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HEADER HYDROLASE 15-FEB-18 6FR2
TITLE SOLUBLE EPOXIDE HYDROLASE IN COMPLEX WITH LK864
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BIFUNCTIONAL EPOXIDE HYDROLASE 2;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.3.2.10,3.1.3.76;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: EPHX2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS INHIBITOR, COMPLEX, SEH, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.S.KRAMER,D.POGORYELOV,M.KRASAVIN,E.PROSCHAK
REVDAT 1 12-SEP-18 6FR2 0
JRNL AUTH A.LUKIN,J.KRAMER,M.HARTMANN,L.WEIZEL,V.HERNANDEZ-OLMOS,
JRNL AUTH 2 K.FALAHATI,I.BURGHARDT,N.KALINCHENKOVA,D.BAGNYUKOVA,
JRNL AUTH 3 N.ZHURILO,J.RAUTIO,M.FORSBERG,J.IHALAINEN,S.AURIOLA,
JRNL AUTH 4 J.LEPPANEN,I.KONSTANTINOV,D.POGORYELOV,E.PROSCHAK,D.DAR'IN,
JRNL AUTH 5 M.KRASAVIN
JRNL TITL DISCOVERY OF POLAR SPIROCYCLIC ORALLY BIOAVAILABLE UREA
JRNL TITL 2 INHIBITORS OF SOLUBLE EPOXIDE HYDROLASE.
JRNL REF BIOORG. CHEM. V. 80 655 2018
JRNL REFN ISSN 1090-2120
JRNL PMID 30059891
JRNL DOI 10.1016/J.BIOORG.2018.07.014
REMARK 2
REMARK 2 RESOLUTION. 2.26 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.12_2829
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) : 2.26
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.09
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 3 NUMBER OF REFLECTIONS : 35259
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.170
REMARK 3 R VALUE (WORKING SET) : 0.168
REMARK 3 FREE R VALUE : 0.210
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.040
REMARK 3 FREE R VALUE TEST SET COUNT : 1776
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 46.0996 - 5.3152 0.99 2593 133 0.1642 0.2014
REMARK 3 2 5.3152 - 4.2197 0.99 2560 179 0.1296 0.1677
REMARK 3 3 4.2197 - 3.6866 0.98 2534 166 0.1365 0.1661
REMARK 3 4 3.6866 - 3.3496 0.99 2597 146 0.1459 0.2065
REMARK 3 5 3.3496 - 3.1096 1.00 2597 130 0.1678 0.2036
REMARK 3 6 3.1096 - 2.9263 1.00 2609 155 0.1757 0.3036
REMARK 3 7 2.9263 - 2.7798 1.00 2619 96 0.1883 0.2219
REMARK 3 8 2.7798 - 2.6588 0.99 2607 133 0.2020 0.2674
REMARK 3 9 2.6588 - 2.5564 1.00 2606 120 0.2060 0.2516
REMARK 3 10 2.5564 - 2.4682 1.00 2631 132 0.2296 0.2516
REMARK 3 11 2.4682 - 2.3911 1.00 2561 140 0.2432 0.3240
REMARK 3 12 2.3911 - 2.3227 1.00 2627 129 0.2653 0.2859
REMARK 3 13 2.3227 - 2.2616 0.90 2342 117 0.3071 0.3418
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) : 0.250
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.190
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 46.28
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 54.68
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 : 0.011 2710
REMARK 3 ANGLE : 0.955 3688
REMARK 3 CHIRALITY : 0.060 379
REMARK 3 PLANARITY : 0.007 474
REMARK 3 DIHEDRAL : 25.429 1010
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 9
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 237 THROUGH 292 )
REMARK 3 ORIGIN FOR THE GROUP (A): -6.6249 -7.1319 -34.1435
REMARK 3 T TENSOR
REMARK 3 T11: 0.2202 T22: 0.2227
REMARK 3 T33: 0.2385 T12: -0.0026
REMARK 3 T13: 0.0255 T23: -0.0017
REMARK 3 L TENSOR
REMARK 3 L11: 0.4883 L22: 0.7117
REMARK 3 L33: 0.3092 L12: 0.7476
REMARK 3 L13: -0.0650 L23: -0.1065
REMARK 3 S TENSOR
REMARK 3 S11: -0.0217 S12: -0.0116 S13: 0.0528
REMARK 3 S21: -0.0291 S22: 0.0155 S23: -0.0579
REMARK 3 S31: 0.0330 S32: -0.0023 S33: 0.0000
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 293 THROUGH 328 )
REMARK 3 ORIGIN FOR THE GROUP (A): 2.2884 -15.7093 -37.4347
REMARK 3 T TENSOR
REMARK 3 T11: 0.3306 T22: 0.3087
REMARK 3 T33: 0.3373 T12: -0.0127
REMARK 3 T13: 0.0520 T23: -0.0063
REMARK 3 L TENSOR
REMARK 3 L11: 0.3110 L22: 0.1616
REMARK 3 L33: 0.2562 L12: 0.2036
REMARK 3 L13: -0.1012 L23: 0.1808
REMARK 3 S TENSOR
REMARK 3 S11: -0.1446 S12: -0.0177 S13: -0.0216
REMARK 3 S21: -0.0278 S22: 0.0231 S23: -0.1889
REMARK 3 S31: 0.0115 S32: 0.0685 S33: -0.0000
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 329 THROUGH 370 )
REMARK 3 ORIGIN FOR THE GROUP (A): -3.8212 -23.0067 -27.1340
REMARK 3 T TENSOR
REMARK 3 T11: 0.2401 T22: 0.2903
REMARK 3 T33: 0.3705 T12: 0.0034
REMARK 3 T13: -0.0046 T23: 0.0249
REMARK 3 L TENSOR
REMARK 3 L11: 0.3201 L22: 0.0663
REMARK 3 L33: 0.4912 L12: 0.0507
REMARK 3 L13: -0.0404 L23: 0.2002
REMARK 3 S TENSOR
REMARK 3 S11: -0.0614 S12: -0.2259 S13: -0.2133
REMARK 3 S21: 0.0215 S22: 0.0303 S23: -0.2012
REMARK 3 S31: 0.0632 S32: -0.0537 S33: -0.0000
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 371 THROUGH 399 )
REMARK 3 ORIGIN FOR THE GROUP (A): -13.3053 -31.3425 -45.1712
REMARK 3 T TENSOR
REMARK 3 T11: 0.5637 T22: 0.3929
REMARK 3 T33: 0.4214 T12: -0.0869
REMARK 3 T13: 0.0484 T23: -0.0127
REMARK 3 L TENSOR
REMARK 3 L11: 0.2713 L22: 0.2135
REMARK 3 L33: 0.0449 L12: 0.0821
REMARK 3 L13: 0.0992 L23: 0.0262
REMARK 3 S TENSOR
REMARK 3 S11: -0.2738 S12: 0.2211 S13: -0.3432
REMARK 3 S21: -0.3410 S22: 0.1576 S23: -0.0663
REMARK 3 S31: 0.3942 S32: -0.3891 S33: 0.0000
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 400 THROUGH 418 )
REMARK 3 ORIGIN FOR THE GROUP (A): -25.0625 -18.8325 -44.1364
REMARK 3 T TENSOR
REMARK 3 T11: 0.4387 T22: 0.4189
REMARK 3 T33: 0.4011 T12: -0.0433
REMARK 3 T13: -0.0736 T23: 0.0516
REMARK 3 L TENSOR
REMARK 3 L11: 0.1158 L22: 0.0579
REMARK 3 L33: 0.0048 L12: 0.0051
REMARK 3 L13: -0.0561 L23: 0.0629
REMARK 3 S TENSOR
REMARK 3 S11: 0.1155 S12: -0.1004 S13: -0.1432
REMARK 3 S21: -0.1951 S22: 0.0782 S23: 0.4641
REMARK 3 S31: 0.1648 S32: 0.1270 S33: -0.0000
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 419 THROUGH 435 )
REMARK 3 ORIGIN FOR THE GROUP (A): -24.5846 -28.3296 -48.5732
REMARK 3 T TENSOR
REMARK 3 T11: 0.7719 T22: 0.7208
REMARK 3 T33: 0.7253 T12: -0.1121
REMARK 3 T13: -0.1203 T23: -0.0747
REMARK 3 L TENSOR
REMARK 3 L11: 0.0612 L22: 0.0299
REMARK 3 L33: 0.0693 L12: 0.0340
REMARK 3 L13: -0.0039 L23: 0.1146
REMARK 3 S TENSOR
REMARK 3 S11: -0.1248 S12: -0.0381 S13: -0.4049
REMARK 3 S21: -0.3272 S22: 0.1865 S23: 0.0546
REMARK 3 S31: 0.0440 S32: -0.4081 S33: -0.0000
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 436 THROUGH 509 )
REMARK 3 ORIGIN FOR THE GROUP (A): -11.4401 -22.3832 -35.1620
REMARK 3 T TENSOR
REMARK 3 T11: 0.2993 T22: 0.2419
REMARK 3 T33: 0.2392 T12: -0.0135
REMARK 3 T13: 0.0121 T23: 0.0258
REMARK 3 L TENSOR
REMARK 3 L11: 0.9913 L22: 1.1227
REMARK 3 L33: 0.6097 L12: 0.0661
REMARK 3 L13: 0.1301 L23: -0.1306
REMARK 3 S TENSOR
REMARK 3 S11: -0.0459 S12: -0.0544 S13: -0.1275
REMARK 3 S21: -0.1108 S22: 0.0134 S23: -0.0435
REMARK 3 S31: 0.0675 S32: -0.0676 S33: -0.0000
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 510 THROUGH 530 )
REMARK 3 ORIGIN FOR THE GROUP (A): -17.9137 -19.8895 -24.4577
REMARK 3 T TENSOR
REMARK 3 T11: 0.3508 T22: 0.4221
REMARK 3 T33: 0.3879 T12: -0.0270
REMARK 3 T13: 0.0333 T23: 0.0635
REMARK 3 L TENSOR
REMARK 3 L11: 0.3250 L22: 0.4341
REMARK 3 L33: 0.0740 L12: -0.2097
REMARK 3 L13: -0.2247 L23: 0.3601
REMARK 3 S TENSOR
REMARK 3 S11: -0.0034 S12: -0.2008 S13: 0.0156
REMARK 3 S21: 0.0061 S22: 0.0412 S23: 0.1788
REMARK 3 S31: -0.0501 S32: -0.1574 S33: 0.0000
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 531 THROUGH 548 )
REMARK 3 ORIGIN FOR THE GROUP (A): -14.1672 -10.4860 -18.8647
REMARK 3 T TENSOR
REMARK 3 T11: 0.3921 T22: 0.4543
REMARK 3 T33: 0.3113 T12: 0.0210
REMARK 3 T13: 0.0013 T23: -0.0195
REMARK 3 L TENSOR
REMARK 3 L11: 0.0966 L22: 0.3126
REMARK 3 L33: 0.3010 L12: -0.0499
REMARK 3 L13: -0.2172 L23: 0.1357
REMARK 3 S TENSOR
REMARK 3 S11: -0.1270 S12: -0.4046 S13: 0.2106
REMARK 3 S21: 0.2733 S22: 0.1594 S23: 0.0719
REMARK 3 S31: -0.3123 S32: -0.1852 S33: -0.0000
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 6FR2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 16-FEB-18.
REMARK 100 THE DEPOSITION ID IS D_1200008485.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-SEP-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0-6.55
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID29
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.072
REMARK 200 MONOCHROMATOR : 1.072
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 35335
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.260
REMARK 200 RESOLUTION RANGE LOW (A) : 46.090
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 200 DATA REDUNDANCY : 3.400
REMARK 200 R MERGE (I) : 0.08100
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 9.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.26
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.30
REMARK 200 COMPLETENESS FOR SHELL (%) : 82.7
REMARK 200 DATA REDUNDANCY IN SHELL : 2.98
REMARK 200 R MERGE FOR SHELL (I) : 0.78800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.710
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: 4JNC
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.39
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1 UL PROTEIN SOLUTION PROTEIN (5-10
REMARK 280 MG/ML , 50 MM NACL, 50 MM SODIUM PHOSPHATE, 10% GLYCEROL (98%),
REMARK 280 2 MM DTT AT PH 7.4) WAS MIXED IN DIFFERENT RATIOS (2/1, 1/1, 1/2)
REMARK 280 WITH PRECIPITANT SOLUTION (23 %-28 % (W/V) POLYETHYLENGLYCOL
REMARK 280 (PEG) 6000, 70 MM AMMONIUM ACETAT, 200 MM MAGNESIUM ACETAT, 100
REMARK 280 MM SODIUM CACODYLATE AT PH 6.1-6.5), VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2
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,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z+1/2
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 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 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 40.04550
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 46.09000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 53.49900
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 40.04550
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 46.09000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 53.49900
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 40.04550
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 46.09000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 53.49900
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 40.04550
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 46.09000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 53.49900
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 100 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12810 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 KCAL/MOL
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 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 A 786 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 MET A 219
REMARK 465 ALA A 220
REMARK 465 SER A 221
REMARK 465 LEU A 222
REMARK 465 ASN A 223
REMARK 465 THR A 224
REMARK 465 PRO A 225
REMARK 465 ALA A 226
REMARK 465 PRO A 227
REMARK 465 LEU A 228
REMARK 465 ASN A 548
REMARK 465 PRO A 549
REMARK 465 PRO A 550
REMARK 465 VAL A 551
REMARK 465 VAL A 552
REMARK 465 SER A 553
REMARK 465 LYS A 554
REMARK 465 MET A 555
REMARK 465 LEU A 556
REMARK 465 LEU A 557
REMARK 465 GLU A 558
REMARK 465 HIS A 559
REMARK 465 HIS A 560
REMARK 465 HIS A 561
REMARK 465 HIS A 562
REMARK 465 HIS A 563
REMARK 465 HIS A 564
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 LYS A 376 CG CD CE NZ
REMARK 470 LYS A 421 CG CD CE NZ
REMARK 470 GLU A 424 CG CD OE1 OE2
REMARK 470 TRP A 510 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP A 510 CZ3 CH2
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 SER A 231 -163.54 -109.47
REMARK 500 GLU A 269 -140.87 -119.91
REMARK 500 ASP A 335 -129.92 64.74
REMARK 500 ASN A 359 -43.80 77.09
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 MET A 291 ASP A 292 147.71
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 602 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 509 OD1
REMARK 620 2 ASP A 509 OD2 57.2
REMARK 620 3 HOH A 802 O 95.7 95.5
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue E3N A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 602
DBREF 6FR2 A 222 555 UNP P34913 HYES_HUMAN 169 502
SEQADV 6FR2 MET A 219 UNP P34913 INITIATING METHIONINE
SEQADV 6FR2 ALA A 220 UNP P34913 EXPRESSION TAG
SEQADV 6FR2 SER A 221 UNP P34913 EXPRESSION TAG
SEQADV 6FR2 LEU A 556 UNP P34913 EXPRESSION TAG
SEQADV 6FR2 LEU A 557 UNP P34913 EXPRESSION TAG
SEQADV 6FR2 GLU A 558 UNP P34913 EXPRESSION TAG
SEQADV 6FR2 HIS A 559 UNP P34913 EXPRESSION TAG
SEQADV 6FR2 HIS A 560 UNP P34913 EXPRESSION TAG
SEQADV 6FR2 HIS A 561 UNP P34913 EXPRESSION TAG
SEQADV 6FR2 HIS A 562 UNP P34913 EXPRESSION TAG
SEQADV 6FR2 HIS A 563 UNP P34913 EXPRESSION TAG
SEQADV 6FR2 HIS A 564 UNP P34913 EXPRESSION TAG
SEQRES 1 A 346 MET ALA SER LEU ASN THR PRO ALA PRO LEU PRO THR SER
SEQRES 2 A 346 CYS ASN PRO SER ASP MET SER HIS GLY TYR VAL THR VAL
SEQRES 3 A 346 LYS PRO ARG VAL ARG LEU HIS PHE VAL GLU LEU GLY SER
SEQRES 4 A 346 GLY PRO ALA VAL CYS LEU CYS HIS GLY PHE PRO GLU SER
SEQRES 5 A 346 TRP TYR SER TRP ARG TYR GLN ILE PRO ALA LEU ALA GLN
SEQRES 6 A 346 ALA GLY TYR ARG VAL LEU ALA MET ASP MET LYS GLY TYR
SEQRES 7 A 346 GLY GLU SER SER ALA PRO PRO GLU ILE GLU GLU TYR CYS
SEQRES 8 A 346 MET GLU VAL LEU CYS LYS GLU MET VAL THR PHE LEU ASP
SEQRES 9 A 346 LYS LEU GLY LEU SER GLN ALA VAL PHE ILE GLY HIS ASP
SEQRES 10 A 346 TRP GLY GLY MET LEU VAL TRP TYR MET ALA LEU PHE TYR
SEQRES 11 A 346 PRO GLU ARG VAL ARG ALA VAL ALA SER LEU ASN THR PRO
SEQRES 12 A 346 PHE ILE PRO ALA ASN PRO ASN MET SER PRO LEU GLU SER
SEQRES 13 A 346 ILE LYS ALA ASN PRO VAL PHE ASP TYR GLN LEU TYR PHE
SEQRES 14 A 346 GLN GLU PRO GLY VAL ALA GLU ALA GLU LEU GLU GLN ASN
SEQRES 15 A 346 LEU SER ARG THR PHE LYS SER LEU PHE ARG ALA SER ASP
SEQRES 16 A 346 GLU SER VAL LEU SER MET HIS LYS VAL CYS GLU ALA GLY
SEQRES 17 A 346 GLY LEU PHE VAL ASN SER PRO GLU GLU PRO SER LEU SER
SEQRES 18 A 346 ARG MET VAL THR GLU GLU GLU ILE GLN PHE TYR VAL GLN
SEQRES 19 A 346 GLN PHE LYS LYS SER GLY PHE ARG GLY PRO LEU ASN TRP
SEQRES 20 A 346 TYR ARG ASN MET GLU ARG ASN TRP LYS TRP ALA CYS LYS
SEQRES 21 A 346 SER LEU GLY ARG LYS ILE LEU ILE PRO ALA LEU MET VAL
SEQRES 22 A 346 THR ALA GLU LYS ASP PHE VAL LEU VAL PRO GLN MET SER
SEQRES 23 A 346 GLN HIS MET GLU ASP TRP ILE PRO HIS LEU LYS ARG GLY
SEQRES 24 A 346 HIS ILE GLU ASP CYS GLY HIS TRP THR GLN MET ASP LYS
SEQRES 25 A 346 PRO THR GLU VAL ASN GLN ILE LEU ILE LYS TRP LEU ASP
SEQRES 26 A 346 SER ASP ALA ARG ASN PRO PRO VAL VAL SER LYS MET LEU
SEQRES 27 A 346 LEU GLU HIS HIS HIS HIS HIS HIS
HET E3N A 601 33
HET MG A 602 1
HETNAM E3N 1-[(4~{S})-9-PROPAN-2-YLSULFONYL-1-OXA-9-
HETNAM 2 E3N AZASPIRO[5.5]UNDECAN-4-YL]-3-[[4-(TRIFLUOROMETHYLOXY)
HETNAM 3 E3N PHENYL]METHYL]UREA
HETNAM MG MAGNESIUM ION
FORMUL 2 E3N C21 H30 F3 N3 O5 S
FORMUL 3 MG MG 2+
FORMUL 4 HOH *107(H2 O)
HELIX 1 AA1 ASN A 233 MET A 237 5 5
HELIX 2 AA2 SER A 270 ARG A 275 5 6
HELIX 3 AA3 GLN A 277 ALA A 284 1 8
HELIX 4 AA4 GLU A 304 TYR A 308 5 5
HELIX 5 AA5 CYS A 309 LEU A 324 1 16
HELIX 6 AA6 ASP A 335 TYR A 348 1 14
HELIX 7 AA7 SER A 370 ALA A 377 1 8
HELIX 8 AA8 ASN A 378 PHE A 381 5 4
HELIX 9 AA9 ASP A 382 PHE A 387 1 6
HELIX 10 AB1 GLY A 391 ASN A 400 1 10
HELIX 11 AB2 ASN A 400 PHE A 409 1 10
HELIX 12 AB3 ALA A 411 SER A 415 5 5
HELIX 13 AB4 SER A 418 HIS A 420 5 3
HELIX 14 AB5 LYS A 421 GLY A 426 1 6
HELIX 15 AB6 THR A 443 LYS A 455 1 13
HELIX 16 AB7 PHE A 459 ASN A 464 1 6
HELIX 17 AB8 TRP A 465 ARG A 467 5 3
HELIX 18 AB9 ASN A 468 LYS A 478 1 11
HELIX 19 AC1 VAL A 500 GLN A 505 5 6
HELIX 20 AC2 HIS A 506 TRP A 510 5 5
HELIX 21 AC3 TRP A 525 LYS A 530 1 6
HELIX 22 AC4 LYS A 530 ALA A 546 1 17
SHEET 1 AA1 8 SER A 238 LYS A 245 0
SHEET 2 AA1 8 VAL A 248 LEU A 255 -1 O PHE A 252 N GLY A 240
SHEET 3 AA1 8 ARG A 287 MET A 291 -1 O VAL A 288 N LEU A 255
SHEET 4 AA1 8 ALA A 260 CYS A 264 1 N VAL A 261 O ARG A 287
SHEET 5 AA1 8 ALA A 329 HIS A 334 1 O VAL A 330 N CYS A 262
SHEET 6 AA1 8 VAL A 352 LEU A 358 1 O LEU A 358 N GLY A 333
SHEET 7 AA1 8 ALA A 488 ALA A 493 1 O VAL A 491 N SER A 357
SHEET 8 AA1 8 LEU A 514 ILE A 519 1 O LYS A 515 N ALA A 488
LINK OD1 ASP A 509 MG MG A 602 1555 1555 2.36
LINK OD2 ASP A 509 MG MG A 602 1555 1555 2.24
LINK MG MG A 602 O HOH A 802 1555 1555 2.65
CISPEP 1 PHE A 267 PRO A 268 0 -10.38
SITE 1 AC1 16 ASP A 335 TRP A 336 MET A 339 ILE A 375
SITE 2 AC1 16 PHE A 381 TYR A 383 GLN A 384 SER A 415
SITE 3 AC1 16 MET A 419 TYR A 466 MET A 469 VAL A 498
SITE 4 AC1 16 HIS A 524 TRP A 525 HOH A 717 HOH A 805
SITE 1 AC2 3 HIS A 506 ASP A 509 HOH A 802
CRYST1 80.091 92.180 106.998 90.00 90.00 90.00 I 2 2 2 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 0.012486 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010848 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009346 0.00000
TER 2595 ARG A 547
MASTER 467 0 2 22 8 0 5 6 2689 1 37 27
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