| content |
HEADER HYDROLASE 11-DEC-23 8VB3
TITLE DIENELACTONE HYDROLASE FROM SOLIMONAS FLUMINIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIENELACTONE HYDROLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SOLIMONAS FLUMINIS;
SOURCE 3 ORGANISM_TAXID: 2086571;
SOURCE 4 GENE: C3942_20560;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS HYDROLASE, DIENELACTONE, METAGENOMIC, SOLIMONAS FLUMINIS, ESTERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.D.F.SCHNETTLER FERNANDEZ,E.C.CAMPBELL,F.HOLLFELDER
REVDAT 1 18-DEC-24 8VB3 0
JRNL AUTH J.D.F.SCHNETTLER FERNANDEZ,E.C.CAMPBELL,R.KHASHIEV,
JRNL AUTH 2 J.O.KLEIN,F.HOLLFELDER
JRNL TITL METAL-INDEPENDENT ORGANOPHOSPHATE HYDROLYSIS IN A PROTEIN
JRNL TITL 2 FAMILY POSSESSING A CATALYTIC TRIAD
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.45 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.20.1_4487
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 : GEOSTD + MONOMER LIBRARY + CDL V1.2
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.45
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.63
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.400
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 86212
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.159
REMARK 3 R VALUE (WORKING SET) : 0.158
REMARK 3 FREE R VALUE : 0.186
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.080
REMARK 3 FREE R VALUE TEST SET COUNT : 4382
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 39.6300 - 4.5000 1.00 2784 166 0.1621 0.1899
REMARK 3 2 4.5000 - 3.5800 1.00 2774 146 0.1403 0.1759
REMARK 3 3 3.5700 - 3.1200 1.00 2737 153 0.1595 0.1844
REMARK 3 4 3.1200 - 2.8400 1.00 2735 144 0.1684 0.1947
REMARK 3 5 2.8400 - 2.6300 1.00 2740 146 0.1719 0.1861
REMARK 3 6 2.6300 - 2.4800 1.00 2749 151 0.1698 0.1932
REMARK 3 7 2.4800 - 2.3600 1.00 2730 142 0.1662 0.1821
REMARK 3 8 2.3600 - 2.2500 1.00 2738 155 0.1509 0.1867
REMARK 3 9 2.2500 - 2.1700 1.00 2741 142 0.1562 0.1778
REMARK 3 10 2.1700 - 2.0900 1.00 2726 150 0.1563 0.1870
REMARK 3 11 2.0900 - 2.0300 1.00 2750 153 0.1454 0.1829
REMARK 3 12 2.0300 - 1.9700 1.00 2721 147 0.1470 0.1549
REMARK 3 13 1.9700 - 1.9200 1.00 2699 146 0.1545 0.1890
REMARK 3 14 1.9200 - 1.8700 1.00 2756 136 0.1643 0.2076
REMARK 3 15 1.8700 - 1.8300 1.00 2683 149 0.1623 0.1879
REMARK 3 16 1.8300 - 1.7900 1.00 2763 160 0.1536 0.1631
REMARK 3 17 1.7900 - 1.7500 1.00 2682 141 0.1512 0.1727
REMARK 3 18 1.7500 - 1.7200 1.00 2771 150 0.1483 0.1873
REMARK 3 19 1.7200 - 1.6900 1.00 2717 130 0.1575 0.2382
REMARK 3 20 1.6900 - 1.6600 1.00 2719 134 0.1458 0.1735
REMARK 3 21 1.6600 - 1.6300 1.00 2776 108 0.1415 0.1643
REMARK 3 22 1.6300 - 1.6100 1.00 2723 114 0.1500 0.1933
REMARK 3 23 1.6100 - 1.5800 1.00 2728 156 0.1526 0.1832
REMARK 3 24 1.5800 - 1.5600 0.99 2733 158 0.1628 0.2005
REMARK 3 25 1.5600 - 1.5400 1.00 2667 149 0.1711 0.2215
REMARK 3 26 1.5400 - 1.5200 0.99 2710 165 0.1665 0.2143
REMARK 3 27 1.5200 - 1.5000 0.99 2716 145 0.1714 0.1909
REMARK 3 28 1.5000 - 1.4800 0.99 2653 152 0.1759 0.2005
REMARK 3 29 1.4800 - 1.4700 0.99 2712 149 0.1807 0.1947
REMARK 3 30 1.4700 - 1.4500 0.99 2697 145 0.1829 0.2309
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
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) : 0.115
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.450
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 15.15
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.11
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 : 0.015 3893
REMARK 3 ANGLE : 1.520 5308
REMARK 3 CHIRALITY : 0.112 566
REMARK 3 PLANARITY : 0.014 715
REMARK 3 DIHEDRAL : 13.183 558
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 13
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID -2 THROUGH 30 )
REMARK 3 ORIGIN FOR THE GROUP (A): -7.8072 -12.7695 8.8741
REMARK 3 T TENSOR
REMARK 3 T11: 0.2289 T22: 0.2244
REMARK 3 T33: 0.1966 T12: 0.0034
REMARK 3 T13: -0.0179 T23: -0.0283
REMARK 3 L TENSOR
REMARK 3 L11: 0.3926 L22: 0.0774
REMARK 3 L33: 0.1849 L12: 0.0473
REMARK 3 L13: -0.0817 L23: 0.1000
REMARK 3 S TENSOR
REMARK 3 S11: 0.0663 S12: 0.1887 S13: -0.2382
REMARK 3 S21: -0.1007 S22: -0.1081 S23: 0.1597
REMARK 3 S31: 0.1736 S32: 0.0766 S33: -0.0126
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 31 THROUGH 73 )
REMARK 3 ORIGIN FOR THE GROUP (A): -1.1181 -4.9611 12.3977
REMARK 3 T TENSOR
REMARK 3 T11: 0.1626 T22: 0.2426
REMARK 3 T33: 0.1259 T12: 0.0086
REMARK 3 T13: -0.0033 T23: -0.0052
REMARK 3 L TENSOR
REMARK 3 L11: 0.4796 L22: 0.3458
REMARK 3 L33: 0.3763 L12: -0.1499
REMARK 3 L13: 0.0573 L23: 0.2447
REMARK 3 S TENSOR
REMARK 3 S11: 0.1033 S12: 0.2078 S13: -0.0536
REMARK 3 S21: -0.0550 S22: -0.0014 S23: -0.0646
REMARK 3 S31: 0.0813 S32: 0.1712 S33: 0.0645
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 74 THROUGH 87 )
REMARK 3 ORIGIN FOR THE GROUP (A): -2.9753 12.5568 7.0056
REMARK 3 T TENSOR
REMARK 3 T11: 0.3024 T22: 0.5610
REMARK 3 T33: 0.3463 T12: 0.0283
REMARK 3 T13: 0.1135 T23: 0.2025
REMARK 3 L TENSOR
REMARK 3 L11: 0.0645 L22: 0.1898
REMARK 3 L33: 0.0806 L12: -0.0464
REMARK 3 L13: 0.0089 L23: 0.1020
REMARK 3 S TENSOR
REMARK 3 S11: 0.0204 S12: 0.1528 S13: 0.2345
REMARK 3 S21: -0.2423 S22: 0.1350 S23: 0.0484
REMARK 3 S31: -0.0636 S32: -0.0549 S33: 0.0976
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 88 THROUGH 204 )
REMARK 3 ORIGIN FOR THE GROUP (A): -8.5249 4.8986 21.9875
REMARK 3 T TENSOR
REMARK 3 T11: 0.1188 T22: 0.1505
REMARK 3 T33: 0.1328 T12: 0.0116
REMARK 3 T13: 0.0113 T23: 0.0279
REMARK 3 L TENSOR
REMARK 3 L11: 0.9236 L22: 0.2143
REMARK 3 L33: 0.6900 L12: -0.2186
REMARK 3 L13: -0.0904 L23: 0.1579
REMARK 3 S TENSOR
REMARK 3 S11: 0.0780 S12: 0.1901 S13: 0.1293
REMARK 3 S21: -0.0187 S22: -0.0260 S23: -0.0118
REMARK 3 S31: -0.0510 S32: -0.0164 S33: 0.0610
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 205 THROUGH 238 )
REMARK 3 ORIGIN FOR THE GROUP (A): 3.2898 -2.1335 24.5739
REMARK 3 T TENSOR
REMARK 3 T11: 0.1398 T22: 0.2102
REMARK 3 T33: 0.1413 T12: 0.0132
REMARK 3 T13: -0.0093 T23: -0.0001
REMARK 3 L TENSOR
REMARK 3 L11: 0.3375 L22: 0.3035
REMARK 3 L33: 0.4628 L12: 0.0012
REMARK 3 L13: 0.2021 L23: 0.3843
REMARK 3 S TENSOR
REMARK 3 S11: 0.0629 S12: 0.3349 S13: -0.0010
REMARK 3 S21: 0.0360 S22: 0.0777 S23: -0.0199
REMARK 3 S31: 0.1288 S32: 0.0663 S33: 0.0809
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 21 )
REMARK 3 ORIGIN FOR THE GROUP (A): 6.7651 -5.7128 65.9077
REMARK 3 T TENSOR
REMARK 3 T11: 0.2566 T22: 0.3806
REMARK 3 T33: 0.1928 T12: 0.0294
REMARK 3 T13: -0.0431 T23: 0.0376
REMARK 3 L TENSOR
REMARK 3 L11: 0.3068 L22: 0.0711
REMARK 3 L33: 0.1287 L12: -0.0829
REMARK 3 L13: -0.0411 L23: -0.0782
REMARK 3 S TENSOR
REMARK 3 S11: -0.0938 S12: -0.6154 S13: -0.1277
REMARK 3 S21: 0.2459 S22: 0.2942 S23: -0.0530
REMARK 3 S31: 0.1230 S32: -0.2893 S33: 0.0030
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 22 THROUGH 35 )
REMARK 3 ORIGIN FOR THE GROUP (A): 8.4066 -13.7492 52.4593
REMARK 3 T TENSOR
REMARK 3 T11: 0.2036 T22: 0.1679
REMARK 3 T33: 0.3751 T12: -0.0139
REMARK 3 T13: -0.0539 T23: 0.0274
REMARK 3 L TENSOR
REMARK 3 L11: 0.0565 L22: 0.0379
REMARK 3 L33: 0.0879 L12: 0.0064
REMARK 3 L13: -0.0322 L23: -0.0048
REMARK 3 S TENSOR
REMARK 3 S11: 0.1107 S12: -0.1974 S13: -0.5358
REMARK 3 S21: 0.2420 S22: -0.1183 S23: 0.0830
REMARK 3 S31: 0.1378 S32: -0.1621 S33: -0.0019
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 36 THROUGH 54 )
REMARK 3 ORIGIN FOR THE GROUP (A): -2.7588 -5.3294 55.6007
REMARK 3 T TENSOR
REMARK 3 T11: 0.1767 T22: 0.3032
REMARK 3 T33: 0.2012 T12: -0.0404
REMARK 3 T13: -0.0224 T23: 0.0631
REMARK 3 L TENSOR
REMARK 3 L11: 0.2212 L22: 0.1326
REMARK 3 L33: 0.2678 L12: 0.0040
REMARK 3 L13: 0.1406 L23: 0.0365
REMARK 3 S TENSOR
REMARK 3 S11: 0.0477 S12: -0.2125 S13: -0.1814
REMARK 3 S21: -0.1441 S22: 0.1567 S23: 0.1790
REMARK 3 S31: 0.0687 S32: -0.4789 S33: 0.0443
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 55 THROUGH 87 )
REMARK 3 ORIGIN FOR THE GROUP (A): 0.5581 5.3440 61.7646
REMARK 3 T TENSOR
REMARK 3 T11: 0.2038 T22: 0.3627
REMARK 3 T33: 0.1907 T12: 0.0564
REMARK 3 T13: 0.0046 T23: -0.0209
REMARK 3 L TENSOR
REMARK 3 L11: 0.6305 L22: 0.5813
REMARK 3 L33: 0.6980 L12: -0.0678
REMARK 3 L13: 0.1422 L23: -0.1561
REMARK 3 S TENSOR
REMARK 3 S11: -0.0753 S12: -0.3909 S13: 0.0678
REMARK 3 S21: 0.0619 S22: 0.3015 S23: 0.0489
REMARK 3 S31: -0.0847 S32: -0.2104 S33: 0.2438
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 88 THROUGH 103 )
REMARK 3 ORIGIN FOR THE GROUP (A): 13.8392 4.0920 57.9051
REMARK 3 T TENSOR
REMARK 3 T11: 0.1780 T22: 0.2834
REMARK 3 T33: 0.1703 T12: 0.0000
REMARK 3 T13: -0.0219 T23: -0.0503
REMARK 3 L TENSOR
REMARK 3 L11: 0.0480 L22: 0.0308
REMARK 3 L33: -0.0049 L12: 0.0154
REMARK 3 L13: 0.0073 L23: -0.0158
REMARK 3 S TENSOR
REMARK 3 S11: 0.0533 S12: -0.2576 S13: 0.0740
REMARK 3 S21: 0.0769 S22: 0.0000 S23: -0.1763
REMARK 3 S31: -0.0210 S32: 0.1647 S33: -0.0004
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 104 THROUGH 204 )
REMARK 3 ORIGIN FOR THE GROUP (A): 5.6742 6.3911 45.6865
REMARK 3 T TENSOR
REMARK 3 T11: 0.1273 T22: 0.1439
REMARK 3 T33: 0.1551 T12: -0.0045
REMARK 3 T13: 0.0078 T23: -0.0257
REMARK 3 L TENSOR
REMARK 3 L11: 0.6206 L22: 0.2673
REMARK 3 L33: 0.6993 L12: 0.0723
REMARK 3 L13: 0.3459 L23: -0.0195
REMARK 3 S TENSOR
REMARK 3 S11: 0.0342 S12: -0.0676 S13: 0.0841
REMARK 3 S21: 0.0149 S22: -0.0030 S23: -0.0212
REMARK 3 S31: -0.0323 S32: -0.0165 S33: 0.1609
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 205 THROUGH 218 )
REMARK 3 ORIGIN FOR THE GROUP (A): -13.8852 5.5983 51.9339
REMARK 3 T TENSOR
REMARK 3 T11: 0.1590 T22: 0.3253
REMARK 3 T33: 0.1766 T12: -0.0151
REMARK 3 T13: 0.0178 T23: -0.0444
REMARK 3 L TENSOR
REMARK 3 L11: 0.0277 L22: 0.0393
REMARK 3 L33: 0.0935 L12: -0.0244
REMARK 3 L13: 0.0057 L23: -0.0645
REMARK 3 S TENSOR
REMARK 3 S11: 0.0752 S12: -0.4562 S13: 0.1507
REMARK 3 S21: 0.0586 S22: -0.0520 S23: 0.0141
REMARK 3 S31: -0.0378 S32: -0.0595 S33: 0.0012
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 219 THROUGH 238 )
REMARK 3 ORIGIN FOR THE GROUP (A): 1.0155 -5.6769 41.3487
REMARK 3 T TENSOR
REMARK 3 T11: 0.1854 T22: 0.1479
REMARK 3 T33: 0.1773 T12: 0.0071
REMARK 3 T13: -0.0411 T23: -0.0297
REMARK 3 L TENSOR
REMARK 3 L11: 0.0618 L22: 0.1937
REMARK 3 L33: 0.2212 L12: -0.0710
REMARK 3 L13: 0.0011 L23: -0.1930
REMARK 3 S TENSOR
REMARK 3 S11: 0.1422 S12: 0.0108 S13: -0.2752
REMARK 3 S21: -0.0984 S22: -0.0073 S23: 0.1447
REMARK 3 S31: 0.1793 S32: -0.0282 S33: 0.0717
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 8VB3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-DEC-23.
REMARK 100 THE DEPOSITION ID IS D_1000279843.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-FEB-19
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I03
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.976
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 86395
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.450
REMARK 200 RESOLUTION RANGE LOW (A) : 39.630
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 6.500
REMARK 200 R MERGE (I) : 0.06690
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 12.0100
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 (%) : 99.1
REMARK 200 DATA REDUNDANCY IN SHELL : 6.30
REMARK 200 R MERGE FOR SHELL (I) : 0.28750
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 4.430
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.19
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.29
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% W/V PEG3000, 0.1 M TRIS, PH 7, 0.2
REMARK 280 M CALCIUM ACETATE, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 291.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 43.91750
REMARK 290 SMTRY3 2 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3620 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19880 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -123.0 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 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 -28.76200
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 -70.50231
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 -12
REMARK 465 ALA A -11
REMARK 465 SER A -10
REMARK 465 TRP A -9
REMARK 465 SER A -8
REMARK 465 HIS A -7
REMARK 465 PRO A -6
REMARK 465 GLN A -5
REMARK 465 PHE A -4
REMARK 465 GLU A -3
REMARK 465 MET B -12
REMARK 465 ALA B -11
REMARK 465 SER B -10
REMARK 465 TRP B -9
REMARK 465 SER B -8
REMARK 465 HIS B -7
REMARK 465 PRO B -6
REMARK 465 GLN B -5
REMARK 465 PHE B -4
REMARK 465 GLU B -3
REMARK 465 LYS B -2
REMARK 465 GLY B -1
REMARK 465 ALA B 0
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 OE1 GLU B 174 O HOH B 401 2.17
REMARK 500 OD2 CSD A 119 NE2 HIS A 200 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 CYS A 119 CB CYS A 119 SG -0.099
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 CSD A 119 -126.77 58.51
REMARK 500 CYS A 119 -122.15 49.46
REMARK 500 HIS A 142 58.32 33.44
REMARK 500 VAL A 199 -153.20 -117.22
REMARK 500 CSD B 119 -126.36 61.22
REMARK 500 CYS B 119 -119.56 51.35
REMARK 500 HIS B 142 58.47 34.83
REMARK 500 VAL B 199 -151.49 -114.67
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 561 DISTANCE = 6.06 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 NA A 305 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ARG A 103 O
REMARK 620 2 GLN A 105 O 100.1
REMARK 620 3 VAL A 108 O 115.1 89.8
REMARK 620 4 HOH A 516 O 108.8 150.1 71.4
REMARK 620 5 HOH A 524 O 101.2 88.4 143.4 93.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 306 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 131 O
REMARK 620 2 ASP A 208 O 20.7
REMARK 620 3 HOH A 409 O 78.0 60.8
REMARK 620 4 HOH A 424 O 100.7 119.7 170.9
REMARK 620 5 HOH A 432 O 174.5 161.6 101.9 78.4
REMARK 620 6 HOH A 503 O 99.2 88.6 93.7 95.4 86.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 304 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ARG B 103 O
REMARK 620 2 GLN B 105 O 102.6
REMARK 620 3 VAL B 108 O 113.0 92.5
REMARK 620 4 HOH B 479 O 105.5 150.3 67.8
REMARK 620 5 HOH B 529 O 99.6 92.9 144.9 91.7
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 303 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER B 131 O
REMARK 620 2 ASP B 208 O 16.8
REMARK 620 3 HOH B 437 O 176.3 160.4
REMARK 620 4 HOH B 461 O 103.2 119.5 80.0
REMARK 620 5 HOH B 522 O 85.6 69.0 91.4 170.1
REMARK 620 6 HOH B 526 O 90.9 86.2 90.8 94.1 81.0
REMARK 620 N 1 2 3 4 5
DBREF1 8VB3 A 1 238 UNP A0A2S5TB63_9GAMM
DBREF2 8VB3 A A0A2S5TB63 1 238
DBREF1 8VB3 B 1 238 UNP A0A2S5TB63_9GAMM
DBREF2 8VB3 B A0A2S5TB63 1 238
SEQADV 8VB3 MET A -12 UNP A0A2S5TB6 INITIATING METHIONINE
SEQADV 8VB3 ALA A -11 UNP A0A2S5TB6 EXPRESSION TAG
SEQADV 8VB3 SER A -10 UNP A0A2S5TB6 EXPRESSION TAG
SEQADV 8VB3 TRP A -9 UNP A0A2S5TB6 EXPRESSION TAG
SEQADV 8VB3 SER A -8 UNP A0A2S5TB6 EXPRESSION TAG
SEQADV 8VB3 HIS A -7 UNP A0A2S5TB6 EXPRESSION TAG
SEQADV 8VB3 PRO A -6 UNP A0A2S5TB6 EXPRESSION TAG
SEQADV 8VB3 GLN A -5 UNP A0A2S5TB6 EXPRESSION TAG
SEQADV 8VB3 PHE A -4 UNP A0A2S5TB6 EXPRESSION TAG
SEQADV 8VB3 GLU A -3 UNP A0A2S5TB6 EXPRESSION TAG
SEQADV 8VB3 LYS A -2 UNP A0A2S5TB6 EXPRESSION TAG
SEQADV 8VB3 GLY A -1 UNP A0A2S5TB6 EXPRESSION TAG
SEQADV 8VB3 ALA A 0 UNP A0A2S5TB6 EXPRESSION TAG
SEQADV 8VB3 MET B -12 UNP A0A2S5TB6 INITIATING METHIONINE
SEQADV 8VB3 ALA B -11 UNP A0A2S5TB6 EXPRESSION TAG
SEQADV 8VB3 SER B -10 UNP A0A2S5TB6 EXPRESSION TAG
SEQADV 8VB3 TRP B -9 UNP A0A2S5TB6 EXPRESSION TAG
SEQADV 8VB3 SER B -8 UNP A0A2S5TB6 EXPRESSION TAG
SEQADV 8VB3 HIS B -7 UNP A0A2S5TB6 EXPRESSION TAG
SEQADV 8VB3 PRO B -6 UNP A0A2S5TB6 EXPRESSION TAG
SEQADV 8VB3 GLN B -5 UNP A0A2S5TB6 EXPRESSION TAG
SEQADV 8VB3 PHE B -4 UNP A0A2S5TB6 EXPRESSION TAG
SEQADV 8VB3 GLU B -3 UNP A0A2S5TB6 EXPRESSION TAG
SEQADV 8VB3 LYS B -2 UNP A0A2S5TB6 EXPRESSION TAG
SEQADV 8VB3 GLY B -1 UNP A0A2S5TB6 EXPRESSION TAG
SEQADV 8VB3 ALA B 0 UNP A0A2S5TB6 EXPRESSION TAG
SEQRES 1 A 251 MET ALA SER TRP SER HIS PRO GLN PHE GLU LYS GLY ALA
SEQRES 2 A 251 MET HIS GLN GLN PRO ILE GLU THR THR GLU ASN GLY GLN
SEQRES 3 A 251 ARG HIS ILE HIS GLN PHE PHE LEU ASP GLU THR LEU GLN
SEQRES 4 A 251 GLY PRO ARG PRO GLY VAL LEU VAL PHE PRO GLU ALA PHE
SEQRES 5 A 251 GLY LEU GLY ASP HIS ALA LEU GLN ARG ALA ARG ARG LEU
SEQRES 6 A 251 ALA GLU LEU GLY TYR ALA ALA LEU ALA VAL ASP ILE HIS
SEQRES 7 A 251 GLY GLU GLY ARG GLU PHE GLN ASP LEU ALA GLN VAL ARG
SEQRES 8 A 251 PRO ALA ILE LEU ALA LEU PHE GLY ASP ARG ALA ALA TRP
SEQRES 9 A 251 ARG ALA ARG LEU GLN ALA ALA HIS GLU LEU LEU ARG ALA
SEQRES 10 A 251 GLN PRO GLN VAL ASP ALA ALA ARG THR ALA ALA ILE GLY
SEQRES 11 A 251 PHE CSD PHE GLY GLY ALA CYS SER LEU GLU LEU ALA ARG
SEQRES 12 A 251 SER GLY ALA PRO LEU SER ALA ILE VAL THR PHE HIS ALA
SEQRES 13 A 251 GLY LEU GLN PRO PRO LEU GLU ALA ASP ALA GLY LYS ILE
SEQRES 14 A 251 LYS ALA LYS VAL LEU VAL CYS HIS GLY ALA GLU ASP PRO
SEQRES 15 A 251 LEU MET LYS PRO GLU PRO LEU ALA ALA ILE LEU ALA GLU
SEQRES 16 A 251 LEU THR ARG ASP LYS VAL ASP TRP GLN LEU LEU SER HIS
SEQRES 17 A 251 GLY ASN VAL VAL HIS SER PHE THR ASN PRO ASP ALA ASP
SEQRES 18 A 251 ALA ARG GLY ALA PRO GLY PHE ALA TYR ASN ALA GLY ALA
SEQRES 19 A 251 ASP ARG ARG SER TRP ALA ALA MET GLN GLY LEU PHE ALA
SEQRES 20 A 251 GLU VAL PHE ALA
SEQRES 1 B 251 MET ALA SER TRP SER HIS PRO GLN PHE GLU LYS GLY ALA
SEQRES 2 B 251 MET HIS GLN GLN PRO ILE GLU THR THR GLU ASN GLY GLN
SEQRES 3 B 251 ARG HIS ILE HIS GLN PHE PHE LEU ASP GLU THR LEU GLN
SEQRES 4 B 251 GLY PRO ARG PRO GLY VAL LEU VAL PHE PRO GLU ALA PHE
SEQRES 5 B 251 GLY LEU GLY ASP HIS ALA LEU GLN ARG ALA ARG ARG LEU
SEQRES 6 B 251 ALA GLU LEU GLY TYR ALA ALA LEU ALA VAL ASP ILE HIS
SEQRES 7 B 251 GLY GLU GLY ARG GLU PHE GLN ASP LEU ALA GLN VAL ARG
SEQRES 8 B 251 PRO ALA ILE LEU ALA LEU PHE GLY ASP ARG ALA ALA TRP
SEQRES 9 B 251 ARG ALA ARG LEU GLN ALA ALA HIS GLU LEU LEU ARG ALA
SEQRES 10 B 251 GLN PRO GLN VAL ASP ALA ALA ARG THR ALA ALA ILE GLY
SEQRES 11 B 251 PHE CSD PHE GLY GLY ALA CYS SER LEU GLU LEU ALA ARG
SEQRES 12 B 251 SER GLY ALA PRO LEU SER ALA ILE VAL THR PHE HIS ALA
SEQRES 13 B 251 GLY LEU GLN PRO PRO LEU GLU ALA ASP ALA GLY LYS ILE
SEQRES 14 B 251 LYS ALA LYS VAL LEU VAL CYS HIS GLY ALA GLU ASP PRO
SEQRES 15 B 251 LEU MET LYS PRO GLU PRO LEU ALA ALA ILE LEU ALA GLU
SEQRES 16 B 251 LEU THR ARG ASP LYS VAL ASP TRP GLN LEU LEU SER HIS
SEQRES 17 B 251 GLY ASN VAL VAL HIS SER PHE THR ASN PRO ASP ALA ASP
SEQRES 18 B 251 ALA ARG GLY ALA PRO GLY PHE ALA TYR ASN ALA GLY ALA
SEQRES 19 B 251 ASP ARG ARG SER TRP ALA ALA MET GLN GLY LEU PHE ALA
SEQRES 20 B 251 GLU VAL PHE ALA
MODRES 8VB3 CSD A 119 CYS MODIFIED RESIDUE
MODRES 8VB3 CSD B 119 CYS MODIFIED RESIDUE
HET CSD A 119 8
HET CSD B 119 8
HET MPD A 301 8
HET MPD A 302 8
HET MPD A 303 8
HET NA A 304 1
HET NA A 305 1
HET NA A 306 1
HET MPD B 301 8
HET MPD B 302 8
HET NA B 303 1
HET NA B 304 1
HET MPD B 305 8
HET MPD B 306 8
HETNAM CSD 3-SULFINOALANINE
HETNAM MPD (4S)-2-METHYL-2,4-PENTANEDIOL
HETNAM NA SODIUM ION
HETSYN CSD S-CYSTEINESULFINIC ACID; S-SULFINOCYSTEINE
FORMUL 1 CSD 2(C3 H7 N O4 S)
FORMUL 3 MPD 7(C6 H14 O2)
FORMUL 6 NA 5(NA 1+)
FORMUL 15 HOH *314(H2 O)
HELIX 1 AA1 GLY A 42 LEU A 55 1 14
HELIX 2 AA2 ASP A 73 GLY A 86 1 14
HELIX 3 AA3 ASP A 87 GLN A 105 1 19
HELIX 4 AA4 CSD A 119 SER A 131 1 13
HELIX 5 AA5 LEU A 149 ALA A 153 5 5
HELIX 6 AA6 LYS A 172 ASP A 186 1 15
HELIX 7 AA7 ASN A 204 ARG A 210 5 7
HELIX 8 AA8 ASN A 218 PHE A 237 1 20
HELIX 9 AA9 GLY B 42 LEU B 55 1 14
HELIX 10 AB1 ASP B 73 GLY B 86 1 14
HELIX 11 AB2 ASP B 87 ALA B 104 1 18
HELIX 12 AB3 CSD B 119 SER B 131 1 13
HELIX 13 AB4 LEU B 149 ALA B 153 5 5
HELIX 14 AB5 LYS B 172 ASP B 186 1 15
HELIX 15 AB6 ASN B 204 ARG B 210 5 7
HELIX 16 AB7 ASN B 218 PHE B 237 1 20
SHEET 1 AA116 HIS A 2 GLU A 10 0
SHEET 2 AA116 GLN A 13 LEU A 21 -1 O LEU A 21 N HIS A 2
SHEET 3 AA116 ALA A 58 ALA A 61 -1 O ALA A 59 N PHE A 20
SHEET 4 AA116 ARG A 29 PHE A 35 1 N VAL A 34 O LEU A 60
SHEET 5 AA116 VAL A 108 PHE A 118 1 O ILE A 116 N LEU A 33
SHEET 6 AA116 ALA A 137 PHE A 141 1 O PHE A 141 N GLY A 117
SHEET 7 AA116 LYS A 159 GLY A 165 1 O CYS A 163 N THR A 140
SHEET 8 AA116 TRP A 190 HIS A 195 1 O LEU A 193 N VAL A 162
SHEET 9 AA116 TRP B 190 HIS B 195 -1 O SER B 194 N LEU A 192
SHEET 10 AA116 LYS B 159 GLY B 165 1 N HIS B 164 O LEU B 193
SHEET 11 AA116 ALA B 137 PHE B 141 1 N THR B 140 O CYS B 163
SHEET 12 AA116 VAL B 108 PHE B 118 1 N GLY B 117 O PHE B 141
SHEET 13 AA116 ARG B 29 PHE B 35 1 N LEU B 33 O ILE B 116
SHEET 14 AA116 ALA B 58 ALA B 61 1 O ALA B 58 N PRO B 30
SHEET 15 AA116 GLN B 13 LEU B 21 -1 N GLN B 18 O ALA B 61
SHEET 16 AA116 HIS B 2 GLU B 10 -1 N HIS B 2 O LEU B 21
LINK C PHE A 118 N ACSD A 119 1555 1555 1.33
LINK C ACSD A 119 N PHE A 120 1555 1555 1.33
LINK C PHE B 118 N ACSD B 119 1555 1555 1.32
LINK C ACSD B 119 N PHE B 120 1555 1555 1.32
LINK O ARG A 103 NA NA A 305 1555 1555 2.28
LINK O GLN A 105 NA NA A 305 1555 1555 2.38
LINK O VAL A 108 NA NA A 305 1555 1555 2.43
LINK O SER A 131 NA NA A 306 1555 1555 2.20
LINK O ASP A 208 NA NA A 306 1555 1655 2.52
LINK NA NA A 305 O HOH A 516 1555 1555 2.66
LINK NA NA A 305 O HOH A 524 1555 1555 2.31
LINK NA NA A 306 O HOH A 409 1555 1555 2.94
LINK NA NA A 306 O HOH A 424 1555 1555 2.41
LINK NA NA A 306 O HOH A 432 1555 1455 2.53
LINK NA NA A 306 O HOH A 503 1555 1555 2.20
LINK O ARG B 103 NA NA B 304 1555 1555 2.34
LINK O GLN B 105 NA NA B 304 1555 1555 2.44
LINK O VAL B 108 NA NA B 304 1555 1555 2.37
LINK O SER B 131 NA NA B 303 1555 1555 2.29
LINK O ASP B 208 NA NA B 303 1555 1455 2.41
LINK NA NA B 303 O HOH B 437 1555 1655 2.46
LINK NA NA B 303 O HOH B 461 1555 1655 2.32
LINK NA NA B 303 O HOH B 522 1555 1555 2.52
LINK NA NA B 303 O HOH B 526 1555 1555 2.33
LINK NA NA B 304 O HOH B 479 1555 1555 2.74
LINK NA NA B 304 O HOH B 529 1555 1555 2.19
CRYST1 40.143 87.835 71.415 90.00 99.17 90.00 P 1 21 1 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 0.024911 0.000000 0.004021 0.00000
SCALE2 0.000000 0.011385 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014184 0.00000
TER 1879 ALA A 238
TER 3744 ALA B 238
MASTER 557 0 14 16 16 0 0 6 4033 2 99 40
END |