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HEADER HYDROLASE 14-MAY-12 4F60
TITLE CRYSTAL STRUCTURE OF RHODOCOCCUS RHODOCHROUS HALOALKANE DEHALOGENASE
TITLE 2 MUTANT (T148L, G171Q, A172V, C176F).
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HALOALKANE DEHALOGENASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.8.1.5;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RHODOCOCCUS RHODOCHROUS;
SOURCE 3 ORGANISM_TAXID: 1829;
SOURCE 4 GENE: DHAA;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS MUTATION IN ACCESS TUNNEL, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.PLEVAKA,I.KUTA-SMATANOVA,P.REZACOVA
REVDAT 1 23-JAN-13 4F60 0
JRNL AUTH T.KOUDELAKOVA,R.CHALOUPKOVA,J.BREZOVSKY,Z.PROKOP,
JRNL AUTH 2 E.SEBESTOVA,M.HESSELER,M.KHABIRI,M.PLEVAKA,D.KULIK,
JRNL AUTH 3 I.KUTA SMATANOVA,P.REZACOVA,R.ETTRICH,U.T.BORNSCHEUER,
JRNL AUTH 4 J.DAMBORSKY
JRNL TITL ENGINEERING ENZYME STABILITY AND RESISTANCE TO AN ORGANIC
JRNL TITL 2 COSOLVENT BY MODIFICATION OF RESIDUES IN THE ACCESS TUNNEL.
JRNL REF ANGEW.CHEM.INT.ED.ENGL. 2013
JRNL REFN ESSN 1521-3773
JRNL PMID 23303607
JRNL DOI 10.1002/ANIE.201206708
REMARK 2
REMARK 2 RESOLUTION. 1.45 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.3.0037
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.45
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.02
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.8
REMARK 3 NUMBER OF REFLECTIONS : 50998
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.151
REMARK 3 R VALUE (WORKING SET) : 0.150
REMARK 3 FREE R VALUE : 0.171
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2721
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.45
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.49
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2698
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 70.05
REMARK 3 BIN R VALUE (WORKING SET) : 0.1790
REMARK 3 BIN FREE R VALUE SET COUNT : 160
REMARK 3 BIN FREE R VALUE : 0.2250
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2342
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 1
REMARK 3 SOLVENT ATOMS : 500
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 17.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.68
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.81000
REMARK 3 B22 (A**2) : -0.14000
REMARK 3 B33 (A**2) : -0.66000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.061
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.061
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.038
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.908
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.975
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.969
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2473 ; 0.012 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3396 ; 1.467 ; 1.959
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 305 ; 5.484 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 122 ;33.438 ;23.607
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 380 ;11.636 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 17 ;19.896 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 358 ; 0.096 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1969 ; 0.008 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1257 ; 0.209 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1694 ; 0.321 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 390 ; 0.152 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 16 ; 0.150 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 33 ; 0.221 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1515 ; 0.754 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2426 ; 1.090 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1093 ; 1.745 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 962 ; 2.677 ; 4.500
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 15
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 4 A 10
REMARK 3 ORIGIN FOR THE GROUP (A): -33.1640 9.3530 20.7300
REMARK 3 T TENSOR
REMARK 3 T11: -0.0788 T22: -0.1010
REMARK 3 T33: -0.0672 T12: -0.0003
REMARK 3 T13: 0.0354 T23: 0.0188
REMARK 3 L TENSOR
REMARK 3 L11: 2.6288 L22: 11.2964
REMARK 3 L33: 2.0433 L12: -0.5244
REMARK 3 L13: -0.3188 L23: -0.7719
REMARK 3 S TENSOR
REMARK 3 S11: 0.0418 S12: -0.1039 S13: -0.0812
REMARK 3 S21: -0.0983 S22: 0.0120 S23: 0.6348
REMARK 3 S31: -0.0036 S32: -0.1254 S33: -0.0538
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 11 A 32
REMARK 3 ORIGIN FOR THE GROUP (A): -19.9060 -3.5370 20.6790
REMARK 3 T TENSOR
REMARK 3 T11: -0.0194 T22: -0.1142
REMARK 3 T33: -0.0820 T12: 0.0086
REMARK 3 T13: 0.0146 T23: 0.0215
REMARK 3 L TENSOR
REMARK 3 L11: 1.6033 L22: 1.5604
REMARK 3 L33: 1.5242 L12: 0.2591
REMARK 3 L13: 0.0170 L23: -0.6585
REMARK 3 S TENSOR
REMARK 3 S11: 0.0178 S12: -0.0575 S13: -0.1649
REMARK 3 S21: -0.0074 S22: -0.0208 S23: -0.0930
REMARK 3 S31: 0.1822 S32: 0.1292 S33: 0.0030
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 33 A 70
REMARK 3 ORIGIN FOR THE GROUP (A): -22.3400 6.6170 16.2930
REMARK 3 T TENSOR
REMARK 3 T11: -0.0892 T22: -0.1391
REMARK 3 T33: -0.1464 T12: -0.0015
REMARK 3 T13: 0.0090 T23: 0.0117
REMARK 3 L TENSOR
REMARK 3 L11: 0.8689 L22: 1.4702
REMARK 3 L33: 0.9275 L12: 0.0189
REMARK 3 L13: 0.0973 L23: -0.0657
REMARK 3 S TENSOR
REMARK 3 S11: -0.0083 S12: -0.0333 S13: -0.0621
REMARK 3 S21: 0.0134 S22: -0.0066 S23: 0.0464
REMARK 3 S31: 0.0812 S32: -0.0018 S33: 0.0149
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 71 A 87
REMARK 3 ORIGIN FOR THE GROUP (A): -7.8960 6.0810 27.4290
REMARK 3 T TENSOR
REMARK 3 T11: -0.0242 T22: -0.0175
REMARK 3 T33: -0.0925 T12: 0.0336
REMARK 3 T13: -0.0581 T23: 0.0473
REMARK 3 L TENSOR
REMARK 3 L11: 1.2309 L22: 3.0422
REMARK 3 L33: 2.4858 L12: 1.1906
REMARK 3 L13: -1.1519 L23: -0.1861
REMARK 3 S TENSOR
REMARK 3 S11: -0.0061 S12: -0.2332 S13: -0.1074
REMARK 3 S21: 0.2624 S22: -0.0585 S23: -0.2951
REMARK 3 S31: 0.1698 S32: 0.3764 S33: 0.0647
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 88 A 132
REMARK 3 ORIGIN FOR THE GROUP (A): -11.2230 6.3170 11.3370
REMARK 3 T TENSOR
REMARK 3 T11: -0.0878 T22: -0.1181
REMARK 3 T33: -0.1142 T12: 0.0203
REMARK 3 T13: 0.0170 T23: 0.0174
REMARK 3 L TENSOR
REMARK 3 L11: 1.0477 L22: 1.2256
REMARK 3 L33: 1.2563 L12: -0.1493
REMARK 3 L13: -0.1863 L23: -0.2655
REMARK 3 S TENSOR
REMARK 3 S11: -0.0508 S12: -0.0370 S13: -0.1129
REMARK 3 S21: -0.0479 S22: -0.0333 S23: -0.0944
REMARK 3 S31: 0.1806 S32: 0.1038 S33: 0.0842
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 133 A 137
REMARK 3 ORIGIN FOR THE GROUP (A): -5.3420 26.1880 13.7530
REMARK 3 T TENSOR
REMARK 3 T11: -0.0251 T22: -0.0212
REMARK 3 T33: -0.0025 T12: -0.0365
REMARK 3 T13: 0.0286 T23: 0.0008
REMARK 3 L TENSOR
REMARK 3 L11: 2.1053 L22: 11.1943
REMARK 3 L33: 2.7286 L12: 2.1424
REMARK 3 L13: 0.6982 L23: 5.2093
REMARK 3 S TENSOR
REMARK 3 S11: 0.0882 S12: 0.2173 S13: 0.4557
REMARK 3 S21: -0.1849 S22: 0.1603 S23: -0.4129
REMARK 3 S31: -0.4053 S32: 0.1341 S33: -0.2485
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 138 A 177
REMARK 3 ORIGIN FOR THE GROUP (A): -13.5710 26.3590 28.0680
REMARK 3 T TENSOR
REMARK 3 T11: -0.0106 T22: -0.0623
REMARK 3 T33: -0.0667 T12: -0.0073
REMARK 3 T13: -0.0337 T23: -0.0499
REMARK 3 L TENSOR
REMARK 3 L11: 1.6955 L22: 1.4413
REMARK 3 L33: 1.3810 L12: -0.0015
REMARK 3 L13: -0.0519 L23: -0.0804
REMARK 3 S TENSOR
REMARK 3 S11: 0.0104 S12: -0.2026 S13: 0.2236
REMARK 3 S21: 0.2618 S22: 0.0177 S23: -0.1509
REMARK 3 S31: -0.1444 S32: 0.1476 S33: -0.0281
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 178 A 183
REMARK 3 ORIGIN FOR THE GROUP (A): -31.3600 22.1200 23.9570
REMARK 3 T TENSOR
REMARK 3 T11: -0.0509 T22: -0.0745
REMARK 3 T33: -0.0573 T12: 0.0081
REMARK 3 T13: 0.0390 T23: -0.0190
REMARK 3 L TENSOR
REMARK 3 L11: 0.5302 L22: 8.4467
REMARK 3 L33: 4.5864 L12: 1.5854
REMARK 3 L13: -1.1689 L23: -5.4661
REMARK 3 S TENSOR
REMARK 3 S11: 0.0698 S12: -0.3302 S13: 0.1164
REMARK 3 S21: 0.4274 S22: -0.0348 S23: 0.3444
REMARK 3 S31: -0.0872 S32: 0.1460 S33: -0.0349
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 184 A 197
REMARK 3 ORIGIN FOR THE GROUP (A): -24.0470 13.0320 32.4330
REMARK 3 T TENSOR
REMARK 3 T11: 0.0207 T22: -0.0673
REMARK 3 T33: -0.1266 T12: 0.0039
REMARK 3 T13: 0.0333 T23: 0.0121
REMARK 3 L TENSOR
REMARK 3 L11: 3.2485 L22: 1.4253
REMARK 3 L33: 3.4411 L12: 0.1797
REMARK 3 L13: 1.7835 L23: 0.5327
REMARK 3 S TENSOR
REMARK 3 S11: 0.0179 S12: -0.2488 S13: -0.1105
REMARK 3 S21: 0.2775 S22: 0.0397 S23: 0.0856
REMARK 3 S31: 0.1568 S32: 0.0049 S33: -0.0577
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 198 A 214
REMARK 3 ORIGIN FOR THE GROUP (A): -7.3920 18.3520 27.2240
REMARK 3 T TENSOR
REMARK 3 T11: -0.0640 T22: -0.0268
REMARK 3 T33: -0.0921 T12: 0.0040
REMARK 3 T13: -0.0572 T23: -0.0195
REMARK 3 L TENSOR
REMARK 3 L11: 1.3587 L22: 2.2809
REMARK 3 L33: 5.1411 L12: 0.3363
REMARK 3 L13: -2.0129 L23: -0.8617
REMARK 3 S TENSOR
REMARK 3 S11: 0.0628 S12: -0.1878 S13: 0.1059
REMARK 3 S21: 0.2024 S22: 0.0449 S23: -0.1857
REMARK 3 S31: -0.1000 S32: 0.3345 S33: -0.1077
REMARK 3
REMARK 3 TLS GROUP : 11
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 215 A 246
REMARK 3 ORIGIN FOR THE GROUP (A): -8.7690 17.5790 8.3280
REMARK 3 T TENSOR
REMARK 3 T11: -0.1001 T22: -0.1104
REMARK 3 T33: -0.1115 T12: -0.0036
REMARK 3 T13: 0.0118 T23: 0.0243
REMARK 3 L TENSOR
REMARK 3 L11: 1.9296 L22: 0.7620
REMARK 3 L33: 0.8128 L12: -0.4088
REMARK 3 L13: -0.5165 L23: 0.2189
REMARK 3 S TENSOR
REMARK 3 S11: -0.0107 S12: -0.0261 S13: 0.0889
REMARK 3 S21: -0.0398 S22: -0.0004 S23: -0.1384
REMARK 3 S31: -0.0181 S32: 0.1397 S33: 0.0111
REMARK 3
REMARK 3 TLS GROUP : 12
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 247 A 255
REMARK 3 ORIGIN FOR THE GROUP (A): -14.0940 26.6890 5.2650
REMARK 3 T TENSOR
REMARK 3 T11: -0.0658 T22: -0.0798
REMARK 3 T33: -0.0357 T12: -0.0276
REMARK 3 T13: 0.0346 T23: 0.0233
REMARK 3 L TENSOR
REMARK 3 L11: 8.1211 L22: 9.8421
REMARK 3 L33: 8.6118 L12: -7.5530
REMARK 3 L13: -5.6821 L23: 3.0929
REMARK 3 S TENSOR
REMARK 3 S11: 0.1447 S12: -0.1585 S13: 0.4769
REMARK 3 S21: -0.2204 S22: 0.1888 S23: -0.6798
REMARK 3 S31: -0.5448 S32: 0.2047 S33: -0.3335
REMARK 3
REMARK 3 TLS GROUP : 13
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 256 A 267
REMARK 3 ORIGIN FOR THE GROUP (A): -16.8790 19.5420 0.2470
REMARK 3 T TENSOR
REMARK 3 T11: -0.0538 T22: -0.0507
REMARK 3 T33: -0.0837 T12: 0.0075
REMARK 3 T13: 0.0099 T23: 0.0441
REMARK 3 L TENSOR
REMARK 3 L11: 3.9023 L22: 3.0581
REMARK 3 L33: 1.3789 L12: -2.7244
REMARK 3 L13: -1.9159 L23: 1.1977
REMARK 3 S TENSOR
REMARK 3 S11: 0.1267 S12: 0.3840 S13: 0.3406
REMARK 3 S21: -0.2355 S22: -0.1423 S23: -0.3126
REMARK 3 S31: -0.1311 S32: -0.0678 S33: 0.0155
REMARK 3
REMARK 3 TLS GROUP : 14
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 268 A 288
REMARK 3 ORIGIN FOR THE GROUP (A): -26.3430 17.6060 10.9590
REMARK 3 T TENSOR
REMARK 3 T11: -0.1137 T22: -0.1365
REMARK 3 T33: -0.1350 T12: 0.0090
REMARK 3 T13: 0.0007 T23: 0.0030
REMARK 3 L TENSOR
REMARK 3 L11: 0.7785 L22: 1.4496
REMARK 3 L33: 1.6471 L12: 0.0696
REMARK 3 L13: -0.1861 L23: 0.6090
REMARK 3 S TENSOR
REMARK 3 S11: 0.0034 S12: 0.0004 S13: 0.0617
REMARK 3 S21: 0.0242 S22: -0.0417 S23: 0.1077
REMARK 3 S31: 0.0162 S32: -0.1057 S33: 0.0384
REMARK 3
REMARK 3 TLS GROUP : 15
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 289 A 293
REMARK 3 ORIGIN FOR THE GROUP (A): -21.7020 6.6450 -0.7350
REMARK 3 T TENSOR
REMARK 3 T11: -0.0500 T22: -0.0766
REMARK 3 T33: -0.1183 T12: -0.0026
REMARK 3 T13: 0.0145 T23: -0.0386
REMARK 3 L TENSOR
REMARK 3 L11: 16.3442 L22: 12.7671
REMARK 3 L33: 5.1974 L12: -0.2425
REMARK 3 L13: 1.0868 L23: 1.3851
REMARK 3 S TENSOR
REMARK 3 S11: -0.0944 S12: 0.7079 S13: -0.3691
REMARK 3 S21: -0.8254 S22: 0.1603 S23: -0.2451
REMARK 3 S31: 0.2786 S32: 0.1265 S33: -0.0659
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 4F60 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-MAY-12.
REMARK 100 THE RCSB ID CODE IS RCSB072498.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-JAN-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : BESSY
REMARK 200 BEAMLINE : 14.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.978
REMARK 200 MONOCHROMATOR : SI 111 DOUBLE CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 53781
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.450
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.9
REMARK 200 DATA REDUNDANCY : 6.900
REMARK 200 R MERGE (I) : 0.03300
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 65.8400
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.45
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.50
REMARK 200 COMPLETENESS FOR SHELL (%) : 74.2
REMARK 200 DATA REDUNDANCY IN SHELL : 4.80
REMARK 200 R MERGE FOR SHELL (I) : 0.25800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 3FBW
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.70
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.27
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M BISTRIS PROPANE PH6.5, 0.2M
REMARK 280 SODIUM FLUORIDE,20% PEG3350, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 26.00900
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 42.67600
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 34.96500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 42.67600
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 26.00900
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 34.96500
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 SER A 2
REMARK 465 GLU A 3
REMARK 465 HIS A 294
REMARK 465 HIS A 295
REMARK 465 HIS A 296
REMARK 465 HIS A 297
REMARK 465 HIS A 298
REMARK 465 HIS A 299
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 OD1 ASP A 82 O HOH A 895 2.09
REMARK 500 O HOH A 436 O HOH A 898 2.11
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 O HOH A 484 O HOH A 860 4455 2.15
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 PRO A 42 45.50 -102.82
REMARK 500 THR A 43 -158.90 -102.40
REMARK 500 GLU A 98 -93.40 -105.00
REMARK 500 ASP A 106 -129.99 53.19
REMARK 500 ASP A 156 -56.74 72.47
REMARK 500 VAL A 245 -65.28 -131.77
REMARK 500 LEU A 271 -97.20 -118.16
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 872 DISTANCE = 5.29 ANGSTROMS
REMARK 525 HOH A 875 DISTANCE = 6.44 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE F A 301
DBREF 4F60 A 1 293 UNP P0A3G2 DHAA_RHORH 1 293
SEQADV 4F60 LEU A 148 UNP P0A3G2 THR 148 ENGINEERED MUTATION
SEQADV 4F60 GLN A 171 UNP P0A3G2 GLY 171 ENGINEERED MUTATION
SEQADV 4F60 VAL A 172 UNP P0A3G2 ALA 172 ENGINEERED MUTATION
SEQADV 4F60 PHE A 176 UNP P0A3G2 CYS 176 ENGINEERED MUTATION
SEQADV 4F60 HIS A 294 UNP P0A3G2 EXPRESSION TAG
SEQADV 4F60 HIS A 295 UNP P0A3G2 EXPRESSION TAG
SEQADV 4F60 HIS A 296 UNP P0A3G2 EXPRESSION TAG
SEQADV 4F60 HIS A 297 UNP P0A3G2 EXPRESSION TAG
SEQADV 4F60 HIS A 298 UNP P0A3G2 EXPRESSION TAG
SEQADV 4F60 HIS A 299 UNP P0A3G2 EXPRESSION TAG
SEQRES 1 A 299 MET SER GLU ILE GLY THR GLY PHE PRO PHE ASP PRO HIS
SEQRES 2 A 299 TYR VAL GLU VAL LEU GLY GLU ARG MET HIS TYR VAL ASP
SEQRES 3 A 299 VAL GLY PRO ARG ASP GLY THR PRO VAL LEU PHE LEU HIS
SEQRES 4 A 299 GLY ASN PRO THR SER SER TYR LEU TRP ARG ASN ILE ILE
SEQRES 5 A 299 PRO HIS VAL ALA PRO SER HIS ARG CYS ILE ALA PRO ASP
SEQRES 6 A 299 LEU ILE GLY MET GLY LYS SER ASP LYS PRO ASP LEU ASP
SEQRES 7 A 299 TYR PHE PHE ASP ASP HIS VAL ARG TYR LEU ASP ALA PHE
SEQRES 8 A 299 ILE GLU ALA LEU GLY LEU GLU GLU VAL VAL LEU VAL ILE
SEQRES 9 A 299 HIS ASP TRP GLY SER ALA LEU GLY PHE HIS TRP ALA LYS
SEQRES 10 A 299 ARG ASN PRO GLU ARG VAL LYS GLY ILE ALA CYS MET GLU
SEQRES 11 A 299 PHE ILE ARG PRO ILE PRO THR TRP ASP GLU TRP PRO GLU
SEQRES 12 A 299 PHE ALA ARG GLU LEU PHE GLN ALA PHE ARG THR ALA ASP
SEQRES 13 A 299 VAL GLY ARG GLU LEU ILE ILE ASP GLN ASN ALA PHE ILE
SEQRES 14 A 299 GLU GLN VAL LEU PRO LYS PHE VAL VAL ARG PRO LEU THR
SEQRES 15 A 299 GLU VAL GLU MET ASP HIS TYR ARG GLU PRO PHE LEU LYS
SEQRES 16 A 299 PRO VAL ASP ARG GLU PRO LEU TRP ARG PHE PRO ASN GLU
SEQRES 17 A 299 LEU PRO ILE ALA GLY GLU PRO ALA ASN ILE VAL ALA LEU
SEQRES 18 A 299 VAL GLU ALA TYR MET ASN TRP LEU HIS GLN SER PRO VAL
SEQRES 19 A 299 PRO LYS LEU LEU PHE TRP GLY THR PRO GLY VAL LEU ILE
SEQRES 20 A 299 PRO PRO ALA GLU ALA ALA ARG LEU ALA GLU SER LEU PRO
SEQRES 21 A 299 ASN CYS LYS THR VAL ASP ILE GLY PRO GLY LEU HIS TYR
SEQRES 22 A 299 LEU GLN GLU ASP ASN PRO ASP LEU ILE GLY SER GLU ILE
SEQRES 23 A 299 ALA ARG TRP LEU PRO ALA LEU HIS HIS HIS HIS HIS HIS
HET F A 301 1
HETNAM F FLUORIDE ION
FORMUL 2 F F 1-
FORMUL 3 HOH *500(H2 O)
HELIX 1 1 SER A 44 ARG A 49 5 6
HELIX 2 2 ILE A 51 ALA A 56 1 6
HELIX 3 3 PHE A 80 LEU A 95 1 16
HELIX 4 4 ASP A 106 ASN A 119 1 14
HELIX 5 5 THR A 137 TRP A 141 5 5
HELIX 6 6 PRO A 142 PHE A 144 5 3
HELIX 7 7 ALA A 145 ARG A 153 1 9
HELIX 8 8 ASP A 156 ILE A 163 1 8
HELIX 9 9 ASN A 166 GLN A 171 1 6
HELIX 10 10 GLN A 171 PHE A 176 1 6
HELIX 11 11 THR A 182 GLU A 191 1 10
HELIX 12 12 PRO A 192 LEU A 194 5 3
HELIX 13 13 LYS A 195 ASP A 198 5 4
HELIX 14 14 ARG A 199 LEU A 209 1 11
HELIX 15 15 PRO A 215 SER A 232 1 18
HELIX 16 16 PRO A 248 LEU A 259 1 12
HELIX 17 17 TYR A 273 ASN A 278 1 6
HELIX 18 18 ASN A 278 LEU A 290 1 13
HELIX 19 19 PRO A 291 LEU A 293 5 3
SHEET 1 A 8 HIS A 13 VAL A 17 0
SHEET 2 A 8 GLU A 20 VAL A 27 -1 O GLU A 20 N VAL A 17
SHEET 3 A 8 CYS A 61 PRO A 64 -1 O CYS A 61 N VAL A 27
SHEET 4 A 8 VAL A 35 LEU A 38 1 N VAL A 35 O ILE A 62
SHEET 5 A 8 VAL A 100 HIS A 105 1 O VAL A 101 N LEU A 36
SHEET 6 A 8 VAL A 123 MET A 129 1 O ALA A 127 N LEU A 102
SHEET 7 A 8 LYS A 236 PRO A 243 1 O LEU A 237 N CYS A 128
SHEET 8 A 8 CYS A 262 GLY A 270 1 O ILE A 267 N TRP A 240
CISPEP 1 ASN A 41 PRO A 42 0 -6.74
CISPEP 2 GLU A 214 PRO A 215 0 -7.56
CISPEP 3 THR A 242 PRO A 243 0 4.02
SITE 1 AC1 6 ASN A 41 TRP A 107 PHE A 168 PHE A 205
SITE 2 AC1 6 PRO A 206 HOH A 685
CRYST1 52.018 69.930 85.352 90.00 90.00 90.00 P 21 21 21 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.019224 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014300 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011716 0.00000
TER 2384 LEU A 293
MASTER 590 0 1 19 8 0 2 6 2843 1 0 23
END |