY GLY GLN GLY PRO LEU VAL MET LEU VAL HIS GLY PHE
SEQRES 4 D 301 GLY GLN THR TRP TYR GLU TRP HIS GLN LEU MET PRO GLU
SEQRES 5 D 301 LEU ALA LYS ARG PHE THR VAL ILE ALA PRO ASP LEU PRO
SEQRES 6 D 301 GLY LEU GLY GLN SER GLU PRO PRO LYS THR GLY TYR SER
SEQRES 7 D 301 GLY GLU GLN VAL ALA VAL TYR LEU HIS LYS LEU ALA ARG
SEQRES 8 D 301 GLN PHE SER PRO ASP ARG PRO PHE ASP LEU VAL ALA HIS
SEQRES 9 D 301 ASP ILE GLY ILE TRP ASN THR TYR PRO MET VAL VAL LYS
SEQRES 10 D 301 ASN GLN ALA ASP ILE ALA ARG LEU VAL TYR MET GLN ALA
SEQRES 11 D 301 PRO ILE PRO ASP ALA ARG ILE TYR ARG PHE PRO ALA PHE
SEQRES 12 D 301 THR ALA GLN GLY GLU SER LEU VAL TRP HIS PHE SER PHE
SEQRES 13 D 301 PHE ALA ALA ASP ASP ARG LEU ALA GLU THR LEU ILE ALA
SEQRES 14 D 301 GLY LYS GLU ARG PHE PHE LEU GLU HIS PHE ILE LYS SER
SEQRES 15 D 301 HIS ALA SER ASN THR GLU VAL PHE SER GLU ARG LEU LEU
SEQRES 16 D 301 ASP LEU TYR ALA ARG SER TYR ALA LYS PRO HIS SER LEU
SEQRES 17 D 301 ASN ALA SER PHE GLU TYR TYR ARG ALA LEU ASN GLU SER
SEQRES 18 D 301 VAL ARG GLN ASN ALA GLU LEU ALA LYS THR ARG LEU GLN
SEQRES 19 D 301 MET PRO THR MET THR LEU ALA GLY GLY GLY HIS GLY GLY
SEQRES 20 D 301 MET GLY THR PHE GLN LEU GLU GLN MET LYS ALA TYR ALA
SEQRES 21 D 301 GLU ASP VAL GLU GLY HIS VAL LEU PRO GLY CYS GLY HIS
SEQRES 22 D 301 TRP LEU PRO GLU GLU CYS ALA ALA PRO MET ASN ARG LEU
SEQRES 23 D 301 VAL ILE ASP PHE LEU SER ARG GLY ARG HIS HIS HIS HIS
SEQRES 24 D 301 HIS HIS
HET EET A 401 23
HET EET B 401 23
HET EET C 401 23
HET EET D 401 23
HETNAM EET (5~{Z},11~{Z},14~{R},15~{R})-14,15-BIS(OXIDANYL)ICOSA-
HETNAM 2 EET 5,8,11-TRIENOIC ACID
FORMUL 5 EET 4(C20 H34 O4)
FORMUL 9 HOH *801(H2 O)
HELIX 1 AA1 THR A 66 HIS A 71 5 6
HELIX 2 AA2 LEU A 73 ALA A 78 1 6
HELIX 3 AA3 SER A 102 SER A 118 1 17
HELIX 4 AA4 ASP A 129 ASN A 134 1 6
HELIX 5 AA5 THR A 135 ASN A 142 1 8
HELIX 6 AA6 ASP A 158 PHE A 164 5 7
HELIX 7 AA7 TRP A 176 ALA A 183 1 8
HELIX 8 AA8 ARG A 186 ALA A 193 1 8
HELIX 9 AA9 LYS A 195 HIS A 207 1 13
HELIX 10 AB1 ASN A 210 PHE A 214 5 5
HELIX 11 AB2 SER A 215 ALA A 227 1 13
HELIX 12 AB3 LYS A 228 ALA A 241 1 14
HELIX 13 AB4 ALA A 241 ALA A 253 1 13
HELIX 14 AB5 THR A 274 ALA A 282 1 9
HELIX 15 AB6 TRP A 298 CYS A 303 1 6
HELIX 16 AB7 CYS A 303 SER A 316 1 14
HELIX 17 AB8 THR B 66 HIS B 71 5 6
HELIX 18 AB9 GLN B 72 ALA B 78 1 7
HELIX 19 AC1 SER B 102 SER B 118 1 17
HELIX 20 AC2 ASP B 129 ASN B 134 1 6
HELIX 21 AC3 THR B 135 ASN B 142 1 8
HELIX 22 AC4 ASP B 158 PHE B 164 5 7
HELIX 23 AC5 TRP B 176 ALA B 183 1 8
HELIX 24 AC6 ARG B 186 ALA B 193 1 8
HELIX 25 AC7 LYS B 195 HIS B 207 1 13
HELIX 26 AC8 ASN B 210 PHE B 214 5 5
HELIX 27 AC9 SER B 215 LYS B 228 1 14
HELIX 28 AD1 LYS B 228 ALA B 241 1 14
HELIX 29 AD2 ALA B 241 ALA B 253 1 13
HELIX 30 AD3 THR B 274 ALA B 284 1 11
HELIX 31 AD4 TRP B 298 CYS B 303 1 6
HELIX 32 AD5 CYS B 303 ARG B 317 1 15
HELIX 33 AD6 THR C 66 HIS C 71 5 6
HELIX 34 AD7 GLN C 72 ALA C 78 1 7
HELIX 35 AD8 SER C 102 SER C 118 1 17
HELIX 36 AD9 ASP C 129 ASN C 134 1 6
HELIX 37 AE1 THR C 135 ASN C 142 1 8
HELIX 38 AE2 ASP C 158 ARG C 163 5 6
HELIX 39 AE3 TRP C 176 ALA C 183 1 8
HELIX 40 AE4 ARG C 186 ALA C 193 1 8
HELIX 41 AE5 LYS C 195 HIS C 207 1 13
HELIX 42 AE6 ASN C 210 PHE C 214 5 5
HELIX 43 AE7 SER C 215 ALA C 227 1 13
HELIX 44 AE8 LYS C 228 ALA C 241 1 14
HELIX 45 AE9 ALA C 241 ALA C 253 1 13
HELIX 46 AF1 THR C 274 LYS C 281 1 8
HELIX 47 AF2 TRP C 298 CYS C 303 1 6
HELIX 48 AF3 CYS C 303 SER C 316 1 14
HELIX 49 AF4 THR D 66 HIS D 71 5 6
HELIX 50 AF5 GLN D 72 ALA D 78 1 7
HELIX 51 AF6 SER D 102 SER D 118 1 17
HELIX 52 AF7 ASP D 129 ASN D 134 1 6
HELIX 53 AF8 THR D 135 ASN D 142 1 8
HELIX 54 AF9 ASP D 158 PHE D 164 5 7
HELIX 55 AG1 TRP D 176 ALA D 183 1 8
HELIX 56 AG2 ARG D 186 ALA D 193 1 8
HELIX 57 AG3 LYS D 195 HIS D 207 1 13
HELIX 58 AG4 ASN D 210 PHE D 214 5 5
HELIX 59 AG5 SER D 215 ALA D 227 1 13
HELIX 60 AG6 LYS D 228 ALA D 241 1 14
HELIX 61 AG7 ALA D 241 ALA D 253 1 13
HELIX 62 AG8 THR D 274 ALA D 284 1 11
HELIX 63 AG9 TRP D 298 CYS D 303 1 6
HELIX 64 AH1 CYS D 303 ARG D 317 1 15
SHEET 1 AA1 8 GLU A 35 VAL A 41 0
SHEET 2 AA1 8 VAL A 44 GLY A 52 -1 O VAL A 44 N VAL A 41
SHEET 3 AA1 8 THR A 82 PRO A 86 -1 O VAL A 83 N GLY A 51
SHEET 4 AA1 8 LEU A 56 VAL A 60 1 N VAL A 57 O THR A 82
SHEET 5 AA1 8 PHE A 123 HIS A 128 1 O ASP A 124 N LEU A 56
SHEET 6 AA1 8 ILE A 146 MET A 152 1 O ALA A 147 N PHE A 123
SHEET 7 AA1 8 THR A 261 GLY A 266 1 O MET A 262 N TYR A 151
SHEET 8 AA1 8 VAL A 287 LEU A 292 1 O LEU A 292 N ALA A 265
SHEET 1 AA2 8 PHE B 34 VAL B 41 0
SHEET 2 AA2 8 VAL B 44 GLY B 52 -1 O LEU B 46 N ARG B 39
SHEET 3 AA2 8 THR B 82 PRO B 86 -1 O VAL B 83 N GLY B 51
SHEET 4 AA2 8 LEU B 56 VAL B 60 1 N VAL B 57 O THR B 82
SHEET 5 AA2 8 PHE B 123 HIS B 128 1 O VAL B 126 N VAL B 60
SHEET 6 AA2 8 ILE B 146 MET B 152 1 O VAL B 150 N LEU B 125
SHEET 7 AA2 8 THR B 261 GLY B 266 1 O MET B 262 N LEU B 149
SHEET 8 AA2 8 VAL B 287 LEU B 292 1 O LEU B 292 N ALA B 265
SHEET 1 AA3 2 PHE B 167 THR B 168 0
SHEET 2 AA3 2 GLY B 171 GLU B 172 -1 O GLY B 171 N THR B 168
SHEET 1 AA4 8 PHE C 34 VAL C 41 0
SHEET 2 AA4 8 VAL C 44 GLY C 52 -1 O VAL C 44 N VAL C 41
SHEET 3 AA4 8 THR C 82 PRO C 86 -1 O VAL C 83 N GLY C 51
SHEET 4 AA4 8 LEU C 56 VAL C 60 1 N VAL C 57 O THR C 82
SHEET 5 AA4 8 PHE C 123 HIS C 128 1 O VAL C 126 N VAL C 60
SHEET 6 AA4 8 ILE C 146 MET C 152 1 O VAL C 150 N LEU C 125
SHEET 7 AA4 8 THR C 261 GLY C 266 1 O MET C 262 N TYR C 151
SHEET 8 AA4 8 VAL C 287 LEU C 292 1 O LEU C 292 N ALA C 265
SHEET 1 AA5 8 GLU D 35 VAL D 41 0
SHEET 2 AA5 8 VAL D 44 GLY D 52 -1 O LEU D 46 N ARG D 39
SHEET 3 AA5 8 THR D 82 PRO D 86 -1 O VAL D 83 N GLY D 51
SHEET 4 AA5 8 LEU D 56 VAL D 60 1 N VAL D 57 O THR D 82
SHEET 5 AA5 8 PHE D 123 HIS D 128 1 O VAL D 126 N VAL D 60
SHEET 6 AA5 8 ILE D 146 MET D 152 1 O VAL D 150 N LEU D 125
SHEET 7 AA5 8 THR D 261 GLY D 266 1 O MET D 262 N LEU D 149
SHEET 8 AA5 8 VAL D 287 LEU D 292 1 O LEU D 292 N ALA D 265
SHEET 1 AA6 2 PHE D 167 THR D 168 0
SHEET 2 AA6 2 GLY D 171 GLU D 172 -1 O GLY D 171 N THR D 168
SSBOND 1 CYS A 295 CYS A 303 1555 1555 2.01
SSBOND 2 CYS B 295 CYS B 303 1555 1555 2.00
SSBOND 3 CYS C 295 CYS C 303 1555 1555 2.00
SSBOND 4 CYS D 295 CYS D 303 1555 1555 1.99
LINK OD2 ASP A 129 C6 EET A 401 1555 1555 1.39
LINK OD2 ASP B 129 C6 EET B 401 1555 1555 1.38
LINK OD2 ASP C 129 C6 EET C 401 1555 1555 1.38
LINK OD2 ASP D 129 C6 EET D 401 1555 1555 1.38
SITE 1 AC1 13 ASP A 129 GLN A 153 PHE A 164 PRO A 165
SITE 2 AC1 13 VAL A 175 HIS A 177 PHE A 178 HIS A 207
SITE 3 AC1 13 TYR A 239 MET A 272 HIS A 297 TRP A 298
SITE 4 AC1 13 HOH A 507
SITE 1 AC2 17 PHE B 63 HIS B 128 ILE B 130 GLY B 131
SITE 2 AC2 17 ILE B 132 MET B 152 GLN B 153 ALA B 154
SITE 3 AC2 17 VAL B 175 HIS B 177 PHE B 178 PHE B 203
SITE 4 AC2 17 TYR B 239 MET B 272 PHE B 275 HIS B 297
SITE 5 AC2 17 HOH B 619
SITE 1 AC3 19 PHE C 63 HIS C 128 ILE C 130 GLY C 131
SITE 2 AC3 19 ILE C 132 MET C 152 GLN C 153 ALA C 154
SITE 3 AC3 19 PHE C 164 PRO C 165 VAL C 175 HIS C 177
SITE 4 AC3 19 PHE C 178 HIS C 207 TYR C 239 MET C 272
SITE 5 AC3 19 HIS C 297 TRP C 298 HOH C 594
SITE 1 AC4 19 PHE D 63 HIS D 128 ILE D 130 GLY D 131
SITE 2 AC4 19 ILE D 132 MET D 152 GLN D 153 ALA D 154
SITE 3 AC4 19 PHE D 164 VAL D 175 HIS D 177 PHE D 178
SITE 4 AC4 19 PHE D 203 HIS D 207 TYR D 239 MET D 272
SITE 5 AC4 19 HIS D 297 HOH D 593 HOH D 623
CRYST1 168.930 83.602 89.241 90.00 100.38 90.00 C 1 2 1 16
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 0.005919 0.000000 0.001084 0.00000
SCALE2 0.000000 0.011961 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011392 0.00000
TER 2400 HIS A 321
TER 4796 HIS B 321
TER 7179 HIS C 321
TER 9581 HIS D 321
MASTER 387 0 4 64 36 0 19 610385 4 104 96
END |