HEADER RIBOSOME 14-JAN-16 5HL7
TITLE THE CRYSTAL STRUCTURE OF THE LARGE RIBOSOMAL SUBUNIT OF STAPHYLOCOCCUS
TITLE 2 AUREUS IN COMPLEX WITH LEFAMULIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 50S RIBOSOMAL PROTEIN L2;
COMPND 3 CHAIN: A;
COMPND 4 MOL_ID: 2;
COMPND 5 MOLECULE: 23S RIBOSOMAL RNA;
COMPND 6 CHAIN: X;
COMPND 7 MOL_ID: 3;
COMPND 8 MOLECULE: 5S RIBOSOMAL RNA;
COMPND 9 CHAIN: Y;
COMPND 10 MOL_ID: 4;
COMPND 11 MOLECULE: 50S RIBOSOMAL PROTEIN L3;
COMPND 12 CHAIN: B;
COMPND 13 MOL_ID: 5;
COMPND 14 MOLECULE: 50S RIBOSOMAL PROTEIN L4;
COMPND 15 CHAIN: C;
COMPND 16 MOL_ID: 6;
COMPND 17 MOLECULE: 50S RIBOSOMAL PROTEIN L5;
COMPND 18 CHAIN: D;
COMPND 19 MOL_ID: 7;
COMPND 20 MOLECULE: 50S RIBOSOMAL PROTEIN L6;
COMPND 21 CHAIN: E;
COMPND 22 MOL_ID: 8;
COMPND 23 MOLECULE: 50S RIBOSOMAL PROTEIN L13;
COMPND 24 CHAIN: G;
COMPND 25 MOL_ID: 9;
COMPND 26 MOLECULE: 50S RIBOSOMAL PROTEIN L14;
COMPND 27 CHAIN: H;
COMPND 28 MOL_ID: 10;
COMPND 29 MOLECULE: 50S RIBOSOMAL PROTEIN L15;
COMPND 30 CHAIN: I;
COMPND 31 MOL_ID: 11;
COMPND 32 MOLECULE: 50S RIBOSOMAL PROTEIN L16;
COMPND 33 CHAIN: J;
COMPND 34 MOL_ID: 12;
COMPND 35 MOLECULE: 50S RIBOSOMAL PROTEIN L17;
COMPND 36 CHAIN: K;
COMPND 37 MOL_ID: 13;
COMPND 38 MOLECULE: 50S RIBOSOMAL PROTEIN L18;
COMPND 39 CHAIN: L;
COMPND 40 MOL_ID: 14;
COMPND 41 MOLECULE: 50S RIBOSOMAL PROTEIN L19;
COMPND 42 CHAIN: M;
COMPND 43 MOL_ID: 15;
COMPND 44 MOLECULE: 50S RIBOSOMAL PROTEIN L20;
COMPND 45 CHAIN: N;
COMPND 46 MOL_ID: 16;
COMPND 47 MOLECULE: 50S RIBOSOMAL PROTEIN L21;
COMPND 48 CHAIN: O;
COMPND 49 MOL_ID: 17;
COMPND 50 MOLECULE: 50S RIBOSOMAL PROTEIN L22;
COMPND 51 CHAIN: P;
COMPND 52 MOL_ID: 18;
COMPND 53 MOLECULE: 50S RIBOSOMAL PROTEIN L23;
COMPND 54 CHAIN: Q;
COMPND 55 MOL_ID: 19;
COMPND 56 MOLECULE: 50S RIBOSOMAL PROTEIN L24;
COMPND 57 CHAIN: R;
COMPND 58 MOL_ID: 20;
COMPND 59 MOLECULE: 50S RIBOSOMAL PROTEIN L25;
COMPND 60 CHAIN: S;
COMPND 61 SYNONYM: GENERAL STRESS PROTEIN CTC;
COMPND 62 MOL_ID: 21;
COMPND 63 MOLECULE: 50S RIBOSOMAL PROTEIN L27;
COMPND 64 CHAIN: T;
COMPND 65 MOL_ID: 22;
COMPND 66 MOLECULE: 50S RIBOSOMAL PROTEIN L28;
COMPND 67 CHAIN: U;
COMPND 68 MOL_ID: 23;
COMPND 69 MOLECULE: 50S RIBOSOMAL PROTEIN L29;
COMPND 70 CHAIN: V;
COMPND 71 MOL_ID: 24;
COMPND 72 MOLECULE: 50S RIBOSOMAL PROTEIN L30;
COMPND 73 CHAIN: W;
COMPND 74 MOL_ID: 25;
COMPND 75 MOLECULE: 50S RIBOSOMAL PROTEIN L32;
COMPND 76 CHAIN: Z;
COMPND 77 MOL_ID: 26;
COMPND 78 MOLECULE: 50S RIBOSOMAL PROTEIN L34;
COMPND 79 CHAIN: 2;
COMPND 80 MOL_ID: 27;
COMPND 81 MOLECULE: 50S RIBOSOMAL PROTEIN L35;
COMPND 82 CHAIN: 3;
COMPND 83 MOL_ID: 28;
COMPND 84 MOLECULE: 50S RIBOSOMAL PROTEIN L36;
COMPND 85 CHAIN: 4
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS SUBSP. AUREUS NCTC 8325;
SOURCE 3 ORGANISM_TAXID: 93061;
SOURCE 4 MOL_ID: 2;
SOURCE 5 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS SUBSP. AUREUS NCTC 8325;
SOURCE 6 ORGANISM_TAXID: 93061;
SOURCE 7 MOL_ID: 3;
SOURCE 8 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS SUBSP. AUREUS NCTC 8325;
SOURCE 9 ORGANISM_TAXID: 93061;
SOURCE 10 MOL_ID: 4;
SOURCE 11 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS SUBSP. AUREUS NCTC 8325;
SOURCE 12 ORGANISM_TAXID: 93061;
SOURCE 13 MOL_ID: 5;
SOURCE 14 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS SUBSP. AUREUS NCTC 8325;
SOURCE 15 ORGANISM_TAXID: 93061;
SOURCE 16 MOL_ID: 6;
SOURCE 17 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS SUBSP. AUREUS NCTC 8325;
SOURCE 18 ORGANISM_TAXID: 93061;
SOURCE 19 MOL_ID: 7;
SOURCE 20 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS SUBSP. AUREUS NCTC 8325;
SOURCE 21 ORGANISM_TAXID: 93061;
SOURCE 22 MOL_ID: 8;
SOURCE 23 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS SUBSP. AUREUS NCTC 8325;
SOURCE 24 ORGANISM_TAXID: 93061;
SOURCE 25 MOL_ID: 9;
SOURCE 26 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS SUBSP. AUREUS NCTC 8325;
SOURCE 27 ORGANISM_TAXID: 93061;
SOURCE 28 MOL_ID: 10;
SOURCE 29 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS SUBSP. AUREUS NCTC 8325;
SOURCE 30 ORGANISM_TAXID: 93061;
SOURCE 31 MOL_ID: 11;
SOURCE 32 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS SUBSP. AUREUS NCTC 8325;
SOURCE 33 ORGANISM_TAXID: 93061;
SOURCE 34 MOL_ID: 12;
SOURCE 35 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS SUBSP. AUREUS NCTC 8325;
SOURCE 36 ORGANISM_TAXID: 93061;
SOURCE 37 MOL_ID: 13;
SOURCE 38 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS SUBSP. AUREUS NCTC 8325;
SOURCE 39 ORGANISM_TAXID: 93061;
SOURCE 40 MOL_ID: 14;
SOURCE 41 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS SUBSP. AUREUS NCTC 8325;
SOURCE 42 ORGANISM_TAXID: 93061;
SOURCE 43 MOL_ID: 15;
SOURCE 44 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS SUBSP. AUREUS NCTC 8325;
SOURCE 45 ORGANISM_TAXID: 93061;
SOURCE 46 MOL_ID: 16;
SOURCE 47 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS SUBSP. AUREUS NCTC 8325;
SOURCE 48 ORGANISM_TAXID: 93061;
SOURCE 49 MOL_ID: 17;
SOURCE 50 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS SUBSP. AUREUS NCTC 8325;
SOURCE 51 ORGANISM_TAXID: 93061;
SOURCE 52 MOL_ID: 18;
SOURCE 53 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS SUBSP. AUREUS NCTC 8325;
SOURCE 54 ORGANISM_TAXID: 93061;
SOURCE 55 MOL_ID: 19;
SOURCE 56 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS SUBSP. AUREUS NCTC 8325;
SOURCE 57 ORGANISM_TAXID: 93061;
SOURCE 58 MOL_ID: 20;
SOURCE 59 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS SUBSP. AUREUS NCTC 8325;
SOURCE 60 ORGANISM_TAXID: 93061;
SOURCE 61 MOL_ID: 21;
SOURCE 62 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS SUBSP. AUREUS NCTC 8325;
SOURCE 63 ORGANISM_TAXID: 93061;
SOURCE 64 MOL_ID: 22;
SOURCE 65 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS SUBSP. AUREUS NCTC 8325;
SOURCE 66 ORGANISM_TAXID: 93061;
SOURCE 67 MOL_ID: 23;
SOURCE 68 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS SUBSP. AUREUS NCTC 8325;
SOURCE 69 ORGANISM_TAXID: 93061;
SOURCE 70 MOL_ID: 24;
SOURCE 71 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS SUBSP. AUREUS NCTC 8325;
SOURCE 72 ORGANISM_TAXID: 93061;
SOURCE 73 MOL_ID: 25;
SOURCE 74 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS SUBSP. AUREUS NCTC 8325;
SOURCE 75 ORGANISM_TAXID: 93061;
SOURCE 76 MOL_ID: 26;
SOURCE 77 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS SUBSP. AUREUS NCTC 8325;
SOURCE 78 ORGANISM_TAXID: 93061;
SOURCE 79 MOL_ID: 27;
SOURCE 80 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS SUBSP. AUREUS NCTC 8325;
SOURCE 81 ORGANISM_TAXID: 93061;
SOURCE 82 MOL_ID: 28;
SOURCE 83 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS SUBSP. AUREUS NCTC 8325;
SOURCE 84 ORGANISM_TAXID: 93061
KEYWDS RIBOSOME, LEFAMULIN, RNA, ANTIBIOTIC
EXPDTA X-RAY DIFFRACTION
AUTHOR Z.EYAL,D.MATZOV,M.KRUPKIN,H.ROZENBERG,E.ZIMMERMAN,A.BASHAN,A.YONATH
REVDAT 2 10-JAN-24 5HL7 1 LINK
REVDAT 1 21-DEC-16 5HL7 0
JRNL AUTH Z.EYAL,D.MATZOV,M.KRUPKIN,S.PAUKNER,R.RIEDL,H.ROZENBERG,
JRNL AUTH 2 E.ZIMMERMAN,A.BASHAN,A.YONATH
JRNL TITL A NOVEL PLEUROMUTILIN ANTIBACTERIAL COMPOUND, ITS BINDING
JRNL TITL 2 MODE AND SELECTIVITY MECHANISM.
JRNL REF SCI REP V. 6 39004 2016
JRNL REFN ESSN 2045-2322
JRNL PMID 27958389
JRNL DOI 10.1038/SREP39004
REMARK 2
REMARK 2 RESOLUTION. 3.55 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
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) : 3.55
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.93
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.4
REMARK 3 NUMBER OF REFLECTIONS : 235811
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.189
REMARK 3 R VALUE (WORKING SET) : 0.187
REMARK 3 FREE R VALUE : 0.227
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.020
REMARK 3 FREE R VALUE TEST SET COUNT : 11845
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 49.9352 - 10.9816 0.96 8164 445 0.2295 0.2425
REMARK 3 2 10.9816 - 8.7316 0.97 7897 423 0.1657 0.1907
REMARK 3 3 8.7316 - 7.6323 0.98 7823 407 0.1633 0.2221
REMARK 3 4 7.6323 - 6.9365 0.98 7787 440 0.1558 0.1972
REMARK 3 5 6.9365 - 6.4404 0.98 7776 374 0.1557 0.2004
REMARK 3 6 6.4404 - 6.0614 0.98 7740 401 0.1596 0.2058
REMARK 3 7 6.0614 - 5.7583 0.98 7655 433 0.1540 0.2158
REMARK 3 8 5.7583 - 5.5080 0.98 7730 376 0.1562 0.1934
REMARK 3 9 5.5080 - 5.2962 0.98 7711 409 0.1582 0.1992
REMARK 3 10 5.2962 - 5.1136 0.98 7702 401 0.1595 0.2165
REMARK 3 11 5.1136 - 4.9539 0.97 7572 391 0.1682 0.2110
REMARK 3 12 4.9539 - 4.8124 0.94 7348 377 0.1691 0.2023
REMARK 3 13 4.8124 - 4.6858 0.94 7346 381 0.1707 0.2119
REMARK 3 14 4.6858 - 4.5715 0.95 7384 413 0.1755 0.2245
REMARK 3 15 4.5715 - 4.4677 0.94 7313 392 0.1756 0.2343
REMARK 3 16 4.4677 - 4.3727 0.95 7370 393 0.1858 0.2125
REMARK 3 17 4.3727 - 4.2852 0.94 7292 358 0.1823 0.2198
REMARK 3 18 4.2852 - 4.2044 0.94 7314 403 0.1844 0.2298
REMARK 3 19 4.2044 - 4.1294 0.95 7380 357 0.1888 0.2274
REMARK 3 20 4.1294 - 4.0594 0.95 7321 408 0.2014 0.2768
REMARK 3 21 4.0594 - 3.9939 0.95 7291 413 0.2089 0.2333
REMARK 3 22 3.9939 - 3.9325 0.95 7301 396 0.2121 0.2563
REMARK 3 23 3.9325 - 3.8747 0.95 7329 389 0.2076 0.2551
REMARK 3 24 3.8747 - 3.8201 0.95 7329 342 0.2179 0.2513
REMARK 3 25 3.8201 - 3.7685 0.94 7305 368 0.2325 0.2599
REMARK 3 26 3.7685 - 3.7196 0.94 7270 403 0.2348 0.2887
REMARK 3 27 3.7196 - 3.6731 0.95 7308 404 0.2376 0.2823
REMARK 3 28 3.6731 - 3.6289 0.95 7289 392 0.2539 0.2942
REMARK 3 29 3.6289 - 3.5867 0.95 7308 389 0.2622 0.3089
REMARK 3 30 3.5867 - 3.5464 0.86 6611 367 0.2724 0.3163
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) : 0.370
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.490
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 105.6
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 110.8
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 : 0.010 88398
REMARK 3 ANGLE : 1.610 133592
REMARK 3 CHIRALITY : 0.071 17454
REMARK 3 PLANARITY : 0.007 6515
REMARK 3 DIHEDRAL : 17.119 40843
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 32
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'X' AND (RESID 2 THROUGH 722 )
REMARK 3 ORIGIN FOR THE GROUP (A): 21.9446 -64.3893 -60.1431
REMARK 3 T TENSOR
REMARK 3 T11: 0.8720 T22: 1.3659
REMARK 3 T33: 0.8942 T12: 0.0198
REMARK 3 T13: -0.0157 T23: 0.5555
REMARK 3 L TENSOR
REMARK 3 L11: 0.5545 L22: 0.4021
REMARK 3 L33: 0.3998 L12: -0.0022
REMARK 3 L13: -0.1222 L23: -0.1221
REMARK 3 S TENSOR
REMARK 3 S11: -0.0810 S12: 0.5863 S13: 0.4127
REMARK 3 S21: -0.1843 S22: 0.0117 S23: -0.0639
REMARK 3 S31: -0.2268 S32: -0.0880 S33: 0.0859
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'X' AND (RESID 723 THROUGH 948 )
REMARK 3 ORIGIN FOR THE GROUP (A): 19.9147 -64.6349 -8.1739
REMARK 3 T TENSOR
REMARK 3 T11: 0.8230 T22: 0.7146
REMARK 3 T33: 0.7606 T12: 0.1734
REMARK 3 T13: -0.0731 T23: 0.2229
REMARK 3 L TENSOR
REMARK 3 L11: 0.7301 L22: 0.3397
REMARK 3 L33: 0.2998 L12: -0.1312
REMARK 3 L13: -0.1019 L23: 0.0554
REMARK 3 S TENSOR
REMARK 3 S11: -0.0903 S12: 0.0530 S13: 0.3529
REMARK 3 S21: 0.1032 S22: 0.0317 S23: -0.0525
REMARK 3 S31: -0.2442 S32: -0.0479 S33: 0.0849
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'X' AND (RESID 949 THROUGH 1790 )
REMARK 3 ORIGIN FOR THE GROUP (A): -4.1208 -76.8659 -16.9069
REMARK 3 T TENSOR
REMARK 3 T11: 0.7358 T22: 0.8283
REMARK 3 T33: 0.5778 T12: 0.1831
REMARK 3 T13: 0.0580 T23: 0.2127
REMARK 3 L TENSOR
REMARK 3 L11: 0.8142 L22: 0.3945
REMARK 3 L33: 0.3867 L12: -0.0928
REMARK 3 L13: -0.1415 L23: 0.0633
REMARK 3 S TENSOR
REMARK 3 S11: -0.0989 S12: 0.1688 S13: 0.2610
REMARK 3 S21: 0.0540 S22: 0.0270 S23: 0.0832
REMARK 3 S31: -0.1892 S32: -0.2004 S33: 0.0777
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'X' AND (RESID 1791 THROUGH 2021 )
REMARK 3 ORIGIN FOR THE GROUP (A): 15.7093 -36.7431 0.6827
REMARK 3 T TENSOR
REMARK 3 T11: 1.1810 T22: 0.7273
REMARK 3 T33: 1.3960 T12: 0.2790
REMARK 3 T13: -0.1572 T23: -0.0192
REMARK 3 L TENSOR
REMARK 3 L11: 1.0456 L22: 0.1295
REMARK 3 L33: 0.6452 L12: 0.2608
REMARK 3 L13: -0.2630 L23: 0.0396
REMARK 3 S TENSOR
REMARK 3 S11: -0.1895 S12: -0.3025 S13: 0.8113
REMARK 3 S21: 0.0344 S22: 0.0766 S23: -0.0023
REMARK 3 S31: -0.2961 S32: 0.1022 S33: 0.0729
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'X' AND (RESID 2022 THROUGH 2921 )
REMARK 3 ORIGIN FOR THE GROUP (A): 18.2689 -82.6902 2.7132
REMARK 3 T TENSOR
REMARK 3 T11: 0.7701 T22: 0.7485
REMARK 3 T33: 0.5691 T12: 0.2540
REMARK 3 T13: -0.0076 T23: 0.0833
REMARK 3 L TENSOR
REMARK 3 L11: 0.7442 L22: 0.3812
REMARK 3 L33: 0.4462 L12: 0.0611
REMARK 3 L13: -0.0856 L23: -0.0565
REMARK 3 S TENSOR
REMARK 3 S11: -0.1368 S12: -0.2459 S13: 0.1655
REMARK 3 S21: 0.2386 S22: 0.0297 S23: -0.0726
REMARK 3 S31: -0.1368 S32: -0.0406 S33: 0.0988
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'Y' AND (RESID 1 THROUGH 114 )
REMARK 3 ORIGIN FOR THE GROUP (A): 102.9485 -82.2688 15.0324
REMARK 3 T TENSOR
REMARK 3 T11: 0.9275 T22: 1.0157
REMARK 3 T33: 1.2124 T12: 0.0476
REMARK 3 T13: -0.3324 T23: -0.0041
REMARK 3 L TENSOR
REMARK 3 L11: 0.9287 L22: 0.4614
REMARK 3 L33: 1.0126 L12: 0.0112
REMARK 3 L13: 0.2017 L23: -0.0736
REMARK 3 S TENSOR
REMARK 3 S11: -0.3491 S12: -0.2182 S13: 0.4647
REMARK 3 S21: 0.0922 S22: 0.1644 S23: -0.2858
REMARK 3 S31: -0.3341 S32: 0.2745 S33: 0.2029
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 3 THROUGH 271 )
REMARK 3 ORIGIN FOR THE GROUP (A): -5.9043 -17.9934 -11.8178
REMARK 3 T TENSOR
REMARK 3 T11: 1.4778 T22: 0.6091
REMARK 3 T33: 1.7747 T12: 0.2895
REMARK 3 T13: -0.0700 T23: 0.1568
REMARK 3 L TENSOR
REMARK 3 L11: 0.1534 L22: 0.1643
REMARK 3 L33: 0.1384 L12: 0.1381
REMARK 3 L13: -0.1178 L23: -0.1565
REMARK 3 S TENSOR
REMARK 3 S11: -0.0255 S12: -0.0368 S13: 0.2561
REMARK 3 S21: 0.4241 S22: 0.1094 S23: -0.1557
REMARK 3 S31: -0.2818 S32: -0.1308 S33: -0.1130
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 2 THROUGH 216 )
REMARK 3 ORIGIN FOR THE GROUP (A): -18.9982-121.9541 14.1547
REMARK 3 T TENSOR
REMARK 3 T11: 0.9796 T22: 0.9920
REMARK 3 T33: 0.6562 T12: 0.1720
REMARK 3 T13: 0.3554 T23: 0.1253
REMARK 3 L TENSOR
REMARK 3 L11: 0.8621 L22: 0.5932
REMARK 3 L33: 0.2012 L12: 0.1763
REMARK 3 L13: -0.2598 L23: -0.1189
REMARK 3 S TENSOR
REMARK 3 S11: -0.0079 S12: 0.1609 S13: -0.0898
REMARK 3 S21: 0.3332 S22: 0.0950 S23: 0.2028
REMARK 3 S31: 0.0235 S32: -0.1694 S33: -0.0685
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 3 THROUGH 201 )
REMARK 3 ORIGIN FOR THE GROUP (A): 39.9986 -85.4598 -72.9830
REMARK 3 T TENSOR
REMARK 3 T11: 0.7082 T22: 1.5628
REMARK 3 T33: 0.6817 T12: -0.1878
REMARK 3 T13: 0.0956 T23: 0.4007
REMARK 3 L TENSOR
REMARK 3 L11: 0.3018 L22: 0.2617
REMARK 3 L33: 0.9102 L12: 0.1117
REMARK 3 L13: -0.5340 L23: -0.1650
REMARK 3 S TENSOR
REMARK 3 S11: -0.2093 S12: 0.5067 S13: 0.0211
REMARK 3 S21: -0.1428 S22: 0.0807 S23: -0.0620
REMARK 3 S31: -0.0602 S32: -0.1249 S33: 0.0427
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 5 THROUGH 179 )
REMARK 3 ORIGIN FOR THE GROUP (A): 104.8619 -49.2872 36.4469
REMARK 3 T TENSOR
REMARK 3 T11: 1.5928 T22: 1.4560
REMARK 3 T33: 1.4917 T12: 0.0540
REMARK 3 T13: -0.5282 T23: -0.3785
REMARK 3 L TENSOR
REMARK 3 L11: 4.5105 L22: 1.4572
REMARK 3 L33: 2.0147 L12: -1.4387
REMARK 3 L13: 0.0870 L23: -1.4480
REMARK 3 S TENSOR
REMARK 3 S11: 0.3086 S12: -1.4047 S13: 0.4128
REMARK 3 S21: 1.2270 S22: 0.3044 S23: -0.9222
REMARK 3 S31: -0.0606 S32: 0.6413 S33: -0.5770
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 18 THROUGH 174 )
REMARK 3 ORIGIN FOR THE GROUP (A): 24.0513-135.3011 51.1397
REMARK 3 T TENSOR
REMARK 3 T11: 1.0689 T22: 1.1692
REMARK 3 T33: 2.2659 T12: 0.4187
REMARK 3 T13: 0.3146 T23: 0.3934
REMARK 3 L TENSOR
REMARK 3 L11: 0.7688 L22: 1.5706
REMARK 3 L33: 0.1324 L12: -1.0797
REMARK 3 L13: 0.0772 L23: -0.0194
REMARK 3 S TENSOR
REMARK 3 S11: 0.0935 S12: 0.2111 S13: -0.6277
REMARK 3 S21: 0.4501 S22: 0.0507 S23: 1.0848
REMARK 3 S31: 0.3620 S32: -0.0605 S33: -0.1547
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'G' AND (RESID 1 THROUGH 142)
REMARK 3 ORIGIN FOR THE GROUP (A): 22.2527-136.7040 2.1431
REMARK 3 T TENSOR
REMARK 3 T11: 0.9538 T22: 0.7384
REMARK 3 T33: 0.8011 T12: 0.3183
REMARK 3 T13: 0.2449 T23: 0.2148
REMARK 3 L TENSOR
REMARK 3 L11: 1.2633 L22: 0.4154
REMARK 3 L33: 0.6112 L12: 0.6226
REMARK 3 L13: -0.0608 L23: -0.1001
REMARK 3 S TENSOR
REMARK 3 S11: -0.1130 S12: -0.3727 S13: -0.5261
REMARK 3 S21: 0.5149 S22: -0.0029 S23: 0.0169
REMARK 3 S31: 0.0955 S32: -0.2755 S33: 0.0932
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 1 THROUGH 122 )
REMARK 3 ORIGIN FOR THE GROUP (A): -20.1746 -85.9105 41.2431
REMARK 3 T TENSOR
REMARK 3 T11: 1.5347 T22: 1.5584
REMARK 3 T33: 0.5925 T12: 0.4200
REMARK 3 T13: 0.2202 T23: -0.0709
REMARK 3 L TENSOR
REMARK 3 L11: 1.4205 L22: 0.7813
REMARK 3 L33: 1.2764 L12: 0.9302
REMARK 3 L13: -0.1826 L23: 0.0057
REMARK 3 S TENSOR
REMARK 3 S11: 0.1622 S12: -0.5350 S13: 0.2195
REMARK 3 S21: 0.6626 S22: -0.1625 S23: 0.2739
REMARK 3 S31: -0.0241 S32: -0.0840 S33: -0.0051
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'J' AND (RESID 1 THROUGH 141 )
REMARK 3 ORIGIN FOR THE GROUP (A): 57.5794 -89.8300 31.1462
REMARK 3 T TENSOR
REMARK 3 T11: 0.7938 T22: 1.5549
REMARK 3 T33: 0.6611 T12: 0.2201
REMARK 3 T13: -0.0715 T23: 0.0366
REMARK 3 L TENSOR
REMARK 3 L11: 1.6490 L22: 2.3782
REMARK 3 L33: 2.8640 L12: 0.7155
REMARK 3 L13: -0.1852 L23: 0.2271
REMARK 3 S TENSOR
REMARK 3 S11: -0.2632 S12: -1.2625 S13: 0.0590
REMARK 3 S21: 0.5046 S22: -0.2412 S23: -0.2696
REMARK 3 S31: 0.4403 S32: 0.2139 S33: 0.4882
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'K' AND (RESID 4 THROUGH 122 )
REMARK 3 ORIGIN FOR THE GROUP (A): -48.3806-101.8331 -13.9565
REMARK 3 T TENSOR
REMARK 3 T11: 0.4713 T22: 1.0547
REMARK 3 T33: 0.7538 T12: 0.1978
REMARK 3 T13: 0.2336 T23: 0.1140
REMARK 3 L TENSOR
REMARK 3 L11: 2.5300 L22: 1.8209
REMARK 3 L33: 0.3488 L12: -0.2826
REMARK 3 L13: -0.4697 L23: 0.7346
REMARK 3 S TENSOR
REMARK 3 S11: -0.0108 S12: 0.2312 S13: 0.0344
REMARK 3 S21: 0.2065 S22: -0.2141 S23: 0.5505
REMARK 3 S31: -0.1054 S32: -0.9025 S33: 0.2141
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'L' AND (RESID 5 THROUGH 111 )
REMARK 3 ORIGIN FOR THE GROUP (A): 117.7730 -66.7711 -1.9682
REMARK 3 T TENSOR
REMARK 3 T11: 0.6373 T22: 0.8709
REMARK 3 T33: 1.5847 T12: -0.1412
REMARK 3 T13: -0.3452 T23: 0.3240
REMARK 3 L TENSOR
REMARK 3 L11: 2.7767 L22: 1.4587
REMARK 3 L33: 2.8241 L12: 0.5338
REMARK 3 L13: -1.8360 L23: 0.3016
REMARK 3 S TENSOR
REMARK 3 S11: -0.3815 S12: 0.4301 S13: 0.5977
REMARK 3 S21: 0.1937 S22: -0.0737 S23: -0.7048
REMARK 3 S31: -0.3098 S32: 0.4641 S33: 0.4345
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'M' AND (RESID 1 THROUGH 110 )
REMARK 3 ORIGIN FOR THE GROUP (A): -42.7911 -98.6956 32.4881
REMARK 3 T TENSOR
REMARK 3 T11: 0.8404 T22: 1.4102
REMARK 3 T33: 0.7744 T12: 0.3444
REMARK 3 T13: 0.3631 T23: 0.0643
REMARK 3 L TENSOR
REMARK 3 L11: 2.4932 L22: 3.5196
REMARK 3 L33: 1.6326 L12: -0.0744
REMARK 3 L13: -1.3726 L23: 0.5736
REMARK 3 S TENSOR
REMARK 3 S11: -0.0936 S12: -0.4934 S13: 0.0510
REMARK 3 S21: 0.4883 S22: 0.0773 S23: 0.2774
REMARK 3 S31: -0.0527 S32: -0.1117 S33: 0.0126
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN 'N' AND (RESID 2 THROUGH 117 )
REMARK 3 ORIGIN FOR THE GROUP (A): 35.4690-127.4057 -23.2580
REMARK 3 T TENSOR
REMARK 3 T11: 0.6223 T22: 0.7576
REMARK 3 T33: 0.6772 T12: 0.1630
REMARK 3 T13: 0.3477 T23: 0.0756
REMARK 3 L TENSOR
REMARK 3 L11: 1.3380 L22: 1.5192
REMARK 3 L33: 0.6330 L12: -0.6863
REMARK 3 L13: 0.1505 L23: -0.2981
REMARK 3 S TENSOR
REMARK 3 S11: -0.2875 S12: 0.2110 S13: -0.4327
REMARK 3 S21: 0.2085 S22: 0.1540 S23: -0.0099
REMARK 3 S31: 0.0889 S32: -0.0797 S33: 0.1213
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: CHAIN 'O' AND (RESID 1 THROUGH 101 )
REMARK 3 ORIGIN FOR THE GROUP (A): 43.6296-134.8646 -35.1406
REMARK 3 T TENSOR
REMARK 3 T11: 0.5447 T22: 0.6712
REMARK 3 T33: 0.7100 T12: 0.1121
REMARK 3 T13: 0.2637 T23: -0.0181
REMARK 3 L TENSOR
REMARK 3 L11: 1.4989 L22: 2.0680
REMARK 3 L33: 1.7337 L12: -0.2586
REMARK 3 L13: -0.1361 L23: 0.1291
REMARK 3 S TENSOR
REMARK 3 S11: -0.0104 S12: 0.5066 S13: -0.4366
REMARK 3 S21: -0.2350 S22: -0.2254 S23: 0.0206
REMARK 3 S31: 0.5845 S32: 0.3627 S33: 0.2152
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: CHAIN 'P' AND (RESID 1 THROUGH 112 )
REMARK 3 ORIGIN FOR THE GROUP (A): -14.8657-111.0819 -39.6728
REMARK 3 T TENSOR
REMARK 3 T11: 0.6676 T22: 1.3013
REMARK 3 T33: 0.5859 T12: -0.1133
REMARK 3 T13: 0.1960 T23: 0.1085
REMARK 3 L TENSOR
REMARK 3 L11: 1.9416 L22: 3.1213
REMARK 3 L33: 1.7055 L12: 1.1421
REMARK 3 L13: 0.7062 L23: 0.1835
REMARK 3 S TENSOR
REMARK 3 S11: -0.3769 S12: 0.1910 S13: -0.3292
REMARK 3 S21: -0.3178 S22: 0.3511 S23: 0.0866
REMARK 3 S31: 0.4256 S32: -0.3804 S33: 0.0563
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: CHAIN 'Q' AND (RESID 2 THROUGH 91 )
REMARK 3 ORIGIN FOR THE GROUP (A): -34.7505 -60.7925 -62.2885
REMARK 3 T TENSOR
REMARK 3 T11: 1.0147 T22: 1.5203
REMARK 3 T33: 1.2128 T12: 0.2901
REMARK 3 T13: -0.0493 T23: 0.6797
REMARK 3 L TENSOR
REMARK 3 L11: 2.6864 L22: 2.1799
REMARK 3 L33: 2.8322 L12: -0.5868
REMARK 3 L13: 0.8803 L23: -1.1459
REMARK 3 S TENSOR
REMARK 3 S11: -0.0871 S12: 0.1211 S13: 0.0624
REMARK 3 S21: -0.0976 S22: 0.0121 S23: 0.0023
REMARK 3 S31: -0.1937 S32: -0.6531 S33: 0.0245
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: CHAIN 'R' AND (RESID 3 THROUGH 102 )
REMARK 3 ORIGIN FOR THE GROUP (A): -4.2614 -95.9300 -90.4977
REMARK 3 T TENSOR
REMARK 3 T11: 0.7087 T22: 1.8408
REMARK 3 T33: 0.7235 T12: -0.1739
REMARK 3 T13: 0.1085 T23: -0.0285
REMARK 3 L TENSOR
REMARK 3 L11: 3.4768 L22: 2.1586
REMARK 3 L33: 3.2237 L12: 0.9067
REMARK 3 L13: 0.5923 L23: -0.6835
REMARK 3 S TENSOR
REMARK 3 S11: -0.1898 S12: 0.9693 S13: 0.0682
REMARK 3 S21: -0.1311 S22: 0.2686 S23: -0.3554
REMARK 3 S31: 0.1680 S32: -0.5667 S33: -0.1674
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: CHAIN 'S' AND (RESID 3 THROUGH 169 )
REMARK 3 ORIGIN FOR THE GROUP (A): 83.1046-107.8543 34.9331
REMARK 3 T TENSOR
REMARK 3 T11: 0.8039 T22: 1.2382
REMARK 3 T33: 0.8047 T12: 0.2635
REMARK 3 T13: -0.1458 T23: 0.1253
REMARK 3 L TENSOR
REMARK 3 L11: 3.4864 L22: 3.4925
REMARK 3 L33: 2.2075 L12: -0.3894
REMARK 3 L13: -0.4091 L23: 1.0751
REMARK 3 S TENSOR
REMARK 3 S11: -0.1289 S12: -1.0055 S13: 0.3075
REMARK 3 S21: 0.5032 S22: 0.4159 S23: -0.1718
REMARK 3 S31: 0.2855 S32: 0.1498 S33: -0.2662
REMARK 3 TLS GROUP : 24
REMARK 3 SELECTION: CHAIN 'T' AND (RESID 19 THROUGH 94 )
REMARK 3 ORIGIN FOR THE GROUP (A): 84.6876 -77.0680 -8.1695
REMARK 3 T TENSOR
REMARK 3 T11: 0.6418 T22: 0.7758
REMARK 3 T33: 1.0628 T12: -0.0019
REMARK 3 T13: -0.2244 T23: 0.2378
REMARK 3 L TENSOR
REMARK 3 L11: 5.7985 L22: 3.0935
REMARK 3 L33: 2.6930 L12: -0.9379
REMARK 3 L13: -1.1274 L23: 0.6977
REMARK 3 S TENSOR
REMARK 3 S11: 0.0360 S12: -0.8301 S13: 0.2796
REMARK 3 S21: 0.0656 S22: -0.1631 S23: -0.9376
REMARK 3 S31: 0.2113 S32: 0.4569 S33: 0.1624
REMARK 3 TLS GROUP : 25
REMARK 3 SELECTION: CHAIN 'U' AND (RESID 13 THROUGH 54 )
REMARK 3 ORIGIN FOR THE GROUP (A): 25.0966 -24.7850 -41.3529
REMARK 3 T TENSOR
REMARK 3 T11: 2.1696 T22: 1.5220
REMARK 3 T33: 2.4438 T12: 0.2568
REMARK 3 T13: -0.1036 T23: 1.0066
REMARK 3 L TENSOR
REMARK 3 L11: 2.2180 L22: 2.9089
REMARK 3 L33: 0.6813 L12: -0.4955
REMARK 3 L13: -1.0896 L23: 0.8829
REMARK 3 S TENSOR
REMARK 3 S11: 0.2968 S12: 0.1253 S13: -0.1255
REMARK 3 S21: -0.3794 S22: -0.1508 S23: 0.1308
REMARK 3 S31: -0.1076 S32: -0.2811 S33: -0.1384
REMARK 3 TLS GROUP : 26
REMARK 3 SELECTION: CHAIN 'V' AND (RESID 2 THROUGH 66 )
REMARK 3 ORIGIN FOR THE GROUP (A): -25.2202 -59.2235 -83.9137
REMARK 3 T TENSOR
REMARK 3 T11: 1.9451 T22: 2.3073
REMARK 3 T33: 0.9817 T12: 0.6144
REMARK 3 T13: -0.2190 T23: 0.4832
REMARK 3 L TENSOR
REMARK 3 L11: 2.1286 L22: 0.6000
REMARK 3 L33: 1.7913 L12: 0.5126
REMARK 3 L13: -0.0179 L23: -0.0324
REMARK 3 S TENSOR
REMARK 3 S11: -0.1392 S12: 0.4948 S13: 0.5239
REMARK 3 S21: -0.4582 S22: -0.0441 S23: -0.1388
REMARK 3 S31: 0.4803 S32: -0.1419 S33: 0.1892
REMARK 3 TLS GROUP : 27
REMARK 3 SELECTION: CHAIN 'W' AND (RESID 2 THROUGH 58 )
REMARK 3 ORIGIN FOR THE GROUP (A): 68.7796-113.7764 -15.3595
REMARK 3 T TENSOR
REMARK 3 T11: 0.5956 T22: 0.5593
REMARK 3 T33: 0.7686 T12: 0.0359
REMARK 3 T13: 0.0521 T23: 0.0984
REMARK 3 L TENSOR
REMARK 3 L11: 7.7309 L22: 3.4215
REMARK 3 L33: 5.5481 L12: 0.7853
REMARK 3 L13: -1.2274 L23: 1.5175
REMARK 3 S TENSOR
REMARK 3 S11: -0.2029 S12: 0.1322 S13: -0.2456
REMARK 3 S21: -0.1126 S22: 0.0783 S23: -0.8303
REMARK 3 S31: 0.4984 S32: 0.1508 S33: 0.1182
REMARK 3 TLS GROUP : 28
REMARK 3 SELECTION: CHAIN 'Z' AND (RESID 2 THROUGH 44 )
REMARK 3 ORIGIN FOR THE GROUP (A): -14.7962-113.6837 -24.5189
REMARK 3 T TENSOR
REMARK 3 T11: 0.6157 T22: 0.9666
REMARK 3 T33: 0.6011 T12: -0.0515
REMARK 3 T13: 0.3524 T23: 0.1313
REMARK 3 L TENSOR
REMARK 3 L11: 1.6244 L22: 0.9663
REMARK 3 L33: 0.9108 L12: -0.5088
REMARK 3 L13: -0.4246 L23: -0.3030
REMARK 3 S TENSOR
REMARK 3 S11: -0.3427 S12: 0.4397 S13: -0.7194
REMARK 3 S21: 0.1403 S22: 0.2146 S23: 0.2431
REMARK 3 S31: 0.3932 S32: -0.4294 S33: 0.1113
REMARK 3 TLS GROUP : 29
REMARK 3 SELECTION: CHAIN '2' AND (RESID 2 THROUGH 44 )
REMARK 3 ORIGIN FOR THE GROUP (A): -3.4025 -54.7272 -43.1261
REMARK 3 T TENSOR
REMARK 3 T11: 0.7574 T22: 1.3712
REMARK 3 T33: 0.9977 T12: 0.0920
REMARK 3 T13: -0.1179 T23: 0.5999
REMARK 3 L TENSOR
REMARK 3 L11: 0.6058 L22: 0.4063
REMARK 3 L33: 1.0047 L12: 0.0269
REMARK 3 L13: 0.1384 L23: -0.2069
REMARK 3 S TENSOR
REMARK 3 S11: -0.0118 S12: 0.1947 S13: 0.3495
REMARK 3 S21: -0.0715 S22: 0.0008 S23: 0.1037
REMARK 3 S31: -0.2611 S32: -0.2389 S33: -0.0492
REMARK 3 TLS GROUP : 30
REMARK 3 SELECTION: CHAIN '3' AND (RESID 2 THROUGH 61 )
REMARK 3 ORIGIN FOR THE GROUP (A): 63.7041 -61.6483 -33.2823
REMARK 3 T TENSOR
REMARK 3 T11: 0.5496 T22: 0.8139
REMARK 3 T33: 0.8691 T12: -0.0229
REMARK 3 T13: -0.0987 T23: 0.3469
REMARK 3 L TENSOR
REMARK 3 L11: 1.3054 L22: 1.2051
REMARK 3 L33: 0.3320 L12: -0.3603
REMARK 3 L13: -0.4323 L23: -0.3253
REMARK 3 S TENSOR
REMARK 3 S11: -0.2680 S12: -0.0538 S13: 0.1677
REMARK 3 S21: -0.0960 S22: 0.4258 S23: -0.0082
REMARK 3 S31: -0.0149 S32: -0.1493 S33: -0.1458
REMARK 3 TLS GROUP : 31
REMARK 3 SELECTION: CHAIN '4' AND (RESID 1 THROUGH 36 )
REMARK 3 ORIGIN FOR THE GROUP (A): 36.1488-112.4689 43.6527
REMARK 3 T TENSOR
REMARK 3 T11: 2.6871 T22: 2.0621
REMARK 3 T33: 1.3522 T12: -0.1679
REMARK 3 T13: -0.1600 T23: 0.3865
REMARK 3 L TENSOR
REMARK 3 L11: 3.3086 L22: 1.2211
REMARK 3 L33: 8.8757 L12: 0.4249
REMARK 3 L13: 1.0149 L23: 0.1556
REMARK 3 S TENSOR
REMARK 3 S11: 0.3141 S12: 0.1156 S13: -0.1840
REMARK 3 S21: 0.1256 S22: 0.2544 S23: 0.2333
REMARK 3 S31: 0.3715 S32: -0.5019 S33: -0.5168
REMARK 3 TLS GROUP : 32
REMARK 3 SELECTION: CHAIN 'I' AND (RESID 1 THROUGH 131 )
REMARK 3 ORIGIN FOR THE GROUP (A): 63.5328 -70.2218 -53.6786
REMARK 3 T TENSOR
REMARK 3 T11: 0.7795 T22: 1.3087
REMARK 3 T33: 0.9039 T12: -0.0835
REMARK 3 T13: 0.1004 T23: 0.4561
REMARK 3 L TENSOR
REMARK 3 L11: 0.7376 L22: 0.3791
REMARK 3 L33: 0.0558 L12: 0.4776
REMARK 3 L13: -0.1613 L23: -0.1041
REMARK 3 S TENSOR
REMARK 3 S11: -0.1414 S12: 0.4681 S13: -0.0545
REMARK 3 S21: -0.1125 S22: 0.0324 S23: -0.3302
REMARK 3 S31: -0.2364 S32: 0.3011 S33: 0.0810
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 5HL7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-JAN-16.
REMARK 100 THE DEPOSITION ID IS D_1000217244.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-JUN-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.971
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 : NULL
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 236087
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.550
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.7
REMARK 200 DATA REDUNDANCY : 11.00
REMARK 200 R MERGE (I) : 0.20900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.55
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.61
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.6
REMARK 200 DATA REDUNDANCY IN SHELL : 9.20
REMARK 200 R MERGE FOR SHELL (I) : 0.99400
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: NULL
REMARK 200 STARTING MODEL: 4WCE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 67.27
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.76
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1:2 MPD:ETOH 10MM HEPES PH=7.6 10MM
REMARK 280 MG2CL 60MM NH4CL 15MM KCL, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
REMARK 290 7555 Y,X,-Z+2/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+1/3
REMARK 290 10555 -Y,-X,-Z+1/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+5/6
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 583.56200
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 291.78100
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 437.67150
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 145.89050
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 729.45250
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 583.56200
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 291.78100
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 145.89050
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 437.67150
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 729.45250
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 28-MERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: 28-MERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 131140 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 467320 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -1270.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, X, Y, B, C, D, E, G, H, I,
REMARK 350 AND CHAINS: J, K, L, M, N, O, P, Q, R,
REMARK 350 AND CHAINS: S, T, U, V, W, Z, 2, 3, 4
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 MET A 1
REMARK 465 ALA A 2
REMARK 465 ARG A 272
REMARK 465 GLY A 273
REMARK 465 ARG A 274
REMARK 465 LYS A 275
REMARK 465 LYS A 276
REMARK 465 LYS A 277
REMARK 465 G X 1
REMARK 465 G X 160
REMARK 465 A X 161
REMARK 465 A X 314
REMARK 465 C X 315
REMARK 465 G X 316
REMARK 465 U X 759
REMARK 465 A X 760
REMARK 465 A X 761
REMARK 465 C X 762
REMARK 465 A X 763
REMARK 465 G X 926
REMARK 465 G X 927
REMARK 465 C X 928
REMARK 465 C X 929
REMARK 465 C X 930
REMARK 465 C X 931
REMARK 465 U X 932
REMARK 465 C X 933
REMARK 465 U X 934
REMARK 465 C X 935
REMARK 465 G X 936
REMARK 465 G X 937
REMARK 465 G X 1100
REMARK 465 A X 1101
REMARK 465 U X 1102
REMARK 465 G X 1103
REMARK 465 U X 1104
REMARK 465 U X 1105
REMARK 465 G X 1106
REMARK 465 G X 1107
REMARK 465 C X 1108
REMARK 465 U X 1109
REMARK 465 U X 1110
REMARK 465 A X 1111
REMARK 465 G X 1112
REMARK 465 A X 1113
REMARK 465 A X 1114
REMARK 465 G X 1115
REMARK 465 C X 1116
REMARK 465 A X 1117
REMARK 465 G X 1118
REMARK 465 C X 1119
REMARK 465 C X 1120
REMARK 465 A X 1121
REMARK 465 U X 1122
REMARK 465 C X 1123
REMARK 465 A X 1124
REMARK 465 U X 1125
REMARK 465 U X 1126
REMARK 465 U X 1127
REMARK 465 A X 1128
REMARK 465 A X 1129
REMARK 465 A X 1130
REMARK 465 G X 1131
REMARK 465 A X 1132
REMARK 465 G X 1133
REMARK 465 U X 1134
REMARK 465 G X 1135
REMARK 465 C X 1136
REMARK 465 G X 1137
REMARK 465 U X 1138
REMARK 465 A X 1139
REMARK 465 A X 1140
REMARK 465 U X 1141
REMARK 465 A X 1142
REMARK 465 G X 1143
REMARK 465 U X 1216
REMARK 465 U X 1448
REMARK 465 A X 1449
REMARK 465 A X 1450
REMARK 465 U X 1451
REMARK 465 U X 1455
REMARK 465 U X 1456
REMARK 465 U X 1457
REMARK 465 A X 1458
REMARK 465 A X 1520
REMARK 465 U X 1525
REMARK 465 U X 1531
REMARK 465 U X 1532
REMARK 465 A X 1533
REMARK 465 G X 1534
REMARK 465 G X 1535
REMARK 465 C X 1536
REMARK 465 A X 1537
REMARK 465 A X 1538
REMARK 465 U X 1552
REMARK 465 A X 1553
REMARK 465 A X 1554
REMARK 465 C X 1579
REMARK 465 A X 1580
REMARK 465 U X 1581
REMARK 465 U X 1582
REMARK 465 G X 1583
REMARK 465 A X 1584
REMARK 465 G X 1585
REMARK 465 U X 1586
REMARK 465 C X 1587
REMARK 465 U X 1588
REMARK 465 U X 1589
REMARK 465 C X 1590
REMARK 465 A X 1633
REMARK 465 A X 1634
REMARK 465 G X 1866
REMARK 465 U X 1897
REMARK 465 C X 1898
REMARK 465 U X 1899
REMARK 465 C X 1935
REMARK 465 C X 1936
REMARK 465 G X 1937
REMARK 465 U X 1938
REMARK 465 A X 1939
REMARK 465 A X 1940
REMARK 465 C X 1941
REMARK 465 U X 1942
REMARK 465 A X 1943
REMARK 465 U X 1944
REMARK 465 A X 1945
REMARK 465 A X 1946
REMARK 465 C X 1947
REMARK 465 G X 1948
REMARK 465 G X 1949
REMARK 465 U X 1950
REMARK 465 C X 1951
REMARK 465 G X 2128
REMARK 465 C X 2129
REMARK 465 A X 2130
REMARK 465 C X 2131
REMARK 465 A X 2132
REMARK 465 G X 2133
REMARK 465 C X 2134
REMARK 465 U X 2135
REMARK 465 U X 2136
REMARK 465 G X 2137
REMARK 465 U X 2138
REMARK 465 A X 2139
REMARK 465 C X 2140
REMARK 465 A X 2141
REMARK 465 G X 2142
REMARK 465 G X 2143
REMARK 465 A X 2144
REMARK 465 U X 2145
REMARK 465 A X 2146
REMARK 465 G X 2147
REMARK 465 G X 2148
REMARK 465 U X 2149
REMARK 465 A X 2150
REMARK 465 G X 2151
REMARK 465 G X 2152
REMARK 465 A X 2153
REMARK 465 G X 2154
REMARK 465 C X 2155
REMARK 465 C X 2156
REMARK 465 U X 2157
REMARK 465 U X 2158
REMARK 465 U X 2159
REMARK 465 G X 2160
REMARK 465 A X 2161
REMARK 465 A X 2162
REMARK 465 A X 2163
REMARK 465 C X 2164
REMARK 465 G X 2165
REMARK 465 U X 2166
REMARK 465 G X 2167
REMARK 465 A X 2168
REMARK 465 G X 2169
REMARK 465 C X 2170
REMARK 465 G X 2171
REMARK 465 C X 2172
REMARK 465 U X 2173
REMARK 465 A X 2174
REMARK 465 G X 2175
REMARK 465 C X 2176
REMARK 465 U X 2177
REMARK 465 U X 2178
REMARK 465 A X 2179
REMARK 465 C X 2180
REMARK 465 G X 2181
REMARK 465 U X 2182
REMARK 465 G X 2183
REMARK 465 G X 2184
REMARK 465 A X 2185
REMARK 465 G X 2186
REMARK 465 G X 2187
REMARK 465 C X 2188
REMARK 465 G X 2189
REMARK 465 C X 2190
REMARK 465 U X 2191
REMARK 465 G X 2192
REMARK 465 G X 2193
REMARK 465 U X 2194
REMARK 465 G X 2195
REMARK 465 G X 2196
REMARK 465 G X 2197
REMARK 465 A X 2198
REMARK 465 U X 2199
REMARK 465 A X 2200
REMARK 465 C X 2201
REMARK 465 U X 2202
REMARK 465 A X 2203
REMARK 465 C X 2204
REMARK 465 C X 2205
REMARK 465 C X 2206
REMARK 465 U X 2207
REMARK 465 A X 2208
REMARK 465 G X 2209
REMARK 465 C X 2210
REMARK 465 U X 2211
REMARK 465 G X 2212
REMARK 465 U X 2213
REMARK 465 G X 2214
REMARK 465 U X 2215
REMARK 465 U X 2216
REMARK 465 G X 2335
REMARK 465 C X 2822
REMARK 465 C X 2921
REMARK 465 A X 2922
REMARK 465 A X 2923
REMARK 465 MET B 1
REMARK 465 LYS B 217
REMARK 465 GLY B 218
REMARK 465 ASN B 219
REMARK 465 LYS B 220
REMARK 465 MET C 1
REMARK 465 ALA C 2
REMARK 465 VAL C 202
REMARK 465 GLU C 203
REMARK 465 GLU C 204
REMARK 465 VAL C 205
REMARK 465 LEU C 206
REMARK 465 GLY C 207
REMARK 465 MET D 1
REMARK 465 ASN D 2
REMARK 465 ARG D 3
REMARK 465 LEU D 4
REMARK 465 LEU D 170
REMARK 465 ALA D 171
REMARK 465 ASN D 172
REMARK 465 PHE D 173
REMARK 465 GLY D 174
REMARK 465 MET D 175
REMARK 465 PRO D 176
REMARK 465 PHE D 177
REMARK 465 ARG D 178
REMARK 465 LYS D 179
REMARK 465 MET E 1
REMARK 465 SER E 2
REMARK 465 ARG E 3
REMARK 465 VAL E 4
REMARK 465 GLY E 5
REMARK 465 LYS E 6
REMARK 465 LYS E 7
REMARK 465 ILE E 8
REMARK 465 ILE E 9
REMARK 465 ASP E 10
REMARK 465 ILE E 11
REMARK 465 PRO E 12
REMARK 465 SER E 13
REMARK 465 ASP E 14
REMARK 465 VAL E 15
REMARK 465 THR E 16
REMARK 465 VAL E 17
REMARK 465 LYS E 175
REMARK 465 THR E 176
REMARK 465 GLY E 177
REMARK 465 LYS E 178
REMARK 465 ALA I 132
REMARK 465 ALA I 133
REMARK 465 GLU I 134
REMARK 465 ALA I 135
REMARK 465 ILE I 136
REMARK 465 ASP I 137
REMARK 465 ALA I 138
REMARK 465 LYS I 139
REMARK 465 GLY I 140
REMARK 465 GLY J 139
REMARK 465 GLU J 140
REMARK 465 THR J 141
REMARK 465 ASN J 142
REMARK 465 GLU J 143
REMARK 465 SER J 144
REMARK 465 MET K 1
REMARK 465 GLY K 2
REMARK 465 TYR K 3
REMARK 465 MET L 1
REMARK 465 ALA L 111
REMARK 465 ALA L 112
REMARK 465 ARG L 113
REMARK 465 GLU L 114
REMARK 465 SER L 115
REMARK 465 GLY L 116
REMARK 465 LEU L 117
REMARK 465 GLU L 118
REMARK 465 PHE L 119
REMARK 465 ARG M 111
REMARK 465 ILE M 112
REMARK 465 GLN M 113
REMARK 465 GLU M 114
REMARK 465 ILE M 115
REMARK 465 ARG M 116
REMARK 465 MET N 1
REMARK 465 LYS N 118
REMARK 465 GLU P 113
REMARK 465 ALA P 114
REMARK 465 LYS P 115
REMARK 465 GLU P 116
REMARK 465 ALA P 117
REMARK 465 MET Q 1
REMARK 465 MET R 1
REMARK 465 HIS R 2
REMARK 465 ASN R 105
REMARK 465 MET S 1
REMARK 465 ALA S 2
REMARK 465 ASP S 170
REMARK 465 SER S 171
REMARK 465 ALA S 172
REMARK 465 GLU S 173
REMARK 465 SER S 174
REMARK 465 VAL S 175
REMARK 465 VAL S 176
REMARK 465 THR S 177
REMARK 465 VAL S 178
REMARK 465 VAL S 179
REMARK 465 ALA S 180
REMARK 465 PRO S 181
REMARK 465 THR S 182
REMARK 465 GLU S 183
REMARK 465 GLU S 184
REMARK 465 PRO S 185
REMARK 465 THR S 186
REMARK 465 GLU S 187
REMARK 465 GLU S 188
REMARK 465 GLU S 189
REMARK 465 ILE S 190
REMARK 465 GLU S 191
REMARK 465 ALA S 192
REMARK 465 MET S 193
REMARK 465 GLU S 194
REMARK 465 GLY S 195
REMARK 465 GLU S 196
REMARK 465 GLN S 197
REMARK 465 GLN S 198
REMARK 465 THR S 199
REMARK 465 GLU S 200
REMARK 465 GLU S 201
REMARK 465 PRO S 202
REMARK 465 GLU S 203
REMARK 465 VAL S 204
REMARK 465 VAL S 205
REMARK 465 GLY S 206
REMARK 465 GLU S 207
REMARK 465 SER S 208
REMARK 465 LYS S 209
REMARK 465 GLU S 210
REMARK 465 ASP S 211
REMARK 465 GLU S 212
REMARK 465 GLU S 213
REMARK 465 LYS S 214
REMARK 465 THR S 215
REMARK 465 GLU S 216
REMARK 465 GLU S 217
REMARK 465 MET T 1
REMARK 465 LEU T 2
REMARK 465 LYS T 3
REMARK 465 LEU T 4
REMARK 465 ASN T 5
REMARK 465 LEU T 6
REMARK 465 GLN T 7
REMARK 465 PHE T 8
REMARK 465 PHE T 9
REMARK 465 ALA T 10
REMARK 465 SER T 11
REMARK 465 LYS T 12
REMARK 465 LYS T 13
REMARK 465 GLY T 14
REMARK 465 VAL T 15
REMARK 465 SER T 16
REMARK 465 SER T 17
REMARK 465 THR T 18
REMARK 465 GLU T 94
REMARK 465 MET U 1
REMARK 465 GLY U 2
REMARK 465 LYS U 3
REMARK 465 GLN U 4
REMARK 465 CYS U 5
REMARK 465 PHE U 6
REMARK 465 VAL U 7
REMARK 465 THR U 8
REMARK 465 GLY U 9
REMARK 465 ARG U 10
REMARK 465 LYS U 11
REMARK 465 ALA U 12
REMARK 465 LYS U 55
REMARK 465 SER U 56
REMARK 465 GLY U 57
REMARK 465 LYS U 58
REMARK 465 VAL U 59
REMARK 465 THR U 60
REMARK 465 ARG U 61
REMARK 465 VAL U 62
REMARK 465 MET V 1
REMARK 465 ALA V 67
REMARK 465 ASN V 68
REMARK 465 GLN V 69
REMARK 465 MET W 1
REMARK 465 LYS W 59
REMARK 465 MET Z 1
REMARK 465 LYS Z 45
REMARK 465 ASN Z 46
REMARK 465 CYS Z 47
REMARK 465 GLY Z 48
REMARK 465 SER Z 49
REMARK 465 TYR Z 50
REMARK 465 ASN Z 51
REMARK 465 GLY Z 52
REMARK 465 GLU Z 53
REMARK 465 GLU Z 54
REMARK 465 VAL Z 55
REMARK 465 ALA Z 56
REMARK 465 ALA Z 57
REMARK 465 LYS Z 58
REMARK 465 MET 2 1
REMARK 465 ALA 2 45
REMARK 465 MET 3 1
REMARK 465 LEU 3 62
REMARK 465 ALA 3 63
REMARK 465 TYR 3 64
REMARK 465 LYS 3 65
REMARK 465 LYS 3 66
REMARK 465 GLY 4 37
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ILE A 3 CG1 CG2 CD1
REMARK 470 LYS A 4 CG CD CE NZ
REMARK 470 LYS A 5 CG CD CE NZ
REMARK 470 LYS A 7 CG CD CE NZ
REMARK 470 ARG A 13 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 19 CG CD1 CD2
REMARK 470 ASP A 20 CG OD1 OD2
REMARK 470 PHE A 21 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU A 23 CG CD OE1 OE2
REMARK 470 ILE A 24 CG1 CG2 CD1
REMARK 470 THR A 25 OG1 CG2
REMARK 470 LYS A 26 CG CD CE NZ
REMARK 470 THR A 28 OG1 CG2
REMARK 470 LYS A 31 CG CD CE NZ
REMARK 470 LEU A 34 CG CD1 CD2
REMARK 470 LYS A 35 CG CD CE NZ
REMARK 470 PRO A 36 CG CD
REMARK 470 LEU A 37 CG CD1 CD2
REMARK 470 LYS A 39 CG CD CE NZ
REMARK 470 LYS A 40 CG CD CE NZ
REMARK 470 THR A 50 OG1 CG2
REMARK 470 VAL A 51 CG1 CG2
REMARK 470 ARG A 52 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 61 CG CD OE1 NE2
REMARK 470 TYR A 62 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ARG A 63 CG CD NE CZ NH1 NH2
REMARK 470 VAL A 64 CG1 CG2
REMARK 470 ILE A 65 CG1 CG2 CD1
REMARK 470 ASP A 66 CG OD1 OD2
REMARK 470 PHE A 67 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS A 68 CG CD CE NZ
REMARK 470 ARG A 69 CG CD NE CZ NH1 NH2
REMARK 470 ASN A 70 CG OD1 ND2
REMARK 470 LYS A 71 CG CD CE NZ
REMARK 470 ASP A 72 CG OD1 OD2
REMARK 470 ILE A 74 CG1 CG2 CD1
REMARK 470 LYS A 77 CG CD CE NZ
REMARK 470 GLN A 82 CG CD OE1 NE2
REMARK 470 TYR A 83 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ARG A 87 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 93 CG CD1 CD2
REMARK 470 VAL A 94 CG1 CG2
REMARK 470 GLU A 100 CG CD OE1 OE2
REMARK 470 LYS A 101 CG CD CE NZ
REMARK 470 ARG A 102 CG CD NE CZ NH1 NH2
REMARK 470 ILE A 104 CG1 CG2 CD1
REMARK 470 LYS A 108 CG CD CE NZ
REMARK 470 LEU A 110 CG CD1 CD2
REMARK 470 GLU A 111 CG CD OE1 OE2
REMARK 470 VAL A 112 CG1 CG2
REMARK 470 GLN A 114 CG CD OE1 NE2
REMARK 470 ILE A 115 CG1 CG2 CD1
REMARK 470 VAL A 116 CG1 CG2
REMARK 470 GLU A 117 CG CD OE1 OE2
REMARK 470 SER A 118 OG
REMARK 470 GLU A 121 CG CD OE1 OE2
REMARK 470 ILE A 124 CG1 CG2 CD1
REMARK 470 LYS A 125 CG CD CE NZ
REMARK 470 VAL A 126 CG1 CG2
REMARK 470 LEU A 132 CG CD1 CD2
REMARK 470 GLN A 133 CG CD OE1 NE2
REMARK 470 ASN A 134 CG OD1 ND2
REMARK 470 ILE A 135 CG1 CG2 CD1
REMARK 470 VAL A 137 CG1 CG2
REMARK 470 THR A 139 OG1 CG2
REMARK 470 GLU A 145 CG CD OE1 OE2
REMARK 470 LEU A 146 CG CD1 CD2
REMARK 470 LYS A 147 CG CD CE NZ
REMARK 470 LYS A 150 CG CD CE NZ
REMARK 470 GLN A 163 CG CD OE1 NE2
REMARK 470 VAL A 164 CG1 CG2
REMARK 470 LEU A 165 CG CD1 CD2
REMARK 470 LYS A 167 CG CD CE NZ
REMARK 470 GLU A 168 CG CD OE1 OE2
REMARK 470 LYS A 170 CG CD CE NZ
REMARK 470 VAL A 172 CG1 CG2
REMARK 470 LEU A 173 CG CD1 CD2
REMARK 470 ILE A 174 CG1 CG2 CD1
REMARK 470 ARG A 175 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 176 CG CD1 CD2
REMARK 470 ARG A 177 CG CD NE CZ NH1 NH2
REMARK 470 SER A 178 OG
REMARK 470 GLU A 180 CG CD OE1 OE2
REMARK 470 ILE A 184 CG1 CG2 CD1
REMARK 470 LEU A 185 CG CD1 CD2
REMARK 470 ARG A 189 CG CD NE CZ NH1 NH2
REMARK 470 ILE A 192 CG1 CG2 CD1
REMARK 470 LYS A 207 CG CD CE NZ
REMARK 470 ARG A 210 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 214 CG CD CE NZ
REMARK 470 ARG A 238 CG CD NE CZ NH1 NH2
REMARK 470 SER A 245 OG
REMARK 470 SER A 248 OG
REMARK 470 LYS A 252 CG CD CE NZ
REMARK 470 LEU A 255 CG CD1 CD2
REMARK 470 LYS A 257 CG CD CE NZ
REMARK 470 LYS A 258 CG CD CE NZ
REMARK 470 THR A 259 OG1 CG2
REMARK 470 ARG A 260 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 261 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 263 CG CD CE NZ
REMARK 470 LYS A 264 CG CD CE NZ
REMARK 470 ASP A 267 CG OD1 OD2
REMARK 470 LYS A 268 CG CD CE NZ
REMARK 470 LEU A 269 CG CD1 CD2
REMARK 470 ILE A 270 CG1 CG2 CD1
REMARK 470 A X 417 N9 C8 N7 C5 C6 N6 N1
REMARK 470 A X 417 C2 N3 C4
REMARK 470 U X 690 N1 C2 O2 N3 C4 O4 C5
REMARK 470 U X 690 C6
REMARK 470 A X1070 N9 C8 N7 C5 C6 N6 N1
REMARK 470 A X1070 C2 N3 C4
REMARK 470 A X1147 N9 C8 N7 C5 C6 N6 N1
REMARK 470 A X1147 C2 N3 C4
REMARK 470 LYS B 3 CG CD CE NZ
REMARK 470 GLU B 18 CG CD OE1 OE2
REMARK 470 GLU B 21 CG CD OE1 OE2
REMARK 470 LYS B 31 CG CD CE NZ
REMARK 470 GLU B 42 CG CD OE1 OE2
REMARK 470 TYR B 59 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS B 60 CG CD CE NZ
REMARK 470 LYS B 64 CG CD CE NZ
REMARK 470 LYS B 79 CG CD CE NZ
REMARK 470 ASN B 93 CG OD1 ND2
REMARK 470 VAL B 94 CG1 CG2
REMARK 470 ASP B 95 CG OD1 OD2
REMARK 470 VAL B 96 CG1 CG2
REMARK 470 ASP B 108 CG OD1 OD2
REMARK 470 THR B 119 OG1 CG2
REMARK 470 LYS B 123 CG CD CE NZ
REMARK 470 LYS B 125 CG CD CE NZ
REMARK 470 ILE B 131 CG1 CG2 CD1
REMARK 470 SER B 137 OG
REMARK 470 ASN B 176 CG OD1 ND2
REMARK 470 GLU B 184 CG CD OE1 OE2
REMARK 470 GLN B 187 CG CD OE1 NE2
REMARK 470 GLU B 191 CG CD OE1 OE2
REMARK 470 ASN C 3 CG OD1 ND2
REMARK 470 TYR C 4 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LEU C 9 CG CD1 CD2
REMARK 470 THR C 12 OG1 CG2
REMARK 470 LYS C 13 CG CD CE NZ
REMARK 470 GLU C 18 CG CD OE1 OE2
REMARK 470 SER C 20 OG
REMARK 470 ILE C 26 CG1 CG2 CD1
REMARK 470 GLU C 35 CG CD OE1 OE2
REMARK 470 GLN C 40 CG CD OE1 NE2
REMARK 470 ARG C 45 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 52 CG CD CE NZ
REMARK 470 SER C 55 OG
REMARK 470 SER C 58 OG
REMARK 470 ARG C 62 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 63 CG CD CE NZ
REMARK 470 SER C 96 OG
REMARK 470 LYS C 100 CG CD CE NZ
REMARK 470 LYS C 103 CG CD CE NZ
REMARK 470 ARG C 107 CG CD NE CZ NH1 NH2
REMARK 470 PHE C 116 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLN C 119 CG CD OE1 NE2
REMARK 470 GLU C 120 CG CD OE1 OE2
REMARK 470 VAL C 126 CG1 CG2
REMARK 470 ASP C 127 CG OD1 OD2
REMARK 470 ASN C 130 CG OD1 ND2
REMARK 470 PHE C 131 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU C 132 CG CD OE1 OE2
REMARK 470 LYS C 135 CG CD CE NZ
REMARK 470 LYS C 137 CG CD CE NZ
REMARK 470 GLU C 138 CG CD OE1 OE2
REMARK 470 PHE C 139 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASN C 141 CG OD1 ND2
REMARK 470 LEU C 143 CG CD1 CD2
REMARK 470 LYS C 150 CG CD CE NZ
REMARK 470 LYS C 151 CG CD CE NZ
REMARK 470 LEU C 153 CG CD1 CD2
REMARK 470 VAL C 154 CG1 CG2
REMARK 470 THR C 156 OG1 CG2
REMARK 470 GLU C 157 CG CD OE1 OE2
REMARK 470 ASN C 158 CG OD1 ND2
REMARK 470 GLU C 159 CG CD OE1 OE2
REMARK 470 ASP C 160 CG OD1 OD2
REMARK 470 ASN C 162 CG OD1 ND2
REMARK 470 ARG C 168 CG CD NE CZ NH1 NH2
REMARK 470 ILE C 170 CG1 CG2 CD1
REMARK 470 GLN C 174 CG CD OE1 NE2
REMARK 470 VAL C 175 CG1 CG2
REMARK 470 LEU C 184 CG CD1 CD2
REMARK 470 ASP C 185 CG OD1 OD2
REMARK 470 SER C 191 OG
REMARK 470 LEU C 192 CG CD1 CD2
REMARK 470 VAL C 193 CG1 CG2
REMARK 470 ILE C 194 CG1 CG2 CD1
REMARK 470 THR C 195 OG1 CG2
REMARK 470 LYS C 200 CG CD CE NZ
REMARK 470 LYS C 201 CG CD CE NZ
REMARK 470 LYS D 5 CG CD CE NZ
REMARK 470 GLU D 6 CG CD OE1 OE2
REMARK 470 LYS D 7 CG CD CE NZ
REMARK 470 PHE D 8 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASN D 9 CG OD1 ND2
REMARK 470 GLU D 11 CG CD OE1 OE2
REMARK 470 VAL D 12 CG1 CG2
REMARK 470 THR D 13 OG1 CG2
REMARK 470 GLU D 14 CG CD OE1 OE2
REMARK 470 ASN D 15 CG OD1 ND2
REMARK 470 LYS D 18 CG CD CE NZ
REMARK 470 LYS D 19 CG CD CE NZ
REMARK 470 ASN D 21 CG OD1 ND2
REMARK 470 TYR D 22 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 VAL D 25 CG1 CG2
REMARK 470 VAL D 28 CG1 CG2
REMARK 470 LYS D 30 CG CD CE NZ
REMARK 470 ILE D 31 CG1 CG2 CD1
REMARK 470 ASP D 32 CG OD1 OD2
REMARK 470 LYS D 33 CG CD CE NZ
REMARK 470 ILE D 34 CG1 CG2 CD1
REMARK 470 VAL D 35 CG1 CG2
REMARK 470 VAL D 36 CG1 CG2
REMARK 470 ASN D 37 CG OD1 ND2
REMARK 470 MET D 38 CG SD CE
REMARK 470 VAL D 40 CG1 CG2
REMARK 470 ASP D 42 CG OD1 OD2
REMARK 470 VAL D 44 CG1 CG2
REMARK 470 GLN D 45 CG CD OE1 NE2
REMARK 470 ASN D 46 CG OD1 ND2
REMARK 470 SER D 47 OG
REMARK 470 LYS D 48 CG CD CE NZ
REMARK 470 VAL D 49 CG1 CG2
REMARK 470 LEU D 50 CG CD1 CD2
REMARK 470 ASP D 51 CG OD1 OD2
REMARK 470 ASN D 52 CG OD1 ND2
REMARK 470 VAL D 54 CG1 CG2
REMARK 470 GLU D 55 CG CD OE1 OE2
REMARK 470 GLU D 56 CG CD OE1 OE2
REMARK 470 LEU D 57 CG CD1 CD2
REMARK 470 GLU D 58 CG CD OE1 OE2
REMARK 470 LEU D 59 CG CD1 CD2
REMARK 470 ILE D 60 CG1 CG2 CD1
REMARK 470 GLN D 63 CG CD OE1 NE2
REMARK 470 LYS D 64 CG CD CE NZ
REMARK 470 PRO D 65 CG CD
REMARK 470 LEU D 66 CG CD1 CD2
REMARK 470 VAL D 67 CG1 CG2
REMARK 470 THR D 68 OG1 CG2
REMARK 470 LYS D 69 CG CD CE NZ
REMARK 470 LYS D 71 CG CD CE NZ
REMARK 470 LYS D 72 CG CD CE NZ
REMARK 470 SER D 73 OG
REMARK 470 ILE D 74 CG1 CG2 CD1
REMARK 470 THR D 76 OG1 CG2
REMARK 470 PHE D 77 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG D 78 CG CD NE CZ NH1 NH2
REMARK 470 LEU D 79 CG CD1 CD2
REMARK 470 ARG D 80 CG CD NE CZ NH1 NH2
REMARK 470 GLU D 81 CG CD OE1 OE2
REMARK 470 MET D 83 CG SD CE
REMARK 470 PRO D 84 CG CD
REMARK 470 ILE D 85 CG1 CG2 CD1
REMARK 470 LYS D 88 CG CD CE NZ
REMARK 470 VAL D 89 CG1 CG2
REMARK 470 THR D 90 OG1 CG2
REMARK 470 LEU D 91 CG CD1 CD2
REMARK 470 ARG D 92 CG CD NE CZ NH1 NH2
REMARK 470 ARG D 95 CG CD NE CZ NH1 NH2
REMARK 470 MET D 96 CG SD CE
REMARK 470 TYR D 97 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU D 98 CG CD OE1 OE2
REMARK 470 PHE D 99 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LEU D 100 CG CD1 CD2
REMARK 470 ASP D 101 CG OD1 OD2
REMARK 470 LYS D 102 CG CD CE NZ
REMARK 470 LEU D 103 CG CD1 CD2
REMARK 470 ILE D 104 CG1 CG2 CD1
REMARK 470 VAL D 106 CG1 CG2
REMARK 470 SER D 107 OG
REMARK 470 LEU D 108 CG CD1 CD2
REMARK 470 PRO D 109 CG CD
REMARK 470 ARG D 110 CG CD NE CZ NH1 NH2
REMARK 470 VAL D 111 CG1 CG2
REMARK 470 ARG D 112 CG CD NE CZ NH1 NH2
REMARK 470 ASP D 113 CG OD1 OD2
REMARK 470 PHE D 114 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLN D 115 CG CD OE1 NE2
REMARK 470 VAL D 117 CG1 CG2
REMARK 470 SER D 118 OG
REMARK 470 LYS D 119 CG CD CE NZ
REMARK 470 LYS D 120 CG CD CE NZ
REMARK 470 PHE D 122 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASP D 123 CG OD1 OD2
REMARK 470 ARG D 125 CG CD NE CZ NH1 NH2
REMARK 470 ASN D 127 CG OD1 ND2
REMARK 470 TYR D 128 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 THR D 129 OG1 CG2
REMARK 470 LYS D 133 CG CD CE NZ
REMARK 470 GLU D 134 CG CD OE1 OE2
REMARK 470 GLN D 135 CG CD OE1 NE2
REMARK 470 LEU D 136 CG CD1 CD2
REMARK 470 ILE D 137 CG1 CG2 CD1
REMARK 470 PHE D 138 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU D 140 CG CD OE1 OE2
REMARK 470 ILE D 141 CG1 CG2 CD1
REMARK 470 ASP D 142 CG OD1 OD2
REMARK 470 TYR D 143 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ASP D 144 CG OD1 OD2
REMARK 470 LYS D 145 CG CD CE NZ
REMARK 470 VAL D 146 CG1 CG2
REMARK 470 SER D 147 OG
REMARK 470 LYS D 148 CG CD CE NZ
REMARK 470 VAL D 149 CG1 CG2
REMARK 470 ARG D 150 CG CD NE CZ NH1 NH2
REMARK 470 MET D 152 CG SD CE
REMARK 470 ASP D 153 CG OD1 OD2
REMARK 470 ILE D 154 CG1 CG2 CD1
REMARK 470 VAL D 155 CG1 CG2
REMARK 470 ILE D 156 CG1 CG2 CD1
REMARK 470 VAL D 157 CG1 CG2
REMARK 470 THR D 158 OG1 CG2
REMARK 470 THR D 159 OG1 CG2
REMARK 470 ASN D 161 CG OD1 ND2
REMARK 470 THR D 162 OG1 CG2
REMARK 470 ASP D 163 CG OD1 OD2
REMARK 470 GLU D 164 CG CD OE1 OE2
REMARK 470 GLU D 165 CG CD OE1 OE2
REMARK 470 ARG D 167 CG CD NE CZ NH1 NH2
REMARK 470 GLU D 168 CG CD OE1 OE2
REMARK 470 LEU D 169 CG CD1 CD2
REMARK 470 PHE E 19 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASP E 20 CG OD1 OD2
REMARK 470 ASN E 22 CG OD1 ND2
REMARK 470 LYS E 27 CG CD CE NZ
REMARK 470 LYS E 30 CG CD CE NZ
REMARK 470 SER E 34 OG
REMARK 470 ARG E 35 CG CD NE CZ NH1 NH2
REMARK 470 LEU E 37 CG CD1 CD2
REMARK 470 ASN E 38 CG OD1 ND2
REMARK 470 GLU E 39 CG CD OE1 OE2
REMARK 470 ARG E 40 CG CD NE CZ NH1 NH2
REMARK 470 PHE E 43 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU E 46 CG CD OE1 OE2
REMARK 470 GLU E 47 CG CD OE1 OE2
REMARK 470 ASN E 48 CG OD1 ND2
REMARK 470 ILE E 50 CG1 CG2 CD1
REMARK 470 GLU E 51 CG CD OE1 OE2
REMARK 470 VAL E 52 CG1 CG2
REMARK 470 ARG E 54 CG CD NE CZ NH1 NH2
REMARK 470 PRO E 55 CG CD
REMARK 470 SER E 56 OG
REMARK 470 ASP E 57 CG OD1 OD2
REMARK 470 LYS E 59 CG CD CE NZ
REMARK 470 GLU E 60 CG CD OE1 OE2
REMARK 470 ASP E 61 CG OD1 OD2
REMARK 470 ARG E 62 CG CD NE CZ NH1 NH2
REMARK 470 ARG E 69 CG CD NE CZ NH1 NH2
REMARK 470 LEU E 71 CG CD1 CD2
REMARK 470 LEU E 72 CG CD1 CD2
REMARK 470 ASN E 74 CG OD1 ND2
REMARK 470 VAL E 76 CG1 CG2
REMARK 470 GLN E 77 CG CD OE1 NE2
REMARK 470 SER E 80 OG
REMARK 470 GLN E 81 CG CD OE1 NE2
REMARK 470 LYS E 85 CG CD CE NZ
REMARK 470 VAL E 86 CG1 CG2
REMARK 470 GLU E 88 CG CD OE1 OE2
REMARK 470 LEU E 89 CG CD1 CD2
REMARK 470 VAL E 90 CG1 CG2
REMARK 470 TYR E 94 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ARG E 95 CG CD NE CZ NH1 NH2
REMARK 470 GLN E 97 CG CD OE1 NE2
REMARK 470 MET E 98 CG SD CE
REMARK 470 GLN E 99 CG CD OE1 NE2
REMARK 470 LYS E 101 CG CD CE NZ
REMARK 470 ASP E 102 CG OD1 OD2
REMARK 470 LEU E 103 CG CD1 CD2
REMARK 470 ILE E 104 CG1 CG2 CD1
REMARK 470 LEU E 105 CG CD1 CD2
REMARK 470 ASN E 106 CG OD1 ND2
REMARK 470 VAL E 107 CG1 CG2
REMARK 470 GLU E 114 CG CD OE1 OE2
REMARK 470 LYS E 116 CG CD CE NZ
REMARK 470 GLU E 118 CG CD OE1 OE2
REMARK 470 GLU E 119 CG CD OE1 OE2
REMARK 470 ASN E 120 CG OD1 ND2
REMARK 470 THR E 122 OG1 CG2
REMARK 470 PHE E 123 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 SER E 124 OG
REMARK 470 VAL E 125 CG1 CG2
REMARK 470 GLU E 126 CG CD OE1 OE2
REMARK 470 LYS E 127 CG CD CE NZ
REMARK 470 ASN E 128 CG OD1 ND2
REMARK 470 THR E 129 OG1 CG2
REMARK 470 VAL E 130 CG1 CG2
REMARK 470 LYS E 132 CG CD CE NZ
REMARK 470 GLU E 134 CG CD OE1 OE2
REMARK 470 LYS E 138 CG CD CE NZ
REMARK 470 LEU E 144 CG CD1 CD2
REMARK 470 ILE E 148 CG1 CG2 CD1
REMARK 470 ARG E 149 CG CD NE CZ NH1 NH2
REMARK 470 ARG E 152 CG CD NE CZ NH1 NH2
REMARK 470 GLU E 155 CG CD OE1 OE2
REMARK 470 LYS E 158 CG CD CE NZ
REMARK 470 LYS E 160 CG CD CE NZ
REMARK 470 ILE E 162 CG1 CG2 CD1
REMARK 470 TYR E 164 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLN E 165 CG CD OE1 NE2
REMARK 470 GLU E 167 CG CD OE1 OE2
REMARK 470 TYR E 168 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 VAL E 169 CG1 CG2
REMARK 470 ARG E 170 CG CD NE CZ NH1 NH2
REMARK 470 ARG E 171 CG CD NE CZ NH1 NH2
REMARK 470 LYS E 172 CG CD CE NZ
REMARK 470 GLU E 173 CG CD OE1 OE2
REMARK 470 LYS E 174 CG CD CE NZ
REMARK 470 ASN G 8 CG OD1 ND2
REMARK 470 GLU G 9 CG CD OE1 OE2
REMARK 470 SER G 10 OG
REMARK 470 ASN G 11 CG OD1 ND2
REMARK 470 GLU G 13 CG CD OE1 OE2
REMARK 470 LYS G 15 CG CD CE NZ
REMARK 470 GLU G 70 CG CD OE1 OE2
REMARK 470 SER G 87 OG
REMARK 470 ILE G 88 CG1 CG2 CD1
REMARK 470 GLU G 92 CG CD OE1 OE2
REMARK 470 LEU G 93 CG CD1 CD2
REMARK 470 LYS G 118 CG CD CE NZ
REMARK 470 LYS G 121 CG CD CE NZ
REMARK 470 LYS G 122 CG CD CE NZ
REMARK 470 GLU G 130 CG CD OE1 OE2
REMARK 470 GLU G 139 CG CD OE1 OE2
REMARK 470 ARG G 144 CG CD NE CZ NH1 NH2
REMARK 470 LYS H 9 CG CD CE NZ
REMARK 470 ARG H 17 CG CD NE CZ NH1 NH2
REMARK 470 GLU H 18 CG CD OE1 OE2
REMARK 470 LYS H 44 CG CD CE NZ
REMARK 470 LYS H 53 CG CD CE NZ
REMARK 470 GLU H 108 CG CD OE1 OE2
REMARK 470 LYS H 113 CG CD CE NZ
REMARK 470 ILE H 114 CG1 CG2 CD1
REMARK 470 VAL H 115 CG1 CG2
REMARK 470 GLU I 15 CG CD OE1 OE2
REMARK 470 LYS I 29 CG CD CE NZ
REMARK 470 HIS I 35 CG ND1 CD2 CE1 NE2
REMARK 470 LYS I 39 CG CD CE NZ
REMARK 470 ARG I 41 CG CD NE CZ NH1 NH2
REMARK 470 SER I 42 OG
REMARK 470 VAL I 46 CG1 CG2
REMARK 470 PHE I 58 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG I 59 CG CD NE CZ NH1 NH2
REMARK 470 ARG I 60 CG CD NE CZ NH1 NH2
REMARK 470 LYS I 63 CG CD CE NZ
REMARK 470 ARG I 64 CG CD NE CZ NH1 NH2
REMARK 470 THR I 67 OG1 CG2
REMARK 470 ASN I 68 CG OD1 ND2
REMARK 470 ILE I 69 CG1 CG2 CD1
REMARK 470 ARG I 71 CG CD NE CZ NH1 NH2
REMARK 470 LYS I 72 CG CD CE NZ
REMARK 470 GLU I 73 CG CD OE1 OE2
REMARK 470 TYR I 74 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 VAL I 77 CG1 CG2
REMARK 470 LEU I 79 CG CD1 CD2
REMARK 470 ASP I 80 CG OD1 OD2
REMARK 470 GLN I 81 CG CD OE1 NE2
REMARK 470 PHE I 85 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU I 86 CG CD OE1 OE2
REMARK 470 ASP I 87 CG OD1 OD2
REMARK 470 LEU I 96 CG CD1 CD2
REMARK 470 GLU I 98 CG CD OE1 OE2
REMARK 470 SER I 99 OG
REMARK 470 VAL I 101 CG1 CG2
REMARK 470 VAL I 102 CG1 CG2
REMARK 470 LYS I 103 CG CD CE NZ
REMARK 470 ASN I 104 CG OD1 ND2
REMARK 470 GLU I 105 CG CD OE1 OE2
REMARK 470 LYS I 106 CG CD CE NZ
REMARK 470 ILE I 109 CG1 CG2 CD1
REMARK 470 LYS I 110 CG CD CE NZ
REMARK 470 ILE I 111 CG1 CG2 CD1
REMARK 470 LEU I 117 CG CD1 CD2
REMARK 470 ASP I 118 CG OD1 OD2
REMARK 470 LYS I 119 CG CD CE NZ
REMARK 470 LYS I 120 CG CD CE NZ
REMARK 470 LEU I 121 CG CD1 CD2
REMARK 470 THR I 122 OG1 CG2
REMARK 470 LYS I 124 CG CD CE NZ
REMARK 470 HIS I 126 CG ND1 CD2 CE1 NE2
REMARK 470 LYS I 127 CG CD CE NZ
REMARK 470 SER I 129 OG
REMARK 470 MET J 1 CG SD CE
REMARK 470 LEU J 3 CG CD1 CD2
REMARK 470 PRO J 4 CG CD
REMARK 470 LYS J 5 CG CD CE NZ
REMARK 470 ARG J 6 CG CD NE CZ NH1 NH2
REMARK 470 LYS J 8 CG CD CE NZ
REMARK 470 TYR J 9 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ARG J 10 CG CD NE CZ NH1 NH2
REMARK 470 GLN J 12 CG CD OE1 NE2
REMARK 470 ARG J 20 CG CD NE CZ NH1 NH2
REMARK 470 LYS J 22 CG CD CE NZ
REMARK 470 ASN J 25 CG OD1 ND2
REMARK 470 GLU J 31 CG CD OE1 OE2
REMARK 470 GLU J 48 CG CD OE1 OE2
REMARK 470 ARG J 56 CG CD NE CZ NH1 NH2
REMARK 470 LYS J 59 CG CD CE NZ
REMARK 470 LYS J 63 CG CD CE NZ
REMARK 470 LEU J 79 CG CD1 CD2
REMARK 470 LYS J 98 CG CD CE NZ
REMARK 470 GLU J 105 CG CD OE1 OE2
REMARK 470 GLU J 112 CG CD OE1 OE2
REMARK 470 LYS J 133 CG CD CE NZ
REMARK 470 GLU J 136 CG CD OE1 OE2
REMARK 470 LEU J 137 CG CD1 CD2
REMARK 470 ARG K 4 CG CD NE CZ NH1 NH2
REMARK 470 GLU K 70 CG CD OE1 OE2
REMARK 470 ILE K 71 CG1 CG2 CD1
REMARK 470 LEU K 72 CG CD1 CD2
REMARK 470 GLU K 74 CG CD OE1 OE2
REMARK 470 ASP K 75 CG OD1 OD2
REMARK 470 THR K 77 OG1 CG2
REMARK 470 THR K 78 OG1 CG2
REMARK 470 ARG K 96 CG CD NE CZ NH1 NH2
REMARK 470 ILE L 2 CG1 CG2 CD1
REMARK 470 LYS L 4 CG CD CE NZ
REMARK 470 ILE L 5 CG1 CG2 CD1
REMARK 470 ASP L 6 CG OD1 OD2
REMARK 470 LYS L 7 CG CD CE NZ
REMARK 470 ASN L 8 CG OD1 ND2
REMARK 470 LYS L 9 CG CD CE NZ
REMARK 470 LEU L 12 CG CD1 CD2
REMARK 470 LYS L 13 CG CD CE NZ
REMARK 470 ARG L 14 CG CD NE CZ NH1 NH2
REMARK 470 ARG L 19 CG CD NE CZ NH1 NH2
REMARK 470 ASN L 21 CG OD1 ND2
REMARK 470 SER L 23 OG
REMARK 470 THR L 25 OG1 CG2
REMARK 470 GLU L 27 CG CD OE1 OE2
REMARK 470 LYS L 28 CG CD CE NZ
REMARK 470 ASN L 32 CG OD1 ND2
REMARK 470 LYS L 38 CG CD CE NZ
REMARK 470 ILE L 40 CG1 CG2 CD1
REMARK 470 GLN L 55 CG CD OE1 NE2
REMARK 470 LYS L 59 CG CD CE NZ
REMARK 470 ASP L 60 CG OD1 OD2
REMARK 470 ASP L 62 CG OD1 OD2
REMARK 470 ILE L 63 CG1 CG2 CD1
REMARK 470 THR L 65 OG1 CG2
REMARK 470 THR L 68 OG1 CG2
REMARK 470 LYS L 69 CG CD CE NZ
REMARK 470 VAL L 70 CG1 CG2
REMARK 470 GLU L 71 CG CD OE1 OE2
REMARK 470 LEU L 72 CG CD1 CD2
REMARK 470 THR L 74 OG1 CG2
REMARK 470 LYS L 75 CG CD CE NZ
REMARK 470 GLU L 78 CG CD OE1 OE2
REMARK 470 ILE L 80 CG1 CG2 CD1
REMARK 470 LYS L 82 CG CD CE NZ
REMARK 470 ASP L 86 CG OD1 OD2
REMARK 470 LYS L 90 CG CD CE NZ
REMARK 470 GLU L 91 CG CD OE1 OE2
REMARK 470 ILE L 92 CG1 CG2 CD1
REMARK 470 VAL L 93 CG1 CG2
REMARK 470 ASP L 95 CG OD1 OD2
REMARK 470 TYR L 99 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LEU L 100 CG CD1 CD2
REMARK 470 TYR L 101 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 HIS L 102 CG ND1 CD2 CE1 NE2
REMARK 470 ARG L 104 CG CD NE CZ NH1 NH2
REMARK 470 LYS L 106 CG CD CE NZ
REMARK 470 LEU L 108 CG CD1 CD2
REMARK 470 MET M 1 CG SD CE
REMARK 470 THR M 2 OG1 CG2
REMARK 470 ASN M 3 CG OD1 ND2
REMARK 470 LYS M 12 CG CD CE NZ
REMARK 470 ASP M 18 CG OD1 OD2
REMARK 470 LEU M 28 CG CD1 CD2
REMARK 470 ARG M 29 CG CD NE CZ NH1 NH2
REMARK 470 VAL M 30 CG1 CG2
REMARK 470 ARG M 33 CG CD NE CZ NH1 NH2
REMARK 470 GLU M 36 CG CD OE1 OE2
REMARK 470 ARG M 39 CG CD NE CZ NH1 NH2
REMARK 470 GLU M 40 CG CD OE1 OE2
REMARK 470 GLU M 46 CG CD OE1 OE2
REMARK 470 LYS M 65 CG CD CE NZ
REMARK 470 GLU M 73 CG CD OE1 OE2
REMARK 470 GLU M 84 CG CD OE1 OE2
REMARK 470 LYS M 85 CG CD CE NZ
REMARK 470 LYS M 93 CG CD CE NZ
REMARK 470 SER M 104 OG
REMARK 470 LEU M 105 CG CD1 CD2
REMARK 470 LYS M 108 CG CD CE NZ
REMARK 470 ARG N 11 CG CD NE CZ NH1 NH2
REMARK 470 LYS N 22 CG CD CE NZ
REMARK 470 ASN N 91 CG OD1 ND2
REMARK 470 GLU N 103 CG CD OE1 OE2
REMARK 470 LYS N 104 CG CD CE NZ
REMARK 470 GLU O 15 CG CD OE1 OE2
REMARK 470 ASP O 26 CG OD1 OD2
REMARK 470 ASP O 31 CG OD1 OD2
REMARK 470 ASP O 36 CG OD1 OD2
REMARK 470 ASP O 44 CG OD1 OD2
REMARK 470 LYS O 47 CG CD CE NZ
REMARK 470 THR O 52 OG1 CG2
REMARK 470 VAL O 53 CG1 CG2
REMARK 470 GLU O 54 CG CD OE1 OE2
REMARK 470 THR O 57 OG1 CG2
REMARK 470 VAL O 58 CG1 CG2
REMARK 470 LYS O 64 CG CD CE NZ
REMARK 470 LYS O 80 CG CD CE NZ
REMARK 470 LYS O 99 CG CD CE NZ
REMARK 470 ILE O 100 CG1 CG2 CD1
REMARK 470 ARG P 8 CG CD NE CZ NH1 NH2
REMARK 470 ILE P 96 CG1 CG2 CD1
REMARK 470 GLU Q 2 CG CD OE1 OE2
REMARK 470 ARG Q 4 CG CD NE CZ NH1 NH2
REMARK 470 LEU Q 7 CG CD1 CD2
REMARK 470 LYS Q 8 CG CD CE NZ
REMARK 470 ARG Q 9 CG CD NE CZ NH1 NH2
REMARK 470 LYS Q 15 CG CD CE NZ
REMARK 470 GLU Q 18 CG CD OE1 OE2
REMARK 470 GLU Q 22 CG CD OE1 OE2
REMARK 470 ASP Q 23 CG OD1 OD2
REMARK 470 LYS Q 24 CG CD CE NZ
REMARK 470 PHE Q 27 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASP Q 28 CG OD1 OD2
REMARK 470 VAL Q 29 CG1 CG2
REMARK 470 ARG Q 32 CG CD NE CZ NH1 NH2
REMARK 470 LYS Q 35 CG CD CE NZ
REMARK 470 LYS Q 39 CG CD CE NZ
REMARK 470 VAL Q 42 CG1 CG2
REMARK 470 GLU Q 43 CG CD OE1 OE2
REMARK 470 GLU Q 44 CG CD OE1 OE2
REMARK 470 ILE Q 45 CG1 CG2 CD1
REMARK 470 ASN Q 47 CG OD1 ND2
REMARK 470 VAL Q 48 CG1 CG2
REMARK 470 SER Q 52 OG
REMARK 470 VAL Q 53 CG1 CG2
REMARK 470 LYS Q 59 CG CD CE NZ
REMARK 470 LYS Q 62 CG CD CE NZ
REMARK 470 ARG Q 64 CG CD NE CZ NH1 NH2
REMARK 470 MET Q 65 CG SD CE
REMARK 470 GLN Q 69 CG CD OE1 NE2
REMARK 470 ASN Q 73 CG OD1 ND2
REMARK 470 LYS Q 74 CG CD CE NZ
REMARK 470 ARG Q 75 CG CD NE CZ NH1 NH2
REMARK 470 LYS Q 77 CG CD CE NZ
REMARK 470 ILE Q 79 CG1 CG2 CD1
REMARK 470 LYS Q 83 CG CD CE NZ
REMARK 470 GLU Q 84 CG CD OE1 OE2
REMARK 470 SER Q 86 OG
REMARK 470 ASP Q 88 CG OD1 OD2
REMARK 470 PHE Q 90 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASN Q 91 CG OD1 ND2
REMARK 470 LYS R 5 CG CD CE NZ
REMARK 470 ILE R 12 CG1 CG2 CD1
REMARK 470 LYS R 15 CG CD CE NZ
REMARK 470 LYS R 17 CG CD CE NZ
REMARK 470 LYS R 19 CG CD CE NZ
REMARK 470 GLU R 20 CG CD OE1 OE2
REMARK 470 LYS R 22 CG CD CE NZ
REMARK 470 THR R 26 OG1 CG2
REMARK 470 LEU R 27 CG CD1 CD2
REMARK 470 LYS R 29 CG CD CE NZ
REMARK 470 LYS R 30 CG CD CE NZ
REMARK 470 VAL R 35 CG1 CG2
REMARK 470 VAL R 38 CG1 CG2
REMARK 470 LYS R 42 CG CD CE NZ
REMARK 470 HIS R 44 CG ND1 CD2 CE1 NE2
REMARK 470 GLN R 45 CG CD OE1 NE2
REMARK 470 LYS R 46 CG CD CE NZ
REMARK 470 PRO R 47 CG CD
REMARK 470 THR R 48 OG1 CG2
REMARK 470 GLN R 49 CG CD OE1 NE2
REMARK 470 LEU R 50 CG CD1 CD2
REMARK 470 ASN R 51 CG OD1 ND2
REMARK 470 GLU R 53 CG CD OE1 OE2
REMARK 470 LEU R 57 CG CD1 CD2
REMARK 470 GLU R 60 CG CD OE1 OE2
REMARK 470 ILE R 63 CG1 CG2 CD1
REMARK 470 LEU R 71 CG CD1 CD2
REMARK 470 LYS R 74 CG CD CE NZ
REMARK 470 GLU R 77 CG CD OE1 OE2
REMARK 470 THR R 79 OG1 CG2
REMARK 470 TYR R 83 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS R 84 CG CD CE NZ
REMARK 470 PHE R 85 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 VAL R 86 CG1 CG2
REMARK 470 ASP R 87 CG OD1 OD2
REMARK 470 LYS R 89 CG CD CE NZ
REMARK 470 ARG R 92 CG CD NE CZ NH1 NH2
REMARK 470 LYS R 95 CG CD CE NZ
REMARK 470 GLU R 99 CG CD OE1 OE2
REMARK 470 GLU R 100 CG CD OE1 OE2
REMARK 470 ILE R 101 CG1 CG2 CD1
REMARK 470 LYS R 102 CG CD CE NZ
REMARK 470 ASN R 104 CG OD1 ND2
REMARK 470 SER S 3 OG
REMARK 470 LEU S 4 CG CD1 CD2
REMARK 470 LYS S 5 CG CD CE NZ
REMARK 470 ILE S 7 CG1 CG2 CD1
REMARK 470 ARG S 9 CG CD NE CZ NH1 NH2
REMARK 470 LYS S 12 CG CD CE NZ
REMARK 470 GLN S 13 CG CD OE1 NE2
REMARK 470 ARG S 15 CG CD NE CZ NH1 NH2
REMARK 470 LYS S 23 CG CD CE NZ
REMARK 470 THR S 36 OG1 CG2
REMARK 470 LYS S 37 CG CD CE NZ
REMARK 470 VAL S 39 CG1 CG2
REMARK 470 ILE S 49 CG1 CG2 CD1
REMARK 470 ARG S 53 CG CD NE CZ NH1 NH2
REMARK 470 ILE S 61 CG1 CG2 CD1
REMARK 470 GLU S 62 CG CD OE1 OE2
REMARK 470 LEU S 63 CG CD1 CD2
REMARK 470 SER S 67 OG
REMARK 470 LYS S 71 CG CD CE NZ
REMARK 470 GLU S 98 CG CD OE1 OE2
REMARK 470 GLU S 99 CG CD OE1 OE2
REMARK 470 ARG S 100 CG CD NE CZ NH1 NH2
REMARK 470 VAL S 102 CG1 CG2
REMARK 470 GLU S 103 CG CD OE1 OE2
REMARK 470 VAL S 106 CG1 CG2
REMARK 470 GLN S 107 CG CD OE1 NE2
REMARK 470 VAL S 109 CG1 CG2
REMARK 470 GLU S 111 CG CD OE1 OE2
REMARK 470 LYS S 116 CG CD CE NZ
REMARK 470 GLU S 117 CG CD OE1 OE2
REMARK 470 VAL S 121 CG1 CG2
REMARK 470 GLU S 122 CG CD OE1 OE2
REMARK 470 PHE S 126 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASN S 127 CG OD1 ND2
REMARK 470 LEU S 128 CG CD1 CD2
REMARK 470 GLU S 129 CG CD OE1 OE2
REMARK 470 ASP S 135 CG OD1 OD2
REMARK 470 GLU S 139 CG CD OE1 OE2
REMARK 470 ILE S 141 CG1 CG2 CD1
REMARK 470 GLU S 142 CG CD OE1 OE2
REMARK 470 ASP S 144 CG OD1 OD2
REMARK 470 ILE S 145 CG1 CG2 CD1
REMARK 470 THR S 146 OG1 CG2
REMARK 470 GLU S 147 CG CD OE1 OE2
REMARK 470 LEU S 148 CG CD1 CD2
REMARK 470 ASN S 149 CG OD1 ND2
REMARK 470 ILE S 150 CG1 CG2 CD1
REMARK 470 ASN S 151 CG OD1 ND2
REMARK 470 SER S 153 OG
REMARK 470 VAL S 156 CG1 CG2
REMARK 470 LYS S 160 CG CD CE NZ
REMARK 470 THR S 162 OG1 CG2
REMARK 470 ASP S 164 CG OD1 OD2
REMARK 470 PHE S 165 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS S 166 CG CD CE NZ
REMARK 470 ILE S 167 CG1 CG2 CD1
REMARK 470 GLU S 168 CG CD OE1 OE2
REMARK 470 ASN S 169 CG OD1 ND2
REMARK 470 ASP T 23 CG OD1 OD2
REMARK 470 GLU T 25 CG CD OE1 OE2
REMARK 470 ASP T 64 CG OD1 OD2
REMARK 470 ASP T 65 CG OD1 OD2
REMARK 470 ARG T 79 CG CD NE CZ NH1 NH2
REMARK 470 SER U 13 OG
REMARK 470 THR U 14 OG1 CG2
REMARK 470 ASN U 16 CG OD1 ND2
REMARK 470 ARG U 17 CG CD NE CZ NH1 NH2
REMARK 470 ARG U 18 CG CD NE CZ NH1 NH2
REMARK 470 LEU U 22 CG CD1 CD2
REMARK 470 ASN U 23 CG OD1 ND2
REMARK 470 SER U 24 OG
REMARK 470 THR U 25 OG1 CG2
REMARK 470 LYS U 26 CG CD CE NZ
REMARK 470 ARG U 27 CG CD NE CZ NH1 NH2
REMARK 470 ARG U 28 CG CD NE CZ NH1 NH2
REMARK 470 LEU U 33 CG CD1 CD2
REMARK 470 GLN U 34 CG CD OE1 NE2
REMARK 470 LYS U 35 CG CD CE NZ
REMARK 470 VAL U 36 CG1 CG2
REMARK 470 ARG U 37 CG CD NE CZ NH1 NH2
REMARK 470 ILE U 38 CG1 CG2 CD1
REMARK 470 LEU U 39 CG CD1 CD2
REMARK 470 VAL U 40 CG1 CG2
REMARK 470 ASP U 41 CG OD1 OD2
REMARK 470 LYS U 43 CG CD CE NZ
REMARK 470 LYS U 45 CG CD CE NZ
REMARK 470 LYS U 46 CG CD CE NZ
REMARK 470 VAL U 49 CG1 CG2
REMARK 470 SER U 50 OG
REMARK 470 ARG U 52 CG CD NE CZ NH1 NH2
REMARK 470 LEU U 54 CG CD1 CD2
REMARK 470 LYS V 2 CG CD CE NZ
REMARK 470 LYS V 4 CG CD CE NZ
REMARK 470 GLU V 5 CG CD OE1 OE2
REMARK 470 ILE V 6 CG1 CG2 CD1
REMARK 470 ARG V 7 CG CD NE CZ NH1 NH2
REMARK 470 ASP V 8 CG OD1 OD2
REMARK 470 LEU V 9 CG CD1 CD2
REMARK 470 ILE V 14 CG1 CG2 CD1
REMARK 470 ARG V 58 CG CD NE CZ NH1 NH2
REMARK 470 ARG V 60 CG CD NE CZ NH1 NH2
REMARK 470 GLU V 61 CG CD OE1 OE2
REMARK 470 GLN V 64 CG CD OE1 NE2
REMARK 470 LYS W 51 CG CD CE NZ
REMARK 470 ARG Z 35 CG CD NE CZ NH1 NH2
REMARK 470 ARG Z 42 CG CD NE CZ NH1 NH2
REMARK 470 SER 2 14 OG
REMARK 470 LYS 2 15 CG CD CE NZ
REMARK 470 PHE 2 19 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG 2 40 CG CD NE CZ NH1 NH2
REMARK 470 LYS 3 3 CG CD CE NZ
REMARK 470 LYS 3 12 CG CD CE NZ
REMARK 470 ARG 3 13 CG CD NE CZ NH1 NH2
REMARK 470 ARG 3 16 CG CD NE CZ NH1 NH2
REMARK 470 GLN 3 21 CG CD OE1 NE2
REMARK 470 LEU 3 22 CG CD1 CD2
REMARK 470 LYS 3 23 CG CD CE NZ
REMARK 470 SER 3 25 OG
REMARK 470 LEU 3 32 CG CD1 CD2
REMARK 470 LYS 3 36 CG CD CE NZ
REMARK 470 LYS 3 39 CG CD CE NZ
REMARK 470 LYS 3 41 CG CD CE NZ
REMARK 470 ARG 3 42 CG CD NE CZ NH1 NH2
REMARK 470 GLN 3 43 CG CD OE1 NE2
REMARK 470 ARG 3 45 CG CD NE CZ NH1 NH2
REMARK 470 LYS 3 46 CG CD CE NZ
REMARK 470 ARG 3 48 CG CD NE CZ NH1 NH2
REMARK 470 ARG 3 57 CG CD NE CZ NH1 NH2
REMARK 470 LEU 3 61 CG CD1 CD2
REMARK 470 MET 4 1 CG SD CE
REMARK 470 LYS 4 2 CG CD CE NZ
REMARK 470 VAL 4 3 CG1 CG2
REMARK 470 ARG 4 4 CG CD NE CZ NH1 NH2
REMARK 470 PRO 4 5 CG CD
REMARK 470 SER 4 6 OG
REMARK 470 VAL 4 7 CG1 CG2
REMARK 470 LYS 4 8 CG CD CE NZ
REMARK 470 PRO 4 9 CG CD
REMARK 470 ILE 4 10 CG1 CG2 CD1
REMARK 470 GLU 4 12 CG CD OE1 OE2
REMARK 470 LYS 4 13 CG CD CE NZ
REMARK 470 CYS 4 14 SG
REMARK 470 LYS 4 15 CG CD CE NZ
REMARK 470 VAL 4 16 CG1 CG2
REMARK 470 ILE 4 17 CG1 CG2 CD1
REMARK 470 LYS 4 18 CG CD CE NZ
REMARK 470 ARG 4 19 CG CD NE CZ NH1 NH2
REMARK 470 LYS 4 20 CG CD CE NZ
REMARK 470 LYS 4 22 CG CD CE NZ
REMARK 470 VAL 4 23 CG1 CG2
REMARK 470 MET 4 24 CG SD CE
REMARK 470 VAL 4 25 CG1 CG2
REMARK 470 ILE 4 26 CG1 CG2 CD1
REMARK 470 GLU 4 28 CG CD OE1 OE2
REMARK 470 ASN 4 29 CG OD1 ND2
REMARK 470 PRO 4 30 CG CD
REMARK 470 LYS 4 31 CG CD CE NZ
REMARK 470 HIS 4 32 CG ND1 CD2 CE1 NE2
REMARK 470 LYS 4 33 CG CD CE NZ
REMARK 470 GLN 4 34 CG CD OE1 NE2
REMARK 470 ARG 4 35 CG CD NE CZ NH1 NH2
REMARK 470 GLN 4 36 CG CD OE1 NE2
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 OE2 GLU J 135 O4 MPD J 201 2.01
REMARK 500 O LEU C 108 OG SER C 112 2.02
REMARK 500 O2' G X 1467 O2' G X 1543 2.02
REMARK 500 O2' A X 1796 OP1 C X 1985 2.03
REMARK 500 OH TYR A 171 OP1 A X 2250 2.05
REMARK 500 OP2 U X 1185 OG1 THR G 66 2.05
REMARK 500 O THR V 10 N SER V 12 2.05
REMARK 500 O2' G X 2007 OP2 U X 2009 2.05
REMARK 500 OP2 G X 1290 NH2 ARG N 13 2.07
REMARK 500 O2' A X 788 OP1 U X 1703 2.09
REMARK 500 O2 C X 460 O2' U X 1891 2.09
REMARK 500 O4 U X 657 N6 A X 659 2.10
REMARK 500 O2' U X 2649 N2 G X 2845 2.13
REMARK 500 O2' A X 1440 O2' A X 1514 2.13
REMARK 500 O2' A X 2805 O2' G X 2807 2.13
REMARK 500 OE1 GLU J 116 NH1 ARG J 119 2.13
REMARK 500 O2' G X 904 O6 G X 961 2.15
REMARK 500 OP1 G X 1302 NH2 ARG Z 16 2.15
REMARK 500 O2' A X 621 OP2 C X 623 2.15
REMARK 500 OP2 G X 1313 O2' G X 1689 2.16
REMARK 500 O PRO S 81 N LYS S 83 2.16
REMARK 500 O2 C X 2382 N2 G X 2389 2.16
REMARK 500 O6 G X 1894 N2 G X 1902 2.17
REMARK 500 NH1 ARG G 14 O ASP G 50 2.17
REMARK 500 O2' C X 1423 O2 U X 1512 2.17
REMARK 500 OP2 A X 864 N2 G X 1226 2.17
REMARK 500 O2' A X 645 O2' G X 647 2.18
REMARK 500 N2 G X 1876 O2 C X 1920 2.18
REMARK 500 OP1 C X 1362 O2' G X 1691 2.18
REMARK 500 N2 G X 1711 O4 U X 2020 2.18
REMARK 500 O4 U X 589 N6 A X 592 2.19
REMARK 500 N4 C X 1472 OP2 A X 1617 2.19
REMARK 500 NZ LYS B 38 O VAL B 96 2.19
REMARK 500 OP1 A X 1289 NH1 ARG N 13 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 G X 24 C5 G X 24 N7 -0.039
REMARK 500 A X 373 C4 A X 373 C5 0.046
REMARK 500 G X 515 C4 G X 515 C5 0.049
REMARK 500 G X 515 C8 G X 515 N9 0.043
REMARK 500 A X 574 N9 A X 574 C4 -0.043
REMARK 500 A X 621 C4 A X 621 C5 -0.047
REMARK 500 A X 660 O3' U X 661 P 0.080
REMARK 500 G X 681 C5 G X 681 N7 -0.036
REMARK 500 A X 720 N3 A X 720 C4 -0.040
REMARK 500 A X 721 N3 A X 721 C4 -0.037
REMARK 500 A X 721 C5 A X 721 C6 -0.055
REMARK 500 A X 721 C5 A X 721 N7 -0.038
REMARK 500 A X 721 N9 A X 721 C4 -0.050
REMARK 500 A X 865 N9 A X 865 C4 -0.042
REMARK 500 A X1040 N9 A X1040 C4 -0.037
REMARK 500 A X1065 C5 A X1065 N7 -0.044
REMARK 500 A X1065 N9 A X1065 C4 -0.055
REMARK 500 A X1186 N9 A X1186 C4 -0.077
REMARK 500 A X1285 N9 A X1285 C4 -0.039
REMARK 500 A X1289 N3 A X1289 C4 -0.038
REMARK 500 A X1289 C4 A X1289 C5 0.054
REMARK 500 A X1289 N9 A X1289 C4 -0.070
REMARK 500 C X1295 N3 C X1295 C4 -0.060
REMARK 500 G X1302 C2 G X1302 N3 -0.053
REMARK 500 A X1310 N9 A X1310 C4 -0.045
REMARK 500 A X1312 N9 A X1312 C4 -0.036
REMARK 500 G X1395 C5 G X1395 N7 0.037
REMARK 500 G X1395 N9 G X1395 C4 0.063
REMARK 500 C X1719 N1 C X1719 C6 -0.040
REMARK 500 G X2037 C4 G X2037 C5 -0.047
REMARK 500 A X2050 C6 A X2050 N1 -0.045
REMARK 500 G X2066 C5 G X2066 N7 -0.036
REMARK 500 A X2087 N9 A X2087 C4 -0.042
REMARK 500 A X2355 N9 A X2355 C4 -0.039
REMARK 500 C X2595 N1 C X2595 C6 -0.037
REMARK 500 A X2604 N3 A X2604 C4 -0.040
REMARK 500 G X2648 N1 G X2648 C2 -0.061
REMARK 500 G X2648 C6 G X2648 N1 -0.044
REMARK 500 A X2661 C4 A X2661 C5 -0.044
REMARK 500 A X2661 C6 A X2661 N1 -0.043
REMARK 500 C X2707 N1 C X2707 C6 -0.040
REMARK 500 A X2738 N9 A X2738 C4 -0.042
REMARK 500 A X2740 C5 A X2740 N7 -0.041
REMARK 500 A X2740 N9 A X2740 C4 -0.054
REMARK 500 G X2845 C2 G X2845 N3 -0.060
REMARK 500 G X2845 C5 G X2845 C6 -0.063
REMARK 500 G X2845 N9 G X2845 C4 -0.077
REMARK 500 G Y 58 N9 G Y 58 C4 -0.055
REMARK 500 A Y 68 N9 A Y 68 C4 -0.045
REMARK 500 G Y 92 N1 G Y 92 C2 0.049
REMARK 500
REMARK 500 THIS ENTRY HAS 52 BOND DEVIATIONS.
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 U X 12 N1 - C2 - O2 ANGL. DEV. = 4.6 DEGREES
REMARK 500 U X 12 N3 - C2 - O2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 U X 12 C2 - N1 - C1' ANGL. DEV. = 7.9 DEGREES
REMARK 500 A X 13 O3' - P - OP2 ANGL. DEV. = 7.6 DEGREES
REMARK 500 A X 13 C8 - N9 - C4 ANGL. DEV. = 3.0 DEGREES
REMARK 500 G X 17 N1 - C6 - O6 ANGL. DEV. = 4.3 DEGREES
REMARK 500 C X 20 C6 - N1 - C2 ANGL. DEV. = 2.9 DEGREES
REMARK 500 C X 20 C5 - C4 - N4 ANGL. DEV. = -5.0 DEGREES
REMARK 500 G X 24 C4 - C5 - C6 ANGL. DEV. = 3.7 DEGREES
REMARK 500 G X 24 C6 - C5 - N7 ANGL. DEV. = -4.1 DEGREES
REMARK 500 G X 24 N1 - C6 - O6 ANGL. DEV. = 4.4 DEGREES
REMARK 500 C X 32 C6 - N1 - C2 ANGL. DEV. = 3.1 DEGREES
REMARK 500 G X 35 C2 - N3 - C4 ANGL. DEV. = -3.4 DEGREES
REMARK 500 G X 35 C8 - N9 - C4 ANGL. DEV. = 3.7 DEGREES
REMARK 500 G X 36 N3 - C4 - N9 ANGL. DEV. = 4.1 DEGREES
REMARK 500 G X 58 N1 - C6 - O6 ANGL. DEV. = -3.7 DEGREES
REMARK 500 G X 70 C3' - O3' - P ANGL. DEV. = 7.9 DEGREES
REMARK 500 A X 71 O5' - P - OP1 ANGL. DEV. = -6.0 DEGREES
REMARK 500 G X 96 N1 - C6 - O6 ANGL. DEV. = 3.9 DEGREES
REMARK 500 A X 102 C5 - N7 - C8 ANGL. DEV. = -3.1 DEGREES
REMARK 500 A X 102 N1 - C6 - N6 ANGL. DEV. = 4.0 DEGREES
REMARK 500 U X 113 C2 - N1 - C1' ANGL. DEV. = 7.5 DEGREES
REMARK 500 C X 129 C6 - N1 - C2 ANGL. DEV. = 2.6 DEGREES
REMARK 500 G X 135 N1 - C6 - O6 ANGL. DEV. = 3.7 DEGREES
REMARK 500 G X 181 N3 - C4 - C5 ANGL. DEV. = 3.3 DEGREES
REMARK 500 A X 198 C8 - N9 - C4 ANGL. DEV. = 2.7 DEGREES
REMARK 500 A X 198 N9 - C4 - C5 ANGL. DEV. = -2.5 DEGREES
REMARK 500 A X 198 N1 - C6 - N6 ANGL. DEV. = 3.7 DEGREES
REMARK 500 A X 199 N1 - C6 - N6 ANGL. DEV. = 4.3 DEGREES
REMARK 500 U X 205 C5 - C6 - N1 ANGL. DEV. = -3.3 DEGREES
REMARK 500 C X 211 C6 - N1 - C2 ANGL. DEV. = 4.2 DEGREES
REMARK 500 C X 211 N3 - C4 - C5 ANGL. DEV. = 2.5 DEGREES
REMARK 500 U X 243 C5 - C6 - N1 ANGL. DEV. = -3.1 DEGREES
REMARK 500 G X 245 C8 - N9 - C4 ANGL. DEV. = 3.1 DEGREES
REMARK 500 G X 251 N1 - C6 - O6 ANGL. DEV. = 4.4 DEGREES
REMARK 500 G X 255 O5' - P - OP2 ANGL. DEV. = -5.4 DEGREES
REMARK 500 G X 263 N3 - C4 - C5 ANGL. DEV. = -3.1 DEGREES
REMARK 500 G X 263 C8 - N9 - C4 ANGL. DEV. = -2.9 DEGREES
REMARK 500 A X 268 O4' - C1' - N9 ANGL. DEV. = 6.3 DEGREES
REMARK 500 C X 323 C6 - N1 - C2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 C X 323 N3 - C2 - O2 ANGL. DEV. = -4.9 DEGREES
REMARK 500 G X 341 C4 - C5 - N7 ANGL. DEV. = 3.1 DEGREES
REMARK 500 G X 341 C5 - C6 - O6 ANGL. DEV. = -4.0 DEGREES
REMARK 500 A X 342 N1 - C6 - N6 ANGL. DEV. = 3.8 DEGREES
REMARK 500 G X 350 O4' - C1' - N9 ANGL. DEV. = 5.5 DEGREES
REMARK 500 A X 353 O4' - C1' - N9 ANGL. DEV. = 6.2 DEGREES
REMARK 500 A X 354 O5' - P - OP2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 G X 355 C4 - C5 - C6 ANGL. DEV. = 4.0 DEGREES
REMARK 500 G X 355 C6 - C5 - N7 ANGL. DEV. = -4.1 DEGREES
REMARK 500 G X 355 C8 - N9 - C1' ANGL. DEV. = -8.5 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 822 ANGLE DEVIATIONS.
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 PRO A 8 65.63 -69.16
REMARK 500 ARG A 13 16.05 58.54
REMARK 500 PHE A 21 44.71 -71.57
REMARK 500 THR A 25 -103.34 24.77
REMARK 500 THR A 27 129.83 50.57
REMARK 500 LYS A 35 -81.05 -137.64
REMARK 500 PRO A 36 -47.41 44.23
REMARK 500 LEU A 37 100.58 65.92
REMARK 500 LYS A 39 -144.78 -77.11
REMARK 500 GLN A 46 -4.49 73.08
REMARK 500 VAL A 51 84.23 5.27
REMARK 500 VAL A 78 -170.29 56.66
REMARK 500 ASP A 79 -73.64 -176.73
REMARK 500 GLN A 82 -164.20 53.03
REMARK 500 LEU A 110 111.93 66.23
REMARK 500 ALA A 120 -98.94 52.28
REMARK 500 VAL A 126 -148.34 53.03
REMARK 500 ASN A 128 -164.67 -101.04
REMARK 500 ILE A 135 126.29 76.73
REMARK 500 ALA A 155 74.99 56.86
REMARK 500 ARG A 156 -108.39 -117.46
REMARK 500 SER A 157 -158.08 53.02
REMARK 500 ALA A 158 -106.07 -89.51
REMARK 500 LYS A 170 -69.33 55.48
REMARK 500 THR A 187 -6.33 -147.47
REMARK 500 ILE A 192 -126.71 -69.82
REMARK 500 LYS A 214 -159.57 -83.08
REMARK 500 VAL A 224 -141.47 -87.97
REMARK 500 MET A 225 -160.46 59.35
REMARK 500 SER A 245 115.61 62.99
REMARK 500 LYS A 252 133.17 66.52
REMARK 500 PHE B 53 -128.08 -68.39
REMARK 500 ALA B 58 -155.25 41.98
REMARK 500 LYS B 60 58.70 -65.42
REMARK 500 ASP B 62 41.85 80.81
REMARK 500 VAL B 94 -163.82 -109.07
REMARK 500 VAL B 96 -10.45 51.08
REMARK 500 TYR B 99 96.52 108.63
REMARK 500 LYS B 123 -134.09 35.83
REMARK 500 SER B 142 -174.51 63.68
REMARK 500 HIS B 146 58.71 -118.47
REMARK 500 HIS B 148 -79.12 -139.33
REMARK 500 MET B 156 -151.88 -93.76
REMARK 500 ALA B 157 -130.16 -97.48
REMARK 500 ASP B 159 -64.47 -93.57
REMARK 500 ARG B 162 -167.83 -109.32
REMARK 500 ASN B 176 115.70 67.23
REMARK 500 ASN B 182 80.96 62.01
REMARK 500 PRO B 204 -102.81 -105.44
REMARK 500 LYS B 206 11.22 58.50
REMARK 500
REMARK 500 THIS ENTRY HAS 356 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 LYS A 77 VAL A 78 145.06
REMARK 500 LYS B 57 ALA B 58 146.89
REMARK 500 GLU B 104 VAL B 105 148.86
REMARK 500 GLU C 27 PRO C 28 -148.86
REMARK 500 VAL C 161 ASN C 162 148.56
REMARK 500 HIS I 35 LYS I 36 144.55
REMARK 500 LYS O 80 ASN O 81 -145.59
REMARK 500 VAL P 70 VAL P 71 142.89
REMARK 500 ASP S 17 LEU S 18 145.25
REMARK 500 ALA 3 10 ALA 3 11 146.10
REMARK 500 THR 3 17 ALA 3 18 -148.07
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 MG X3345 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A X 13 O2'
REMARK 620 2 G X 16 O6 133.9
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN X3098 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A X 14 OP2
REMARK 620 2 G X 15 OP2 103.1
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG X3284 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 C X 20 OP1
REMARK 620 2 G X1257 OP1 116.7
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG X3273 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A X 130 OP1
REMARK 620 2 A X 130 OP2 65.0
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN X3127 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 C X 195 OP1
REMARK 620 2 U X2270 OP1 112.3
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN X3080 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A X 198 N7
REMARK 620 2 A X 200 OP1 71.4
REMARK 620 3 C X 201 OP2 96.0 82.4
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG X3299 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 C X 323 OP1
REMARK 620 2 A X 324 OP2 62.7
REMARK 620 3 A X 326 OP2 134.5 72.5
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN X3189 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 G X 416 O6
REMARK 620 2 A X 468 OP2 112.1
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN X3234 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 U X 438 OP1
REMARK 620 2 A X 455 OP1 86.9
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN X3200 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 G X 457 OP1
REMARK 620 2 A X2434 OP1 76.1
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG X3309 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A X 476 OP1
REMARK 620 2 A X 476 OP2 51.2
REMARK 620 3 U X 477 O4 101.7 72.2
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN X3104 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 G X 496 O6
REMARK 620 2 A X 499 OP1 96.5
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN X3118 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 C X 555 OP1
REMARK 620 2 U X 556 OP2 106.9
REMARK 620 3 G X 557 N7 84.1 78.2
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG X3504 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 G X 563 OP1
REMARK 620 2 ASN Z 14 OD1 138.7
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN X3055 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A X 571 OP1
REMARK 620 2 C X 572 OP1 70.2
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN X3015 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 G X 613 O6
REMARK 620 2 A X2475 OP1 163.0
REMARK 620 3 C X2526 OP1 98.9 88.8
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG X3390 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A X 618 OP1
REMARK 620 2 A X2057 O2' 142.1
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN X3126 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 U X 619 OP1
REMARK 620 2 A X2530 OP1 92.7
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG X3356 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 U X 642 O4
REMARK 620 2 G X 643 O6 84.1
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN X3270 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A X 775 OP2
REMARK 620 2 C X 776 OP2 67.6
REMARK 620 3 A X 806 OP1 87.5 70.5
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN X3407 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 G X 778 N7
REMARK 620 2 A X 806 N7 92.1
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN X3220 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 C X 782 OP1
REMARK 620 2 U X1665 OP1 81.8
REMARK 620 3 A X1666 OP1 164.2 102.3
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN X3215 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 C X 785 OP2
REMARK 620 2 A X1810 OP1 162.9
REMARK 620 3 A X1811 OP2 105.7 71.1
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN X3152 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A X 796 OP1
REMARK 620 2 A X1658 OP1 166.4
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN X3050 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A X 828 OP2
REMARK 620 2 U X 829 OP2 83.8
REMARK 620 3 A X2616 OP1 81.3 82.6
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN X3049 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 U X 829 OP1
REMARK 620 2 G X2615 OP1 87.1
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN X3217 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 C X 832 OP1
REMARK 620 2 U X 835 OP2 149.2
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN X3107 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 G X 863 OP2
REMARK 620 2 G X1226 O6 65.3
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN X3022 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 U X 871 OP1
REMARK 620 2 C X2454 OP1 156.4
REMARK 620 3 G X2455 OP1 84.7 73.7
REMARK 620 4 G X2456 OP1 88.6 96.1 78.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN X3023 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 U X 872 OP1
REMARK 620 2 G X2456 OP2 84.0
REMARK 620 3 A X2457 OP2 129.9 73.3
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG X3373 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 C X 960 O3'
REMARK 620 2 G X 961 OP1 52.0
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN X3206 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A X 989 OP2
REMARK 620 2 G X 990 OP2 93.1
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN X3018 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A X 992 OP1
REMARK 620 2 G X1006 OP1 85.8
REMARK 620 3 U X1007 OP2 170.3 88.6
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN X3042 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A X1034 OP2
REMARK 620 2 C X1035 OP2 72.4
REMARK 620 3 G X1225 OP2 136.3 93.0
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG X3353 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A X1034 OP1
REMARK 620 2 C X1202 OP1 125.3
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN X3156 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 U X1043 OP2
REMARK 620 2 C X1197 OP2 124.5
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN X3095 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A X1053 OP2
REMARK 620 2 A X1054 OP2 76.4
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN X3201 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 U X1067 OP2
REMARK 620 2 G X1068 OP2 98.8
REMARK 620 3 G X1069 O2' 72.1 82.9
REMARK 620 4 A X1070 OP1 168.6 75.3 97.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG X3438 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 G X1069 O3'
REMARK 620 2 C X1179 O5' 165.5
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN X3041 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 G X1201 OP1
REMARK 620 2 C X1202 OP2 87.7
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN X3136 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A X1228 OP2
REMARK 620 2 G X1229 N7 82.7
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG X3123 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 G X1271 O6
REMARK 620 2 U X1272 O4 70.5
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN X3063 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 U X1287 OP1
REMARK 620 2 G X1288 OP1 73.1
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN X3035 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A X1303 OP2
REMARK 620 2 U X2642 OP1 91.9
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN X3219 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 G X1309 OP2
REMARK 620 2 A X1310 OP1 74.5
REMARK 620 3 G X1691 OP1 161.7 88.2
REMARK 620 4 C X1692 OP1 95.1 158.6 103.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN X3257 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 C X1335 OP2
REMARK 620 2 U X1683 OP2 161.5
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG X3295 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A X1379 OP2
REMARK 620 2 U X1646 O4 77.2
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN X3197 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A X1396 OP1
REMARK 620 2 G X1397 OP2 108.3
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN X3188 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 U X1416 OP2
REMARK 620 2 G X1417 OP2 104.6
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN X3170 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 U X1431 OP1
REMARK 620 2 C X1648 OP1 97.1
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN X3169 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A X1432 OP1
REMARK 620 2 A X1647 OP1 86.4
REMARK 620 3 C X1648 OP2 96.4 79.5
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN X3264 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 U X1499 OP2
REMARK 620 2 G X1500 OP2 107.1
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG X3221 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 C X1651 O2
REMARK 620 2 G X1664 OP2 129.8
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN X3093 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A X1685 OP2
REMARK 620 2 G X1686 N7 83.1
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN X3053 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 C X1702 OP1
REMARK 620 2 HIS B 148 NE2 90.3
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN X3100 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A X1708 OP1
REMARK 620 2 A X1709 OP2 103.6
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN X3075 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A X1713 OP2
REMARK 620 2 C X1714 OP2 71.4
REMARK 620 3 U X1715 O4 74.4 93.2
REMARK 620 4 G X2577 OP1 92.9 80.1 167.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN X3076 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 C X1714 OP1
REMARK 620 2 U X1715 OP2 83.7
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG X3292 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A X1745 OP2
REMARK 620 2 G X1746 O6 106.9
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN X3216 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A X1807 OP1
REMARK 620 2 C X1809 OP1 92.1
REMARK 620 3 A X1810 OP2 149.2 80.0
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG X3277 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 G X1995 OP1
REMARK 620 2 G X2619 OP1 78.2
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN X3085 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 G X2083 OP2
REMARK 620 2 G X2084 OP2 65.3
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN X3013 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 G X2088 OP2
REMARK 620 2 G X2529 OP2 75.9
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN X3092 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 C X2275 OP2
REMARK 620 2 U X2276 O4 86.7
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN X3161 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A X2295 OP1
REMARK 620 2 A X2296 OP1 89.3
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN X3179 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A X2379 OP2
REMARK 620 2 G X2380 N7 78.2
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG X3429 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A X2459 OP2
REMARK 620 2 A X2460 OP2 97.3
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN X3016 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A X2475 OP2
REMARK 620 2 C X2525 OP2 83.6
REMARK 620 3 C X2526 OP2 94.8 93.9
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG X3285 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A X2480 OP1
REMARK 620 2 U X2519 OP1 149.7
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN X3145 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 C X2600 OP1
REMARK 620 2 G X2601 OP1 92.1
REMARK 620 3 C X2602 OP2 82.0 84.2
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN X3057 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 G X2603 OP1
REMARK 620 2 A X2604 OP1 92.9
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN X3132 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 G X2609 OP2
REMARK 620 2 G X2610 OP2 88.2
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN X3223 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A X2629 OP2
REMARK 620 2 G X2630 OP2 91.6
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN X3079 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A X2666 OP2
REMARK 620 2 G X2667 N7 77.5
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN X3105 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 U X2709 OP2
REMARK 620 2 A X2748 OP1 129.7
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN X3251 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A X2738 OP2
REMARK 620 2 G X2741 OP2 90.1
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN X3071 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A X2830 OP2
REMARK 620 2 G X2831 N7 77.7
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG Y 209 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 G Y 31 O6
REMARK 620 2 A Y 43 OP2 87.6
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 62B X 3003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD X 3004
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD X 3005
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD X 3006
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD X 3007
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD X 3008
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD X 3009
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD X 3010
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD X 3011
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3012
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3013
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3014
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3015
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3016
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3017
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3018
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3019
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3021
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3022
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3023
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3024
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3026
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3027
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3028
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3032
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3033
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3034
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3035
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3036
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3037
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3038
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3039
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3040
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3041
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3042
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3043
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3045
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3046
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3048
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3049
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3050
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3051
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3053
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3055
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3056
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3057
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3059
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3060
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3061
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3062
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3063
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3064
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3065
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3066
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3067
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3068
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3071
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3072
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3075
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3076
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3077
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3078
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3079
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3080
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3081
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3082
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3083
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3084
REMARK 800
REMARK 800 SITE_IDENTIFIER: AK1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3085
REMARK 800
REMARK 800 SITE_IDENTIFIER: AK2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3086
REMARK 800
REMARK 800 SITE_IDENTIFIER: AK3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3087
REMARK 800
REMARK 800 SITE_IDENTIFIER: AK4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3088
REMARK 800
REMARK 800 SITE_IDENTIFIER: AK5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3089
REMARK 800
REMARK 800 SITE_IDENTIFIER: AK6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3090
REMARK 800
REMARK 800 SITE_IDENTIFIER: AK7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3092
REMARK 800
REMARK 800 SITE_IDENTIFIER: AK8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3093
REMARK 800
REMARK 800 SITE_IDENTIFIER: AK9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3094
REMARK 800
REMARK 800 SITE_IDENTIFIER: AL1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3095
REMARK 800
REMARK 800 SITE_IDENTIFIER: AL2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3097
REMARK 800
REMARK 800 SITE_IDENTIFIER: AL3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3098
REMARK 800
REMARK 800 SITE_IDENTIFIER: AL4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3099
REMARK 800
REMARK 800 SITE_IDENTIFIER: AL5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3100
REMARK 800
REMARK 800 SITE_IDENTIFIER: AL6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3103
REMARK 800
REMARK 800 SITE_IDENTIFIER: AL7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3104
REMARK 800
REMARK 800 SITE_IDENTIFIER: AL8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3105
REMARK 800
REMARK 800 SITE_IDENTIFIER: AL9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3106
REMARK 800
REMARK 800 SITE_IDENTIFIER: AM1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3107
REMARK 800
REMARK 800 SITE_IDENTIFIER: AM2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3108
REMARK 800
REMARK 800 SITE_IDENTIFIER: AM3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3110
REMARK 800
REMARK 800 SITE_IDENTIFIER: AM4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3111
REMARK 800
REMARK 800 SITE_IDENTIFIER: AM5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3113
REMARK 800
REMARK 800 SITE_IDENTIFIER: AM6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3114
REMARK 800
REMARK 800 SITE_IDENTIFIER: AM7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3115
REMARK 800
REMARK 800 SITE_IDENTIFIER: AM8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3116
REMARK 800
REMARK 800 SITE_IDENTIFIER: AM9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3117
REMARK 800
REMARK 800 SITE_IDENTIFIER: AN1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3118
REMARK 800
REMARK 800 SITE_IDENTIFIER: AN2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3119
REMARK 800
REMARK 800 SITE_IDENTIFIER: AN3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3121
REMARK 800
REMARK 800 SITE_IDENTIFIER: AN4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3122
REMARK 800
REMARK 800 SITE_IDENTIFIER: AN5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3123
REMARK 800
REMARK 800 SITE_IDENTIFIER: AN6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3125
REMARK 800
REMARK 800 SITE_IDENTIFIER: AN7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3126
REMARK 800
REMARK 800 SITE_IDENTIFIER: AN8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3127
REMARK 800
REMARK 800 SITE_IDENTIFIER: AN9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3128
REMARK 800
REMARK 800 SITE_IDENTIFIER: AO1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3130
REMARK 800
REMARK 800 SITE_IDENTIFIER: AO2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3131
REMARK 800
REMARK 800 SITE_IDENTIFIER: AO3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3132
REMARK 800
REMARK 800 SITE_IDENTIFIER: AO4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3133
REMARK 800
REMARK 800 SITE_IDENTIFIER: AO5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3134
REMARK 800
REMARK 800 SITE_IDENTIFIER: AO6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3136
REMARK 800
REMARK 800 SITE_IDENTIFIER: AO7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3137
REMARK 800
REMARK 800 SITE_IDENTIFIER: AO8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3140
REMARK 800
REMARK 800 SITE_IDENTIFIER: AO9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3141
REMARK 800
REMARK 800 SITE_IDENTIFIER: AP1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3144
REMARK 800
REMARK 800 SITE_IDENTIFIER: AP2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3145
REMARK 800
REMARK 800 SITE_IDENTIFIER: AP3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3146
REMARK 800
REMARK 800 SITE_IDENTIFIER: AP4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3147
REMARK 800
REMARK 800 SITE_IDENTIFIER: AP5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3149
REMARK 800
REMARK 800 SITE_IDENTIFIER: AP6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3152
REMARK 800
REMARK 800 SITE_IDENTIFIER: AP7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3154
REMARK 800
REMARK 800 SITE_IDENTIFIER: AP8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3155
REMARK 800
REMARK 800 SITE_IDENTIFIER: AP9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3156
REMARK 800
REMARK 800 SITE_IDENTIFIER: AQ1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3157
REMARK 800
REMARK 800 SITE_IDENTIFIER: AQ2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3158
REMARK 800
REMARK 800 SITE_IDENTIFIER: AQ3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3159
REMARK 800
REMARK 800 SITE_IDENTIFIER: AQ4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3160
REMARK 800
REMARK 800 SITE_IDENTIFIER: AQ5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3161
REMARK 800
REMARK 800 SITE_IDENTIFIER: AQ6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3162
REMARK 800
REMARK 800 SITE_IDENTIFIER: AQ7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3163
REMARK 800
REMARK 800 SITE_IDENTIFIER: AQ8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3164
REMARK 800
REMARK 800 SITE_IDENTIFIER: AQ9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3165
REMARK 800
REMARK 800 SITE_IDENTIFIER: AR1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3167
REMARK 800
REMARK 800 SITE_IDENTIFIER: AR2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3168
REMARK 800
REMARK 800 SITE_IDENTIFIER: AR3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3169
REMARK 800
REMARK 800 SITE_IDENTIFIER: AR4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3170
REMARK 800
REMARK 800 SITE_IDENTIFIER: AR5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3171
REMARK 800
REMARK 800 SITE_IDENTIFIER: AR6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3172
REMARK 800
REMARK 800 SITE_IDENTIFIER: AR7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3173
REMARK 800
REMARK 800 SITE_IDENTIFIER: AR8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3174
REMARK 800
REMARK 800 SITE_IDENTIFIER: AR9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3176
REMARK 800
REMARK 800 SITE_IDENTIFIER: AS1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3177
REMARK 800
REMARK 800 SITE_IDENTIFIER: AS2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3178
REMARK 800
REMARK 800 SITE_IDENTIFIER: AS3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3179
REMARK 800
REMARK 800 SITE_IDENTIFIER: AS4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3180
REMARK 800
REMARK 800 SITE_IDENTIFIER: AS5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3181
REMARK 800
REMARK 800 SITE_IDENTIFIER: AS6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3183
REMARK 800
REMARK 800 SITE_IDENTIFIER: AS7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3184
REMARK 800
REMARK 800 SITE_IDENTIFIER: AS8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3185
REMARK 800
REMARK 800 SITE_IDENTIFIER: AS9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3187
REMARK 800
REMARK 800 SITE_IDENTIFIER: AT1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3188
REMARK 800
REMARK 800 SITE_IDENTIFIER: AT2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3189
REMARK 800
REMARK 800 SITE_IDENTIFIER: AT3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3190
REMARK 800
REMARK 800 SITE_IDENTIFIER: AT4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3191
REMARK 800
REMARK 800 SITE_IDENTIFIER: AT5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3192
REMARK 800
REMARK 800 SITE_IDENTIFIER: AT6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3193
REMARK 800
REMARK 800 SITE_IDENTIFIER: AT7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3194
REMARK 800
REMARK 800 SITE_IDENTIFIER: AT8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3195
REMARK 800
REMARK 800 SITE_IDENTIFIER: AT9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3196
REMARK 800
REMARK 800 SITE_IDENTIFIER: AU1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3197
REMARK 800
REMARK 800 SITE_IDENTIFIER: AU2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3198
REMARK 800
REMARK 800 SITE_IDENTIFIER: AU3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3199
REMARK 800
REMARK 800 SITE_IDENTIFIER: AU4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3200
REMARK 800
REMARK 800 SITE_IDENTIFIER: AU5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AU6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AU7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3204
REMARK 800
REMARK 800 SITE_IDENTIFIER: AU8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3205
REMARK 800
REMARK 800 SITE_IDENTIFIER: AU9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3206
REMARK 800
REMARK 800 SITE_IDENTIFIER: AV1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3207
REMARK 800
REMARK 800 SITE_IDENTIFIER: AV2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3209
REMARK 800
REMARK 800 SITE_IDENTIFIER: AV3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3210
REMARK 800
REMARK 800 SITE_IDENTIFIER: AV4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3211
REMARK 800
REMARK 800 SITE_IDENTIFIER: AV5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3214
REMARK 800
REMARK 800 SITE_IDENTIFIER: AV6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3215
REMARK 800
REMARK 800 SITE_IDENTIFIER: AV7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3216
REMARK 800
REMARK 800 SITE_IDENTIFIER: AV8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3217
REMARK 800
REMARK 800 SITE_IDENTIFIER: AV9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3218
REMARK 800
REMARK 800 SITE_IDENTIFIER: AW1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3219
REMARK 800
REMARK 800 SITE_IDENTIFIER: AW2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3220
REMARK 800
REMARK 800 SITE_IDENTIFIER: AW3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3221
REMARK 800
REMARK 800 SITE_IDENTIFIER: AW4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3222
REMARK 800
REMARK 800 SITE_IDENTIFIER: AW5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3223
REMARK 800
REMARK 800 SITE_IDENTIFIER: AW6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3224
REMARK 800
REMARK 800 SITE_IDENTIFIER: AW7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3225
REMARK 800
REMARK 800 SITE_IDENTIFIER: AW8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3226
REMARK 800
REMARK 800 SITE_IDENTIFIER: AW9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3227
REMARK 800
REMARK 800 SITE_IDENTIFIER: AX1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3228
REMARK 800
REMARK 800 SITE_IDENTIFIER: AX2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3231
REMARK 800
REMARK 800 SITE_IDENTIFIER: AX3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3233
REMARK 800
REMARK 800 SITE_IDENTIFIER: AX4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3234
REMARK 800
REMARK 800 SITE_IDENTIFIER: AX5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3235
REMARK 800
REMARK 800 SITE_IDENTIFIER: AX6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3236
REMARK 800
REMARK 800 SITE_IDENTIFIER: AX7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3237
REMARK 800
REMARK 800 SITE_IDENTIFIER: AX8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3238
REMARK 800
REMARK 800 SITE_IDENTIFIER: AX9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3242
REMARK 800
REMARK 800 SITE_IDENTIFIER: AY1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3244
REMARK 800
REMARK 800 SITE_IDENTIFIER: AY2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3245
REMARK 800
REMARK 800 SITE_IDENTIFIER: AY3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3248
REMARK 800
REMARK 800 SITE_IDENTIFIER: AY4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3250
REMARK 800
REMARK 800 SITE_IDENTIFIER: AY5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3251
REMARK 800
REMARK 800 SITE_IDENTIFIER: AY6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3252
REMARK 800
REMARK 800 SITE_IDENTIFIER: AY7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3253
REMARK 800
REMARK 800 SITE_IDENTIFIER: AY8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3254
REMARK 800
REMARK 800 SITE_IDENTIFIER: AY9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3256
REMARK 800
REMARK 800 SITE_IDENTIFIER: AZ1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3257
REMARK 800
REMARK 800 SITE_IDENTIFIER: AZ2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3258
REMARK 800
REMARK 800 SITE_IDENTIFIER: AZ3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3259
REMARK 800
REMARK 800 SITE_IDENTIFIER: AZ4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3261
REMARK 800
REMARK 800 SITE_IDENTIFIER: AZ5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3262
REMARK 800
REMARK 800 SITE_IDENTIFIER: AZ6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3263
REMARK 800
REMARK 800 SITE_IDENTIFIER: AZ7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3264
REMARK 800
REMARK 800 SITE_IDENTIFIER: AZ8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3265
REMARK 800
REMARK 800 SITE_IDENTIFIER: AZ9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3267
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3268
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3269
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3270
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3271
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3272
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3273
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3274
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3275
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3276
REMARK 800
REMARK 800 SITE_IDENTIFIER: BD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3277
REMARK 800
REMARK 800 SITE_IDENTIFIER: BD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3278
REMARK 800
REMARK 800 SITE_IDENTIFIER: BD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3279
REMARK 800
REMARK 800 SITE_IDENTIFIER: BD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3280
REMARK 800
REMARK 800 SITE_IDENTIFIER: BD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3281
REMARK 800
REMARK 800 SITE_IDENTIFIER: BD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3283
REMARK 800
REMARK 800 SITE_IDENTIFIER: BD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3284
REMARK 800
REMARK 800 SITE_IDENTIFIER: BD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3285
REMARK 800
REMARK 800 SITE_IDENTIFIER: BD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3286
REMARK 800
REMARK 800 SITE_IDENTIFIER: BE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3287
REMARK 800
REMARK 800 SITE_IDENTIFIER: BE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3288
REMARK 800
REMARK 800 SITE_IDENTIFIER: BE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3289
REMARK 800
REMARK 800 SITE_IDENTIFIER: BE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3291
REMARK 800
REMARK 800 SITE_IDENTIFIER: BE5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3292
REMARK 800
REMARK 800 SITE_IDENTIFIER: BE6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3293
REMARK 800
REMARK 800 SITE_IDENTIFIER: BE7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3294
REMARK 800
REMARK 800 SITE_IDENTIFIER: BE8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3295
REMARK 800
REMARK 800 SITE_IDENTIFIER: BE9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3297
REMARK 800
REMARK 800 SITE_IDENTIFIER: BF1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3299
REMARK 800
REMARK 800 SITE_IDENTIFIER: BF2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3301
REMARK 800
REMARK 800 SITE_IDENTIFIER: BF3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3302
REMARK 800
REMARK 800 SITE_IDENTIFIER: BF4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3303
REMARK 800
REMARK 800 SITE_IDENTIFIER: BF5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3304
REMARK 800
REMARK 800 SITE_IDENTIFIER: BF6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3305
REMARK 800
REMARK 800 SITE_IDENTIFIER: BF7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3306
REMARK 800
REMARK 800 SITE_IDENTIFIER: BF8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3307
REMARK 800
REMARK 800 SITE_IDENTIFIER: BF9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3308
REMARK 800
REMARK 800 SITE_IDENTIFIER: BG1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3309
REMARK 800
REMARK 800 SITE_IDENTIFIER: BG2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3310
REMARK 800
REMARK 800 SITE_IDENTIFIER: BG3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3311
REMARK 800
REMARK 800 SITE_IDENTIFIER: BG4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3312
REMARK 800
REMARK 800 SITE_IDENTIFIER: BG5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3313
REMARK 800
REMARK 800 SITE_IDENTIFIER: BG6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3315
REMARK 800
REMARK 800 SITE_IDENTIFIER: BG7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3316
REMARK 800
REMARK 800 SITE_IDENTIFIER: BG8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3318
REMARK 800
REMARK 800 SITE_IDENTIFIER: BG9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3320
REMARK 800
REMARK 800 SITE_IDENTIFIER: BH1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3321
REMARK 800
REMARK 800 SITE_IDENTIFIER: BH2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3322
REMARK 800
REMARK 800 SITE_IDENTIFIER: BH3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3323
REMARK 800
REMARK 800 SITE_IDENTIFIER: BH4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3324
REMARK 800
REMARK 800 SITE_IDENTIFIER: BH5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3325
REMARK 800
REMARK 800 SITE_IDENTIFIER: BH6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3326
REMARK 800
REMARK 800 SITE_IDENTIFIER: BH7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3327
REMARK 800
REMARK 800 SITE_IDENTIFIER: BH8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3328
REMARK 800
REMARK 800 SITE_IDENTIFIER: BH9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3329
REMARK 800
REMARK 800 SITE_IDENTIFIER: BI1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3330
REMARK 800
REMARK 800 SITE_IDENTIFIER: BI2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3331
REMARK 800
REMARK 800 SITE_IDENTIFIER: BI3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3332
REMARK 800
REMARK 800 SITE_IDENTIFIER: BI4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3333
REMARK 800
REMARK 800 SITE_IDENTIFIER: BI5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3334
REMARK 800
REMARK 800 SITE_IDENTIFIER: BI6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3335
REMARK 800
REMARK 800 SITE_IDENTIFIER: BI7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3338
REMARK 800
REMARK 800 SITE_IDENTIFIER: BI8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3339
REMARK 800
REMARK 800 SITE_IDENTIFIER: BI9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3340
REMARK 800
REMARK 800 SITE_IDENTIFIER: BJ1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3341
REMARK 800
REMARK 800 SITE_IDENTIFIER: BJ2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3345
REMARK 800
REMARK 800 SITE_IDENTIFIER: BJ3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3346
REMARK 800
REMARK 800 SITE_IDENTIFIER: BJ4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3348
REMARK 800
REMARK 800 SITE_IDENTIFIER: BJ5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3349
REMARK 800
REMARK 800 SITE_IDENTIFIER: BJ6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3350
REMARK 800
REMARK 800 SITE_IDENTIFIER: BJ7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3351
REMARK 800
REMARK 800 SITE_IDENTIFIER: BJ8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3352
REMARK 800
REMARK 800 SITE_IDENTIFIER: BJ9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3353
REMARK 800
REMARK 800 SITE_IDENTIFIER: BK1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3354
REMARK 800
REMARK 800 SITE_IDENTIFIER: BK2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3355
REMARK 800
REMARK 800 SITE_IDENTIFIER: BK3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3356
REMARK 800
REMARK 800 SITE_IDENTIFIER: BK4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3358
REMARK 800
REMARK 800 SITE_IDENTIFIER: BK5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3359
REMARK 800
REMARK 800 SITE_IDENTIFIER: BK6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3361
REMARK 800
REMARK 800 SITE_IDENTIFIER: BK7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3363
REMARK 800
REMARK 800 SITE_IDENTIFIER: BK8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3364
REMARK 800
REMARK 800 SITE_IDENTIFIER: BK9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3365
REMARK 800
REMARK 800 SITE_IDENTIFIER: BL1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3366
REMARK 800
REMARK 800 SITE_IDENTIFIER: BL2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3367
REMARK 800
REMARK 800 SITE_IDENTIFIER: BL3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3368
REMARK 800
REMARK 800 SITE_IDENTIFIER: BL4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3371
REMARK 800
REMARK 800 SITE_IDENTIFIER: BL5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3373
REMARK 800
REMARK 800 SITE_IDENTIFIER: BL6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3374
REMARK 800
REMARK 800 SITE_IDENTIFIER: BL7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3375
REMARK 800
REMARK 800 SITE_IDENTIFIER: BL8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3377
REMARK 800
REMARK 800 SITE_IDENTIFIER: BL9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3378
REMARK 800
REMARK 800 SITE_IDENTIFIER: BM1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3380
REMARK 800
REMARK 800 SITE_IDENTIFIER: BM2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3382
REMARK 800
REMARK 800 SITE_IDENTIFIER: BM3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3383
REMARK 800
REMARK 800 SITE_IDENTIFIER: BM4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3384
REMARK 800
REMARK 800 SITE_IDENTIFIER: BM5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3385
REMARK 800
REMARK 800 SITE_IDENTIFIER: BM6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3386
REMARK 800
REMARK 800 SITE_IDENTIFIER: BM7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3387
REMARK 800
REMARK 800 SITE_IDENTIFIER: BM8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3388
REMARK 800
REMARK 800 SITE_IDENTIFIER: BM9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3390
REMARK 800
REMARK 800 SITE_IDENTIFIER: BN1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3391
REMARK 800
REMARK 800 SITE_IDENTIFIER: BN2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3392
REMARK 800
REMARK 800 SITE_IDENTIFIER: BN3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3394
REMARK 800
REMARK 800 SITE_IDENTIFIER: BN4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3395
REMARK 800
REMARK 800 SITE_IDENTIFIER: BN5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3396
REMARK 800
REMARK 800 SITE_IDENTIFIER: BN6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3397
REMARK 800
REMARK 800 SITE_IDENTIFIER: BN7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3398
REMARK 800
REMARK 800 SITE_IDENTIFIER: BN8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3400
REMARK 800
REMARK 800 SITE_IDENTIFIER: BN9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3401
REMARK 800
REMARK 800 SITE_IDENTIFIER: BO1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3403
REMARK 800
REMARK 800 SITE_IDENTIFIER: BO2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3404
REMARK 800
REMARK 800 SITE_IDENTIFIER: BO3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3405
REMARK 800
REMARK 800 SITE_IDENTIFIER: BO4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3406
REMARK 800
REMARK 800 SITE_IDENTIFIER: BO5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3407
REMARK 800
REMARK 800 SITE_IDENTIFIER: BO6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3409
REMARK 800
REMARK 800 SITE_IDENTIFIER: BO7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3410
REMARK 800
REMARK 800 SITE_IDENTIFIER: BO8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3411
REMARK 800
REMARK 800 SITE_IDENTIFIER: BO9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3412
REMARK 800
REMARK 800 SITE_IDENTIFIER: BP1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3413
REMARK 800
REMARK 800 SITE_IDENTIFIER: BP2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3414
REMARK 800
REMARK 800 SITE_IDENTIFIER: BP3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3415
REMARK 800
REMARK 800 SITE_IDENTIFIER: BP4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3416
REMARK 800
REMARK 800 SITE_IDENTIFIER: BP5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3419
REMARK 800
REMARK 800 SITE_IDENTIFIER: BP6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3420
REMARK 800
REMARK 800 SITE_IDENTIFIER: BP7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3421
REMARK 800
REMARK 800 SITE_IDENTIFIER: BP8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3422
REMARK 800
REMARK 800 SITE_IDENTIFIER: BP9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3423
REMARK 800
REMARK 800 SITE_IDENTIFIER: BQ1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3425
REMARK 800
REMARK 800 SITE_IDENTIFIER: BQ2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3426
REMARK 800
REMARK 800 SITE_IDENTIFIER: BQ3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3427
REMARK 800
REMARK 800 SITE_IDENTIFIER: BQ4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3428
REMARK 800
REMARK 800 SITE_IDENTIFIER: BQ5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3429
REMARK 800
REMARK 800 SITE_IDENTIFIER: BQ6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3430
REMARK 800
REMARK 800 SITE_IDENTIFIER: BQ7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3432
REMARK 800
REMARK 800 SITE_IDENTIFIER: BQ8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3433
REMARK 800
REMARK 800 SITE_IDENTIFIER: BQ9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3434
REMARK 800
REMARK 800 SITE_IDENTIFIER: BR1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3435
REMARK 800
REMARK 800 SITE_IDENTIFIER: BR2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3436
REMARK 800
REMARK 800 SITE_IDENTIFIER: BR3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3437
REMARK 800
REMARK 800 SITE_IDENTIFIER: BR4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3438
REMARK 800
REMARK 800 SITE_IDENTIFIER: BR5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3439
REMARK 800
REMARK 800 SITE_IDENTIFIER: BR6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3440
REMARK 800
REMARK 800 SITE_IDENTIFIER: BR7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3442
REMARK 800
REMARK 800 SITE_IDENTIFIER: BR8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3444
REMARK 800
REMARK 800 SITE_IDENTIFIER: BR9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3445
REMARK 800
REMARK 800 SITE_IDENTIFIER: BS1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3447
REMARK 800
REMARK 800 SITE_IDENTIFIER: BS2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3448
REMARK 800
REMARK 800 SITE_IDENTIFIER: BS3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3449
REMARK 800
REMARK 800 SITE_IDENTIFIER: BS4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3450
REMARK 800
REMARK 800 SITE_IDENTIFIER: BS5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3451
REMARK 800
REMARK 800 SITE_IDENTIFIER: BS6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3452
REMARK 800
REMARK 800 SITE_IDENTIFIER: BS7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3454
REMARK 800
REMARK 800 SITE_IDENTIFIER: BS8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3457
REMARK 800
REMARK 800 SITE_IDENTIFIER: BS9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3459
REMARK 800
REMARK 800 SITE_IDENTIFIER: BT1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3460
REMARK 800
REMARK 800 SITE_IDENTIFIER: BT2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3461
REMARK 800
REMARK 800 SITE_IDENTIFIER: BT3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3464
REMARK 800
REMARK 800 SITE_IDENTIFIER: BT4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3465
REMARK 800
REMARK 800 SITE_IDENTIFIER: BT5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3466
REMARK 800
REMARK 800 SITE_IDENTIFIER: BT6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3467
REMARK 800
REMARK 800 SITE_IDENTIFIER: BT7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3468
REMARK 800
REMARK 800 SITE_IDENTIFIER: BT8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3469
REMARK 800
REMARK 800 SITE_IDENTIFIER: BT9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3471
REMARK 800
REMARK 800 SITE_IDENTIFIER: BU1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3472
REMARK 800
REMARK 800 SITE_IDENTIFIER: BU2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3476
REMARK 800
REMARK 800 SITE_IDENTIFIER: BU3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3477
REMARK 800
REMARK 800 SITE_IDENTIFIER: BU4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3478
REMARK 800
REMARK 800 SITE_IDENTIFIER: BU5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3479
REMARK 800
REMARK 800 SITE_IDENTIFIER: BU6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3481
REMARK 800
REMARK 800 SITE_IDENTIFIER: BU7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3482
REMARK 800
REMARK 800 SITE_IDENTIFIER: BU8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3483
REMARK 800
REMARK 800 SITE_IDENTIFIER: BU9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3484
REMARK 800
REMARK 800 SITE_IDENTIFIER: BV1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3485
REMARK 800
REMARK 800 SITE_IDENTIFIER: BV2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3486
REMARK 800
REMARK 800 SITE_IDENTIFIER: BV3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3488
REMARK 800
REMARK 800 SITE_IDENTIFIER: BV4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3489
REMARK 800
REMARK 800 SITE_IDENTIFIER: BV5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3490
REMARK 800
REMARK 800 SITE_IDENTIFIER: BV6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3491
REMARK 800
REMARK 800 SITE_IDENTIFIER: BV7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SPD X 3492
REMARK 800
REMARK 800 SITE_IDENTIFIER: BV8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SPD X 3493
REMARK 800
REMARK 800 SITE_IDENTIFIER: BV9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SPD X 3494
REMARK 800
REMARK 800 SITE_IDENTIFIER: BW1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SPD X 3495
REMARK 800
REMARK 800 SITE_IDENTIFIER: BW2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SPD X 3496
REMARK 800
REMARK 800 SITE_IDENTIFIER: BW3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SPD X 3497
REMARK 800
REMARK 800 SITE_IDENTIFIER: BW4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SPD X 3498
REMARK 800
REMARK 800 SITE_IDENTIFIER: BW5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EOH X 3499
REMARK 800
REMARK 800 SITE_IDENTIFIER: BW6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EOH X 3500
REMARK 800
REMARK 800 SITE_IDENTIFIER: BW7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3501
REMARK 800
REMARK 800 SITE_IDENTIFIER: BW8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3502
REMARK 800
REMARK 800 SITE_IDENTIFIER: BW9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN X 3503
REMARK 800
REMARK 800 SITE_IDENTIFIER: BX1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 3504
REMARK 800
REMARK 800 SITE_IDENTIFIER: BX2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG Y 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: BX3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN Y 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: BX4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG Y 204
REMARK 800
REMARK 800 SITE_IDENTIFIER: BX5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG Y 206
REMARK 800
REMARK 800 SITE_IDENTIFIER: BX6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG Y 207
REMARK 800
REMARK 800 SITE_IDENTIFIER: BX7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN Y 208
REMARK 800
REMARK 800 SITE_IDENTIFIER: BX8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG Y 209
REMARK 800
REMARK 800 SITE_IDENTIFIER: BX9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG Y 210
REMARK 800
REMARK 800 SITE_IDENTIFIER: BY1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG Y 211
REMARK 800
REMARK 800 SITE_IDENTIFIER: BY2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG Y 212
REMARK 800
REMARK 800 SITE_IDENTIFIER: BY3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SPD Y 213
REMARK 800
REMARK 800 SITE_IDENTIFIER: BY4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG C 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: BY5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG C 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: BY6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG G 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: BY7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG G 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: BY8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG I 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: BY9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD J 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: BZ1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG J 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: BZ2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG M 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: BZ3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EPE N 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: BZ4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG P 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: BZ5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD Q 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: BZ6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN R 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: BZ7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN T 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: BZ8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD Z 101
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4WCE RELATED DB: PDB
REMARK 900 RELATED ID: 4WF9 RELATED DB: PDB
REMARK 900 RELATED ID: 4WFB RELATED DB: PDB
REMARK 900 RELATED ID: 4WFA RELATED DB: PDB
DBREF 5HL7 A 1 277 UNP P60430 RL2_STAA8 1 277
DBREF1 5HL7 X 1 2923 GB CP000253.1
DBREF2 5HL7 X 87201381 450739 453661
DBREF1 5HL7 Y 1 114 GB CP000253.1
DBREF2 5HL7 Y 87201381 453734 453847
DBREF 5HL7 B 1 220 UNP Q2FW06 RL3_STAA8 1 220
DBREF 5HL7 C 1 207 UNP Q2FW07 RL4_STAA8 1 207
DBREF 5HL7 D 1 179 UNP Q2FW18 RL5_STAA8 1 179
DBREF 5HL7 E 1 178 UNP Q2FW21 RL6_STAA8 1 178
DBREF 5HL7 G 1 145 UNP Q2FW38 RL13_STAA8 1 145
DBREF 5HL7 H 1 122 UNP Q2FW16 RL14_STAA8 1 122
DBREF 5HL7 I 1 140 UNP P0A0F8 RL15_STAA8 1 140
DBREF 5HL7 J 1 144 UNP Q2FW13 RL16_STAA8 1 144
DBREF 5HL7 K 1 122 UNP Q2FW33 RL17_STAA8 1 122
DBREF 5HL7 L 1 119 UNP Q2FW22 RL18_STAA8 1 119
DBREF 5HL7 M 1 116 UNP Q2FZ42 RL19_STAA8 1 116
DBREF 5HL7 N 1 118 UNP Q2FXQ1 RL20_STAA8 1 118
DBREF 5HL7 O 1 102 UNP Q2FXS8 RL21_STAA8 1 102
DBREF 5HL7 P 1 117 UNP Q2FW11 RL22_STAA8 1 117
DBREF 5HL7 Q 1 91 UNP Q2FW08 RL23_STAA8 1 91
DBREF 5HL7 R 1 105 UNP Q2FW17 RL24_STAA8 1 105
DBREF 5HL7 S 1 217 UNP Q2G0S0 Q2G0S0_STAA8 1 217
DBREF 5HL7 T 1 94 UNP Q2FXT0 RL27_STAA8 1 94
DBREF 5HL7 U 1 62 UNP Q2FZ60 RL28_STAA8 1 62
DBREF 5HL7 V 1 69 UNP Q2FW14 RL29_STAA8 1 69
DBREF 5HL7 W 1 59 UNP P0A0G2 RL30_STAA8 1 59
DBREF 5HL7 Z 1 58 UNP Q2FZF1 RL32_STAA8 1 58
DBREF 5HL7 2 1 45 UNP Q2FUQ0 RL34_STAA8 1 45
DBREF 5HL7 3 1 66 UNP Q2FXQ0 RL35_STAA8 1 66
DBREF 5HL7 4 1 37 UNP Q2FW29 RL36_STAA8 1 37
SEQADV 5HL7 LYS E 174 UNP Q2FW21 GLY 174 CONFLICT
SEQRES 1 A 277 MET ALA ILE LYS LYS TYR LYS PRO ILE THR ASN GLY ARG
SEQRES 2 A 277 ARG ASN MET THR SER LEU ASP PHE ALA GLU ILE THR LYS
SEQRES 3 A 277 THR THR PRO GLU LYS SER LEU LEU LYS PRO LEU PRO LYS
SEQRES 4 A 277 LYS ALA GLY ARG ASN ASN GLN GLY LYS LEU THR VAL ARG
SEQRES 5 A 277 HIS HIS GLY GLY GLY HIS LYS ARG GLN TYR ARG VAL ILE
SEQRES 6 A 277 ASP PHE LYS ARG ASN LYS ASP GLY ILE ASN ALA LYS VAL
SEQRES 7 A 277 ASP SER ILE GLN TYR ASP PRO ASN ARG SER ALA ASN ILE
SEQRES 8 A 277 ALA LEU VAL VAL TYR ALA ASP GLY GLU LYS ARG TYR ILE
SEQRES 9 A 277 ILE ALA PRO LYS GLY LEU GLU VAL GLY GLN ILE VAL GLU
SEQRES 10 A 277 SER GLY ALA GLU ALA ASP ILE LYS VAL GLY ASN ALA LEU
SEQRES 11 A 277 PRO LEU GLN ASN ILE PRO VAL GLY THR VAL VAL HIS ASN
SEQRES 12 A 277 ILE GLU LEU LYS PRO GLY LYS GLY GLY GLN ILE ALA ARG
SEQRES 13 A 277 SER ALA GLY ALA SER ALA GLN VAL LEU GLY LYS GLU GLY
SEQRES 14 A 277 LYS TYR VAL LEU ILE ARG LEU ARG SER GLY GLU VAL ARG
SEQRES 15 A 277 MET ILE LEU SER THR CYS ARG ALA THR ILE GLY GLN VAL
SEQRES 16 A 277 GLY ASN LEU GLN HIS GLU LEU VAL ASN VAL GLY LYS ALA
SEQRES 17 A 277 GLY ARG SER ARG TRP LYS GLY ILE ARG PRO THR VAL ARG
SEQRES 18 A 277 GLY SER VAL MET ASN PRO ASN ASP HIS PRO HIS GLY GLY
SEQRES 19 A 277 GLY GLU GLY ARG ALA PRO ILE GLY ARG PRO SER PRO MET
SEQRES 20 A 277 SER PRO TRP GLY LYS PRO THR LEU GLY LYS LYS THR ARG
SEQRES 21 A 277 ARG GLY LYS LYS SER SER ASP LYS LEU ILE VAL ARG GLY
SEQRES 22 A 277 ARG LYS LYS LYS
SEQRES 1 X 2923 G A U U A A G U U A U U A
SEQRES 2 X 2923 A G G G C G C A C G G U G
SEQRES 3 X 2923 G A U G C C U U G G C A C
SEQRES 4 X 2923 U A G A A G C C A A U G A
SEQRES 5 X 2923 A G G A C G U U A C U A A
SEQRES 6 X 2923 C G A C G A U A U G C U U
SEQRES 7 X 2923 U G G G G A G C U G U A A
SEQRES 8 X 2923 G U A A G C U U U G A U C
SEQRES 9 X 2923 C A G A G A U U U C C G A
SEQRES 10 X 2923 A U G G G G A A A C C C A
SEQRES 11 X 2923 G C A U G A G U U A U G U
SEQRES 12 X 2923 C A U G U U A U C G A U A
SEQRES 13 X 2923 U G U G A A U A C A U A G
SEQRES 14 X 2923 C A U A U C A G A A G G C
SEQRES 15 X 2923 A C A C C C G G A G A A C
SEQRES 16 X 2923 U G A A A C A U C U U A G
SEQRES 17 X 2923 U A C C C G G A G G A A G
SEQRES 18 X 2923 A G A A A G A A A A U U C
SEQRES 19 X 2923 G A U U C C C U U A G U A
SEQRES 20 X 2923 G C G G C G A G C G A A A
SEQRES 21 X 2923 C G G G A A G A G C C C A
SEQRES 22 X 2923 A A C C A A C A A G C U U
SEQRES 23 X 2923 G C U U G U U G G G G U U
SEQRES 24 X 2923 G U A G G A C A C U C U A
SEQRES 25 X 2923 U A C G G A G U U A C A A
SEQRES 26 X 2923 A G G A C G A C A U U A G
SEQRES 27 X 2923 A C G A A U C A U C U G G
SEQRES 28 X 2923 A A A G A U G A A U C A A
SEQRES 29 X 2923 A G A A G G U A A U A A U
SEQRES 30 X 2923 C C U G U A G U C G A A A
SEQRES 31 X 2923 A U G U U G U C U C U C U
SEQRES 32 X 2923 U G A G U G G A U C C U G
SEQRES 33 X 2923 A G U A C G A C G G A G C
SEQRES 34 X 2923 A C G U G A A A U U C C G
SEQRES 35 X 2923 U C G G A A U C U G G G A
SEQRES 36 X 2923 G G A C C A U C U C C U A
SEQRES 37 X 2923 A G G C U A A A U A C U C
SEQRES 38 X 2923 U C U A G U G A C C G A U
SEQRES 39 X 2923 A G U G A A C C A G U A C
SEQRES 40 X 2923 C G U G A G G G A A A G G
SEQRES 41 X 2923 U G A A A A G C A C C C C
SEQRES 42 X 2923 G G A A G G G G A G U G A
SEQRES 43 X 2923 A A U A G A A C C U G A A
SEQRES 44 X 2923 A C C G U G U G C U U A C
SEQRES 45 X 2923 A A G U A G U C A G A G C
SEQRES 46 X 2923 C C G U U A A U G G G U G
SEQRES 47 X 2923 A U G G C G U G C C U U U
SEQRES 48 X 2923 U G U A G A A U G A A C C
SEQRES 49 X 2923 G G C G A G U U A C G A U
SEQRES 50 X 2923 U U G A U G C A A G G U U
SEQRES 51 X 2923 A A G C A G U A A A U G U
SEQRES 52 X 2923 G G A G C C G U A G C G A
SEQRES 53 X 2923 A A G C G A G U C U G A A
SEQRES 54 X 2923 U A G G G C G U U U A G U
SEQRES 55 X 2923 A U U U G G U C G U A G A
SEQRES 56 X 2923 C C C G A A A C C A G G U
SEQRES 57 X 2923 G A U C U A C C C U U G G
SEQRES 58 X 2923 U C A G G U U G A A G U U
SEQRES 59 X 2923 C A G G U A A C A C U G A
SEQRES 60 X 2923 A U G G A G G A C C G A A
SEQRES 61 X 2923 C C G A C U U A C G U U G
SEQRES 62 X 2923 A A A A G U G A G C G G A
SEQRES 63 X 2923 U G A A C U G A G G G U A
SEQRES 64 X 2923 G C G G A G A A A U U C C
SEQRES 65 X 2923 A A U C G A A C C U G G A
SEQRES 66 X 2923 G A U A G C U G G U U C U
SEQRES 67 X 2923 C U C C G A A A U A G C U
SEQRES 68 X 2923 U U A G G G C U A G C C U
SEQRES 69 X 2923 C A A G U G A U G A U U A
SEQRES 70 X 2923 U U G G A G G U A G A G C
SEQRES 71 X 2923 A C U G U U U G G A C G A
SEQRES 72 X 2923 G G G G C C C C U C U C G
SEQRES 73 X 2923 G G U U A C C G A A U U C
SEQRES 74 X 2923 A G A C A A A C U C C G A
SEQRES 75 X 2923 A U G C C A A U U A A U U
SEQRES 76 X 2923 U A A C U U G G G A G U C
SEQRES 77 X 2923 A G A A C A U G G G U G A
SEQRES 78 X 2923 U A A G G U C C G U G U U
SEQRES 79 X 2923 C G A A A G G G A A A C A
SEQRES 80 X 2923 G C C C A G A C C A C C A
SEQRES 81 X 2923 G C U A A G G U C C C A A
SEQRES 82 X 2923 A A U A U A U G U U A A G
SEQRES 83 X 2923 U G G A A A A G G A U G U
SEQRES 84 X 2923 G G C G U U G C C C A G A
SEQRES 85 X 2923 C A A C U A G G A U G U U
SEQRES 86 X 2923 G G C U U A G A A G C A G
SEQRES 87 X 2923 C C A U C A U U U A A A G
SEQRES 88 X 2923 A G U G C G U A A U A G C
SEQRES 89 X 2923 U C A C U A G U C G A G U
SEQRES 90 X 2923 G A C A C U G C G C C G A
SEQRES 91 X 2923 A A A U G U A C C G G G G
SEQRES 92 X 2923 C U A A A C A U A U U A C
SEQRES 93 X 2923 C G A A G C U G U G G A U
SEQRES 94 X 2923 U G U C C U U U G G A C A
SEQRES 95 X 2923 A U G G U A G G A G A G C
SEQRES 96 X 2923 G U U C U A A G G G C G U
SEQRES 97 X 2923 U G A A G C A U G A U C G
SEQRES 98 X 2923 U A A G G A C A U G U G G
SEQRES 99 X 2923 A G C G C U U A G A A G U
SEQRES 100 X 2923 G A G A A U G C C G G U G
SEQRES 101 X 2923 U G A G U A G C G A A A G
SEQRES 102 X 2923 A C G G G U G A G A A U C
SEQRES 103 X 2923 C C G U C C A C C G A U U
SEQRES 104 X 2923 G A C U A A G G U U U C C
SEQRES 105 X 2923 A G A G G A A G G C U C G
SEQRES 106 X 2923 U C C G C U C U G G G U U
SEQRES 107 X 2923 A G U C G G G U C C U A A
SEQRES 108 X 2923 G C U G A G G C C G A C A
SEQRES 109 X 2923 G G C G U A G G C G A U G
SEQRES 110 X 2923 G A U A A C A G G U U G A
SEQRES 111 X 2923 U A U U C C U G U A C C A
SEQRES 112 X 2923 C C U A U A A U C G U U U
SEQRES 113 X 2923 U A A U C G A U G G G G G
SEQRES 114 X 2923 G A C G C A G U A G G A U
SEQRES 115 X 2923 A G G C G A A G C G U G C
SEQRES 116 X 2923 G A U U G G A U U G C A C
SEQRES 117 X 2923 G U C U A A G C A G U A A
SEQRES 118 X 2923 G G C U G A G U A U U A G
SEQRES 119 X 2923 G C A A A U C C G G U A C
SEQRES 120 X 2923 U C G U U A A G G C U G A
SEQRES 121 X 2923 G C U G U G A U G G G G A
SEQRES 122 X 2923 G A A G A C A U U G A G U
SEQRES 123 X 2923 C U U C G A G U C G U U G
SEQRES 124 X 2923 A U U U C A C A C U G C C
SEQRES 125 X 2923 G A G A A A A G C C U C U
SEQRES 126 X 2923 A G A U A G A A A A U A G
SEQRES 127 X 2923 G U G C C C G U A C C G C
SEQRES 128 X 2923 A A A C C G A C A C A G G
SEQRES 129 X 2923 U A G U C A A G A U G A G
SEQRES 130 X 2923 A A U U C U A A G G U G A
SEQRES 131 X 2923 G C G A G C G A A C U C U
SEQRES 132 X 2923 C G U U A A G G A A C U C
SEQRES 133 X 2923 G G C A A A A U G A C C C
SEQRES 134 X 2923 C G U A A C U U C G G G A
SEQRES 135 X 2923 G A A G G G G U G C U C U
SEQRES 136 X 2923 U U A G G G U U A A C G C
SEQRES 137 X 2923 C C A G A A G A G C C G C
SEQRES 138 X 2923 A G U G A A U A G G C C C
SEQRES 139 X 2923 A A G C G A C U G U U U A
SEQRES 140 X 2923 U C A A A A A C A C A G G
SEQRES 141 X 2923 U C U C U G C U A A A C C
SEQRES 142 X 2923 G U A A G G U G A U G U A
SEQRES 143 X 2923 U A G G G G C U G A C G C
SEQRES 144 X 2923 C U G C C C G G U G C U G
SEQRES 145 X 2923 G A A G G U U A A G A G G
SEQRES 146 X 2923 A G U G G U U A G C U U C
SEQRES 147 X 2923 U G C G A A G C U A C G A
SEQRES 148 X 2923 A U C G A A G C C C C A G
SEQRES 149 X 2923 U A A A C G G C G G C C G
SEQRES 150 X 2923 U A A C U A U A A C G G U
SEQRES 151 X 2923 C C U A A G G U A G C G A
SEQRES 152 X 2923 A A U U C C U U G U C G G
SEQRES 153 X 2923 G U A A G U U C C G A C C
SEQRES 154 X 2923 C G C A C G A A A G G C G
SEQRES 155 X 2923 U A A C G A U U U G G G C
SEQRES 156 X 2923 A C U G U C U C A A C G A
SEQRES 157 X 2923 G A G A C U C G G U G A A
SEQRES 158 X 2923 A U C A U A G U A C C U G
SEQRES 159 X 2923 U G A A G A U G C A G G U
SEQRES 160 X 2923 U A C C C G C G A C A G G
SEQRES 161 X 2923 A C G G A A A G A C C C C
SEQRES 162 X 2923 G U G G A G C U U U A C U
SEQRES 163 X 2923 G U A G C C U G A U A U U
SEQRES 164 X 2923 G A A A U U C G G C A C A
SEQRES 165 X 2923 G C U U G U A C A G G A U
SEQRES 166 X 2923 A G G U A G G A G C C U U
SEQRES 167 X 2923 U G A A A C G U G A G C G
SEQRES 168 X 2923 C U A G C U U A C G U G G
SEQRES 169 X 2923 A G G C G C U G G U G G G
SEQRES 170 X 2923 A U A C U A C C C U A G C
SEQRES 171 X 2923 U G U G U U G G C U U U C
SEQRES 172 X 2923 U A A C C C G C A C C A C
SEQRES 173 X 2923 U U A U C G U G G U G G G
SEQRES 174 X 2923 A G A C A G U G U C A A G
SEQRES 175 X 2923 C G G G C A G U U U G A C
SEQRES 176 X 2923 U G G G G C G G U C G C C
SEQRES 177 X 2923 U C C U A A A A G G U A A
SEQRES 178 X 2923 C G G A G G C G C U C A A
SEQRES 179 X 2923 A G G U U C C C U C A G A
SEQRES 180 X 2923 A U G G U U G G A A A U C
SEQRES 181 X 2923 A U U C A U A G A G U G U
SEQRES 182 X 2923 A A A G G C A U A A G G G
SEQRES 183 X 2923 A G C U U G A C U G C G A
SEQRES 184 X 2923 G A C C U A C A A G U C G
SEQRES 185 X 2923 A G C A G G G U C G A A A
SEQRES 186 X 2923 G A C G G A C U U A G U G
SEQRES 187 X 2923 A U C C G G U G G U U C C
SEQRES 188 X 2923 G C A U G G A A G G G C C
SEQRES 189 X 2923 A U C G C U C A A C G G A
SEQRES 190 X 2923 U A A A A G C U A C C C C
SEQRES 191 X 2923 G G G G A U A A C A G G C
SEQRES 192 X 2923 U U A U C U C C C C C A A
SEQRES 193 X 2923 G A G U U C A C A U C G A
SEQRES 194 X 2923 C G G G G A G G U U U G G
SEQRES 195 X 2923 C A C C U C G A U G U C G
SEQRES 196 X 2923 G C U C A U C G C A U C C
SEQRES 197 X 2923 U G G G G C U G U A G U C
SEQRES 198 X 2923 G G U C C C A A G G G U U
SEQRES 199 X 2923 G G G C U G U U C G C C C
SEQRES 200 X 2923 A U U A A A G C G G U A C
SEQRES 201 X 2923 G C G A G C U G G G U U C
SEQRES 202 X 2923 A G A A C G U C G U G A G
SEQRES 203 X 2923 A C A G U U C G G U C C C
SEQRES 204 X 2923 U A U C C G U C G U G G G
SEQRES 205 X 2923 C G U A G G A A A U U U G
SEQRES 206 X 2923 A G A G G A G C U G U C C
SEQRES 207 X 2923 U U A G U A C G A G A G G
SEQRES 208 X 2923 A C C G G G A U G G A C A
SEQRES 209 X 2923 U A C C U C U G G U G U A
SEQRES 210 X 2923 C C A G U U G U C G U G C
SEQRES 211 X 2923 C A A C G G C A U A G C U
SEQRES 212 X 2923 G G G U A G C U A U G U G
SEQRES 213 X 2923 U G G A C G G G A U A A G
SEQRES 214 X 2923 U G C U G A A A G C A U C
SEQRES 215 X 2923 U A A G C A U G A A G C C
SEQRES 216 X 2923 C C C C U C A A G A U G A
SEQRES 217 X 2923 G A U U U C C C A A C U U
SEQRES 218 X 2923 C G G U U A U A A G A U C
SEQRES 219 X 2923 C C U C A A A G A U G A U
SEQRES 220 X 2923 G A G G U U A A U A G G U
SEQRES 221 X 2923 U C G A G G U G G A A G C
SEQRES 222 X 2923 A U G G U G A C A U G U G
SEQRES 223 X 2923 G A G C U G A C G A A U A
SEQRES 224 X 2923 C U A A U C G A U C G A A
SEQRES 225 X 2923 G A C U U A A U C A A
SEQRES 1 Y 114 U C U G G U G A C U A U A
SEQRES 2 Y 114 G C A A G G A G G U C A C
SEQRES 3 Y 114 A C C U G U U C C C A U G
SEQRES 4 Y 114 C C G A A C A C A G A A G
SEQRES 5 Y 114 U U A A G G U C U U U A G
SEQRES 6 Y 114 C G A C G A U G G U A G C
SEQRES 7 Y 114 C A A C U U A C G U U C C
SEQRES 8 Y 114 G C U A G A G U A G A A C
SEQRES 9 Y 114 G U U G C C A G G C
SEQRES 1 B 220 MET THR LYS GLY ILE LEU GLY ARG LYS ILE GLY MET THR
SEQRES 2 B 220 GLN VAL PHE GLY GLU ASN GLY GLU LEU ILE PRO VAL THR
SEQRES 3 B 220 VAL VAL GLU ALA LYS GLU ASN VAL VAL LEU GLN LYS LYS
SEQRES 4 B 220 THR VAL GLU VAL ASP GLY TYR ASN ALA ILE GLN VAL GLY
SEQRES 5 B 220 PHE GLU ASP LYS LYS ALA TYR LYS LYS ASP ALA LYS SER
SEQRES 6 B 220 ASN LYS TYR ALA ASN LYS PRO ALA GLU GLY HIS ALA LYS
SEQRES 7 B 220 LYS ALA ASP ALA ALA PRO LYS ARG PHE ILE ARG GLU PHE
SEQRES 8 B 220 ARG ASN VAL ASP VAL ASP ALA TYR GLU VAL GLY GLN GLU
SEQRES 9 B 220 VAL SER VAL ASP THR PHE VAL ALA GLY ASP VAL ILE ASP
SEQRES 10 B 220 VAL THR GLY VAL SER LYS GLY LYS GLY PHE GLN GLY ALA
SEQRES 11 B 220 ILE LYS ARG HIS GLY GLN SER ARG GLY PRO MET SER HIS
SEQRES 12 B 220 GLY SER HIS PHE HIS ARG ALA PRO GLY SER VAL GLY MET
SEQRES 13 B 220 ALA SER ASP ALA SER ARG VAL PHE LYS GLY GLN LYS MET
SEQRES 14 B 220 PRO GLY ARG MET GLY GLY ASN THR VAL THR VAL GLN ASN
SEQRES 15 B 220 LEU GLU VAL VAL GLN VAL ASP THR GLU ASN LYS VAL ILE
SEQRES 16 B 220 LEU VAL LYS GLY ASN VAL PRO GLY PRO LYS LYS GLY LEU
SEQRES 17 B 220 VAL GLU ILE ARG THR SER ILE LYS LYS GLY ASN LYS
SEQRES 1 C 207 MET ALA ASN TYR ASP VAL LEU LYS LEU ASP GLY THR LYS
SEQRES 2 C 207 SER GLY SER ILE GLU LEU SER ASP ALA VAL PHE GLY ILE
SEQRES 3 C 207 GLU PRO ASN ASN SER VAL LEU PHE GLU ALA ILE ASN LEU
SEQRES 4 C 207 GLN ARG ALA SER LEU ARG GLN GLY THR HIS ALA VAL LYS
SEQRES 5 C 207 ASN ARG SER ALA VAL SER GLY GLY GLY ARG LYS PRO TRP
SEQRES 6 C 207 LYS GLN LYS GLY THR GLY ARG ALA ARG GLN GLY THR ILE
SEQRES 7 C 207 ARG ALA PRO GLN TRP ARG GLY GLY GLY ILE VAL PHE GLY
SEQRES 8 C 207 PRO THR PRO ARG SER TYR ALA TYR LYS MET PRO LYS LYS
SEQRES 9 C 207 MET ARG ARG LEU ALA LEU ARG SER ALA LEU SER PHE LYS
SEQRES 10 C 207 ALA GLN GLU ASN GLY LEU THR VAL VAL ASP ALA PHE ASN
SEQRES 11 C 207 PHE GLU ALA PRO LYS THR LYS GLU PHE LYS ASN VAL LEU
SEQRES 12 C 207 SER THR LEU GLU GLN PRO LYS LYS VAL LEU VAL VAL THR
SEQRES 13 C 207 GLU ASN GLU ASP VAL ASN VAL GLU LEU SER ALA ARG ASN
SEQRES 14 C 207 ILE PRO GLY VAL GLN VAL THR THR ALA GLN GLY LEU ASN
SEQRES 15 C 207 VAL LEU ASP ILE THR ASN ALA ASP SER LEU VAL ILE THR
SEQRES 16 C 207 GLU ALA ALA ALA LYS LYS VAL GLU GLU VAL LEU GLY
SEQRES 1 D 179 MET ASN ARG LEU LYS GLU LYS PHE ASN THR GLU VAL THR
SEQRES 2 D 179 GLU ASN LEU MET LYS LYS PHE ASN TYR SER SER VAL MET
SEQRES 3 D 179 GLU VAL PRO LYS ILE ASP LYS ILE VAL VAL ASN MET GLY
SEQRES 4 D 179 VAL GLY ASP ALA VAL GLN ASN SER LYS VAL LEU ASP ASN
SEQRES 5 D 179 ALA VAL GLU GLU LEU GLU LEU ILE THR GLY GLN LYS PRO
SEQRES 6 D 179 LEU VAL THR LYS ALA LYS LYS SER ILE ALA THR PHE ARG
SEQRES 7 D 179 LEU ARG GLU GLY MET PRO ILE GLY ALA LYS VAL THR LEU
SEQRES 8 D 179 ARG GLY GLU ARG MET TYR GLU PHE LEU ASP LYS LEU ILE
SEQRES 9 D 179 SER VAL SER LEU PRO ARG VAL ARG ASP PHE GLN GLY VAL
SEQRES 10 D 179 SER LYS LYS ALA PHE ASP GLY ARG GLY ASN TYR THR LEU
SEQRES 11 D 179 GLY VAL LYS GLU GLN LEU ILE PHE PRO GLU ILE ASP TYR
SEQRES 12 D 179 ASP LYS VAL SER LYS VAL ARG GLY MET ASP ILE VAL ILE
SEQRES 13 D 179 VAL THR THR ALA ASN THR ASP GLU GLU ALA ARG GLU LEU
SEQRES 14 D 179 LEU ALA ASN PHE GLY MET PRO PHE ARG LYS
SEQRES 1 E 178 MET SER ARG VAL GLY LYS LYS ILE ILE ASP ILE PRO SER
SEQRES 2 E 178 ASP VAL THR VAL THR PHE ASP GLY ASN HIS VAL THR VAL
SEQRES 3 E 178 LYS GLY PRO LYS GLY GLU LEU SER ARG THR LEU ASN GLU
SEQRES 4 E 178 ARG MET THR PHE LYS GLN GLU GLU ASN THR ILE GLU VAL
SEQRES 5 E 178 VAL ARG PRO SER ASP SER LYS GLU ASP ARG THR ASN HIS
SEQRES 6 E 178 GLY THR THR ARG ALA LEU LEU ASN ASN MET VAL GLN GLY
SEQRES 7 E 178 VAL SER GLN GLY TYR VAL LYS VAL LEU GLU LEU VAL GLY
SEQRES 8 E 178 VAL GLY TYR ARG ALA GLN MET GLN GLY LYS ASP LEU ILE
SEQRES 9 E 178 LEU ASN VAL GLY TYR SER HIS PRO VAL GLU ILE LYS ALA
SEQRES 10 E 178 GLU GLU ASN ILE THR PHE SER VAL GLU LYS ASN THR VAL
SEQRES 11 E 178 VAL LYS VAL GLU GLY ILE SER LYS GLU GLN VAL GLY ALA
SEQRES 12 E 178 LEU ALA SER ASN ILE ARG SER VAL ARG PRO PRO GLU PRO
SEQRES 13 E 178 TYR LYS GLY LYS GLY ILE ARG TYR GLN GLY GLU TYR VAL
SEQRES 14 E 178 ARG ARG LYS GLU LYS LYS THR GLY LYS
SEQRES 1 G 145 MET ARG GLN THR PHE MET ALA ASN GLU SER ASN ILE GLU
SEQRES 2 G 145 ARG LYS TRP TYR VAL ILE ASP ALA GLU GLY GLN THR LEU
SEQRES 3 G 145 GLY ARG LEU SER SER GLU VAL ALA SER ILE LEU ARG GLY
SEQRES 4 G 145 LYS ASN LYS VAL THR TYR THR PRO HIS VAL ASP THR GLY
SEQRES 5 G 145 ASP TYR VAL ILE VAL ILE ASN ALA SER LYS ILE GLU PHE
SEQRES 6 G 145 THR GLY ASN LYS GLU THR ASP LYS VAL TYR TYR ARG HIS
SEQRES 7 G 145 SER ASN HIS PRO GLY GLY ILE LYS SER ILE THR ALA GLY
SEQRES 8 G 145 GLU LEU ARG ARG THR ASN PRO GLU ARG LEU ILE GLU ASN
SEQRES 9 G 145 SER ILE LYS GLY MET LEU PRO SER THR ARG LEU GLY GLU
SEQRES 10 G 145 LYS GLN GLY LYS LYS LEU PHE VAL TYR GLY GLY ALA GLU
SEQRES 11 G 145 HIS PRO HIS ALA ALA GLN GLN PRO GLU ASN TYR GLU LEU
SEQRES 12 G 145 ARG GLY
SEQRES 1 H 122 MET ILE GLN GLN GLU THR ARG LEU LYS VAL ALA ASP ASN
SEQRES 2 H 122 SER GLY ALA ARG GLU VAL LEU THR ILE LYS VAL LEU GLY
SEQRES 3 H 122 GLY SER GLY ARG LYS THR ALA ASN ILE GLY ASP VAL ILE
SEQRES 4 H 122 VAL CYS THR VAL LYS ASN ALA THR PRO GLY GLY VAL VAL
SEQRES 5 H 122 LYS LYS GLY ASP VAL VAL LYS ALA VAL ILE VAL ARG THR
SEQRES 6 H 122 LYS SER GLY VAL ARG ARG ASN ASP GLY SER TYR ILE LYS
SEQRES 7 H 122 PHE ASP GLU ASN ALA CYS VAL ILE ILE ARG ASP ASP LYS
SEQRES 8 H 122 GLY PRO ARG GLY THR ARG ILE PHE GLY PRO VAL ALA ARG
SEQRES 9 H 122 GLU LEU ARG GLU GLY ASN PHE MET LYS ILE VAL SER LEU
SEQRES 10 H 122 ALA PRO GLU VAL LEU
SEQRES 1 I 140 MET LYS LEU HIS GLU LEU LYS PRO ALA GLU GLY SER ARG
SEQRES 2 I 140 LYS GLU ARG ASN ARG VAL GLY ARG GLY VAL ALA THR GLY
SEQRES 3 I 140 ASN GLY LYS THR SER GLY ARG GLY HIS LYS GLY GLN LYS
SEQRES 4 I 140 ALA ARG SER GLY GLY GLY VAL ARG PRO GLY PHE GLU GLY
SEQRES 5 I 140 GLY GLN LEU PRO LEU PHE ARG ARG LEU PRO LYS ARG GLY
SEQRES 6 I 140 PHE THR ASN ILE ASN ARG LYS GLU TYR ALA ILE VAL ASN
SEQRES 7 I 140 LEU ASP GLN LEU ASN LYS PHE GLU ASP GLY THR GLU VAL
SEQRES 8 I 140 THR PRO ALA LEU LEU VAL GLU SER GLY VAL VAL LYS ASN
SEQRES 9 I 140 GLU LYS SER GLY ILE LYS ILE LEU GLY ASN GLY SER LEU
SEQRES 10 I 140 ASP LYS LYS LEU THR VAL LYS ALA HIS LYS PHE SER ALA
SEQRES 11 I 140 SER ALA ALA GLU ALA ILE ASP ALA LYS GLY
SEQRES 1 J 144 MET LEU LEU PRO LYS ARG VAL LYS TYR ARG ARG GLN HIS
SEQRES 2 J 144 ARG PRO LYS THR THR GLY ARG SER LYS GLY GLY ASN TYR
SEQRES 3 J 144 VAL THR PHE GLY GLU PHE GLY LEU GLN ALA THR THR THR
SEQRES 4 J 144 SER TRP ILE THR SER ARG GLN ILE GLU SER ALA ARG ILE
SEQRES 5 J 144 ALA MET THR ARG TYR MET LYS ARG GLY GLY LYS VAL TRP
SEQRES 6 J 144 ILE LYS ILE PHE PRO HIS THR PRO TYR THR LYS LYS PRO
SEQRES 7 J 144 LEU GLU VAL ARG MET GLY ALA GLY LYS GLY ALA VAL GLU
SEQRES 8 J 144 GLY TRP ILE ALA VAL VAL LYS PRO GLY ARG ILE LEU PHE
SEQRES 9 J 144 GLU VAL ALA GLY VAL SER GLU GLU VAL ALA ARG GLU ALA
SEQRES 10 J 144 LEU ARG LEU ALA SER HIS LYS LEU PRO VAL LYS THR LYS
SEQRES 11 J 144 PHE VAL LYS ARG GLU GLU LEU GLY GLY GLU THR ASN GLU
SEQRES 12 J 144 SER
SEQRES 1 K 122 MET GLY TYR ARG LYS LEU GLY ARG THR SER ASP GLN ARG
SEQRES 2 K 122 LYS ALA MET LEU ARG ASP LEU ALA THR SER LEU ILE ILE
SEQRES 3 K 122 SER GLU ARG ILE GLU THR THR GLU ALA ARG ALA LYS GLU
SEQRES 4 K 122 VAL ARG SER VAL VAL GLU LYS LEU ILE THR LEU GLY LYS
SEQRES 5 K 122 LYS GLY ASP LEU ALA SER ARG ARG ASN ALA ALA LYS THR
SEQRES 6 K 122 LEU ARG ASN VAL GLU ILE LEU ASN GLU ASP GLU THR THR
SEQRES 7 K 122 GLN THR ALA LEU GLN LYS LEU PHE GLY GLU ILE ALA GLU
SEQRES 8 K 122 ARG TYR THR GLU ARG GLN GLY GLY TYR THR ARG ILE LEU
SEQRES 9 K 122 LYS GLN GLY PRO ARG ARG GLY ASP GLY ALA GLU SER VAL
SEQRES 10 K 122 ILE ILE GLU LEU VAL
SEQRES 1 L 119 MET ILE SER LYS ILE ASP LYS ASN LYS VAL ARG LEU LYS
SEQRES 2 L 119 ARG HIS ALA ARG VAL ARG THR ASN LEU SER GLY THR ALA
SEQRES 3 L 119 GLU LYS PRO ARG LEU ASN VAL TYR ARG SER ASN LYS HIS
SEQRES 4 L 119 ILE TYR ALA GLN ILE ILE ASP ASP ASN LYS GLY VAL THR
SEQRES 5 L 119 LEU ALA GLN ALA SER SER LYS ASP SER ASP ILE ALA THR
SEQRES 6 L 119 THR ALA THR LYS VAL GLU LEU ALA THR LYS VAL GLY GLU
SEQRES 7 L 119 ALA ILE ALA LYS LYS ALA ALA ASP LYS GLY ILE LYS GLU
SEQRES 8 L 119 ILE VAL PHE ASP ARG GLY GLY TYR LEU TYR HIS GLY ARG
SEQRES 9 L 119 VAL LYS ALA LEU ALA GLU ALA ALA ARG GLU SER GLY LEU
SEQRES 10 L 119 GLU PHE
SEQRES 1 M 116 MET THR ASN HIS LYS LEU ILE GLU ALA VAL THR LYS SER
SEQRES 2 M 116 GLN LEU ARG THR ASP LEU PRO SER PHE ARG PRO GLY ASP
SEQRES 3 M 116 THR LEU ARG VAL HIS VAL ARG ILE ILE GLU GLY THR ARG
SEQRES 4 M 116 GLU ARG ILE GLN VAL PHE GLU GLY VAL VAL ILE LYS ARG
SEQRES 5 M 116 ARG GLY GLY GLY VAL SER GLU THR PHE THR VAL ARG LYS
SEQRES 6 M 116 ILE SER SER GLY VAL GLY VAL GLU ARG THR PHE PRO LEU
SEQRES 7 M 116 HIS THR PRO LYS ILE GLU LYS ILE GLU VAL LYS ARG ARG
SEQRES 8 M 116 GLY LYS VAL ARG ARG ALA LYS LEU TYR TYR LEU ARG SER
SEQRES 9 M 116 LEU ARG GLY LYS ALA ALA ARG ILE GLN GLU ILE ARG
SEQRES 1 N 118 MET PRO ARG VAL LYS GLY GLY THR VAL THR ARG ALA ARG
SEQRES 2 N 118 ARG LYS LYS THR ILE LYS LEU ALA LYS GLY TYR PHE GLY
SEQRES 3 N 118 SER LYS HIS THR LEU TYR LYS VAL ALA LYS GLN GLN VAL
SEQRES 4 N 118 MET LYS SER GLY GLN TYR ALA PHE ARG ASP ARG ARG GLN
SEQRES 5 N 118 ARG LYS ARG ASP PHE ARG LYS LEU TRP ILE THR ARG ILE
SEQRES 6 N 118 ASN ALA ALA ALA ARG GLN HIS GLU MET SER TYR SER ARG
SEQRES 7 N 118 LEU MET ASN GLY LEU LYS LYS ALA GLY ILE ASP ILE ASN
SEQRES 8 N 118 ARG LYS MET LEU SER GLU ILE ALA ILE SER ASP GLU LYS
SEQRES 9 N 118 ALA PHE ALA GLN LEU VAL THR LYS ALA LYS ASP ALA LEU
SEQRES 10 N 118 LYS
SEQRES 1 O 102 MET PHE ALA ILE ILE GLU THR GLY GLY LYS GLN ILE LYS
SEQRES 2 O 102 VAL GLU GLU GLY GLN GLU ILE PHE VAL GLU LYS LEU ASP
SEQRES 3 O 102 VAL ASN GLU GLY ASP THR PHE THR PHE ASP LYS VAL LEU
SEQRES 4 O 102 PHE VAL GLY GLY ASP SER VAL LYS VAL GLY ALA PRO THR
SEQRES 5 O 102 VAL GLU GLY ALA THR VAL THR ALA THR VAL ASN LYS GLN
SEQRES 6 O 102 GLY ARG GLY LYS LYS ILE THR VAL PHE THR TYR LYS ARG
SEQRES 7 O 102 ARG LYS ASN SER LYS ARG LYS LYS GLY HIS ARG GLN PRO
SEQRES 8 O 102 TYR THR LYS LEU THR ILE ASP LYS ILE ASN ALA
SEQRES 1 P 117 MET GLU ALA LYS ALA VAL ALA ARG THR ILE ARG ILE ALA
SEQRES 2 P 117 PRO ARG LYS VAL ARG LEU VAL LEU ASP LEU ILE ARG GLY
SEQRES 3 P 117 LYS ASN ALA ALA GLU ALA ILE ALA ILE LEU LYS LEU THR
SEQRES 4 P 117 ASN LYS ALA SER SER PRO VAL ILE GLU LYS VAL LEU MET
SEQRES 5 P 117 SER ALA LEU ALA ASN ALA GLU HIS ASN TYR ASP MET ASN
SEQRES 6 P 117 THR ASP GLU LEU VAL VAL LYS GLU ALA TYR ALA ASN GLU
SEQRES 7 P 117 GLY PRO THR LEU LYS ARG PHE ARG PRO ARG ALA GLN GLY
SEQRES 8 P 117 ARG ALA SER ALA ILE ASN LYS ARG THR SER HIS ILE THR
SEQRES 9 P 117 ILE VAL VAL SER ASP GLY LYS GLU GLU ALA LYS GLU ALA
SEQRES 1 Q 91 MET GLU ALA ARG ASP ILE LEU LYS ARG PRO VAL ILE THR
SEQRES 2 Q 91 GLU LYS SER SER GLU ALA MET ALA GLU ASP LYS TYR THR
SEQRES 3 Q 91 PHE ASP VAL ASP THR ARG VAL ASN LYS THR GLN VAL LYS
SEQRES 4 Q 91 MET ALA VAL GLU GLU ILE PHE ASN VAL LYS VAL ALA SER
SEQRES 5 Q 91 VAL ASN ILE MET ASN TYR LYS PRO LYS LYS LYS ARG MET
SEQRES 6 Q 91 GLY ARG TYR GLN GLY TYR THR ASN LYS ARG ARG LYS ALA
SEQRES 7 Q 91 ILE VAL THR LEU LYS GLU GLY SER ILE ASP LEU PHE ASN
SEQRES 1 R 105 MET HIS ILE LYS LYS GLY ASP ASN VAL LYS VAL ILE ALA
SEQRES 2 R 105 GLY LYS ASP LYS GLY LYS GLU GLY LYS VAL ILE ALA THR
SEQRES 3 R 105 LEU PRO LYS LYS ASP ARG VAL VAL VAL GLU GLY VAL ASN
SEQRES 4 R 105 ILE MET LYS LYS HIS GLN LYS PRO THR GLN LEU ASN PRO
SEQRES 5 R 105 GLU GLY GLY ILE LEU GLU THR GLU ALA ALA ILE HIS VAL
SEQRES 6 R 105 SER ASN VAL GLN LEU LEU ASP PRO LYS THR ASN GLU PRO
SEQRES 7 R 105 THR ARG VAL GLY TYR LYS PHE VAL ASP GLY LYS LYS VAL
SEQRES 8 R 105 ARG ILE ALA LYS LYS SER GLY GLU GLU ILE LYS SER ASN
SEQRES 9 R 105 ASN
SEQRES 1 S 217 MET ALA SER LEU LYS SER ILE ILE ARG GLN GLY LYS GLN
SEQRES 2 S 217 THR ARG SER ASP LEU LYS GLN LEU ARG LYS SER GLY LYS
SEQRES 3 S 217 VAL PRO ALA VAL VAL TYR GLY TYR GLY THR LYS ASN VAL
SEQRES 4 S 217 SER VAL LYS VAL ASP GLU VAL GLU PHE ILE LYS VAL ILE
SEQRES 5 S 217 ARG GLU VAL GLY ARG ASN GLY VAL ILE GLU LEU GLY VAL
SEQRES 6 S 217 GLY SER LYS THR ILE LYS VAL MET VAL ALA ASP TYR GLN
SEQRES 7 S 217 PHE ASP PRO LEU LYS ASN GLN ILE THR HIS ILE ASP PHE
SEQRES 8 S 217 LEU ALA ILE ASN MET SER GLU GLU ARG THR VAL GLU VAL
SEQRES 9 S 217 PRO VAL GLN LEU VAL GLY GLU ALA VAL GLY ALA LYS GLU
SEQRES 10 S 217 GLY GLY VAL VAL GLU GLN PRO LEU PHE ASN LEU GLU VAL
SEQRES 11 S 217 THR ALA THR PRO ASP ASN ILE PRO GLU ALA ILE GLU VAL
SEQRES 12 S 217 ASP ILE THR GLU LEU ASN ILE ASN ASP SER LEU THR VAL
SEQRES 13 S 217 ALA ASP VAL LYS VAL THR GLY ASP PHE LYS ILE GLU ASN
SEQRES 14 S 217 ASP SER ALA GLU SER VAL VAL THR VAL VAL ALA PRO THR
SEQRES 15 S 217 GLU GLU PRO THR GLU GLU GLU ILE GLU ALA MET GLU GLY
SEQRES 16 S 217 GLU GLN GLN THR GLU GLU PRO GLU VAL VAL GLY GLU SER
SEQRES 17 S 217 LYS GLU ASP GLU GLU LYS THR GLU GLU
SEQRES 1 T 94 MET LEU LYS LEU ASN LEU GLN PHE PHE ALA SER LYS LYS
SEQRES 2 T 94 GLY VAL SER SER THR LYS ASN GLY ARG ASP SER GLU SER
SEQRES 3 T 94 LYS ARG LEU GLY ALA LYS ARG ALA ASP GLY GLN PHE VAL
SEQRES 4 T 94 THR GLY GLY SER ILE LEU TYR ARG GLN ARG GLY THR LYS
SEQRES 5 T 94 ILE TYR PRO GLY GLU ASN VAL GLY ARG GLY GLY ASP ASP
SEQRES 6 T 94 THR LEU PHE ALA LYS ILE ASP GLY VAL VAL LYS PHE GLU
SEQRES 7 T 94 ARG LYS GLY ARG ASP LYS LYS GLN VAL SER VAL TYR ALA
SEQRES 8 T 94 VAL ALA GLU
SEQRES 1 U 62 MET GLY LYS GLN CYS PHE VAL THR GLY ARG LYS ALA SER
SEQRES 2 U 62 THR GLY ASN ARG ARG SER HIS ALA LEU ASN SER THR LYS
SEQRES 3 U 62 ARG ARG TRP ASN ALA ASN LEU GLN LYS VAL ARG ILE LEU
SEQRES 4 U 62 VAL ASP GLY LYS PRO LYS LYS VAL TRP VAL SER ALA ARG
SEQRES 5 U 62 ALA LEU LYS SER GLY LYS VAL THR ARG VAL
SEQRES 1 V 69 MET LYS ALA LYS GLU ILE ARG ASP LEU THR THR SER GLU
SEQRES 2 V 69 ILE GLU GLU GLN ILE LYS SER SER LYS GLU GLU LEU PHE
SEQRES 3 V 69 ASN LEU ARG PHE GLN LEU ALA THR GLY GLN LEU GLU GLU
SEQRES 4 V 69 THR ALA ARG ILE ARG THR VAL ARG LYS THR ILE ALA ARG
SEQRES 5 V 69 LEU LYS THR VAL ALA ARG GLU ARG GLU ILE GLU GLN SER
SEQRES 6 V 69 LYS ALA ASN GLN
SEQRES 1 W 59 MET ALA LYS LEU GLN ILE THR LEU THR ARG SER VAL ILE
SEQRES 2 W 59 GLY ARG PRO GLU THR GLN ARG LYS THR VAL GLU ALA LEU
SEQRES 3 W 59 GLY LEU LYS LYS THR ASN SER SER VAL VAL VAL GLU ASP
SEQRES 4 W 59 ASN PRO ALA ILE ARG GLY GLN ILE ASN LYS VAL LYS HIS
SEQRES 5 W 59 LEU VAL THR VAL GLU GLU LYS
SEQRES 1 Z 58 MET ALA VAL PRO LYS ARG ARG THR SER LYS THR ARG LYS
SEQRES 2 Z 58 ASN LYS ARG ARG THR HIS PHE LYS ILE SER VAL PRO GLY
SEQRES 3 Z 58 MET THR GLU CYS PRO ASN CYS GLY ARG GLU TYR LYS LEU
SEQRES 4 Z 58 SER HIS ARG VAL CYS LYS ASN CYS GLY SER TYR ASN GLY
SEQRES 5 Z 58 GLU GLU VAL ALA ALA LYS
SEQRES 1 2 45 MET VAL LYS ARG THR TYR GLN PRO ASN LYS ARG LYS HIS
SEQRES 2 2 45 SER LYS VAL HIS GLY PHE ARG LYS ARG MET SER THR LYS
SEQRES 3 2 45 ASN GLY ARG LYS VAL LEU ALA ARG ARG ARG ARG LYS GLY
SEQRES 4 2 45 ARG LYS VAL LEU SER ALA
SEQRES 1 3 66 MET PRO LYS MET LYS THR HIS ARG GLY ALA ALA LYS ARG
SEQRES 2 3 66 VAL LYS ARG THR ALA SER GLY GLN LEU LYS ARG SER ARG
SEQRES 3 3 66 ALA PHE THR SER HIS LEU PHE ALA ASN LYS SER THR LYS
SEQRES 4 3 66 GLN LYS ARG GLN LEU ARG LYS ALA ARG LEU VAL SER LYS
SEQRES 5 3 66 SER ASP MET LYS ARG VAL LYS GLN LEU LEU ALA TYR LYS
SEQRES 6 3 66 LYS
SEQRES 1 4 37 MET LYS VAL ARG PRO SER VAL LYS PRO ILE CYS GLU LYS
SEQRES 2 4 37 CYS LYS VAL ILE LYS ARG LYS GLY LYS VAL MET VAL ILE
SEQRES 3 4 37 CYS GLU ASN PRO LYS HIS LYS GLN ARG GLN GLY
HET MN A 301 1
HET MG A 302 1
HET MG A 303 1
HET MG A 304 1
HET MN X3001 1
HET MG X3002 1
HET 62B X3003 35
HET MPD X3004 8
HET MPD X3005 8
HET MPD X3006 8
HET MPD X3007 8
HET MPD X3008 8
HET MPD X3009 8
HET MPD X3010 8
HET MPD X3011 8
HET MN X3012 1
HET MN X3013 1
HET MN X3014 1
HET MN X3015 1
HET MN X3016 1
HET MN X3017 1
HET MN X3018 1
HET MN X3019 1
HET MN X3020 1
HET MN X3021 1
HET MN X3022 1
HET MN X3023 1
HET MN X3024 1
HET MN X3025 1
HET MN X3026 1
HET MN X3027 1
HET MN X3028 1
HET MN X3029 1
HET MN X3030 1
HET MN X3031 1
HET MN X3032 1
HET MN X3033 1
HET MN X3034 1
HET MN X3035 1
HET MN X3036 1
HET MN X3037 1
HET MN X3038 1
HET MN X3039 1
HET MN X3040 1
HET MN X3041 1
HET MN X3042 1
HET MN X3043 1
HET MN X3044 1
HET MN X3045 1
HET MN X3046 1
HET MN X3047 1
HET MN X3048 1
HET MN X3049 1
HET MN X3050 1
HET MN X3051 1
HET MN X3052 1
HET MN X3053 1
HET MN X3054 1
HET MN X3055 1
HET MN X3056 1
HET MN X3057 1
HET MN X3058 1
HET MN X3059 1
HET MN X3060 1
HET MN X3061 1
HET MN X3062 1
HET MN X3063 1
HET MN X3064 1
HET MN X3065 1
HET MN X3066 1
HET MN X3067 1
HET MN X3068 1
HET MN X3069 1
HET MN X3070 1
HET MN X3071 1
HET MN X3072 1
HET MN X3073 1
HET MN X3074 1
HET MN X3075 1
HET MN X3076 1
HET MN X3077 1
HET MN X3078 1
HET MN X3079 1
HET MN X3080 1
HET MN X3081 1
HET MN X3082 1
HET MN X3083 1
HET MN X3084 1
HET MN X3085 1
HET MN X3086 1
HET MG X3087 1
HET MN X3088 1
HET MN X3089 1
HET MN X3090 1
HET MN X3091 1
HET MN X3092 1
HET MN X3093 1
HET MN X3094 1
HET MN X3095 1
HET MN X3096 1
HET MN X3097 1
HET MN X3098 1
HET MN X3099 1
HET MN X3100 1
HET MN X3101 1
HET MN X3102 1
HET MN X3103 1
HET MN X3104 1
HET MN X3105 1
HET MN X3106 1
HET MN X3107 1
HET MN X3108 1
HET MN X3109 1
HET MN X3110 1
HET MN X3111 1
HET MN X3112 1
HET MN X3113 1
HET MN X3114 1
HET MN X3115 1
HET MN X3116 1
HET MN X3117 1
HET MN X3118 1
HET MN X3119 1
HET MN X3120 1
HET MN X3121 1
HET MN X3122 1
HET MG X3123 1
HET MN X3124 1
HET MN X3125 1
HET MN X3126 1
HET MN X3127 1
HET MN X3128 1
HET MG X3129 1
HET MG X3130 1
HET MN X3131 1
HET MN X3132 1
HET MN X3133 1
HET MN X3134 1
HET MN X3135 1
HET MN X3136 1
HET MG X3137 1
HET MG X3138 1
HET MN X3139 1
HET MN X3140 1
HET MG X3141 1
HET MG X3142 1
HET MG X3143 1
HET MG X3144 1
HET MN X3145 1
HET MN X3146 1
HET MN X3147 1
HET MN X3148 1
HET MN X3149 1
HET MN X3150 1
HET MN X3151 1
HET MN X3152 1
HET MN X3153 1
HET MN X3154 1
HET MN X3155 1
HET MN X3156 1
HET MN X3157 1
HET MN X3158 1
HET MN X3159 1
HET MN X3160 1
HET MN X3161 1
HET MN X3162 1
HET MN X3163 1
HET MN X3164 1
HET MG X3165 1
HET MN X3166 1
HET MG X3167 1
HET MN X3168 1
HET MN X3169 1
HET MN X3170 1
HET MN X3171 1
HET MN X3172 1
HET MN X3173 1
HET MN X3174 1
HET MN X3175 1
HET MN X3176 1
HET MN X3177 1
HET MN X3178 1
HET MN X3179 1
HET MG X3180 1
HET MN X3181 1
HET MN X3182 1
HET MN X3183 1
HET MN X3184 1
HET MN X3185 1
HET MN X3186 1
HET MN X3187 1
HET MN X3188 1
HET MN X3189 1
HET MN X3190 1
HET MN X3191 1
HET MN X3192 1
HET MN X3193 1
HET MN X3194 1
HET MN X3195 1
HET MG X3196 1
HET MN X3197 1
HET MN X3198 1
HET MN X3199 1
HET MN X3200 1
HET MN X3201 1
HET MN X3202 1
HET MN X3203 1
HET MG X3204 1
HET MG X3205 1
HET MN X3206 1
HET MG X3207 1
HET MN X3208 1
HET MN X3209 1
HET MN X3210 1
HET MN X3211 1
HET MG X3212 1
HET MG X3213 1
HET MG X3214 1
HET MN X3215 1
HET MN X3216 1
HET MN X3217 1
HET MG X3218 1
HET MN X3219 1
HET MN X3220 1
HET MG X3221 1
HET MG X3222 1
HET MN X3223 1
HET MG X3224 1
HET MN X3225 1
HET MG X3226 1
HET MG X3227 1
HET MG X3228 1
HET MG X3229 1
HET MG X3230 1
HET MN X3231 1
HET MG X3232 1
HET MG X3233 1
HET MN X3234 1
HET MN X3235 1
HET MG X3236 1
HET MN X3237 1
HET MG X3238 1
HET MG X3239 1
HET MG X3240 1
HET MG X3241 1
HET MG X3242 1
HET MN X3243 1
HET MG X3244 1
HET MN X3245 1
HET MG X3246 1
HET MG X3247 1
HET MG X3248 1
HET MG X3249 1
HET MG X3250 1
HET MN X3251 1
HET MG X3252 1
HET MG X3253 1
HET MG X3254 1
HET MG X3255 1
HET MG X3256 1
HET MN X3257 1
HET MG X3258 1
HET MG X3259 1
HET MG X3260 1
HET MG X3261 1
HET MN X3262 1
HET MN X3263 1
HET MN X3264 1
HET MG X3265 1
HET MG X3266 1
HET MG X3267 1
HET MG X3268 1
HET MG X3269 1
HET MN X3270 1
HET MG X3271 1
HET MG X3272 1
HET MG X3273 1
HET MG X3274 1
HET MG X3275 1
HET MG X3276 1
HET MG X3277 1
HET MG X3278 1
HET MG X3279 1
HET MG X3280 1
HET MG X3281 1
HET MG X3282 1
HET MG X3283 1
HET MG X3284 1
HET MG X3285 1
HET MG X3286 1
HET MG X3287 1
HET MG X3288 1
HET MG X3289 1
HET MG X3290 1
HET MG X3291 1
HET MG X3292 1
HET MG X3293 1
HET MG X3294 1
HET MG X3295 1
HET MG X3296 1
HET MG X3297 1
HET MG X3298 1
HET MG X3299 1
HET MG X3300 1
HET MG X3301 1
HET MG X3302 1
HET MG X3303 1
HET MG X3304 1
HET MG X3305 1
HET MG X3306 1
HET MG X3307 1
HET MG X3308 1
HET MG X3309 1
HET MG X3310 1
HET MN X3311 1
HET MN X3312 1
HET MN X3313 1
HET MN X3314 1
HET MN X3315 1
HET MN X3316 1
HET MN X3317 1
HET MN X3318 1
HET MN X3319 1
HET MN X3320 1
HET MN X3321 1
HET MN X3322 1
HET MN X3323 1
HET MN X3324 1
HET MN X3325 1
HET MN X3326 1
HET MG X3327 1
HET MG X3328 1
HET MG X3329 1
HET MN X3330 1
HET MG X3331 1
HET MG X3332 1
HET MG X3333 1
HET MG X3334 1
HET MG X3335 1
HET MG X3336 1
HET MG X3337 1
HET MG X3338 1
HET MG X3339 1
HET MG X3340 1
HET MG X3341 1
HET MG X3342 1
HET MG X3343 1
HET MG X3344 1
HET MG X3345 1
HET MG X3346 1
HET MG X3347 1
HET MG X3348 1
HET MG X3349 1
HET MG X3350 1
HET MG X3351 1
HET MG X3352 1
HET MG X3353 1
HET MG X3354 1
HET MG X3355 1
HET MG X3356 1
HET MG X3357 1
HET MG X3358 1
HET MG X3359 1
HET MN X3360 1
HET MG X3361 1
HET MG X3362 1
HET MG X3363 1
HET MG X3364 1
HET MG X3365 1
HET MG X3366 1
HET MG X3367 1
HET MG X3368 1
HET MG X3369 1
HET MG X3370 1
HET MG X3371 1
HET MG X3372 1
HET MG X3373 1
HET MN X3374 1
HET MG X3375 1
HET MN X3376 1
HET MG X3377 1
HET MG X3378 1
HET MN X3379 1
HET MN X3380 1
HET MG X3381 1
HET MG X3382 1
HET MG X3383 1
HET MG X3384 1
HET MG X3385 1
HET MG X3386 1
HET MG X3387 1
HET MG X3388 1
HET MG X3389 1
HET MG X3390 1
HET MG X3391 1
HET MN X3392 1
HET MG X3393 1
HET MG X3394 1
HET MG X3395 1
HET MG X3396 1
HET MG X3397 1
HET MG X3398 1
HET MG X3399 1
HET MG X3400 1
HET MN X3401 1
HET MN X3402 1
HET MN X3403 1
HET MN X3404 1
HET MN X3405 1
HET MG X3406 1
HET MN X3407 1
HET MG X3408 1
HET MN X3409 1
HET MG X3410 1
HET MG X3411 1
HET MG X3412 1
HET MG X3413 1
HET MG X3414 1
HET MG X3415 1
HET MG X3416 1
HET MG X3417 1
HET MN X3418 1
HET MG X3419 1
HET MG X3420 1
HET MN X3421 1
HET MN X3422 1
HET MG X3423 1
HET MG X3424 1
HET MN X3425 1
HET MG X3426 1
HET MG X3427 1
HET MG X3428 1
HET MG X3429 1
HET MG X3430 1
HET MG X3431 1
HET MG X3432 1
HET MG X3433 1
HET MG X3434 1
HET MG X3435 1
HET MN X3436 1
HET MN X3437 1
HET MG X3438 1
HET MN X3439 1
HET MG X3440 1
HET MG X3441 1
HET MG X3442 1
HET MG X3443 1
HET MG X3444 1
HET MG X3445 1
HET MN X3446 1
HET MN X3447 1
HET MG X3448 1
HET MG X3449 1
HET MG X3450 1
HET MG X3451 1
HET MN X3452 1
HET MN X3453 1
HET MN X3454 1
HET MN X3455 1
HET MN X3456 1
HET MN X3457 1
HET MN X3458 1
HET MN X3459 1
HET MN X3460 1
HET MN X3461 1
HET MN X3462 1
HET MN X3463 1
HET MN X3464 1
HET MN X3465 1
HET MN X3466 1
HET MN X3467 1
HET MN X3468 1
HET MN X3469 1
HET MN X3470 1
HET MN X3471 1
HET MN X3472 1
HET MG X3473 1
HET MG X3474 1
HET MG X3475 1
HET MG X3476 1
HET MG X3477 1
HET MN X3478 1
HET MN X3479 1
HET MN X3480 1
HET MG X3481 1
HET MG X3482 1
HET MG X3483 1
HET MG X3484 1
HET MG X3485 1
HET MG X3486 1
HET MG X3487 1
HET MG X3488 1
HET MG X3489 1
HET MG X3490 1
HET MG X3491 1
HET SPD X3492 10
HET SPD X3493 10
HET SPD X3494 10
HET SPD X3495 10
HET SPD X3496 10
HET SPD X3497 10
HET SPD X3498 10
HET EOH X3499 3
HET EOH X3500 3
HET MG X3501 1
HET MN X3502 1
HET MN X3503 1
HET MG X3504 1
HET MG Y 201 1
HET MN Y 202 1
HET MG Y 203 1
HET MG Y 204 1
HET MG Y 205 1
HET MG Y 206 1
HET MG Y 207 1
HET MN Y 208 1
HET MG Y 209 1
HET MG Y 210 1
HET MG Y 211 1
HET MG Y 212 1
HET SPD Y 213 10
HET MG C 301 1
HET MG C 302 1
HET MG G 201 1
HET MG G 202 1
HET MG I 201 1
HET MPD J 201 8
HET MG J 202 1
HET MG M 201 1
HET EPE N 201 15
HET MG O 201 1
HET MG P 201 1
HET MPD Q 101 8
HET MN R 201 1
HET EOH S 301 3
HET MN T 101 1
HET MPD Z 101 8
HET MN Z 102 1
HETNAM MN MANGANESE (II) ION
HETNAM MG MAGNESIUM ION
HETNAM 62B LEFAMULIN
HETNAM MPD (4S)-2-METHYL-2,4-PENTANEDIOL
HETNAM SPD SPERMIDINE
HETNAM EOH ETHANOL
HETNAM EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID
HETSYN SPD N-(2-AMINO-PROPYL)-1,4-DIAMINOBUTANE; PA(34)
HETSYN EPE HEPES
FORMUL 29 MN 274(MN 2+)
FORMUL 30 MG 240(MG 2+)
FORMUL 35 62B C28 H45 N O5 S
FORMUL 36 MPD 11(C6 H14 O2)
FORMUL 24 SPD 8(C7 H19 N3)
FORMUL 31 EOH 3(C2 H6 O)
FORMUL 58 EPE C8 H18 N2 O4 S
HELIX 1 AA1 ASP A 20 THR A 25 5 6
HELIX 2 AA2 ASN A 197 VAL A 203 5 7
HELIX 3 AA3 GLY A 209 LYS A 214 1 6
HELIX 4 AA4 SER A 266 ILE A 270 5 5
HELIX 5 AA5 THR B 40 GLY B 45 1 6
HELIX 6 AA6 ASN B 70 LYS B 79 1 10
HELIX 7 AA7 SER B 106 PHE B 110 5 5
HELIX 8 AA8 GLY B 129 HIS B 134 1 6
HELIX 9 AA9 ASN C 29 ARG C 45 1 17
HELIX 10 AB1 PRO C 102 GLU C 120 1 19
HELIX 11 AB2 PRO C 134 PHE C 139 1 6
HELIX 12 AB3 GLN C 179 LEU C 184 1 6
HELIX 13 AB4 SER C 191 LYS C 200 1 10
HELIX 14 AB5 GLU D 6 PHE D 20 1 15
HELIX 15 AB6 GLN D 45 GLU D 58 1 14
HELIX 16 AB7 VAL D 89 GLU D 98 1 10
HELIX 17 AB8 ILE D 154 GLU D 164 1 11
HELIX 18 AB9 SER E 58 GLU E 60 5 3
HELIX 19 AC1 ASP E 61 SER E 80 1 20
HELIX 20 AC2 SER E 137 ARG E 149 1 13
HELIX 21 AC3 THR G 25 ARG G 38 1 14
HELIX 22 AC4 ALA G 60 ILE G 63 5 4
HELIX 23 AC5 GLY G 91 THR G 96 1 6
HELIX 24 AC6 PRO G 98 GLY G 108 1 11
HELIX 25 AC7 THR G 113 LYS G 121 1 9
HELIX 26 AC8 HIS G 133 GLN G 137 5 5
HELIX 27 AC9 ARG H 104 GLY H 109 1 6
HELIX 28 AD1 PHE H 111 ALA H 118 1 8
HELIX 29 AD2 LEU I 82 ASP I 87 5 6
HELIX 30 AD3 GLY I 115 HIS I 126 1 12
HELIX 31 AD4 SER J 44 MET J 58 1 15
HELIX 32 AD5 SER J 110 HIS J 123 1 14
HELIX 33 AD6 THR K 9 ILE K 26 1 18
HELIX 34 AD7 GLU K 34 GLY K 54 1 21
HELIX 35 AD8 ASP K 55 LEU K 66 1 12
HELIX 36 AD9 ALA K 81 GLY K 87 1 7
HELIX 37 AE1 GLY K 87 TYR K 93 1 7
HELIX 38 AE2 ASP L 6 ARG L 19 1 14
HELIX 39 AE3 LYS L 69 LYS L 82 1 14
HELIX 40 AE4 GLY L 97 ALA L 109 1 13
HELIX 41 AE5 LYS M 5 LYS M 12 1 8
HELIX 42 AE6 SER M 13 LEU M 15 5 3
HELIX 43 AE7 ILE M 66 VAL M 70 5 5
HELIX 44 AE8 THR N 8 LEU N 20 1 13
HELIX 45 AE9 PHE N 25 HIS N 29 5 5
HELIX 46 AF1 LEU N 31 GLN N 71 1 41
HELIX 47 AF2 SER N 75 GLY N 87 1 13
HELIX 48 AF3 LYS N 93 SER N 101 1 9
HELIX 49 AF4 ASP N 102 ASP N 115 1 14
HELIX 50 AF5 ALA P 13 ARG P 25 1 13
HELIX 51 AF6 ASN P 28 THR P 39 1 12
HELIX 52 AF7 ALA P 42 ASP P 63 1 22
HELIX 53 AF8 ALA P 89 GLY P 91 5 3
HELIX 54 AF9 THR Q 13 ALA Q 21 1 9
HELIX 55 AG1 ASN Q 34 ASN Q 47 1 14
HELIX 56 AG2 LEU S 18 SER S 24 1 7
HELIX 57 AG3 GLU S 45 GLY S 56 1 12
HELIX 58 AG4 SER V 12 THR V 34 1 23
HELIX 59 AG5 THR V 40 GLN V 64 1 25
HELIX 60 AG6 PRO W 16 LEU W 26 1 11
HELIX 61 AG7 ASN W 40 VAL W 50 1 11
HELIX 62 AG8 SER Z 9 ARG Z 17 1 9
HELIX 63 AG9 THR Z 18 PHE Z 20 5 3
HELIX 64 AH1 ASN 2 9 GLY 2 18 1 10
HELIX 65 AH2 GLY 2 18 SER 2 24 1 7
HELIX 66 AH3 THR 2 25 GLY 2 39 1 15
HELIX 67 AH4 LEU 3 49 ASP 3 54 1 6
HELIX 68 AH5 ASN 4 29 LYS 4 33 5 5
SHEET 1 AA1 3 ASP A 79 SER A 80 0
SHEET 2 AA1 3 ILE A 91 VAL A 95 -1 O LEU A 93 N SER A 80
SHEET 3 AA1 3 LYS A 101 ILE A 105 -1 O ARG A 102 N VAL A 94
SHEET 1 AA2 2 LEU A 130 PRO A 131 0
SHEET 2 AA2 2 ARG A 189 ALA A 190 -1 O ALA A 190 N LEU A 130
SHEET 1 AA3 3 ALA A 162 GLN A 163 0
SHEET 2 AA3 3 TYR A 171 LEU A 176 -1 O ARG A 175 N GLN A 163
SHEET 3 AA3 3 VAL A 181 LEU A 185 -1 O ARG A 182 N ILE A 174
SHEET 1 AA4 2 MET A 247 SER A 248 0
SHEET 2 AA4 2 GLY A 251 PRO A 253 -1 O LYS A 252 N SER A 248
SHEET 1 AA5 7 GLY B 4 PHE B 16 0
SHEET 2 AA5 7 LEU B 22 GLU B 29 -1 O VAL B 27 N GLY B 11
SHEET 3 AA5 7 VAL B 194 LYS B 198 -1 O VAL B 197 N THR B 26
SHEET 4 AA5 7 THR B 177 ASP B 189 -1 N GLU B 184 O LYS B 198
SHEET 5 AA5 7 VAL B 115 VAL B 121 -1 N ILE B 116 O LEU B 183
SHEET 6 AA5 7 LEU B 208 THR B 213 -1 O ARG B 212 N ASP B 117
SHEET 7 AA5 7 GLY B 4 PHE B 16 -1 N GLY B 7 O VAL B 209
SHEET 1 AA6 3 VAL B 34 LYS B 39 0
SHEET 2 AA6 3 ALA B 48 GLY B 52 -1 O GLN B 50 N LEU B 36
SHEET 3 AA6 3 ILE B 88 PHE B 91 -1 O PHE B 91 N ILE B 49
SHEET 1 AA7 2 PHE B 127 GLN B 128 0
SHEET 2 AA7 2 GLY B 171 ARG B 172 -1 O GLY B 171 N GLN B 128
SHEET 1 AA8 2 TYR C 4 ASP C 5 0
SHEET 2 AA8 2 ILE C 17 GLU C 18 -1 O ILE C 17 N ASP C 5
SHEET 1 AA9 2 GLN C 148 PRO C 149 0
SHEET 2 AA9 2 ARG C 168 ASN C 169 1 O ASN C 169 N GLN C 148
SHEET 1 AB1 3 MET D 83 ALA D 87 0
SHEET 2 AB1 3 ILE D 31 MET D 38 -1 N ILE D 34 O ALA D 87
SHEET 3 AB1 3 VAL D 146 ARG D 150 -1 O VAL D 149 N LYS D 33
SHEET 1 AB2 3 VAL E 130 LYS E 132 0
SHEET 2 AB2 3 VAL E 86 LEU E 89 -1 N LEU E 87 O VAL E 131
SHEET 3 AB2 3 ILE E 162 TYR E 164 -1 O ARG E 163 N GLU E 88
SHEET 1 AB3 4 LEU G 123 TYR G 126 0
SHEET 2 AB3 4 TYR G 54 ILE G 58 1 N VAL G 57 O TYR G 126
SHEET 3 AB3 4 TRP G 16 ASP G 20 1 N ILE G 19 O ILE G 58
SHEET 4 AB3 4 GLU G 139 ASN G 140 1 O GLU G 139 N TRP G 16
SHEET 1 AB4 6 ARG H 7 VAL H 10 0
SHEET 2 AB4 6 ALA H 16 LYS H 23 -1 O ARG H 17 N VAL H 10
SHEET 3 AB4 6 VAL H 38 ALA H 46 -1 O VAL H 40 N ILE H 22
SHEET 4 AB4 6 VAL H 57 ILE H 62 -1 O ALA H 60 N ILE H 39
SHEET 5 AB4 6 ALA H 83 ILE H 86 -1 O VAL H 85 N VAL H 61
SHEET 6 AB4 6 ARG H 7 VAL H 10 1 N LYS H 9 O CYS H 84
SHEET 1 AB5 6 TYR H 76 PHE H 79 0
SHEET 2 AB5 6 VAL M 72 PHE M 76 -1 O GLU M 73 N LYS H 78
SHEET 3 AB5 6 THR M 60 LYS M 65 -1 N VAL M 63 O ARG M 74
SHEET 4 AB5 6 GLU M 40 ARG M 53 -1 N ILE M 50 O THR M 62
SHEET 5 AB5 6 THR M 27 ILE M 35 -1 N VAL M 32 O GLN M 43
SHEET 6 AB5 6 ILE M 83 ARG M 90 -1 O GLU M 87 N ARG M 29
SHEET 1 AB6 2 THR I 67 ASN I 70 0
SHEET 2 AB6 2 LEU I 95 GLU I 98 1 O LEU I 96 N ILE I 69
SHEET 1 AB7 4 LYS J 63 ILE J 66 0
SHEET 2 AB7 4 ILE J 102 ALA J 107 -1 O GLU J 105 N TRP J 65
SHEET 3 AB7 4 PHE J 32 ALA J 36 -1 N LEU J 34 O PHE J 104
SHEET 4 AB7 4 THR J 129 VAL J 132 -1 O LYS J 130 N GLN J 35
SHEET 1 AB8 3 SER J 40 THR J 43 0
SHEET 2 AB8 3 VAL J 90 VAL J 97 -1 O ALA J 95 N ILE J 42
SHEET 3 AB8 3 THR J 72 THR J 75 -1 N TYR J 74 O GLU J 91
SHEET 1 AB9 3 ARG K 29 THR K 33 0
SHEET 2 AB9 3 GLU K 115 GLU K 120 -1 O VAL K 117 N THR K 32
SHEET 3 AB9 3 ARG K 102 PRO K 108 -1 N LEU K 104 O ILE K 118
SHEET 1 AC1 2 LEU K 72 ASN K 73 0
SHEET 2 AC1 2 THR K 78 GLN K 79 -1 O GLN K 79 N LEU K 72
SHEET 1 AC2 2 ARG L 30 TYR L 34 0
SHEET 2 AC2 2 TYR L 41 ILE L 45 -1 O TYR L 41 N TYR L 34
SHEET 1 AC3 4 GLN O 11 VAL O 14 0
SHEET 2 AC3 4 ALA O 3 GLU O 6 -1 N ALA O 3 O VAL O 14
SHEET 3 AC3 4 VAL O 38 VAL O 41 -1 O LEU O 39 N ILE O 4
SHEET 4 AC3 4 LYS O 47 VAL O 48 -1 O LYS O 47 N VAL O 41
SHEET 1 AC4 4 GLU O 19 GLU O 23 0
SHEET 2 AC4 4 TYR O 92 ILE O 100 -1 O LEU O 95 N ILE O 20
SHEET 3 AC4 4 VAL O 58 LYS O 64 -1 N THR O 59 O ASP O 98
SHEET 4 AC4 4 THR O 32 PHE O 35 -1 N PHE O 33 O ALA O 60
SHEET 1 AC5 2 ILE O 71 LYS O 77 0
SHEET 2 AC5 2 SER O 82 HIS O 88 -1 O LYS O 86 N VAL O 73
SHEET 1 AC6 3 LYS P 4 ALA P 7 0
SHEET 2 AC6 3 SER P 101 VAL P 106 -1 O ILE P 105 N ALA P 5
SHEET 3 AC6 3 GLU P 73 GLU P 78 -1 N GLU P 73 O VAL P 106
SHEET 1 AC7 2 LEU P 82 PRO P 87 0
SHEET 2 AC7 2 ALA P 93 LYS P 98 -1 O ILE P 96 N ARG P 84
SHEET 1 AC8 4 LEU Q 7 PRO Q 10 0
SHEET 2 AC8 4 LYS Q 24 VAL Q 29 -1 O ASP Q 28 N ARG Q 9
SHEET 3 AC8 4 ALA Q 78 THR Q 81 -1 O VAL Q 80 N TYR Q 25
SHEET 4 AC8 4 SER Q 52 ILE Q 55 -1 N SER Q 52 O THR Q 81
SHEET 1 AC9 2 LYS Q 62 LYS Q 63 0
SHEET 2 AC9 2 GLY Q 70 TYR Q 71 -1 O GLY Q 70 N LYS Q 63
SHEET 1 AD1 4 ASN R 8 LYS R 10 0
SHEET 2 AD1 4 GLU R 20 ILE R 24 -1 O GLY R 21 N VAL R 9
SHEET 3 AD1 4 ARG R 32 VAL R 35 -1 O VAL R 34 N ILE R 24
SHEET 4 AD1 4 ILE R 63 HIS R 64 -1 O ILE R 63 N VAL R 33
SHEET 1 AD2 2 ASN R 39 ILE R 40 0
SHEET 2 AD2 2 THR R 59 GLU R 60 -1 O THR R 59 N ILE R 40
SHEET 1 AD3 5 ILE S 8 ARG S 9 0
SHEET 2 AD3 5 VAL S 39 ASP S 44 -1 O LYS S 42 N ILE S 8
SHEET 3 AD3 5 LYS S 26 GLY S 33 -1 N ALA S 29 O VAL S 41
SHEET 4 AD3 5 GLN S 85 ALA S 93 1 O PHE S 91 N VAL S 30
SHEET 5 AD3 5 ASP S 76 ASP S 80 -1 N ASP S 80 O GLN S 85
SHEET 1 AD4 2 ILE S 61 GLY S 64 0
SHEET 2 AD4 2 THR S 69 VAL S 72 -1 O VAL S 72 N ILE S 61
SHEET 1 AD5 2 GLU S 99 GLU S 103 0
SHEET 2 AD5 2 LEU S 125 GLU S 129 -1 O LEU S 125 N GLU S 103
SHEET 1 AD6 4 GLY T 30 ALA T 31 0
SHEET 2 AD6 4 ILE T 44 ARG T 47 -1 O ARG T 47 N GLY T 30
SHEET 3 AD6 4 LEU T 67 ALA T 69 -1 O LEU T 67 N LEU T 45
SHEET 4 AD6 4 VAL T 59 ARG T 61 -1 N GLY T 60 O PHE T 68
SHEET 1 AD7 4 PHE T 38 VAL T 39 0
SHEET 2 AD7 4 GLY T 73 ARG T 79 -1 O GLY T 73 N VAL T 39
SHEET 3 AD7 4 LYS T 85 TYR T 90 -1 O GLN T 86 N GLU T 78
SHEET 4 AD7 4 TYR T 54 PRO T 55 1 N TYR T 54 O LYS T 85
SHEET 1 AD8 2 LYS U 35 ILE U 38 0
SHEET 2 AD8 2 VAL U 47 SER U 50 -1 O VAL U 47 N ILE U 38
SHEET 1 AD9 3 SER W 34 GLU W 38 0
SHEET 2 AD9 3 LYS W 3 LEU W 8 -1 N LEU W 4 O VAL W 37
SHEET 3 AD9 3 VAL W 54 THR W 55 -1 O THR W 55 N THR W 7
SHEET 1 AE1 2 MET Z 27 GLU Z 29 0
SHEET 2 AE1 2 GLU Z 36 LYS Z 38 -1 O TYR Z 37 N THR Z 28
SHEET 1 AE2 2 ARG 3 13 LYS 3 15 0
SHEET 2 AE2 2 GLY 3 20 LEU 3 22 -1 O GLN 3 21 N VAL 3 14
SHEET 1 AE3 3 LYS 4 15 LYS 4 18 0
SHEET 2 AE3 3 VAL 4 23 ILE 4 26 -1 O MET 4 24 N ILE 4 17
SHEET 3 AE3 3 GLN 4 34 ARG 4 35 -1 O GLN 4 34 N VAL 4 25
SSBOND 1 CYS 4 11 CYS 4 27 1555 1555 2.03
LINK O2' A X 13 MG MG X3345 1555 1555 2.72
LINK OP2 A X 14 MN MN X3098 1555 1555 2.19
LINK OP2 G X 15 MN MN X3098 1555 1555 2.19
LINK O6 G X 16 MG MG X3345 1555 1555 2.96
LINK OP1 C X 20 MG MG X3284 1555 1555 2.56
LINK OP1 C X 31 MN MN X3122 1555 1555 2.29
LINK OP2 A X 91 MG MG X3259 1555 1555 2.57
LINK OP2 U X 119 MN MN X3194 1555 1555 2.51
LINK OP1 U X 119 MN MN X3195 1555 1555 2.12
LINK OP2 A X 126 MG MG X3331 1555 1555 3.00
LINK OP1 A X 130 MG MG X3273 1555 1555 2.66
LINK OP2 A X 130 MG MG X3273 1555 1555 2.07
LINK O4 U X 159 MN MN X3210 1555 1555 2.33
LINK OP1 G X 177 MN MN X3181 1555 1555 2.44
LINK OP1 C X 195 MN MN X3127 1555 1555 2.10
LINK N7 A X 198 MN MN X3080 1555 1555 2.29
LINK OP1 A X 200 MN MN X3080 1555 1555 2.09
LINK OP2 C X 201 MN MN X3080 1555 1555 2.18
LINK OP2 G X 208 MN MN X3111 1555 1555 2.19
LINK OP2 G X 221 MN MN X3119 1555 1555 2.55
LINK OP1 C X 252 MN MN X3024 1555 1555 2.53
LINK OP2 G X 300 MG MG X3382 1555 1555 2.81
LINK OP1 C X 323 MG MG X3299 1555 1555 1.91
LINK OP2 A X 324 MG MG X3299 1555 1555 2.88
LINK OP2 A X 326 MG MG X3299 1555 1555 2.00
LINK N7 G X 341 MN MN X3110 1555 1555 2.50
LINK OP1 A X 354 MN MN X3172 1555 1555 2.78
LINK OP2 U X 374 MN MN X3436 1555 1555 2.45
LINK OP2 A X 383 MN MN X3059 1555 1555 2.67
LINK O6 G X 410 MG MG X3387 1555 1555 2.64
LINK O6 G X 416 MN MN X3189 1555 1555 2.18
LINK OP1 G X 422 MN MN X3235 1555 1555 2.17
LINK OP1 U X 438 MN MN X3234 1555 1555 2.18
LINK OP1 A X 455 MN MN X3234 1555 1555 2.10
LINK OP1 G X 457 MN MN X3200 1555 1555 2.07
LINK OP2 A X 468 MN MN X3189 1555 1555 1.75
LINK OP1 A X 476 MG MG X3309 1555 1555 2.98
LINK OP2 A X 476 MG MG X3309 1555 1555 2.86
LINK O4 U X 477 MG MG X3309 1555 1555 2.33
LINK OP2 G X 492 MN MN X3121 1555 1555 2.19
LINK O6 G X 496 MN MN X3104 1555 1555 1.86
LINK OP2 G X 498 MN MN X3103 1555 1555 2.73
LINK OP1 A X 499 MN MN X3104 1555 1555 2.39
LINK O6 G X 511 MG MG X3395 1555 1555 2.43
LINK N7 G X 545 MN MN X3125 1555 1555 2.67
LINK OP1 C X 555 MN MN X3118 1555 1555 2.11
LINK OP2 U X 556 MN MN X3118 1555 1555 2.01
LINK N7 G X 557 MN MN X3118 1555 1555 2.53
LINK OP1 G X 563 MG MG X3504 1555 1555 2.45
LINK O4 U X 566 MG MG X3365 1555 1555 2.97
LINK OP1 A X 571 MN MN X3055 1555 1555 2.38
LINK OP1 C X 572 MN MN X3055 1555 1555 2.53
LINK OP2 G X 598 MN MN X3405 1555 1555 2.39
LINK OP2 A X 599 MG MG X3442 1555 1555 1.87
LINK O6 G X 601 MG MG X3329 1555 1555 2.98
LINK OP1 U X 610 MN MN X3083 1555 1555 2.24
LINK O6 G X 613 MN MN X3015 1555 1555 2.08
LINK OP1 A X 618 MG MG X3390 1555 1555 2.51
LINK OP1 U X 619 MN MN X3126 1555 1555 2.20
LINK OP2 A X 621 MN MN X3032 1555 1555 2.54
LINK O4 U X 642 MG MG X3356 1555 1555 2.85
LINK O6 G X 643 MG MG X3356 1555 1555 2.85
LINK OP2 C X 716 MN MN X3330 1555 1555 2.33
LINK OP2 A X 725 MG MG X3297 1555 1555 2.73
LINK OP2 U X 731 MG MG X3366 1555 1555 2.50
LINK OP2 A X 744 MG MG X3226 1555 1555 2.75
LINK OP2 A X 775 MN MN X3270 1555 1555 2.13
LINK OP2 C X 776 MN MN X3270 1555 1555 2.45
LINK OP1 G X 778 MG MG X3227 1555 1555 2.14
LINK N7 G X 778 MN MN X3407 1555 1555 2.40
LINK OP1 C X 782 MN MN X3220 1555 1555 2.78
LINK OP1 A X 784 MG MG X3267 1555 1555 1.85
LINK OP2 C X 785 MN MN X3215 1555 1555 2.22
LINK OP1 U X 786 MG MG X3218 1555 1555 2.77
LINK O4 U X 791 MG MG X3415 1555 1555 2.56
LINK OP1 A X 794 MG MG X3481 1555 1555 2.45
LINK OP1 A X 796 MN MN X3152 1555 1555 2.30
LINK O4 U X 799 MG MG X3340 1555 1555 2.88
LINK OP1 G X 805 MG MG X3271 1555 1555 2.33
LINK OP1 A X 806 MN MN X3270 1555 1555 2.68
LINK N7 A X 806 MN MN X3407 1555 1555 2.43
LINK OP2 A X 828 MN MN X3050 1555 1555 2.28
LINK OP1 U X 829 MN MN X3049 1555 1555 2.13
LINK OP2 U X 829 MN MN X3050 1555 1555 2.37
LINK OP2 U X 830 MN MN X3403 1555 1555 2.10
LINK OP1 C X 832 MN MN X3217 1555 1555 1.88
LINK OP2 U X 835 MN MN X3217 1555 1555 2.09
LINK OP1 A X 839 MN MN X3082 1555 1555 2.28
LINK OP1 A X 845 MN MN X3056 1555 1555 2.00
LINK OP1 A X 847 MN MN X3066 1555 1555 2.45
LINK OP2 G X 863 MN MN X3107 1555 1555 2.29
LINK OP1 C X 870 MN MN X3404 1555 1555 2.43
LINK OP1 U X 871 MN MN X3022 1555 1555 2.08
LINK OP1 U X 872 MN MN X3023 1555 1555 2.25
LINK OP2 G X 893 MN MN X3089 1555 1555 2.69
LINK OP2 G X 907 MN MN X3021 1555 1555 2.20
LINK OP2 A X 952 MN MN X3171 1555 1555 2.78
LINK O4 U X 958 MG MG X3420 1555 1555 2.86
LINK O3' C X 960 MG MG X3373 1555 1555 2.83
LINK OP1 G X 961 MG MG X3373 1555 1555 2.94
LINK OP2 A X 972 MG MG X3428 1555 1555 2.48
LINK OP2 U X 987 MN MN X3503 1555 1555 2.16
LINK OP2 A X 989 MN MN X3206 1555 1555 2.39
LINK OP2 G X 990 MN MN X3206 1555 1555 1.89
LINK OP1 G X 990 MG MG X3275 1555 1555 2.45
LINK OP1 A X 992 MN MN X3018 1555 1555 2.26
LINK OP1 G X1006 MN MN X3018 1555 1555 2.11
LINK OP1 U X1007 MN MN X3017 1555 1555 2.40
LINK OP2 U X1007 MN MN X3018 1555 1555 2.08
LINK O4 U X1011 MG MG X3268 1555 1555 1.93
LINK OP2 A X1019 MN MN X3060 1555 1555 2.33
LINK OP1 A X1019 MN MN X3061 1555 1555 2.23
LINK OP1 A X1025 MN MN X3086 1555 1555 2.30
LINK OP2 A X1034 MN MN X3042 1555 1555 2.34
LINK OP1 A X1034 MG MG X3353 1555 1555 1.78
LINK OP2 C X1035 MN MN X3042 1555 1555 2.35
LINK OP2 U X1043 MN MN X3156 1555 1555 2.29
LINK OP2 A X1045 MN MN X3149 1555 1555 2.75
LINK OP1 A X1052 MN MN X3116 1555 1555 2.29
LINK OP2 A X1053 MN MN X3095 1555 1555 2.34
LINK OP2 A X1054 MN MN X3095 1555 1555 2.56
LINK OP2 U X1067 MN MN X3201 1555 1555 2.34
LINK OP2 G X1068 MN MN X3201 1555 1555 2.04
LINK O2' G X1069 MN MN X3201 1555 1555 2.40
LINK O3' G X1069 MG MG X3438 1555 1555 2.75
LINK OP1 A X1070 MN MN X3201 1555 1555 2.41
LINK OP2 A X1072 MG MG X3363 1555 1555 2.95
LINK O6 G X1080 MG MG X3272 1555 1555 2.79
LINK O6 G X1081 MG MG X3396 1555 1555 2.68
LINK OP2 U X1085 MG MG X3269 1555 1555 2.30
LINK OP2 A X1173 MG MG X3491 1555 1555 2.14
LINK O5' C X1179 MG MG X3438 1555 1555 2.84
LINK OP1 G X1181 MN MN X3401 1555 1555 2.55
LINK OP2 C X1197 MN MN X3156 1555 1555 2.25
LINK OP2 A X1200 MN MN X3040 1555 1555 2.28
LINK OP1 G X1201 MN MN X3041 1555 1555 2.19
LINK OP2 C X1202 MN MN X3041 1555 1555 2.19
LINK OP1 C X1202 MG MG X3353 1555 1555 2.75
LINK OP2 G X1225 MN MN X3042 1555 1555 1.81
LINK O6 G X1226 MN MN X3107 1555 1555 2.52
LINK OP2 G X1226 MN MN X3409 1555 1555 2.14
LINK OP2 A X1228 MN MN X3136 1555 1555 2.08
LINK N7 G X1229 MN MN X3136 1555 1555 2.29
LINK OP2 A X1231 MN MN X3502 1555 1555 2.36
LINK OP1 U X1237 MG MG X3364 1555 1555 2.21
LINK OP1 G X1257 MG MG X3284 1555 1555 2.67
LINK O6 G X1271 MG MG X3123 1555 1555 2.97
LINK O4 U X1272 MG MG X3123 1555 1555 2.83
LINK OP2 U X1272 MG MG X3341 1555 1555 2.91
LINK OP1 A X1275 MN MN X3313 1555 1555 2.62
LINK OP2 A X1275 MG MG X3332 1555 1555 2.71
LINK O6 G X1278 MG MG X3334 1555 1555 2.75
LINK OP1 U X1287 MN MN X3063 1555 1555 2.55
LINK OP1 G X1288 MN MN X3063 1555 1555 2.10
LINK O2' U X1293 MG MG X3432 1555 1555 2.78
LINK OP2 A X1303 MN MN X3035 1555 1555 2.21
LINK OP1 U X1305 MN MN X3038 1555 1555 2.42
LINK OP2 G X1309 MN MN X3219 1555 1555 2.25
LINK OP1 A X1310 MN MN X3219 1555 1555 2.50
LINK OP2 A X1311 MG MG X3291 1555 1555 2.95
LINK OP2 C X1335 MN MN X3257 1555 1555 2.20
LINK OP2 C X1364 MN MN X3039 1555 1555 2.17
LINK OP2 A X1379 MG MG X3295 1555 1555 2.27
LINK OP1 A X1396 MN MN X3197 1555 1555 2.51
LINK OP2 G X1397 MN MN X3197 1555 1555 2.32
LINK OP2 G X1414 MN MN X3464 1555 1555 2.32
LINK OP2 U X1416 MN MN X3188 1555 1555 2.73
LINK OP2 G X1417 MN MN X3188 1555 1555 2.60
LINK O4 U X1420 MG MG X3244 1555 1555 2.40
LINK OP1 U X1431 MN MN X3170 1555 1555 2.23
LINK OP1 A X1432 MN MN X3169 1555 1555 2.43
LINK OP1 C X1472 MN MN X3380 1555 1555 2.63
LINK OP2 U X1499 MN MN X3264 1555 1555 2.46
LINK OP2 G X1500 MN MN X3264 1555 1555 2.41
LINK O5' A X1521 MN MN X3237 1555 1555 2.45
LINK OP1 G X1613 MG MG X3002 1555 1555 2.94
LINK O4 U X1646 MG MG X3295 1555 1555 1.90
LINK OP1 A X1647 MN MN X3169 1555 1555 2.31
LINK OP2 C X1648 MN MN X3169 1555 1555 2.00
LINK OP1 C X1648 MN MN X3170 1555 1555 2.24
LINK OP2 G X1650 MG MG X3261 1555 1555 2.43
LINK O2 C X1651 MG MG X3221 1555 1555 2.80
LINK OP1 C X1655 MG MG X3141 1555 1555 2.40
LINK OP1 A X1658 MN MN X3152 1555 1555 1.86
LINK OP2 G X1664 MG MG X3221 1555 1555 2.96
LINK OP1 U X1665 MN MN X3220 1555 1555 2.41
LINK OP1 A X1666 MN MN X3220 1555 1555 2.01
LINK OP2 U X1680 MN MN X3106 1555 1555 2.63
LINK OP2 U X1683 MN MN X3257 1555 1555 2.24
LINK OP1 U X1683 MG MG X3258 1555 1555 2.35
LINK OP2 A X1685 MN MN X3093 1555 1555 2.04
LINK N7 G X1686 MN MN X3093 1555 1555 2.20
LINK OP1 G X1691 MN MN X3219 1555 1555 2.43
LINK OP2 G X1691 MG MG X3482 1555 1555 2.29
LINK OP1 C X1692 MN MN X3219 1555 1555 2.10
LINK OP1 G X1693 MG MG X3483 1555 1555 2.83
LINK OP1 C X1702 MN MN X3053 1555 1555 1.92
LINK OP1 U X1706 MN MN X3312 1555 1555 2.42
LINK OP2 A X1708 MN MN X3099 1555 1555 2.24
LINK OP1 A X1708 MN MN X3100 1555 1555 2.68
LINK OP2 A X1709 MN MN X3100 1555 1555 2.31
LINK OP2 A X1713 MN MN X3075 1555 1555 2.39
LINK OP2 C X1714 MN MN X3075 1555 1555 2.27
LINK OP1 C X1714 MN MN X3076 1555 1555 2.22
LINK O4 U X1715 MN MN X3075 1555 1555 2.07
LINK OP2 U X1715 MN MN X3076 1555 1555 2.29
LINK OP2 A X1720 MN MN X3062 1555 1555 2.26
LINK OP2 A X1745 MG MG X3292 1555 1555 2.33
LINK O6 G X1746 MG MG X3292 1555 1555 2.01
LINK OP1 G X1797 MG MG X3350 1555 1555 2.79
LINK OP1 C X1801 MN MN X3097 1555 1555 2.16
LINK OP2 G X1803 MN MN X3065 1555 1555 1.99
LINK OP1 A X1807 MN MN X3216 1555 1555 2.00
LINK OP1 C X1809 MN MN X3216 1555 1555 2.42
LINK OP1 A X1810 MN MN X3215 1555 1555 2.15
LINK OP2 A X1810 MN MN X3216 1555 1555 2.19
LINK OP2 A X1811 MN MN X3215 1555 1555 2.64
LINK OP1 A X1836 MG MG X3304 1555 1555 2.04
LINK OP2 U X1840 MG MG X3391 1555 1555 2.56
LINK OP1 G X1855 MN MN X3164 1555 1555 1.82
LINK OP2 G X1855 MG MG X3165 1555 1555 1.82
LINK O6 G X1884 MN MN X3325 1555 1555 2.34
LINK O6 G X1918 MN MN X3263 1555 1555 2.51
LINK OP1 G X1995 MG MG X3277 1555 1555 2.53
LINK OP1 A X1997 MN MN X3176 1555 1555 2.39
LINK OP2 A X1997 MN MN X3177 1555 1555 2.04
LINK OP1 G X2012 MN MN X3133 1555 1555 2.43
LINK OP1 U X2022 MN MN X3168 1555 1555 2.37
LINK N7 G X2029 MN MN X3392 1555 1555 2.37
LINK OP1 A X2032 MN MN X3036 1555 1555 2.36
LINK OP1 C X2033 MN MN X3034 1555 1555 2.11
LINK OP2 A X2041 MG MG X3476 1555 1555 2.88
LINK OP2 A X2042 MG MG X3335 1555 1555 2.58
LINK OP1 U X2043 MN MN X3043 1555 1555 2.58
LINK OP2 G X2056 MN MN X3033 1555 1555 2.19
LINK O2' A X2057 MG MG X3390 1555 1555 2.95
LINK N7 G X2059 MN MN X3028 1555 1555 2.48
LINK OP1 A X2069 MN MN X3051 1555 1555 2.35
LINK OP2 G X2083 MN MN X3085 1555 1555 2.29
LINK OP2 G X2084 MN MN X3085 1555 1555 2.52
LINK OP2 G X2088 MN MN X3013 1555 1555 2.30
LINK OP1 A X2089 MN MN X3012 1555 1555 2.57
LINK OP1 U X2101 MN MN X3067 1555 1555 2.25
LINK OP2 G X2110 MG MG X3281 1555 1555 2.62
LINK O4 U X2116 MG MG X3450 1555 1555 2.60
LINK O6 G X2230 MG MG X3349 1555 1555 2.52
LINK OP1 U X2270 MN MN X3127 1555 1555 2.40
LINK OP2 U X2271 MN MN X3323 1555 1555 2.70
LINK OP2 C X2275 MN MN X3092 1555 1555 2.23
LINK O4 U X2276 MN MN X3092 1555 1555 2.44
LINK OP1 G X2278 MN MN X3185 1555 1555 2.75
LINK OP2 G X2282 MG MG X3278 1555 1555 2.68
LINK OP1 A X2295 MN MN X3161 1555 1555 2.29
LINK OP1 A X2296 MN MN X3161 1555 1555 2.43
LINK OP2 G X2297 MN MN X3160 1555 1555 2.05
LINK OP2 A X2301 MN MN X3193 1555 1555 2.48
LINK OP2 A X2355 MN MN X3326 1555 1555 2.25
LINK O6 G X2358 MG MG X3328 1555 1555 2.97
LINK OP2 A X2379 MN MN X3179 1555 1555 2.76
LINK N7 G X2380 MN MN X3179 1555 1555 2.61
LINK OP2 A X2403 MG MG X3377 1555 1555 2.94
LINK N7 G X2410 MN MN X3191 1555 1555 2.60
LINK OP2 A X2411 MN MN X3190 1555 1555 2.03
LINK OP1 C X2412 MN MN X3192 1555 1555 2.37
LINK O2 C X2421 MG MG X3333 1555 1555 2.87
LINK O6 G X2427 MG MG X3293 1555 1555 2.99
LINK OP2 C X2433 MN MN X3199 1555 1555 2.17
LINK OP1 A X2434 MN MN X3200 1555 1555 2.29
LINK OP1 C X2454 MN MN X3022 1555 1555 2.01
LINK OP1 G X2455 MN MN X3022 1555 1555 2.48
LINK OP1 G X2456 MN MN X3022 1555 1555 2.14
LINK OP2 G X2456 MN MN X3023 1555 1555 2.39
LINK OP2 A X2457 MN MN X3023 1555 1555 2.03
LINK OP2 A X2459 MG MG X3429 1555 1555 2.81
LINK OP2 A X2460 MG MG X3429 1555 1555 2.92
LINK OP1 A X2475 MN MN X3015 1555 1555 1.92
LINK OP2 A X2475 MN MN X3016 1555 1555 2.30
LINK OP1 C X2479 MN MN X3311 1555 1555 1.99
LINK OP1 A X2480 MG MG X3285 1555 1555 2.95
LINK OP2 C X2494 MN MN X3469 1555 1555 2.72
LINK OP2 G X2513 MG MG X3204 1555 1555 2.16
LINK O6 G X2517 MN MN X3315 1555 1555 2.13
LINK OP2 U X2518 MN MN X3472 1555 1555 2.34
LINK OP1 U X2519 MG MG X3285 1555 1555 2.93
LINK OP2 C X2525 MN MN X3016 1555 1555 2.30
LINK OP1 C X2526 MN MN X3015 1555 1555 2.05
LINK OP2 C X2526 MN MN X3016 1555 1555 2.48
LINK OP2 G X2529 MN MN X3013 1555 1555 2.13
LINK N7 G X2529 MN MN X3014 1555 1555 2.37
LINK OP1 A X2530 MN MN X3126 1555 1555 2.03
LINK O2' C X2539 MG MG X3501 1555 1555 2.91
LINK OP2 A X2545 MN MN X3108 1555 1555 2.10
LINK OP1 U X2549 MG MG X3490 1555 1555 2.18
LINK OP1 G X2563 MG MG X3444 1555 1555 2.78
LINK OP1 C X2566 MG MG X3485 1555 1555 2.90
LINK OP1 G X2571 MG MG X3361 1555 1555 2.64
LINK OP1 G X2577 MN MN X3075 1555 1555 2.01
LINK O6 G X2596 MG MG X3144 1555 1555 2.60
LINK OP1 C X2600 MN MN X3145 1555 1555 2.13
LINK OP1 G X2601 MN MN X3145 1555 1555 2.24
LINK OP2 C X2602 MN MN X3145 1555 1555 2.22
LINK OP1 G X2603 MN MN X3057 1555 1555 2.39
LINK OP1 A X2604 MN MN X3057 1555 1555 2.06
LINK OP2 G X2609 MN MN X3132 1555 1555 2.08
LINK OP2 G X2610 MN MN X3132 1555 1555 2.06
LINK OP1 C X2613 MN MN X3131 1555 1555 2.39
LINK OP2 G X2615 MN MN X3048 1555 1555 2.25
LINK OP1 G X2615 MN MN X3049 1555 1555 2.17
LINK OP1 A X2616 MN MN X3050 1555 1555 2.32
LINK OP1 G X2619 MG MG X3277 1555 1555 2.10
LINK OP1 A X2625 MN MN X3001 1555 1555 2.23
LINK OP1 C X2628 MG MG X3265 1555 1555 2.95
LINK OP2 A X2629 MN MN X3223 1555 1555 2.50
LINK OP2 G X2630 MN MN X3223 1555 1555 2.38
LINK OP1 G X2634 MG MG X3416 1555 1555 2.74
LINK OP1 U X2642 MN MN X3035 1555 1555 2.44
LINK OP1 C X2644 MG MG X3338 1555 1555 2.82
LINK OP2 A X2666 MN MN X3079 1555 1555 2.14
LINK N7 G X2667 MN MN X3079 1555 1555 2.51
LINK O6 G X2686 MN MN X3321 1555 1555 2.44
LINK OP2 U X2709 MN MN X3105 1555 1555 2.24
LINK OP1 G X2721 MG MG X3411 1555 1555 2.15
LINK N7 G X2729 MN MN X3245 1555 1555 2.60
LINK OP2 A X2732 MN MN X3077 1555 1555 2.31
LINK O6 G X2735 MG MG X3397 1555 1555 2.73
LINK OP2 A X2738 MN MN X3251 1555 1555 1.94
LINK OP2 G X2741 MN MN X3251 1555 1555 2.45
LINK OP1 A X2748 MN MN X3105 1555 1555 2.24
LINK OP2 U X2753 MG MG X3388 1555 1555 2.68
LINK O2' A X2760 MG MG X3400 1555 1555 2.90
LINK OP2 A X2775 MN MN X3262 1555 1555 2.16
LINK OP1 G X2804 MG MG X3430 1555 1555 2.75
LINK OP2 G X2809 MN MN X3046 1555 1555 2.26
LINK OP2 G X2809 MG MG X3406 1555 1555 2.96
LINK OP2 A X2830 MN MN X3071 1555 1555 2.63
LINK N7 G X2831 MN MN X3071 1555 1555 2.63
LINK OP1 C X2836 MG MG X3214 1555 1555 2.88
LINK OP1 A X2840 MN MN X3114 1555 1555 2.58
LINK OP2 A X2857 MG MG X3383 1555 1555 2.34
LINK OP2 G X2866 MN MN X3146 1555 1555 2.11
LINK N7 G X2877 MN MN X3084 1555 1555 2.46
LINK MN MN X3053 NE2 HIS B 148 1555 1555 2.64
LINK MG MG X3504 OD1 ASN Z 14 1555 1555 2.61
LINK O6 G Y 31 MG MG Y 209 1555 1555 2.16
LINK OP2 A Y 43 MG MG Y 209 1555 1555 2.98
LINK OP2 G Y 74 MG MG Y 204 1555 1555 2.87
LINK OP2 A Y 97 MN MN Y 202 1555 1555 2.30
LINK OG1 THR J 43 MG MG J 202 1555 1555 2.99
SITE 1 AC1 1 TYR A 6
SITE 1 AC2 3 SER A 223 GLY A 235 GLY A 237
SITE 1 AC3 3 HIS A 232 ILE A 241 A X2625
SITE 1 AC4 2 MET A 16 G X1613
SITE 1 AC5 9 G X2088 A X2089 A X2478 C X2479
SITE 2 AC5 9 A X2530 U X2531 G X2532 U X2533
SITE 3 AC5 9 U X2612
SITE 1 AC6 5 G X1480 A X1560 G X1561 C X1604
SITE 2 AC6 5 A X1605
SITE 1 AC7 7 C X2708 U X2711 G X2712 G X2713
SITE 2 AC7 7 U X2714 U X2747 A X2748
SITE 1 AC8 5 GLU G 117 C X 572 A X 573 U X2806
SITE 2 AC8 5 G X2807
SITE 1 AC9 4 U X 79 G X 80 G X 81 G X 82
SITE 1 AD1 5 G X2763 G X2764 A X2792 G X2793
SITE 2 AD1 5 C X2794
SITE 1 AD2 3 U X1823 A X1848 G X1849
SITE 1 AD3 3 U X1750 G X1751 G X1783
SITE 1 AD4 5 G X2651 G X2652 C X2653 G X2804
SITE 2 AD4 5 MG X3430
SITE 1 AD5 1 A X2089
SITE 1 AD6 2 G X2088 G X2529
SITE 1 AD7 2 G X2473 G X2529
SITE 1 AD8 3 G X 613 A X2475 C X2526
SITE 1 AD9 4 A X2475 A X2524 C X2525 C X2526
SITE 1 AE1 1 U X1007
SITE 1 AE2 3 A X 992 G X1006 U X1007
SITE 1 AE3 1 G X1005
SITE 1 AE4 2 G X 907 A X 955
SITE 1 AE5 4 U X 871 C X2454 G X2455 G X2456
SITE 1 AE6 4 U X 871 U X 872 G X2456 A X2457
SITE 1 AE7 2 C X 252 A X2459
SITE 1 AE8 1 A X1017
SITE 1 AE9 1 G X 604
SITE 1 AF1 2 G X2059 C X2082
SITE 1 AF2 3 A X 621 C X2044 A X2045
SITE 1 AF3 1 G X2056
SITE 1 AF4 2 A X1306 C X2033
SITE 1 AF5 2 A X1303 U X2642
SITE 1 AF6 2 G X1307 A X2032
SITE 1 AF7 1 U X2038
SITE 1 AF8 1 U X1305
SITE 1 AF9 1 C X1364
SITE 1 AG1 1 A X1200
SITE 1 AG2 3 G X1201 C X1202 MG X3353
SITE 1 AG3 3 A X1034 C X1035 G X1225
SITE 1 AG4 2 U X2043 MG X3432
SITE 1 AG5 2 G X2265 G X2269
SITE 1 AG6 1 G X2809
SITE 1 AG7 2 GLU A 236 G X2615
SITE 1 AG8 2 U X 829 G X2615
SITE 1 AG9 3 A X 828 U X 829 A X2616
SITE 1 AH1 1 A X2069
SITE 1 AH2 2 HIS B 148 C X1702
SITE 1 AH3 2 A X 571 C X 572
SITE 1 AH4 1 A X 845
SITE 1 AH5 2 G X2603 A X2604
SITE 1 AH6 2 A X 383 G X 384
SITE 1 AH7 2 A X1018 A X1019
SITE 1 AH8 1 A X1019
SITE 1 AH9 1 A X1720
SITE 1 AI1 3 A X 629 U X1287 G X1288
SITE 1 AI2 2 G X2054 A X2060
SITE 1 AI3 1 G X1803
SITE 1 AI4 1 A X 847
SITE 1 AI5 3 PRO A 227 U X2101 G X2266
SITE 1 AI6 1 U X2620
SITE 1 AI7 2 A X2830 G X2831
SITE 1 AI8 1 G X2906
SITE 1 AI9 4 A X1713 C X1714 U X1715 G X2577
SITE 1 AJ1 2 C X1714 U X1715
SITE 1 AJ2 1 A X2732
SITE 1 AJ3 1 C X2730
SITE 1 AJ4 2 A X2666 G X2667
SITE 1 AJ5 3 A X 198 A X 200 C X 201
SITE 1 AJ6 1 G X 846
SITE 1 AJ7 1 A X 839
SITE 1 AJ8 1 U X 610
SITE 1 AJ9 1 G X2877
SITE 1 AK1 2 G X2083 G X2084
SITE 1 AK2 1 A X1025
SITE 1 AK3 1 G X1022
SITE 1 AK4 2 A X 615 A X1027
SITE 1 AK5 1 G X 893
SITE 1 AK6 1 G X2522
SITE 1 AK7 3 C X2093 C X2275 U X2276
SITE 1 AK8 2 A X1685 G X1686
SITE 1 AK9 2 U X 521 G X 522
SITE 1 AL1 4 LYS G 40 C X1050 A X1053 A X1054
SITE 1 AL2 1 C X1801
SITE 1 AL3 2 A X 14 G X 15
SITE 1 AL4 3 A X1708 G X1711 G X2019
SITE 1 AL5 2 A X1708 A X1709
SITE 1 AL6 2 G X 496 G X 498
SITE 1 AL7 2 G X 496 A X 499
SITE 1 AL8 2 U X2709 A X2748
SITE 1 AL9 1 U X1680
SITE 1 AM1 2 G X 863 G X1226
SITE 1 AM2 1 A X2545
SITE 1 AM3 1 G X 341
SITE 1 AM4 1 G X 208
SITE 1 AM5 1 A X1024
SITE 1 AM6 1 A X2840
SITE 1 AM7 1 G X 428
SITE 1 AM8 1 A X1052
SITE 1 AM9 1 G X 27
SITE 1 AN1 4 C X 554 C X 555 U X 556 G X 557
SITE 1 AN2 1 G X 221
SITE 1 AN3 1 G X 492
SITE 1 AN4 2 C X 31 C X1277
SITE 1 AN5 2 G X1271 U X1272
SITE 1 AN6 2 G X 545 A X 547
SITE 1 AN7 2 U X 619 A X2530
SITE 1 AN8 2 C X 195 U X2270
SITE 1 AN9 1 G X 630
SITE 1 AO1 1 G X1283
SITE 1 AO2 2 C X2613 G X2634
SITE 1 AO3 2 G X2609 G X2610
SITE 1 AO4 2 U X2011 G X2012
SITE 1 AO5 2 A X1965 C X1984
SITE 1 AO6 2 A X1228 G X1229
SITE 1 AO7 1 SER G 112
SITE 1 AO8 1 G X 381
SITE 1 AO9 1 C X1655
SITE 1 AP1 3 U X2541 G X2596 G X2597
SITE 1 AP2 4 C X2534 C X2600 G X2601 C X2602
SITE 1 AP3 2 ARG M 52 G X2866
SITE 1 AP4 1 C X 532
SITE 1 AP5 1 A X1045
SITE 1 AP6 2 A X 796 A X1658
SITE 1 AP7 1 G X1675
SITE 1 AP8 2 G X2744 G X2745
SITE 1 AP9 2 U X1043 C X1197
SITE 1 AQ1 2 A X 581 G X 582
SITE 1 AQ2 1 G X1317
SITE 1 AQ3 3 G X1340 C X1651 A X1652
SITE 1 AQ4 1 G X2297
SITE 1 AQ5 2 A X2295 A X2296
SITE 1 AQ6 2 G X1346 U X1348
SITE 1 AQ7 1 A X2765
SITE 1 AQ8 1 G X1855
SITE 1 AQ9 3 ARG A 221 G X1855 G X1999
SITE 1 AR1 1 U X2646
SITE 1 AR2 1 U X2022
SITE 1 AR3 3 A X1432 A X1647 C X1648
SITE 1 AR4 2 U X1431 C X1648
SITE 1 AR5 1 A X 952
SITE 1 AR6 1 A X 354
SITE 1 AR7 1 U X 357
SITE 1 AR8 1 A X2899
SITE 1 AR9 2 A X1997 A X1998
SITE 1 AS1 1 A X1997
SITE 1 AS2 2 A X 53 G X 54
SITE 1 AS3 2 A X2379 G X2380
SITE 1 AS4 1 U X2384
SITE 1 AS5 2 G X 177 A X 178
SITE 1 AS6 1 G X 214
SITE 1 AS7 1 G X 180
SITE 1 AS8 2 G X2278 G X2279
SITE 1 AS9 2 G X1931 C X1932
SITE 1 AT1 3 A X1415 U X1416 G X1417
SITE 1 AT2 2 G X 416 A X 468
SITE 1 AT3 1 A X2411
SITE 1 AT4 1 G X2410
SITE 1 AT5 3 G X2352 G X2364 C X2412
SITE 1 AT6 1 A X2301
SITE 1 AT7 2 U X 119 G X 122
SITE 1 AT8 1 U X 119
SITE 1 AT9 1 C X1968
SITE 1 AU1 2 A X1396 G X1397
SITE 1 AU2 1 A X2457
SITE 1 AU3 1 C X2433
SITE 1 AU4 2 G X 457 A X2434
SITE 1 AU5 4 U X1067 G X1068 G X1069 A X1070
SITE 1 AU6 1 C X 165
SITE 1 AU7 2 G X2513 MN X3322
SITE 1 AU8 3 G X2513 G X2514 MN X3322
SITE 1 AU9 2 A X 989 G X 990
SITE 1 AV1 1 C X 988
SITE 1 AV2 2 C X2263 G X2264
SITE 1 AV3 2 G X 158 U X 159
SITE 1 AV4 1 G X1384
SITE 1 AV5 1 C X2836
SITE 1 AV6 3 C X 785 A X1810 A X1811
SITE 1 AV7 3 A X1807 C X1809 A X1810
SITE 1 AV8 2 C X 832 U X 835
SITE 1 AV9 2 U X 786 G X2634
SITE 1 AW1 4 G X1309 A X1310 G X1691 C X1692
SITE 1 AW2 3 C X 782 U X1665 A X1666
SITE 1 AW3 2 C X1651 G X1664
SITE 1 AW4 1 G X2736
SITE 1 AW5 2 A X2629 G X2630
SITE 1 AW6 1 G X1298
SITE 1 AW7 2 G X1411 G X1412
SITE 1 AW8 2 A X 744 G X 745
SITE 1 AW9 1 G X 778
SITE 1 AX1 1 G X1915
SITE 1 AX2 1 A X1600
SITE 1 AX3 2 LYS 2 38 G X 515
SITE 1 AX4 3 U X 438 G X 454 A X 455
SITE 1 AX5 1 G X 422
SITE 1 AX6 1 U X 818
SITE 1 AX7 1 A X1521
SITE 1 AX8 1 G X2746
SITE 1 AX9 2 G X 24 A X 559
SITE 1 AY1 1 U X1420
SITE 1 AY2 1 G X2729
SITE 1 AY3 1 G X2056
SITE 1 AY4 1 G X2013
SITE 1 AY5 2 A X2738 G X2741
SITE 1 AY6 1 A X 108
SITE 1 AY7 1 C X1472
SITE 1 AY8 1 G X 36
SITE 1 AY9 1 G X1180
SITE 1 AZ1 2 C X1335 U X1683
SITE 1 AZ2 3 C X1334 U X1683 G X2736
SITE 1 AZ3 2 G X 88 A X 91
SITE 1 AZ4 1 G X1650
SITE 1 AZ5 2 A X2775 U X2781
SITE 1 AZ6 3 U X1878 A X1917 G X1918
SITE 1 AZ7 2 U X1499 G X1500
SITE 1 AZ8 1 C X2628
SITE 1 AZ9 2 A X 784 U X1805
SITE 1 BC1 1 U X1011
SITE 1 BC2 1 U X1085
SITE 1 BC3 4 A X 775 C X 776 A X 806 G X 808
SITE 1 BC4 2 C X 777 G X 805
SITE 1 BC5 4 U X1079 G X1080 U X1163 MG X3396
SITE 1 BC6 2 C X 129 A X 130
SITE 1 BC7 1 G X 350
SITE 1 BC8 2 A X 989 G X 990
SITE 1 BC9 1 G X 990
SITE 1 BD1 2 G X1995 G X2619
SITE 1 BD2 1 G X2282
SITE 1 BD3 2 C X1696 G X2031
SITE 1 BD4 1 G X1462
SITE 1 BD5 1 G X2110
SITE 1 BD6 2 C X2685 G X2686
SITE 1 BD7 3 C X 20 U X1256 G X1257
SITE 1 BD8 2 A X2480 U X2519
SITE 1 BD9 1 A X1787
SITE 1 BE1 1 A X2261
SITE 1 BE2 1 G X1250
SITE 1 BE3 1 G X2406
SITE 1 BE4 1 A X1311
SITE 1 BE5 2 A X1745 G X1746
SITE 1 BE6 2 G X2427 G X2442
SITE 1 BE7 1 G X2440
SITE 1 BE8 4 ILE Q 55 A X1379 C X1644 U X1646
SITE 1 BE9 2 A X 725 C X 821
SITE 1 BF1 3 C X 323 A X 324 A X 326
SITE 1 BF2 1 A X 365
SITE 1 BF3 1 MN X3437
SITE 1 BF4 1 A X2765
SITE 1 BF5 1 A X1836
SITE 1 BF6 1 G X 235
SITE 1 BF7 1 G X2280
SITE 1 BF8 1 A X 622
SITE 1 BF9 1 U X 642
SITE 1 BG1 3 A X 219 A X 476 U X 477
SITE 1 BG2 1 A X1573
SITE 1 BG3 1 C X2479
SITE 1 BG4 1 U X1706
SITE 1 BG5 2 G X 522 A X1275
SITE 1 BG6 2 G X2516 G X2517
SITE 1 BG7 2 U X2820 G X2823
SITE 1 BG8 3 U X 684 G X 694 G X 696
SITE 1 BG9 4 G X 997 G X 998 U X 999 G X1006
SITE 1 BH1 1 G X2686
SITE 1 BH2 3 G X2513 MG X3204 MG X3205
SITE 1 BH3 1 U X2271
SITE 1 BH4 2 A X1881 G X1882
SITE 1 BH5 2 G X1884 G X1885
SITE 1 BH6 2 A X2354 A X2355
SITE 1 BH7 2 A X2349 G X2350
SITE 1 BH8 2 U X2351 G X2358
SITE 1 BH9 4 G X 578 U X 579 G X 601 G X 602
SITE 1 BI1 3 U X 631 A X 715 C X 716
SITE 1 BI2 1 A X 126
SITE 1 BI3 2 U X1248 A X1275
SITE 1 BI4 1 C X2421
SITE 1 BI5 4 G X1244 G X1245 C X1277 G X1278
SITE 1 BI6 3 U X1301 A X2042 U X2043
SITE 1 BI7 1 C X2644
SITE 1 BI8 1 U X1381
SITE 1 BI9 2 U X 787 U X 799
SITE 1 BJ1 1 U X1272
SITE 1 BJ2 5 A X 13 G X 15 G X 16 U X 569
SITE 2 BJ2 5 U X 570
SITE 1 BJ3 2 G X 514 MG X3477
SITE 1 BJ4 2 G X2094 G X2096
SITE 1 BJ5 1 G X2230
SITE 1 BJ6 1 G X1797
SITE 1 BJ7 1 C X 182
SITE 1 BJ8 1 G X1851
SITE 1 BJ9 3 A X1034 C X1202 MN X3041
SITE 1 BK1 2 G X 707 G X 708
SITE 1 BK2 1 MG X3491
SITE 1 BK3 4 U X 642 G X 643 G X 701 U X 702
SITE 1 BK4 1 G X 370
SITE 1 BK5 1 A X1699
SITE 1 BK6 2 G X2571 A X2671
SITE 1 BK7 2 A X1072 G X1169
SITE 1 BK8 1 U X1237
SITE 1 BK9 2 G X 565 U X 566
SITE 1 BL1 1 U X 731
SITE 1 BL2 3 A X 198 A X 199 A X 200
SITE 1 BL3 1 U X 196
SITE 1 BL4 2 C X2673 G X2759
SITE 1 BL5 2 C X 960 G X 961
SITE 1 BL6 1 G X1320
SITE 1 BL7 2 C X2468 MG X3484
SITE 1 BL8 2 G X2402 A X2403
SITE 1 BL9 1 C X 883
SITE 1 BM1 3 G X1470 A X1471 C X1472
SITE 1 BM2 3 A X 225 G X 300 U X 467
SITE 1 BM3 2 A X2855 A X2857
SITE 1 BM4 2 U X1750 G X1751
SITE 1 BM5 1 U X 11
SITE 1 BM6 2 G X 189 G X 190
SITE 1 BM7 2 G X 304 G X 410
SITE 1 BM8 1 U X2753
SITE 1 BM9 4 U X 614 A X 618 A X2057 C X2526
SITE 1 BN1 2 U X1840 A X1842
SITE 1 BN2 1 G X2029
SITE 1 BN3 1 G X 888
SITE 1 BN4 3 G X 509 G X 511 A X 833
SITE 1 BN5 3 G X1080 G X1081 MG X3272
SITE 1 BN6 3 U X2725 G X2735 G X2736
SITE 1 BN7 2 A X2588 U X2589
SITE 1 BN8 2 A X2760 C X2761
SITE 1 BN9 2 C X1179 G X1181
SITE 1 BO1 2 U X 830 C X 831
SITE 1 BO2 1 C X 870
SITE 1 BO3 1 G X 598
SITE 1 BO4 4 U X2655 A X2803 A X2808 G X2809
SITE 1 BO5 2 G X 778 A X 806
SITE 1 BO6 2 C X 862 G X1226
SITE 1 BO7 2 U X2908 C X2909
SITE 1 BO8 1 G X2721
SITE 1 BO9 1 G X2696
SITE 1 BP1 2 G X2594 C X2595
SITE 1 BP2 2 G X2575 G X2576
SITE 1 BP3 3 HIS B 146 U X 791 C X2638
SITE 1 BP4 1 G X2634
SITE 1 BP5 2 G X 70 U X 111
SITE 1 BP6 2 U X 905 U X 958
SITE 1 BP7 2 G X2572 U X2573
SITE 1 BP8 2 G X 120 U X 149
SITE 1 BP9 1 G X 595
SITE 1 BQ1 2 A X2760 C X2797
SITE 1 BQ2 1 G X2264
SITE 1 BQ3 1 U X 605
SITE 1 BQ4 2 U X 971 A X 972
SITE 1 BQ5 3 U X2458 A X2459 A X2460
SITE 1 BQ6 3 G X2654 G X2804 MPD X3011
SITE 1 BQ7 3 U X1293 G X1294 MN X3043
SITE 1 BQ8 1 G X1492
SITE 1 BQ9 1 G X 850
SITE 1 BR1 2 U X1891 G X1905
SITE 1 BR2 1 U X 374
SITE 1 BR3 1 MG X3302
SITE 1 BR4 4 G X1069 A X1070 C X1178 C X1179
SITE 1 BR5 2 A X 617 G X 620
SITE 1 BR6 3 A X2569 G X2570 G X2571
SITE 1 BR7 2 G X 598 A X 599
SITE 1 BR8 1 G X2563
SITE 1 BR9 1 G X1426
SITE 1 BS1 2 G X2865 G X2866
SITE 1 BS2 1 G X 790
SITE 1 BS3 1 G X1320
SITE 1 BS4 1 U X2116
SITE 1 BS5 1 G X 771
SITE 1 BS6 1 A X 542
SITE 1 BS7 1 G X2635
SITE 1 BS8 1 U X2390
SITE 1 BS9 1 C X 204
SITE 1 BT1 1 G X 295
SITE 1 BT2 1 G X 264
SITE 1 BT3 1 G X1414
SITE 1 BT4 2 C X2638 C X2639
SITE 1 BT5 3 G X1741 A X1742 C X2006
SITE 1 BT6 2 A X1291 MG X3489
SITE 1 BT7 2 G X 843 G X 844
SITE 1 BT8 1 C X2494
SITE 1 BT9 2 A X1173 U X2518
SITE 1 BU1 2 G X2517 U X2518
SITE 1 BU2 3 U X1301 G X1302 A X2041
SITE 1 BU3 1 MG X3346
SITE 1 BU4 1 A X 655
SITE 1 BU5 1 C X2565
SITE 1 BU6 2 A X 794 C X1308
SITE 1 BU7 1 G X1691
SITE 1 BU8 2 A X1690 G X1693
SITE 1 BU9 3 C X2468 C X2469 MG X3375
SITE 1 BV1 1 C X2566
SITE 1 BV2 1 U X 905
SITE 1 BV3 1 A X2300
SITE 1 BV4 4 A X1291 A X1292 G X1294 MN X3467
SITE 1 BV5 1 U X2549
SITE 1 BV6 2 A X1173 MG X3355
SITE 1 BV7 4 G X1975 G X1976 G X1977 U X1978
SITE 1 BV8 3 G X2669 G X2670 G X2672
SITE 1 BV9 4 G X 534 A X 537 G X 538 G X 539
SITE 1 BW1 5 U X 884 U X 981 G X 982 G X 983
SITE 2 BW1 5 G X 984
SITE 1 BW2 4 U X 3 G X2657 G X2658 G X2913
SITE 1 BW3 3 C X 533 G X 534 A X 536
SITE 1 BW4 4 G X 355 U X 374 G X1247 U X1248
SITE 1 BW5 1 C X2799
SITE 1 BW6 1 U X 739
SITE 1 BW7 4 GLY B 152 SER B 153 GLN B 167 C X2539
SITE 1 BW8 2 ASN I 17 A X1231
SITE 1 BW9 3 ARG I 33 HIS I 35 U X 987
SITE 1 BX1 3 G X 563 ASN Z 14 ARG Z 17
SITE 1 BX2 1 G Y 92
SITE 1 BX3 2 A Y 97 U Y 99
SITE 1 BX4 1 G Y 74
SITE 1 BX5 1 G Y 4
SITE 1 BX6 3 G Y 77 C Y 78 U Y 94
SITE 1 BX7 1 U Y 106
SITE 1 BX8 2 G Y 31 A Y 43
SITE 1 BX9 1 G Y 70
SITE 1 BY1 2 A X2817 U Y 1
SITE 1 BY2 2 A Y 80 SPD Y 213
SITE 1 BY3 4 U X 995 C Y 86 U Y 88 MG Y 212
SITE 1 BY4 4 LYS C 63 TRP C 65 GLN C 75 A X 720
SITE 1 BY5 1 ARG C 62
SITE 1 BY6 1 GLU G 99
SITE 1 BY7 2 PHE G 65 ARG G 94
SITE 1 BY8 3 GLN I 54 LEU I 55 G X 253
SITE 1 BY9 1 GLU J 135
SITE 1 BZ1 5 THR J 43 SER J 44 ARG J 45 GLY J 92
SITE 2 BZ1 5 TRP J 93
SITE 1 BZ2 1 TYR M 100
SITE 1 BZ3 10 GLY N 6 GLY N 7 THR N 8 VAL N 9
SITE 2 BZ3 10 THR N 10 ARG N 11 G X 626 C X 627
SITE 3 BZ3 10 G X 628 A X1289
SITE 1 BZ4 2 ARG P 8 G X 539
SITE 1 BZ5 3 ALA Q 21 ASP Q 23 TYR Q 25
SITE 1 BZ6 2 PRO R 78 U X 344
SITE 1 BZ7 2 LYS T 27 C X2290
SITE 1 BZ8 2 CYS Z 33 CYS Z 44
CRYST1 282.112 282.112 875.343 90.00 90.00 120.00 P 65 2 2 12
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 0.003545 0.002047 0.000000 0.00000
SCALE2 0.000000 0.004093 0.000000 0.00000
SCALE3 0.000000 0.000000 0.001142 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
