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HEADER HYDROLASE 17-JAN-21 7DWC
TITLE BACTEROIDES THETAIOTAOMICRON VPI5482 BTAXE1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: XYLANASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACTEROIDES THETAIOTAOMICRON (STRAIN ATCC 29148
SOURCE 3 / DSM 2079 / NCTC 10582 / E50 / VPI-5482);
SOURCE 4 ORGANISM_TAXID: 226186;
SOURCE 5 GENE: BT_1008;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS BACTEROIDES THETAIOTAOMICRON VPI5482, ACETYL XYLAN ESTERASE, GUT
KEYWDS 2 BACTERIA-DERIVED, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR L.Y.WANG,Y.L.WANG,F.J.XIN,L.C.SUN
REVDAT 1 19-JAN-22 7DWC 0
JRNL AUTH L.Y.WANG,Y.L.WANG,F.J.XIN,L.C.SUN
JRNL TITL RATIONAL DESIGN OF A NOVEL ACETYL XYLAN ESTERASE FROM
JRNL TITL 2 BACTEROIDES THETAIOTAOMICRON VPI5482 FOR EXPANDED SUBSTRATE
JRNL TITL 3 SPECIFICITY WITH ENHANCED ACTIVITY
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.12_2829
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.07
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.380
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 3 NUMBER OF REFLECTIONS : 83576
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) : 0.175
REMARK 3 FREE R VALUE : 0.208
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.760
REMARK 3 FREE R VALUE TEST SET COUNT : 3976
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 28.0670 - 5.4637 0.99 2921 144 0.1627 0.1887
REMARK 3 2 5.4637 - 4.3419 0.99 2898 132 0.1307 0.1834
REMARK 3 3 4.3419 - 3.7946 1.00 2899 163 0.1298 0.1443
REMARK 3 4 3.7946 - 3.4483 1.00 2861 161 0.1472 0.1555
REMARK 3 5 3.4483 - 3.2015 1.00 2890 132 0.1556 0.1806
REMARK 3 6 3.2015 - 3.0130 1.00 2917 115 0.1719 0.2380
REMARK 3 7 3.0130 - 2.8623 1.00 2865 149 0.1794 0.2082
REMARK 3 8 2.8623 - 2.7378 1.00 2877 134 0.1840 0.2030
REMARK 3 9 2.7378 - 2.6325 1.00 2857 147 0.1845 0.2280
REMARK 3 10 2.6325 - 2.5417 1.00 2877 160 0.1860 0.2415
REMARK 3 11 2.5417 - 2.4623 1.00 2850 136 0.1792 0.2196
REMARK 3 12 2.4623 - 2.3919 1.00 2894 127 0.1840 0.2056
REMARK 3 13 2.3919 - 2.3290 1.00 2845 151 0.1740 0.2290
REMARK 3 14 2.3290 - 2.2722 0.99 2857 158 0.1724 0.2217
REMARK 3 15 2.2722 - 2.2205 1.00 2854 143 0.1787 0.2119
REMARK 3 16 2.2205 - 2.1733 0.99 2803 158 0.1886 0.2196
REMARK 3 17 2.1733 - 2.1299 1.00 2847 153 0.1951 0.2439
REMARK 3 18 2.1299 - 2.0897 1.00 2856 160 0.1990 0.2471
REMARK 3 19 2.0897 - 2.0524 1.00 2860 141 0.2154 0.2831
REMARK 3 20 2.0524 - 2.0176 1.00 2871 145 0.2246 0.2624
REMARK 3 21 2.0176 - 1.9850 1.00 2846 138 0.2291 0.2414
REMARK 3 22 1.9850 - 1.9545 1.00 2882 135 0.2335 0.3089
REMARK 3 23 1.9545 - 1.9258 1.00 2855 148 0.2461 0.2718
REMARK 3 24 1.9258 - 1.8987 0.99 2823 109 0.2643 0.3070
REMARK 3 25 1.8987 - 1.8730 0.99 2896 131 0.2727 0.3222
REMARK 3 26 1.8730 - 1.8487 0.99 2816 129 0.2905 0.2832
REMARK 3 27 1.8487 - 1.8256 0.98 2835 152 0.3011 0.3362
REMARK 3 28 1.8256 - 1.8040 0.80 2248 125 0.3018 0.3286
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) : 0.220
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.790
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 38.76
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 : 0.007 8373
REMARK 3 ANGLE : 0.891 11380
REMARK 3 CHIRALITY : 0.062 1250
REMARK 3 PLANARITY : 0.007 1467
REMARK 3 DIHEDRAL : 16.459 4942
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 31
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID -1 THROUGH 24 )
REMARK 3 ORIGIN FOR THE GROUP (A): 5.7675 10.8907 37.6821
REMARK 3 T TENSOR
REMARK 3 T11: 0.3878 T22: 0.6241
REMARK 3 T33: 0.4738 T12: 0.0109
REMARK 3 T13: -0.1578 T23: 0.0508
REMARK 3 L TENSOR
REMARK 3 L11: 1.4457 L22: 2.5017
REMARK 3 L33: 1.2017 L12: -1.2504
REMARK 3 L13: -0.9276 L23: -0.1151
REMARK 3 S TENSOR
REMARK 3 S11: -0.1581 S12: -0.4630 S13: -0.2507
REMARK 3 S21: 0.1473 S22: 0.1938 S23: -0.4412
REMARK 3 S31: 0.0986 S32: 0.2079 S33: 0.0319
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 25 THROUGH 97 )
REMARK 3 ORIGIN FOR THE GROUP (A): -3.5171 14.8605 32.7938
REMARK 3 T TENSOR
REMARK 3 T11: 0.2733 T22: 0.3539
REMARK 3 T33: 0.2582 T12: -0.0099
REMARK 3 T13: -0.0609 T23: 0.0235
REMARK 3 L TENSOR
REMARK 3 L11: 2.0566 L22: 1.8667
REMARK 3 L33: 2.3486 L12: 0.0572
REMARK 3 L13: 0.9681 L23: -0.9028
REMARK 3 S TENSOR
REMARK 3 S11: 0.0894 S12: -0.2671 S13: -0.2422
REMARK 3 S21: 0.2661 S22: -0.0324 S23: -0.2253
REMARK 3 S31: 0.1022 S32: 0.0086 S33: -0.0868
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 98 THROUGH 119 )
REMARK 3 ORIGIN FOR THE GROUP (A): 5.8765 23.7730 28.5381
REMARK 3 T TENSOR
REMARK 3 T11: 0.2504 T22: 0.5834
REMARK 3 T33: 0.3183 T12: -0.0966
REMARK 3 T13: -0.0620 T23: 0.0189
REMARK 3 L TENSOR
REMARK 3 L11: 3.8438 L22: 3.3997
REMARK 3 L33: 3.3508 L12: -1.6317
REMARK 3 L13: -0.7225 L23: 0.0584
REMARK 3 S TENSOR
REMARK 3 S11: -0.0545 S12: -0.1552 S13: 0.0541
REMARK 3 S21: 0.2839 S22: 0.0140 S23: -0.6564
REMARK 3 S31: -0.3703 S32: 0.8120 S33: 0.0835
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 120 THROUGH 138 )
REMARK 3 ORIGIN FOR THE GROUP (A): -5.9339 23.9880 24.1743
REMARK 3 T TENSOR
REMARK 3 T11: 0.2043 T22: 0.2397
REMARK 3 T33: 0.2246 T12: -0.0003
REMARK 3 T13: 0.0169 T23: -0.0135
REMARK 3 L TENSOR
REMARK 3 L11: 2.1476 L22: 1.9144
REMARK 3 L33: 2.5686 L12: 0.3139
REMARK 3 L13: 0.3600 L23: -0.5027
REMARK 3 S TENSOR
REMARK 3 S11: -0.0202 S12: -0.0470 S13: 0.0760
REMARK 3 S21: 0.0865 S22: -0.0096 S23: -0.2296
REMARK 3 S31: -0.2046 S32: 0.2357 S33: -0.0053
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 139 THROUGH 164 )
REMARK 3 ORIGIN FOR THE GROUP (A): -9.1809 27.1146 21.9675
REMARK 3 T TENSOR
REMARK 3 T11: 0.2572 T22: 0.2829
REMARK 3 T33: 0.2369 T12: -0.0231
REMARK 3 T13: 0.0198 T23: 0.0164
REMARK 3 L TENSOR
REMARK 3 L11: 1.9703 L22: 2.4067
REMARK 3 L33: 2.0827 L12: -0.4905
REMARK 3 L13: 0.0939 L23: 0.5019
REMARK 3 S TENSOR
REMARK 3 S11: 0.0327 S12: 0.2074 S13: 0.2430
REMARK 3 S21: 0.0019 S22: -0.0153 S23: -0.1589
REMARK 3 S31: -0.4047 S32: 0.0929 S33: 0.0077
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 165 THROUGH 247 )
REMARK 3 ORIGIN FOR THE GROUP (A): -15.2737 24.6850 21.1523
REMARK 3 T TENSOR
REMARK 3 T11: 0.2312 T22: 0.2625
REMARK 3 T33: 0.1987 T12: 0.0149
REMARK 3 T13: -0.0057 T23: 0.0095
REMARK 3 L TENSOR
REMARK 3 L11: 2.2089 L22: 1.8580
REMARK 3 L33: 2.8510 L12: 0.2071
REMARK 3 L13: 0.5029 L23: 0.6490
REMARK 3 S TENSOR
REMARK 3 S11: 0.0050 S12: -0.0184 S13: 0.1245
REMARK 3 S21: 0.0362 S22: -0.0110 S23: -0.0341
REMARK 3 S31: -0.2838 S32: -0.1761 S33: 0.0069
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 248 THROUGH 262 )
REMARK 3 ORIGIN FOR THE GROUP (A): -7.9958 8.5858 15.2253
REMARK 3 T TENSOR
REMARK 3 T11: 0.3490 T22: 0.2915
REMARK 3 T33: 0.3278 T12: 0.0807
REMARK 3 T13: -0.0475 T23: -0.0517
REMARK 3 L TENSOR
REMARK 3 L11: 5.8582 L22: 3.5956
REMARK 3 L33: 6.7150 L12: 1.0872
REMARK 3 L13: -0.8631 L23: 0.0019
REMARK 3 S TENSOR
REMARK 3 S11: -0.0063 S12: 0.4429 S13: -0.5527
REMARK 3 S21: -0.4678 S22: 0.1446 S23: -0.3697
REMARK 3 S31: 0.8434 S32: 0.3376 S33: -0.0842
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID -1 THROUGH 24 )
REMARK 3 ORIGIN FOR THE GROUP (A): 18.3878 9.9764 0.7755
REMARK 3 T TENSOR
REMARK 3 T11: 0.2672 T22: 0.5939
REMARK 3 T33: 0.3382 T12: 0.0005
REMARK 3 T13: -0.0699 T23: 0.0682
REMARK 3 L TENSOR
REMARK 3 L11: 2.4882 L22: 2.0721
REMARK 3 L33: 2.1604 L12: -1.2272
REMARK 3 L13: -0.5745 L23: -0.6206
REMARK 3 S TENSOR
REMARK 3 S11: 0.0613 S12: -0.4523 S13: -0.2444
REMARK 3 S21: 0.3311 S22: -0.1027 S23: -0.1815
REMARK 3 S31: 0.1607 S32: -0.1125 S33: 0.1593
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 25 THROUGH 43 )
REMARK 3 ORIGIN FOR THE GROUP (A): 11.0373 12.6527 2.7121
REMARK 3 T TENSOR
REMARK 3 T11: 0.3288 T22: 0.7492
REMARK 3 T33: 0.2924 T12: -0.0673
REMARK 3 T13: -0.0378 T23: 0.0717
REMARK 3 L TENSOR
REMARK 3 L11: 2.2060 L22: 2.9658
REMARK 3 L33: 3.4864 L12: 0.6429
REMARK 3 L13: -0.1368 L23: 0.2882
REMARK 3 S TENSOR
REMARK 3 S11: 0.2926 S12: -0.7823 S13: -0.1843
REMARK 3 S21: 0.5305 S22: -0.2921 S23: 0.0371
REMARK 3 S31: 0.3082 S32: -0.3966 S33: -0.0194
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 44 THROUGH 56 )
REMARK 3 ORIGIN FOR THE GROUP (A): 16.8286 10.0383 -12.2364
REMARK 3 T TENSOR
REMARK 3 T11: 0.2758 T22: 0.4408
REMARK 3 T33: 0.3013 T12: 0.0160
REMARK 3 T13: -0.0381 T23: 0.0193
REMARK 3 L TENSOR
REMARK 3 L11: 3.5718 L22: 1.5105
REMARK 3 L33: 3.7502 L12: -0.3141
REMARK 3 L13: -0.8454 L23: 0.7202
REMARK 3 S TENSOR
REMARK 3 S11: 0.1523 S12: -0.2269 S13: -0.3717
REMARK 3 S21: -0.0187 S22: 0.0597 S23: -0.0790
REMARK 3 S31: 0.5797 S32: 0.1173 S33: -0.0459
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 57 THROUGH 97 )
REMARK 3 ORIGIN FOR THE GROUP (A): 7.1724 16.6962 -5.6097
REMARK 3 T TENSOR
REMARK 3 T11: 0.2093 T22: 0.4881
REMARK 3 T33: 0.2362 T12: -0.0012
REMARK 3 T13: -0.0163 T23: -0.0094
REMARK 3 L TENSOR
REMARK 3 L11: 1.3577 L22: 1.9509
REMARK 3 L33: 1.2805 L12: 0.1094
REMARK 3 L13: 0.3272 L23: -0.0819
REMARK 3 S TENSOR
REMARK 3 S11: -0.0378 S12: -0.5113 S13: 0.0345
REMARK 3 S21: 0.2498 S22: 0.0084 S23: -0.0166
REMARK 3 S31: 0.0691 S32: -0.3156 S33: 0.0246
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 98 THROUGH 119 )
REMARK 3 ORIGIN FOR THE GROUP (A): 19.9885 22.3031 -9.1769
REMARK 3 T TENSOR
REMARK 3 T11: 0.1793 T22: 0.4530
REMARK 3 T33: 0.2269 T12: -0.0211
REMARK 3 T13: -0.0162 T23: 0.0001
REMARK 3 L TENSOR
REMARK 3 L11: 3.5742 L22: 2.5224
REMARK 3 L33: 1.8245 L12: -1.3358
REMARK 3 L13: -0.5528 L23: 0.4642
REMARK 3 S TENSOR
REMARK 3 S11: -0.0296 S12: -0.0295 S13: 0.0110
REMARK 3 S21: -0.0700 S22: -0.0141 S23: -0.2070
REMARK 3 S31: -0.0765 S32: 0.3840 S33: 0.0447
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 120 THROUGH 138 )
REMARK 3 ORIGIN FOR THE GROUP (A): 8.4044 23.3037 -13.8393
REMARK 3 T TENSOR
REMARK 3 T11: 0.2019 T22: 0.3802
REMARK 3 T33: 0.2278 T12: 0.0024
REMARK 3 T13: -0.0243 T23: -0.0145
REMARK 3 L TENSOR
REMARK 3 L11: 2.9421 L22: 1.2054
REMARK 3 L33: 1.7538 L12: -0.1540
REMARK 3 L13: -0.6324 L23: -0.4212
REMARK 3 S TENSOR
REMARK 3 S11: -0.0527 S12: -0.2603 S13: -0.0433
REMARK 3 S21: 0.0217 S22: -0.0770 S23: 0.0620
REMARK 3 S31: -0.1561 S32: 0.2904 S33: 0.0875
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 139 THROUGH 164 )
REMARK 3 ORIGIN FOR THE GROUP (A): 5.2822 26.6492 -16.2859
REMARK 3 T TENSOR
REMARK 3 T11: 0.2521 T22: 0.3933
REMARK 3 T33: 0.2434 T12: 0.0184
REMARK 3 T13: -0.0348 T23: -0.0106
REMARK 3 L TENSOR
REMARK 3 L11: 2.3402 L22: 1.8906
REMARK 3 L33: 1.4078 L12: 0.1339
REMARK 3 L13: -0.2730 L23: -0.0185
REMARK 3 S TENSOR
REMARK 3 S11: -0.0237 S12: 0.0486 S13: 0.2077
REMARK 3 S21: -0.0573 S22: -0.1265 S23: -0.0941
REMARK 3 S31: -0.2844 S32: -0.1864 S33: 0.1292
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 165 THROUGH 184 )
REMARK 3 ORIGIN FOR THE GROUP (A): -0.8072 37.3233 -8.0562
REMARK 3 T TENSOR
REMARK 3 T11: 0.4443 T22: 0.6260
REMARK 3 T33: 0.4655 T12: 0.1539
REMARK 3 T13: -0.1048 T23: -0.1825
REMARK 3 L TENSOR
REMARK 3 L11: 3.3007 L22: 1.2648
REMARK 3 L33: 3.3576 L12: 0.1125
REMARK 3 L13: 0.4123 L23: 1.2342
REMARK 3 S TENSOR
REMARK 3 S11: -0.3240 S12: -0.7192 S13: 0.9064
REMARK 3 S21: -0.0913 S22: -0.1409 S23: 0.3384
REMARK 3 S31: -0.8671 S32: -0.5499 S33: 0.2070
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 185 THROUGH 247 )
REMARK 3 ORIGIN FOR THE GROUP (A): -0.5942 20.2171 -20.5614
REMARK 3 T TENSOR
REMARK 3 T11: 0.1581 T22: 0.3308
REMARK 3 T33: 0.1684 T12: 0.0244
REMARK 3 T13: 0.0032 T23: -0.0167
REMARK 3 L TENSOR
REMARK 3 L11: 2.3551 L22: 1.5606
REMARK 3 L33: 1.7750 L12: 0.3995
REMARK 3 L13: 1.1776 L23: 0.5080
REMARK 3 S TENSOR
REMARK 3 S11: -0.0730 S12: -0.1046 S13: -0.0650
REMARK 3 S21: -0.0722 S22: 0.0521 S23: 0.0723
REMARK 3 S31: -0.0861 S32: -0.1650 S33: 0.0535
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 248 THROUGH 262 )
REMARK 3 ORIGIN FOR THE GROUP (A): 4.9727 7.6248 -21.7865
REMARK 3 T TENSOR
REMARK 3 T11: 0.2875 T22: 0.3435
REMARK 3 T33: 0.2802 T12: 0.0700
REMARK 3 T13: -0.0096 T23: -0.0166
REMARK 3 L TENSOR
REMARK 3 L11: 6.1488 L22: 2.8699
REMARK 3 L33: 6.6246 L12: 0.3856
REMARK 3 L13: -0.3346 L23: 0.3770
REMARK 3 S TENSOR
REMARK 3 S11: 0.1739 S12: 0.1081 S13: -0.4559
REMARK 3 S21: -0.2545 S22: 0.0618 S23: -0.2617
REMARK 3 S31: 0.7016 S32: 0.4031 S33: -0.1759
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN 'C' AND (RESID -1 THROUGH 24 )
REMARK 3 ORIGIN FOR THE GROUP (A): -31.4501 -3.7562 -14.1878
REMARK 3 T TENSOR
REMARK 3 T11: 0.6073 T22: 0.5320
REMARK 3 T33: 0.5684 T12: 0.0836
REMARK 3 T13: -0.2172 T23: -0.1758
REMARK 3 L TENSOR
REMARK 3 L11: 1.3439 L22: 4.4844
REMARK 3 L33: 1.8205 L12: 0.2834
REMARK 3 L13: -1.5564 L23: -0.4516
REMARK 3 S TENSOR
REMARK 3 S11: 0.3145 S12: 0.5361 S13: -0.5692
REMARK 3 S21: -0.3151 S22: 0.0811 S23: 0.0092
REMARK 3 S31: 0.7879 S32: 0.0960 S33: -0.2900
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 25 THROUGH 43 )
REMARK 3 ORIGIN FOR THE GROUP (A): -26.1059 1.8496 -16.4223
REMARK 3 T TENSOR
REMARK 3 T11: 0.3315 T22: 0.6072
REMARK 3 T33: 0.3687 T12: 0.0763
REMARK 3 T13: -0.0942 T23: -0.1805
REMARK 3 L TENSOR
REMARK 3 L11: 3.6450 L22: 2.4024
REMARK 3 L33: 3.3753 L12: -0.8082
REMARK 3 L13: 0.6297 L23: 0.6220
REMARK 3 S TENSOR
REMARK 3 S11: 0.3405 S12: 0.6297 S13: -0.3524
REMARK 3 S21: -0.3204 S22: 0.2464 S23: -0.3340
REMARK 3 S31: 0.3324 S32: 0.6921 S33: -0.3416
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 44 THROUGH 56 )
REMARK 3 ORIGIN FOR THE GROUP (A): -30.8524 -1.7914 -0.9345
REMARK 3 T TENSOR
REMARK 3 T11: 0.5166 T22: 0.2969
REMARK 3 T33: 0.4454 T12: -0.0264
REMARK 3 T13: -0.2080 T23: -0.0015
REMARK 3 L TENSOR
REMARK 3 L11: 1.5983 L22: 3.1429
REMARK 3 L33: 2.6534 L12: 1.0999
REMARK 3 L13: -0.7201 L23: -0.7511
REMARK 3 S TENSOR
REMARK 3 S11: 0.4068 S12: 0.0344 S13: -0.7785
REMARK 3 S21: 0.4918 S22: 0.0216 S23: -0.1610
REMARK 3 S31: 0.9486 S32: 0.3308 S33: -0.2662
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 57 THROUGH 97 )
REMARK 3 ORIGIN FOR THE GROUP (A): -25.1672 8.3441 -9.2490
REMARK 3 T TENSOR
REMARK 3 T11: 0.2313 T22: 0.4250
REMARK 3 T33: 0.2455 T12: 0.0163
REMARK 3 T13: -0.0206 T23: -0.0747
REMARK 3 L TENSOR
REMARK 3 L11: 1.7823 L22: 2.3966
REMARK 3 L33: 1.9149 L12: 0.0876
REMARK 3 L13: 1.0684 L23: 0.6593
REMARK 3 S TENSOR
REMARK 3 S11: 0.1837 S12: 0.3356 S13: -0.2710
REMARK 3 S21: -0.0764 S22: 0.0202 S23: -0.1813
REMARK 3 S31: 0.1265 S32: 0.4907 S33: -0.2295
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 98 THROUGH 119 )
REMARK 3 ORIGIN FOR THE GROUP (A): -39.0220 7.8504 -6.3140
REMARK 3 T TENSOR
REMARK 3 T11: 0.2653 T22: 0.4480
REMARK 3 T33: 0.2968 T12: -0.0249
REMARK 3 T13: -0.0556 T23: -0.0303
REMARK 3 L TENSOR
REMARK 3 L11: 1.7801 L22: 5.0858
REMARK 3 L33: 2.2724 L12: 1.7422
REMARK 3 L13: -0.9090 L23: -2.0292
REMARK 3 S TENSOR
REMARK 3 S11: 0.0558 S12: 0.1848 S13: -0.1742
REMARK 3 S21: -0.1682 S22: -0.0386 S23: 0.2165
REMARK 3 S31: 0.1680 S32: -0.3409 S33: -0.2213
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 120 THROUGH 164 )
REMARK 3 ORIGIN FOR THE GROUP (A): -29.4130 17.8593 -1.1496
REMARK 3 T TENSOR
REMARK 3 T11: 0.1776 T22: 0.3314
REMARK 3 T33: 0.1652 T12: 0.0022
REMARK 3 T13: -0.0204 T23: -0.0009
REMARK 3 L TENSOR
REMARK 3 L11: 2.1730 L22: 1.8123
REMARK 3 L33: 2.1780 L12: -0.2006
REMARK 3 L13: 0.1362 L23: 0.2129
REMARK 3 S TENSOR
REMARK 3 S11: -0.0651 S12: -0.0564 S13: -0.0998
REMARK 3 S21: 0.0113 S22: 0.0164 S23: 0.0475
REMARK 3 S31: -0.2322 S32: 0.0035 S33: 0.0353
REMARK 3 TLS GROUP : 24
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 165 THROUGH 184 )
REMARK 3 ORIGIN FOR THE GROUP (A): -28.3300 30.2659 -10.2825
REMARK 3 T TENSOR
REMARK 3 T11: 0.5306 T22: 0.3995
REMARK 3 T33: 0.2469 T12: -0.0570
REMARK 3 T13: -0.0546 T23: 0.0722
REMARK 3 L TENSOR
REMARK 3 L11: 3.4492 L22: 2.8863
REMARK 3 L33: 4.1373 L12: 0.5826
REMARK 3 L13: 0.1127 L23: 0.4658
REMARK 3 S TENSOR
REMARK 3 S11: -0.2850 S12: 0.3017 S13: 0.3581
REMARK 3 S21: -0.2659 S22: 0.0439 S23: 0.1279
REMARK 3 S31: -0.9352 S32: 0.1715 S33: 0.1163
REMARK 3 TLS GROUP : 25
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 185 THROUGH 232 )
REMARK 3 ORIGIN FOR THE GROUP (A): -24.0262 20.1706 6.3128
REMARK 3 T TENSOR
REMARK 3 T11: 0.2440 T22: 0.3288
REMARK 3 T33: 0.1772 T12: -0.0089
REMARK 3 T13: 0.0060 T23: 0.0011
REMARK 3 L TENSOR
REMARK 3 L11: 1.9175 L22: 1.4918
REMARK 3 L33: 2.3190 L12: 0.0004
REMARK 3 L13: 1.2218 L23: 0.1295
REMARK 3 S TENSOR
REMARK 3 S11: -0.0832 S12: 0.0067 S13: 0.0406
REMARK 3 S21: -0.0361 S22: 0.0747 S23: -0.0031
REMARK 3 S31: -0.3432 S32: -0.0147 S33: -0.0283
REMARK 3 TLS GROUP : 26
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 233 THROUGH 262 )
REMARK 3 ORIGIN FOR THE GROUP (A): -15.6957 6.9923 4.0227
REMARK 3 T TENSOR
REMARK 3 T11: 0.2877 T22: 0.4380
REMARK 3 T33: 0.3246 T12: 0.0529
REMARK 3 T13: -0.0697 T23: -0.0808
REMARK 3 L TENSOR
REMARK 3 L11: 3.2594 L22: 2.2764
REMARK 3 L33: 3.1606 L12: 0.8093
REMARK 3 L13: 0.3427 L23: 0.5635
REMARK 3 S TENSOR
REMARK 3 S11: 0.2113 S12: 0.1898 S13: -0.2784
REMARK 3 S21: 0.1313 S22: 0.1711 S23: -0.2651
REMARK 3 S31: 0.3730 S32: 0.5938 S33: -0.3025
REMARK 3 TLS GROUP : 27
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 1 THROUGH 24 )
REMARK 3 ORIGIN FOR THE GROUP (A): -48.0653 -2.4876 24.4126
REMARK 3 T TENSOR
REMARK 3 T11: 0.6694 T22: 0.4643
REMARK 3 T33: 0.4836 T12: -0.1291
REMARK 3 T13: -0.1017 T23: -0.1206
REMARK 3 L TENSOR
REMARK 3 L11: 2.8259 L22: 4.6329
REMARK 3 L33: 2.6695 L12: -0.1315
REMARK 3 L13: -0.6657 L23: -0.4314
REMARK 3 S TENSOR
REMARK 3 S11: 0.0438 S12: 0.6143 S13: -0.4915
REMARK 3 S21: -0.7874 S22: 0.0058 S23: 0.5217
REMARK 3 S31: 0.9833 S32: -0.3861 S33: -0.1129
REMARK 3 TLS GROUP : 28
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 25 THROUGH 97 )
REMARK 3 ORIGIN FOR THE GROUP (A): -41.2302 5.0484 29.2318
REMARK 3 T TENSOR
REMARK 3 T11: 0.3733 T22: 0.4209
REMARK 3 T33: 0.2896 T12: -0.0751
REMARK 3 T13: -0.0539 T23: 0.0074
REMARK 3 L TENSOR
REMARK 3 L11: 1.8621 L22: 2.1337
REMARK 3 L33: 2.6005 L12: -0.2094
REMARK 3 L13: 0.6214 L23: 1.1045
REMARK 3 S TENSOR
REMARK 3 S11: -0.0175 S12: 0.0206 S13: -0.2560
REMARK 3 S21: -0.3211 S22: 0.1736 S23: 0.1218
REMARK 3 S31: 0.4040 S32: -0.1173 S33: -0.1715
REMARK 3 TLS GROUP : 29
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 98 THROUGH 119 )
REMARK 3 ORIGIN FOR THE GROUP (A): -53.7595 9.2365 32.3736
REMARK 3 T TENSOR
REMARK 3 T11: 0.3953 T22: 0.6280
REMARK 3 T33: 0.3925 T12: -0.0370
REMARK 3 T13: -0.0866 T23: -0.0100
REMARK 3 L TENSOR
REMARK 3 L11: 3.2839 L22: 3.9553
REMARK 3 L33: 2.9256 L12: 1.8852
REMARK 3 L13: -1.7594 L23: -1.2464
REMARK 3 S TENSOR
REMARK 3 S11: -0.2565 S12: 0.0090 S13: -0.2343
REMARK 3 S21: -0.0403 S22: -0.0606 S23: 0.1850
REMARK 3 S31: 0.0059 S32: -0.6193 S33: 0.3342
REMARK 3 TLS GROUP : 30
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 120 THROUGH 247 )
REMARK 3 ORIGIN FOR THE GROUP (A): -38.2016 19.8333 38.0423
REMARK 3 T TENSOR
REMARK 3 T11: 0.2185 T22: 0.3566
REMARK 3 T33: 0.1729 T12: -0.0047
REMARK 3 T13: -0.0212 T23: 0.0129
REMARK 3 L TENSOR
REMARK 3 L11: 1.8169 L22: 1.9498
REMARK 3 L33: 2.3565 L12: 0.1763
REMARK 3 L13: 0.5116 L23: 0.3761
REMARK 3 S TENSOR
REMARK 3 S11: -0.0978 S12: -0.0693 S13: 0.1539
REMARK 3 S21: -0.2020 S22: 0.0760 S23: 0.1168
REMARK 3 S31: -0.1868 S32: -0.1612 S33: 0.0743
REMARK 3 TLS GROUP : 31
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 248 THROUGH 262 )
REMARK 3 ORIGIN FOR THE GROUP (A): -35.2366 4.3832 47.6059
REMARK 3 T TENSOR
REMARK 3 T11: 0.3837 T22: 0.3941
REMARK 3 T33: 0.2444 T12: -0.0165
REMARK 3 T13: -0.0475 T23: 0.0617
REMARK 3 L TENSOR
REMARK 3 L11: 4.4684 L22: 3.2344
REMARK 3 L33: 4.9564 L12: 0.7186
REMARK 3 L13: -1.5339 L23: -0.0186
REMARK 3 S TENSOR
REMARK 3 S11: -0.2433 S12: -0.6385 S13: -0.3943
REMARK 3 S21: 0.0599 S22: 0.2723 S23: 0.0277
REMARK 3 S31: 1.0500 S32: -0.2360 S33: -0.0572
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 1
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: (CHAIN A AND (RESID 1 OR (RESID 2 THROUGH
REMARK 3 3 AND (NAME N OR NAME CA OR NAME C OR
REMARK 3 NAME O OR NAME CB )) OR RESID 4 THROUGH
REMARK 3 11 OR (RESID 12 AND (NAME N OR NAME CA OR
REMARK 3 NAME C OR NAME O OR NAME CB )) OR RESID
REMARK 3 13 THROUGH 18 OR (RESID 19 AND (NAME N OR
REMARK 3 NAME CA OR NAME C OR NAME O OR NAME CB ))
REMARK 3 OR RESID 20 THROUGH 21 OR (RESID 22 AND
REMARK 3 (NAME N OR NAME CA OR NAME C OR NAME O OR
REMARK 3 NAME CB )) OR RESID 23 THROUGH 26 OR
REMARK 3 (RESID 27 AND (NAME N OR NAME CA OR NAME
REMARK 3 C OR NAME O OR NAME CB )) OR RESID 28
REMARK 3 THROUGH 45 OR (RESID 46 THROUGH 47 AND
REMARK 3 (NAME N OR NAME CA OR NAME C OR NAME O OR
REMARK 3 NAME CB )) OR RESID 48 THROUGH 78 OR
REMARK 3 (RESID 79 AND (NAME N OR NAME CA OR NAME
REMARK 3 C OR NAME O OR NAME CB )) OR RESID 80
REMARK 3 THROUGH 111 OR (RESID 112 AND (NAME N OR
REMARK 3 NAME CA OR NAME C OR NAME O OR NAME CB ))
REMARK 3 OR RESID 113 THROUGH 142 OR (RESID 143
REMARK 3 AND (NAME N OR NAME CA OR NAME C OR NAME
REMARK 3 O OR NAME CB )) OR RESID 144 THROUGH 168
REMARK 3 OR (RESID 169 AND (NAME N OR NAME CA OR
REMARK 3 NAME C OR NAME O OR NAME CB )) OR RESID
REMARK 3 170 THROUGH 173 OR (RESID 174 AND (NAME N
REMARK 3 OR NAME CA OR NAME C OR NAME O OR NAME CB
REMARK 3 )) OR RESID 175 THROUGH 181 OR (RESID 182
REMARK 3 THROUGH 183 AND (NAME N OR NAME CA OR
REMARK 3 NAME C OR NAME O OR NAME CB )) OR RESID
REMARK 3 184 THROUGH 221 OR (RESID 222 THROUGH 223
REMARK 3 AND (NAME N OR NAME CA OR NAME C OR NAME
REMARK 3 O OR NAME CB )) OR RESID 224 THROUGH 248
REMARK 3 OR (RESID 249 AND (NAME N OR NAME CA OR
REMARK 3 NAME C OR NAME O OR NAME CB )) OR RESID
REMARK 3 250 THROUGH 262))
REMARK 3 SELECTION : (CHAIN B AND (RESID 1 OR (RESID 2 THROUGH
REMARK 3 3 AND (NAME N OR NAME CA OR NAME C OR
REMARK 3 NAME O OR NAME CB )) OR RESID 4 THROUGH
REMARK 3 18 OR (RESID 19 AND (NAME N OR NAME CA OR
REMARK 3 NAME C OR NAME O OR NAME CB )) OR RESID
REMARK 3 20 THROUGH 21 OR (RESID 22 AND (NAME N OR
REMARK 3 NAME CA OR NAME C OR NAME O OR NAME CB ))
REMARK 3 OR RESID 23 THROUGH 26 OR (RESID 27 AND
REMARK 3 (NAME N OR NAME CA OR NAME C OR NAME O OR
REMARK 3 NAME CB )) OR RESID 28 THROUGH 45 OR
REMARK 3 (RESID 46 THROUGH 47 AND (NAME N OR NAME
REMARK 3 CA OR NAME C OR NAME O OR NAME CB )) OR
REMARK 3 RESID 48 THROUGH 74 OR (RESID 75 AND
REMARK 3 (NAME N OR NAME CA OR NAME C OR NAME O OR
REMARK 3 NAME CB )) OR RESID 76 THROUGH 78 OR
REMARK 3 (RESID 79 AND (NAME N OR NAME CA OR NAME
REMARK 3 C OR NAME O OR NAME CB )) OR RESID 80
REMARK 3 THROUGH 111 OR (RESID 112 AND (NAME N OR
REMARK 3 NAME CA OR NAME C OR NAME O OR NAME CB ))
REMARK 3 OR RESID 113 THROUGH 168 OR (RESID 169
REMARK 3 AND (NAME N OR NAME CA OR NAME C OR NAME
REMARK 3 O OR NAME CB )) OR RESID 170 THROUGH 173
REMARK 3 OR (RESID 174 AND (NAME N OR NAME CA OR
REMARK 3 NAME C OR NAME O OR NAME CB )) OR RESID
REMARK 3 175 THROUGH 181 OR (RESID 182 THROUGH 183
REMARK 3 AND (NAME N OR NAME CA OR NAME C OR NAME
REMARK 3 O OR NAME CB )) OR RESID 184 THROUGH 221
REMARK 3 OR (RESID 222 THROUGH 223 AND (NAME N OR
REMARK 3 NAME CA OR NAME C OR NAME O OR NAME CB ))
REMARK 3 OR RESID 224 THROUGH 248 OR (RESID 249
REMARK 3 AND (NAME N OR NAME CA OR NAME C OR NAME
REMARK 3 O OR NAME CB )) OR RESID 250 THROUGH 262))
REMARK 3 ATOM PAIRS NUMBER : 4868
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 2
REMARK 3 REFERENCE SELECTION: (CHAIN A AND (RESID 1 OR (RESID 2 THROUGH
REMARK 3 3 AND (NAME N OR NAME CA OR NAME C OR
REMARK 3 NAME O OR NAME CB )) OR RESID 4 THROUGH
REMARK 3 11 OR (RESID 12 AND (NAME N OR NAME CA OR
REMARK 3 NAME C OR NAME O OR NAME CB )) OR RESID
REMARK 3 13 THROUGH 18 OR (RESID 19 AND (NAME N OR
REMARK 3 NAME CA OR NAME C OR NAME O OR NAME CB ))
REMARK 3 OR RESID 20 THROUGH 21 OR (RESID 22 AND
REMARK 3 (NAME N OR NAME CA OR NAME C OR NAME O OR
REMARK 3 NAME CB )) OR RESID 23 THROUGH 26 OR
REMARK 3 (RESID 27 AND (NAME N OR NAME CA OR NAME
REMARK 3 C OR NAME O OR NAME CB )) OR RESID 28
REMARK 3 THROUGH 45 OR (RESID 46 THROUGH 47 AND
REMARK 3 (NAME N OR NAME CA OR NAME C OR NAME O OR
REMARK 3 NAME CB )) OR RESID 48 THROUGH 78 OR
REMARK 3 (RESID 79 AND (NAME N OR NAME CA OR NAME
REMARK 3 C OR NAME O OR NAME CB )) OR RESID 80
REMARK 3 THROUGH 111 OR (RESID 112 AND (NAME N OR
REMARK 3 NAME CA OR NAME C OR NAME O OR NAME CB ))
REMARK 3 OR RESID 113 THROUGH 142 OR (RESID 143
REMARK 3 AND (NAME N OR NAME CA OR NAME C OR NAME
REMARK 3 O OR NAME CB )) OR RESID 144 THROUGH 168
REMARK 3 OR (RESID 169 AND (NAME N OR NAME CA OR
REMARK 3 NAME C OR NAME O OR NAME CB )) OR RESID
REMARK 3 170 THROUGH 173 OR (RESID 174 AND (NAME N
REMARK 3 OR NAME CA OR NAME C OR NAME O OR NAME CB
REMARK 3 )) OR RESID 175 THROUGH 181 OR (RESID 182
REMARK 3 THROUGH 183 AND (NAME N OR NAME CA OR
REMARK 3 NAME C OR NAME O OR NAME CB )) OR RESID
REMARK 3 184 THROUGH 221 OR (RESID 222 THROUGH 223
REMARK 3 AND (NAME N OR NAME CA OR NAME C OR NAME
REMARK 3 O OR NAME CB )) OR RESID 224 THROUGH 248
REMARK 3 OR (RESID 249 AND (NAME N OR NAME CA OR
REMARK 3 NAME C OR NAME O OR NAME CB )) OR RESID
REMARK 3 250 THROUGH 262))
REMARK 3 SELECTION : (CHAIN C AND (RESID 1 THROUGH 2 OR (RESID
REMARK 3 3 AND (NAME N OR NAME CA OR NAME C OR
REMARK 3 NAME O OR NAME CB )) OR RESID 4 THROUGH
REMARK 3 18 OR (RESID 19 AND (NAME N OR NAME CA OR
REMARK 3 NAME C OR NAME O OR NAME CB )) OR RESID
REMARK 3 20 THROUGH 21 OR (RESID 22 AND (NAME N OR
REMARK 3 NAME CA OR NAME C OR NAME O OR NAME CB ))
REMARK 3 OR RESID 23 THROUGH 45 OR (RESID 46
REMARK 3 THROUGH 47 AND (NAME N OR NAME CA OR NAME
REMARK 3 C OR NAME O OR NAME CB )) OR RESID 48
REMARK 3 THROUGH 74 OR (RESID 75 AND (NAME N OR
REMARK 3 NAME CA OR NAME C OR NAME O OR NAME CB ))
REMARK 3 OR RESID 76 THROUGH 78 OR (RESID 79 AND
REMARK 3 (NAME N OR NAME CA OR NAME C OR NAME O OR
REMARK 3 NAME CB )) OR RESID 80 THROUGH 142 OR
REMARK 3 (RESID 143 AND (NAME N OR NAME CA OR NAME
REMARK 3 C OR NAME O OR NAME CB )) OR RESID 144
REMARK 3 THROUGH 181 OR (RESID 182 THROUGH 183 AND
REMARK 3 (NAME N OR NAME CA OR NAME C OR NAME O OR
REMARK 3 NAME CB )) OR RESID 184 THROUGH 221 OR
REMARK 3 (RESID 222 THROUGH 223 AND (NAME N OR
REMARK 3 NAME CA OR NAME C OR NAME O OR NAME CB ))
REMARK 3 OR RESID 224 THROUGH 262))
REMARK 3 ATOM PAIRS NUMBER : 4868
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 3
REMARK 3 REFERENCE SELECTION: (CHAIN A AND (RESID 1 OR (RESID 2 THROUGH
REMARK 3 3 AND (NAME N OR NAME CA OR NAME C OR
REMARK 3 NAME O OR NAME CB )) OR RESID 4 THROUGH
REMARK 3 11 OR (RESID 12 AND (NAME N OR NAME CA OR
REMARK 3 NAME C OR NAME O OR NAME CB )) OR RESID
REMARK 3 13 THROUGH 18 OR (RESID 19 AND (NAME N OR
REMARK 3 NAME CA OR NAME C OR NAME O OR NAME CB ))
REMARK 3 OR RESID 20 THROUGH 21 OR (RESID 22 AND
REMARK 3 (NAME N OR NAME CA OR NAME C OR NAME O OR
REMARK 3 NAME CB )) OR RESID 23 THROUGH 26 OR
REMARK 3 (RESID 27 AND (NAME N OR NAME CA OR NAME
REMARK 3 C OR NAME O OR NAME CB )) OR RESID 28
REMARK 3 THROUGH 45 OR (RESID 46 THROUGH 47 AND
REMARK 3 (NAME N OR NAME CA OR NAME C OR NAME O OR
REMARK 3 NAME CB )) OR RESID 48 THROUGH 78 OR
REMARK 3 (RESID 79 AND (NAME N OR NAME CA OR NAME
REMARK 3 C OR NAME O OR NAME CB )) OR RESID 80
REMARK 3 THROUGH 111 OR (RESID 112 AND (NAME N OR
REMARK 3 NAME CA OR NAME C OR NAME O OR NAME CB ))
REMARK 3 OR RESID 113 THROUGH 142 OR (RESID 143
REMARK 3 AND (NAME N OR NAME CA OR NAME C OR NAME
REMARK 3 O OR NAME CB )) OR RESID 144 THROUGH 168
REMARK 3 OR (RESID 169 AND (NAME N OR NAME CA OR
REMARK 3 NAME C OR NAME O OR NAME CB )) OR RESID
REMARK 3 170 THROUGH 173 OR (RESID 174 AND (NAME N
REMARK 3 OR NAME CA OR NAME C OR NAME O OR NAME CB
REMARK 3 )) OR RESID 175 THROUGH 181 OR (RESID 182
REMARK 3 THROUGH 183 AND (NAME N OR NAME CA OR
REMARK 3 NAME C OR NAME O OR NAME CB )) OR RESID
REMARK 3 184 THROUGH 221 OR (RESID 222 THROUGH 223
REMARK 3 AND (NAME N OR NAME CA OR NAME C OR NAME
REMARK 3 O OR NAME CB )) OR RESID 224 THROUGH 248
REMARK 3 OR (RESID 249 AND (NAME N OR NAME CA OR
REMARK 3 NAME C OR NAME O OR NAME CB )) OR RESID
REMARK 3 250 THROUGH 262))
REMARK 3 SELECTION : (CHAIN D AND (RESID 1 THROUGH 26 OR
REMARK 3 (RESID 27 AND (NAME N OR NAME CA OR NAME
REMARK 3 C OR NAME O OR NAME CB )) OR RESID 28
REMARK 3 THROUGH 111 OR (RESID 112 AND (NAME N OR
REMARK 3 NAME CA OR NAME C OR NAME O OR NAME CB ))
REMARK 3 OR RESID 113 THROUGH 173 OR (RESID 174
REMARK 3 AND (NAME N OR NAME CA OR NAME C OR NAME
REMARK 3 O OR NAME CB )) OR RESID 175 THROUGH 248
REMARK 3 OR (RESID 249 AND (NAME N OR NAME CA OR
REMARK 3 NAME C OR NAME O OR NAME CB )) OR RESID
REMARK 3 250 THROUGH 262))
REMARK 3 ATOM PAIRS NUMBER : 4868
REMARK 3 RMSD : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 7DWC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-JAN-21.
REMARK 100 THE DEPOSITION ID IS D_1300020291.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-SEP-20
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL19U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97852
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 S 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 83576
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 6.300
REMARK 200 R MERGE (I) : 0.10000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 5.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.93
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6
REMARK 200 DATA REDUNDANCY IN SHELL : 5.70
REMARK 200 R MERGE FOR SHELL (I) : 0.57400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: 6A6O
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 37.82
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.98
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 3350, 0.1M NACL, 0.1M TRIS PH
REMARK 280 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293.15K
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 41.29000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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 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 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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
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 SER D -1
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 ARG A 47 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 75 CG CD OE1 OE2
REMARK 470 ASP B 12 CG OD1 OD2
REMARK 470 ARG B 47 CG CD NE CZ NH1 NH2
REMARK 470 ASP B 143 CG OD1 OD2
REMARK 470 SER C -1 OG
REMARK 470 LYS C 2 CG CD CE NZ
REMARK 470 ASP C 12 CG OD1 OD2
REMARK 470 GLU C 27 CG CD OE1 OE2
REMARK 470 GLU C 169 CG CD OE1 OE2
REMARK 470 GLN C 183 CG CD OE1 NE2
REMARK 470 GLN C 249 CG CD OE1 NE2
REMARK 470 HIS D 0 CG ND1 CD2 CE1 NE2
REMARK 470 LYS D 2 CG CD CE NZ
REMARK 470 LYS D 3 CG CD CE NZ
REMARK 470 ASP D 12 CG OD1 OD2
REMARK 470 ASP D 19 CG OD1 OD2
REMARK 470 LYS D 22 CG CD CE NZ
REMARK 470 ASP D 46 CG OD1 OD2
REMARK 470 ARG D 47 CG CD NE CZ NH1 NH2
REMARK 470 GLU D 75 CG CD OE1 OE2
REMARK 470 LYS D 79 CG CD CE NZ
REMARK 470 ASP D 143 CG OD1 OD2
REMARK 470 GLU D 169 CG CD OE1 OE2
REMARK 470 GLU D 182 CG CD OE1 OE2
REMARK 470 GLN D 183 CG CD OE1 NE2
REMARK 470 LYS D 222 CG CD CE NZ
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 LYS A 2 -64.95 -95.16
REMARK 500 GLU A 67 -73.05 -96.32
REMARK 500 SER A 127 -129.69 59.11
REMARK 500 THR A 138 -50.55 -129.15
REMARK 500 TYR A 153 55.89 35.38
REMARK 500 LYS B 2 -65.61 -90.78
REMARK 500 GLU B 67 -71.37 -96.18
REMARK 500 SER B 127 -127.72 58.16
REMARK 500 THR B 138 -52.16 -132.06
REMARK 500 TYR B 153 56.45 33.79
REMARK 500 LYS C 2 -72.79 -99.04
REMARK 500 GLU C 67 -72.79 -96.21
REMARK 500 SER C 127 -128.85 55.24
REMARK 500 THR C 138 -54.31 -129.77
REMARK 500 TYR C 153 56.38 35.03
REMARK 500 LYS D 2 -66.97 -92.34
REMARK 500 GLU D 67 -72.27 -97.60
REMARK 500 SER D 127 -130.04 57.54
REMARK 500 THR D 138 -51.67 -128.90
REMARK 500 TYR D 153 56.54 34.26
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 439 DISTANCE = 5.83 ANGSTROMS
DBREF 7DWC A 1 262 UNP Q8A909 Q8A909_BACTN 1 262
DBREF 7DWC B 1 262 UNP Q8A909 Q8A909_BACTN 1 262
DBREF 7DWC C 1 262 UNP Q8A909 Q8A909_BACTN 1 262
DBREF 7DWC D 1 262 UNP Q8A909 Q8A909_BACTN 1 262
SEQADV 7DWC SER A -1 UNP Q8A909 EXPRESSION TAG
SEQADV 7DWC HIS A 0 UNP Q8A909 EXPRESSION TAG
SEQADV 7DWC SER B -1 UNP Q8A909 EXPRESSION TAG
SEQADV 7DWC HIS B 0 UNP Q8A909 EXPRESSION TAG
SEQADV 7DWC SER C -1 UNP Q8A909 EXPRESSION TAG
SEQADV 7DWC HIS C 0 UNP Q8A909 EXPRESSION TAG
SEQADV 7DWC SER D -1 UNP Q8A909 EXPRESSION TAG
SEQADV 7DWC HIS D 0 UNP Q8A909 EXPRESSION TAG
SEQRES 1 A 264 SER HIS MET LYS LYS LEU ILE CYS ILE SER LEU TYR GLU
SEQRES 2 A 264 ASP LEU SER MET THR THR TYR ASP LEU SER LYS VAL ASP
SEQRES 3 A 264 ASN ALA GLU LEU ILE GLY ILE VAL GLU ASN ALA SER GLU
SEQRES 4 A 264 GLY THR LEU PHE VAL PHE THR CYS ASP ARG PRO ASN GLY
SEQRES 5 A 264 SER SER VAL ILE MET CYS PRO GLY GLY GLY PHE LEU LYS
SEQRES 6 A 264 THR ASN LEU GLU ASN GLU GLY ILE ASP PHE ALA GLU TRP
SEQRES 7 A 264 PHE THR LYS LEU GLY ILE THR TYR ILE VAL PHE LYS TYR
SEQRES 8 A 264 ARG MET PRO HIS GLY ASN PRO ASP VAL PRO GLU GLN ASP
SEQRES 9 A 264 THR ARG LEU ALA LEU LYS VAL VAL ARG GLU LYS PHE PRO
SEQRES 10 A 264 GLU PHE CYS ASP LYS LEU GLY VAL MET GLY ALA SER ILE
SEQRES 11 A 264 GLY GLY TYR LEU ALA THR PHE SER ALA THR LEU LEU PRO
SEQRES 12 A 264 ASP ASP GLU LYS PRO ASP PHE GLN ILE LEU MET TYR PRO
SEQRES 13 A 264 VAL VAL SER VAL ASP ASP ARG LEU THR HIS PHE PRO CYS
SEQRES 14 A 264 ARG GLU ARG MET PHE GLY HIS SER TYR SER PRO ASP LYS
SEQRES 15 A 264 MET GLU GLN TYR SER PRO ILE GLU HIS ILE THR SER GLY
SEQRES 16 A 264 THR PRO ALA ALA PHE ILE VAL ALA ALA ALA ASP ASP ALA
SEQRES 17 A 264 VAL VAL SER PRO LEU ASN GLY ILE MET TYR ALA ALA ARG
SEQRES 18 A 264 LEU GLN LYS ALA ASP ILE PRO ILE SER LEU HIS ILE TYR
SEQRES 19 A 264 PRO ALA GLY GLY HIS GLY PHE GLY TYR ASN ASP SER PHE
SEQRES 20 A 264 VAL TYR LYS GLN GLU TRP LEU GLN GLU LEU GLY GLU TRP
SEQRES 21 A 264 LEU ALA LYS LEU
SEQRES 1 B 264 SER HIS MET LYS LYS LEU ILE CYS ILE SER LEU TYR GLU
SEQRES 2 B 264 ASP LEU SER MET THR THR TYR ASP LEU SER LYS VAL ASP
SEQRES 3 B 264 ASN ALA GLU LEU ILE GLY ILE VAL GLU ASN ALA SER GLU
SEQRES 4 B 264 GLY THR LEU PHE VAL PHE THR CYS ASP ARG PRO ASN GLY
SEQRES 5 B 264 SER SER VAL ILE MET CYS PRO GLY GLY GLY PHE LEU LYS
SEQRES 6 B 264 THR ASN LEU GLU ASN GLU GLY ILE ASP PHE ALA GLU TRP
SEQRES 7 B 264 PHE THR LYS LEU GLY ILE THR TYR ILE VAL PHE LYS TYR
SEQRES 8 B 264 ARG MET PRO HIS GLY ASN PRO ASP VAL PRO GLU GLN ASP
SEQRES 9 B 264 THR ARG LEU ALA LEU LYS VAL VAL ARG GLU LYS PHE PRO
SEQRES 10 B 264 GLU PHE CYS ASP LYS LEU GLY VAL MET GLY ALA SER ILE
SEQRES 11 B 264 GLY GLY TYR LEU ALA THR PHE SER ALA THR LEU LEU PRO
SEQRES 12 B 264 ASP ASP GLU LYS PRO ASP PHE GLN ILE LEU MET TYR PRO
SEQRES 13 B 264 VAL VAL SER VAL ASP ASP ARG LEU THR HIS PHE PRO CYS
SEQRES 14 B 264 ARG GLU ARG MET PHE GLY HIS SER TYR SER PRO ASP LYS
SEQRES 15 B 264 MET GLU GLN TYR SER PRO ILE GLU HIS ILE THR SER GLY
SEQRES 16 B 264 THR PRO ALA ALA PHE ILE VAL ALA ALA ALA ASP ASP ALA
SEQRES 17 B 264 VAL VAL SER PRO LEU ASN GLY ILE MET TYR ALA ALA ARG
SEQRES 18 B 264 LEU GLN LYS ALA ASP ILE PRO ILE SER LEU HIS ILE TYR
SEQRES 19 B 264 PRO ALA GLY GLY HIS GLY PHE GLY TYR ASN ASP SER PHE
SEQRES 20 B 264 VAL TYR LYS GLN GLU TRP LEU GLN GLU LEU GLY GLU TRP
SEQRES 21 B 264 LEU ALA LYS LEU
SEQRES 1 C 264 SER HIS MET LYS LYS LEU ILE CYS ILE SER LEU TYR GLU
SEQRES 2 C 264 ASP LEU SER MET THR THR TYR ASP LEU SER LYS VAL ASP
SEQRES 3 C 264 ASN ALA GLU LEU ILE GLY ILE VAL GLU ASN ALA SER GLU
SEQRES 4 C 264 GLY THR LEU PHE VAL PHE THR CYS ASP ARG PRO ASN GLY
SEQRES 5 C 264 SER SER VAL ILE MET CYS PRO GLY GLY GLY PHE LEU LYS
SEQRES 6 C 264 THR ASN LEU GLU ASN GLU GLY ILE ASP PHE ALA GLU TRP
SEQRES 7 C 264 PHE THR LYS LEU GLY ILE THR TYR ILE VAL PHE LYS TYR
SEQRES 8 C 264 ARG MET PRO HIS GLY ASN PRO ASP VAL PRO GLU GLN ASP
SEQRES 9 C 264 THR ARG LEU ALA LEU LYS VAL VAL ARG GLU LYS PHE PRO
SEQRES 10 C 264 GLU PHE CYS ASP LYS LEU GLY VAL MET GLY ALA SER ILE
SEQRES 11 C 264 GLY GLY TYR LEU ALA THR PHE SER ALA THR LEU LEU PRO
SEQRES 12 C 264 ASP ASP GLU LYS PRO ASP PHE GLN ILE LEU MET TYR PRO
SEQRES 13 C 264 VAL VAL SER VAL ASP ASP ARG LEU THR HIS PHE PRO CYS
SEQRES 14 C 264 ARG GLU ARG MET PHE GLY HIS SER TYR SER PRO ASP LYS
SEQRES 15 C 264 MET GLU GLN TYR SER PRO ILE GLU HIS ILE THR SER GLY
SEQRES 16 C 264 THR PRO ALA ALA PHE ILE VAL ALA ALA ALA ASP ASP ALA
SEQRES 17 C 264 VAL VAL SER PRO LEU ASN GLY ILE MET TYR ALA ALA ARG
SEQRES 18 C 264 LEU GLN LYS ALA ASP ILE PRO ILE SER LEU HIS ILE TYR
SEQRES 19 C 264 PRO ALA GLY GLY HIS GLY PHE GLY TYR ASN ASP SER PHE
SEQRES 20 C 264 VAL TYR LYS GLN GLU TRP LEU GLN GLU LEU GLY GLU TRP
SEQRES 21 C 264 LEU ALA LYS LEU
SEQRES 1 D 264 SER HIS MET LYS LYS LEU ILE CYS ILE SER LEU TYR GLU
SEQRES 2 D 264 ASP LEU SER MET THR THR TYR ASP LEU SER LYS VAL ASP
SEQRES 3 D 264 ASN ALA GLU LEU ILE GLY ILE VAL GLU ASN ALA SER GLU
SEQRES 4 D 264 GLY THR LEU PHE VAL PHE THR CYS ASP ARG PRO ASN GLY
SEQRES 5 D 264 SER SER VAL ILE MET CYS PRO GLY GLY GLY PHE LEU LYS
SEQRES 6 D 264 THR ASN LEU GLU ASN GLU GLY ILE ASP PHE ALA GLU TRP
SEQRES 7 D 264 PHE THR LYS LEU GLY ILE THR TYR ILE VAL PHE LYS TYR
SEQRES 8 D 264 ARG MET PRO HIS GLY ASN PRO ASP VAL PRO GLU GLN ASP
SEQRES 9 D 264 THR ARG LEU ALA LEU LYS VAL VAL ARG GLU LYS PHE PRO
SEQRES 10 D 264 GLU PHE CYS ASP LYS LEU GLY VAL MET GLY ALA SER ILE
SEQRES 11 D 264 GLY GLY TYR LEU ALA THR PHE SER ALA THR LEU LEU PRO
SEQRES 12 D 264 ASP ASP GLU LYS PRO ASP PHE GLN ILE LEU MET TYR PRO
SEQRES 13 D 264 VAL VAL SER VAL ASP ASP ARG LEU THR HIS PHE PRO CYS
SEQRES 14 D 264 ARG GLU ARG MET PHE GLY HIS SER TYR SER PRO ASP LYS
SEQRES 15 D 264 MET GLU GLN TYR SER PRO ILE GLU HIS ILE THR SER GLY
SEQRES 16 D 264 THR PRO ALA ALA PHE ILE VAL ALA ALA ALA ASP ASP ALA
SEQRES 17 D 264 VAL VAL SER PRO LEU ASN GLY ILE MET TYR ALA ALA ARG
SEQRES 18 D 264 LEU GLN LYS ALA ASP ILE PRO ILE SER LEU HIS ILE TYR
SEQRES 19 D 264 PRO ALA GLY GLY HIS GLY PHE GLY TYR ASN ASP SER PHE
SEQRES 20 D 264 VAL TYR LYS GLN GLU TRP LEU GLN GLU LEU GLY GLU TRP
SEQRES 21 D 264 LEU ALA LYS LEU
FORMUL 5 HOH *572(H2 O)
HELIX 1 AA1 SER A 21 VAL A 23 5 3
HELIX 2 AA2 ASP A 24 ALA A 35 1 12
HELIX 3 AA3 GLY A 70 ASP A 72 5 3
HELIX 4 AA4 PHE A 73 LEU A 80 1 8
HELIX 5 AA5 ASP A 97 PHE A 114 1 18
HELIX 6 AA6 PRO A 115 CYS A 118 5 4
HELIX 7 AA7 ILE A 128 LEU A 139 1 12
HELIX 8 AA8 HIS A 164 GLY A 173 1 10
HELIX 9 AA9 SER A 177 HIS A 189 5 13
HELIX 10 AB1 PRO A 210 ALA A 223 1 14
HELIX 11 AB2 TYR A 247 LYS A 261 1 15
HELIX 12 AB3 SER B 21 VAL B 23 5 3
HELIX 13 AB4 ASP B 24 ALA B 35 1 12
HELIX 14 AB5 GLY B 70 ASP B 72 5 3
HELIX 15 AB6 PHE B 73 LEU B 80 1 8
HELIX 16 AB7 ASP B 97 PHE B 114 1 18
HELIX 17 AB8 PRO B 115 CYS B 118 5 4
HELIX 18 AB9 ILE B 128 ALA B 137 1 10
HELIX 19 AC1 HIS B 164 GLY B 173 1 10
HELIX 20 AC2 SER B 177 ILE B 190 5 14
HELIX 21 AC3 PRO B 210 ALA B 223 1 14
HELIX 22 AC4 TYR B 247 LYS B 261 1 15
HELIX 23 AC5 SER C 21 VAL C 23 5 3
HELIX 24 AC6 ASP C 24 ALA C 35 1 12
HELIX 25 AC7 GLY C 70 ASP C 72 5 3
HELIX 26 AC8 PHE C 73 LEU C 80 1 8
HELIX 27 AC9 ASP C 97 PHE C 114 1 18
HELIX 28 AD1 PRO C 115 CYS C 118 5 4
HELIX 29 AD2 ILE C 128 LEU C 139 1 12
HELIX 30 AD3 HIS C 164 GLY C 173 1 10
HELIX 31 AD4 SER C 177 ILE C 190 5 14
HELIX 32 AD5 PRO C 210 ALA C 223 1 14
HELIX 33 AD6 TYR C 247 LYS C 261 1 15
HELIX 34 AD7 SER D 21 VAL D 23 5 3
HELIX 35 AD8 ASP D 24 ALA D 35 1 12
HELIX 36 AD9 GLY D 70 ASP D 72 5 3
HELIX 37 AE1 PHE D 73 LEU D 80 1 8
HELIX 38 AE2 ASP D 97 PHE D 114 1 18
HELIX 39 AE3 PRO D 115 CYS D 118 5 4
HELIX 40 AE4 ILE D 128 LEU D 139 1 12
HELIX 41 AE5 HIS D 164 GLY D 173 1 10
HELIX 42 AE6 SER D 177 ILE D 190 5 14
HELIX 43 AE7 PRO D 210 ALA D 223 1 14
HELIX 44 AE8 TYR D 247 LYS D 261 1 15
SHEET 1 AA118 MET A 15 ASP A 19 0
SHEET 2 AA118 MET A 1 SER A 8 -1 N CYS A 6 O THR A 16
SHEET 3 AA118 THR A 39 CYS A 45 -1 O VAL A 42 N ILE A 5
SHEET 4 AA118 THR A 83 LYS A 88 -1 O TYR A 84 N PHE A 43
SHEET 5 AA118 SER A 51 CYS A 56 1 N MET A 55 O ILE A 85
SHEET 6 AA118 LYS A 120 ALA A 126 1 O MET A 124 N CYS A 56
SHEET 7 AA118 PHE A 148 MET A 152 1 O MET A 152 N GLY A 125
SHEET 8 AA118 ALA A 196 ALA A 202 1 O PHE A 198 N LEU A 151
SHEET 9 AA118 ILE A 227 TYR A 232 1 O HIS A 230 N ILE A 199
SHEET 10 AA118 ILE C 227 TYR C 232 -1 O ILE C 231 N LEU A 229
SHEET 11 AA118 ALA C 196 ALA C 202 1 N ILE C 199 O SER C 228
SHEET 12 AA118 PHE C 148 MET C 152 1 N LEU C 151 O PHE C 198
SHEET 13 AA118 LYS C 120 ALA C 126 1 N GLY C 125 O MET C 152
SHEET 14 AA118 SER C 51 CYS C 56 1 N SER C 52 O GLY C 122
SHEET 15 AA118 THR C 83 LYS C 88 1 O ILE C 85 N MET C 55
SHEET 16 AA118 THR C 39 CYS C 45 -1 N PHE C 43 O TYR C 84
SHEET 17 AA118 MET C 1 SER C 8 -1 N ILE C 5 O VAL C 42
SHEET 18 AA118 MET C 15 ASP C 19 -1 O THR C 16 N CYS C 6
SHEET 1 AA2 9 MET B 15 ASP B 19 0
SHEET 2 AA2 9 MET B 1 SER B 8 -1 N CYS B 6 O THR B 16
SHEET 3 AA2 9 THR B 39 CYS B 45 -1 O VAL B 42 N ILE B 5
SHEET 4 AA2 9 THR B 83 LYS B 88 -1 O TYR B 84 N PHE B 43
SHEET 5 AA2 9 SER B 51 CYS B 56 1 N MET B 55 O ILE B 85
SHEET 6 AA2 9 LYS B 120 ALA B 126 1 O GLY B 122 N SER B 52
SHEET 7 AA2 9 PHE B 148 MET B 152 1 O MET B 152 N GLY B 125
SHEET 8 AA2 9 ALA B 196 ALA B 202 1 O PHE B 198 N LEU B 151
SHEET 9 AA2 9 ILE B 227 TYR B 232 1 O SER B 228 N ILE B 199
SHEET 1 AA3 9 MET D 15 ASP D 19 0
SHEET 2 AA3 9 LYS D 3 SER D 8 -1 N CYS D 6 O THR D 16
SHEET 3 AA3 9 THR D 39 PHE D 43 -1 O VAL D 42 N ILE D 5
SHEET 4 AA3 9 THR D 83 LYS D 88 -1 O TYR D 84 N PHE D 43
SHEET 5 AA3 9 SER D 51 CYS D 56 1 N MET D 55 O ILE D 85
SHEET 6 AA3 9 LYS D 120 ALA D 126 1 O GLY D 122 N SER D 52
SHEET 7 AA3 9 PHE D 148 MET D 152 1 O MET D 152 N GLY D 125
SHEET 8 AA3 9 ALA D 196 ALA D 202 1 O PHE D 198 N LEU D 151
SHEET 9 AA3 9 ILE D 227 TYR D 232 1 O SER D 228 N ILE D 199
CRYST1 73.796 82.580 81.534 90.00 110.17 90.00 P 1 21 1 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 0.013551 0.000000 0.004978 0.00000
SCALE2 0.000000 0.012109 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013066 0.00000
TER 2062 LEU A 262
TER 4122 LEU B 262
TER 6170 LEU C 262
TER 8177 LEU D 262
MASTER 964 0 0 44 36 0 0 6 8745 4 0 84
END |