HEADER PROTEIN BINDING 05-JAN-16 5HE8
TITLE BACTERIAL INITIATION PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HELICASE LOADER;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H, I, J, L, K;
COMPND 4 SYNONYM: PRIMOSOMAL PROTEIN DNAI;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS;
SOURCE 3 ORGANISM_TAXID: 1280;
SOURCE 4 GENE: DNAI;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HELICASE LOADER, PROTEIN BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR I.V.HOOD,J.M.BERGER
REVDAT 3 04-DEC-19 5HE8 1 REMARK
REVDAT 2 20-SEP-17 5HE8 1 REMARK
REVDAT 1 08-JUN-16 5HE8 0
JRNL AUTH I.V.HOOD,J.M.BERGER
JRNL TITL BACTERIAL INITIATION PROTEIN
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.10_2155: ???)
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) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.24
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 81007
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.227
REMARK 3 R VALUE (WORKING SET) : 0.225
REMARK 3 FREE R VALUE : 0.270
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.910
REMARK 3 FREE R VALUE TEST SET COUNT : 3975
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 47.2489 - 7.8833 0.99 2961 150 0.1959 0.2319
REMARK 3 2 7.8833 - 6.2619 1.00 2867 128 0.2193 0.2455
REMARK 3 3 6.2619 - 5.4716 1.00 2820 143 0.2253 0.2544
REMARK 3 4 5.4716 - 4.9720 1.00 2829 127 0.1886 0.2250
REMARK 3 5 4.9720 - 4.6159 1.00 2773 154 0.1743 0.2183
REMARK 3 6 4.6159 - 4.3440 1.00 2769 132 0.1607 0.2213
REMARK 3 7 4.3440 - 4.1266 1.00 2783 153 0.1665 0.1965
REMARK 3 8 4.1266 - 3.9470 1.00 2768 134 0.1897 0.2239
REMARK 3 9 3.9470 - 3.7951 1.00 2768 150 0.1959 0.2526
REMARK 3 10 3.7951 - 3.6642 1.00 2746 143 0.1976 0.2283
REMARK 3 11 3.6642 - 3.5497 1.00 2731 165 0.2004 0.2395
REMARK 3 12 3.5497 - 3.4483 1.00 2767 133 0.2178 0.2774
REMARK 3 13 3.4483 - 3.3575 1.00 2735 161 0.2331 0.3149
REMARK 3 14 3.3575 - 3.2756 1.00 2709 156 0.2392 0.3039
REMARK 3 15 3.2756 - 3.2012 1.00 2739 145 0.2484 0.3037
REMARK 3 16 3.2012 - 3.1331 1.00 2730 146 0.2753 0.3405
REMARK 3 17 3.1331 - 3.0704 1.00 2738 144 0.2890 0.3384
REMARK 3 18 3.0704 - 3.0125 1.00 2727 150 0.2833 0.3267
REMARK 3 19 3.0125 - 2.9587 1.00 2760 133 0.2847 0.3164
REMARK 3 20 2.9587 - 2.9085 1.00 2714 128 0.2968 0.3866
REMARK 3 21 2.9085 - 2.8616 1.00 2714 149 0.3172 0.3697
REMARK 3 22 2.8616 - 2.8176 1.00 2722 140 0.3200 0.3726
REMARK 3 23 2.8176 - 2.7762 1.00 2733 124 0.3386 0.3600
REMARK 3 24 2.7762 - 2.7371 0.99 2700 145 0.3682 0.3576
REMARK 3 25 2.7371 - 2.7001 0.99 2706 135 0.4191 0.4899
REMARK 3 26 2.7001 - 2.6650 0.99 2753 119 0.5241 0.5602
REMARK 3 27 2.6650 - 2.6317 0.99 2677 141 0.5907 0.6723
REMARK 3 28 2.6317 - 2.6000 0.95 2593 147 0.7110 0.6216
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) : 0.510
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.270
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 : 0.003 16195
REMARK 3 ANGLE : 0.509 21838
REMARK 3 CHIRALITY : 0.039 2401
REMARK 3 PLANARITY : 0.003 2764
REMARK 3 DIHEDRAL : 8.428 9662
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 56
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 138 THROUGH 153 )
REMARK 3 ORIGIN FOR THE GROUP (A): 9.6242 151.3231 56.5602
REMARK 3 T TENSOR
REMARK 3 T11: 0.8364 T22: 0.4904
REMARK 3 T33: 0.7447 T12: 0.0645
REMARK 3 T13: 0.2235 T23: -0.1086
REMARK 3 L TENSOR
REMARK 3 L11: 6.9465 L22: 7.4409
REMARK 3 L33: 10.0025 L12: 6.6873
REMARK 3 L13: -1.6093 L23: 1.0980
REMARK 3 S TENSOR
REMARK 3 S11: 0.0823 S12: -0.0890 S13: 0.2409
REMARK 3 S21: -0.8703 S22: 0.5574 S23: -0.1326
REMARK 3 S31: -2.3801 S32: 0.4119 S33: -0.5678
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 154 THROUGH 184 )
REMARK 3 ORIGIN FOR THE GROUP (A): 11.1630 143.1683 53.5240
REMARK 3 T TENSOR
REMARK 3 T11: 0.5639 T22: 0.4965
REMARK 3 T33: 0.5309 T12: 0.0429
REMARK 3 T13: 0.1360 T23: -0.0641
REMARK 3 L TENSOR
REMARK 3 L11: 3.8087 L22: 0.8865
REMARK 3 L33: 2.7507 L12: 0.5826
REMARK 3 L13: -0.2456 L23: -1.1938
REMARK 3 S TENSOR
REMARK 3 S11: -0.0027 S12: -0.0875 S13: -0.0789
REMARK 3 S21: -0.1306 S22: -0.0277 S23: -0.1634
REMARK 3 S31: -0.2236 S32: 0.0735 S33: -0.0364
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 185 THROUGH 203 )
REMARK 3 ORIGIN FOR THE GROUP (A): 10.1713 133.9691 40.9858
REMARK 3 T TENSOR
REMARK 3 T11: 0.8710 T22: 0.7380
REMARK 3 T33: 0.6013 T12: -0.1539
REMARK 3 T13: 0.0999 T23: -0.0201
REMARK 3 L TENSOR
REMARK 3 L11: 6.2714 L22: 7.7116
REMARK 3 L33: 7.3286 L12: -3.3281
REMARK 3 L13: -6.1702 L23: 3.1854
REMARK 3 S TENSOR
REMARK 3 S11: 0.0134 S12: 0.2290 S13: -0.4887
REMARK 3 S21: -0.8169 S22: -0.3511 S23: 0.1584
REMARK 3 S31: 0.0574 S32: -0.7814 S33: 0.1905
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 204 THROUGH 217 )
REMARK 3 ORIGIN FOR THE GROUP (A): 12.6850 134.6744 29.6925
REMARK 3 T TENSOR
REMARK 3 T11: 0.9421 T22: 0.7645
REMARK 3 T33: 0.8271 T12: -0.0489
REMARK 3 T13: 0.1595 T23: -0.0279
REMARK 3 L TENSOR
REMARK 3 L11: 3.8370 L22: 9.4313
REMARK 3 L33: 9.7971 L12: 5.7605
REMARK 3 L13: 2.9782 L23: 2.8466
REMARK 3 S TENSOR
REMARK 3 S11: 0.2213 S12: 0.4207 S13: -0.5741
REMARK 3 S21: -0.2549 S22: 0.3450 S23: -0.4984
REMARK 3 S31: 0.4882 S32: 0.0931 S33: -0.4543
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 218 THROUGH 271 )
REMARK 3 ORIGIN FOR THE GROUP (A): 20.5227 139.0501 42.1932
REMARK 3 T TENSOR
REMARK 3 T11: 0.6570 T22: 0.5624
REMARK 3 T33: 0.6443 T12: -0.1076
REMARK 3 T13: 0.2226 T23: -0.0385
REMARK 3 L TENSOR
REMARK 3 L11: 3.0927 L22: 1.8768
REMARK 3 L33: 4.2280 L12: 0.4205
REMARK 3 L13: -1.2718 L23: 0.1577
REMARK 3 S TENSOR
REMARK 3 S11: -0.0747 S12: 0.3266 S13: -0.1365
REMARK 3 S21: -0.3901 S22: -0.0104 S23: -0.3248
REMARK 3 S31: 0.2779 S32: -0.2168 S33: 0.0457
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 272 THROUGH 300 )
REMARK 3 ORIGIN FOR THE GROUP (A): 27.7372 139.6582 45.0023
REMARK 3 T TENSOR
REMARK 3 T11: 0.5812 T22: 0.6273
REMARK 3 T33: 0.8388 T12: -0.0713
REMARK 3 T13: 0.2491 T23: -0.0855
REMARK 3 L TENSOR
REMARK 3 L11: 5.5504 L22: 2.2728
REMARK 3 L33: 8.1496 L12: -0.8876
REMARK 3 L13: -2.7858 L23: 2.7437
REMARK 3 S TENSOR
REMARK 3 S11: -0.0929 S12: -0.3310 S13: -0.0623
REMARK 3 S21: -0.5166 S22: 0.3424 S23: -0.2559
REMARK 3 S31: -0.0400 S32: 1.5146 S33: -0.1421
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 138 THROUGH 152 )
REMARK 3 ORIGIN FOR THE GROUP (A): 10.5913 101.4310 39.3255
REMARK 3 T TENSOR
REMARK 3 T11: 0.7778 T22: 0.5244
REMARK 3 T33: 0.8607 T12: 0.1228
REMARK 3 T13: -0.3090 T23: -0.0024
REMARK 3 L TENSOR
REMARK 3 L11: 4.4325 L22: 9.8845
REMARK 3 L33: 2.0411 L12: -0.6798
REMARK 3 L13: -0.3235 L23: -0.8753
REMARK 3 S TENSOR
REMARK 3 S11: 0.2762 S12: 0.2273 S13: -0.7829
REMARK 3 S21: -0.5457 S22: 0.2151 S23: 1.0388
REMARK 3 S31: 0.6057 S32: -0.4358 S33: -0.5181
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 153 THROUGH 184 )
REMARK 3 ORIGIN FOR THE GROUP (A): 11.3282 108.3694 43.1179
REMARK 3 T TENSOR
REMARK 3 T11: 0.6175 T22: 0.4526
REMARK 3 T33: 0.6442 T12: 0.0104
REMARK 3 T13: -0.1518 T23: -0.0089
REMARK 3 L TENSOR
REMARK 3 L11: 9.2717 L22: 2.7701
REMARK 3 L33: 4.4097 L12: 1.0195
REMARK 3 L13: -0.3114 L23: 0.1536
REMARK 3 S TENSOR
REMARK 3 S11: -0.1824 S12: 0.4087 S13: -0.4456
REMARK 3 S21: -0.5524 S22: 0.2636 S23: 0.1738
REMARK 3 S31: 0.8234 S32: 0.2082 S33: -0.2449
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 185 THROUGH 200 )
REMARK 3 ORIGIN FOR THE GROUP (A): 9.2122 117.0321 54.4627
REMARK 3 T TENSOR
REMARK 3 T11: 0.3879 T22: 0.6199
REMARK 3 T33: 0.6787 T12: 0.0485
REMARK 3 T13: -0.0254 T23: 0.1689
REMARK 3 L TENSOR
REMARK 3 L11: 4.7604 L22: 8.6977
REMARK 3 L33: 6.5643 L12: 1.5507
REMARK 3 L13: 1.3600 L23: 1.6946
REMARK 3 S TENSOR
REMARK 3 S11: 0.4545 S12: -0.8975 S13: 0.6176
REMARK 3 S21: -0.1651 S22: -0.1407 S23: 0.5792
REMARK 3 S31: 0.3268 S32: -0.6930 S33: -0.2620
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 201 THROUGH 233 )
REMARK 3 ORIGIN FOR THE GROUP (A): 13.7670 116.5899 60.6847
REMARK 3 T TENSOR
REMARK 3 T11: 0.6789 T22: 0.7230
REMARK 3 T33: 0.6577 T12: 0.0878
REMARK 3 T13: -0.1049 T23: 0.0370
REMARK 3 L TENSOR
REMARK 3 L11: 2.4444 L22: 4.0621
REMARK 3 L33: 4.1234 L12: -0.4714
REMARK 3 L13: -0.8412 L23: -0.4479
REMARK 3 S TENSOR
REMARK 3 S11: 0.1202 S12: -0.7925 S13: 0.1045
REMARK 3 S21: 0.3887 S22: 0.1608 S23: -0.0866
REMARK 3 S31: -0.3753 S32: -0.0841 S33: -0.3283
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 234 THROUGH 271 )
REMARK 3 ORIGIN FOR THE GROUP (A): 21.8601 111.6809 55.6634
REMARK 3 T TENSOR
REMARK 3 T11: 0.3979 T22: 0.4281
REMARK 3 T33: 0.5186 T12: -0.0271
REMARK 3 T13: -0.0663 T23: 0.0701
REMARK 3 L TENSOR
REMARK 3 L11: 5.8354 L22: 1.4083
REMARK 3 L33: 8.5775 L12: -1.7545
REMARK 3 L13: 3.3161 L23: -0.0517
REMARK 3 S TENSOR
REMARK 3 S11: -0.1202 S12: -0.4039 S13: -0.0821
REMARK 3 S21: 0.0946 S22: 0.0219 S23: -0.2288
REMARK 3 S31: -0.0244 S32: 0.0493 S33: 0.1255
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 272 THROUGH 278 )
REMARK 3 ORIGIN FOR THE GROUP (A): 33.2631 122.0793 60.2878
REMARK 3 T TENSOR
REMARK 3 T11: 0.8605 T22: 0.8957
REMARK 3 T33: 1.1578 T12: -0.2000
REMARK 3 T13: -0.2561 T23: 0.0185
REMARK 3 L TENSOR
REMARK 3 L11: 4.1549 L22: 7.5962
REMARK 3 L33: 6.2976 L12: -1.6153
REMARK 3 L13: 1.7489 L23: 1.9046
REMARK 3 S TENSOR
REMARK 3 S11: -0.5810 S12: 0.1838 S13: 1.5220
REMARK 3 S21: -0.4919 S22: 0.8885 S23: -0.5164
REMARK 3 S31: -1.7155 S32: 0.3514 S33: -0.1819
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 279 THROUGH 301 )
REMARK 3 ORIGIN FOR THE GROUP (A): 25.4529 109.1380 49.0342
REMARK 3 T TENSOR
REMARK 3 T11: 0.5310 T22: 0.5307
REMARK 3 T33: 0.6148 T12: -0.0186
REMARK 3 T13: -0.0957 T23: 0.0159
REMARK 3 L TENSOR
REMARK 3 L11: 6.8940 L22: 2.5952
REMARK 3 L33: 2.5071 L12: 0.5971
REMARK 3 L13: 3.4234 L23: 1.5490
REMARK 3 S TENSOR
REMARK 3 S11: 0.2785 S12: -0.0381 S13: -0.6898
REMARK 3 S21: 0.1181 S22: -0.1176 S23: -0.3179
REMARK 3 S31: 0.0359 S32: 1.0615 S33: -0.1469
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 136 THROUGH 152 )
REMARK 3 ORIGIN FOR THE GROUP (A): -21.0943 111.1686 31.5271
REMARK 3 T TENSOR
REMARK 3 T11: 0.5487 T22: 0.5338
REMARK 3 T33: 0.5531 T12: 0.0351
REMARK 3 T13: 0.1204 T23: -0.0540
REMARK 3 L TENSOR
REMARK 3 L11: 6.2429 L22: 4.0139
REMARK 3 L33: 7.0048 L12: -4.4124
REMARK 3 L13: 2.4289 L23: -3.8292
REMARK 3 S TENSOR
REMARK 3 S11: 0.4905 S12: -0.1177 S13: 0.5101
REMARK 3 S21: -0.4718 S22: -0.4725 S23: -1.4257
REMARK 3 S31: -0.0577 S32: 0.0410 S33: 0.0514
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 153 THROUGH 183 )
REMARK 3 ORIGIN FOR THE GROUP (A): -25.8911 110.1078 38.8972
REMARK 3 T TENSOR
REMARK 3 T11: 0.4538 T22: 0.3836
REMARK 3 T33: 0.4121 T12: -0.0512
REMARK 3 T13: 0.0185 T23: 0.0212
REMARK 3 L TENSOR
REMARK 3 L11: 3.7854 L22: 4.0495
REMARK 3 L33: 5.9003 L12: -0.0232
REMARK 3 L13: 1.2727 L23: 0.4226
REMARK 3 S TENSOR
REMARK 3 S11: 0.2494 S12: 0.0343 S13: -0.0843
REMARK 3 S21: -0.3960 S22: -0.2413 S23: -0.1722
REMARK 3 S31: 0.0426 S32: -0.1444 S33: -0.0653
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 184 THROUGH 192 )
REMARK 3 ORIGIN FOR THE GROUP (A): -28.5299 100.4925 42.7350
REMARK 3 T TENSOR
REMARK 3 T11: 0.7036 T22: 0.5742
REMARK 3 T33: 0.6036 T12: -0.0351
REMARK 3 T13: -0.0864 T23: 0.0344
REMARK 3 L TENSOR
REMARK 3 L11: 6.1930 L22: 9.6519
REMARK 3 L33: 9.9033 L12: -4.3339
REMARK 3 L13: -2.8592 L23: 5.3823
REMARK 3 S TENSOR
REMARK 3 S11: -0.5914 S12: -0.1645 S13: -0.4582
REMARK 3 S21: 0.9298 S22: 0.4302 S23: 0.3548
REMARK 3 S31: 1.8962 S32: 0.0004 S33: -0.1324
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 193 THROUGH 218 )
REMARK 3 ORIGIN FOR THE GROUP (A): -28.6931 100.7962 60.6096
REMARK 3 T TENSOR
REMARK 3 T11: 0.5549 T22: 0.6038
REMARK 3 T33: 0.7533 T12: -0.1358
REMARK 3 T13: -0.0512 T23: 0.0089
REMARK 3 L TENSOR
REMARK 3 L11: 5.2127 L22: 5.4488
REMARK 3 L33: 8.5329 L12: -5.1865
REMARK 3 L13: -0.0385 L23: -0.8463
REMARK 3 S TENSOR
REMARK 3 S11: -0.2646 S12: -0.6254 S13: -0.7763
REMARK 3 S21: -0.0863 S22: 0.1483 S23: 0.7524
REMARK 3 S31: 0.4687 S32: -1.2586 S33: 0.0753
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 219 THROUGH 297 )
REMARK 3 ORIGIN FOR THE GROUP (A): -20.8005 113.1760 54.5385
REMARK 3 T TENSOR
REMARK 3 T11: 0.4169 T22: 0.4234
REMARK 3 T33: 0.4226 T12: -0.0591
REMARK 3 T13: -0.0073 T23: -0.0034
REMARK 3 L TENSOR
REMARK 3 L11: 2.2071 L22: 2.5326
REMARK 3 L33: 4.9929 L12: -0.6425
REMARK 3 L13: 1.3578 L23: 0.0145
REMARK 3 S TENSOR
REMARK 3 S11: -0.0812 S12: 0.0777 S13: 0.1054
REMARK 3 S21: -0.0556 S22: 0.1039 S23: -0.0344
REMARK 3 S31: 0.0418 S32: -0.0115 S33: -0.0728
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 298 THROUGH 306 )
REMARK 3 ORIGIN FOR THE GROUP (A): -28.1636 125.9890 28.9930
REMARK 3 T TENSOR
REMARK 3 T11: 0.8070 T22: 0.9587
REMARK 3 T33: 0.8188 T12: -0.1086
REMARK 3 T13: 0.1688 T23: 0.0296
REMARK 3 L TENSOR
REMARK 3 L11: 2.7546 L22: 5.7735
REMARK 3 L33: 8.8809 L12: 0.2180
REMARK 3 L13: 4.7293 L23: -1.9706
REMARK 3 S TENSOR
REMARK 3 S11: -0.3070 S12: 0.5389 S13: 1.6900
REMARK 3 S21: -0.7993 S22: 0.6232 S23: 0.2063
REMARK 3 S31: -1.9283 S32: 0.2312 S33: -0.6364
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 135 THROUGH 152 )
REMARK 3 ORIGIN FOR THE GROUP (A): -22.9989 141.6836 64.5169
REMARK 3 T TENSOR
REMARK 3 T11: 0.5972 T22: 0.7646
REMARK 3 T33: 0.6331 T12: 0.0031
REMARK 3 T13: -0.0250 T23: -0.1805
REMARK 3 L TENSOR
REMARK 3 L11: 5.9318 L22: 9.1737
REMARK 3 L33: 8.1152 L12: 4.8203
REMARK 3 L13: 1.0816 L23: -2.5869
REMARK 3 S TENSOR
REMARK 3 S11: -0.0708 S12: 0.1386 S13: -0.4587
REMARK 3 S21: 1.1986 S22: 0.9769 S23: -0.9345
REMARK 3 S31: 0.1298 S32: 0.2419 S33: -0.9039
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 153 THROUGH 188 )
REMARK 3 ORIGIN FOR THE GROUP (A): -27.9266 145.0392 57.3882
REMARK 3 T TENSOR
REMARK 3 T11: 0.5698 T22: 0.5994
REMARK 3 T33: 0.5675 T12: -0.0290
REMARK 3 T13: 0.1248 T23: -0.0304
REMARK 3 L TENSOR
REMARK 3 L11: 4.1694 L22: 4.9139
REMARK 3 L33: 5.2911 L12: -0.3509
REMARK 3 L13: -1.2533 L23: 1.2379
REMARK 3 S TENSOR
REMARK 3 S11: 0.2177 S12: -0.1428 S13: 0.2951
REMARK 3 S21: -0.1812 S22: 0.0207 S23: -0.3445
REMARK 3 S31: -0.4876 S32: -0.2206 S33: -0.2336
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 189 THROUGH 233 )
REMARK 3 ORIGIN FOR THE GROUP (A): -29.8980 148.3113 38.9821
REMARK 3 T TENSOR
REMARK 3 T11: 0.4710 T22: 0.6111
REMARK 3 T33: 0.6101 T12: 0.0027
REMARK 3 T13: 0.0861 T23: 0.0078
REMARK 3 L TENSOR
REMARK 3 L11: 0.9460 L22: 4.3513
REMARK 3 L33: 4.5497 L12: -0.5829
REMARK 3 L13: -0.7935 L23: -2.8065
REMARK 3 S TENSOR
REMARK 3 S11: 0.1265 S12: 0.1864 S13: 0.4492
REMARK 3 S21: -0.0403 S22: 0.2785 S23: 0.5870
REMARK 3 S31: -0.1724 S32: -0.7282 S33: -0.3180
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 234 THROUGH 297 )
REMARK 3 ORIGIN FOR THE GROUP (A): -20.0739 139.5881 41.4745
REMARK 3 T TENSOR
REMARK 3 T11: 0.3848 T22: 0.3118
REMARK 3 T33: 0.4271 T12: -0.0123
REMARK 3 T13: 0.0372 T23: -0.0350
REMARK 3 L TENSOR
REMARK 3 L11: 3.3725 L22: 3.6399
REMARK 3 L33: 6.2238 L12: 0.7136
REMARK 3 L13: -1.7581 L23: -1.9494
REMARK 3 S TENSOR
REMARK 3 S11: 0.1386 S12: -0.1260 S13: 0.1890
REMARK 3 S21: -0.1594 S22: -0.0341 S23: -0.2453
REMARK 3 S31: -0.2153 S32: -0.0506 S33: -0.0885
REMARK 3 TLS GROUP : 24
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 298 THROUGH 304 )
REMARK 3 ORIGIN FOR THE GROUP (A): -30.0520 126.7285 64.5979
REMARK 3 T TENSOR
REMARK 3 T11: 1.1689 T22: 1.1644
REMARK 3 T33: 0.8254 T12: 0.2925
REMARK 3 T13: 0.2771 T23: 0.0977
REMARK 3 L TENSOR
REMARK 3 L11: 0.0092 L22: 0.0148
REMARK 3 L33: 0.0250 L12: 0.0498
REMARK 3 L13: -0.0334 L23: -0.0347
REMARK 3 S TENSOR
REMARK 3 S11: -0.8805 S12: -1.7782 S13: -0.3998
REMARK 3 S21: 2.3822 S22: 0.7024 S23: 0.0824
REMARK 3 S31: 1.1576 S32: -0.6827 S33: 0.2160
REMARK 3 TLS GROUP : 25
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 138 THROUGH 152 )
REMARK 3 ORIGIN FOR THE GROUP (A): 8.6785 118.6925 31.4260
REMARK 3 T TENSOR
REMARK 3 T11: 0.6494 T22: 0.4528
REMARK 3 T33: 0.6330 T12: -0.0044
REMARK 3 T13: -0.1110 T23: 0.0242
REMARK 3 L TENSOR
REMARK 3 L11: 7.9404 L22: 2.4471
REMARK 3 L33: 8.2570 L12: 4.3569
REMARK 3 L13: 0.3496 L23: -0.1334
REMARK 3 S TENSOR
REMARK 3 S11: 0.7344 S12: 0.0812 S13: -0.5240
REMARK 3 S21: -0.5076 S22: 0.0516 S23: 0.8148
REMARK 3 S31: -0.8218 S32: 0.5803 S33: -0.8835
REMARK 3 TLS GROUP : 26
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 153 THROUGH 200 )
REMARK 3 ORIGIN FOR THE GROUP (A): -0.4132 109.9081 28.8975
REMARK 3 T TENSOR
REMARK 3 T11: 0.4533 T22: 0.3262
REMARK 3 T33: 0.5266 T12: 0.0893
REMARK 3 T13: -0.0859 T23: 0.0469
REMARK 3 L TENSOR
REMARK 3 L11: 4.2605 L22: 1.7006
REMARK 3 L33: 4.3455 L12: -0.0066
REMARK 3 L13: 1.0258 L23: 2.6693
REMARK 3 S TENSOR
REMARK 3 S11: 0.0778 S12: 0.0054 S13: 0.2700
REMARK 3 S21: 0.1514 S22: 0.1292 S23: -0.3000
REMARK 3 S31: 0.0637 S32: 0.3274 S33: -0.2581
REMARK 3 TLS GROUP : 27
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 201 THROUGH 218 )
REMARK 3 ORIGIN FOR THE GROUP (A): -17.8025 106.6255 18.7331
REMARK 3 T TENSOR
REMARK 3 T11: 0.4671 T22: 0.3510
REMARK 3 T33: 0.5581 T12: 0.0430
REMARK 3 T13: 0.0033 T23: -0.0061
REMARK 3 L TENSOR
REMARK 3 L11: 9.6140 L22: 7.0236
REMARK 3 L33: 8.4944 L12: -3.2711
REMARK 3 L13: -1.0649 L23: -0.8083
REMARK 3 S TENSOR
REMARK 3 S11: 0.1591 S12: 0.1417 S13: -0.6649
REMARK 3 S21: 0.9250 S22: -0.4081 S23: 1.0672
REMARK 3 S31: 0.5643 S32: -0.7169 S33: 0.1452
REMARK 3 TLS GROUP : 28
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 219 THROUGH 302 )
REMARK 3 ORIGIN FOR THE GROUP (A): -0.1873 107.4660 15.2346
REMARK 3 T TENSOR
REMARK 3 T11: 0.4107 T22: 0.3777
REMARK 3 T33: 0.5159 T12: 0.0323
REMARK 3 T13: -0.0426 T23: 0.0277
REMARK 3 L TENSOR
REMARK 3 L11: 2.5349 L22: 2.7356
REMARK 3 L33: 4.7298 L12: -0.3882
REMARK 3 L13: 0.6052 L23: 1.2099
REMARK 3 S TENSOR
REMARK 3 S11: -0.0154 S12: 0.0647 S13: 0.1810
REMARK 3 S21: 0.1356 S22: 0.0605 S23: -0.3064
REMARK 3 S31: 0.0129 S32: 0.2801 S33: -0.0711
REMARK 3 TLS GROUP : 29
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 138 THROUGH 169 )
REMARK 3 ORIGIN FOR THE GROUP (A): 4.9859 136.2412 67.2078
REMARK 3 T TENSOR
REMARK 3 T11: 0.4303 T22: 0.3756
REMARK 3 T33: 0.4869 T12: 0.0023
REMARK 3 T13: 0.0844 T23: -0.0224
REMARK 3 L TENSOR
REMARK 3 L11: 1.0637 L22: 2.1725
REMARK 3 L33: 4.3682 L12: 0.2211
REMARK 3 L13: 0.0066 L23: -0.2029
REMARK 3 S TENSOR
REMARK 3 S11: -0.0551 S12: -0.1181 S13: -0.1624
REMARK 3 S21: -0.3036 S22: -0.1459 S23: -0.1559
REMARK 3 S31: 0.2936 S32: 0.2460 S33: 0.2109
REMARK 3 TLS GROUP : 30
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 170 THROUGH 200 )
REMARK 3 ORIGIN FOR THE GROUP (A): -5.4788 143.9070 64.8455
REMARK 3 T TENSOR
REMARK 3 T11: 0.5210 T22: 0.4632
REMARK 3 T33: 0.5139 T12: -0.1190
REMARK 3 T13: 0.0055 T23: -0.0133
REMARK 3 L TENSOR
REMARK 3 L11: 3.5964 L22: 2.2680
REMARK 3 L33: 4.8491 L12: -1.1546
REMARK 3 L13: -3.2932 L23: 0.7681
REMARK 3 S TENSOR
REMARK 3 S11: 0.1268 S12: 0.3567 S13: -0.1101
REMARK 3 S21: -0.1179 S22: -0.1853 S23: 0.2155
REMARK 3 S31: -0.2413 S32: -0.0951 S33: 0.1245
REMARK 3 TLS GROUP : 31
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 201 THROUGH 217 )
REMARK 3 ORIGIN FOR THE GROUP (A): -19.9871 146.7021 77.6123
REMARK 3 T TENSOR
REMARK 3 T11: 0.6690 T22: 0.3963
REMARK 3 T33: 0.6632 T12: 0.1130
REMARK 3 T13: -0.0733 T23: -0.0539
REMARK 3 L TENSOR
REMARK 3 L11: 8.8974 L22: 5.9427
REMARK 3 L33: 2.2801 L12: 5.6284
REMARK 3 L13: 2.5140 L23: 1.8432
REMARK 3 S TENSOR
REMARK 3 S11: -0.2378 S12: 0.1455 S13: 1.6842
REMARK 3 S21: -0.2395 S22: 0.0515 S23: 0.1580
REMARK 3 S31: -1.3497 S32: -0.2762 S33: -0.1929
REMARK 3 TLS GROUP : 32
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 218 THROUGH 271 )
REMARK 3 ORIGIN FOR THE GROUP (A): -4.9005 143.9027 78.9478
REMARK 3 T TENSOR
REMARK 3 T11: 0.3327 T22: 0.3243
REMARK 3 T33: 0.4097 T12: -0.0408
REMARK 3 T13: 0.0403 T23: -0.0131
REMARK 3 L TENSOR
REMARK 3 L11: 4.0285 L22: 2.6307
REMARK 3 L33: 3.2901 L12: 0.0310
REMARK 3 L13: -0.2287 L23: 0.1919
REMARK 3 S TENSOR
REMARK 3 S11: -0.0350 S12: 0.0516 S13: -0.0490
REMARK 3 S21: -0.0485 S22: 0.0303 S23: 0.0085
REMARK 3 S31: -0.1310 S32: 0.0204 S33: -0.0236
REMARK 3 TLS GROUP : 33
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 272 THROUGH 301 )
REMARK 3 ORIGIN FOR THE GROUP (A): 1.4169 144.5869 83.5484
REMARK 3 T TENSOR
REMARK 3 T11: 0.3674 T22: 0.3102
REMARK 3 T33: 0.4600 T12: -0.0003
REMARK 3 T13: -0.0249 T23: 0.0190
REMARK 3 L TENSOR
REMARK 3 L11: 6.6121 L22: 4.4358
REMARK 3 L33: 7.6968 L12: -0.4446
REMARK 3 L13: -1.7414 L23: 2.2115
REMARK 3 S TENSOR
REMARK 3 S11: 0.1286 S12: -0.3543 S13: 0.0226
REMARK 3 S21: 0.0856 S22: -0.2098 S23: -0.1708
REMARK 3 S31: -0.1479 S32: 0.1528 S33: 0.0398
REMARK 3 TLS GROUP : 34
REMARK 3 SELECTION: CHAIN 'G' AND (RESID 137 THROUGH 184 )
REMARK 3 ORIGIN FOR THE GROUP (A): -39.7138 139.2556 66.9027
REMARK 3 T TENSOR
REMARK 3 T11: 0.4536 T22: 0.5860
REMARK 3 T33: 0.5194 T12: -0.0881
REMARK 3 T13: 0.0114 T23: -0.0769
REMARK 3 L TENSOR
REMARK 3 L11: 4.2387 L22: 3.8785
REMARK 3 L33: 6.3129 L12: -1.5749
REMARK 3 L13: -1.7214 L23: 0.9064
REMARK 3 S TENSOR
REMARK 3 S11: -0.0326 S12: 0.7546 S13: -0.4173
REMARK 3 S21: -0.2959 S22: 0.0394 S23: 0.4529
REMARK 3 S31: 0.2387 S32: -0.7423 S33: -0.0544
REMARK 3 TLS GROUP : 35
REMARK 3 SELECTION: CHAIN 'G' AND (RESID 185 THROUGH 203 )
REMARK 3 ORIGIN FOR THE GROUP (A): -39.2115 153.6667 78.8621
REMARK 3 T TENSOR
REMARK 3 T11: 0.4822 T22: 0.5723
REMARK 3 T33: 0.6159 T12: 0.0491
REMARK 3 T13: 0.0955 T23: 0.0909
REMARK 3 L TENSOR
REMARK 3 L11: 3.8777 L22: 2.8249
REMARK 3 L33: 8.5952 L12: 2.2029
REMARK 3 L13: 3.8582 L23: 3.8015
REMARK 3 S TENSOR
REMARK 3 S11: -0.2532 S12: 0.0565 S13: 0.3752
REMARK 3 S21: -0.0647 S22: -0.1398 S23: 0.0175
REMARK 3 S31: -1.0619 S32: -0.4175 S33: 0.2949
REMARK 3 TLS GROUP : 36
REMARK 3 SELECTION: CHAIN 'G' AND (RESID 204 THROUGH 233 )
REMARK 3 ORIGIN FOR THE GROUP (A): -42.8669 152.2604 84.0433
REMARK 3 T TENSOR
REMARK 3 T11: 0.5711 T22: 0.6479
REMARK 3 T33: 0.6213 T12: 0.0289
REMARK 3 T13: 0.0837 T23: 0.0395
REMARK 3 L TENSOR
REMARK 3 L11: 2.5831 L22: 3.9802
REMARK 3 L33: 9.8266 L12: 0.5222
REMARK 3 L13: -1.7436 L23: 2.9742
REMARK 3 S TENSOR
REMARK 3 S11: 0.0788 S12: 0.4265 S13: 0.3578
REMARK 3 S21: -0.1991 S22: -0.1682 S23: 0.1428
REMARK 3 S31: -0.5757 S32: -0.0866 S33: 0.0664
REMARK 3 TLS GROUP : 37
REMARK 3 SELECTION: CHAIN 'G' AND (RESID 234 THROUGH 301 )
REMARK 3 ORIGIN FOR THE GROUP (A): -41.2696 139.5634 85.9017
REMARK 3 T TENSOR
REMARK 3 T11: 0.3926 T22: 0.4552
REMARK 3 T33: 0.4660 T12: 0.0191
REMARK 3 T13: 0.0683 T23: 0.0216
REMARK 3 L TENSOR
REMARK 3 L11: 1.9642 L22: 2.1633
REMARK 3 L33: 7.8148 L12: -0.9746
REMARK 3 L13: -2.7962 L23: 2.1072
REMARK 3 S TENSOR
REMARK 3 S11: -0.2362 S12: 0.1972 S13: -0.2360
REMARK 3 S21: 0.1735 S22: 0.2046 S23: 0.0424
REMARK 3 S31: 0.2732 S32: 0.2234 S33: 0.0095
REMARK 3 TLS GROUP : 38
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 137 THROUGH 152 )
REMARK 3 ORIGIN FOR THE GROUP (A): -39.3960 117.1454 32.4988
REMARK 3 T TENSOR
REMARK 3 T11: 0.6295 T22: 0.8472
REMARK 3 T33: 0.6946 T12: 0.1125
REMARK 3 T13: 0.0140 T23: 0.0243
REMARK 3 L TENSOR
REMARK 3 L11: 0.5257 L22: 2.0085
REMARK 3 L33: 1.5513 L12: -0.1588
REMARK 3 L13: 0.9649 L23: -0.8013
REMARK 3 S TENSOR
REMARK 3 S11: 0.2406 S12: -0.3646 S13: 1.2317
REMARK 3 S21: 0.5183 S22: -0.4587 S23: 1.2080
REMARK 3 S31: -0.2130 S32: -0.9390 S33: 0.0199
REMARK 3 TLS GROUP : 39
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 153 THROUGH 183 )
REMARK 3 ORIGIN FOR THE GROUP (A): -36.5266 111.6231 26.4905
REMARK 3 T TENSOR
REMARK 3 T11: 0.4735 T22: 0.4551
REMARK 3 T33: 0.4686 T12: -0.0366
REMARK 3 T13: -0.0061 T23: -0.0268
REMARK 3 L TENSOR
REMARK 3 L11: 4.1657 L22: 2.2907
REMARK 3 L33: 4.3108 L12: 0.8579
REMARK 3 L13: 1.7407 L23: 0.3378
REMARK 3 S TENSOR
REMARK 3 S11: 0.0860 S12: -0.6943 S13: 0.4719
REMARK 3 S21: 0.2982 S22: 0.0844 S23: 0.3199
REMARK 3 S31: 0.1850 S32: -0.5258 S33: -0.1464
REMARK 3 TLS GROUP : 40
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 184 THROUGH 200 )
REMARK 3 ORIGIN FOR THE GROUP (A): -37.6626 99.9358 19.3806
REMARK 3 T TENSOR
REMARK 3 T11: 0.5471 T22: 0.6409
REMARK 3 T33: 0.6422 T12: 0.0037
REMARK 3 T13: -0.1041 T23: 0.2059
REMARK 3 L TENSOR
REMARK 3 L11: 3.1135 L22: 5.8446
REMARK 3 L33: 6.7797 L12: -0.0719
REMARK 3 L13: -2.4359 L23: 3.1373
REMARK 3 S TENSOR
REMARK 3 S11: 0.1829 S12: -0.3582 S13: -0.0767
REMARK 3 S21: -0.0723 S22: -0.1936 S23: -0.5248
REMARK 3 S31: 0.7136 S32: -0.2444 S33: 0.1474
REMARK 3 TLS GROUP : 41
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 201 THROUGH 217 )
REMARK 3 ORIGIN FOR THE GROUP (A): -43.7620 94.7553 8.4069
REMARK 3 T TENSOR
REMARK 3 T11: 0.9369 T22: 0.5780
REMARK 3 T33: 0.8565 T12: -0.0044
REMARK 3 T13: -0.1311 T23: 0.1132
REMARK 3 L TENSOR
REMARK 3 L11: 8.9993 L22: 4.9864
REMARK 3 L33: 3.1939 L12: 2.3576
REMARK 3 L13: -0.9526 L23: 0.9140
REMARK 3 S TENSOR
REMARK 3 S11: -0.3607 S12: -0.5119 S13: -1.7041
REMARK 3 S21: 0.0671 S22: 0.5238 S23: 0.0537
REMARK 3 S31: 2.2355 S32: 1.2525 S33: -0.0713
REMARK 3 TLS GROUP : 42
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 218 THROUGH 259 )
REMARK 3 ORIGIN FOR THE GROUP (A): -41.8073 107.0299 12.6197
REMARK 3 T TENSOR
REMARK 3 T11: 0.4304 T22: 0.4372
REMARK 3 T33: 0.4779 T12: -0.0688
REMARK 3 T13: -0.0414 T23: 0.0488
REMARK 3 L TENSOR
REMARK 3 L11: 4.1614 L22: 2.2238
REMARK 3 L33: 7.9916 L12: 0.1259
REMARK 3 L13: 1.7830 L23: 1.0179
REMARK 3 S TENSOR
REMARK 3 S11: 0.2747 S12: -0.5045 S13: 0.0318
REMARK 3 S21: 0.0390 S22: -0.0221 S23: 0.1646
REMARK 3 S31: 0.6033 S32: -0.4965 S33: -0.2166
REMARK 3 TLS GROUP : 43
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 260 THROUGH 301 )
REMARK 3 ORIGIN FOR THE GROUP (A): -35.8277 116.4201 8.7386
REMARK 3 T TENSOR
REMARK 3 T11: 0.4101 T22: 0.3415
REMARK 3 T33: 0.5214 T12: -0.0123
REMARK 3 T13: -0.0445 T23: 0.0596
REMARK 3 L TENSOR
REMARK 3 L11: 2.7191 L22: 2.7626
REMARK 3 L33: 8.3762 L12: 1.2408
REMARK 3 L13: 1.8654 L23: 2.0516
REMARK 3 S TENSOR
REMARK 3 S11: -0.1834 S12: 0.0646 S13: 0.3431
REMARK 3 S21: -0.2615 S22: 0.1660 S23: 0.0392
REMARK 3 S31: -0.1855 S32: 0.0783 S33: 0.0507
REMARK 3 TLS GROUP : 44
REMARK 3 SELECTION: CHAIN 'I' AND (RESID 138 THROUGH 152 )
REMARK 3 ORIGIN FOR THE GROUP (A): 12.3726 139.6464 11.4655
REMARK 3 T TENSOR
REMARK 3 T11: 0.7029 T22: 1.0858
REMARK 3 T33: 1.0129 T12: 0.1210
REMARK 3 T13: 0.2541 T23: -0.0301
REMARK 3 L TENSOR
REMARK 3 L11: 5.3636 L22: 4.7769
REMARK 3 L33: 7.2234 L12: -2.8681
REMARK 3 L13: 0.2126 L23: -1.2341
REMARK 3 S TENSOR
REMARK 3 S11: -0.1736 S12: 0.1648 S13: -0.5377
REMARK 3 S21: -0.7495 S22: -0.2581 S23: -1.6600
REMARK 3 S31: 0.9412 S32: 1.3035 S33: 0.2140
REMARK 3 TLS GROUP : 45
REMARK 3 SELECTION: CHAIN 'I' AND (RESID 153 THROUGH 188 )
REMARK 3 ORIGIN FOR THE GROUP (A): 4.0013 139.8679 10.7802
REMARK 3 T TENSOR
REMARK 3 T11: 0.6548 T22: 0.7567
REMARK 3 T33: 0.7988 T12: 0.0350
REMARK 3 T13: 0.2304 T23: -0.0204
REMARK 3 L TENSOR
REMARK 3 L11: 3.7222 L22: 2.6346
REMARK 3 L33: 4.2600 L12: 0.7598
REMARK 3 L13: 0.3257 L23: 1.2321
REMARK 3 S TENSOR
REMARK 3 S11: -0.1935 S12: 0.3790 S13: -0.7880
REMARK 3 S21: -0.1655 S22: -0.0549 S23: -0.8260
REMARK 3 S31: 0.6255 S32: 0.8162 S33: 0.2229
REMARK 3 TLS GROUP : 46
REMARK 3 SELECTION: CHAIN 'I' AND (RESID 189 THROUGH 217 )
REMARK 3 ORIGIN FOR THE GROUP (A): -17.0081 137.7565 14.7762
REMARK 3 T TENSOR
REMARK 3 T11: 0.9021 T22: 0.6565
REMARK 3 T33: 0.5321 T12: -0.0371
REMARK 3 T13: 0.0898 T23: -0.0166
REMARK 3 L TENSOR
REMARK 3 L11: 6.2619 L22: 5.0727
REMARK 3 L33: 6.7202 L12: 3.8027
REMARK 3 L13: -2.5787 L23: -1.2995
REMARK 3 S TENSOR
REMARK 3 S11: -0.3422 S12: 1.0053 S13: 0.0426
REMARK 3 S21: -1.0928 S22: 0.3133 S23: 0.1819
REMARK 3 S31: 0.2828 S32: -1.0159 S33: 0.0098
REMARK 3 TLS GROUP : 47
REMARK 3 SELECTION: CHAIN 'I' AND (RESID 218 THROUGH 278 )
REMARK 3 ORIGIN FOR THE GROUP (A): -8.9144 145.3401 21.3654
REMARK 3 T TENSOR
REMARK 3 T11: 0.5204 T22: 0.3176
REMARK 3 T33: 0.4326 T12: 0.0018
REMARK 3 T13: 0.0668 T23: -0.0239
REMARK 3 L TENSOR
REMARK 3 L11: 5.9171 L22: 2.1314
REMARK 3 L33: 5.3897 L12: 2.2070
REMARK 3 L13: -0.3903 L23: -1.2369
REMARK 3 S TENSOR
REMARK 3 S11: -0.1041 S12: 0.1272 S13: -0.0933
REMARK 3 S21: -0.0638 S22: 0.1022 S23: 0.0797
REMARK 3 S31: 0.2975 S32: 0.1545 S33: -0.0029
REMARK 3 TLS GROUP : 48
REMARK 3 SELECTION: CHAIN 'I' AND (RESID 279 THROUGH 302 )
REMARK 3 ORIGIN FOR THE GROUP (A): -0.1273 149.1460 22.4697
REMARK 3 T TENSOR
REMARK 3 T11: 0.4575 T22: 0.5313
REMARK 3 T33: 0.4523 T12: -0.0374
REMARK 3 T13: -0.0141 T23: 0.0611
REMARK 3 L TENSOR
REMARK 3 L11: 2.8265 L22: 5.5819
REMARK 3 L33: 5.9639 L12: -0.7805
REMARK 3 L13: -2.2257 L23: 1.3820
REMARK 3 S TENSOR
REMARK 3 S11: -0.6257 S12: -0.4071 S13: -0.0266
REMARK 3 S21: 0.0161 S22: 0.2220 S23: -0.3590
REMARK 3 S31: 0.4284 S32: 0.6227 S33: 0.3187
REMARK 3 TLS GROUP : 49
REMARK 3 SELECTION: CHAIN 'J' AND (RESID 138 THROUGH 152 )
REMARK 3 ORIGIN FOR THE GROUP (A): 9.9601 116.8817 87.5288
REMARK 3 T TENSOR
REMARK 3 T11: 0.7502 T22: 0.9015
REMARK 3 T33: 0.9373 T12: -0.1608
REMARK 3 T13: -0.2656 T23: 0.1211
REMARK 3 L TENSOR
REMARK 3 L11: 6.9391 L22: 7.5976
REMARK 3 L33: 8.8239 L12: 4.9059
REMARK 3 L13: 2.2945 L23: -3.2928
REMARK 3 S TENSOR
REMARK 3 S11: -0.2784 S12: 0.2145 S13: 1.0870
REMARK 3 S21: 0.3567 S22: -0.3390 S23: -1.4469
REMARK 3 S31: -0.3047 S32: 1.0426 S33: 0.6543
REMARK 3 TLS GROUP : 50
REMARK 3 SELECTION: CHAIN 'J' AND (RESID 153 THROUGH 200 )
REMARK 3 ORIGIN FOR THE GROUP (A): -2.9594 114.4967 87.9910
REMARK 3 T TENSOR
REMARK 3 T11: 0.7066 T22: 0.5514
REMARK 3 T33: 0.5754 T12: 0.0620
REMARK 3 T13: -0.0884 T23: -0.1040
REMARK 3 L TENSOR
REMARK 3 L11: 4.8420 L22: 1.0263
REMARK 3 L33: 3.8509 L12: -2.4728
REMARK 3 L13: 1.5682 L23: -1.2839
REMARK 3 S TENSOR
REMARK 3 S11: -0.4617 S12: -0.0733 S13: 0.4660
REMARK 3 S21: 0.4201 S22: 0.2036 S23: -0.4552
REMARK 3 S31: -0.4336 S32: 0.2179 S33: 0.2816
REMARK 3 TLS GROUP : 51
REMARK 3 SELECTION: CHAIN 'J' AND (RESID 201 THROUGH 300 )
REMARK 3 ORIGIN FOR THE GROUP (A): -9.7489 110.2998 76.3393
REMARK 3 T TENSOR
REMARK 3 T11: 0.4614 T22: 0.4167
REMARK 3 T33: 0.3914 T12: 0.0214
REMARK 3 T13: -0.0520 T23: -0.0267
REMARK 3 L TENSOR
REMARK 3 L11: 3.7443 L22: 4.1254
REMARK 3 L33: 1.9920 L12: -1.5909
REMARK 3 L13: -0.0286 L23: -0.2789
REMARK 3 S TENSOR
REMARK 3 S11: -0.2436 S12: -0.1891 S13: 0.0978
REMARK 3 S21: 0.2173 S22: 0.3212 S23: -0.1330
REMARK 3 S31: 0.0746 S32: 0.0936 S33: -0.0797
REMARK 3 TLS GROUP : 52
REMARK 3 SELECTION: CHAIN 'L' AND (RESID 139 THROUGH 169 )
REMARK 3 ORIGIN FOR THE GROUP (A): 7.5654 106.5549 103.0031
REMARK 3 T TENSOR
REMARK 3 T11: 0.9557 T22: 0.9790
REMARK 3 T33: 0.8762 T12: -0.1159
REMARK 3 T13: -0.3928 T23: -0.0536
REMARK 3 L TENSOR
REMARK 3 L11: 5.4871 L22: 2.2283
REMARK 3 L33: 7.9421 L12: -1.9836
REMARK 3 L13: -0.3206 L23: 0.3017
REMARK 3 S TENSOR
REMARK 3 S11: 0.3032 S12: 0.6409 S13: -0.5223
REMARK 3 S21: 0.3189 S22: 0.3723 S23: -0.0445
REMARK 3 S31: 2.0535 S32: -0.1375 S33: -0.5881
REMARK 3 TLS GROUP : 53
REMARK 3 SELECTION: CHAIN 'L' AND (RESID 170 THROUGH 218 )
REMARK 3 ORIGIN FOR THE GROUP (A): 12.3589 122.1217 110.7126
REMARK 3 T TENSOR
REMARK 3 T11: 0.9497 T22: 1.0458
REMARK 3 T33: 0.8564 T12: -0.0377
REMARK 3 T13: -0.2926 T23: -0.0340
REMARK 3 L TENSOR
REMARK 3 L11: 2.0827 L22: 0.7865
REMARK 3 L33: 5.5020 L12: -0.9452
REMARK 3 L13: 0.5602 L23: 0.2923
REMARK 3 S TENSOR
REMARK 3 S11: 0.0444 S12: -0.0863 S13: 0.4281
REMARK 3 S21: 0.0945 S22: -0.3466 S23: 0.0115
REMARK 3 S31: -0.7559 S32: 0.2171 S33: 0.3060
REMARK 3 TLS GROUP : 54
REMARK 3 SELECTION: CHAIN 'L' AND (RESID 219 THROUGH 301 )
REMARK 3 ORIGIN FOR THE GROUP (A): 21.7222 111.4447 111.2415
REMARK 3 T TENSOR
REMARK 3 T11: 0.7784 T22: 0.9082
REMARK 3 T33: 0.7457 T12: -0.0136
REMARK 3 T13: -0.2912 T23: -0.0789
REMARK 3 L TENSOR
REMARK 3 L11: 4.5485 L22: 2.6270
REMARK 3 L33: 8.2137 L12: 0.0486
REMARK 3 L13: 4.7589 L23: 0.8912
REMARK 3 S TENSOR
REMARK 3 S11: 0.0620 S12: 0.8720 S13: -0.3275
REMARK 3 S21: -0.0001 S22: 0.0706 S23: -0.2622
REMARK 3 S31: 0.5244 S32: 0.7548 S33: -0.0629
REMARK 3 TLS GROUP : 55
REMARK 3 SELECTION: CHAIN 'K' AND (RESID 137 THROUGH 209 )
REMARK 3 ORIGIN FOR THE GROUP (A): 11.7615 139.6348 -7.3200
REMARK 3 T TENSOR
REMARK 3 T11: 0.8683 T22: 1.0712
REMARK 3 T33: 0.7889 T12: -0.0419
REMARK 3 T13: 0.1963 T23: -0.0442
REMARK 3 L TENSOR
REMARK 3 L11: 2.1526 L22: 3.2000
REMARK 3 L33: 4.6356 L12: -2.2709
REMARK 3 L13: -2.9537 L23: 3.3775
REMARK 3 S TENSOR
REMARK 3 S11: 0.0090 S12: -0.2478 S13: -0.1264
REMARK 3 S21: 0.0586 S22: -0.1614 S23: 0.0305
REMARK 3 S31: -0.1460 S32: 0.0939 S33: 0.1401
REMARK 3 TLS GROUP : 56
REMARK 3 SELECTION: CHAIN 'K' AND (RESID 210 THROUGH 300 )
REMARK 3 ORIGIN FOR THE GROUP (A): 22.0965 141.4394 -14.6668
REMARK 3 T TENSOR
REMARK 3 T11: 0.6123 T22: 0.7765
REMARK 3 T33: 0.5983 T12: -0.0935
REMARK 3 T13: 0.1485 T23: -0.0611
REMARK 3 L TENSOR
REMARK 3 L11: 4.6851 L22: 4.0802
REMARK 3 L33: 8.1123 L12: -1.5338
REMARK 3 L13: -2.6430 L23: 3.5094
REMARK 3 S TENSOR
REMARK 3 S11: 0.0373 S12: -0.8942 S13: 0.0283
REMARK 3 S21: 0.2878 S22: -0.1088 S23: 0.1084
REMARK 3 S31: 0.1517 S32: -0.0598 S33: 0.0463
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 5HE8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-JAN-16.
REMARK 100 THE DEPOSITION ID IS D_1000216448.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-FEB-15
REMARK 200 TEMPERATURE (KELVIN) : 80
REMARK 200 PH : 4.0
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X25
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 81324
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 48.130
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 13.20
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 3.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> 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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.85
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.92
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% GLYCEROL, 0.1 M CITRIC ACID PH
REMARK 280 4.0, 0.8 M AMMONIUM SULFATE, 50 MM HEPES-KOH PH 7.5, 10 MM MGCL2,
REMARK 280 10% GLYCEROL, 2 MM ADP-BEF3, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 294.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 56.54950
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 91.67200
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 63.13050
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 91.67200
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 56.54950
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 63.13050
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, 3, 4, 5, 6
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: 2630 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16070 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -98.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, F
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2150 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16100 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -62.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, E
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3310 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16670 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -107.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, H
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2490 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16730 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -67.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, G
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: 5
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: 2350 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16410 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -75.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: I, K
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: 6
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: 2150 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16080 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -71.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: J, L
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 A 133
REMARK 465 ASN A 134
REMARK 465 ALA A 135
REMARK 465 ASP A 136
REMARK 465 ARG A 137
REMARK 465 GLU A 301
REMARK 465 ASN A 302
REMARK 465 PHE A 303
REMARK 465 ARG A 304
REMARK 465 ASN A 305
REMARK 465 ASN A 306
REMARK 465 SER B 133
REMARK 465 ASN B 134
REMARK 465 ALA B 135
REMARK 465 ASP B 136
REMARK 465 ARG B 137
REMARK 465 ASN B 302
REMARK 465 PHE B 303
REMARK 465 ARG B 304
REMARK 465 ASN B 305
REMARK 465 ASN B 306
REMARK 465 SER C 133
REMARK 465 ASN C 134
REMARK 465 ALA C 135
REMARK 465 SER D 133
REMARK 465 ASN D 134
REMARK 465 ASN D 305
REMARK 465 ASN D 306
REMARK 465 SER E 133
REMARK 465 ASN E 134
REMARK 465 ALA E 135
REMARK 465 ASP E 136
REMARK 465 ARG E 137
REMARK 465 PHE E 303
REMARK 465 ARG E 304
REMARK 465 ASN E 305
REMARK 465 ASN E 306
REMARK 465 SER F 133
REMARK 465 ASN F 134
REMARK 465 ALA F 135
REMARK 465 ASP F 136
REMARK 465 ARG F 137
REMARK 465 ASN F 302
REMARK 465 PHE F 303
REMARK 465 ARG F 304
REMARK 465 ASN F 305
REMARK 465 ASN F 306
REMARK 465 SER G 133
REMARK 465 ASN G 134
REMARK 465 ALA G 135
REMARK 465 ASP G 136
REMARK 465 ASN G 302
REMARK 465 PHE G 303
REMARK 465 ARG G 304
REMARK 465 ASN G 305
REMARK 465 ASN G 306
REMARK 465 SER H 133
REMARK 465 ASN H 134
REMARK 465 ALA H 135
REMARK 465 ASP H 136
REMARK 465 ASN H 302
REMARK 465 PHE H 303
REMARK 465 ARG H 304
REMARK 465 ASN H 305
REMARK 465 ASN H 306
REMARK 465 SER I 133
REMARK 465 ASN I 134
REMARK 465 ALA I 135
REMARK 465 ASP I 136
REMARK 465 ARG I 137
REMARK 465 PHE I 303
REMARK 465 ARG I 304
REMARK 465 ASN I 305
REMARK 465 ASN I 306
REMARK 465 SER J 133
REMARK 465 ASN J 134
REMARK 465 ALA J 135
REMARK 465 ASP J 136
REMARK 465 ARG J 137
REMARK 465 GLU J 301
REMARK 465 ASN J 302
REMARK 465 PHE J 303
REMARK 465 ARG J 304
REMARK 465 ASN J 305
REMARK 465 ASN J 306
REMARK 465 SER L 133
REMARK 465 ASN L 134
REMARK 465 ALA L 135
REMARK 465 ASP L 136
REMARK 465 ARG L 137
REMARK 465 LEU L 138
REMARK 465 ASN L 302
REMARK 465 PHE L 303
REMARK 465 ARG L 304
REMARK 465 ASN L 305
REMARK 465 ASN L 306
REMARK 465 SER K 133
REMARK 465 ASN K 134
REMARK 465 ALA K 135
REMARK 465 ASP K 136
REMARK 465 GLU K 301
REMARK 465 ASN K 302
REMARK 465 PHE K 303
REMARK 465 ARG K 304
REMARK 465 ASN K 305
REMARK 465 ASN K 306
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 O HOH F 507 O HOH F 510 0.27
REMARK 500 O HOH B 506 O HOH B 507 0.47
REMARK 500 O HOH G 511 O HOH G 514 0.59
REMARK 500 O HOH G 507 O HOH G 519 0.90
REMARK 500 ND2 ASN C 302 HA ARG H 137 0.90
REMARK 500 CG ASN C 302 HA ARG H 137 1.01
REMARK 500 HG2 LYS A 281 HH21 ARG A 284 1.13
REMARK 500 HG2 LYS A 281 NH2 ARG A 284 1.14
REMARK 500 HG2 LYS A 281 HH22 ARG A 284 1.15
REMARK 500 O LEU H 138 HH TYR H 296 1.20
REMARK 500 HE1 PHE F 204 CD1 TRP F 235 1.55
REMARK 500 OD1 ASP C 146 HH11 ARG E 215 1.58
REMARK 500 ND2 ASN C 302 CB ARG H 137 1.65
REMARK 500 O HOH B 501 O HOH B 502 1.70
REMARK 500 CE1 PHE F 204 CD1 TRP F 235 1.85
REMARK 500 CG ASN C 302 CA ARG H 137 1.92
REMARK 500 CE1 PHE F 204 CG TRP F 235 1.93
REMARK 500 O LEU H 138 OH TYR H 296 2.04
REMARK 500 CG LYS A 281 NH2 ARG A 284 2.04
REMARK 500 O2 SO4 C 404 O HOH C 501 2.07
REMARK 500 O SER C 299 N GLU C 301 2.08
REMARK 500 CZ PHE F 204 CG TRP F 235 2.10
REMARK 500 O HOH H 512 O HOH H 519 2.10
REMARK 500 CD1 ILE L 197 OE1 GLU L 230 2.16
REMARK 500 O HOH K 501 O HOH K 508 2.17
REMARK 500 O LEU F 200 N GLY F 202 2.17
REMARK 500 O PHE F 196 OG1 THR F 199 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 NZ LYS A 185 OE2 GLU B 155 3555 2.19
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 VAL A 240 -66.54 -128.36
REMARK 500 GLU A 252 72.89 48.49
REMARK 500 VAL B 240 -64.99 -132.36
REMARK 500 SER B 299 142.62 177.55
REMARK 500 LEU C 138 41.32 -101.88
REMARK 500 VAL C 240 -62.16 -123.66
REMARK 500 GLU C 301 -83.70 -55.25
REMARK 500 ASN C 302 99.42 47.86
REMARK 500 PHE C 303 -1.63 -145.56
REMARK 500 ARG C 304 61.41 33.12
REMARK 500 VAL D 240 -67.42 -124.04
REMARK 500 ASN D 302 -154.66 -141.86
REMARK 500 ASP E 226 37.94 71.19
REMARK 500 GLU E 231 100.73 87.32
REMARK 500 VAL E 240 -68.05 -120.14
REMARK 500 SER E 299 -167.50 -78.95
REMARK 500 PRO F 165 171.57 -58.56
REMARK 500 LYS F 201 71.98 -48.76
REMARK 500 PHE F 204 7.57 -65.80
REMARK 500 LYS F 205 -82.95 -113.65
REMARK 500 ASP F 226 39.07 70.28
REMARK 500 VAL F 240 -73.61 -127.85
REMARK 500 ASP G 226 48.60 73.93
REMARK 500 VAL G 240 -69.71 -127.43
REMARK 500 ASP H 226 37.90 71.65
REMARK 500 VAL H 240 -71.44 -132.43
REMARK 500 TYR I 161 75.84 -114.33
REMARK 500 VAL I 240 -69.69 -125.89
REMARK 500 ASP J 139 110.38 59.17
REMARK 500 VAL J 240 -73.21 -124.14
REMARK 500 ASN L 220 -48.43 90.21
REMARK 500 VAL L 232 111.74 86.05
REMARK 500 VAL L 240 -49.95 -136.30
REMARK 500 LYS L 279 57.34 -69.69
REMARK 500 THR L 280 -61.24 -145.52
REMARK 500 GLU K 155 106.64 -59.12
REMARK 500 TYR K 161 79.84 -108.95
REMARK 500 ASP K 206 -4.18 92.51
REMARK 500 VAL K 240 -50.28 -141.66
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 D 518 DISTANCE = 8.58 ANGSTROMS
REMARK 525 HOH D 519 DISTANCE = 9.77 ANGSTROMS
REMARK 525 HOH F 526 DISTANCE = 7.53 ANGSTROMS
REMARK 525 HOH G 523 DISTANCE = 6.86 ANGSTROMS
REMARK 525 HOH G 524 DISTANCE = 11.03 ANGSTROMS
REMARK 525 HOH H 522 DISTANCE = 11.51 ANGSTROMS
REMARK 525 HOH J 518 DISTANCE = 5.90 ANGSTROMS
REMARK 525 HOH J 519 DISTANCE = 6.11 ANGSTROMS
REMARK 525 HOH L 503 DISTANCE = 7.21 ANGSTROMS
REMARK 525 HOH L 504 DISTANCE = 7.62 ANGSTROMS
REMARK 525 HOH L 505 DISTANCE = 13.56 ANGSTROMS
REMARK 525 HOH K 510 DISTANCE = 8.31 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 E 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 E 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 F 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 F 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 G 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 G 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 H 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 H 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 H 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 H 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 I 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 I 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 J 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 J 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 L 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 L 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 K 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 K 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide ARG H 137 and ASN C
REMARK 800 302
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5HE9 RELATED DB: PDB
DBREF 5HE8 A 136 306 UNP W8TSU2 W8TSU2_STAAU 136 306
DBREF 5HE8 B 136 306 UNP W8TSU2 W8TSU2_STAAU 136 306
DBREF 5HE8 C 136 306 UNP W8TSU2 W8TSU2_STAAU 136 306
DBREF 5HE8 D 136 306 UNP W8TSU2 W8TSU2_STAAU 136 306
DBREF 5HE8 E 136 306 UNP W8TSU2 W8TSU2_STAAU 136 306
DBREF 5HE8 F 136 306 UNP W8TSU2 W8TSU2_STAAU 136 306
DBREF 5HE8 G 136 306 UNP W8TSU2 W8TSU2_STAAU 136 306
DBREF 5HE8 H 136 306 UNP W8TSU2 W8TSU2_STAAU 136 306
DBREF 5HE8 I 136 306 UNP W8TSU2 W8TSU2_STAAU 136 306
DBREF 5HE8 J 136 306 UNP W8TSU2 W8TSU2_STAAU 136 306
DBREF 5HE8 L 136 306 UNP W8TSU2 W8TSU2_STAAU 136 306
DBREF 5HE8 K 136 306 UNP W8TSU2 W8TSU2_STAAU 136 306
SEQADV 5HE8 SER A 133 UNP W8TSU2 EXPRESSION TAG
SEQADV 5HE8 ASN A 134 UNP W8TSU2 EXPRESSION TAG
SEQADV 5HE8 ALA A 135 UNP W8TSU2 EXPRESSION TAG
SEQADV 5HE8 SER B 133 UNP W8TSU2 EXPRESSION TAG
SEQADV 5HE8 ASN B 134 UNP W8TSU2 EXPRESSION TAG
SEQADV 5HE8 ALA B 135 UNP W8TSU2 EXPRESSION TAG
SEQADV 5HE8 SER C 133 UNP W8TSU2 EXPRESSION TAG
SEQADV 5HE8 ASN C 134 UNP W8TSU2 EXPRESSION TAG
SEQADV 5HE8 ALA C 135 UNP W8TSU2 EXPRESSION TAG
SEQADV 5HE8 SER D 133 UNP W8TSU2 EXPRESSION TAG
SEQADV 5HE8 ASN D 134 UNP W8TSU2 EXPRESSION TAG
SEQADV 5HE8 ALA D 135 UNP W8TSU2 EXPRESSION TAG
SEQADV 5HE8 SER E 133 UNP W8TSU2 EXPRESSION TAG
SEQADV 5HE8 ASN E 134 UNP W8TSU2 EXPRESSION TAG
SEQADV 5HE8 ALA E 135 UNP W8TSU2 EXPRESSION TAG
SEQADV 5HE8 SER F 133 UNP W8TSU2 EXPRESSION TAG
SEQADV 5HE8 ASN F 134 UNP W8TSU2 EXPRESSION TAG
SEQADV 5HE8 ALA F 135 UNP W8TSU2 EXPRESSION TAG
SEQADV 5HE8 SER G 133 UNP W8TSU2 EXPRESSION TAG
SEQADV 5HE8 ASN G 134 UNP W8TSU2 EXPRESSION TAG
SEQADV 5HE8 ALA G 135 UNP W8TSU2 EXPRESSION TAG
SEQADV 5HE8 SER H 133 UNP W8TSU2 EXPRESSION TAG
SEQADV 5HE8 ASN H 134 UNP W8TSU2 EXPRESSION TAG
SEQADV 5HE8 ALA H 135 UNP W8TSU2 EXPRESSION TAG
SEQADV 5HE8 SER I 133 UNP W8TSU2 EXPRESSION TAG
SEQADV 5HE8 ASN I 134 UNP W8TSU2 EXPRESSION TAG
SEQADV 5HE8 ALA I 135 UNP W8TSU2 EXPRESSION TAG
SEQADV 5HE8 SER J 133 UNP W8TSU2 EXPRESSION TAG
SEQADV 5HE8 ASN J 134 UNP W8TSU2 EXPRESSION TAG
SEQADV 5HE8 ALA J 135 UNP W8TSU2 EXPRESSION TAG
SEQADV 5HE8 SER L 133 UNP W8TSU2 EXPRESSION TAG
SEQADV 5HE8 ASN L 134 UNP W8TSU2 EXPRESSION TAG
SEQADV 5HE8 ALA L 135 UNP W8TSU2 EXPRESSION TAG
SEQADV 5HE8 SER K 133 UNP W8TSU2 EXPRESSION TAG
SEQADV 5HE8 ASN K 134 UNP W8TSU2 EXPRESSION TAG
SEQADV 5HE8 ALA K 135 UNP W8TSU2 EXPRESSION TAG
SEQRES 1 A 174 SER ASN ALA ASP ARG LEU ASP VAL ALA MET ALA ALA ASP
SEQRES 2 A 174 ASP ILE CYS THR ALA ILE THR ASN GLY GLU GLN VAL LYS
SEQRES 3 A 174 GLY LEU TYR LEU TYR GLY PRO PHE GLY THR GLY LYS SER
SEQRES 4 A 174 PHE ILE LEU GLY ALA ILE ALA ASN GLN LEU LYS SER LYS
SEQRES 5 A 174 LYS VAL ARG SER THR ILE ILE TYR LEU PRO GLU PHE ILE
SEQRES 6 A 174 ARG THR LEU LYS GLY GLY PHE LYS ASP GLY SER PHE GLU
SEQRES 7 A 174 LYS LYS LEU HIS ARG VAL ARG GLU ALA ASN ILE LEU MET
SEQRES 8 A 174 LEU ASP ASP ILE GLY ALA GLU GLU VAL THR PRO TRP VAL
SEQRES 9 A 174 ARG ASP GLU VAL ILE GLY PRO LEU LEU HIS TYR ARG MET
SEQRES 10 A 174 VAL HIS GLU LEU PRO THR PHE PHE SER SER ASN PHE ASP
SEQRES 11 A 174 TYR SER GLU LEU GLU HIS HIS LEU ALA MET THR ARG ASP
SEQRES 12 A 174 GLY GLU GLU LYS THR LYS ALA ALA ARG ILE ILE GLU ARG
SEQRES 13 A 174 VAL LYS SER LEU SER THR PRO TYR PHE LEU SER GLY GLU
SEQRES 14 A 174 ASN PHE ARG ASN ASN
SEQRES 1 B 174 SER ASN ALA ASP ARG LEU ASP VAL ALA MET ALA ALA ASP
SEQRES 2 B 174 ASP ILE CYS THR ALA ILE THR ASN GLY GLU GLN VAL LYS
SEQRES 3 B 174 GLY LEU TYR LEU TYR GLY PRO PHE GLY THR GLY LYS SER
SEQRES 4 B 174 PHE ILE LEU GLY ALA ILE ALA ASN GLN LEU LYS SER LYS
SEQRES 5 B 174 LYS VAL ARG SER THR ILE ILE TYR LEU PRO GLU PHE ILE
SEQRES 6 B 174 ARG THR LEU LYS GLY GLY PHE LYS ASP GLY SER PHE GLU
SEQRES 7 B 174 LYS LYS LEU HIS ARG VAL ARG GLU ALA ASN ILE LEU MET
SEQRES 8 B 174 LEU ASP ASP ILE GLY ALA GLU GLU VAL THR PRO TRP VAL
SEQRES 9 B 174 ARG ASP GLU VAL ILE GLY PRO LEU LEU HIS TYR ARG MET
SEQRES 10 B 174 VAL HIS GLU LEU PRO THR PHE PHE SER SER ASN PHE ASP
SEQRES 11 B 174 TYR SER GLU LEU GLU HIS HIS LEU ALA MET THR ARG ASP
SEQRES 12 B 174 GLY GLU GLU LYS THR LYS ALA ALA ARG ILE ILE GLU ARG
SEQRES 13 B 174 VAL LYS SER LEU SER THR PRO TYR PHE LEU SER GLY GLU
SEQRES 14 B 174 ASN PHE ARG ASN ASN
SEQRES 1 C 174 SER ASN ALA ASP ARG LEU ASP VAL ALA MET ALA ALA ASP
SEQRES 2 C 174 ASP ILE CYS THR ALA ILE THR ASN GLY GLU GLN VAL LYS
SEQRES 3 C 174 GLY LEU TYR LEU TYR GLY PRO PHE GLY THR GLY LYS SER
SEQRES 4 C 174 PHE ILE LEU GLY ALA ILE ALA ASN GLN LEU LYS SER LYS
SEQRES 5 C 174 LYS VAL ARG SER THR ILE ILE TYR LEU PRO GLU PHE ILE
SEQRES 6 C 174 ARG THR LEU LYS GLY GLY PHE LYS ASP GLY SER PHE GLU
SEQRES 7 C 174 LYS LYS LEU HIS ARG VAL ARG GLU ALA ASN ILE LEU MET
SEQRES 8 C 174 LEU ASP ASP ILE GLY ALA GLU GLU VAL THR PRO TRP VAL
SEQRES 9 C 174 ARG ASP GLU VAL ILE GLY PRO LEU LEU HIS TYR ARG MET
SEQRES 10 C 174 VAL HIS GLU LEU PRO THR PHE PHE SER SER ASN PHE ASP
SEQRES 11 C 174 TYR SER GLU LEU GLU HIS HIS LEU ALA MET THR ARG ASP
SEQRES 12 C 174 GLY GLU GLU LYS THR LYS ALA ALA ARG ILE ILE GLU ARG
SEQRES 13 C 174 VAL LYS SER LEU SER THR PRO TYR PHE LEU SER GLY GLU
SEQRES 14 C 174 ASN PHE ARG ASN ASN
SEQRES 1 D 174 SER ASN ALA ASP ARG LEU ASP VAL ALA MET ALA ALA ASP
SEQRES 2 D 174 ASP ILE CYS THR ALA ILE THR ASN GLY GLU GLN VAL LYS
SEQRES 3 D 174 GLY LEU TYR LEU TYR GLY PRO PHE GLY THR GLY LYS SER
SEQRES 4 D 174 PHE ILE LEU GLY ALA ILE ALA ASN GLN LEU LYS SER LYS
SEQRES 5 D 174 LYS VAL ARG SER THR ILE ILE TYR LEU PRO GLU PHE ILE
SEQRES 6 D 174 ARG THR LEU LYS GLY GLY PHE LYS ASP GLY SER PHE GLU
SEQRES 7 D 174 LYS LYS LEU HIS ARG VAL ARG GLU ALA ASN ILE LEU MET
SEQRES 8 D 174 LEU ASP ASP ILE GLY ALA GLU GLU VAL THR PRO TRP VAL
SEQRES 9 D 174 ARG ASP GLU VAL ILE GLY PRO LEU LEU HIS TYR ARG MET
SEQRES 10 D 174 VAL HIS GLU LEU PRO THR PHE PHE SER SER ASN PHE ASP
SEQRES 11 D 174 TYR SER GLU LEU GLU HIS HIS LEU ALA MET THR ARG ASP
SEQRES 12 D 174 GLY GLU GLU LYS THR LYS ALA ALA ARG ILE ILE GLU ARG
SEQRES 13 D 174 VAL LYS SER LEU SER THR PRO TYR PHE LEU SER GLY GLU
SEQRES 14 D 174 ASN PHE ARG ASN ASN
SEQRES 1 E 174 SER ASN ALA ASP ARG LEU ASP VAL ALA MET ALA ALA ASP
SEQRES 2 E 174 ASP ILE CYS THR ALA ILE THR ASN GLY GLU GLN VAL LYS
SEQRES 3 E 174 GLY LEU TYR LEU TYR GLY PRO PHE GLY THR GLY LYS SER
SEQRES 4 E 174 PHE ILE LEU GLY ALA ILE ALA ASN GLN LEU LYS SER LYS
SEQRES 5 E 174 LYS VAL ARG SER THR ILE ILE TYR LEU PRO GLU PHE ILE
SEQRES 6 E 174 ARG THR LEU LYS GLY GLY PHE LYS ASP GLY SER PHE GLU
SEQRES 7 E 174 LYS LYS LEU HIS ARG VAL ARG GLU ALA ASN ILE LEU MET
SEQRES 8 E 174 LEU ASP ASP ILE GLY ALA GLU GLU VAL THR PRO TRP VAL
SEQRES 9 E 174 ARG ASP GLU VAL ILE GLY PRO LEU LEU HIS TYR ARG MET
SEQRES 10 E 174 VAL HIS GLU LEU PRO THR PHE PHE SER SER ASN PHE ASP
SEQRES 11 E 174 TYR SER GLU LEU GLU HIS HIS LEU ALA MET THR ARG ASP
SEQRES 12 E 174 GLY GLU GLU LYS THR LYS ALA ALA ARG ILE ILE GLU ARG
SEQRES 13 E 174 VAL LYS SER LEU SER THR PRO TYR PHE LEU SER GLY GLU
SEQRES 14 E 174 ASN PHE ARG ASN ASN
SEQRES 1 F 174 SER ASN ALA ASP ARG LEU ASP VAL ALA MET ALA ALA ASP
SEQRES 2 F 174 ASP ILE CYS THR ALA ILE THR ASN GLY GLU GLN VAL LYS
SEQRES 3 F 174 GLY LEU TYR LEU TYR GLY PRO PHE GLY THR GLY LYS SER
SEQRES 4 F 174 PHE ILE LEU GLY ALA ILE ALA ASN GLN LEU LYS SER LYS
SEQRES 5 F 174 LYS VAL ARG SER THR ILE ILE TYR LEU PRO GLU PHE ILE
SEQRES 6 F 174 ARG THR LEU LYS GLY GLY PHE LYS ASP GLY SER PHE GLU
SEQRES 7 F 174 LYS LYS LEU HIS ARG VAL ARG GLU ALA ASN ILE LEU MET
SEQRES 8 F 174 LEU ASP ASP ILE GLY ALA GLU GLU VAL THR PRO TRP VAL
SEQRES 9 F 174 ARG ASP GLU VAL ILE GLY PRO LEU LEU HIS TYR ARG MET
SEQRES 10 F 174 VAL HIS GLU LEU PRO THR PHE PHE SER SER ASN PHE ASP
SEQRES 11 F 174 TYR SER GLU LEU GLU HIS HIS LEU ALA MET THR ARG ASP
SEQRES 12 F 174 GLY GLU GLU LYS THR LYS ALA ALA ARG ILE ILE GLU ARG
SEQRES 13 F 174 VAL LYS SER LEU SER THR PRO TYR PHE LEU SER GLY GLU
SEQRES 14 F 174 ASN PHE ARG ASN ASN
SEQRES 1 G 174 SER ASN ALA ASP ARG LEU ASP VAL ALA MET ALA ALA ASP
SEQRES 2 G 174 ASP ILE CYS THR ALA ILE THR ASN GLY GLU GLN VAL LYS
SEQRES 3 G 174 GLY LEU TYR LEU TYR GLY PRO PHE GLY THR GLY LYS SER
SEQRES 4 G 174 PHE ILE LEU GLY ALA ILE ALA ASN GLN LEU LYS SER LYS
SEQRES 5 G 174 LYS VAL ARG SER THR ILE ILE TYR LEU PRO GLU PHE ILE
SEQRES 6 G 174 ARG THR LEU LYS GLY GLY PHE LYS ASP GLY SER PHE GLU
SEQRES 7 G 174 LYS LYS LEU HIS ARG VAL ARG GLU ALA ASN ILE LEU MET
SEQRES 8 G 174 LEU ASP ASP ILE GLY ALA GLU GLU VAL THR PRO TRP VAL
SEQRES 9 G 174 ARG ASP GLU VAL ILE GLY PRO LEU LEU HIS TYR ARG MET
SEQRES 10 G 174 VAL HIS GLU LEU PRO THR PHE PHE SER SER ASN PHE ASP
SEQRES 11 G 174 TYR SER GLU LEU GLU HIS HIS LEU ALA MET THR ARG ASP
SEQRES 12 G 174 GLY GLU GLU LYS THR LYS ALA ALA ARG ILE ILE GLU ARG
SEQRES 13 G 174 VAL LYS SER LEU SER THR PRO TYR PHE LEU SER GLY GLU
SEQRES 14 G 174 ASN PHE ARG ASN ASN
SEQRES 1 H 174 SER ASN ALA ASP ARG LEU ASP VAL ALA MET ALA ALA ASP
SEQRES 2 H 174 ASP ILE CYS THR ALA ILE THR ASN GLY GLU GLN VAL LYS
SEQRES 3 H 174 GLY LEU TYR LEU TYR GLY PRO PHE GLY THR GLY LYS SER
SEQRES 4 H 174 PHE ILE LEU GLY ALA ILE ALA ASN GLN LEU LYS SER LYS
SEQRES 5 H 174 LYS VAL ARG SER THR ILE ILE TYR LEU PRO GLU PHE ILE
SEQRES 6 H 174 ARG THR LEU LYS GLY GLY PHE LYS ASP GLY SER PHE GLU
SEQRES 7 H 174 LYS LYS LEU HIS ARG VAL ARG GLU ALA ASN ILE LEU MET
SEQRES 8 H 174 LEU ASP ASP ILE GLY ALA GLU GLU VAL THR PRO TRP VAL
SEQRES 9 H 174 ARG ASP GLU VAL ILE GLY PRO LEU LEU HIS TYR ARG MET
SEQRES 10 H 174 VAL HIS GLU LEU PRO THR PHE PHE SER SER ASN PHE ASP
SEQRES 11 H 174 TYR SER GLU LEU GLU HIS HIS LEU ALA MET THR ARG ASP
SEQRES 12 H 174 GLY GLU GLU LYS THR LYS ALA ALA ARG ILE ILE GLU ARG
SEQRES 13 H 174 VAL LYS SER LEU SER THR PRO TYR PHE LEU SER GLY GLU
SEQRES 14 H 174 ASN PHE ARG ASN ASN
SEQRES 1 I 174 SER ASN ALA ASP ARG LEU ASP VAL ALA MET ALA ALA ASP
SEQRES 2 I 174 ASP ILE CYS THR ALA ILE THR ASN GLY GLU GLN VAL LYS
SEQRES 3 I 174 GLY LEU TYR LEU TYR GLY PRO PHE GLY THR GLY LYS SER
SEQRES 4 I 174 PHE ILE LEU GLY ALA ILE ALA ASN GLN LEU LYS SER LYS
SEQRES 5 I 174 LYS VAL ARG SER THR ILE ILE TYR LEU PRO GLU PHE ILE
SEQRES 6 I 174 ARG THR LEU LYS GLY GLY PHE LYS ASP GLY SER PHE GLU
SEQRES 7 I 174 LYS LYS LEU HIS ARG VAL ARG GLU ALA ASN ILE LEU MET
SEQRES 8 I 174 LEU ASP ASP ILE GLY ALA GLU GLU VAL THR PRO TRP VAL
SEQRES 9 I 174 ARG ASP GLU VAL ILE GLY PRO LEU LEU HIS TYR ARG MET
SEQRES 10 I 174 VAL HIS GLU LEU PRO THR PHE PHE SER SER ASN PHE ASP
SEQRES 11 I 174 TYR SER GLU LEU GLU HIS HIS LEU ALA MET THR ARG ASP
SEQRES 12 I 174 GLY GLU GLU LYS THR LYS ALA ALA ARG ILE ILE GLU ARG
SEQRES 13 I 174 VAL LYS SER LEU SER THR PRO TYR PHE LEU SER GLY GLU
SEQRES 14 I 174 ASN PHE ARG ASN ASN
SEQRES 1 J 174 SER ASN ALA ASP ARG LEU ASP VAL ALA MET ALA ALA ASP
SEQRES 2 J 174 ASP ILE CYS THR ALA ILE THR ASN GLY GLU GLN VAL LYS
SEQRES 3 J 174 GLY LEU TYR LEU TYR GLY PRO PHE GLY THR GLY LYS SER
SEQRES 4 J 174 PHE ILE LEU GLY ALA ILE ALA ASN GLN LEU LYS SER LYS
SEQRES 5 J 174 LYS VAL ARG SER THR ILE ILE TYR LEU PRO GLU PHE ILE
SEQRES 6 J 174 ARG THR LEU LYS GLY GLY PHE LYS ASP GLY SER PHE GLU
SEQRES 7 J 174 LYS LYS LEU HIS ARG VAL ARG GLU ALA ASN ILE LEU MET
SEQRES 8 J 174 LEU ASP ASP ILE GLY ALA GLU GLU VAL THR PRO TRP VAL
SEQRES 9 J 174 ARG ASP GLU VAL ILE GLY PRO LEU LEU HIS TYR ARG MET
SEQRES 10 J 174 VAL HIS GLU LEU PRO THR PHE PHE SER SER ASN PHE ASP
SEQRES 11 J 174 TYR SER GLU LEU GLU HIS HIS LEU ALA MET THR ARG ASP
SEQRES 12 J 174 GLY GLU GLU LYS THR LYS ALA ALA ARG ILE ILE GLU ARG
SEQRES 13 J 174 VAL LYS SER LEU SER THR PRO TYR PHE LEU SER GLY GLU
SEQRES 14 J 174 ASN PHE ARG ASN ASN
SEQRES 1 L 174 SER ASN ALA ASP ARG LEU ASP VAL ALA MET ALA ALA ASP
SEQRES 2 L 174 ASP ILE CYS THR ALA ILE THR ASN GLY GLU GLN VAL LYS
SEQRES 3 L 174 GLY LEU TYR LEU TYR GLY PRO PHE GLY THR GLY LYS SER
SEQRES 4 L 174 PHE ILE LEU GLY ALA ILE ALA ASN GLN LEU LYS SER LYS
SEQRES 5 L 174 LYS VAL ARG SER THR ILE ILE TYR LEU PRO GLU PHE ILE
SEQRES 6 L 174 ARG THR LEU LYS GLY GLY PHE LYS ASP GLY SER PHE GLU
SEQRES 7 L 174 LYS LYS LEU HIS ARG VAL ARG GLU ALA ASN ILE LEU MET
SEQRES 8 L 174 LEU ASP ASP ILE GLY ALA GLU GLU VAL THR PRO TRP VAL
SEQRES 9 L 174 ARG ASP GLU VAL ILE GLY PRO LEU LEU HIS TYR ARG MET
SEQRES 10 L 174 VAL HIS GLU LEU PRO THR PHE PHE SER SER ASN PHE ASP
SEQRES 11 L 174 TYR SER GLU LEU GLU HIS HIS LEU ALA MET THR ARG ASP
SEQRES 12 L 174 GLY GLU GLU LYS THR LYS ALA ALA ARG ILE ILE GLU ARG
SEQRES 13 L 174 VAL LYS SER LEU SER THR PRO TYR PHE LEU SER GLY GLU
SEQRES 14 L 174 ASN PHE ARG ASN ASN
SEQRES 1 K 174 SER ASN ALA ASP ARG LEU ASP VAL ALA MET ALA ALA ASP
SEQRES 2 K 174 ASP ILE CYS THR ALA ILE THR ASN GLY GLU GLN VAL LYS
SEQRES 3 K 174 GLY LEU TYR LEU TYR GLY PRO PHE GLY THR GLY LYS SER
SEQRES 4 K 174 PHE ILE LEU GLY ALA ILE ALA ASN GLN LEU LYS SER LYS
SEQRES 5 K 174 LYS VAL ARG SER THR ILE ILE TYR LEU PRO GLU PHE ILE
SEQRES 6 K 174 ARG THR LEU LYS GLY GLY PHE LYS ASP GLY SER PHE GLU
SEQRES 7 K 174 LYS LYS LEU HIS ARG VAL ARG GLU ALA ASN ILE LEU MET
SEQRES 8 K 174 LEU ASP ASP ILE GLY ALA GLU GLU VAL THR PRO TRP VAL
SEQRES 9 K 174 ARG ASP GLU VAL ILE GLY PRO LEU LEU HIS TYR ARG MET
SEQRES 10 K 174 VAL HIS GLU LEU PRO THR PHE PHE SER SER ASN PHE ASP
SEQRES 11 K 174 TYR SER GLU LEU GLU HIS HIS LEU ALA MET THR ARG ASP
SEQRES 12 K 174 GLY GLU GLU LYS THR LYS ALA ALA ARG ILE ILE GLU ARG
SEQRES 13 K 174 VAL LYS SER LEU SER THR PRO TYR PHE LEU SER GLY GLU
SEQRES 14 K 174 ASN PHE ARG ASN ASN
HET SO4 A 401 5
HET SO4 A 402 5
HET SO4 A 403 5
HET SO4 B 401 5
HET SO4 C 401 5
HET SO4 C 402 5
HET SO4 C 403 5
HET SO4 C 404 5
HET SO4 D 401 5
HET SO4 D 402 5
HET SO4 E 401 5
HET SO4 E 402 5
HET SO4 F 401 5
HET SO4 F 402 5
HET SO4 G 401 5
HET SO4 G 402 5
HET SO4 H 401 5
HET SO4 H 402 5
HET SO4 H 403 5
HET SO4 H 404 5
HET SO4 I 401 5
HET SO4 I 402 5
HET SO4 J 401 5
HET SO4 J 402 5
HET SO4 L 401 5
HET SO4 L 402 5
HET SO4 K 401 5
HET SO4 K 402 5
HETNAM SO4 SULFATE ION
FORMUL 13 SO4 28(O4 S 2-)
FORMUL 41 HOH *207(H2 O)
HELIX 1 AA1 ASP A 139 GLY A 154 1 16
HELIX 2 AA2 GLY A 169 SER A 183 1 15
HELIX 3 AA3 LEU A 193 LYS A 201 1 9
HELIX 4 AA4 GLY A 202 PHE A 204 5 3
HELIX 5 AA5 SER A 208 GLU A 218 1 11
HELIX 6 AA6 THR A 233 VAL A 240 1 8
HELIX 7 AA7 VAL A 240 HIS A 251 1 12
HELIX 8 AA8 ASP A 262 MET A 272 1 11
HELIX 9 AA9 GLU A 278 LEU A 292 1 15
HELIX 10 AB1 ASP B 139 ASN B 153 1 15
HELIX 11 AB2 GLY B 169 LYS B 184 1 16
HELIX 12 AB3 LEU B 193 LYS B 201 1 9
HELIX 13 AB4 SER B 208 GLU B 218 1 11
HELIX 14 AB5 THR B 233 VAL B 240 1 8
HELIX 15 AB6 VAL B 240 HIS B 251 1 12
HELIX 16 AB7 ASP B 262 MET B 272 1 11
HELIX 17 AB8 GLU B 278 LEU B 292 1 15
HELIX 18 AB9 ASP C 139 ASN C 153 1 15
HELIX 19 AC1 GLY C 169 LYS C 184 1 16
HELIX 20 AC2 LEU C 193 LYS C 201 1 9
HELIX 21 AC3 GLY C 202 GLY C 207 5 6
HELIX 22 AC4 SER C 208 GLU C 218 1 11
HELIX 23 AC5 THR C 233 VAL C 240 1 8
HELIX 24 AC6 VAL C 240 HIS C 251 1 12
HELIX 25 AC7 ASP C 262 ALA C 271 1 10
HELIX 26 AC8 GLU C 278 LEU C 292 1 15
HELIX 27 AC9 ASP D 139 ASN D 153 1 15
HELIX 28 AD1 GLY D 169 LYS D 184 1 16
HELIX 29 AD2 LEU D 193 LYS D 201 1 9
HELIX 30 AD3 GLY D 202 PHE D 204 5 3
HELIX 31 AD4 PHE D 209 GLU D 218 1 10
HELIX 32 AD5 THR D 233 VAL D 240 1 8
HELIX 33 AD6 VAL D 240 HIS D 251 1 12
HELIX 34 AD7 ASP D 262 ALA D 271 1 10
HELIX 35 AD8 GLU D 278 LEU D 292 1 15
HELIX 36 AD9 ASP E 139 ASN E 153 1 15
HELIX 37 AE1 GLY E 169 LYS E 184 1 16
HELIX 38 AE2 LEU E 193 LYS E 201 1 9
HELIX 39 AE3 PHE E 209 GLU E 218 1 10
HELIX 40 AE4 THR E 233 VAL E 240 1 8
HELIX 41 AE5 VAL E 240 HIS E 251 1 12
HELIX 42 AE6 ASP E 262 ALA E 271 1 10
HELIX 43 AE7 GLU E 278 LEU E 292 1 15
HELIX 44 AE8 ASP F 139 ASN F 153 1 15
HELIX 45 AE9 GLY F 169 SER F 183 1 15
HELIX 46 AF1 LEU F 193 LYS F 201 1 9
HELIX 47 AF2 PHE F 209 GLU F 218 1 10
HELIX 48 AF3 THR F 233 VAL F 240 1 8
HELIX 49 AF4 VAL F 240 HIS F 251 1 12
HELIX 50 AF5 ASP F 262 ALA F 271 1 10
HELIX 51 AF6 GLU F 278 LEU F 292 1 15
HELIX 52 AF7 ASP G 139 ASN G 153 1 15
HELIX 53 AF8 GLY G 169 LYS G 184 1 16
HELIX 54 AF9 LEU G 193 LYS G 201 1 9
HELIX 55 AG1 GLY G 202 PHE G 204 5 3
HELIX 56 AG2 PHE G 209 GLU G 218 1 10
HELIX 57 AG3 THR G 233 GLU G 239 1 7
HELIX 58 AG4 VAL G 240 HIS G 251 1 12
HELIX 59 AG5 ASP G 262 ALA G 271 1 10
HELIX 60 AG6 GLU G 278 LEU G 292 1 15
HELIX 61 AG7 ASP H 139 ASN H 153 1 15
HELIX 62 AG8 GLY H 169 LYS H 184 1 16
HELIX 63 AG9 LEU H 193 LYS H 201 1 9
HELIX 64 AH1 PHE H 209 GLU H 218 1 10
HELIX 65 AH2 THR H 233 VAL H 240 1 8
HELIX 66 AH3 VAL H 240 HIS H 251 1 12
HELIX 67 AH4 ASP H 262 ALA H 271 1 10
HELIX 68 AH5 GLU H 278 LEU H 292 1 15
HELIX 69 AH6 ASP I 139 ASN I 153 1 15
HELIX 70 AH7 GLY I 169 LYS I 184 1 16
HELIX 71 AH8 LEU I 193 LYS I 201 1 9
HELIX 72 AH9 GLY I 202 PHE I 204 5 3
HELIX 73 AI1 PHE I 209 GLU I 218 1 10
HELIX 74 AI2 THR I 233 VAL I 240 1 8
HELIX 75 AI3 VAL I 240 HIS I 251 1 12
HELIX 76 AI4 ASP I 262 ALA I 271 1 10
HELIX 77 AI5 GLU I 278 LEU I 292 1 15
HELIX 78 AI6 ASP J 139 ASN J 153 1 15
HELIX 79 AI7 GLY J 169 LYS J 184 1 16
HELIX 80 AI8 LEU J 193 LYS J 201 1 9
HELIX 81 AI9 PHE J 209 GLU J 218 1 10
HELIX 82 AJ1 THR J 233 VAL J 240 1 8
HELIX 83 AJ2 VAL J 240 HIS J 251 1 12
HELIX 84 AJ3 ASP J 262 ALA J 271 1 10
HELIX 85 AJ4 GLU J 278 LEU J 292 1 15
HELIX 86 AJ5 VAL L 140 ASN L 153 1 14
HELIX 87 AJ6 GLY L 169 LYS L 184 1 16
HELIX 88 AJ7 LEU L 193 GLY L 202 1 10
HELIX 89 AJ8 SER L 208 ARG L 217 1 10
HELIX 90 AJ9 THR L 233 VAL L 240 1 8
HELIX 91 AK1 VAL L 240 HIS L 251 1 12
HELIX 92 AK2 ASP L 262 MET L 272 1 11
HELIX 93 AK3 THR L 280 LEU L 292 1 13
HELIX 94 AK4 ASP K 139 GLY K 154 1 16
HELIX 95 AK5 GLY K 169 LYS K 184 1 16
HELIX 96 AK6 LEU K 193 LYS K 201 1 9
HELIX 97 AK7 PHE K 209 GLU K 218 1 10
HELIX 98 AK8 THR K 233 VAL K 240 1 8
HELIX 99 AK9 VAL K 240 HIS K 251 1 12
HELIX 100 AL1 ASP K 262 ALA K 271 1 10
HELIX 101 AL2 GLU K 278 LEU K 292 1 15
SHEET 1 AA1 5 THR A 189 TYR A 192 0
SHEET 2 AA1 5 LEU A 222 ILE A 227 1 O ASP A 225 N ILE A 191
SHEET 3 AA1 5 THR A 255 SER A 259 1 O SER A 258 N ILE A 227
SHEET 4 AA1 5 GLY A 159 TYR A 163 1 N LEU A 160 O PHE A 257
SHEET 5 AA1 5 SER A 293 PHE A 297 1 O THR A 294 N TYR A 161
SHEET 1 AA2 5 THR B 189 TYR B 192 0
SHEET 2 AA2 5 LEU B 222 ILE B 227 1 O ASP B 225 N ILE B 191
SHEET 3 AA2 5 THR B 255 SER B 259 1 O PHE B 256 N LEU B 224
SHEET 4 AA2 5 GLY B 159 TYR B 163 1 N LEU B 160 O PHE B 257
SHEET 5 AA2 5 SER B 293 PHE B 297 1 O THR B 294 N TYR B 161
SHEET 1 AA3 5 THR C 189 TYR C 192 0
SHEET 2 AA3 5 LEU C 222 ASP C 225 1 O MET C 223 N ILE C 191
SHEET 3 AA3 5 THR C 255 SER C 259 1 O PHE C 256 N LEU C 224
SHEET 4 AA3 5 GLY C 159 TYR C 163 1 N LEU C 160 O PHE C 257
SHEET 5 AA3 5 SER C 293 PHE C 297 1 O THR C 294 N GLY C 159
SHEET 1 AA4 2 MET C 272 THR C 273 0
SHEET 2 AA4 2 GLY C 276 GLU C 277 -1 O GLY C 276 N THR C 273
SHEET 1 AA5 5 THR D 189 TYR D 192 0
SHEET 2 AA5 5 LEU D 222 ASP D 225 1 O ASP D 225 N ILE D 191
SHEET 3 AA5 5 THR D 255 SER D 259 1 O PHE D 256 N LEU D 224
SHEET 4 AA5 5 GLY D 159 TYR D 163 1 N LEU D 160 O PHE D 257
SHEET 5 AA5 5 SER D 293 PHE D 297 1 O THR D 294 N GLY D 159
SHEET 1 AA6 2 MET D 272 THR D 273 0
SHEET 2 AA6 2 GLY D 276 GLU D 277 -1 O GLY D 276 N THR D 273
SHEET 1 AA7 5 THR E 189 TYR E 192 0
SHEET 2 AA7 5 LEU E 222 ASP E 225 1 O ASP E 225 N ILE E 191
SHEET 3 AA7 5 THR E 255 SER E 259 1 O PHE E 256 N LEU E 224
SHEET 4 AA7 5 GLY E 159 TYR E 163 1 N LEU E 160 O PHE E 257
SHEET 5 AA7 5 SER E 293 PHE E 297 1 O THR E 294 N TYR E 161
SHEET 1 AA8 2 MET E 272 THR E 273 0
SHEET 2 AA8 2 GLY E 276 GLU E 277 -1 O GLY E 276 N THR E 273
SHEET 1 AA9 5 THR F 189 TYR F 192 0
SHEET 2 AA9 5 LEU F 222 ASP F 225 1 O ASP F 225 N ILE F 191
SHEET 3 AA9 5 THR F 255 SER F 259 1 O PHE F 256 N LEU F 222
SHEET 4 AA9 5 GLY F 159 TYR F 163 1 N LEU F 160 O PHE F 257
SHEET 5 AA9 5 SER F 293 PHE F 297 1 O THR F 294 N TYR F 161
SHEET 1 AB1 2 MET F 272 THR F 273 0
SHEET 2 AB1 2 GLY F 276 GLU F 277 -1 O GLY F 276 N THR F 273
SHEET 1 AB2 5 THR G 189 TYR G 192 0
SHEET 2 AB2 5 LEU G 222 ASP G 225 1 O ASP G 225 N ILE G 191
SHEET 3 AB2 5 THR G 255 SER G 259 1 O PHE G 256 N LEU G 224
SHEET 4 AB2 5 GLY G 159 TYR G 163 1 N LEU G 160 O PHE G 257
SHEET 5 AB2 5 SER G 293 PHE G 297 1 O THR G 294 N TYR G 161
SHEET 1 AB3 2 MET G 272 THR G 273 0
SHEET 2 AB3 2 GLY G 276 GLU G 277 -1 O GLY G 276 N THR G 273
SHEET 1 AB4 5 THR H 189 TYR H 192 0
SHEET 2 AB4 5 LEU H 222 ASP H 225 1 O ASP H 225 N ILE H 191
SHEET 3 AB4 5 THR H 255 SER H 259 1 O PHE H 256 N LEU H 224
SHEET 4 AB4 5 GLY H 159 TYR H 163 1 N LEU H 160 O PHE H 257
SHEET 5 AB4 5 SER H 293 PHE H 297 1 O THR H 294 N TYR H 161
SHEET 1 AB5 2 MET H 272 THR H 273 0
SHEET 2 AB5 2 GLY H 276 GLU H 277 -1 O GLY H 276 N THR H 273
SHEET 1 AB6 5 THR I 189 TYR I 192 0
SHEET 2 AB6 5 LEU I 222 ASP I 225 1 O ASP I 225 N ILE I 191
SHEET 3 AB6 5 THR I 255 SER I 259 1 O PHE I 256 N LEU I 224
SHEET 4 AB6 5 GLY I 159 TYR I 163 1 N LEU I 160 O PHE I 257
SHEET 5 AB6 5 SER I 293 PHE I 297 1 O THR I 294 N TYR I 161
SHEET 1 AB7 2 MET I 272 THR I 273 0
SHEET 2 AB7 2 GLY I 276 GLU I 277 -1 O GLY I 276 N THR I 273
SHEET 1 AB8 5 THR J 189 TYR J 192 0
SHEET 2 AB8 5 LEU J 222 ILE J 227 1 O ASP J 225 N ILE J 191
SHEET 3 AB8 5 THR J 255 SER J 259 1 O PHE J 256 N LEU J 224
SHEET 4 AB8 5 GLY J 159 TYR J 163 1 N LEU J 160 O PHE J 257
SHEET 5 AB8 5 SER J 293 PHE J 297 1 O THR J 294 N TYR J 161
SHEET 1 AB9 2 MET J 272 THR J 273 0
SHEET 2 AB9 2 GLY J 276 GLU J 277 -1 O GLY J 276 N THR J 273
SHEET 1 AC1 5 THR L 189 TYR L 192 0
SHEET 2 AC1 5 LEU L 222 ILE L 227 1 O ASP L 225 N ILE L 191
SHEET 3 AC1 5 THR L 255 SER L 259 1 O PHE L 256 N LEU L 222
SHEET 4 AC1 5 GLY L 159 TYR L 163 1 N LEU L 160 O PHE L 257
SHEET 5 AC1 5 SER L 293 PHE L 297 1 O THR L 294 N TYR L 161
SHEET 1 AC2 5 THR K 189 TYR K 192 0
SHEET 2 AC2 5 LEU K 222 ASP K 225 1 O ASP K 225 N ILE K 191
SHEET 3 AC2 5 THR K 255 SER K 259 1 O PHE K 256 N LEU K 224
SHEET 4 AC2 5 GLY K 159 TYR K 163 1 N LEU K 160 O PHE K 257
SHEET 5 AC2 5 SER K 293 PHE K 297 1 O THR K 294 N GLY K 159
SHEET 1 AC3 2 MET K 272 THR K 273 0
SHEET 2 AC3 2 GLY K 276 GLU K 277 -1 O GLY K 276 N THR K 273
LINK ND2 ASN C 302 CA ARG H 137 1555 1555 1.39
CISPEP 1 LEU B 138 ASP B 139 0 1.27
CISPEP 2 SER B 299 GLY B 300 0 2.95
CISPEP 3 ASP C 136 ARG C 137 0 2.17
CISPEP 4 GLU D 301 ASN D 302 0 10.57
CISPEP 5 GLY F 202 GLY F 203 0 0.13
CISPEP 6 GLY H 202 GLY H 203 0 -1.68
CISPEP 7 ASP L 206 GLY L 207 0 0.05
SITE 1 AC1 7 PHE A 166 GLY A 167 THR A 168 GLY A 169
SITE 2 AC1 7 LYS A 170 SER A 171 ARG B 198
SITE 1 AC2 4 GLU A 277 GLU A 278 LYS A 279 THR A 280
SITE 1 AC3 2 HIS A 246 ARG A 288
SITE 1 AC4 7 ARG A 198 PHE B 166 GLY B 167 THR B 168
SITE 2 AC4 7 GLY B 169 LYS B 170 SER B 171
SITE 1 AC5 6 PHE C 166 GLY C 167 THR C 168 GLY C 169
SITE 2 AC5 6 LYS C 170 SER C 171
SITE 1 AC6 4 HIS C 246 ARG C 284 ARG C 288 ARG J 284
SITE 1 AC7 4 GLU C 278 LYS C 279 THR C 280 HIS J 246
SITE 1 AC8 9 GLY C 242 PRO C 243 HIS C 246 ARG C 288
SITE 2 AC8 9 HOH C 501 THR J 280 LYS J 281 ARG J 284
SITE 3 AC8 9 HOH J 501
SITE 1 AC9 6 PHE D 166 GLY D 167 THR D 168 GLY D 169
SITE 2 AC9 6 LYS D 170 SER D 171
SITE 1 AD1 2 LYS D 279 THR D 280
SITE 1 AD2 7 MET B 142 PHE E 166 GLY E 167 THR E 168
SITE 2 AD2 7 GLY E 169 LYS E 170 SER E 171
SITE 1 AD3 5 GLU E 277 GLU E 278 LYS E 279 THR E 280
SITE 2 AD3 5 HOH E 506
SITE 1 AD4 7 MET A 142 PHE F 166 GLY F 167 THR F 168
SITE 2 AD4 7 GLY F 169 LYS F 170 SER F 171
SITE 1 AD5 4 GLU F 277 GLU F 278 LYS F 279 THR F 280
SITE 1 AD6 8 LYS F 211 ARG F 215 PHE G 166 GLY G 167
SITE 2 AD6 8 THR G 168 GLY G 169 LYS G 170 SER G 171
SITE 1 AD7 6 LYS E 281 ARG E 284 GLY G 242 PRO G 243
SITE 2 AD7 6 HIS G 246 ARG G 288
SITE 1 AD8 7 LYS E 211 PHE H 166 GLY H 167 THR H 168
SITE 2 AD8 7 GLY H 169 LYS H 170 SER H 171
SITE 1 AD9 6 HIS F 246 MET F 249 ARG F 284 ARG F 288
SITE 2 AD9 6 ARG H 284 ARG J 187
SITE 1 AE1 5 HIS F 246 GLU H 277 GLU H 278 LYS H 279
SITE 2 AE1 5 THR H 280
SITE 1 AE2 5 ARG F 284 HIS H 246 MET H 249 ARG H 284
SITE 2 AE2 5 ARG H 288
SITE 1 AE3 6 PHE I 166 GLY I 167 THR I 168 GLY I 169
SITE 2 AE3 6 LYS I 170 SER I 171
SITE 1 AE4 3 GLU B 252 GLU I 277 LYS I 279
SITE 1 AE5 7 PRO J 165 PHE J 166 GLY J 167 THR J 168
SITE 2 AE5 7 GLY J 169 LYS J 170 SER J 171
SITE 1 AE6 6 GLU J 277 GLU J 278 LYS J 279 THR J 280
SITE 2 AE6 6 HOH J 501 HOH J 503
SITE 1 AE7 6 PHE L 166 GLY L 167 THR L 168 GLY L 169
SITE 2 AE7 6 LYS L 170 SER L 171
SITE 1 AE8 7 THR A 280 LYS A 281 ARG A 284 GLY L 242
SITE 2 AE8 7 PRO L 243 HIS L 246 ARG L 288
SITE 1 AE9 6 PHE K 166 GLY K 167 THR K 168 GLY K 169
SITE 2 AE9 6 LYS K 170 SER K 171
SITE 1 AF1 4 GLU K 277 GLU K 278 LYS K 279 THR K 280
SITE 1 AF2 10 ASP C 136 LEU C 138 ASP C 139 ALA C 143
SITE 2 AF2 10 TYR C 296 GLU C 301 PHE C 303 ARG C 304
SITE 3 AF2 10 ARG E 187 LEU H 138
CRYST1 113.099 126.261 183.344 90.00 90.00 90.00 P 21 21 21 48
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 0.008842 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007920 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005454 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
