| content |
HEADER HYDROLASE 23-AUG-18 6HGV
TITLE SOLUBLE EPOXIDE HYDROLASE IN COMPLEX WITH TALINOLOL
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,K.HIESINGER,E.PROSCHAK
REVDAT 1 03-JUL-19 6HGV 0
JRNL AUTH K.HIESINGER,J.S.KRAMER,J.ACHENBACH,D.MOSER,J.WEBER,
JRNL AUTH 2 S.K.WITTMANN,C.MORISSEAU,C.ANGIONI,G.GEISSLINGER,A.S.KAHNT,
JRNL AUTH 3 A.KAISER,A.PROSCHAK,D.STEINHILBER,D.POGORYELOV,K.WAGNER,
JRNL AUTH 4 B.D.HAMMOCK,E.PROSCHAK
JRNL TITL COMPUTER-AIDED SELECTIVE OPTIMIZATION OF SIDE ACTIVITIES OF
JRNL TITL 2 TALINOLOL.
JRNL REF ACS MED.CHEM.LETT. V. 10 899 2019
JRNL REFN ISSN 1948-5875
JRNL PMID 31223445
JRNL DOI 10.1021/ACSMEDCHEMLETT.9B00075
REMARK 2
REMARK 2 RESOLUTION. 2.00 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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.94
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 26655
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.176
REMARK 3 R VALUE (WORKING SET) : 0.174
REMARK 3 FREE R VALUE : 0.204
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 6.370
REMARK 3 FREE R VALUE TEST SET COUNT : 1698
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 45.9521 - 4.5776 1.00 2213 151 0.1747 0.1926
REMARK 3 2 4.5776 - 3.6338 1.00 2105 144 0.1405 0.1652
REMARK 3 3 3.6338 - 3.1746 1.00 2107 143 0.1651 0.1882
REMARK 3 4 3.1746 - 2.8844 1.00 2060 140 0.1832 0.2144
REMARK 3 5 2.8844 - 2.6777 1.00 2091 143 0.1918 0.2556
REMARK 3 6 2.6777 - 2.5198 1.00 2047 138 0.1901 0.2259
REMARK 3 7 2.5198 - 2.3936 1.00 2082 142 0.1891 0.2104
REMARK 3 8 2.3936 - 2.2894 1.00 2066 141 0.1862 0.2388
REMARK 3 9 2.2894 - 2.2013 1.00 2047 140 0.1847 0.2009
REMARK 3 10 2.2013 - 2.1253 1.00 2036 137 0.1992 0.2510
REMARK 3 11 2.1253 - 2.0589 1.00 2081 142 0.2257 0.2782
REMARK 3 12 2.0589 - 2.0000 1.00 2022 137 0.2565 0.2866
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) : 0.220
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.810
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 38.12
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 51.54
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 : 0.005 2763
REMARK 3 ANGLE : 0.806 3760
REMARK 3 CHIRALITY : 0.047 385
REMARK 3 PLANARITY : 0.004 484
REMARK 3 DIHEDRAL : 24.547 1028
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 8
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 229 THROUGH 270 )
REMARK 3 ORIGIN FOR THE GROUP (A): -5.5888 -6.5224 -36.5960
REMARK 3 T TENSOR
REMARK 3 T11: 0.2292 T22: 0.2513
REMARK 3 T33: 0.2695 T12: -0.0015
REMARK 3 T13: 0.0090 T23: 0.0343
REMARK 3 L TENSOR
REMARK 3 L11: 4.3656 L22: 5.1271
REMARK 3 L33: 5.0314 L12: 2.4890
REMARK 3 L13: -0.3925 L23: 0.9882
REMARK 3 S TENSOR
REMARK 3 S11: -0.0953 S12: 0.0337 S13: 0.4166
REMARK 3 S21: -0.3468 S22: 0.0476 S23: 0.0952
REMARK 3 S31: -0.1095 S32: 0.0924 S33: 0.0321
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 271 THROUGH 370 )
REMARK 3 ORIGIN FOR THE GROUP (A): -3.4475 -16.5148 -31.3965
REMARK 3 T TENSOR
REMARK 3 T11: 0.2574 T22: 0.2778
REMARK 3 T33: 0.3087 T12: 0.0062
REMARK 3 T13: 0.0297 T23: 0.0123
REMARK 3 L TENSOR
REMARK 3 L11: 2.7961 L22: 2.3847
REMARK 3 L33: 1.5108 L12: 0.4317
REMARK 3 L13: -0.4915 L23: -0.0614
REMARK 3 S TENSOR
REMARK 3 S11: -0.0699 S12: -0.1184 S13: -0.3150
REMARK 3 S21: -0.1071 S22: 0.0088 S23: -0.3398
REMARK 3 S31: 0.2277 S32: 0.1310 S33: 0.0474
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 371 THROUGH 399 )
REMARK 3 ORIGIN FOR THE GROUP (A): -13.2422 -31.2588 -44.8105
REMARK 3 T TENSOR
REMARK 3 T11: 0.7352 T22: 0.4208
REMARK 3 T33: 0.6229 T12: -0.1183
REMARK 3 T13: 0.1152 T23: -0.0408
REMARK 3 L TENSOR
REMARK 3 L11: 7.1547 L22: 7.2630
REMARK 3 L33: 7.8182 L12: -2.6947
REMARK 3 L13: 0.9903 L23: -2.9180
REMARK 3 S TENSOR
REMARK 3 S11: -0.4029 S12: -0.0857 S13: -1.3470
REMARK 3 S21: -0.2458 S22: 0.3843 S23: 0.2899
REMARK 3 S31: 0.8933 S32: -0.4793 S33: -0.0712
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 400 THROUGH 418 )
REMARK 3 ORIGIN FOR THE GROUP (A): -25.1374 -18.9414 -43.4814
REMARK 3 T TENSOR
REMARK 3 T11: 0.4348 T22: 0.3731
REMARK 3 T33: 0.4124 T12: -0.0623
REMARK 3 T13: -0.0853 T23: 0.0182
REMARK 3 L TENSOR
REMARK 3 L11: 9.8299 L22: 4.7601
REMARK 3 L33: 4.5300 L12: 4.0996
REMARK 3 L13: -6.5703 L23: -3.3963
REMARK 3 S TENSOR
REMARK 3 S11: -0.1918 S12: -0.1028 S13: -0.6035
REMARK 3 S21: -0.5255 S22: -0.0084 S23: 0.2683
REMARK 3 S31: 0.5814 S32: -0.0792 S33: 0.2785
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 419 THROUGH 435 )
REMARK 3 ORIGIN FOR THE GROUP (A): -24.5679 -28.2878 -48.4051
REMARK 3 T TENSOR
REMARK 3 T11: 1.0873 T22: 0.7924
REMARK 3 T33: 1.1069 T12: -0.3259
REMARK 3 T13: -0.2857 T23: -0.0552
REMARK 3 L TENSOR
REMARK 3 L11: 8.9021 L22: 4.3618
REMARK 3 L33: 3.0427 L12: -6.0147
REMARK 3 L13: -2.7989 L23: 2.7215
REMARK 3 S TENSOR
REMARK 3 S11: 0.6287 S12: -0.2206 S13: -2.3503
REMARK 3 S21: -0.4586 S22: 0.0341 S23: 1.1264
REMARK 3 S31: 1.1720 S32: -0.6934 S33: -0.7797
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 436 THROUGH 509 )
REMARK 3 ORIGIN FOR THE GROUP (A): -11.4963 -22.4334 -34.6362
REMARK 3 T TENSOR
REMARK 3 T11: 0.3339 T22: 0.2646
REMARK 3 T33: 0.3285 T12: -0.0450
REMARK 3 T13: 0.0332 T23: 0.0091
REMARK 3 L TENSOR
REMARK 3 L11: 2.4600 L22: 2.2774
REMARK 3 L33: 2.0325 L12: -0.0941
REMARK 3 L13: -0.1053 L23: -0.1264
REMARK 3 S TENSOR
REMARK 3 S11: -0.0930 S12: 0.0018 S13: -0.2564
REMARK 3 S21: -0.1864 S22: 0.0292 S23: -0.1458
REMARK 3 S31: 0.2072 S32: -0.0298 S33: 0.0614
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 510 THROUGH 530 )
REMARK 3 ORIGIN FOR THE GROUP (A): -17.2229 -20.4578 -24.0434
REMARK 3 T TENSOR
REMARK 3 T11: 0.3564 T22: 0.4236
REMARK 3 T33: 0.3043 T12: -0.0355
REMARK 3 T13: 0.0546 T23: 0.0638
REMARK 3 L TENSOR
REMARK 3 L11: 5.5270 L22: 6.2155
REMARK 3 L33: 5.5782 L12: -3.9972
REMARK 3 L13: 5.4399 L23: -4.1990
REMARK 3 S TENSOR
REMARK 3 S11: 0.0052 S12: -0.5257 S13: -0.1560
REMARK 3 S21: -0.0229 S22: 0.0949 S23: 0.2277
REMARK 3 S31: 0.4666 S32: -0.2571 S33: -0.1388
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 531 THROUGH 547 )
REMARK 3 ORIGIN FOR THE GROUP (A): -14.7164 -10.6007 -18.9328
REMARK 3 T TENSOR
REMARK 3 T11: 0.3664 T22: 0.4547
REMARK 3 T33: 0.2307 T12: 0.0263
REMARK 3 T13: 0.0660 T23: -0.0393
REMARK 3 L TENSOR
REMARK 3 L11: 4.5527 L22: 9.6806
REMARK 3 L33: 4.3653 L12: -2.9445
REMARK 3 L13: 4.4155 L23: -2.1268
REMARK 3 S TENSOR
REMARK 3 S11: -0.1589 S12: -1.2162 S13: 0.1451
REMARK 3 S21: 0.9870 S22: 0.3215 S23: 0.1081
REMARK 3 S31: -0.4761 S32: -0.4778 S33: -0.0981
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 6HGV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 23-AUG-18.
REMARK 100 THE DEPOSITION ID IS D_1200011562.
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 : MIRRORS
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 : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26999
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.990
REMARK 200 RESOLUTION RANGE LOW (A) : 45.940
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 13.06
REMARK 200 R MERGE (I) : 0.07300
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 20.2700
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.99
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.04
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.1
REMARK 200 DATA REDUNDANCY IN SHELL : 11.98
REMARK 200 R MERGE FOR SHELL (I) : 0.88600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.650
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: 6FR2
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.78
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.45
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 39.86500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 45.94000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 53.02500
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 39.86500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 45.94000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 53.02500
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 39.86500
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 45.94000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 53.02500
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 39.86500
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 45.94000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 53.02500
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: 12650 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 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 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 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 ASP A 292 N - CA - C ANGL. DEV. = -16.4 DEGREES
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 SER A 231 -161.61 -100.35
REMARK 500 SER A 231 -168.87 -103.96
REMARK 500 GLU A 269 -142.32 -119.47
REMARK 500 ASP A 335 -125.63 61.20
REMARK 500 ASN A 359 -44.86 73.52
REMARK 500 VAL A 498 -61.37 -104.87
REMARK 500 HIS A 513 30.14 -97.32
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 A 849 DISTANCE = 8.88 ANGSTROMS
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 601 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 509 OD1
REMARK 620 2 ASP A 509 OD2 59.0
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue G3Q A 602
DBREF 6HGV A 222 555 UNP P34913 HYES_HUMAN 222 555
SEQADV 6HGV MET A 219 UNP P34913 INITIATING METHIONINE
SEQADV 6HGV ALA A 220 UNP P34913 EXPRESSION TAG
SEQADV 6HGV SER A 221 UNP P34913 EXPRESSION TAG
SEQADV 6HGV LEU A 556 UNP P34913 EXPRESSION TAG
SEQADV 6HGV LEU A 557 UNP P34913 EXPRESSION TAG
SEQADV 6HGV GLU A 558 UNP P34913 EXPRESSION TAG
SEQADV 6HGV HIS A 559 UNP P34913 EXPRESSION TAG
SEQADV 6HGV HIS A 560 UNP P34913 EXPRESSION TAG
SEQADV 6HGV HIS A 561 UNP P34913 EXPRESSION TAG
SEQADV 6HGV HIS A 562 UNP P34913 EXPRESSION TAG
SEQADV 6HGV HIS A 563 UNP P34913 EXPRESSION TAG
SEQADV 6HGV 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 MG A 601 1
HET G3Q A 602 52
HETNAM MG MAGNESIUM ION
HETNAM G3Q R-TALINOLOL
HETSYN G3Q TALINOLOL
FORMUL 2 MG MG 2+
FORMUL 3 G3Q C20 H33 N3 O3
FORMUL 4 HOH *149(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 VAL A 380 5 3
HELIX 9 AA9 PHE A 381 PHE A 387 1 7
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 LYS A 421 GLY A 426 1 6
HELIX 14 AB5 THR A 443 LYS A 455 1 13
HELIX 15 AB6 PHE A 459 TRP A 465 1 7
HELIX 16 AB7 ASN A 468 LYS A 478 1 11
HELIX 17 AB8 VAL A 500 GLN A 505 5 6
HELIX 18 AB9 HIS A 506 TRP A 510 5 5
HELIX 19 AC1 TRP A 525 LYS A 530 1 6
HELIX 20 AC2 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 ASP A 292 -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 LEU A 289
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 MET A 490
LINK OD1 ASP A 509 MG MG A 601 1555 1555 2.33
LINK OD2 ASP A 509 MG MG A 601 1555 1555 2.11
CISPEP 1 PHE A 267 PRO A 268 0 -9.86
SITE 1 AC1 2 HIS A 506 ASP A 509
SITE 1 AC2 14 ASP A 335 TRP A 336 MET A 339 SER A 374
SITE 2 AC2 14 PHE A 381 TYR A 383 GLN A 384 SER A 415
SITE 3 AC2 14 LEU A 417 MET A 419 TYR A 466 PHE A 497
SITE 4 AC2 14 HIS A 524 HOH A 715
CRYST1 79.730 91.880 106.050 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 0.012542 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010884 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009430 0.00000
TER 2624 ARG A 547
MASTER 463 0 2 20 8 0 5 6 2733 1 55 27
END |