| content |
HEADER HYDROLASE 25-APR-14 4Q82
TITLE CRYSTAL STRUCTURE OF PHOSPHOLIPASE/CARBOXYLESTERASE FROM HALIANGIUM
TITLE 2 OCHRACEUM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHOSPHOLIPASE/CARBOXYLESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HALIANGIUM OCHRACEUM;
SOURCE 3 ORGANISM_TAXID: 502025;
SOURCE 4 STRAIN: DSM 14365;
SOURCE 5 GENE: HOCH_6203;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21DE3 GOLD;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PMCSG68
KEYWDS STRUCTURAL GENOMICS, PSI-BIOLOGY, MIDWEST CENTER FOR STRUCTURAL
KEYWDS 2 GENOMICS, MCSG, ALPHA-BETA-FOLD, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.KIM,C.HATZOS-SKINTGES,M.ENDRES,A.JOACHIMIAK,MIDWEST CENTER FOR
AUTHOR 2 STRUCTURAL GENOMICS (MCSG)
REVDAT 1 14-MAY-14 4Q82 0
JRNL AUTH Y.KIM,C.HATZOS-SKINTGES,M.ENDRES,A.JOACHIMIAK
JRNL TITL CRYSTAL STRUCTURE OF PHOSPHOLIPASE/CARBOXYLESTERASE FROM
JRNL TITL 2 HALIANGIUM OCHRACEUM
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.9_1678)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : MLHL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.30
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 3 NUMBER OF REFLECTIONS : 66642
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.154
REMARK 3 R VALUE (WORKING SET) : 0.153
REMARK 3 FREE R VALUE : 0.175
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.060
REMARK 3 FREE R VALUE TEST SET COUNT : 3371
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 41.3068 - 5.3279 0.98 2878 121 0.1750 0.1857
REMARK 3 2 5.3279 - 4.2303 1.00 2787 140 0.1234 0.1489
REMARK 3 3 4.2303 - 3.6959 1.00 2722 155 0.1203 0.1365
REMARK 3 4 3.6959 - 3.3582 1.00 2708 157 0.1355 0.1352
REMARK 3 5 3.3582 - 3.1176 1.00 2676 156 0.1549 0.1674
REMARK 3 6 3.1176 - 2.9338 1.00 2706 148 0.1684 0.2089
REMARK 3 7 2.9338 - 2.7869 1.00 2697 139 0.1714 0.1956
REMARK 3 8 2.7869 - 2.6656 1.00 2710 117 0.1725 0.2036
REMARK 3 9 2.6656 - 2.5630 1.00 2665 154 0.1666 0.1958
REMARK 3 10 2.5630 - 2.4746 1.00 2653 153 0.1667 0.1919
REMARK 3 11 2.4746 - 2.3972 1.00 2691 146 0.1593 0.1710
REMARK 3 12 2.3972 - 2.3287 1.00 2658 150 0.1546 0.1854
REMARK 3 13 2.3287 - 2.2674 1.00 2651 154 0.1530 0.1836
REMARK 3 14 2.2674 - 2.2121 1.00 2641 141 0.1521 0.1829
REMARK 3 15 2.2121 - 2.1618 1.00 2679 143 0.1499 0.1782
REMARK 3 16 2.1618 - 2.1158 1.00 2666 134 0.1455 0.1788
REMARK 3 17 2.1158 - 2.0735 1.00 2656 146 0.1505 0.1801
REMARK 3 18 2.0735 - 2.0343 1.00 2661 125 0.1564 0.1892
REMARK 3 19 2.0343 - 1.9980 0.99 2625 143 0.1541 0.1997
REMARK 3 20 1.9980 - 1.9641 0.99 2636 143 0.1523 0.1661
REMARK 3 21 1.9641 - 1.9325 0.95 2543 128 0.1660 0.2011
REMARK 3 22 1.9325 - 1.9027 0.93 2411 145 0.1730 0.1938
REMARK 3 23 1.9027 - 1.8748 0.88 2376 113 0.1888 0.1890
REMARK 3 24 1.8748 - 1.8483 0.82 2175 120 0.1916 0.2178
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
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) : 0.130
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 15.300
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 18.65
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.90
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 3850
REMARK 3 ANGLE : 1.270 5284
REMARK 3 CHIRALITY : 0.063 542
REMARK 3 PLANARITY : 0.007 728
REMARK 3 DIHEDRAL : 13.666 1368
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 15
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: chain 'A' and (resid 57 through 85 )
REMARK 3 ORIGIN FOR THE GROUP (A): 55.4391 11.2688 41.0074
REMARK 3 T TENSOR
REMARK 3 T11: 0.2695 T22: 0.2534
REMARK 3 T33: 0.3693 T12: 0.0888
REMARK 3 T13: 0.2906 T23: 0.0602
REMARK 3 L TENSOR
REMARK 3 L11: 1.4587 L22: 2.8873
REMARK 3 L33: 2.2613 L12: -0.9838
REMARK 3 L13: -0.4107 L23: 0.6047
REMARK 3 S TENSOR
REMARK 3 S11: -0.1345 S12: -0.2343 S13: -0.2734
REMARK 3 S21: 0.5298 S22: 0.0553 S23: 0.8296
REMARK 3 S31: 0.1841 S32: -0.5847 S33: 0.3471
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: chain 'A' and (resid 86 through 106 )
REMARK 3 ORIGIN FOR THE GROUP (A): 56.5205 12.4842 32.5068
REMARK 3 T TENSOR
REMARK 3 T11: 0.1555 T22: 0.2065
REMARK 3 T33: 0.3520 T12: 0.0444
REMARK 3 T13: 0.0801 T23: 0.0341
REMARK 3 L TENSOR
REMARK 3 L11: 1.4413 L22: 0.8515
REMARK 3 L33: 3.1361 L12: 0.6636
REMARK 3 L13: -0.5006 L23: 1.0245
REMARK 3 S TENSOR
REMARK 3 S11: -0.0024 S12: 0.0953 S13: -0.0549
REMARK 3 S21: 0.1615 S22: -0.0406 S23: 0.7277
REMARK 3 S31: -0.1169 S32: -0.5732 S33: 0.1291
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: chain 'A' and (resid 107 through 120 )
REMARK 3 ORIGIN FOR THE GROUP (A): 67.6101 3.8858 42.5019
REMARK 3 T TENSOR
REMARK 3 T11: 0.4609 T22: 0.2260
REMARK 3 T33: 0.1990 T12: 0.0854
REMARK 3 T13: 0.1071 T23: 0.0387
REMARK 3 L TENSOR
REMARK 3 L11: 0.9947 L22: 1.9453
REMARK 3 L33: 0.9173 L12: 0.8546
REMARK 3 L13: -0.1076 L23: -1.1351
REMARK 3 S TENSOR
REMARK 3 S11: -0.0818 S12: -0.4066 S13: -0.0810
REMARK 3 S21: 0.9596 S22: -0.0344 S23: 0.3087
REMARK 3 S31: 0.2076 S32: 0.0669 S33: 0.0871
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: chain 'A' and (resid 121 through 138 )
REMARK 3 ORIGIN FOR THE GROUP (A): 63.0695 19.2332 35.4559
REMARK 3 T TENSOR
REMARK 3 T11: 0.1894 T22: 0.1578
REMARK 3 T33: 0.1516 T12: 0.0513
REMARK 3 T13: 0.0941 T23: 0.0329
REMARK 3 L TENSOR
REMARK 3 L11: 5.5308 L22: 3.7602
REMARK 3 L33: 3.6679 L12: -0.0454
REMARK 3 L13: -0.4980 L23: 2.5013
REMARK 3 S TENSOR
REMARK 3 S11: -0.0025 S12: -0.3205 S13: 0.3174
REMARK 3 S21: 0.3542 S22: 0.0604 S23: 0.1069
REMARK 3 S31: -0.2998 S32: 0.0244 S33: -0.0403
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: chain 'A' and (resid 139 through 173 )
REMARK 3 ORIGIN FOR THE GROUP (A): 56.4623 2.9146 30.1537
REMARK 3 T TENSOR
REMARK 3 T11: 0.1817 T22: 0.2195
REMARK 3 T33: 0.4448 T12: -0.0364
REMARK 3 T13: 0.0740 T23: 0.0011
REMARK 3 L TENSOR
REMARK 3 L11: 1.6793 L22: 0.9709
REMARK 3 L33: 2.4820 L12: -0.0417
REMARK 3 L13: -0.7736 L23: 0.3547
REMARK 3 S TENSOR
REMARK 3 S11: -0.1724 S12: 0.0090 S13: -0.4253
REMARK 3 S21: 0.2937 S22: 0.0067 S23: 0.7822
REMARK 3 S31: 0.3766 S32: -0.4202 S33: 0.0803
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: chain 'A' and (resid 174 through 209 )
REMARK 3 ORIGIN FOR THE GROUP (A): 63.6959 4.0620 21.0049
REMARK 3 T TENSOR
REMARK 3 T11: 0.1427 T22: 0.1234
REMARK 3 T33: 0.2097 T12: 0.0144
REMARK 3 T13: -0.0364 T23: -0.0240
REMARK 3 L TENSOR
REMARK 3 L11: 2.8176 L22: 2.7496
REMARK 3 L33: 2.9297 L12: -0.1355
REMARK 3 L13: -0.9892 L23: 0.1283
REMARK 3 S TENSOR
REMARK 3 S11: -0.0675 S12: 0.1791 S13: -0.3438
REMARK 3 S21: -0.2141 S22: -0.0323 S23: 0.5199
REMARK 3 S31: 0.2809 S32: -0.2728 S33: 0.0575
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: chain 'A' and (resid 210 through 263 )
REMARK 3 ORIGIN FOR THE GROUP (A): 69.4870 8.8981 12.8431
REMARK 3 T TENSOR
REMARK 3 T11: 0.2533 T22: 0.1866
REMARK 3 T33: 0.1272 T12: 0.0636
REMARK 3 T13: -0.0703 T23: -0.0173
REMARK 3 L TENSOR
REMARK 3 L11: 1.5068 L22: 1.9467
REMARK 3 L33: 1.4827 L12: -0.0081
REMARK 3 L13: -0.0787 L23: -0.2436
REMARK 3 S TENSOR
REMARK 3 S11: 0.1639 S12: 0.3380 S13: -0.1065
REMARK 3 S21: -0.6441 S22: -0.1389 S23: 0.1591
REMARK 3 S31: 0.0432 S32: -0.2011 S33: -0.0270
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: chain 'A' and (resid 264 through 292 )
REMARK 3 ORIGIN FOR THE GROUP (A): 68.3469 17.3627 23.8211
REMARK 3 T TENSOR
REMARK 3 T11: 0.1272 T22: 0.0956
REMARK 3 T33: 0.0962 T12: 0.0446
REMARK 3 T13: -0.0046 T23: 0.0124
REMARK 3 L TENSOR
REMARK 3 L11: 2.7118 L22: 2.7592
REMARK 3 L33: 1.9902 L12: 0.4292
REMARK 3 L13: -0.2076 L23: 0.0292
REMARK 3 S TENSOR
REMARK 3 S11: 0.0980 S12: -0.0131 S13: -0.0267
REMARK 3 S21: -0.0563 S22: -0.0747 S23: 0.2380
REMARK 3 S31: -0.0782 S32: -0.1680 S33: -0.0228
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: chain 'B' and (resid 60 through 85 )
REMARK 3 ORIGIN FOR THE GROUP (A): 96.1756 37.0181 6.2286
REMARK 3 T TENSOR
REMARK 3 T11: 0.1378 T22: 0.4461
REMARK 3 T33: 0.2590 T12: -0.0901
REMARK 3 T13: 0.0209 T23: 0.0568
REMARK 3 L TENSOR
REMARK 3 L11: 2.6845 L22: 4.3211
REMARK 3 L33: 2.2037 L12: 0.8869
REMARK 3 L13: 0.2784 L23: -1.2056
REMARK 3 S TENSOR
REMARK 3 S11: -0.0877 S12: 0.5664 S13: 0.1143
REMARK 3 S21: -0.4319 S22: -0.0428 S23: -0.9461
REMARK 3 S31: -0.1417 S32: 0.7687 S33: 0.1471
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: chain 'B' and (resid 86 through 106 )
REMARK 3 ORIGIN FOR THE GROUP (A): 87.4443 34.2198 5.1772
REMARK 3 T TENSOR
REMARK 3 T11: 0.1122 T22: 0.2876
REMARK 3 T33: 0.1433 T12: -0.0326
REMARK 3 T13: -0.0026 T23: 0.0089
REMARK 3 L TENSOR
REMARK 3 L11: 2.4153 L22: 1.3049
REMARK 3 L33: 4.4787 L12: -0.4021
REMARK 3 L13: -0.1115 L23: -1.5320
REMARK 3 S TENSOR
REMARK 3 S11: -0.0143 S12: 0.5441 S13: -0.0097
REMARK 3 S21: -0.1538 S22: 0.0529 S23: -0.3695
REMARK 3 S31: 0.2190 S32: 0.3988 S33: -0.0267
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: chain 'B' and (resid 107 through 120 )
REMARK 3 ORIGIN FOR THE GROUP (A): 96.9323 41.5200 17.6239
REMARK 3 T TENSOR
REMARK 3 T11: 0.1903 T22: 0.3410
REMARK 3 T33: 0.3325 T12: -0.0908
REMARK 3 T13: -0.1280 T23: 0.0347
REMARK 3 L TENSOR
REMARK 3 L11: 0.9466 L22: 4.3773
REMARK 3 L33: 2.5292 L12: 1.2042
REMARK 3 L13: 0.9520 L23: 0.4443
REMARK 3 S TENSOR
REMARK 3 S11: -0.0644 S12: 0.0425 S13: 0.0158
REMARK 3 S21: 0.2400 S22: -0.1536 S23: -0.7419
REMARK 3 S31: -0.1330 S32: 0.6244 S33: -0.1861
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: chain 'B' and (resid 121 through 138 )
REMARK 3 ORIGIN FOR THE GROUP (A): 89.7332 27.0747 12.2570
REMARK 3 T TENSOR
REMARK 3 T11: 0.0896 T22: 0.2076
REMARK 3 T33: 0.2079 T12: 0.0039
REMARK 3 T13: -0.0056 T23: 0.0205
REMARK 3 L TENSOR
REMARK 3 L11: 6.1239 L22: 5.1592
REMARK 3 L33: 5.3894 L12: -1.3412
REMARK 3 L13: -0.1844 L23: 0.0533
REMARK 3 S TENSOR
REMARK 3 S11: -0.1080 S12: 0.0287 S13: -0.5993
REMARK 3 S21: 0.2394 S22: 0.0215 S23: -0.4968
REMARK 3 S31: 0.5326 S32: 0.5667 S33: -0.0225
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: chain 'B' and (resid 139 through 209 )
REMARK 3 ORIGIN FOR THE GROUP (A): 81.0059 43.0650 8.1547
REMARK 3 T TENSOR
REMARK 3 T11: 0.1946 T22: 0.2145
REMARK 3 T33: 0.1714 T12: -0.0558
REMARK 3 T13: -0.0602 T23: 0.0956
REMARK 3 L TENSOR
REMARK 3 L11: 1.7655 L22: 1.3133
REMARK 3 L33: 1.9431 L12: 0.3163
REMARK 3 L13: -0.0831 L23: -0.2037
REMARK 3 S TENSOR
REMARK 3 S11: -0.1890 S12: 0.4429 S13: 0.5723
REMARK 3 S21: -0.0558 S22: 0.0627 S23: -0.0729
REMARK 3 S31: -0.4394 S32: 0.1773 S33: 0.0528
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: chain 'B' and (resid 210 through 263 )
REMARK 3 ORIGIN FOR THE GROUP (A): 66.9382 38.4007 16.4082
REMARK 3 T TENSOR
REMARK 3 T11: 0.1453 T22: 0.1364
REMARK 3 T33: 0.1435 T12: 0.0478
REMARK 3 T13: -0.0210 T23: 0.0072
REMARK 3 L TENSOR
REMARK 3 L11: 2.1317 L22: 2.2718
REMARK 3 L33: 1.7782 L12: 0.1467
REMARK 3 L13: -0.2322 L23: -0.1617
REMARK 3 S TENSOR
REMARK 3 S11: -0.1036 S12: 0.1122 S13: 0.3119
REMARK 3 S21: 0.1565 S22: 0.0164 S23: 0.3066
REMARK 3 S31: -0.3309 S32: -0.2097 S33: 0.0779
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: chain 'B' and (resid 264 through 292 )
REMARK 3 ORIGIN FOR THE GROUP (A): 77.5193 29.1507 16.0397
REMARK 3 T TENSOR
REMARK 3 T11: 0.0953 T22: 0.1102
REMARK 3 T33: 0.0826 T12: 0.0136
REMARK 3 T13: -0.0054 T23: 0.0129
REMARK 3 L TENSOR
REMARK 3 L11: 2.1696 L22: 2.2958
REMARK 3 L33: 2.2171 L12: 0.2798
REMARK 3 L13: -0.1559 L23: -0.0748
REMARK 3 S TENSOR
REMARK 3 S11: -0.1055 S12: 0.0988 S13: -0.0510
REMARK 3 S21: 0.1427 S22: -0.0305 S23: -0.0579
REMARK 3 S31: -0.0278 S32: 0.0918 S33: 0.1271
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 4Q82 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-APR-14.
REMARK 100 THE RCSB ID CODE IS RCSB085721.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-NOV-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97921
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 67799
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.850
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 (%) : 99.9
REMARK 200 DATA REDUNDANCY : 4.900
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.07000
REMARK 200 FOR THE DATA SET : 12.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.88
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.1
REMARK 200 DATA REDUNDANCY IN SHELL : 3.40
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.64000
REMARK 200 FOR SHELL : 2.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: HKL3000, SHELXS,MLPHARE,DM
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.49
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.28
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BIS TRIS PROPANE PH7.0, 1.8 M
REMARK 280 MAGNESIUM SULFATE, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 100K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 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+1/2,Y+1/2,-Z
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 38.96750
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 73.04200
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 38.96750
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 73.04200
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 300 REMARK: THERE ARE TWO MONOMERS IN THE ASYMMETRIC UNIT.
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 350
REMARK 350 BIOMOLECULE: 2
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: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 640 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 572 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 SER A 16
REMARK 465 ASN A 17
REMARK 465 ALA A 18
REMARK 465 ASP A 19
REMARK 465 ASP A 20
REMARK 465 GLY A 21
REMARK 465 GLY A 22
REMARK 465 ASP A 23
REMARK 465 ASP A 24
REMARK 465 GLY A 25
REMARK 465 GLY A 26
REMARK 465 ALA A 27
REMARK 465 GLU A 28
REMARK 465 THR A 29
REMARK 465 ASP A 30
REMARK 465 ALA A 31
REMARK 465 ALA A 32
REMARK 465 VAL A 33
REMARK 465 ALA A 34
REMARK 465 ILE A 35
REMARK 465 ASP A 36
REMARK 465 ALA A 37
REMARK 465 SER A 38
REMARK 465 PRO A 39
REMARK 465 VAL A 40
REMARK 465 ASP A 41
REMARK 465 ALA A 42
REMARK 465 PRO A 43
REMARK 465 ASP A 44
REMARK 465 PRO A 45
REMARK 465 ILE A 46
REMARK 465 ASP A 47
REMARK 465 ALA A 48
REMARK 465 ALA A 49
REMARK 465 PRO A 50
REMARK 465 ASP A 51
REMARK 465 ALA A 52
REMARK 465 ASN A 53
REMARK 465 GLN A 54
REMARK 465 ILE A 55
REMARK 465 ASP A 56
REMARK 465 SER B 16
REMARK 465 ASN B 17
REMARK 465 ALA B 18
REMARK 465 ASP B 19
REMARK 465 ASP B 20
REMARK 465 GLY B 21
REMARK 465 GLY B 22
REMARK 465 ASP B 23
REMARK 465 ASP B 24
REMARK 465 GLY B 25
REMARK 465 GLY B 26
REMARK 465 ALA B 27
REMARK 465 GLU B 28
REMARK 465 THR B 29
REMARK 465 ASP B 30
REMARK 465 ALA B 31
REMARK 465 ALA B 32
REMARK 465 VAL B 33
REMARK 465 ALA B 34
REMARK 465 ILE B 35
REMARK 465 ASP B 36
REMARK 465 ALA B 37
REMARK 465 SER B 38
REMARK 465 PRO B 39
REMARK 465 VAL B 40
REMARK 465 ASP B 41
REMARK 465 ALA B 42
REMARK 465 PRO B 43
REMARK 465 ASP B 44
REMARK 465 PRO B 45
REMARK 465 ILE B 46
REMARK 465 ASP B 47
REMARK 465 ALA B 48
REMARK 465 ALA B 49
REMARK 465 PRO B 50
REMARK 465 ASP B 51
REMARK 465 ALA B 52
REMARK 465 ASN B 53
REMARK 465 GLN B 54
REMARK 465 ILE B 55
REMARK 465 ASP B 56
REMARK 465 ALA B 57
REMARK 465 MSE B 58
REMARK 465 VAL B 59
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 2ZC A 180 C1 C2 C3 C4 C5 C6 C7
REMARK 470 2ZC A 180 C8 N1
REMARK 470 2ZC B 180 OD2 OD1 C1 C2 C3 C4 C5
REMARK 470 2ZC B 180 C6 C7 C8 N1
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 2ZC A 180 -123.16 56.85
REMARK 500 2ZC B 180 -127.49 53.99
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 PHE A 138 VAL A 139 149.24
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 305
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: MCSG-APC103461 RELATED DB: TARGETTRACK
DBREF 4Q82 A 19 292 UNP D0LMJ0 D0LMJ0_HALO1 19 292
DBREF 4Q82 B 19 292 UNP D0LMJ0 D0LMJ0_HALO1 19 292
SEQADV 4Q82 SER A 16 UNP D0LMJ0 EXPRESSION TAG
SEQADV 4Q82 ASN A 17 UNP D0LMJ0 EXPRESSION TAG
SEQADV 4Q82 ALA A 18 UNP D0LMJ0 EXPRESSION TAG
SEQADV 4Q82 SER B 16 UNP D0LMJ0 EXPRESSION TAG
SEQADV 4Q82 ASN B 17 UNP D0LMJ0 EXPRESSION TAG
SEQADV 4Q82 ALA B 18 UNP D0LMJ0 EXPRESSION TAG
SEQRES 1 A 277 SER ASN ALA ASP ASP GLY GLY ASP ASP GLY GLY ALA GLU
SEQRES 2 A 277 THR ASP ALA ALA VAL ALA ILE ASP ALA SER PRO VAL ASP
SEQRES 3 A 277 ALA PRO ASP PRO ILE ASP ALA ALA PRO ASP ALA ASN GLN
SEQRES 4 A 277 ILE ASP ALA MSE VAL ASP ASP ARG PRO SER SER ALA ARG
SEQRES 5 A 277 LEU SER VAL ARG ALA LEU ASP THR THR GLU ALA GLY ASN
SEQRES 6 A 277 GLY PHE TRP GLU TYR LEU PRO PRO ARG TYR GLY ALA GLU
SEQRES 7 A 277 PRO ALA PRO LEU MSE VAL PHE TRP HIS GLY ILE GLY GLU
SEQRES 8 A 277 ASN GLY ASP GLY SER GLU ALA ALA LEU ASP LYS VAL LEU
SEQRES 9 A 277 ALA ASN GLY PRO PRO ARG TYR ILE GLU ARG ASP GLU TRP
SEQRES 10 A 277 SER ASN GLU ARG PRO PHE VAL VAL LEU SER PRO GLN HIS
SEQRES 11 A 277 ALA GLY GLY GLY CYS PRO SER ALA ASP GLU ILE ARG ASP
SEQRES 12 A 277 PHE LEU ALA PHE ALA VAL ASP THR TYR GLU VAL ASP GLU
SEQRES 13 A 277 SER ARG ILE TYR LEU THR GLY LEU 2ZC CYS GLY ALA ILE
SEQRES 14 A 277 GLY SER TRP ASN TYR LEU ARG ALA HIS LEU ASP THR THR
SEQRES 15 A 277 PRO ILE ALA ALA ALA VAL LEU ILE ALA GLY ASN GLY ARG
SEQRES 16 A 277 PRO ALA PHE ASN ASP HIS GLY CYS ASP LEU ALA GLN VAL
SEQRES 17 A 277 PRO ILE TRP GLY PHE HIS GLY ASP ALA ASP PRO THR VAL
SEQRES 18 A 277 ALA PRO ALA GLY THR ILE GLU PRO MSE ASN GLY LEU ILE
SEQRES 19 A 277 ALA CYS ALA GLN PRO ARG ALA ASP GLN GLN LEU THR VAL
SEQRES 20 A 277 TYR GLU GLY VAL GLY HIS ASP SER TRP SER ARG THR TYR
SEQRES 21 A 277 SER LEU SER ALA GLY HIS ASP ILE TYR ALA TRP LEU LEU
SEQRES 22 A 277 SER GLN SER ARG
SEQRES 1 B 277 SER ASN ALA ASP ASP GLY GLY ASP ASP GLY GLY ALA GLU
SEQRES 2 B 277 THR ASP ALA ALA VAL ALA ILE ASP ALA SER PRO VAL ASP
SEQRES 3 B 277 ALA PRO ASP PRO ILE ASP ALA ALA PRO ASP ALA ASN GLN
SEQRES 4 B 277 ILE ASP ALA MSE VAL ASP ASP ARG PRO SER SER ALA ARG
SEQRES 5 B 277 LEU SER VAL ARG ALA LEU ASP THR THR GLU ALA GLY ASN
SEQRES 6 B 277 GLY PHE TRP GLU TYR LEU PRO PRO ARG TYR GLY ALA GLU
SEQRES 7 B 277 PRO ALA PRO LEU MSE VAL PHE TRP HIS GLY ILE GLY GLU
SEQRES 8 B 277 ASN GLY ASP GLY SER GLU ALA ALA LEU ASP LYS VAL LEU
SEQRES 9 B 277 ALA ASN GLY PRO PRO ARG TYR ILE GLU ARG ASP GLU TRP
SEQRES 10 B 277 SER ASN GLU ARG PRO PHE VAL VAL LEU SER PRO GLN HIS
SEQRES 11 B 277 ALA GLY GLY GLY CYS PRO SER ALA ASP GLU ILE ARG ASP
SEQRES 12 B 277 PHE LEU ALA PHE ALA VAL ASP THR TYR GLU VAL ASP GLU
SEQRES 13 B 277 SER ARG ILE TYR LEU THR GLY LEU 2ZC CYS GLY ALA ILE
SEQRES 14 B 277 GLY SER TRP ASN TYR LEU ARG ALA HIS LEU ASP THR THR
SEQRES 15 B 277 PRO ILE ALA ALA ALA VAL LEU ILE ALA GLY ASN GLY ARG
SEQRES 16 B 277 PRO ALA PHE ASN ASP HIS GLY CYS ASP LEU ALA GLN VAL
SEQRES 17 B 277 PRO ILE TRP GLY PHE HIS GLY ASP ALA ASP PRO THR VAL
SEQRES 18 B 277 ALA PRO ALA GLY THR ILE GLU PRO MSE ASN GLY LEU ILE
SEQRES 19 B 277 ALA CYS ALA GLN PRO ARG ALA ASP GLN GLN LEU THR VAL
SEQRES 20 B 277 TYR GLU GLY VAL GLY HIS ASP SER TRP SER ARG THR TYR
SEQRES 21 B 277 SER LEU SER ALA GLY HIS ASP ILE TYR ALA TRP LEU LEU
SEQRES 22 B 277 SER GLN SER ARG
MODRES 4Q82 MSE A 58 MET SELENOMETHIONINE
MODRES 4Q82 MSE A 98 MET SELENOMETHIONINE
MODRES 4Q82 2ZC A 180 SER
MODRES 4Q82 MSE A 245 MET SELENOMETHIONINE
MODRES 4Q82 MSE B 98 MET SELENOMETHIONINE
MODRES 4Q82 2ZC B 180 SER
MODRES 4Q82 MSE B 245 MET SELENOMETHIONINE
HET MSE A 58 8
HET MSE A 98 8
HET 2ZC A 180 9
HET MSE A 245 8
HET MSE B 98 8
HET 2ZC B 180 7
HET MSE B 245 8
HET CL A 301 1
HET CL A 302 1
HET CL A 303 1
HET GOL B 301 6
HET CL B 302 1
HET FMT B 303 3
HET CL B 304 1
HET CL B 305 1
HETNAM MSE SELENOMETHIONINE
HETNAM 2ZC O-{[4-(2-AMINOETHYL)PHENYL]SULFONYL}-L-SERINE
HETNAM CL CHLORIDE ION
HETNAM GOL GLYCEROL
HETNAM FMT FORMIC ACID
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 1 MSE 5(C5 H11 N O2 SE)
FORMUL 1 2ZC 2(C11 H16 N2 O5 S)
FORMUL 3 CL 6(CL 1-)
FORMUL 6 GOL C3 H8 O3
FORMUL 8 FMT C H2 O2
FORMUL 11 HOH *472(H2 O)
HELIX 1 1 PRO A 63 ALA A 66 5 4
HELIX 2 2 GLY A 103 ASN A 107 5 5
HELIX 3 3 SER A 111 ASP A 116 1 6
HELIX 4 4 LYS A 117 ALA A 120 5 4
HELIX 5 5 ASN A 121 ARG A 129 1 9
HELIX 6 6 SER A 152 TYR A 167 1 16
HELIX 7 7 2ZC A 180 LEU A 194 1 15
HELIX 8 8 GLY A 209 GLY A 217 1 9
HELIX 9 9 CYS A 218 VAL A 223 5 6
HELIX 10 10 PRO A 238 CYS A 251 1 14
HELIX 11 11 TRP A 271 SER A 276 1 6
HELIX 12 12 ASP A 282 SER A 289 1 8
HELIX 13 13 PRO B 63 ALA B 66 5 4
HELIX 14 14 GLY B 103 ASN B 107 5 5
HELIX 15 15 SER B 111 ASP B 116 1 6
HELIX 16 16 LYS B 117 ALA B 120 5 4
HELIX 17 17 ASN B 121 ARG B 129 1 9
HELIX 18 18 SER B 152 TYR B 167 1 16
HELIX 19 19 2ZC B 180 LEU B 194 1 15
HELIX 20 20 GLY B 209 GLY B 217 1 9
HELIX 21 21 CYS B 218 VAL B 223 5 6
HELIX 22 22 PRO B 238 CYS B 251 1 14
HELIX 23 23 TRP B 271 SER B 276 1 6
HELIX 24 24 ASP B 282 SER B 289 1 8
SHEET 1 A 8 LEU A 68 ARG A 71 0
SHEET 2 A 8 PHE A 82 TYR A 85 -1 O GLU A 84 N SER A 69
SHEET 3 A 8 VAL A 139 PRO A 143 -1 O VAL A 140 N TYR A 85
SHEET 4 A 8 ALA A 95 TRP A 101 1 N MSE A 98 O VAL A 139
SHEET 5 A 8 VAL A 169 LEU A 179 1 O TYR A 175 N LEU A 97
SHEET 6 A 8 ALA A 201 ILE A 205 1 O ILE A 205 N GLY A 178
SHEET 7 A 8 ILE A 225 GLY A 230 1 O TRP A 226 N ALA A 202
SHEET 8 A 8 GLN A 258 TYR A 263 1 O GLN A 259 N GLY A 227
SHEET 1 B 8 LEU B 68 ARG B 71 0
SHEET 2 B 8 PHE B 82 TYR B 85 -1 O GLU B 84 N SER B 69
SHEET 3 B 8 VAL B 139 PRO B 143 -1 O VAL B 140 N TYR B 85
SHEET 4 B 8 ALA B 95 TRP B 101 1 N MSE B 98 O VAL B 139
SHEET 5 B 8 VAL B 169 LEU B 179 1 O TYR B 175 N LEU B 97
SHEET 6 B 8 ALA B 201 ILE B 205 1 O ILE B 205 N GLY B 178
SHEET 7 B 8 ILE B 225 GLY B 230 1 O TRP B 226 N ALA B 202
SHEET 8 B 8 GLN B 258 TYR B 263 1 O THR B 261 N GLY B 227
SSBOND 1 CYS A 150 CYS A 181 1555 1555 2.06
SSBOND 2 CYS A 218 CYS A 251 1555 1555 2.04
SSBOND 3 CYS B 150 CYS B 181 1555 1555 2.07
SSBOND 4 CYS B 218 CYS B 251 1555 1555 2.05
LINK C ALA A 57 N MSE A 58 1555 1555 1.33
LINK C MSE A 58 N VAL A 59 1555 1555 1.33
LINK C LEU A 97 N MSE A 98 1555 1555 1.33
LINK C MSE A 98 N VAL A 99 1555 1555 1.33
LINK C PRO A 244 N MSE A 245 1555 1555 1.33
LINK C MSE A 245 N ASN A 246 1555 1555 1.34
LINK C LEU B 97 N MSE B 98 1555 1555 1.34
LINK C MSE B 98 N VAL B 99 1555 1555 1.33
LINK C PRO B 244 N MSE B 245 1555 1555 1.34
LINK C MSE B 245 N ASN B 246 1555 1555 1.34
LINK C LEU A 179 N 2ZC A 180 1555 1555 1.33
LINK C 2ZC A 180 N CYS A 181 1555 1555 1.33
LINK C LEU B 179 N 2ZC B 180 1555 1555 1.32
LINK C 2ZC B 180 N CYS B 181 1555 1555 1.32
CISPEP 1 GLN A 253 PRO A 254 0 -0.52
CISPEP 2 GLN B 253 PRO B 254 0 3.26
SITE 1 AC1 6 ARG A 273 ALA A 279 HOH A 425 ARG B 273
SITE 2 AC1 6 ALA B 279 HOH B 433
SITE 1 AC2 2 ARG A 125 ARG A 129
SITE 1 AC3 1 GLY A 148
SITE 1 AC4 4 ARG A 62 GLY B 148 HOH B 592 HOH B 607
SITE 1 AC5 1 ARG B 129
SITE 1 AC6 2 ARG B 210 ALA B 237
SITE 1 AC7 1 ALA B 153
SITE 1 AC8 1 ARG B 273
CRYST1 77.935 146.084 68.720 90.00 90.00 90.00 P 21 21 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 0.012831 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006845 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014552 0.00000
TER 1863 ARG A 292
TER 3719 ARG B 292
MASTER 626 0 15 24 16 0 9 6 4071 2 87 44
END |