HEADER OXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR 02-AUG-13 4M10
TITLE CRYSTAL STRUCTURE OF MURINE CYCLOOXYGENASE-2 COMPLEX WITH ISOXICAM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROSTAGLANDIN G/H SYNTHASE 2;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: UNP RESIDUES 18-604;
COMPND 5 SYNONYM: CYCLOOXYGENASE-2, COX-2, GLUCOCORTICOID-REGULATED
COMPND 6 INFLAMMATORY CYCLOOXYGENASE, GRIPGHS, MACROPHAGE ACTIVATION-
COMPND 7 ASSOCIATED MARKER PROTEIN P71/73, PES-2, PHS II, PROSTAGLANDIN H2
COMPND 8 SYNTHASE 2, PGH SYNTHASE 2, PGHS-2, PROSTAGLANDIN-ENDOPEROXIDE
COMPND 9 SYNTHASE 2, TIS10 PROTEIN;
COMPND 10 EC: 1.14.99.1;
COMPND 11 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: PTGS2, COX-2, COX2, PGHS-B, TIS10;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: SF21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PVL1393
KEYWDS NSAID, COX, DIOXYGENASE, PEROXIDASE, GLYCOSYLATION, OXIDOREDUCTASE-
KEYWDS 2 OXIDOREDUCTASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR S.XU,D.J.HERMANSON,S.BANERJEE,K.GHEBREELASIE,L.J.MARNETT
REVDAT 5 20-SEP-23 4M10 1 HETSYN
REVDAT 4 29-JUL-20 4M10 1 COMPND REMARK HETNAM LINK
REVDAT 4 2 1 SITE ATOM
REVDAT 3 14-MAY-14 4M10 1 JRNL
REVDAT 2 12-FEB-14 4M10 1 JRNL
REVDAT 1 22-JAN-14 4M10 0
JRNL AUTH S.XU,D.J.HERMANSON,S.BANERJEE,K.GHEBRESELASIE,G.M.CLAYTON,
JRNL AUTH 2 R.M.GARAVITO,L.J.MARNETT
JRNL TITL OXICAMS BIND IN A NOVEL MODE TO THE CYCLOOXYGENASE ACTIVE
JRNL TITL 2 SITE VIA A TWO-WATER-MEDIATED H-BONDING NETWORK.
JRNL REF J.BIOL.CHEM. V. 289 6799 2014
JRNL REFN ISSN 0021-9258
JRNL PMID 24425867
JRNL DOI 10.1074/JBC.M113.517987
REMARK 2
REMARK 2 RESOLUTION. 2.01 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.2_1309)
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) : 2.01
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.27
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 3 NUMBER OF REFLECTIONS : 195768
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.190
REMARK 3 R VALUE (WORKING SET) : 0.189
REMARK 3 FREE R VALUE : 0.220
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 9793
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 49.2881 - 6.2394 0.98 6531 343 0.1815 0.2030
REMARK 3 2 6.2394 - 4.9539 1.00 6403 335 0.1675 0.1794
REMARK 3 3 4.9539 - 4.3281 0.99 6302 332 0.1506 0.1708
REMARK 3 4 4.3281 - 3.9325 1.00 6320 332 0.1533 0.1747
REMARK 3 5 3.9325 - 3.6508 1.00 6306 332 0.1623 0.1804
REMARK 3 6 3.6508 - 3.4356 1.00 6280 331 0.1725 0.1860
REMARK 3 7 3.4356 - 3.2636 0.99 6229 328 0.1881 0.2222
REMARK 3 8 3.2636 - 3.1215 0.99 6220 328 0.1966 0.2188
REMARK 3 9 3.1215 - 3.0014 1.00 6258 330 0.1955 0.2231
REMARK 3 10 3.0014 - 2.8978 1.00 6242 330 0.1924 0.2257
REMARK 3 11 2.8978 - 2.8072 0.99 6202 326 0.1979 0.2553
REMARK 3 12 2.8072 - 2.7270 1.00 6206 324 0.1910 0.2292
REMARK 3 13 2.7270 - 2.6552 0.99 6213 327 0.1887 0.2372
REMARK 3 14 2.6552 - 2.5904 1.00 6203 325 0.1841 0.2278
REMARK 3 15 2.5904 - 2.5315 0.99 6183 324 0.1915 0.2483
REMARK 3 16 2.5315 - 2.4777 0.99 6162 326 0.1876 0.2187
REMARK 3 17 2.4777 - 2.4281 0.99 6184 325 0.1906 0.2393
REMARK 3 18 2.4281 - 2.3823 0.99 6168 325 0.1924 0.2562
REMARK 3 19 2.3823 - 2.3397 0.99 6173 326 0.2012 0.2501
REMARK 3 20 2.3397 - 2.3001 0.99 6137 325 0.2032 0.2660
REMARK 3 21 2.3001 - 2.2630 0.99 6155 326 0.2188 0.2780
REMARK 3 22 2.2630 - 2.2282 0.98 6088 323 0.2411 0.2859
REMARK 3 23 2.2282 - 2.1954 0.98 6093 321 0.2388 0.2669
REMARK 3 24 2.1954 - 2.1645 0.99 6106 321 0.2269 0.2805
REMARK 3 25 2.1645 - 2.1352 0.99 6112 326 0.2319 0.2885
REMARK 3 26 2.1352 - 2.1075 0.99 6156 322 0.2349 0.2730
REMARK 3 27 2.1075 - 2.0811 0.98 6043 319 0.2478 0.2916
REMARK 3 28 2.0811 - 2.0561 0.98 6134 323 0.2509 0.2843
REMARK 3 29 2.0561 - 2.0322 0.99 6087 317 0.2584 0.2970
REMARK 3 30 2.0322 - 2.0100 0.98 6079 321 0.2733 0.2961
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) : 0.190
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.580
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 26.08
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 : 0.011 19051
REMARK 3 ANGLE : 1.222 25852
REMARK 3 CHIRALITY : 0.084 2737
REMARK 3 PLANARITY : 0.006 3298
REMARK 3 DIHEDRAL : 15.090 7000
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 80
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN A AND RESID 33:45)
REMARK 3 ORIGIN FOR THE GROUP (A): 116.3562 61.5748 36.7025
REMARK 3 T TENSOR
REMARK 3 T11: 0.5260 T22: 0.1804
REMARK 3 T33: 0.2617 T12: 0.1003
REMARK 3 T13: 0.1037 T23: 0.0484
REMARK 3 L TENSOR
REMARK 3 L11: 9.2519 L22: 1.6961
REMARK 3 L33: 2.5893 L12: 0.1078
REMARK 3 L13: 1.4601 L23: 1.1777
REMARK 3 S TENSOR
REMARK 3 S11: 0.2973 S12: 0.2683 S13: 0.5273
REMARK 3 S21: 0.0747 S22: -0.0643 S23: 0.0985
REMARK 3 S31: -0.3625 S32: -0.2758 S33: -0.2157
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN A AND RESID 46:56)
REMARK 3 ORIGIN FOR THE GROUP (A): 110.2455 65.1047 42.4978
REMARK 3 T TENSOR
REMARK 3 T11: 0.6050 T22: 0.3122
REMARK 3 T33: 0.4547 T12: 0.2034
REMARK 3 T13: 0.0775 T23: 0.0613
REMARK 3 L TENSOR
REMARK 3 L11: 5.0595 L22: 3.9437
REMARK 3 L33: 2.2940 L12: 0.9787
REMARK 3 L13: -3.4084 L23: -0.7248
REMARK 3 S TENSOR
REMARK 3 S11: 0.4804 S12: 0.3939 S13: 0.8101
REMARK 3 S21: -0.6883 S22: -0.1281 S23: 0.1526
REMARK 3 S31: -0.3740 S32: -0.1735 S33: -0.2489
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN A AND RESID 57:74)
REMARK 3 ORIGIN FOR THE GROUP (A): 125.8055 69.3206 41.3480
REMARK 3 T TENSOR
REMARK 3 T11: 0.5977 T22: 0.1653
REMARK 3 T33: 0.4299 T12: 0.0039
REMARK 3 T13: 0.1530 T23: 0.0203
REMARK 3 L TENSOR
REMARK 3 L11: 1.2824 L22: 3.1642
REMARK 3 L33: 4.1769 L12: 1.8736
REMARK 3 L13: -1.5532 L23: -3.1950
REMARK 3 S TENSOR
REMARK 3 S11: 0.3689 S12: 0.0028 S13: 0.5178
REMARK 3 S21: -0.3588 S22: -0.1793 S23: -0.3663
REMARK 3 S31: -0.7623 S32: -0.0710 S33: -0.2022
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN A AND RESID 75:89)
REMARK 3 ORIGIN FOR THE GROUP (A): 139.1764 64.6631 32.8780
REMARK 3 T TENSOR
REMARK 3 T11: 0.6266 T22: 0.3756
REMARK 3 T33: 0.7233 T12: -0.1294
REMARK 3 T13: 0.2982 T23: -0.0084
REMARK 3 L TENSOR
REMARK 3 L11: 0.8622 L22: 4.2734
REMARK 3 L33: 3.7476 L12: -1.9176
REMARK 3 L13: -1.8017 L23: 3.9951
REMARK 3 S TENSOR
REMARK 3 S11: 0.5662 S12: -0.1292 S13: 0.9108
REMARK 3 S21: -1.0311 S22: 0.5260 S23: -1.2670
REMARK 3 S31: -0.9886 S32: -0.0297 S33: -0.9836
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: (CHAIN A AND RESID 90:114)
REMARK 3 ORIGIN FOR THE GROUP (A): 153.4930 49.5487 32.0569
REMARK 3 T TENSOR
REMARK 3 T11: 0.2949 T22: 0.4151
REMARK 3 T33: 0.4382 T12: -0.1722
REMARK 3 T13: 0.0885 T23: -0.0179
REMARK 3 L TENSOR
REMARK 3 L11: 2.5219 L22: 2.2997
REMARK 3 L33: 3.3039 L12: -1.0669
REMARK 3 L13: -0.1955 L23: -1.5289
REMARK 3 S TENSOR
REMARK 3 S11: 0.3668 S12: 0.0799 S13: 0.2948
REMARK 3 S21: 0.0999 S22: -0.2995 S23: -0.1009
REMARK 3 S31: 0.0702 S32: 0.7165 S33: -0.0449
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: (CHAIN A AND RESID 115:123)
REMARK 3 ORIGIN FOR THE GROUP (A): 139.9528 52.9708 39.7286
REMARK 3 T TENSOR
REMARK 3 T11: 0.5382 T22: 0.2887
REMARK 3 T33: 0.4777 T12: -0.1317
REMARK 3 T13: 0.0723 T23: -0.0537
REMARK 3 L TENSOR
REMARK 3 L11: 9.0500 L22: 0.8139
REMARK 3 L33: 0.6998 L12: -2.5204
REMARK 3 L13: 0.8524 L23: 0.0370
REMARK 3 S TENSOR
REMARK 3 S11: -0.1387 S12: -0.2099 S13: 1.8917
REMARK 3 S21: 0.0477 S22: 0.2397 S23: -0.1149
REMARK 3 S31: -0.7163 S32: 0.3826 S33: 0.0168
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: (CHAIN A AND RESID 124:156)
REMARK 3 ORIGIN FOR THE GROUP (A): 118.5836 47.3058 45.0457
REMARK 3 T TENSOR
REMARK 3 T11: 0.2205 T22: 0.1432
REMARK 3 T33: 0.1639 T12: 0.0613
REMARK 3 T13: 0.0089 T23: 0.0007
REMARK 3 L TENSOR
REMARK 3 L11: 1.0674 L22: 0.8670
REMARK 3 L33: 2.4847 L12: 0.1600
REMARK 3 L13: -0.2357 L23: -0.2237
REMARK 3 S TENSOR
REMARK 3 S11: 0.1711 S12: 0.0289 S13: 0.1895
REMARK 3 S21: -0.0339 S22: -0.1141 S23: -0.0167
REMARK 3 S31: -0.3418 S32: -0.2304 S33: -0.0851
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: (CHAIN A AND RESID 157:183)
REMARK 3 ORIGIN FOR THE GROUP (A): 112.0415 48.1738 21.9766
REMARK 3 T TENSOR
REMARK 3 T11: 0.3636 T22: 0.4642
REMARK 3 T33: 0.3138 T12: 0.1937
REMARK 3 T13: -0.0201 T23: 0.0132
REMARK 3 L TENSOR
REMARK 3 L11: 1.5408 L22: 4.2451
REMARK 3 L33: 2.7680 L12: -2.0022
REMARK 3 L13: -1.4515 L23: 3.2364
REMARK 3 S TENSOR
REMARK 3 S11: 0.2173 S12: 0.4988 S13: 0.0524
REMARK 3 S21: -0.1702 S22: -0.5499 S23: 0.3777
REMARK 3 S31: -0.3170 S32: -0.7185 S33: 0.2650
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: (CHAIN A AND RESID 184:193)
REMARK 3 ORIGIN FOR THE GROUP (A): 134.1923 36.2297 13.9932
REMARK 3 T TENSOR
REMARK 3 T11: 0.3283 T22: 0.3486
REMARK 3 T33: 0.1840 T12: 0.1097
REMARK 3 T13: 0.0609 T23: 0.0263
REMARK 3 L TENSOR
REMARK 3 L11: 5.9535 L22: 2.3869
REMARK 3 L33: 0.5754 L12: 0.0471
REMARK 3 L13: -0.6342 L23: -0.0491
REMARK 3 S TENSOR
REMARK 3 S11: 0.2254 S12: 0.5706 S13: 0.0240
REMARK 3 S21: -0.4963 S22: -0.1851 S23: -0.0875
REMARK 3 S31: -0.3281 S32: -0.0303 S33: -0.0758
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: (CHAIN A AND RESID 194:239)
REMARK 3 ORIGIN FOR THE GROUP (A): 127.9932 30.6234 38.7275
REMARK 3 T TENSOR
REMARK 3 T11: 0.1773 T22: 0.1832
REMARK 3 T33: 0.2035 T12: 0.0030
REMARK 3 T13: -0.0036 T23: -0.0124
REMARK 3 L TENSOR
REMARK 3 L11: 1.6747 L22: 1.4015
REMARK 3 L33: 1.1799 L12: -1.3548
REMARK 3 L13: 0.3066 L23: 0.3553
REMARK 3 S TENSOR
REMARK 3 S11: -0.0320 S12: 0.0708 S13: -0.2400
REMARK 3 S21: -0.0248 S22: -0.0099 S23: 0.1718
REMARK 3 S31: -0.0236 S32: -0.1362 S33: 0.0427
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: (CHAIN A AND RESID 240:266)
REMARK 3 ORIGIN FOR THE GROUP (A): 134.7976 12.9427 44.5459
REMARK 3 T TENSOR
REMARK 3 T11: 0.2479 T22: 0.1306
REMARK 3 T33: 0.3061 T12: 0.0400
REMARK 3 T13: 0.0189 T23: 0.0148
REMARK 3 L TENSOR
REMARK 3 L11: 1.8563 L22: 2.5949
REMARK 3 L33: 3.1607 L12: 0.0995
REMARK 3 L13: -0.1738 L23: 0.8797
REMARK 3 S TENSOR
REMARK 3 S11: 0.0353 S12: 0.0713 S13: -0.4403
REMARK 3 S21: 0.0332 S22: -0.0964 S23: -0.0181
REMARK 3 S31: 0.3985 S32: 0.1626 S33: 0.0525
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: (CHAIN A AND RESID 267:278)
REMARK 3 ORIGIN FOR THE GROUP (A): 122.2651 13.3669 37.5836
REMARK 3 T TENSOR
REMARK 3 T11: 0.2024 T22: 0.2109
REMARK 3 T33: 0.4096 T12: -0.0082
REMARK 3 T13: -0.0180 T23: -0.0922
REMARK 3 L TENSOR
REMARK 3 L11: 3.9265 L22: 6.7741
REMARK 3 L33: 5.8912 L12: 1.7296
REMARK 3 L13: 2.0942 L23: -2.0490
REMARK 3 S TENSOR
REMARK 3 S11: 0.1084 S12: 0.1211 S13: -0.6990
REMARK 3 S21: -0.1933 S22: 0.0532 S23: 0.5142
REMARK 3 S31: 0.4526 S32: -0.3664 S33: 0.0171
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: (CHAIN A AND RESID 279:292)
REMARK 3 ORIGIN FOR THE GROUP (A): 126.2286 15.2586 35.3565
REMARK 3 T TENSOR
REMARK 3 T11: 0.3601 T22: 0.2397
REMARK 3 T33: 0.2813 T12: 0.0221
REMARK 3 T13: -0.0050 T23: -0.0247
REMARK 3 L TENSOR
REMARK 3 L11: 7.0317 L22: 5.2189
REMARK 3 L33: 7.5809 L12: 1.9743
REMARK 3 L13: 3.1388 L23: 2.9831
REMARK 3 S TENSOR
REMARK 3 S11: 0.2881 S12: 0.4941 S13: -0.5079
REMARK 3 S21: -0.2750 S22: -0.3670 S23: 0.3802
REMARK 3 S31: 0.9493 S32: -0.1914 S33: 0.1679
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: (CHAIN A AND RESID 293:352)
REMARK 3 ORIGIN FOR THE GROUP (A): 142.1738 24.6562 43.7979
REMARK 3 T TENSOR
REMARK 3 T11: 0.1354 T22: 0.1927
REMARK 3 T33: 0.1919 T12: 0.0360
REMARK 3 T13: 0.0212 T23: -0.0076
REMARK 3 L TENSOR
REMARK 3 L11: 0.8890 L22: 1.0799
REMARK 3 L33: 2.5637 L12: -0.1291
REMARK 3 L13: -0.0686 L23: -0.1979
REMARK 3 S TENSOR
REMARK 3 S11: 0.0262 S12: -0.0319 S13: -0.0948
REMARK 3 S21: 0.0533 S22: -0.0471 S23: -0.0998
REMARK 3 S31: 0.1741 S32: 0.3094 S33: 0.0240
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: (CHAIN A AND RESID 353:366)
REMARK 3 ORIGIN FOR THE GROUP (A): 148.1158 44.1460 38.1687
REMARK 3 T TENSOR
REMARK 3 T11: 0.1943 T22: 0.3161
REMARK 3 T33: 0.2812 T12: 0.0036
REMARK 3 T13: 0.0669 T23: -0.0220
REMARK 3 L TENSOR
REMARK 3 L11: 1.7356 L22: 1.9259
REMARK 3 L33: 8.5982 L12: 0.8867
REMARK 3 L13: -2.5038 L23: -1.4202
REMARK 3 S TENSOR
REMARK 3 S11: 0.2011 S12: -0.3163 S13: 0.1857
REMARK 3 S21: -0.1681 S22: 0.0771 S23: -0.1504
REMARK 3 S31: -0.0408 S32: 1.2801 S33: -0.2262
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: (CHAIN A AND RESID 367:391)
REMARK 3 ORIGIN FOR THE GROUP (A): 131.7720 42.4577 38.5913
REMARK 3 T TENSOR
REMARK 3 T11: 0.2050 T22: 0.1407
REMARK 3 T33: 0.2182 T12: 0.0179
REMARK 3 T13: 0.0247 T23: 0.0255
REMARK 3 L TENSOR
REMARK 3 L11: 1.4716 L22: 0.4317
REMARK 3 L33: 3.1425 L12: -0.8049
REMARK 3 L13: -0.7008 L23: 0.6907
REMARK 3 S TENSOR
REMARK 3 S11: 0.0505 S12: 0.0627 S13: 0.1561
REMARK 3 S21: -0.1027 S22: -0.0585 S23: -0.1744
REMARK 3 S31: -0.1534 S32: -0.0167 S33: -0.0105
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: (CHAIN A AND RESID 392:429)
REMARK 3 ORIGIN FOR THE GROUP (A): 135.1474 18.5034 21.3382
REMARK 3 T TENSOR
REMARK 3 T11: 0.2624 T22: 0.2730
REMARK 3 T33: 0.2581 T12: 0.0869
REMARK 3 T13: -0.0088 T23: -0.0863
REMARK 3 L TENSOR
REMARK 3 L11: 3.1380 L22: 4.0945
REMARK 3 L33: 1.9756 L12: 0.5031
REMARK 3 L13: 1.5186 L23: -0.9378
REMARK 3 S TENSOR
REMARK 3 S11: 0.1736 S12: 0.5134 S13: -0.3279
REMARK 3 S21: -0.5535 S22: -0.1201 S23: -0.0172
REMARK 3 S31: 0.2233 S32: 0.1145 S33: -0.0596
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: (CHAIN A AND RESID 430:511)
REMARK 3 ORIGIN FOR THE GROUP (A): 123.0889 47.7735 21.5782
REMARK 3 T TENSOR
REMARK 3 T11: 0.3728 T22: 0.3027
REMARK 3 T33: 0.2134 T12: 0.1285
REMARK 3 T13: 0.0249 T23: 0.0600
REMARK 3 L TENSOR
REMARK 3 L11: 1.1535 L22: 0.8294
REMARK 3 L33: 1.5858 L12: -0.0858
REMARK 3 L13: -0.1268 L23: 0.0768
REMARK 3 S TENSOR
REMARK 3 S11: 0.1549 S12: 0.3486 S13: 0.1836
REMARK 3 S21: -0.2986 S22: -0.0732 S23: -0.0043
REMARK 3 S31: -0.3848 S32: -0.2393 S33: -0.0726
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: (CHAIN A AND RESID 512:578)
REMARK 3 ORIGIN FOR THE GROUP (A): 143.3187 35.5786 39.3565
REMARK 3 T TENSOR
REMARK 3 T11: 0.1489 T22: 0.2061
REMARK 3 T33: 0.2009 T12: -0.0176
REMARK 3 T13: 0.0291 T23: -0.0166
REMARK 3 L TENSOR
REMARK 3 L11: 1.3410 L22: 0.3880
REMARK 3 L33: 1.3796 L12: -0.2903
REMARK 3 L13: -0.1907 L23: 0.5640
REMARK 3 S TENSOR
REMARK 3 S11: 0.0564 S12: -0.0279 S13: 0.0701
REMARK 3 S21: -0.0387 S22: 0.0328 S23: -0.1388
REMARK 3 S31: -0.0772 S32: 0.2860 S33: -0.0589
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: (CHAIN A AND RESID 579:583)
REMARK 3 ORIGIN FOR THE GROUP (A): 146.4124 31.4101 23.3939
REMARK 3 T TENSOR
REMARK 3 T11: 0.2036 T22: 0.3314
REMARK 3 T33: 0.1829 T12: 0.0627
REMARK 3 T13: -0.0117 T23: 0.0539
REMARK 3 L TENSOR
REMARK 3 L11: 3.3040 L22: 2.5371
REMARK 3 L33: 9.6388 L12: -0.1402
REMARK 3 L13: -4.6417 L23: 0.6129
REMARK 3 S TENSOR
REMARK 3 S11: 0.0233 S12: 0.1131 S13: 0.1007
REMARK 3 S21: -0.3092 S22: -0.3089 S23: -0.0596
REMARK 3 S31: -0.0563 S32: 1.8043 S33: 0.2201
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: (CHAIN B AND RESID 33:52)
REMARK 3 ORIGIN FOR THE GROUP (A): 149.4417 28.4364 68.0519
REMARK 3 T TENSOR
REMARK 3 T11: 0.3024 T22: 0.6152
REMARK 3 T33: 0.2724 T12: 0.1043
REMARK 3 T13: -0.0174 T23: -0.0074
REMARK 3 L TENSOR
REMARK 3 L11: 1.8081 L22: 2.2285
REMARK 3 L33: 3.1737 L12: -0.5130
REMARK 3 L13: -0.3476 L23: 0.5290
REMARK 3 S TENSOR
REMARK 3 S11: 0.0475 S12: -0.4347 S13: -0.0187
REMARK 3 S21: 0.0847 S22: 0.0485 S23: -0.0923
REMARK 3 S31: 0.4106 S32: 0.3301 S33: -0.1103
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: (CHAIN B AND RESID 53:70)
REMARK 3 ORIGIN FOR THE GROUP (A): 154.9899 34.5953 65.6088
REMARK 3 T TENSOR
REMARK 3 T11: 0.2019 T22: 0.7735
REMARK 3 T33: 0.3409 T12: 0.0389
REMARK 3 T13: -0.0349 T23: -0.1281
REMARK 3 L TENSOR
REMARK 3 L11: 2.0800 L22: 2.6847
REMARK 3 L33: 3.0680 L12: 2.3606
REMARK 3 L13: 0.2306 L23: 0.1740
REMARK 3 S TENSOR
REMARK 3 S11: -0.1303 S12: -0.2621 S13: -0.0826
REMARK 3 S21: 0.1416 S22: 0.1300 S23: -0.5874
REMARK 3 S31: 0.2686 S32: 0.9057 S33: -0.0235
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: (CHAIN B AND RESID 71:81)
REMARK 3 ORIGIN FOR THE GROUP (A): 158.1579 49.6307 68.8380
REMARK 3 T TENSOR
REMARK 3 T11: 0.5150 T22: 0.9144
REMARK 3 T33: 0.7109 T12: -0.2434
REMARK 3 T13: -0.0428 T23: -0.2264
REMARK 3 L TENSOR
REMARK 3 L11: 3.9208 L22: 3.5159
REMARK 3 L33: 3.9361 L12: -3.4057
REMARK 3 L13: 0.8913 L23: 0.6648
REMARK 3 S TENSOR
REMARK 3 S11: -0.1419 S12: -0.7053 S13: 1.6062
REMARK 3 S21: 0.4607 S22: -0.0370 S23: -1.1764
REMARK 3 S31: -0.7803 S32: 0.9499 S33: 0.2200
REMARK 3 TLS GROUP : 24
REMARK 3 SELECTION: (CHAIN B AND RESID 82:92)
REMARK 3 ORIGIN FOR THE GROUP (A): 144.0246 56.6394 79.7785
REMARK 3 T TENSOR
REMARK 3 T11: 0.3057 T22: 0.5052
REMARK 3 T33: 0.7655 T12: -0.0933
REMARK 3 T13: 0.0214 T23: -0.1520
REMARK 3 L TENSOR
REMARK 3 L11: 3.5710 L22: 6.5890
REMARK 3 L33: 2.3706 L12: 0.2491
REMARK 3 L13: 2.7797 L23: -0.9598
REMARK 3 S TENSOR
REMARK 3 S11: 0.5284 S12: -0.9290 S13: 0.3679
REMARK 3 S21: -0.5576 S22: 0.2412 S23: -1.1211
REMARK 3 S31: 0.1733 S32: 0.2393 S33: -0.4844
REMARK 3 TLS GROUP : 25
REMARK 3 SELECTION: (CHAIN B AND RESID 93:110)
REMARK 3 ORIGIN FOR THE GROUP (A): 134.7724 69.3801 75.3783
REMARK 3 T TENSOR
REMARK 3 T11: 0.4633 T22: 0.3454
REMARK 3 T33: 0.4730 T12: -0.1539
REMARK 3 T13: 0.0274 T23: -0.1413
REMARK 3 L TENSOR
REMARK 3 L11: 2.1773 L22: 3.0195
REMARK 3 L33: 7.9344 L12: -0.9454
REMARK 3 L13: 3.1181 L23: -0.2653
REMARK 3 S TENSOR
REMARK 3 S11: -0.4172 S12: -0.0142 S13: 0.1133
REMARK 3 S21: -0.0233 S22: 0.1838 S23: -0.2831
REMARK 3 S31: -1.4277 S32: 0.3633 S33: 0.1984
REMARK 3 TLS GROUP : 26
REMARK 3 SELECTION: (CHAIN B AND RESID 111:122)
REMARK 3 ORIGIN FOR THE GROUP (A): 138.4543 57.6548 66.9495
REMARK 3 T TENSOR
REMARK 3 T11: 0.3196 T22: 0.5267
REMARK 3 T33: 0.4322 T12: -0.1978
REMARK 3 T13: 0.0503 T23: -0.1378
REMARK 3 L TENSOR
REMARK 3 L11: 0.1062 L22: 7.5515
REMARK 3 L33: 1.8496 L12: -0.9104
REMARK 3 L13: 0.3597 L23: -2.2759
REMARK 3 S TENSOR
REMARK 3 S11: -0.1445 S12: -0.2253 S13: 0.1486
REMARK 3 S21: -0.3097 S22: -0.1495 S23: -1.4516
REMARK 3 S31: 0.0952 S32: 0.9472 S33: 0.0800
REMARK 3 TLS GROUP : 27
REMARK 3 SELECTION: (CHAIN B AND RESID 123:160)
REMARK 3 ORIGIN FOR THE GROUP (A): 135.2537 31.3346 63.6573
REMARK 3 T TENSOR
REMARK 3 T11: 0.1588 T22: 0.2194
REMARK 3 T33: 0.1472 T12: 0.0389
REMARK 3 T13: 0.0171 T23: -0.0079
REMARK 3 L TENSOR
REMARK 3 L11: 3.1237 L22: 1.0088
REMARK 3 L33: 3.8509 L12: 0.3487
REMARK 3 L13: 1.1391 L23: 0.6551
REMARK 3 S TENSOR
REMARK 3 S11: -0.1086 S12: -0.3188 S13: -0.0357
REMARK 3 S21: 0.0576 S22: 0.1025 S23: -0.1077
REMARK 3 S31: 0.1679 S32: 0.4343 S33: 0.0131
REMARK 3 TLS GROUP : 28
REMARK 3 SELECTION: (CHAIN B AND RESID 161:186)
REMARK 3 ORIGIN FOR THE GROUP (A): 132.6905 29.2496 89.0552
REMARK 3 T TENSOR
REMARK 3 T11: 0.3784 T22: 0.5241
REMARK 3 T33: 0.1801 T12: 0.1528
REMARK 3 T13: -0.0335 T23: 0.0457
REMARK 3 L TENSOR
REMARK 3 L11: 5.9888 L22: 2.9250
REMARK 3 L33: 2.3164 L12: -2.7182
REMARK 3 L13: -2.8583 L23: 1.5370
REMARK 3 S TENSOR
REMARK 3 S11: -0.1268 S12: -0.2513 S13: -0.3048
REMARK 3 S21: 0.4606 S22: -0.0744 S23: 0.0785
REMARK 3 S31: 0.6260 S32: 0.3151 S33: 0.1453
REMARK 3 TLS GROUP : 29
REMARK 3 SELECTION: (CHAIN B AND RESID 187:212)
REMARK 3 ORIGIN FOR THE GROUP (A): 119.2381 47.6569 79.1308
REMARK 3 T TENSOR
REMARK 3 T11: 0.1785 T22: 0.2620
REMARK 3 T33: 0.1589 T12: -0.0014
REMARK 3 T13: 0.0005 T23: -0.0297
REMARK 3 L TENSOR
REMARK 3 L11: 1.2494 L22: 1.1455
REMARK 3 L33: 1.8573 L12: -0.8385
REMARK 3 L13: -0.3281 L23: 0.9959
REMARK 3 S TENSOR
REMARK 3 S11: -0.0586 S12: -0.2696 S13: 0.0301
REMARK 3 S21: 0.1581 S22: 0.0580 S23: -0.0699
REMARK 3 S31: -0.0556 S32: 0.1208 S33: -0.0238
REMARK 3 TLS GROUP : 30
REMARK 3 SELECTION: (CHAIN B AND RESID 213:222)
REMARK 3 ORIGIN FOR THE GROUP (A): 120.6625 28.9893 67.2786
REMARK 3 T TENSOR
REMARK 3 T11: 0.2735 T22: 0.2161
REMARK 3 T33: 0.2500 T12: 0.0218
REMARK 3 T13: 0.0606 T23: 0.0327
REMARK 3 L TENSOR
REMARK 3 L11: 6.3030 L22: 3.9267
REMARK 3 L33: 7.4950 L12: -3.8533
REMARK 3 L13: 1.9292 L23: -3.5308
REMARK 3 S TENSOR
REMARK 3 S11: -0.1686 S12: -0.2755 S13: -0.6259
REMARK 3 S21: 0.1468 S22: 0.1180 S23: 1.1901
REMARK 3 S31: 0.1742 S32: -0.5033 S33: 0.0065
REMARK 3 TLS GROUP : 31
REMARK 3 SELECTION: (CHAIN B AND RESID 223:267)
REMARK 3 ORIGIN FOR THE GROUP (A): 104.7873 45.3900 62.5597
REMARK 3 T TENSOR
REMARK 3 T11: 0.1760 T22: 0.1908
REMARK 3 T33: 0.1834 T12: 0.0053
REMARK 3 T13: -0.0022 T23: -0.0271
REMARK 3 L TENSOR
REMARK 3 L11: 3.5450 L22: 0.8367
REMARK 3 L33: 2.3906 L12: -0.7504
REMARK 3 L13: -1.3576 L23: 0.3882
REMARK 3 S TENSOR
REMARK 3 S11: 0.0938 S12: 0.0336 S13: -0.0902
REMARK 3 S21: -0.0863 S22: -0.1241 S23: 0.1276
REMARK 3 S31: -0.0075 S32: -0.2864 S33: 0.0298
REMARK 3 TLS GROUP : 32
REMARK 3 SELECTION: (CHAIN B AND RESID 268:278)
REMARK 3 ORIGIN FOR THE GROUP (A): 101.1803 34.9086 70.2589
REMARK 3 T TENSOR
REMARK 3 T11: 0.1567 T22: 0.2607
REMARK 3 T33: 0.3358 T12: 0.0112
REMARK 3 T13: 0.0124 T23: 0.0719
REMARK 3 L TENSOR
REMARK 3 L11: 6.3623 L22: 7.4580
REMARK 3 L33: 6.9741 L12: 0.4268
REMARK 3 L13: 0.8407 L23: -4.7497
REMARK 3 S TENSOR
REMARK 3 S11: -0.1243 S12: -0.0087 S13: -0.7419
REMARK 3 S21: 0.0176 S22: 0.6080 S23: 0.4591
REMARK 3 S31: 0.0187 S32: -0.7376 S33: -0.4013
REMARK 3 TLS GROUP : 33
REMARK 3 SELECTION: (CHAIN B AND RESID 279:364)
REMARK 3 ORIGIN FOR THE GROUP (A): 112.3792 53.5537 66.0553
REMARK 3 T TENSOR
REMARK 3 T11: 0.2007 T22: 0.1609
REMARK 3 T33: 0.1971 T12: 0.0319
REMARK 3 T13: 0.0140 T23: -0.0424
REMARK 3 L TENSOR
REMARK 3 L11: 1.3237 L22: 0.5256
REMARK 3 L33: 1.5942 L12: -0.0012
REMARK 3 L13: 0.0189 L23: 0.1056
REMARK 3 S TENSOR
REMARK 3 S11: 0.0214 S12: -0.1487 S13: 0.1509
REMARK 3 S21: -0.0106 S22: 0.0014 S23: 0.0101
REMARK 3 S31: -0.2832 S32: -0.0952 S33: 0.0035
REMARK 3 TLS GROUP : 34
REMARK 3 SELECTION: (CHAIN B AND RESID 365:394)
REMARK 3 ORIGIN FOR THE GROUP (A): 128.1029 46.1269 70.1986
REMARK 3 T TENSOR
REMARK 3 T11: 0.1572 T22: 0.2695
REMARK 3 T33: 0.1951 T12: -0.0218
REMARK 3 T13: -0.0244 T23: -0.0490
REMARK 3 L TENSOR
REMARK 3 L11: 0.8163 L22: 0.8624
REMARK 3 L33: 1.6707 L12: -0.6720
REMARK 3 L13: -0.2774 L23: 0.5848
REMARK 3 S TENSOR
REMARK 3 S11: -0.0500 S12: -0.2680 S13: 0.0552
REMARK 3 S21: 0.0846 S22: 0.0243 S23: -0.1356
REMARK 3 S31: -0.0991 S32: 0.2233 S33: 0.0097
REMARK 3 TLS GROUP : 35
REMARK 3 SELECTION: (CHAIN B AND RESID 395:407)
REMARK 3 ORIGIN FOR THE GROUP (A): 105.5021 45.6332 90.1123
REMARK 3 T TENSOR
REMARK 3 T11: 0.4351 T22: 0.5073
REMARK 3 T33: 0.3118 T12: 0.0968
REMARK 3 T13: 0.0369 T23: 0.0486
REMARK 3 L TENSOR
REMARK 3 L11: 2.1241 L22: 6.4898
REMARK 3 L33: 2.0775 L12: 1.6491
REMARK 3 L13: 0.0063 L23: 0.4783
REMARK 3 S TENSOR
REMARK 3 S11: -0.0237 S12: -0.7254 S13: 0.1415
REMARK 3 S21: 1.0183 S22: 0.2557 S23: 0.6373
REMARK 3 S31: 0.1789 S32: -0.4608 S33: -0.2870
REMARK 3 TLS GROUP : 36
REMARK 3 SELECTION: (CHAIN B AND RESID 408:430)
REMARK 3 ORIGIN FOR THE GROUP (A): 104.8785 50.4812 83.5413
REMARK 3 T TENSOR
REMARK 3 T11: 0.2667 T22: 0.4035
REMARK 3 T33: 0.2274 T12: 0.0543
REMARK 3 T13: 0.0403 T23: -0.0662
REMARK 3 L TENSOR
REMARK 3 L11: 5.1270 L22: 1.7653
REMARK 3 L33: 2.1719 L12: 0.5378
REMARK 3 L13: 1.9754 L23: -1.2203
REMARK 3 S TENSOR
REMARK 3 S11: -0.1755 S12: -0.5715 S13: 0.0247
REMARK 3 S21: 0.1056 S22: 0.2572 S23: 0.0550
REMARK 3 S31: -0.1167 S32: -0.3878 S33: -0.0607
REMARK 3 TLS GROUP : 37
REMARK 3 SELECTION: (CHAIN B AND RESID 431:482)
REMARK 3 ORIGIN FOR THE GROUP (A): 133.8685 37.1691 83.3225
REMARK 3 T TENSOR
REMARK 3 T11: 0.2187 T22: 0.4132
REMARK 3 T33: 0.1967 T12: 0.0521
REMARK 3 T13: -0.0449 T23: -0.0229
REMARK 3 L TENSOR
REMARK 3 L11: 0.6696 L22: 0.5572
REMARK 3 L33: 1.7072 L12: -0.3200
REMARK 3 L13: -0.2962 L23: 0.4560
REMARK 3 S TENSOR
REMARK 3 S11: -0.0174 S12: -0.3350 S13: 0.0086
REMARK 3 S21: 0.1876 S22: 0.1240 S23: -0.0998
REMARK 3 S31: 0.0481 S32: 0.3572 S33: -0.0970
REMARK 3 TLS GROUP : 38
REMARK 3 SELECTION: (CHAIN B AND RESID 483:493)
REMARK 3 ORIGIN FOR THE GROUP (A): 137.9279 36.8379 96.8067
REMARK 3 T TENSOR
REMARK 3 T11: 0.3310 T22: 0.8217
REMARK 3 T33: 0.2939 T12: 0.1271
REMARK 3 T13: -0.0758 T23: -0.0289
REMARK 3 L TENSOR
REMARK 3 L11: 0.5190 L22: 7.1883
REMARK 3 L33: 3.8744 L12: -1.3943
REMARK 3 L13: -0.3848 L23: -1.5168
REMARK 3 S TENSOR
REMARK 3 S11: -0.2161 S12: -0.4844 S13: 0.0501
REMARK 3 S21: 0.9751 S22: 0.4559 S23: -0.4770
REMARK 3 S31: 0.0260 S32: 0.1892 S33: -0.2013
REMARK 3 TLS GROUP : 39
REMARK 3 SELECTION: (CHAIN B AND RESID 494:578)
REMARK 3 ORIGIN FOR THE GROUP (A): 125.3666 51.9525 72.1259
REMARK 3 T TENSOR
REMARK 3 T11: 0.2147 T22: 0.2332
REMARK 3 T33: 0.2132 T12: -0.0339
REMARK 3 T13: 0.0148 T23: -0.0883
REMARK 3 L TENSOR
REMARK 3 L11: 0.8025 L22: 0.7835
REMARK 3 L33: 1.2765 L12: -0.3096
REMARK 3 L13: -0.0584 L23: -0.2200
REMARK 3 S TENSOR
REMARK 3 S11: -0.0186 S12: -0.2517 S13: 0.1939
REMARK 3 S21: 0.1080 S22: 0.0487 S23: -0.1119
REMARK 3 S31: -0.1992 S32: 0.1453 S33: -0.0271
REMARK 3 TLS GROUP : 40
REMARK 3 SELECTION: (CHAIN B AND RESID 579:583)
REMARK 3 ORIGIN FOR THE GROUP (A): 118.5406 59.7019 83.9227
REMARK 3 T TENSOR
REMARK 3 T11: 0.3937 T22: 0.4449
REMARK 3 T33: 0.3818 T12: -0.0263
REMARK 3 T13: 0.0386 T23: -0.1433
REMARK 3 L TENSOR
REMARK 3 L11: 8.4132 L22: 9.2162
REMARK 3 L33: 4.5989 L12: -2.0353
REMARK 3 L13: 1.9876 L23: -5.9916
REMARK 3 S TENSOR
REMARK 3 S11: 0.2317 S12: -0.5210 S13: 1.3520
REMARK 3 S21: 0.9792 S22: 0.5138 S23: -0.3704
REMARK 3 S31: -1.9712 S32: 1.0101 S33: -0.7104
REMARK 3 TLS GROUP : 41
REMARK 3 SELECTION: (CHAIN C AND RESID 33:45)
REMARK 3 ORIGIN FOR THE GROUP (A): 87.3619 36.9405 25.3909
REMARK 3 T TENSOR
REMARK 3 T11: 0.2483 T22: 0.4296
REMARK 3 T33: 0.2240 T12: -0.0822
REMARK 3 T13: 0.0381 T23: -0.0047
REMARK 3 L TENSOR
REMARK 3 L11: 1.8065 L22: 8.3217
REMARK 3 L33: 2.6578 L12: -0.9985
REMARK 3 L13: 1.0955 L23: -1.0561
REMARK 3 S TENSOR
REMARK 3 S11: 0.0129 S12: 0.1911 S13: 0.1711
REMARK 3 S21: -0.3458 S22: -0.0347 S23: -0.3309
REMARK 3 S31: -0.3736 S32: 0.3610 S33: 0.0363
REMARK 3 TLS GROUP : 42
REMARK 3 SELECTION: (CHAIN C AND RESID 46:56)
REMARK 3 ORIGIN FOR THE GROUP (A): 90.9037 43.0176 31.2082
REMARK 3 T TENSOR
REMARK 3 T11: 0.2688 T22: 0.4165
REMARK 3 T33: 0.2570 T12: -0.1506
REMARK 3 T13: 0.0462 T23: -0.0062
REMARK 3 L TENSOR
REMARK 3 L11: 4.9042 L22: 7.6819
REMARK 3 L33: 3.8014 L12: -3.7371
REMARK 3 L13: -0.1334 L23: 4.2985
REMARK 3 S TENSOR
REMARK 3 S11: -0.0739 S12: 0.2321 S13: 0.0675
REMARK 3 S21: -0.4564 S22: 0.2195 S23: -0.7658
REMARK 3 S31: -0.3484 S32: 0.3961 S33: -0.0979
REMARK 3 TLS GROUP : 43
REMARK 3 SELECTION: (CHAIN C AND RESID 57:73)
REMARK 3 ORIGIN FOR THE GROUP (A): 94.4592 28.2953 30.1416
REMARK 3 T TENSOR
REMARK 3 T11: 0.1864 T22: 0.4806
REMARK 3 T33: 0.2530 T12: 0.0242
REMARK 3 T13: 0.0279 T23: -0.0586
REMARK 3 L TENSOR
REMARK 3 L11: 5.5041 L22: 1.4165
REMARK 3 L33: 4.5431 L12: -0.1573
REMARK 3 L13: -2.5370 L23: 1.3243
REMARK 3 S TENSOR
REMARK 3 S11: 0.0470 S12: 0.2816 S13: -0.2170
REMARK 3 S21: -0.3003 S22: 0.1845 S23: -0.2931
REMARK 3 S31: 0.2031 S32: 0.9144 S33: -0.2219
REMARK 3 TLS GROUP : 44
REMARK 3 SELECTION: (CHAIN C AND RESID 74:83)
REMARK 3 ORIGIN FOR THE GROUP (A): 95.1360 15.1701 25.3831
REMARK 3 T TENSOR
REMARK 3 T11: 0.4885 T22: 0.5890
REMARK 3 T33: 0.6936 T12: 0.2063
REMARK 3 T13: 0.0295 T23: -0.0991
REMARK 3 L TENSOR
REMARK 3 L11: 9.3836 L22: 5.1418
REMARK 3 L33: 6.8817 L12: 0.9855
REMARK 3 L13: 3.3220 L23: 2.0570
REMARK 3 S TENSOR
REMARK 3 S11: 0.3517 S12: 1.1886 S13: -0.6940
REMARK 3 S21: 0.0558 S22: 0.0184 S23: -1.0394
REMARK 3 S31: 1.1488 S32: 0.5609 S33: -0.3711
REMARK 3 TLS GROUP : 45
REMARK 3 SELECTION: (CHAIN C AND RESID 84:89)
REMARK 3 ORIGIN FOR THE GROUP (A): 82.7434 12.4760 15.8289
REMARK 3 T TENSOR
REMARK 3 T11: 0.3122 T22: 0.4190
REMARK 3 T33: 0.6806 T12: 0.0891
REMARK 3 T13: 0.0310 T23: -0.1043
REMARK 3 L TENSOR
REMARK 3 L11: 3.8186 L22: 4.8343
REMARK 3 L33: 1.4175 L12: -1.0824
REMARK 3 L13: 0.6672 L23: 2.2229
REMARK 3 S TENSOR
REMARK 3 S11: 0.7163 S12: 0.7336 S13: -0.9175
REMARK 3 S21: -0.2481 S22: -0.0689 S23: -1.0840
REMARK 3 S31: 0.2276 S32: 0.7427 S33: -0.6210
REMARK 3 TLS GROUP : 46
REMARK 3 SELECTION: (CHAIN C AND RESID 90:114)
REMARK 3 ORIGIN FOR THE GROUP (A): 74.5027 0.0941 20.6475
REMARK 3 T TENSOR
REMARK 3 T11: 0.2516 T22: 0.2442
REMARK 3 T33: 0.3791 T12: 0.0809
REMARK 3 T13: 0.0422 T23: -0.0336
REMARK 3 L TENSOR
REMARK 3 L11: 2.6700 L22: 2.4941
REMARK 3 L33: 5.1812 L12: 0.5260
REMARK 3 L13: -2.3229 L23: 0.2860
REMARK 3 S TENSOR
REMARK 3 S11: -0.2586 S12: 0.1394 S13: -0.0989
REMARK 3 S21: -0.0378 S22: 0.0639 S23: -0.1737
REMARK 3 S31: 0.6553 S32: -0.1804 S33: 0.2099
REMARK 3 TLS GROUP : 47
REMARK 3 SELECTION: (CHAIN C AND RESID 115:122)
REMARK 3 ORIGIN FOR THE GROUP (A): 78.1245 12.5779 28.4100
REMARK 3 T TENSOR
REMARK 3 T11: 0.3957 T22: 0.4956
REMARK 3 T33: 0.5169 T12: 0.0388
REMARK 3 T13: -0.0456 T23: 0.0025
REMARK 3 L TENSOR
REMARK 3 L11: 3.8149 L22: 3.4312
REMARK 3 L33: 4.5337 L12: 3.3987
REMARK 3 L13: 2.2186 L23: 1.2878
REMARK 3 S TENSOR
REMARK 3 S11: 0.0878 S12: -0.5330 S13: -0.2016
REMARK 3 S21: 0.2587 S22: 0.4305 S23: -1.4099
REMARK 3 S31: 0.1846 S32: 0.6902 S33: -0.3418
REMARK 3 TLS GROUP : 48
REMARK 3 SELECTION: (CHAIN C AND RESID 123:156)
REMARK 3 ORIGIN FOR THE GROUP (A): 73.1097 34.6584 33.4998
REMARK 3 T TENSOR
REMARK 3 T11: 0.1290 T22: 0.1235
REMARK 3 T33: 0.1219 T12: -0.0280
REMARK 3 T13: -0.0059 T23: 0.0043
REMARK 3 L TENSOR
REMARK 3 L11: 2.1445 L22: 1.2912
REMARK 3 L33: 3.0372 L12: 0.7753
REMARK 3 L13: -0.1026 L23: -0.5265
REMARK 3 S TENSOR
REMARK 3 S11: -0.0506 S12: 0.0984 S13: -0.0659
REMARK 3 S21: 0.0573 S22: 0.0199 S23: -0.1223
REMARK 3 S31: -0.0844 S32: 0.2725 S33: 0.0367
REMARK 3 TLS GROUP : 49
REMARK 3 SELECTION: (CHAIN C AND RESID 157:174)
REMARK 3 ORIGIN FOR THE GROUP (A): 78.3896 44.5327 14.7577
REMARK 3 T TENSOR
REMARK 3 T11: 0.3517 T22: 0.3552
REMARK 3 T33: 0.2964 T12: -0.1160
REMARK 3 T13: -0.0197 T23: 0.0714
REMARK 3 L TENSOR
REMARK 3 L11: 6.1825 L22: 2.0176
REMARK 3 L33: 3.2170 L12: 3.3947
REMARK 3 L13: 3.6689 L23: 1.6294
REMARK 3 S TENSOR
REMARK 3 S11: -0.5213 S12: 0.5827 S13: 0.5763
REMARK 3 S21: -0.3179 S22: 0.1453 S23: 0.0252
REMARK 3 S31: -0.5477 S32: 0.4766 S33: 0.4206
REMARK 3 TLS GROUP : 50
REMARK 3 SELECTION: (CHAIN C AND RESID 175:214)
REMARK 3 ORIGIN FOR THE GROUP (A): 59.8882 24.7280 12.7657
REMARK 3 T TENSOR
REMARK 3 T11: 0.1393 T22: 0.2126
REMARK 3 T33: 0.1650 T12: 0.0049
REMARK 3 T13: -0.0265 T23: 0.0137
REMARK 3 L TENSOR
REMARK 3 L11: 0.9688 L22: 1.3596
REMARK 3 L33: 1.5340 L12: 0.7021
REMARK 3 L13: -0.0723 L23: -0.1361
REMARK 3 S TENSOR
REMARK 3 S11: -0.0967 S12: 0.1685 S13: 0.0675
REMARK 3 S21: -0.1399 S22: 0.0433 S23: 0.0843
REMARK 3 S31: -0.0709 S32: 0.0182 S33: 0.0511
REMARK 3 TLS GROUP : 51
REMARK 3 SELECTION: (CHAIN C AND RESID 215:228)
REMARK 3 ORIGIN FOR THE GROUP (A): 60.1120 33.7197 31.2592
REMARK 3 T TENSOR
REMARK 3 T11: 0.1286 T22: 0.1901
REMARK 3 T33: 0.2047 T12: 0.0116
REMARK 3 T13: 0.0105 T23: 0.0104
REMARK 3 L TENSOR
REMARK 3 L11: 3.7354 L22: 7.6033
REMARK 3 L33: 5.7221 L12: 3.2764
REMARK 3 L13: -0.9353 L23: -2.4657
REMARK 3 S TENSOR
REMARK 3 S11: 0.0658 S12: 0.0180 S13: 0.5265
REMARK 3 S21: 0.3877 S22: -0.0721 S23: 0.4892
REMARK 3 S31: -0.4399 S32: -0.3574 S33: 0.0361
REMARK 3 TLS GROUP : 52
REMARK 3 SELECTION: (CHAIN C AND RESID 229:271)
REMARK 3 ORIGIN FOR THE GROUP (A): 41.1125 21.7877 33.3976
REMARK 3 T TENSOR
REMARK 3 T11: 0.1526 T22: 0.1566
REMARK 3 T33: 0.1978 T12: 0.0140
REMARK 3 T13: 0.0185 T23: -0.0228
REMARK 3 L TENSOR
REMARK 3 L11: 3.8742 L22: 1.0040
REMARK 3 L33: 3.1686 L12: 0.0908
REMARK 3 L13: 1.2781 L23: 0.6177
REMARK 3 S TENSOR
REMARK 3 S11: -0.0967 S12: -0.0008 S13: 0.1655
REMARK 3 S21: -0.0383 S22: -0.0632 S23: 0.0932
REMARK 3 S31: -0.0941 S32: -0.3253 S33: 0.1558
REMARK 3 TLS GROUP : 53
REMARK 3 SELECTION: (CHAIN C AND RESID 272:289)
REMARK 3 ORIGIN FOR THE GROUP (A): 39.5393 30.3777 23.0594
REMARK 3 T TENSOR
REMARK 3 T11: 0.2191 T22: 0.2142
REMARK 3 T33: 0.2603 T12: 0.0306
REMARK 3 T13: -0.0346 T23: 0.0082
REMARK 3 L TENSOR
REMARK 3 L11: 2.3946 L22: 4.7289
REMARK 3 L33: 5.9862 L12: -1.6189
REMARK 3 L13: 3.6268 L23: -2.9899
REMARK 3 S TENSOR
REMARK 3 S11: -0.1471 S12: -0.0314 S13: 0.5217
REMARK 3 S21: -0.1415 S22: 0.0468 S23: 0.1104
REMARK 3 S31: -0.3927 S32: -0.3721 S33: 0.0376
REMARK 3 TLS GROUP : 54
REMARK 3 SELECTION: (CHAIN C AND RESID 290:357)
REMARK 3 ORIGIN FOR THE GROUP (A): 51.3557 12.3421 30.7006
REMARK 3 T TENSOR
REMARK 3 T11: 0.1492 T22: 0.1202
REMARK 3 T33: 0.1765 T12: -0.0306
REMARK 3 T13: -0.0038 T23: -0.0412
REMARK 3 L TENSOR
REMARK 3 L11: 0.9991 L22: 0.5104
REMARK 3 L33: 2.2080 L12: -0.0599
REMARK 3 L13: -0.4456 L23: 0.0781
REMARK 3 S TENSOR
REMARK 3 S11: 0.0051 S12: 0.0456 S13: -0.0880
REMARK 3 S21: 0.0304 S22: -0.0007 S23: 0.0686
REMARK 3 S31: 0.1868 S32: -0.1278 S33: 0.0392
REMARK 3 TLS GROUP : 55
REMARK 3 SELECTION: (CHAIN C AND RESID 358:407)
REMARK 3 ORIGIN FOR THE GROUP (A): 60.7567 19.0755 21.1041
REMARK 3 T TENSOR
REMARK 3 T11: 0.1291 T22: 0.2021
REMARK 3 T33: 0.1535 T12: 0.0126
REMARK 3 T13: 0.0444 T23: -0.0258
REMARK 3 L TENSOR
REMARK 3 L11: 1.4494 L22: 0.7691
REMARK 3 L33: 2.5138 L12: 0.1921
REMARK 3 L13: 1.1393 L23: -0.3365
REMARK 3 S TENSOR
REMARK 3 S11: -0.0014 S12: 0.2544 S13: -0.0740
REMARK 3 S21: -0.1516 S22: 0.0263 S23: 0.0220
REMARK 3 S31: 0.1269 S32: 0.0035 S33: -0.0372
REMARK 3 TLS GROUP : 56
REMARK 3 SELECTION: (CHAIN C AND RESID 408:430)
REMARK 3 ORIGIN FOR THE GROUP (A): 43.5006 16.7380 12.3599
REMARK 3 T TENSOR
REMARK 3 T11: 0.2034 T22: 0.2578
REMARK 3 T33: 0.2116 T12: -0.0591
REMARK 3 T13: -0.0548 T23: -0.0318
REMARK 3 L TENSOR
REMARK 3 L11: 6.5983 L22: 2.6184
REMARK 3 L33: 3.1667 L12: -1.6613
REMARK 3 L13: -2.2255 L23: -1.4240
REMARK 3 S TENSOR
REMARK 3 S11: -0.0993 S12: 0.2882 S13: -0.0891
REMARK 3 S21: -0.1130 S22: 0.1553 S23: 0.2742
REMARK 3 S31: 0.1013 S32: -0.4118 S33: -0.0729
REMARK 3 TLS GROUP : 57
REMARK 3 SELECTION: (CHAIN C AND RESID 431:482)
REMARK 3 ORIGIN FOR THE GROUP (A): 72.3918 30.3366 12.6720
REMARK 3 T TENSOR
REMARK 3 T11: 0.1739 T22: 0.2726
REMARK 3 T33: 0.1464 T12: -0.0326
REMARK 3 T13: 0.0211 T23: 0.0356
REMARK 3 L TENSOR
REMARK 3 L11: 0.9871 L22: 0.4849
REMARK 3 L33: 1.4525 L12: 0.1126
REMARK 3 L13: 0.8048 L23: 0.1215
REMARK 3 S TENSOR
REMARK 3 S11: -0.0211 S12: 0.2340 S13: 0.0533
REMARK 3 S21: -0.0667 S22: 0.0151 S23: -0.0387
REMARK 3 S31: -0.0581 S32: 0.2513 S33: 0.0077
REMARK 3 TLS GROUP : 58
REMARK 3 SELECTION: (CHAIN C AND RESID 483:506)
REMARK 3 ORIGIN FOR THE GROUP (A): 76.6128 32.9635 5.2764
REMARK 3 T TENSOR
REMARK 3 T11: 0.2125 T22: 0.3700
REMARK 3 T33: 0.1584 T12: -0.0722
REMARK 3 T13: 0.0079 T23: 0.0346
REMARK 3 L TENSOR
REMARK 3 L11: 1.6756 L22: 3.0565
REMARK 3 L33: 5.7346 L12: -0.1475
REMARK 3 L13: -0.0779 L23: -0.3917
REMARK 3 S TENSOR
REMARK 3 S11: -0.0620 S12: 0.5267 S13: 0.2423
REMARK 3 S21: -0.3058 S22: 0.0172 S23: -0.1972
REMARK 3 S31: -0.2597 S32: 0.2461 S33: 0.0459
REMARK 3 TLS GROUP : 59
REMARK 3 SELECTION: (CHAIN C AND RESID 507:577)
REMARK 3 ORIGIN FOR THE GROUP (A): 61.7497 11.6342 26.5855
REMARK 3 T TENSOR
REMARK 3 T11: 0.1926 T22: 0.1698
REMARK 3 T33: 0.1877 T12: -0.0013
REMARK 3 T13: 0.0099 T23: -0.0466
REMARK 3 L TENSOR
REMARK 3 L11: 0.4262 L22: 1.0251
REMARK 3 L33: 0.4126 L12: 0.3073
REMARK 3 L13: 0.2322 L23: -0.1793
REMARK 3 S TENSOR
REMARK 3 S11: -0.0352 S12: 0.0886 S13: -0.1190
REMARK 3 S21: -0.0299 S22: 0.0142 S23: -0.0637
REMARK 3 S31: 0.1549 S32: 0.0081 S33: 0.0551
REMARK 3 TLS GROUP : 60
REMARK 3 SELECTION: (CHAIN C AND RESID 578:582)
REMARK 3 ORIGIN FOR THE GROUP (A): 56.1143 8.2519 13.3808
REMARK 3 T TENSOR
REMARK 3 T11: 0.2465 T22: 0.2182
REMARK 3 T33: 0.2336 T12: -0.0324
REMARK 3 T13: 0.0261 T23: -0.0538
REMARK 3 L TENSOR
REMARK 3 L11: 6.3114 L22: 4.4202
REMARK 3 L33: 2.9471 L12: 2.0887
REMARK 3 L13: -0.6643 L23: -2.0263
REMARK 3 S TENSOR
REMARK 3 S11: -0.1824 S12: -0.0667 S13: -0.0066
REMARK 3 S21: -0.4078 S22: -0.1156 S23: -0.0162
REMARK 3 S31: 0.9717 S32: 0.1585 S33: 0.2629
REMARK 3 TLS GROUP : 61
REMARK 3 SELECTION: (CHAIN D AND RESID 33:52)
REMARK 3 ORIGIN FOR THE GROUP (A): 53.3589 4.5787 56.5277
REMARK 3 T TENSOR
REMARK 3 T11: 0.3886 T22: 0.2099
REMARK 3 T33: 0.2576 T12: -0.0924
REMARK 3 T13: 0.0091 T23: 0.0206
REMARK 3 L TENSOR
REMARK 3 L11: 3.1134 L22: 1.0340
REMARK 3 L33: 2.4075 L12: -0.9332
REMARK 3 L13: 1.8973 L23: 0.4225
REMARK 3 S TENSOR
REMARK 3 S11: 0.0496 S12: -0.2840 S13: -0.2126
REMARK 3 S21: 0.2186 S22: -0.0614 S23: 0.0649
REMARK 3 S31: 0.3382 S32: -0.3056 S33: 0.0276
REMARK 3 TLS GROUP : 62
REMARK 3 SELECTION: (CHAIN D AND RESID 53:80)
REMARK 3 ORIGIN FOR THE GROUP (A): 64.7910 -2.3145 55.0825
REMARK 3 T TENSOR
REMARK 3 T11: 0.4714 T22: 0.1412
REMARK 3 T33: 0.3287 T12: 0.0089
REMARK 3 T13: -0.0908 T23: 0.0322
REMARK 3 L TENSOR
REMARK 3 L11: 4.7235 L22: 3.6646
REMARK 3 L33: 4.5549 L12: -3.0529
REMARK 3 L13: 0.4861 L23: -0.7600
REMARK 3 S TENSOR
REMARK 3 S11: 0.0786 S12: -0.1090 S13: -0.8000
REMARK 3 S21: 0.3329 S22: -0.0863 S23: -0.2915
REMARK 3 S31: 0.7662 S32: 0.1082 S33: 0.0282
REMARK 3 TLS GROUP : 63
REMARK 3 SELECTION: (CHAIN D AND RESID 81:99)
REMARK 3 ORIGIN FOR THE GROUP (A): 85.0985 11.3794 69.0529
REMARK 3 T TENSOR
REMARK 3 T11: 0.2569 T22: 0.2678
REMARK 3 T33: 0.4639 T12: 0.0835
REMARK 3 T13: -0.0666 T23: 0.0370
REMARK 3 L TENSOR
REMARK 3 L11: 3.0557 L22: 6.5061
REMARK 3 L33: 4.7139 L12: -0.6215
REMARK 3 L13: -0.5605 L23: 0.2267
REMARK 3 S TENSOR
REMARK 3 S11: 0.4724 S12: 0.0974 S13: -0.5424
REMARK 3 S21: 0.5147 S22: -0.2350 S23: 0.1796
REMARK 3 S31: 0.6784 S32: 0.3823 S33: -0.2476
REMARK 3 TLS GROUP : 64
REMARK 3 SELECTION: (CHAIN D AND RESID 100:114)
REMARK 3 ORIGIN FOR THE GROUP (A): 94.4475 18.8108 58.8999
REMARK 3 T TENSOR
REMARK 3 T11: 0.2069 T22: 0.4744
REMARK 3 T33: 0.3505 T12: 0.1204
REMARK 3 T13: 0.0192 T23: 0.0488
REMARK 3 L TENSOR
REMARK 3 L11: 5.4431 L22: 4.8209
REMARK 3 L33: 5.1798 L12: -1.3935
REMARK 3 L13: 0.1240 L23: -1.7212
REMARK 3 S TENSOR
REMARK 3 S11: 0.1622 S12: 0.4235 S13: -0.3468
REMARK 3 S21: -0.3713 S22: -0.2127 S23: -0.2490
REMARK 3 S31: -0.0208 S32: 1.2977 S33: 0.0094
REMARK 3 TLS GROUP : 65
REMARK 3 SELECTION: (CHAIN D AND RESID 115:122)
REMARK 3 ORIGIN FOR THE GROUP (A): 79.7835 14.2229 55.8722
REMARK 3 T TENSOR
REMARK 3 T11: 0.5535 T22: 0.3128
REMARK 3 T33: 0.4457 T12: 0.1402
REMARK 3 T13: -0.0295 T23: -0.0989
REMARK 3 L TENSOR
REMARK 3 L11: 6.7510 L22: 3.3324
REMARK 3 L33: 4.2874 L12: 3.7673
REMARK 3 L13: -2.5072 L23: -0.0128
REMARK 3 S TENSOR
REMARK 3 S11: 0.0568 S12: 0.3698 S13: -1.3610
REMARK 3 S21: 0.0078 S22: 0.1835 S23: -0.6826
REMARK 3 S31: 1.1612 S32: 0.0940 S33: -0.1684
REMARK 3 TLS GROUP : 66
REMARK 3 SELECTION: (CHAIN D AND RESID 123:164)
REMARK 3 ORIGIN FOR THE GROUP (A): 55.9819 18.2253 53.4420
REMARK 3 T TENSOR
REMARK 3 T11: 0.1685 T22: 0.1195
REMARK 3 T33: 0.1746 T12: -0.0461
REMARK 3 T13: -0.0008 T23: -0.0123
REMARK 3 L TENSOR
REMARK 3 L11: 0.6572 L22: 1.8059
REMARK 3 L33: 3.5160 L12: -0.4367
REMARK 3 L13: 0.2451 L23: -0.5787
REMARK 3 S TENSOR
REMARK 3 S11: 0.0082 S12: -0.0498 S13: -0.0629
REMARK 3 S21: 0.0002 S22: -0.0665 S23: 0.0847
REMARK 3 S31: 0.2415 S32: -0.2816 S33: 0.0293
REMARK 3 TLS GROUP : 67
REMARK 3 SELECTION: (CHAIN D AND RESID 165:186)
REMARK 3 ORIGIN FOR THE GROUP (A): 55.0100 22.5755 79.0967
REMARK 3 T TENSOR
REMARK 3 T11: 0.2831 T22: 0.2757
REMARK 3 T33: 0.1468 T12: -0.1234
REMARK 3 T13: 0.0413 T23: 0.0191
REMARK 3 L TENSOR
REMARK 3 L11: 2.4625 L22: 7.2864
REMARK 3 L33: 2.8351 L12: 2.4275
REMARK 3 L13: 0.6660 L23: 2.4831
REMARK 3 S TENSOR
REMARK 3 S11: -0.0938 S12: -0.3485 S13: 0.1115
REMARK 3 S21: 0.1166 S22: -0.1435 S23: 0.4408
REMARK 3 S31: 0.2263 S32: -0.3979 S33: 0.1328
REMARK 3 TLS GROUP : 68
REMARK 3 SELECTION: (CHAIN D AND RESID 187:212)
REMARK 3 ORIGIN FOR THE GROUP (A): 73.1078 34.3975 67.7324
REMARK 3 T TENSOR
REMARK 3 T11: 0.1315 T22: 0.1379
REMARK 3 T33: 0.1758 T12: -0.0111
REMARK 3 T13: -0.0069 T23: -0.0036
REMARK 3 L TENSOR
REMARK 3 L11: 0.8320 L22: 1.0194
REMARK 3 L33: 1.4716 L12: 0.5228
REMARK 3 L13: 0.5729 L23: -0.0220
REMARK 3 S TENSOR
REMARK 3 S11: 0.0782 S12: -0.1199 S13: 0.0534
REMARK 3 S21: 0.0115 S22: -0.1142 S23: -0.0863
REMARK 3 S31: 0.0584 S32: 0.1290 S33: 0.0202
REMARK 3 TLS GROUP : 69
REMARK 3 SELECTION: (CHAIN D AND RESID 213:228)
REMARK 3 ORIGIN FOR THE GROUP (A): 58.2069 32.9078 54.1477
REMARK 3 T TENSOR
REMARK 3 T11: 0.1476 T22: 0.1347
REMARK 3 T33: 0.2450 T12: -0.0145
REMARK 3 T13: 0.0010 T23: -0.0292
REMARK 3 L TENSOR
REMARK 3 L11: 5.3175 L22: 3.5000
REMARK 3 L33: 6.0404 L12: 1.5110
REMARK 3 L13: -3.9754 L23: -0.4168
REMARK 3 S TENSOR
REMARK 3 S11: 0.2089 S12: 0.0279 S13: 0.7714
REMARK 3 S21: 0.1358 S22: -0.0088 S23: 0.3948
REMARK 3 S31: -0.3224 S32: -0.3507 S33: -0.1542
REMARK 3 TLS GROUP : 70
REMARK 3 SELECTION: (CHAIN D AND RESID 229:265)
REMARK 3 ORIGIN FOR THE GROUP (A): 72.1935 50.4881 51.0335
REMARK 3 T TENSOR
REMARK 3 T11: 0.1567 T22: 0.1069
REMARK 3 T33: 0.2150 T12: -0.0063
REMARK 3 T13: -0.0181 T23: 0.0215
REMARK 3 L TENSOR
REMARK 3 L11: 1.6849 L22: 2.7269
REMARK 3 L33: 3.4674 L12: 0.2463
REMARK 3 L13: 0.4946 L23: 0.7289
REMARK 3 S TENSOR
REMARK 3 S11: -0.0226 S12: 0.0121 S13: 0.1782
REMARK 3 S21: -0.0700 S22: -0.0355 S23: 0.0540
REMARK 3 S31: -0.2990 S32: -0.0840 S33: 0.0536
REMARK 3 TLS GROUP : 71
REMARK 3 SELECTION: (CHAIN D AND RESID 266:278)
REMARK 3 ORIGIN FOR THE GROUP (A): 61.0445 53.7395 58.5827
REMARK 3 T TENSOR
REMARK 3 T11: 0.1379 T22: 0.1601
REMARK 3 T33: 0.3530 T12: 0.0090
REMARK 3 T13: -0.0154 T23: -0.0192
REMARK 3 L TENSOR
REMARK 3 L11: 5.4964 L22: 5.6147
REMARK 3 L33: 7.6346 L12: -0.0151
REMARK 3 L13: -4.1480 L23: -1.7728
REMARK 3 S TENSOR
REMARK 3 S11: 0.0460 S12: -0.0948 S13: 0.2969
REMARK 3 S21: -0.1096 S22: -0.0520 S23: 0.2982
REMARK 3 S31: -0.3836 S32: -0.3371 S33: -0.0580
REMARK 3 TLS GROUP : 72
REMARK 3 SELECTION: (CHAIN D AND RESID 279:293)
REMARK 3 ORIGIN FOR THE GROUP (A): 65.0207 51.5148 61.0811
REMARK 3 T TENSOR
REMARK 3 T11: 0.1998 T22: 0.1578
REMARK 3 T33: 0.1725 T12: -0.0001
REMARK 3 T13: -0.0190 T23: 0.0094
REMARK 3 L TENSOR
REMARK 3 L11: 5.0651 L22: 5.6003
REMARK 3 L33: 8.4379 L12: -2.5363
REMARK 3 L13: -3.4671 L23: 3.9645
REMARK 3 S TENSOR
REMARK 3 S11: 0.1581 S12: -0.2200 S13: 0.2944
REMARK 3 S21: 0.0245 S22: 0.0006 S23: -0.0022
REMARK 3 S31: -0.6931 S32: -0.1973 S33: -0.0948
REMARK 3 TLS GROUP : 73
REMARK 3 SELECTION: (CHAIN D AND RESID 294:367)
REMARK 3 ORIGIN FOR THE GROUP (A): 82.0819 38.3390 53.1641
REMARK 3 T TENSOR
REMARK 3 T11: 0.1179 T22: 0.1698
REMARK 3 T33: 0.1861 T12: -0.0242
REMARK 3 T13: -0.0204 T23: -0.0065
REMARK 3 L TENSOR
REMARK 3 L11: 0.4337 L22: 0.6760
REMARK 3 L33: 1.4380 L12: -0.1494
REMARK 3 L13: -0.0927 L23: -0.1493
REMARK 3 S TENSOR
REMARK 3 S11: 0.0201 S12: -0.0032 S13: 0.0072
REMARK 3 S21: 0.0124 S22: -0.0301 S23: -0.0895
REMARK 3 S31: -0.0538 S32: 0.2725 S33: 0.0242
REMARK 3 TLS GROUP : 74
REMARK 3 SELECTION: (CHAIN D AND RESID 368:398)
REMARK 3 ORIGIN FOR THE GROUP (A): 70.7019 28.9293 62.4834
REMARK 3 T TENSOR
REMARK 3 T11: 0.1833 T22: 0.1422
REMARK 3 T33: 0.1886 T12: 0.0095
REMARK 3 T13: -0.0149 T23: 0.0249
REMARK 3 L TENSOR
REMARK 3 L11: 0.7019 L22: 1.6127
REMARK 3 L33: 2.1814 L12: 0.3574
REMARK 3 L13: 0.2376 L23: 1.2788
REMARK 3 S TENSOR
REMARK 3 S11: 0.0734 S12: -0.1091 S13: 0.0192
REMARK 3 S21: 0.1359 S22: -0.0776 S23: -0.0618
REMARK 3 S31: 0.0815 S32: 0.0375 S33: 0.0167
REMARK 3 TLS GROUP : 75
REMARK 3 SELECTION: (CHAIN D AND RESID 399:428)
REMARK 3 ORIGIN FOR THE GROUP (A): 73.8963 49.3726 73.8778
REMARK 3 T TENSOR
REMARK 3 T11: 0.2449 T22: 0.2579
REMARK 3 T33: 0.2001 T12: -0.0520
REMARK 3 T13: 0.0187 T23: -0.0418
REMARK 3 L TENSOR
REMARK 3 L11: 4.6329 L22: 3.9905
REMARK 3 L33: 2.1972 L12: -0.9618
REMARK 3 L13: -1.2032 L23: -1.2491
REMARK 3 S TENSOR
REMARK 3 S11: 0.1669 S12: -0.3929 S13: 0.2343
REMARK 3 S21: 0.3409 S22: -0.0681 S23: 0.1361
REMARK 3 S31: -0.2200 S32: 0.0175 S33: -0.0905
REMARK 3 TLS GROUP : 76
REMARK 3 SELECTION: (CHAIN D AND RESID 429:457)
REMARK 3 ORIGIN FOR THE GROUP (A): 62.6390 29.6228 75.2131
REMARK 3 T TENSOR
REMARK 3 T11: 0.2430 T22: 0.2501
REMARK 3 T33: 0.1795 T12: -0.0604
REMARK 3 T13: 0.0181 T23: 0.0106
REMARK 3 L TENSOR
REMARK 3 L11: 1.5951 L22: 0.9221
REMARK 3 L33: 0.9476 L12: 0.8174
REMARK 3 L13: 0.7363 L23: 0.7801
REMARK 3 S TENSOR
REMARK 3 S11: 0.1086 S12: -0.0813 S13: 0.0497
REMARK 3 S21: 0.1402 S22: -0.0739 S23: 0.0775
REMARK 3 S31: 0.1580 S32: -0.2410 S33: -0.0343
REMARK 3 TLS GROUP : 77
REMARK 3 SELECTION: (CHAIN D AND RESID 458:485)
REMARK 3 ORIGIN FOR THE GROUP (A): 63.9153 12.4019 70.9502
REMARK 3 T TENSOR
REMARK 3 T11: 0.2778 T22: 0.1499
REMARK 3 T33: 0.1753 T12: -0.0512
REMARK 3 T13: 0.0006 T23: 0.0328
REMARK 3 L TENSOR
REMARK 3 L11: 1.2679 L22: 1.7533
REMARK 3 L33: 3.4868 L12: 0.1705
REMARK 3 L13: 0.5749 L23: 0.1099
REMARK 3 S TENSOR
REMARK 3 S11: 0.1748 S12: -0.2277 S13: -0.2496
REMARK 3 S21: 0.1550 S22: -0.0346 S23: -0.0169
REMARK 3 S31: 0.7048 S32: 0.0428 S33: -0.1845
REMARK 3 TLS GROUP : 78
REMARK 3 SELECTION: (CHAIN D AND RESID 486:494)
REMARK 3 ORIGIN FOR THE GROUP (A): 59.0723 16.5293 84.5117
REMARK 3 T TENSOR
REMARK 3 T11: 0.3854 T22: 0.3453
REMARK 3 T33: 0.2389 T12: -0.1305
REMARK 3 T13: 0.0391 T23: 0.0376
REMARK 3 L TENSOR
REMARK 3 L11: 3.8691 L22: 5.1826
REMARK 3 L33: 5.4073 L12: -0.1808
REMARK 3 L13: 3.0517 L23: -4.0904
REMARK 3 S TENSOR
REMARK 3 S11: -0.0745 S12: -0.7792 S13: 0.0738
REMARK 3 S21: 0.4283 S22: -0.3308 S23: 0.0510
REMARK 3 S31: 0.2399 S32: -0.1992 S33: 0.4201
REMARK 3 TLS GROUP : 79
REMARK 3 SELECTION: (CHAIN D AND RESID 495:530)
REMARK 3 ORIGIN FOR THE GROUP (A): 67.7555 18.2826 71.6901
REMARK 3 T TENSOR
REMARK 3 T11: 0.2465 T22: 0.1150
REMARK 3 T33: 0.1610 T12: -0.0318
REMARK 3 T13: -0.0201 T23: 0.0336
REMARK 3 L TENSOR
REMARK 3 L11: 1.8523 L22: 1.5727
REMARK 3 L33: 2.6591 L12: 0.0835
REMARK 3 L13: -0.3900 L23: 0.0468
REMARK 3 S TENSOR
REMARK 3 S11: 0.0693 S12: -0.2200 S13: -0.2377
REMARK 3 S21: 0.3237 S22: -0.0791 S23: -0.0539
REMARK 3 S31: 0.1879 S32: -0.0703 S33: 0.0108
REMARK 3 TLS GROUP : 80
REMARK 3 SELECTION: (CHAIN D AND RESID 531:583)
REMARK 3 ORIGIN FOR THE GROUP (A): 85.2255 36.0133 53.8491
REMARK 3 T TENSOR
REMARK 3 T11: 0.1205 T22: 0.2167
REMARK 3 T33: 0.2141 T12: 0.0191
REMARK 3 T13: -0.0224 T23: 0.0024
REMARK 3 L TENSOR
REMARK 3 L11: 0.7616 L22: 1.1131
REMARK 3 L33: 2.4943 L12: 0.6174
REMARK 3 L13: 0.1357 L23: 0.9881
REMARK 3 S TENSOR
REMARK 3 S11: -0.0192 S12: -0.0280 S13: 0.0193
REMARK 3 S21: 0.0530 S22: 0.0816 S23: -0.0579
REMARK 3 S31: 0.0455 S32: 0.3979 S33: -0.0886
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 4M10 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-AUG-13.
REMARK 100 THE DEPOSITION ID IS D_1000081329.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-NOV-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 24-ID-C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9792
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 270
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XSCALE
REMARK 200 DATA SCALING SOFTWARE : XSCALE, SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 197072
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 50.090
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 6.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.09600
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 25.9600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.12
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7
REMARK 200 DATA REDUNDANCY IN SHELL : 6.40
REMARK 200 R MERGE FOR SHELL (I) : 0.75400
REMARK 200 R SYM FOR SHELL (I) : 0.75400
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASES
REMARK 200 STARTING MODEL: PDB ENTRY 3NT1, CHAIN A
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.33
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.75
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MCOX-2 PROTEIN RECONSTITUTED WITH A 2
REMARK 280 -FOLD MOLAR EXCESS OF HEME IN PHOSPHTATE BUFFER, PH 6.7, 100 MM
REMARK 280 NACL, 1.2% (W/V) -OG, AND 0.1% NAN3, AND 10-FOLD MOLAR EXCESS OF
REMARK 280 INHIBITORS FROM 25 MM DMSO STOCKS WERE ADDED TO PROTEIN SAMPLES.
REMARK 280 MIXING 3 UL OF THE PROTEIN-INHIBITOR COMPLEX WITH 3 UL
REMARK 280 CRYSTALLIZATION SOLUTION CONTAINING 50 MM EPPS, PH 8.0, 120 MM
REMARK 280 MGCL2, 22-26% PEG MME-550 AGAINST RESERVOIR SOLUTIONS COMPRISED
REMARK 280 OF 50 MM EPPS PH 8.0, 120 MM MGCL2, 22-26% PEG MME-550, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 2 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 X,-Y,-Z
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 -X,-Y+1/2,Z+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 67.03850
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 90.21950
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 67.03850
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 90.21950
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 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: 12370 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 42010 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, E, 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: 12370 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 41970 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, G, 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 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 ASP A 584
REMARK 465 PRO A 585
REMARK 465 GLN A 586
REMARK 465 PRO A 587
REMARK 465 THR A 588
REMARK 465 LYS A 589
REMARK 465 THR A 590
REMARK 465 ALA A 591
REMARK 465 THR A 592
REMARK 465 ILE A 593
REMARK 465 ASN A 594
REMARK 465 ALA A 595
REMARK 465 SER A 596
REMARK 465 ALA A 597
REMARK 465 SER A 598
REMARK 465 HIS A 599
REMARK 465 SER A 600
REMARK 465 ARG A 601
REMARK 465 LEU A 602
REMARK 465 ASP A 603
REMARK 465 ASP A 604
REMARK 465 ILE A 605
REMARK 465 ASN A 606
REMARK 465 PRO A 607
REMARK 465 THR A 608
REMARK 465 VAL A 609
REMARK 465 LEU A 610
REMARK 465 ILE A 611
REMARK 465 LYS A 612
REMARK 465 ARG A 613
REMARK 465 ARG A 614
REMARK 465 SER A 615
REMARK 465 THR A 616
REMARK 465 GLU A 617
REMARK 465 LEU A 618
REMARK 465 ASP B 584
REMARK 465 PRO B 585
REMARK 465 GLN B 586
REMARK 465 PRO B 587
REMARK 465 THR B 588
REMARK 465 LYS B 589
REMARK 465 THR B 590
REMARK 465 ALA B 591
REMARK 465 THR B 592
REMARK 465 ILE B 593
REMARK 465 ASN B 594
REMARK 465 ALA B 595
REMARK 465 SER B 596
REMARK 465 ALA B 597
REMARK 465 SER B 598
REMARK 465 HIS B 599
REMARK 465 SER B 600
REMARK 465 ARG B 601
REMARK 465 LEU B 602
REMARK 465 ASP B 603
REMARK 465 ASP B 604
REMARK 465 ILE B 605
REMARK 465 ASN B 606
REMARK 465 PRO B 607
REMARK 465 THR B 608
REMARK 465 VAL B 609
REMARK 465 LEU B 610
REMARK 465 ILE B 611
REMARK 465 LYS B 612
REMARK 465 ARG B 613
REMARK 465 ARG B 614
REMARK 465 SER B 615
REMARK 465 THR B 616
REMARK 465 GLU B 617
REMARK 465 LEU B 618
REMARK 465 GLN C 583
REMARK 465 ASP C 584
REMARK 465 PRO C 585
REMARK 465 GLN C 586
REMARK 465 PRO C 587
REMARK 465 THR C 588
REMARK 465 LYS C 589
REMARK 465 THR C 590
REMARK 465 ALA C 591
REMARK 465 THR C 592
REMARK 465 ILE C 593
REMARK 465 ASN C 594
REMARK 465 ALA C 595
REMARK 465 SER C 596
REMARK 465 ALA C 597
REMARK 465 SER C 598
REMARK 465 HIS C 599
REMARK 465 SER C 600
REMARK 465 ARG C 601
REMARK 465 LEU C 602
REMARK 465 ASP C 603
REMARK 465 ASP C 604
REMARK 465 ILE C 605
REMARK 465 ASN C 606
REMARK 465 PRO C 607
REMARK 465 THR C 608
REMARK 465 VAL C 609
REMARK 465 LEU C 610
REMARK 465 ILE C 611
REMARK 465 LYS C 612
REMARK 465 ARG C 613
REMARK 465 ARG C 614
REMARK 465 SER C 615
REMARK 465 THR C 616
REMARK 465 GLU C 617
REMARK 465 LEU C 618
REMARK 465 ASP D 584
REMARK 465 PRO D 585
REMARK 465 GLN D 586
REMARK 465 PRO D 587
REMARK 465 THR D 588
REMARK 465 LYS D 589
REMARK 465 THR D 590
REMARK 465 ALA D 591
REMARK 465 THR D 592
REMARK 465 ILE D 593
REMARK 465 ASN D 594
REMARK 465 ALA D 595
REMARK 465 SER D 596
REMARK 465 ALA D 597
REMARK 465 SER D 598
REMARK 465 HIS D 599
REMARK 465 SER D 600
REMARK 465 ARG D 601
REMARK 465 LEU D 602
REMARK 465 ASP D 603
REMARK 465 ASP D 604
REMARK 465 ILE D 605
REMARK 465 ASN D 606
REMARK 465 PRO D 607
REMARK 465 THR D 608
REMARK 465 VAL D 609
REMARK 465 LEU D 610
REMARK 465 ILE D 611
REMARK 465 LYS D 612
REMARK 465 ARG D 613
REMARK 465 ARG D 614
REMARK 465 SER D 615
REMARK 465 THR D 616
REMARK 465 GLU D 617
REMARK 465 LEU D 618
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 ND2 ASN B 68 O5 NAG B 701 1.62
REMARK 500 ND2 ASN A 68 O5 NAG A 701 1.73
REMARK 500 ND2 ASN D 68 O5 NAG D 701 2.15
REMARK 500 O4 NAG E 1 C2 NAG E 2 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 LEU C 306 CA - CB - CG ANGL. DEV. = 15.4 DEGREES
REMARK 500 LEU D 531 CA - CB - CG ANGL. DEV. = 15.2 DEGREES
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 TYR A 122 -6.44 -144.90
REMARK 500 THR A 129 -91.86 -119.86
REMARK 500 ARG A 185 -80.63 -91.61
REMARK 500 TRP A 387 40.30 -91.17
REMARK 500 GLU A 398 -120.91 53.71
REMARK 500 ASN A 439 20.78 -142.47
REMARK 500 SER A 496 -49.87 65.18
REMARK 500 ARG B 61 19.08 56.84
REMARK 500 LEU B 81 41.69 -68.44
REMARK 500 LEU B 82 11.94 -176.82
REMARK 500 HIS B 95 -167.20 -126.72
REMARK 500 TYR B 122 -3.56 -149.18
REMARK 500 THR B 129 -92.67 -121.45
REMARK 500 ARG B 185 -85.17 -93.40
REMARK 500 TRP B 387 38.49 -96.34
REMARK 500 GLU B 398 -116.39 54.72
REMARK 500 ASN B 410 76.93 -117.87
REMARK 500 ASN B 439 14.02 -143.49
REMARK 500 SER B 496 -46.28 70.57
REMARK 500 THR C 129 -90.20 -120.40
REMARK 500 ARG C 185 -83.67 -96.09
REMARK 500 TRP C 387 43.01 -90.39
REMARK 500 GLU C 398 -113.64 54.11
REMARK 500 ASN C 439 20.55 -143.24
REMARK 500 SER C 496 -46.44 67.31
REMARK 500 ARG D 61 18.47 56.41
REMARK 500 TYR D 122 -9.91 -141.11
REMARK 500 THR D 129 -92.02 -120.53
REMARK 500 ARG D 185 -76.14 -91.85
REMARK 500 TRP D 387 40.73 -95.50
REMARK 500 GLU D 398 -121.15 53.67
REMARK 500 ASN D 410 78.99 -119.70
REMARK 500 SER D 496 -49.52 64.55
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM A 705 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 388 NE2
REMARK 620 2 HEM A 705 NA 92.3
REMARK 620 3 HEM A 705 NB 97.0 86.2
REMARK 620 4 HEM A 705 NC 97.0 170.5 90.9
REMARK 620 5 HEM A 705 ND 90.3 94.5 172.7 87.3
REMARK 620 6 HOH A 952 O 168.3 77.4 88.1 93.5 85.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM B 705 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 388 NE2
REMARK 620 2 HEM B 705 NA 89.6
REMARK 620 3 HEM B 705 NB 97.6 89.3
REMARK 620 4 HEM B 705 NC 97.1 173.2 89.7
REMARK 620 5 HEM B 705 ND 85.5 89.4 176.7 91.2
REMARK 620 6 HOH B 864 O 162.3 73.6 88.0 99.7 88.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM C 705 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 388 NE2
REMARK 620 2 HEM C 705 NA 91.2
REMARK 620 3 HEM C 705 NB 98.8 87.6
REMARK 620 4 HEM C 705 NC 96.1 172.7 90.3
REMARK 620 5 HEM C 705 ND 87.6 92.7 173.6 88.6
REMARK 620 6 HOH C 831 O 164.2 74.5 87.4 98.5 86.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM D 705 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS D 388 NE2
REMARK 620 2 HEM D 705 NA 91.1
REMARK 620 3 HEM D 705 NB 99.3 87.2
REMARK 620 4 HEM D 705 NC 98.6 170.3 90.2
REMARK 620 5 HEM D 705 ND 88.3 92.5 172.4 88.8
REMARK 620 N 1 2 3 4
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4M11 RELATED DB: PDB
DBREF 4M10 A 33 618 UNP Q05769 PGH2_MOUSE 18 604
DBREF 4M10 B 33 618 UNP Q05769 PGH2_MOUSE 18 604
DBREF 4M10 C 33 618 UNP Q05769 PGH2_MOUSE 18 604
DBREF 4M10 D 33 618 UNP Q05769 PGH2_MOUSE 18 604
SEQRES 1 A 587 ALA ASN PRO CYS CYS SER ASN PRO CYS GLN ASN ARG GLY
SEQRES 2 A 587 GLU CYS MET SER THR GLY PHE ASP GLN TYR LYS CYS ASP
SEQRES 3 A 587 CYS THR ARG THR GLY PHE TYR GLY GLU ASN CYS THR THR
SEQRES 4 A 587 PRO GLU PHE LEU THR ARG ILE LYS LEU LEU LEU LYS PRO
SEQRES 5 A 587 THR PRO ASN THR VAL HIS TYR ILE LEU THR HIS PHE LYS
SEQRES 6 A 587 GLY VAL TRP ASN ILE VAL ASN ASN ILE PRO PHE LEU ARG
SEQRES 7 A 587 SER LEU ILE MET LYS TYR VAL LEU THR SER ARG SER TYR
SEQRES 8 A 587 LEU ILE ASP SER PRO PRO THR TYR ASN VAL HIS TYR GLY
SEQRES 9 A 587 TYR LYS SER TRP GLU ALA PHE SER ASN LEU SER TYR TYR
SEQRES 10 A 587 THR ARG ALA LEU PRO PRO VAL ALA ASP ASP CYS PRO THR
SEQRES 11 A 587 PRO MET GLY VAL LYS GLY ASN LYS GLU LEU PRO ASP SER
SEQRES 12 A 587 LYS GLU VAL LEU GLU LYS VAL LEU LEU ARG ARG GLU PHE
SEQRES 13 A 587 ILE PRO ASP PRO GLN GLY SER ASN MET MET PHE ALA PHE
SEQRES 14 A 587 PHE ALA GLN HIS PHE THR HIS GLN PHE PHE LYS THR ASP
SEQRES 15 A 587 HIS LYS ARG GLY PRO GLY PHE THR ARG GLY LEU GLY HIS
SEQRES 16 A 587 GLY VAL ASP LEU ASN HIS ILE TYR GLY GLU THR LEU ASP
SEQRES 17 A 587 ARG GLN HIS LYS LEU ARG LEU PHE LYS ASP GLY LYS LEU
SEQRES 18 A 587 LYS TYR GLN VAL ILE GLY GLY GLU VAL TYR PRO PRO THR
SEQRES 19 A 587 VAL LYS ASP THR GLN VAL GLU MET ILE TYR PRO PRO HIS
SEQRES 20 A 587 ILE PRO GLU ASN LEU GLN PHE ALA VAL GLY GLN GLU VAL
SEQRES 21 A 587 PHE GLY LEU VAL PRO GLY LEU MET MET TYR ALA THR ILE
SEQRES 22 A 587 TRP LEU ARG GLU HIS ASN ARG VAL CYS ASP ILE LEU LYS
SEQRES 23 A 587 GLN GLU HIS PRO GLU TRP GLY ASP GLU GLN LEU PHE GLN
SEQRES 24 A 587 THR SER ARG LEU ILE LEU ILE GLY GLU THR ILE LYS ILE
SEQRES 25 A 587 VAL ILE GLU ASP TYR VAL GLN HIS LEU SER GLY TYR HIS
SEQRES 26 A 587 PHE LYS LEU LYS PHE ASP PRO GLU LEU LEU PHE ASN GLN
SEQRES 27 A 587 GLN PHE GLN TYR GLN ASN ARG ILE ALA SER GLU PHE ASN
SEQRES 28 A 587 THR LEU TYR HIS TRP HIS PRO LEU LEU PRO ASP THR PHE
SEQRES 29 A 587 ASN ILE GLU ASP GLN GLU TYR SER PHE LYS GLN PHE LEU
SEQRES 30 A 587 TYR ASN ASN SER ILE LEU LEU GLU HIS GLY LEU THR GLN
SEQRES 31 A 587 PHE VAL GLU SER PHE THR ARG GLN ILE ALA GLY ARG VAL
SEQRES 32 A 587 ALA GLY GLY ARG ASN VAL PRO ILE ALA VAL GLN ALA VAL
SEQRES 33 A 587 ALA LYS ALA SER ILE ASP GLN SER ARG GLU MET LYS TYR
SEQRES 34 A 587 GLN SER LEU ASN GLU TYR ARG LYS ARG PHE SER LEU LYS
SEQRES 35 A 587 PRO TYR THR SER PHE GLU GLU LEU THR GLY GLU LYS GLU
SEQRES 36 A 587 MET ALA ALA GLU LEU LYS ALA LEU TYR SER ASP ILE ASP
SEQRES 37 A 587 VAL MET GLU LEU TYR PRO ALA LEU LEU VAL GLU LYS PRO
SEQRES 38 A 587 ARG PRO ASP ALA ILE PHE GLY GLU THR MET VAL GLU LEU
SEQRES 39 A 587 GLY ALA PRO PHE SER LEU LYS GLY LEU MET GLY ASN PRO
SEQRES 40 A 587 ILE CYS SER PRO GLN TYR TRP LYS PRO SER THR PHE GLY
SEQRES 41 A 587 GLY GLU VAL GLY PHE LYS ILE ILE ASN THR ALA SER ILE
SEQRES 42 A 587 GLN SER LEU ILE CYS ASN ASN VAL LYS GLY CYS PRO PHE
SEQRES 43 A 587 THR SER PHE ASN VAL GLN ASP PRO GLN PRO THR LYS THR
SEQRES 44 A 587 ALA THR ILE ASN ALA SER ALA SER HIS SER ARG LEU ASP
SEQRES 45 A 587 ASP ILE ASN PRO THR VAL LEU ILE LYS ARG ARG SER THR
SEQRES 46 A 587 GLU LEU
SEQRES 1 B 587 ALA ASN PRO CYS CYS SER ASN PRO CYS GLN ASN ARG GLY
SEQRES 2 B 587 GLU CYS MET SER THR GLY PHE ASP GLN TYR LYS CYS ASP
SEQRES 3 B 587 CYS THR ARG THR GLY PHE TYR GLY GLU ASN CYS THR THR
SEQRES 4 B 587 PRO GLU PHE LEU THR ARG ILE LYS LEU LEU LEU LYS PRO
SEQRES 5 B 587 THR PRO ASN THR VAL HIS TYR ILE LEU THR HIS PHE LYS
SEQRES 6 B 587 GLY VAL TRP ASN ILE VAL ASN ASN ILE PRO PHE LEU ARG
SEQRES 7 B 587 SER LEU ILE MET LYS TYR VAL LEU THR SER ARG SER TYR
SEQRES 8 B 587 LEU ILE ASP SER PRO PRO THR TYR ASN VAL HIS TYR GLY
SEQRES 9 B 587 TYR LYS SER TRP GLU ALA PHE SER ASN LEU SER TYR TYR
SEQRES 10 B 587 THR ARG ALA LEU PRO PRO VAL ALA ASP ASP CYS PRO THR
SEQRES 11 B 587 PRO MET GLY VAL LYS GLY ASN LYS GLU LEU PRO ASP SER
SEQRES 12 B 587 LYS GLU VAL LEU GLU LYS VAL LEU LEU ARG ARG GLU PHE
SEQRES 13 B 587 ILE PRO ASP PRO GLN GLY SER ASN MET MET PHE ALA PHE
SEQRES 14 B 587 PHE ALA GLN HIS PHE THR HIS GLN PHE PHE LYS THR ASP
SEQRES 15 B 587 HIS LYS ARG GLY PRO GLY PHE THR ARG GLY LEU GLY HIS
SEQRES 16 B 587 GLY VAL ASP LEU ASN HIS ILE TYR GLY GLU THR LEU ASP
SEQRES 17 B 587 ARG GLN HIS LYS LEU ARG LEU PHE LYS ASP GLY LYS LEU
SEQRES 18 B 587 LYS TYR GLN VAL ILE GLY GLY GLU VAL TYR PRO PRO THR
SEQRES 19 B 587 VAL LYS ASP THR GLN VAL GLU MET ILE TYR PRO PRO HIS
SEQRES 20 B 587 ILE PRO GLU ASN LEU GLN PHE ALA VAL GLY GLN GLU VAL
SEQRES 21 B 587 PHE GLY LEU VAL PRO GLY LEU MET MET TYR ALA THR ILE
SEQRES 22 B 587 TRP LEU ARG GLU HIS ASN ARG VAL CYS ASP ILE LEU LYS
SEQRES 23 B 587 GLN GLU HIS PRO GLU TRP GLY ASP GLU GLN LEU PHE GLN
SEQRES 24 B 587 THR SER ARG LEU ILE LEU ILE GLY GLU THR ILE LYS ILE
SEQRES 25 B 587 VAL ILE GLU ASP TYR VAL GLN HIS LEU SER GLY TYR HIS
SEQRES 26 B 587 PHE LYS LEU LYS PHE ASP PRO GLU LEU LEU PHE ASN GLN
SEQRES 27 B 587 GLN PHE GLN TYR GLN ASN ARG ILE ALA SER GLU PHE ASN
SEQRES 28 B 587 THR LEU TYR HIS TRP HIS PRO LEU LEU PRO ASP THR PHE
SEQRES 29 B 587 ASN ILE GLU ASP GLN GLU TYR SER PHE LYS GLN PHE LEU
SEQRES 30 B 587 TYR ASN ASN SER ILE LEU LEU GLU HIS GLY LEU THR GLN
SEQRES 31 B 587 PHE VAL GLU SER PHE THR ARG GLN ILE ALA GLY ARG VAL
SEQRES 32 B 587 ALA GLY GLY ARG ASN VAL PRO ILE ALA VAL GLN ALA VAL
SEQRES 33 B 587 ALA LYS ALA SER ILE ASP GLN SER ARG GLU MET LYS TYR
SEQRES 34 B 587 GLN SER LEU ASN GLU TYR ARG LYS ARG PHE SER LEU LYS
SEQRES 35 B 587 PRO TYR THR SER PHE GLU GLU LEU THR GLY GLU LYS GLU
SEQRES 36 B 587 MET ALA ALA GLU LEU LYS ALA LEU TYR SER ASP ILE ASP
SEQRES 37 B 587 VAL MET GLU LEU TYR PRO ALA LEU LEU VAL GLU LYS PRO
SEQRES 38 B 587 ARG PRO ASP ALA ILE PHE GLY GLU THR MET VAL GLU LEU
SEQRES 39 B 587 GLY ALA PRO PHE SER LEU LYS GLY LEU MET GLY ASN PRO
SEQRES 40 B 587 ILE CYS SER PRO GLN TYR TRP LYS PRO SER THR PHE GLY
SEQRES 41 B 587 GLY GLU VAL GLY PHE LYS ILE ILE ASN THR ALA SER ILE
SEQRES 42 B 587 GLN SER LEU ILE CYS ASN ASN VAL LYS GLY CYS PRO PHE
SEQRES 43 B 587 THR SER PHE ASN VAL GLN ASP PRO GLN PRO THR LYS THR
SEQRES 44 B 587 ALA THR ILE ASN ALA SER ALA SER HIS SER ARG LEU ASP
SEQRES 45 B 587 ASP ILE ASN PRO THR VAL LEU ILE LYS ARG ARG SER THR
SEQRES 46 B 587 GLU LEU
SEQRES 1 C 587 ALA ASN PRO CYS CYS SER ASN PRO CYS GLN ASN ARG GLY
SEQRES 2 C 587 GLU CYS MET SER THR GLY PHE ASP GLN TYR LYS CYS ASP
SEQRES 3 C 587 CYS THR ARG THR GLY PHE TYR GLY GLU ASN CYS THR THR
SEQRES 4 C 587 PRO GLU PHE LEU THR ARG ILE LYS LEU LEU LEU LYS PRO
SEQRES 5 C 587 THR PRO ASN THR VAL HIS TYR ILE LEU THR HIS PHE LYS
SEQRES 6 C 587 GLY VAL TRP ASN ILE VAL ASN ASN ILE PRO PHE LEU ARG
SEQRES 7 C 587 SER LEU ILE MET LYS TYR VAL LEU THR SER ARG SER TYR
SEQRES 8 C 587 LEU ILE ASP SER PRO PRO THR TYR ASN VAL HIS TYR GLY
SEQRES 9 C 587 TYR LYS SER TRP GLU ALA PHE SER ASN LEU SER TYR TYR
SEQRES 10 C 587 THR ARG ALA LEU PRO PRO VAL ALA ASP ASP CYS PRO THR
SEQRES 11 C 587 PRO MET GLY VAL LYS GLY ASN LYS GLU LEU PRO ASP SER
SEQRES 12 C 587 LYS GLU VAL LEU GLU LYS VAL LEU LEU ARG ARG GLU PHE
SEQRES 13 C 587 ILE PRO ASP PRO GLN GLY SER ASN MET MET PHE ALA PHE
SEQRES 14 C 587 PHE ALA GLN HIS PHE THR HIS GLN PHE PHE LYS THR ASP
SEQRES 15 C 587 HIS LYS ARG GLY PRO GLY PHE THR ARG GLY LEU GLY HIS
SEQRES 16 C 587 GLY VAL ASP LEU ASN HIS ILE TYR GLY GLU THR LEU ASP
SEQRES 17 C 587 ARG GLN HIS LYS LEU ARG LEU PHE LYS ASP GLY LYS LEU
SEQRES 18 C 587 LYS TYR GLN VAL ILE GLY GLY GLU VAL TYR PRO PRO THR
SEQRES 19 C 587 VAL LYS ASP THR GLN VAL GLU MET ILE TYR PRO PRO HIS
SEQRES 20 C 587 ILE PRO GLU ASN LEU GLN PHE ALA VAL GLY GLN GLU VAL
SEQRES 21 C 587 PHE GLY LEU VAL PRO GLY LEU MET MET TYR ALA THR ILE
SEQRES 22 C 587 TRP LEU ARG GLU HIS ASN ARG VAL CYS ASP ILE LEU LYS
SEQRES 23 C 587 GLN GLU HIS PRO GLU TRP GLY ASP GLU GLN LEU PHE GLN
SEQRES 24 C 587 THR SER ARG LEU ILE LEU ILE GLY GLU THR ILE LYS ILE
SEQRES 25 C 587 VAL ILE GLU ASP TYR VAL GLN HIS LEU SER GLY TYR HIS
SEQRES 26 C 587 PHE LYS LEU LYS PHE ASP PRO GLU LEU LEU PHE ASN GLN
SEQRES 27 C 587 GLN PHE GLN TYR GLN ASN ARG ILE ALA SER GLU PHE ASN
SEQRES 28 C 587 THR LEU TYR HIS TRP HIS PRO LEU LEU PRO ASP THR PHE
SEQRES 29 C 587 ASN ILE GLU ASP GLN GLU TYR SER PHE LYS GLN PHE LEU
SEQRES 30 C 587 TYR ASN ASN SER ILE LEU LEU GLU HIS GLY LEU THR GLN
SEQRES 31 C 587 PHE VAL GLU SER PHE THR ARG GLN ILE ALA GLY ARG VAL
SEQRES 32 C 587 ALA GLY GLY ARG ASN VAL PRO ILE ALA VAL GLN ALA VAL
SEQRES 33 C 587 ALA LYS ALA SER ILE ASP GLN SER ARG GLU MET LYS TYR
SEQRES 34 C 587 GLN SER LEU ASN GLU TYR ARG LYS ARG PHE SER LEU LYS
SEQRES 35 C 587 PRO TYR THR SER PHE GLU GLU LEU THR GLY GLU LYS GLU
SEQRES 36 C 587 MET ALA ALA GLU LEU LYS ALA LEU TYR SER ASP ILE ASP
SEQRES 37 C 587 VAL MET GLU LEU TYR PRO ALA LEU LEU VAL GLU LYS PRO
SEQRES 38 C 587 ARG PRO ASP ALA ILE PHE GLY GLU THR MET VAL GLU LEU
SEQRES 39 C 587 GLY ALA PRO PHE SER LEU LYS GLY LEU MET GLY ASN PRO
SEQRES 40 C 587 ILE CYS SER PRO GLN TYR TRP LYS PRO SER THR PHE GLY
SEQRES 41 C 587 GLY GLU VAL GLY PHE LYS ILE ILE ASN THR ALA SER ILE
SEQRES 42 C 587 GLN SER LEU ILE CYS ASN ASN VAL LYS GLY CYS PRO PHE
SEQRES 43 C 587 THR SER PHE ASN VAL GLN ASP PRO GLN PRO THR LYS THR
SEQRES 44 C 587 ALA THR ILE ASN ALA SER ALA SER HIS SER ARG LEU ASP
SEQRES 45 C 587 ASP ILE ASN PRO THR VAL LEU ILE LYS ARG ARG SER THR
SEQRES 46 C 587 GLU LEU
SEQRES 1 D 587 ALA ASN PRO CYS CYS SER ASN PRO CYS GLN ASN ARG GLY
SEQRES 2 D 587 GLU CYS MET SER THR GLY PHE ASP GLN TYR LYS CYS ASP
SEQRES 3 D 587 CYS THR ARG THR GLY PHE TYR GLY GLU ASN CYS THR THR
SEQRES 4 D 587 PRO GLU PHE LEU THR ARG ILE LYS LEU LEU LEU LYS PRO
SEQRES 5 D 587 THR PRO ASN THR VAL HIS TYR ILE LEU THR HIS PHE LYS
SEQRES 6 D 587 GLY VAL TRP ASN ILE VAL ASN ASN ILE PRO PHE LEU ARG
SEQRES 7 D 587 SER LEU ILE MET LYS TYR VAL LEU THR SER ARG SER TYR
SEQRES 8 D 587 LEU ILE ASP SER PRO PRO THR TYR ASN VAL HIS TYR GLY
SEQRES 9 D 587 TYR LYS SER TRP GLU ALA PHE SER ASN LEU SER TYR TYR
SEQRES 10 D 587 THR ARG ALA LEU PRO PRO VAL ALA ASP ASP CYS PRO THR
SEQRES 11 D 587 PRO MET GLY VAL LYS GLY ASN LYS GLU LEU PRO ASP SER
SEQRES 12 D 587 LYS GLU VAL LEU GLU LYS VAL LEU LEU ARG ARG GLU PHE
SEQRES 13 D 587 ILE PRO ASP PRO GLN GLY SER ASN MET MET PHE ALA PHE
SEQRES 14 D 587 PHE ALA GLN HIS PHE THR HIS GLN PHE PHE LYS THR ASP
SEQRES 15 D 587 HIS LYS ARG GLY PRO GLY PHE THR ARG GLY LEU GLY HIS
SEQRES 16 D 587 GLY VAL ASP LEU ASN HIS ILE TYR GLY GLU THR LEU ASP
SEQRES 17 D 587 ARG GLN HIS LYS LEU ARG LEU PHE LYS ASP GLY LYS LEU
SEQRES 18 D 587 LYS TYR GLN VAL ILE GLY GLY GLU VAL TYR PRO PRO THR
SEQRES 19 D 587 VAL LYS ASP THR GLN VAL GLU MET ILE TYR PRO PRO HIS
SEQRES 20 D 587 ILE PRO GLU ASN LEU GLN PHE ALA VAL GLY GLN GLU VAL
SEQRES 21 D 587 PHE GLY LEU VAL PRO GLY LEU MET MET TYR ALA THR ILE
SEQRES 22 D 587 TRP LEU ARG GLU HIS ASN ARG VAL CYS ASP ILE LEU LYS
SEQRES 23 D 587 GLN GLU HIS PRO GLU TRP GLY ASP GLU GLN LEU PHE GLN
SEQRES 24 D 587 THR SER ARG LEU ILE LEU ILE GLY GLU THR ILE LYS ILE
SEQRES 25 D 587 VAL ILE GLU ASP TYR VAL GLN HIS LEU SER GLY TYR HIS
SEQRES 26 D 587 PHE LYS LEU LYS PHE ASP PRO GLU LEU LEU PHE ASN GLN
SEQRES 27 D 587 GLN PHE GLN TYR GLN ASN ARG ILE ALA SER GLU PHE ASN
SEQRES 28 D 587 THR LEU TYR HIS TRP HIS PRO LEU LEU PRO ASP THR PHE
SEQRES 29 D 587 ASN ILE GLU ASP GLN GLU TYR SER PHE LYS GLN PHE LEU
SEQRES 30 D 587 TYR ASN ASN SER ILE LEU LEU GLU HIS GLY LEU THR GLN
SEQRES 31 D 587 PHE VAL GLU SER PHE THR ARG GLN ILE ALA GLY ARG VAL
SEQRES 32 D 587 ALA GLY GLY ARG ASN VAL PRO ILE ALA VAL GLN ALA VAL
SEQRES 33 D 587 ALA LYS ALA SER ILE ASP GLN SER ARG GLU MET LYS TYR
SEQRES 34 D 587 GLN SER LEU ASN GLU TYR ARG LYS ARG PHE SER LEU LYS
SEQRES 35 D 587 PRO TYR THR SER PHE GLU GLU LEU THR GLY GLU LYS GLU
SEQRES 36 D 587 MET ALA ALA GLU LEU LYS ALA LEU TYR SER ASP ILE ASP
SEQRES 37 D 587 VAL MET GLU LEU TYR PRO ALA LEU LEU VAL GLU LYS PRO
SEQRES 38 D 587 ARG PRO ASP ALA ILE PHE GLY GLU THR MET VAL GLU LEU
SEQRES 39 D 587 GLY ALA PRO PHE SER LEU LYS GLY LEU MET GLY ASN PRO
SEQRES 40 D 587 ILE CYS SER PRO GLN TYR TRP LYS PRO SER THR PHE GLY
SEQRES 41 D 587 GLY GLU VAL GLY PHE LYS ILE ILE ASN THR ALA SER ILE
SEQRES 42 D 587 GLN SER LEU ILE CYS ASN ASN VAL LYS GLY CYS PRO PHE
SEQRES 43 D 587 THR SER PHE ASN VAL GLN ASP PRO GLN PRO THR LYS THR
SEQRES 44 D 587 ALA THR ILE ASN ALA SER ALA SER HIS SER ARG LEU ASP
SEQRES 45 D 587 ASP ILE ASN PRO THR VAL LEU ILE LYS ARG ARG SER THR
SEQRES 46 D 587 GLU LEU
MODRES 4M10 ASN C 68 ASN GLYCOSYLATION SITE
MODRES 4M10 ASN B 68 ASN GLYCOSYLATION SITE
MODRES 4M10 ASN D 68 ASN GLYCOSYLATION SITE
MODRES 4M10 ASN A 68 ASN GLYCOSYLATION SITE
MODRES 4M10 ASN C 410 ASN GLYCOSYLATION SITE
MODRES 4M10 ASN D 144 ASN GLYCOSYLATION SITE
MODRES 4M10 ASN B 144 ASN GLYCOSYLATION SITE
MODRES 4M10 ASN A 144 ASN GLYCOSYLATION SITE
MODRES 4M10 ASN D 410 ASN GLYCOSYLATION SITE
MODRES 4M10 ASN C 144 ASN GLYCOSYLATION SITE
MODRES 4M10 ASN A 410 ASN GLYCOSYLATION SITE
MODRES 4M10 ASN B 410 ASN GLYCOSYLATION SITE
HET NAG E 1 14
HET NAG E 2 14
HET NAG F 1 14
HET NAG F 2 14
HET NAG G 1 14
HET NAG G 2 14
HET NAG H 1 14
HET NAG H 2 14
HET NAG A 701 14
HET NAG A 704 14
HET HEM A 705 43
HET ICD A 706 23
HET NAG B 701 14
HET NAG B 704 14
HET HEM B 705 43
HET ICD B 706 23
HET BOG B 707 20
HET BOG B 708 20
HET NAG C 701 14
HET NAG C 704 14
HET HEM C 705 43
HET ICD C 706 23
HET BOG C 707 20
HET NAG D 701 14
HET NAG D 704 14
HET HEM D 705 43
HET ICD D 706 23
HET BOG D 707 20
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM ICD 4-HYDROXY-2-METHYL-N-(5-METHYL-1,2-OXAZOL-3-YL)-2H-1,2-
HETNAM 2 ICD BENZOTHIAZINE-3-CARBOXAMIDE 1,1-DIOXIDE
HETNAM BOG OCTYL BETA-D-GLUCOPYRANOSIDE
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
HETSYN HEM HEME
HETSYN ICD ISOXICAM
HETSYN BOG BETA-OCTYLGLUCOSIDE; OCTYL BETA-D-GLUCOSIDE; OCTYL D-
HETSYN 2 BOG GLUCOSIDE; OCTYL GLUCOSIDE
FORMUL 5 NAG 16(C8 H15 N O6)
FORMUL 11 HEM 4(C34 H32 FE N4 O4)
FORMUL 12 ICD 4(C14 H13 N3 O5 S)
FORMUL 17 BOG 4(C14 H28 O6)
FORMUL 29 HOH *1738(H2 O)
HELIX 1 1 GLU A 73 LYS A 83 1 11
HELIX 2 2 THR A 85 THR A 94 1 10
HELIX 3 3 PHE A 96 ASN A 105 1 10
HELIX 4 4 ILE A 105A ARG A 120 1 16
HELIX 5 5 SER A 138 ASN A 144 1 7
HELIX 6 6 ASP A 173 LEU A 182 1 10
HELIX 7 7 ASN A 195 HIS A 207 1 13
HELIX 8 8 LEU A 230 GLY A 235 1 6
HELIX 9 9 THR A 237 ARG A 245 1 9
HELIX 10 10 THR A 265 GLN A 270 1 6
HELIX 11 11 PRO A 280 GLN A 284 5 5
HELIX 12 12 VAL A 291 LEU A 294 5 4
HELIX 13 13 VAL A 295 HIS A 320 1 26
HELIX 14 14 GLY A 324 ASP A 347 1 24
HELIX 15 15 ASP A 347 GLY A 354 1 8
HELIX 16 16 ASP A 362 PHE A 367 5 6
HELIX 17 17 ALA A 378 TYR A 385 1 8
HELIX 18 18 HIS A 386 LEU A 391 5 6
HELIX 19 19 SER A 403 LEU A 408 1 6
HELIX 20 20 ASN A 410 GLN A 429 1 20
HELIX 21 21 PRO A 441 ALA A 443 5 3
HELIX 22 22 VAL A 444 MET A 458 1 15
HELIX 23 23 SER A 462 PHE A 470 1 9
HELIX 24 24 SER A 477 GLY A 483 1 7
HELIX 25 25 LYS A 485 SER A 496 1 12
HELIX 26 26 ASP A 497 MET A 501 5 5
HELIX 27 27 GLU A 502 GLU A 510 1 9
HELIX 28 28 GLY A 519 GLY A 536 1 18
HELIX 29 29 ASN A 537 SER A 541 5 5
HELIX 30 30 LYS A 546 GLY A 551 5 6
HELIX 31 31 GLY A 552 THR A 561 1 10
HELIX 32 32 SER A 563 VAL A 572 1 10
HELIX 33 33 GLU B 73 LEU B 81 1 9
HELIX 34 34 THR B 85 THR B 94 1 10
HELIX 35 35 PHE B 96 ASN B 105 1 10
HELIX 36 36 ILE B 105A ARG B 120 1 16
HELIX 37 37 SER B 138 ASN B 144 1 7
HELIX 38 38 ASP B 173 LEU B 182 1 10
HELIX 39 39 ASN B 195 HIS B 207 1 13
HELIX 40 40 LEU B 230 GLY B 235 1 6
HELIX 41 41 THR B 237 ARG B 245 1 9
HELIX 42 42 THR B 265 GLN B 270 1 6
HELIX 43 43 PRO B 280 GLN B 284 5 5
HELIX 44 44 VAL B 291 LEU B 294 5 4
HELIX 45 45 VAL B 295 HIS B 320 1 26
HELIX 46 46 GLY B 324 ASP B 347 1 24
HELIX 47 47 ASP B 347 GLY B 354 1 8
HELIX 48 48 ASP B 362 PHE B 367 5 6
HELIX 49 49 ALA B 378 TYR B 385 1 8
HELIX 50 50 TRP B 387 LEU B 391 5 5
HELIX 51 51 SER B 403 LEU B 408 1 6
HELIX 52 52 ASN B 411 GLN B 429 1 19
HELIX 53 53 PRO B 441 ALA B 443 5 3
HELIX 54 54 VAL B 444 MET B 458 1 15
HELIX 55 55 SER B 462 PHE B 470 1 9
HELIX 56 56 SER B 477 GLY B 483 1 7
HELIX 57 57 LYS B 485 SER B 496 1 12
HELIX 58 58 ASP B 497 MET B 501 5 5
HELIX 59 59 GLU B 502 GLU B 510 1 9
HELIX 60 60 GLY B 519 GLY B 536 1 18
HELIX 61 61 ASN B 537 SER B 541 5 5
HELIX 62 62 LYS B 546 GLY B 551 5 6
HELIX 63 63 GLY B 552 THR B 561 1 10
HELIX 64 64 SER B 563 VAL B 572 1 10
HELIX 65 65 GLU C 73 LYS C 83 1 11
HELIX 66 66 THR C 85 THR C 94 1 10
HELIX 67 67 PHE C 96 ASN C 105 1 10
HELIX 68 68 ILE C 105A ARG C 120 1 16
HELIX 69 69 SER C 138 ASN C 144 1 7
HELIX 70 70 ASP C 173 LEU C 182 1 10
HELIX 71 71 ASN C 195 HIS C 207 1 13
HELIX 72 72 LEU C 230 GLY C 235 1 6
HELIX 73 73 THR C 237 ARG C 245 1 9
HELIX 74 74 THR C 265 GLN C 270 1 6
HELIX 75 75 PRO C 280 GLN C 284 5 5
HELIX 76 76 VAL C 291 LEU C 294 5 4
HELIX 77 77 VAL C 295 HIS C 320 1 26
HELIX 78 78 GLY C 324 ASP C 347 1 24
HELIX 79 79 ASP C 347 GLY C 354 1 8
HELIX 80 80 ASP C 362 PHE C 367 5 6
HELIX 81 81 ALA C 378 TYR C 385 1 8
HELIX 82 82 HIS C 386 LEU C 391 5 6
HELIX 83 83 SER C 403 LEU C 408 1 6
HELIX 84 84 ASN C 411 GLN C 429 1 19
HELIX 85 85 PRO C 441 ALA C 443 5 3
HELIX 86 86 VAL C 444 MET C 458 1 15
HELIX 87 87 SER C 462 PHE C 470 1 9
HELIX 88 88 SER C 477 GLY C 483 1 7
HELIX 89 89 LYS C 485 SER C 496 1 12
HELIX 90 90 ASP C 497 MET C 501 5 5
HELIX 91 91 GLU C 502 GLU C 510 1 9
HELIX 92 92 GLY C 519 GLY C 536 1 18
HELIX 93 93 ASN C 537 SER C 541 5 5
HELIX 94 94 LYS C 546 GLY C 551 5 6
HELIX 95 95 GLY C 552 THR C 561 1 10
HELIX 96 96 SER C 563 VAL C 572 1 10
HELIX 97 97 GLU D 73 LYS D 83 1 11
HELIX 98 98 THR D 85 HIS D 95 1 11
HELIX 99 99 PHE D 96 ASN D 105 1 10
HELIX 100 100 ILE D 105A ARG D 120 1 16
HELIX 101 101 SER D 138 ASN D 144 1 7
HELIX 102 102 ASP D 173 LEU D 182 1 10
HELIX 103 103 ASN D 195 HIS D 207 1 13
HELIX 104 104 LEU D 230 GLY D 235 1 6
HELIX 105 105 THR D 237 ARG D 245 1 9
HELIX 106 106 THR D 265 GLN D 270 1 6
HELIX 107 107 PRO D 280 GLN D 284 5 5
HELIX 108 108 VAL D 295 HIS D 320 1 26
HELIX 109 109 GLY D 324 ASP D 347 1 24
HELIX 110 110 ASP D 347 GLY D 354 1 8
HELIX 111 111 ASP D 362 PHE D 367 5 6
HELIX 112 112 ALA D 378 TYR D 385 1 8
HELIX 113 113 TRP D 387 LEU D 391 5 5
HELIX 114 114 SER D 403 LEU D 408 1 6
HELIX 115 115 ASN D 411 GLN D 429 1 19
HELIX 116 116 PRO D 441 ALA D 443 5 3
HELIX 117 117 VAL D 444 MET D 458 1 15
HELIX 118 118 SER D 462 PHE D 470 1 9
HELIX 119 119 SER D 477 GLY D 483 1 7
HELIX 120 120 LYS D 485 SER D 496 1 12
HELIX 121 121 ASP D 497 MET D 501 5 5
HELIX 122 122 GLU D 502 GLU D 510 1 9
HELIX 123 123 GLY D 519 GLY D 536 1 18
HELIX 124 124 ASN D 537 SER D 541 5 5
HELIX 125 125 LYS D 546 GLY D 551 5 6
HELIX 126 126 GLY D 552 THR D 561 1 10
HELIX 127 127 SER D 563 VAL D 572 1 10
SHEET 1 A 2 GLU A 46 GLY A 51 0
SHEET 2 A 2 GLN A 54 ASP A 58 -1 O LYS A 56 N MET A 48
SHEET 1 B 2 PHE A 64 TYR A 65 0
SHEET 2 B 2 THR A 71 PRO A 72 -1 O THR A 71 N TYR A 65
SHEET 1 C 2 TYR A 130 ASN A 131 0
SHEET 2 C 2 THR A 149 ARG A 150 -1 O ARG A 150 N TYR A 130
SHEET 1 D 2 GLN A 255 ILE A 257 0
SHEET 2 D 2 GLU A 260 TYR A 262 -1 O GLU A 260 N ILE A 257
SHEET 1 E 2 PHE A 395 ILE A 397 0
SHEET 2 E 2 GLN A 400 TYR A 402 -1 O TYR A 402 N PHE A 395
SHEET 1 F 2 GLU B 46 SER B 49 0
SHEET 2 F 2 TYR B 55 ASP B 58 -1 O LYS B 56 N MET B 48
SHEET 1 G 2 PHE B 64 TYR B 65 0
SHEET 2 G 2 THR B 71 PRO B 72 -1 O THR B 71 N TYR B 65
SHEET 1 H 2 TYR B 130 ASN B 131 0
SHEET 2 H 2 THR B 149 ARG B 150 -1 O ARG B 150 N TYR B 130
SHEET 1 I 2 GLN B 255 ILE B 257 0
SHEET 2 I 2 GLU B 260 TYR B 262 -1 O TYR B 262 N GLN B 255
SHEET 1 J 2 PHE B 395 ILE B 397 0
SHEET 2 J 2 GLN B 400 TYR B 402 -1 O TYR B 402 N PHE B 395
SHEET 1 K 2 GLU C 46 SER C 49 0
SHEET 2 K 2 TYR C 55 ASP C 58 -1 O LYS C 56 N MET C 48
SHEET 1 L 2 PHE C 64 TYR C 65 0
SHEET 2 L 2 THR C 71 PRO C 72 -1 O THR C 71 N TYR C 65
SHEET 1 M 2 TYR C 130 ASN C 131 0
SHEET 2 M 2 THR C 149 ARG C 150 -1 O ARG C 150 N TYR C 130
SHEET 1 N 2 GLN C 255 ILE C 257 0
SHEET 2 N 2 GLU C 260 TYR C 262 -1 O GLU C 260 N ILE C 257
SHEET 1 O 2 PHE C 395 ILE C 397 0
SHEET 2 O 2 GLN C 400 TYR C 402 -1 O TYR C 402 N PHE C 395
SHEET 1 P 2 GLU D 46 SER D 49 0
SHEET 2 P 2 TYR D 55 ASP D 58 -1 O ASP D 58 N GLU D 46
SHEET 1 Q 2 PHE D 64 TYR D 65 0
SHEET 2 Q 2 THR D 71 PRO D 72 -1 O THR D 71 N TYR D 65
SHEET 1 R 2 TYR D 130 ASN D 131 0
SHEET 2 R 2 THR D 149 ARG D 150 -1 O ARG D 150 N TYR D 130
SHEET 1 S 2 GLN D 255 ILE D 257 0
SHEET 2 S 2 GLU D 260 TYR D 262 -1 O GLU D 260 N ILE D 257
SHEET 1 T 2 PHE D 395 ILE D 397 0
SHEET 2 T 2 GLN D 400 TYR D 402 -1 O TYR D 402 N PHE D 395
SSBOND 1 CYS A 36 CYS A 47 1555 1555 2.07
SSBOND 2 CYS A 37 CYS A 159 1555 1555 2.04
SSBOND 3 CYS A 41 CYS A 57 1555 1555 2.02
SSBOND 4 CYS A 59 CYS A 69 1555 1555 2.04
SSBOND 5 CYS A 569 CYS A 575 1555 1555 2.05
SSBOND 6 CYS B 36 CYS B 47 1555 1555 2.06
SSBOND 7 CYS B 37 CYS B 159 1555 1555 2.05
SSBOND 8 CYS B 41 CYS B 57 1555 1555 2.02
SSBOND 9 CYS B 59 CYS B 69 1555 1555 2.05
SSBOND 10 CYS B 569 CYS B 575 1555 1555 2.05
SSBOND 11 CYS C 36 CYS C 47 1555 1555 2.05
SSBOND 12 CYS C 37 CYS C 159 1555 1555 2.04
SSBOND 13 CYS C 41 CYS C 57 1555 1555 2.03
SSBOND 14 CYS C 59 CYS C 69 1555 1555 2.05
SSBOND 15 CYS C 569 CYS C 575 1555 1555 2.05
SSBOND 16 CYS D 36 CYS D 47 1555 1555 2.07
SSBOND 17 CYS D 37 CYS D 159 1555 1555 2.05
SSBOND 18 CYS D 41 CYS D 57 1555 1555 2.02
SSBOND 19 CYS D 59 CYS D 69 1555 1555 2.04
SSBOND 20 CYS D 569 CYS D 575 1555 1555 2.06
LINK ND2 ASN A 68 C1 NAG A 701 1555 1555 1.44
LINK ND2 ASN A 144 C1 NAG E 1 1555 1555 1.49
LINK ND2 ASN A 410 C1 NAG A 704 1555 1555 1.51
LINK ND2 ASN B 68 C1 NAG B 701 1555 1555 1.34
LINK ND2 ASN B 144 C1 NAG F 1 1555 1555 1.48
LINK ND2 ASN B 410 C1 NAG B 704 1555 1555 1.86
LINK ND2 ASN C 68 C1 NAG C 701 1555 1555 1.31
LINK ND2 ASN C 144 C1 NAG G 1 1555 1555 1.51
LINK ND2 ASN C 410 C1 NAG C 704 1555 1555 1.46
LINK ND2 ASN D 68 C1 NAG D 701 1555 1555 1.43
LINK ND2 ASN D 144 C1 NAG H 1 1555 1555 1.47
LINK ND2 ASN D 410 C1 NAG D 704 1555 1555 1.51
LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.49
LINK O4 NAG F 1 C1 NAG F 2 1555 1555 1.49
LINK O4 NAG G 1 C1 NAG G 2 1555 1555 1.49
LINK O4 NAG H 1 C1 NAG H 2 1555 1555 1.52
LINK NE2 HIS A 388 FE HEM A 705 1555 1555 2.32
LINK FE HEM A 705 O HOH A 952 1555 1555 2.68
LINK NE2 HIS B 388 FE HEM B 705 1555 1555 2.39
LINK FE HEM B 705 O HOH B 864 1555 1555 2.55
LINK NE2 HIS C 388 FE HEM C 705 1555 1555 2.33
LINK FE HEM C 705 O HOH C 831 1555 1555 2.64
LINK NE2 HIS D 388 FE HEM D 705 1555 1555 2.32
CISPEP 1 SER A 126 PRO A 127 0 1.72
CISPEP 2 SER B 126 PRO B 127 0 4.77
CISPEP 3 SER C 126 PRO C 127 0 2.44
CISPEP 4 SER D 126 PRO D 127 0 0.09
CRYST1 122.612 134.077 180.439 90.00 90.00 90.00 P 2 21 21 16
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 0.008156 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007458 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005542 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
