HEADER RIBOSOME/ANTIBIOTIC 05-AUG-10 3OAR
TITLE CRYSTAL STRUCTURE OF THE E. COLI RIBOSOME BOUND TO TELITHROMYCIN. THIS
TITLE 2 FILE CONTAINS THE 30S SUBUNIT OF THE SECOND 70S RIBOSOME.
SPLIT 3OAQ 3OAR 3OAS 3OAT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 16S RRNA;
COMPND 3 CHAIN: A;
COMPND 4 MOL_ID: 2;
COMPND 5 MOLECULE: 30S RIBOSOMAL PROTEIN S2;
COMPND 6 CHAIN: B;
COMPND 7 MOL_ID: 3;
COMPND 8 MOLECULE: 30S RIBOSOMAL PROTEIN S3;
COMPND 9 CHAIN: C;
COMPND 10 MOL_ID: 4;
COMPND 11 MOLECULE: 30S RIBOSOMAL PROTEIN S4;
COMPND 12 CHAIN: D;
COMPND 13 MOL_ID: 5;
COMPND 14 MOLECULE: 30S RIBOSOMAL PROTEIN S5;
COMPND 15 CHAIN: E;
COMPND 16 MOL_ID: 6;
COMPND 17 MOLECULE: 30S RIBOSOMAL PROTEIN S6;
COMPND 18 CHAIN: F;
COMPND 19 MOL_ID: 7;
COMPND 20 MOLECULE: 30S RIBOSOMAL PROTEIN S7;
COMPND 21 CHAIN: G;
COMPND 22 MOL_ID: 8;
COMPND 23 MOLECULE: 30S RIBOSOMAL PROTEIN S8;
COMPND 24 CHAIN: H;
COMPND 25 MOL_ID: 9;
COMPND 26 MOLECULE: 30S RIBOSOMAL PROTEIN S9;
COMPND 27 CHAIN: I;
COMPND 28 MOL_ID: 10;
COMPND 29 MOLECULE: 30S RIBOSOMAL PROTEIN S10;
COMPND 30 CHAIN: J;
COMPND 31 MOL_ID: 11;
COMPND 32 MOLECULE: 30S RIBOSOMAL PROTEIN S11;
COMPND 33 CHAIN: K;
COMPND 34 MOL_ID: 12;
COMPND 35 MOLECULE: 30S RIBOSOMAL PROTEIN S12;
COMPND 36 CHAIN: L;
COMPND 37 MOL_ID: 13;
COMPND 38 MOLECULE: 30S RIBOSOMAL PROTEIN S13;
COMPND 39 CHAIN: M;
COMPND 40 MOL_ID: 14;
COMPND 41 MOLECULE: 30S RIBOSOMAL PROTEIN S14;
COMPND 42 CHAIN: N;
COMPND 43 MOL_ID: 15;
COMPND 44 MOLECULE: 30S RIBOSOMAL PROTEIN S15;
COMPND 45 CHAIN: O;
COMPND 46 MOL_ID: 16;
COMPND 47 MOLECULE: 30S RIBOSOMAL PROTEIN S16;
COMPND 48 CHAIN: P;
COMPND 49 MOL_ID: 17;
COMPND 50 MOLECULE: 30S RIBOSOMAL PROTEIN S17;
COMPND 51 CHAIN: Q;
COMPND 52 MOL_ID: 18;
COMPND 53 MOLECULE: 30S RIBOSOMAL PROTEIN S18;
COMPND 54 CHAIN: R;
COMPND 55 MOL_ID: 19;
COMPND 56 MOLECULE: 30S RIBOSOMAL PROTEIN S19;
COMPND 57 CHAIN: S;
COMPND 58 MOL_ID: 20;
COMPND 59 MOLECULE: 30S RIBOSOMAL PROTEIN S20;
COMPND 60 CHAIN: T;
COMPND 61 MOL_ID: 21;
COMPND 62 MOLECULE: 30S RIBOSOMAL PROTEIN S21;
COMPND 63 CHAIN: U
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 MOL_ID: 2;
SOURCE 5 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 6 ORGANISM_TAXID: 83333;
SOURCE 7 STRAIN: K-12;
SOURCE 8 MOL_ID: 3;
SOURCE 9 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 10 ORGANISM_TAXID: 83333;
SOURCE 11 STRAIN: K-12;
SOURCE 12 MOL_ID: 4;
SOURCE 13 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 14 ORGANISM_TAXID: 83333;
SOURCE 15 STRAIN: K-12;
SOURCE 16 MOL_ID: 5;
SOURCE 17 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 18 ORGANISM_TAXID: 83333;
SOURCE 19 STRAIN: K-12;
SOURCE 20 MOL_ID: 6;
SOURCE 21 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 22 ORGANISM_TAXID: 83333;
SOURCE 23 STRAIN: K-12;
SOURCE 24 MOL_ID: 7;
SOURCE 25 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 26 ORGANISM_TAXID: 83333;
SOURCE 27 STRAIN: K-12;
SOURCE 28 MOL_ID: 8;
SOURCE 29 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 30 ORGANISM_TAXID: 83333;
SOURCE 31 STRAIN: K-12;
SOURCE 32 MOL_ID: 9;
SOURCE 33 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 34 ORGANISM_TAXID: 83333;
SOURCE 35 STRAIN: K-12;
SOURCE 36 MOL_ID: 10;
SOURCE 37 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 38 ORGANISM_TAXID: 83333;
SOURCE 39 STRAIN: K-12;
SOURCE 40 MOL_ID: 11;
SOURCE 41 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 42 ORGANISM_TAXID: 83333;
SOURCE 43 STRAIN: K-12;
SOURCE 44 MOL_ID: 12;
SOURCE 45 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 46 ORGANISM_TAXID: 83333;
SOURCE 47 STRAIN: K-12;
SOURCE 48 MOL_ID: 13;
SOURCE 49 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 50 ORGANISM_TAXID: 83333;
SOURCE 51 STRAIN: K-12;
SOURCE 52 MOL_ID: 14;
SOURCE 53 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 54 ORGANISM_TAXID: 83333;
SOURCE 55 STRAIN: K-12;
SOURCE 56 MOL_ID: 15;
SOURCE 57 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 58 ORGANISM_TAXID: 83333;
SOURCE 59 STRAIN: K-12;
SOURCE 60 MOL_ID: 16;
SOURCE 61 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 62 ORGANISM_TAXID: 83333;
SOURCE 63 STRAIN: K-12;
SOURCE 64 MOL_ID: 17;
SOURCE 65 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 66 ORGANISM_TAXID: 83333;
SOURCE 67 STRAIN: K-12;
SOURCE 68 MOL_ID: 18;
SOURCE 69 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 70 ORGANISM_TAXID: 83333;
SOURCE 71 STRAIN: K-12;
SOURCE 72 MOL_ID: 19;
SOURCE 73 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 74 ORGANISM_TAXID: 83333;
SOURCE 75 STRAIN: K-12;
SOURCE 76 MOL_ID: 20;
SOURCE 77 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 78 ORGANISM_TAXID: 83333;
SOURCE 79 STRAIN: K-12;
SOURCE 80 MOL_ID: 21;
SOURCE 81 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 82 ORGANISM_TAXID: 83333;
SOURCE 83 STRAIN: K-12
KEYWDS PROTEIN BIOSYNTHESIS, RIBOSOMES, RNA, TRNA, TRANSFER, TELITHROMYCIN,
KEYWDS 2 KETOLIDE, MACROLIDE, ANTIBIOTIC, EXIT, PEPTIDYL, 30S, 70S, 16S,
KEYWDS 3 RIBOSOMAL SUBUNIT, SMALL, RIBOSOME, RIBOSOME-ANTIBIOTIC COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.A.DUNKLE,L.XIONG,A.S.MANKIN,J.H.D.CATE
REVDAT 2 06-MAR-13 3OAR 1 CRYST1 SCALE1 SCALE2 SCALE3
REVDAT 2 2 1 VERSN
REVDAT 1 15-DEC-10 3OAR 0
JRNL AUTH J.A.DUNKLE,L.XIONG,A.S.MANKIN,J.H.CATE
JRNL TITL STRUCTURES OF THE ESCHERICHIA COLI RIBOSOME WITH ANTIBIOTICS
JRNL TITL 2 BOUND NEAR THE PEPTIDYL TRANSFERASE CENTER EXPLAIN SPECTRA
JRNL TITL 3 OF DRUG ACTION.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 107 17152 2010
JRNL REFN ISSN 0027-8424
JRNL PMID 20876128
JRNL DOI 10.1073/PNAS.1007988107
REMARK 2
REMARK 2 RESOLUTION. 3.25 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.6.1_357)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.25
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 85.22
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.020
REMARK 3 COMPLETENESS FOR RANGE (%) : 85.8
REMARK 3 NUMBER OF REFLECTIONS : 754750
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.194
REMARK 3 R VALUE (WORKING SET) : 0.193
REMARK 3 FREE R VALUE : 0.245
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.020
REMARK 3 FREE R VALUE TEST SET COUNT : 15234
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 85.2473 - 10.1078 0.97 28942 606 0.2032 0.2257
REMARK 3 2 10.1078 - 8.0248 0.98 28585 561 0.1821 0.2289
REMARK 3 3 8.0248 - 7.0109 0.97 28242 592 0.1660 0.2081
REMARK 3 4 7.0109 - 6.3702 0.96 27854 570 0.1621 0.2258
REMARK 3 5 6.3702 - 5.9137 0.95 27572 609 0.1743 0.2485
REMARK 3 6 5.9137 - 5.5651 0.95 27421 552 0.1641 0.2296
REMARK 3 7 5.5651 - 5.2864 0.94 27158 558 0.1619 0.2275
REMARK 3 8 5.2864 - 5.0563 0.93 26835 533 0.1664 0.2281
REMARK 3 9 5.0563 - 4.8617 0.91 26275 547 0.1733 0.2250
REMARK 3 10 4.8617 - 4.6940 0.91 26129 575 0.1713 0.2203
REMARK 3 11 4.6940 - 4.5472 0.90 25855 544 0.1708 0.2349
REMARK 3 12 4.5472 - 4.4172 0.90 25713 536 0.1759 0.2225
REMARK 3 13 4.4172 - 4.3009 0.90 25722 500 0.1805 0.2215
REMARK 3 14 4.3009 - 4.1960 0.89 25518 521 0.1780 0.2346
REMARK 3 15 4.1960 - 4.1006 0.89 25430 522 0.1782 0.2275
REMARK 3 16 4.1006 - 4.0134 0.88 25215 514 0.1850 0.2339
REMARK 3 17 4.0134 - 3.9331 0.87 24986 538 0.1898 0.2297
REMARK 3 18 3.9331 - 3.8589 0.86 24561 487 0.1878 0.2796
REMARK 3 19 3.8589 - 3.7899 0.85 24266 482 0.2015 0.2640
REMARK 3 20 3.7899 - 3.7257 0.83 23859 480 0.2120 0.2596
REMARK 3 21 3.7257 - 3.6656 0.82 23501 467 0.2117 0.2567
REMARK 3 22 3.6656 - 3.6092 0.80 22922 496 0.2177 0.2772
REMARK 3 23 3.6092 - 3.5561 0.79 22732 430 0.2329 0.2928
REMARK 3 24 3.5561 - 3.5060 0.77 22050 470 0.2378 0.3067
REMARK 3 25 3.5060 - 3.4587 0.76 21604 446 0.2494 0.2931
REMARK 3 26 3.4587 - 3.4137 0.75 21263 487 0.2540 0.3072
REMARK 3 27 3.4137 - 3.3711 0.72 20662 421 0.2610 0.3079
REMARK 3 28 3.3711 - 3.3304 0.71 20216 430 0.2668 0.3065
REMARK 3 29 3.3304 - 3.2917 0.69 19668 372 0.2682 0.2936
REMARK 3 30 3.2917 - 3.2547 0.66 18760 388 0.2889 0.3373
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 : 0.23
REMARK 3 B_SOL : 32.48
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.370
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.500
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.25550
REMARK 3 B22 (A**2) : -12.54200
REMARK 3 B33 (A**2) : 9.45610
REMARK 3 B12 (A**2) : -0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
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 : 0.006 308548
REMARK 3 ANGLE : 0.923 462238
REMARK 3 CHIRALITY : 0.063 58599
REMARK 3 PLANARITY : 0.005 24723
REMARK 3 DIHEDRAL : 19.323 143175
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 38
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ((chain QA and (resid 2:8 or resid 27:557)) or
REMARK 3 (chain QD and resid 1:205) or (chain QP and resid 1:
REMARK 3 82) or (chain QT and resid 2:86) or (chain QL and
REMARK 3 resid 22:123) or (chain ZQ and (resid 299 or resid
REMARK 3 315 or resid 362 or resid 417 or resid 509 or resid
REMARK 3 547 or resid 533 or resid 608 or resid 536 or resid
REMARK 3 116 or resid 352 or resid 324 or resid 100 or resid
REMARK 3 195 or resid 259 or resid 258)))
REMARK 3 ORIGIN FOR THE GROUP (A): -62.4936 12.5497 -76.2693
REMARK 3 T TENSOR
REMARK 3 T11: 0.3424 T22: 0.2526
REMARK 3 T33: 0.2576 T12: 0.1352
REMARK 3 T13: 0.1586 T23: 0.2179
REMARK 3 L TENSOR
REMARK 3 L11: 0.0602 L22: 0.1304
REMARK 3 L33: 0.1904 L12: 0.0446
REMARK 3 L13: -0.0190 L23: -0.0547
REMARK 3 S TENSOR
REMARK 3 S11: -0.0465 S12: 0.0608 S13: 0.0049
REMARK 3 S21: -0.2039 S22: -0.0190 S23: -0.0935
REMARK 3 S31: -0.1289 S32: -0.0777 S33: -0.0779
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: ((chain QA and (resid 9:26 or resid 558:562 or resid
REMARK 3 564:566 or resid 914:925 or resid 1391:1396)) or
REMARK 3 (chain QL and resid 1:21) or (chain ZQ and (resid 21
REMARK 3 or resid 560)))
REMARK 3 ORIGIN FOR THE GROUP (A): -85.8115 36.3717 -31.1254
REMARK 3 T TENSOR
REMARK 3 T11: 0.2168 T22: 0.1643
REMARK 3 T33: 0.1913 T12: 0.0866
REMARK 3 T13: -0.0017 T23: 0.0582
REMARK 3 L TENSOR
REMARK 3 L11: 0.0016 L22: 0.0076
REMARK 3 L33: 0.0031 L12: -0.0042
REMARK 3 L13: 0.0022 L23: -0.0063
REMARK 3 S TENSOR
REMARK 3 S11: -0.0008 S12: 0.0062 S13: 0.0084
REMARK 3 S21: 0.0035 S22: -0.0119 S23: 0.0059
REMARK 3 S31: -0.0096 S32: 0.0024 S33: 0.0000
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (chain QE and resid 9:73)
REMARK 3 ORIGIN FOR THE GROUP (A): -98.5708 57.1263 -40.0678
REMARK 3 T TENSOR
REMARK 3 T11: 0.3692 T22: 0.3555
REMARK 3 T33: 0.3791 T12: 0.0317
REMARK 3 T13: 0.0064 T23: 0.0396
REMARK 3 L TENSOR
REMARK 3 L11: 0.0011 L22: 0.0015
REMARK 3 L33: 0.0002 L12: -0.0017
REMARK 3 L13: -0.0001 L23: -0.0001
REMARK 3 S TENSOR
REMARK 3 S11: -0.0023 S12: -0.0023 S13: -0.0006
REMARK 3 S21: -0.0003 S22: -0.0017 S23: 0.0013
REMARK 3 S31: -0.0003 S32: -0.0010 S33: -0.0000
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (chain QE and resid 74:149)
REMARK 3 ORIGIN FOR THE GROUP (A): -79.9036 55.3041 -47.5425
REMARK 3 T TENSOR
REMARK 3 T11: 0.3471 T22: 0.3454
REMARK 3 T33: 0.3495 T12: 0.0283
REMARK 3 T13: 0.0027 T23: 0.0410
REMARK 3 L TENSOR
REMARK 3 L11: 0.0005 L22: 0.0005
REMARK 3 L33: 0.0003 L12: -0.0007
REMARK 3 L13: 0.0000 L23: -0.0003
REMARK 3 S TENSOR
REMARK 3 S11: -0.0035 S12: -0.0006 S13: -0.0015
REMARK 3 S21: -0.0007 S22: -0.0007 S23: 0.0007
REMARK 3 S31: -0.0006 S32: -0.0020 S33: -0.0000
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: (chain QB and (resid 8:107 or resid 147:225))
REMARK 3 ORIGIN FOR THE GROUP (A): -86.3956 85.8377 -20.1264
REMARK 3 T TENSOR
REMARK 3 T11: 0.8414 T22: 0.8104
REMARK 3 T33: 0.8421 T12: 0.0133
REMARK 3 T13: -0.0040 T23: 0.0124
REMARK 3 L TENSOR
REMARK 3 L11: 0.0007 L22: 0.0018
REMARK 3 L33: 0.0006 L12: -0.0002
REMARK 3 L13: -0.0002 L23: 0.0001
REMARK 3 S TENSOR
REMARK 3 S11: -0.0007 S12: -0.0006 S13: -0.0014
REMARK 3 S21: 0.0003 S22: -0.0021 S23: -0.0014
REMARK 3 S31: -0.0010 S32: 0.0013 S33: -0.0000
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: (chain QB and resid 108:146)
REMARK 3 ORIGIN FOR THE GROUP (A):-118.3242 84.3356 -17.8434
REMARK 3 T TENSOR
REMARK 3 T11: 1.1851 T22: 1.1820
REMARK 3 T33: 1.1901 T12: 0.0069
REMARK 3 T13: -0.0011 T23: 0.0035
REMARK 3 L TENSOR
REMARK 3 L11: 0.0000 L22: 0.0002
REMARK 3 L33: 0.0001 L12: -0.0000
REMARK 3 L13: 0.0000 L23: -0.0001
REMARK 3 S TENSOR
REMARK 3 S11: 0.0008 S12: 0.0001 S13: 0.0000
REMARK 3 S21: -0.0008 S22: 0.0001 S23: 0.0001
REMARK 3 S31: 0.0006 S32: 0.0001 S33: -0.0000
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: ((chain QA and (resid 926:986 or resid 1048:1390))
REMARK 3 or (chain QC and resid 1:206) or (chain QG and resid
REMARK 3 1:151) or (chain QI and resid 3:129) or (chain QJ and
REMARK 3 resid 5:102) or (chain QM and resid 1:114) or (chain
REMARK 3 QN and resid 1:100) or (chain QS and resid 2:80) or
REMARK 3 (chain ZQ and (resid 934 or resid 937 or resid 980 or
REMARK 3 resid 1048 or resid 1076 or resid 1054 or resid 1303
REMARK 3 or resid 1386 or resid 964 or resid 1222 or resid
REMARK 3 1110 or resid 1108)))
REMARK 3 ORIGIN FOR THE GROUP (A):-146.2973 44.1281 -3.7577
REMARK 3 T TENSOR
REMARK 3 T11: 0.6004 T22: 0.4671
REMARK 3 T33: 0.6764 T12: 0.2169
REMARK 3 T13: 0.1563 T23: 0.2840
REMARK 3 L TENSOR
REMARK 3 L11: 0.0887 L22: 0.0616
REMARK 3 L33: 0.0464 L12: -0.0331
REMARK 3 L13: -0.0097 L23: -0.0412
REMARK 3 S TENSOR
REMARK 3 S11: 0.0785 S12: -0.0267 S13: 0.0023
REMARK 3 S21: 0.0269 S22: 0.0913 S23: 0.0007
REMARK 3 S31: 0.0656 S32: -0.1028 S33: -0.0000
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: (chain QA and resid 987:1047)
REMARK 3 ORIGIN FOR THE GROUP (A):-168.2108 20.5165 -45.7227
REMARK 3 T TENSOR
REMARK 3 T11: 1.2677 T22: 1.2667
REMARK 3 T33: 1.2743 T12: -0.0073
REMARK 3 T13: -0.0145 T23: 0.0203
REMARK 3 L TENSOR
REMARK 3 L11: 0.0015 L22: 0.0013
REMARK 3 L33: 0.0004 L12: 0.0012
REMARK 3 L13: 0.0006 L23: -0.0003
REMARK 3 S TENSOR
REMARK 3 S11: 0.0025 S12: 0.0005 S13: -0.0049
REMARK 3 S21: 0.0005 S22: -0.0016 S23: -0.0022
REMARK 3 S31: 0.0000 S32: -0.0033 S33: -0.0000
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: ((chain QA and (resid 563 or resid 567:913 or resid
REMARK 3 1496:1530)) or (chain QF and resid 1:100) or (chain
REMARK 3 QH and resid 1:129) or (chain QK and resid 12:128) or
REMARK 3 (chain QO and resid 1:88) or (chain QR and resid 19:
REMARK 3 73) or (chain QU and resid 3:53) or (chain ZQ and
REMARK 3 (resid 572 or resid 578 or resid 593 or resid 770 or
REMARK 3 resid 814 or resid 891 or resid 1500 or resid 1499 or
REMARK 3 resid 781 or resid 869 or resid 1525)))
REMARK 3 ORIGIN FOR THE GROUP (A): -64.6075 38.7659 -2.8373
REMARK 3 T TENSOR
REMARK 3 T11: 0.4213 T22: 0.1016
REMARK 3 T33: 0.3773 T12: 0.0898
REMARK 3 T13: -0.0220 T23: 0.0481
REMARK 3 L TENSOR
REMARK 3 L11: 0.0742 L22: 0.1266
REMARK 3 L33: 0.0323 L12: -0.0704
REMARK 3 L13: 0.0049 L23: 0.0196
REMARK 3 S TENSOR
REMARK 3 S11: -0.0413 S12: -0.0315 S13: 0.1664
REMARK 3 S21: 0.0838 S22: 0.0571 S23: -0.0431
REMARK 3 S31: -0.1188 S32: 0.0015 S33: 0.0019
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: ((chain QA and resid 1397:1495) or (chain ZQ and
REMARK 3 (resid 1417 or resid 8201)))
REMARK 3 ORIGIN FOR THE GROUP (A): -55.9463 -6.5931 -41.9904
REMARK 3 T TENSOR
REMARK 3 T11: 0.1834 T22: 0.1828
REMARK 3 T33: 0.2339 T12: 0.0640
REMARK 3 T13: 0.1135 T23: 0.0861
REMARK 3 L TENSOR
REMARK 3 L11: 0.0054 L22: 0.0607
REMARK 3 L33: 0.0306 L12: 0.0112
REMARK 3 L13: -0.0017 L23: -0.0478
REMARK 3 S TENSOR
REMARK 3 S11: -0.0544 S12: -0.0034 S13: 0.0146
REMARK 3 S21: -0.0267 S22: -0.0234 S23: -0.0106
REMARK 3 S31: -0.0193 S32: 0.0017 S33: -0.0001
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: ((chain XA and (resid 2:8 or resid 27:557)) or
REMARK 3 (chain XD and resid 1:205) or (chain XP and resid 1:
REMARK 3 82) or (chain XT and resid 2:86) or (chain XL and
REMARK 3 resid 22:123) or (chain ZU and (resid 299 or resid
REMARK 3 315 or resid 362 or resid 417 or resid 509 or resid
REMARK 3 547 or resid 533 or resid 608 or resid 536 or resid
REMARK 3 116 or resid 352 or resid 324 or resid 100 or resid
REMARK 3 195 or resid 259 or resid 258)))
REMARK 3 ORIGIN FOR THE GROUP (A): -29.4221 34.7279 104.1461
REMARK 3 T TENSOR
REMARK 3 T11: 0.5567 T22: 0.1608
REMARK 3 T33: 0.3404 T12: 0.0140
REMARK 3 T13: -0.1431 T23: 0.0366
REMARK 3 L TENSOR
REMARK 3 L11: 0.0613 L22: 0.0902
REMARK 3 L33: 0.1125 L12: -0.0097
REMARK 3 L13: -0.0376 L23: 0.0252
REMARK 3 S TENSOR
REMARK 3 S11: -0.0878 S12: -0.0573 S13: -0.1542
REMARK 3 S21: 0.0584 S22: 0.0246 S23: -0.0133
REMARK 3 S31: 0.0145 S32: 0.1037 S33: -0.0032
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: ((chain XA and (resid 9:26 or resid 558:562 or resid
REMARK 3 564:566 or resid 914:925 or resid 1391:1396)) or
REMARK 3 (chain XL and resid 1:21) or (chain ZU and (resid 21
REMARK 3 or resid 560)))
REMARK 3 ORIGIN FOR THE GROUP (A): -41.1884 81.7420 75.6394
REMARK 3 T TENSOR
REMARK 3 T11: 0.3412 T22: 0.2422
REMARK 3 T33: 0.2494 T12: -0.0901
REMARK 3 T13: -0.1012 T23: 0.0105
REMARK 3 L TENSOR
REMARK 3 L11: 0.0032 L22: 0.0039
REMARK 3 L33: 0.0050 L12: 0.0043
REMARK 3 L13: 0.0045 L23: 0.0047
REMARK 3 S TENSOR
REMARK 3 S11: -0.0000 S12: 0.0059 S13: -0.0054
REMARK 3 S21: -0.0117 S22: -0.0041 S23: -0.0006
REMARK 3 S31: -0.0060 S32: -0.0115 S33: 0.0000
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: (chain XE and resid 9:73)
REMARK 3 ORIGIN FOR THE GROUP (A): -51.3590 73.7920 52.8351
REMARK 3 T TENSOR
REMARK 3 T11: 0.4050 T22: 0.3891
REMARK 3 T33: 0.3765 T12: -0.0162
REMARK 3 T13: -0.0484 T23: -0.0166
REMARK 3 L TENSOR
REMARK 3 L11: 0.0005 L22: 0.0000
REMARK 3 L33: 0.0010 L12: -0.0000
REMARK 3 L13: 0.0011 L23: 0.0003
REMARK 3 S TENSOR
REMARK 3 S11: 0.0002 S12: 0.0011 S13: -0.0004
REMARK 3 S21: 0.0017 S22: 0.0000 S23: 0.0003
REMARK 3 S31: -0.0010 S32: 0.0004 S33: 0.0000
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: (chain XE and resid 74:149)
REMARK 3 ORIGIN FOR THE GROUP (A): -34.6376 63.6062 58.3993
REMARK 3 T TENSOR
REMARK 3 T11: 0.4334 T22: 0.4066
REMARK 3 T33: 0.4245 T12: -0.0326
REMARK 3 T13: -0.0298 T23: -0.0130
REMARK 3 L TENSOR
REMARK 3 L11: 0.0004 L22: 0.0004
REMARK 3 L33: 0.0005 L12: 0.0003
REMARK 3 L13: 0.0004 L23: -0.0001
REMARK 3 S TENSOR
REMARK 3 S11: -0.0018 S12: -0.0018 S13: 0.0009
REMARK 3 S21: 0.0008 S22: -0.0016 S23: -0.0003
REMARK 3 S31: 0.0009 S32: 0.0030 S33: -0.0000
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: (chain XB and (resid 8:107 or resid 147:225))
REMARK 3 ORIGIN FOR THE GROUP (A): -31.0590 89.6693 26.5164
REMARK 3 T TENSOR
REMARK 3 T11: 0.9231 T22: 0.9124
REMARK 3 T33: 0.8991 T12: -0.0115
REMARK 3 T13: -0.0034 T23: -0.0075
REMARK 3 L TENSOR
REMARK 3 L11: 0.0008 L22: 0.0009
REMARK 3 L33: 0.0010 L12: -0.0002
REMARK 3 L13: -0.0003 L23: -0.0003
REMARK 3 S TENSOR
REMARK 3 S11: 0.0035 S12: 0.0032 S13: 0.0003
REMARK 3 S21: -0.0030 S22: 0.0023 S23: -0.0012
REMARK 3 S31: 0.0006 S32: -0.0037 S33: 0.0000
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: (chain XB and resid 108:146)
REMARK 3 ORIGIN FOR THE GROUP (A): -62.0554 96.6575 21.7540
REMARK 3 T TENSOR
REMARK 3 T11: 1.3379 T22: 1.3345
REMARK 3 T33: 1.3338 T12: -0.0006
REMARK 3 T13: -0.0026 T23: -0.0002
REMARK 3 L TENSOR
REMARK 3 L11: 0.0001 L22: 0.0002
REMARK 3 L33: 0.0002 L12: 0.0000
REMARK 3 L13: 0.0001 L23: 0.0000
REMARK 3 S TENSOR
REMARK 3 S11: -0.0001 S12: 0.0003 S13: 0.0008
REMARK 3 S21: 0.0005 S22: -0.0003 S23: 0.0006
REMARK 3 S31: -0.0001 S32: 0.0001 S33: -0.0000
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: ((chain XA and (resid 926:986 or resid 1048:1390))
REMARK 3 or (chain XC and resid 1:206) or (chain XG and resid
REMARK 3 1:151) or (chain XI and resid 3:129) or (chain XJ and
REMARK 3 resid 5:102) or (chain XM and resid 1:114) or (chain
REMARK 3 XN and resid 1:100) or (chain XS and resid 2:80) or
REMARK 3 (chain ZU and (resid 934 or resid 937 or resid 980 or
REMARK 3 resid 1048 or resid 1076 or resid 1054 or resid 1303
REMARK 3 or resid 1386 or resid 964 or resid 1222 or resid
REMARK 3 1110 or resid 1108)))
REMARK 3 ORIGIN FOR THE GROUP (A): -95.5129 114.7187 55.3982
REMARK 3 T TENSOR
REMARK 3 T11: 0.5646 T22: 0.4630
REMARK 3 T33: 0.5219 T12: -0.1055
REMARK 3 T13: -0.1779 T23: 0.1207
REMARK 3 L TENSOR
REMARK 3 L11: 0.0386 L22: 0.0176
REMARK 3 L33: 0.0165 L12: -0.0178
REMARK 3 L13: 0.0197 L23: 0.0054
REMARK 3 S TENSOR
REMARK 3 S11: -0.0398 S12: -0.0102 S13: 0.0503
REMARK 3 S21: 0.0494 S22: 0.0194 S23: 0.0670
REMARK 3 S31: 0.0109 S32: -0.0425 S33: -0.0000
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: (chain XA and resid 987:1047)
REMARK 3 ORIGIN FOR THE GROUP (A):-125.7223 75.3189 74.0612
REMARK 3 T TENSOR
REMARK 3 T11: 2.0380 T22: 2.0412
REMARK 3 T33: 2.0409 T12: -0.0085
REMARK 3 T13: -0.0015 T23: 0.0096
REMARK 3 L TENSOR
REMARK 3 L11: 0.0002 L22: 0.0003
REMARK 3 L33: 0.0004 L12: -0.0002
REMARK 3 L13: -0.0001 L23: -0.0006
REMARK 3 S TENSOR
REMARK 3 S11: 0.0019 S12: 0.0022 S13: -0.0027
REMARK 3 S21: -0.0007 S22: -0.0043 S23: 0.0050
REMARK 3 S31: 0.0002 S32: -0.0020 S33: 0.0000
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: ((chain XA and (resid 563 or resid 567:913 or resid
REMARK 3 1496:1530)) or (chain XF and resid 1:100) or (chain
REMARK 3 XH and resid 1:129) or (chain XK and resid 12:128) or
REMARK 3 (chain XO and resid 1:88) or (chain XR and resid 19:
REMARK 3 73) or (chain XU and resid 3:53) or (chain ZU and
REMARK 3 (resid 572 or resid 578 or resid 593 or resid 770 or
REMARK 3 resid 814 or resid 891 or resid 1500 or resid 1499 or
REMARK 3 resid 781 or resid 869 or resid 1525)))
REMARK 3 ORIGIN FOR THE GROUP (A): -15.2210 106.2725 76.3150
REMARK 3 T TENSOR
REMARK 3 T11: 0.6625 T22: 0.2589
REMARK 3 T33: 0.2853 T12: -0.3041
REMARK 3 T13: -0.1502 T23: 0.0115
REMARK 3 L TENSOR
REMARK 3 L11: 0.1335 L22: 0.0483
REMARK 3 L33: 0.0849 L12: 0.0382
REMARK 3 L13: 0.0568 L23: -0.0181
REMARK 3 S TENSOR
REMARK 3 S11: 0.0339 S12: 0.0224 S13: -0.0363
REMARK 3 S21: 0.0257 S22: -0.0883 S23: -0.1442
REMARK 3 S31: -0.0858 S32: 0.0613 S33: -0.0009
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: ((chain XA and resid 1397:1495) or (chain ZU and
REMARK 3 (resid 1417 or resid 8201)))
REMARK 3 ORIGIN FOR THE GROUP (A): -22.8696 69.1828 123.7988
REMARK 3 T TENSOR
REMARK 3 T11: 0.6075 T22: 0.5276
REMARK 3 T33: 0.4960 T12: -0.0239
REMARK 3 T13: -0.1110 T23: 0.0583
REMARK 3 L TENSOR
REMARK 3 L11: 0.0121 L22: 0.0349
REMARK 3 L33: 0.0175 L12: 0.0232
REMARK 3 L13: 0.0098 L23: 0.0262
REMARK 3 S TENSOR
REMARK 3 S11: -0.0427 S12: -0.0061 S13: -0.0296
REMARK 3 S21: -0.0214 S22: 0.0274 S23: -0.0244
REMARK 3 S31: 0.0061 S32: 0.0473 S33: 0.0000
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: ((chain RA and (resid 1:876 or resid 902:1038 or
REMARK 3 resid 1116:1905 or resid 1930:2092 or resid 2198:2296
REMARK 3 or resid 2322:2903)) or (chain RC and resid 1:271) or
REMARK 3 (chain RS and resid 1:110) or (chain RT and resid 1:
REMARK 3 93) or (chain RU and resid 1:102) or (chain RD and
REMARK 3 resid 1:209) or (chain RE and resid 1:201) or (chain
REMARK 3 RG and resid 1:176) or (chain RJ and resid 1:142) or
REMARK 3 (chain RK and resid 1:122) or (chain RL and resid 2:
REMARK 3 144) or (chain RM and resid 1:136) or (chain RN and
REMARK 3 resid 1:120) or (chainR
REMARK 3 ORIGIN FOR THE GROUP (A): -65.3390 -59.5004 15.1820
REMARK 3 T TENSOR
REMARK 3 T11: -0.0979 T22: 0.0155
REMARK 3 T33: 0.0325 T12: -0.0141
REMARK 3 T13: -0.0824 T23: -0.0201
REMARK 3 L TENSOR
REMARK 3 L11: 0.1974 L22: 0.1530
REMARK 3 L33: 0.0851 L12: -0.0100
REMARK 3 L13: -0.0663 L23: 0.0075
REMARK 3 S TENSOR
REMARK 3 S11: -0.0089 S12: -0.0227 S13: 0.0300
REMARK 3 S21: 0.0808 S22: 0.0121 S23: -0.0499
REMARK 3 S31: -0.0325 S32: 0.0138 S33: -0.0518
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: ((chain RA and resid 1039:1115) or (chain RI and
REMARK 3 resid 1:141))
REMARK 3 ORIGIN FOR THE GROUP (A):-139.1133 -50.5317 -63.3635
REMARK 3 T TENSOR
REMARK 3 T11: 0.2865 T22: 0.3149
REMARK 3 T33: 0.3499 T12: -0.0034
REMARK 3 T13: -0.0558 T23: 0.0534
REMARK 3 L TENSOR
REMARK 3 L11: 0.0146 L22: 0.0028
REMARK 3 L33: 0.0056 L12: 0.0044
REMARK 3 L13: 0.0106 L23: -0.0027
REMARK 3 S TENSOR
REMARK 3 S11: 0.0410 S12: -0.0250 S13: -0.0065
REMARK 3 S21: -0.0132 S22: 0.0235 S23: -0.0148
REMARK 3 S31: -0.0117 S32: -0.0078 S33: -0.0000
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: (chain RA and resid 1906:1929)
REMARK 3 ORIGIN FOR THE GROUP (A):-103.1497 -3.8306 -3.3464
REMARK 3 T TENSOR
REMARK 3 T11: 0.3193 T22: 0.3377
REMARK 3 T33: 0.3221 T12: -0.0077
REMARK 3 T13: 0.0093 T23: 0.0062
REMARK 3 L TENSOR
REMARK 3 L11: 0.0011 L22: 0.0001
REMARK 3 L33: 0.0002 L12: -0.0005
REMARK 3 L13: -0.0002 L23: -0.0001
REMARK 3 S TENSOR
REMARK 3 S11: -0.0034 S12: -0.0049 S13: 0.0024
REMARK 3 S21: -0.0057 S22: 0.0043 S23: 0.0042
REMARK 3 S31: -0.0002 S32: -0.0005 S33: -0.0000
REMARK 3 TLS GROUP : 24
REMARK 3 SELECTION: (chain RA and resid 2093:2197)
REMARK 3 ORIGIN FOR THE GROUP (A): -94.9282 19.4761 79.1891
REMARK 3 T TENSOR
REMARK 3 T11: 0.4638 T22: 0.4565
REMARK 3 T33: 0.4634 T12: 0.0042
REMARK 3 T13: 0.0101 T23: -0.0221
REMARK 3 L TENSOR
REMARK 3 L11: 0.0023 L22: 0.0026
REMARK 3 L33: 0.0023 L12: 0.0027
REMARK 3 L13: 0.0025 L23: 0.0035
REMARK 3 S TENSOR
REMARK 3 S11: 0.0038 S12: 0.0013 S13: -0.0074
REMARK 3 S21: -0.0007 S22: 0.0186 S23: 0.0034
REMARK 3 S31: -0.0079 S32: -0.0146 S33: 0.0000
REMARK 3 TLS GROUP : 25
REMARK 3 SELECTION: (chain RA and resid 877:901)
REMARK 3 ORIGIN FOR THE GROUP (A):-148.4924 -27.2211 -12.1955
REMARK 3 T TENSOR
REMARK 3 T11: 1.0791 T22: 1.0674
REMARK 3 T33: 1.0760 T12: 0.0021
REMARK 3 T13: 0.0056 T23: 0.0019
REMARK 3 L TENSOR
REMARK 3 L11: 0.0002 L22: 0.0001
REMARK 3 L33: 0.0003 L12: -0.0001
REMARK 3 L13: -0.0003 L23: 0.0001
REMARK 3 S TENSOR
REMARK 3 S11: -0.0013 S12: 0.0015 S13: 0.0023
REMARK 3 S21: 0.0012 S22: -0.0013 S23: 0.0007
REMARK 3 S31: 0.0014 S32: -0.0003 S33: -0.0000
REMARK 3 TLS GROUP : 26
REMARK 3 SELECTION: ((chain RA and resid 2297:2321) or (chain RF and
REMARK 3 resid 1:177) or (chain ZR and resid 2304))
REMARK 3 ORIGIN FOR THE GROUP (A):-165.7519 -23.4158 16.2248
REMARK 3 T TENSOR
REMARK 3 T11: 0.2408 T22: 0.3121
REMARK 3 T33: 0.3528 T12: -0.0141
REMARK 3 T13: 0.0161 T23: 0.0166
REMARK 3 L TENSOR
REMARK 3 L11: 0.0049 L22: 0.0067
REMARK 3 L33: 0.0034 L12: 0.0009
REMARK 3 L13: 0.0007 L23: -0.0028
REMARK 3 S TENSOR
REMARK 3 S11: -0.0021 S12: 0.0111 S13: -0.0047
REMARK 3 S21: -0.0008 S22: 0.0084 S23: 0.0039
REMARK 3 S31: -0.0244 S32: 0.0116 S33: -0.0000
REMARK 3 TLS GROUP : 27
REMARK 3 SELECTION: ((chain RB and (resid 2:69 or resid 108:119)) or
REMARK 3 (chain RO and resid 2:117))
REMARK 3 ORIGIN FOR THE GROUP (A):-174.1428 -53.7098 30.2781
REMARK 3 T TENSOR
REMARK 3 T11: 0.0951 T22: 0.2711
REMARK 3 T33: 0.3213 T12: 0.0369
REMARK 3 T13: 0.1041 T23: 0.0088
REMARK 3 L TENSOR
REMARK 3 L11: 0.0168 L22: 0.0037
REMARK 3 L33: 0.0063 L12: -0.0077
REMARK 3 L13: -0.0033 L23: -0.0001
REMARK 3 S TENSOR
REMARK 3 S11: 0.0175 S12: -0.0009 S13: -0.0070
REMARK 3 S21: 0.0118 S22: -0.0277 S23: 0.0221
REMARK 3 S31: -0.0039 S32: -0.0036 S33: -0.0000
REMARK 3 TLS GROUP : 28
REMARK 3 SELECTION: ((chain RB and resid 70:107) or (chain RV and resid
REMARK 3 1:94) or (chain ZR and resid 6095:6100))
REMARK 3 ORIGIN FOR THE GROUP (A):-143.2501 -80.0193 -7.7824
REMARK 3 T TENSOR
REMARK 3 T11: -0.0079 T22: 0.1193
REMARK 3 T33: 0.1436 T12: -0.0036
REMARK 3 T13: -0.0163 T23: -0.0591
REMARK 3 L TENSOR
REMARK 3 L11: 0.0057 L22: 0.0108
REMARK 3 L33: 0.0079 L12: 0.0015
REMARK 3 L13: 0.0017 L23: -0.0027
REMARK 3 S TENSOR
REMARK 3 S11: -0.0167 S12: -0.0009 S13: 0.0070
REMARK 3 S21: -0.0159 S22: -0.0039 S23: 0.0111
REMARK 3 S31: 0.0004 S32: -0.0076 S33: -0.0002
REMARK 3 TLS GROUP : 29
REMARK 3 SELECTION: (chain RH and resid 49:149)
REMARK 3 ORIGIN FOR THE GROUP (A): -64.8094 20.5731 122.1096
REMARK 3 T TENSOR
REMARK 3 T11: 0.9082 T22: 0.9060
REMARK 3 T33: 0.8998 T12: -0.0055
REMARK 3 T13: 0.0029 T23: -0.0088
REMARK 3 L TENSOR
REMARK 3 L11: 0.0003 L22: 0.0004
REMARK 3 L33: 0.0010 L12: 0.0002
REMARK 3 L13: -0.0006 L23: -0.0006
REMARK 3 S TENSOR
REMARK 3 S11: 0.0021 S12: -0.0022 S13: 0.0058
REMARK 3 S21: 0.0002 S22: -0.0002 S23: 0.0014
REMARK 3 S31: -0.0052 S32: -0.0012 S33: 0.0000
REMARK 3 TLS GROUP : 30
REMARK 3 SELECTION: ((chain YA and (resid 1:876 or resid 902:1038 or
REMARK 3 resid 1116:1905 or resid 1930:2092 or resid 2198:2296
REMARK 3 or resid 2322:2903)) or (chain YC and resid 1:271) or
REMARK 3 (chain YS and resid 1:110) or (chain YT and resid 1:
REMARK 3 93) or (chain YU and resid 1:102) or (chain YD and
REMARK 3 resid 1:209) or (chain YE and resid 1:201) or (chain
REMARK 3 YG and resid 1:176) or (chain YJ and resid 1:142) or
REMARK 3 (chain YK and resid 1:122) or (chain YL and resid 2:
REMARK 3 144) or (chain YM and resid 1:136) or (chain YN and
REMARK 3 resid 1:120) or (chain YP and resid 1:114) or (chain
REMARK 3 YQ and resid 1:117) or (chain YR and resid 1:103) or
REMARK 3 (chain YW and resid 6:84) or (chain YY and resid 1:
REMARK 3 63) or (chain YZ and resid 1:58) or (chain YX and
REMARK 3 resid 1:77) or (chain Y0 and resid 1:56) or (chain Y1
REMARK 3 and resid 3:52) or (chain Y2 and resid 1:46) or
REMARK 3 (chain Y3 and resid 1:64) or (chain Y4 and resid 1:
REMARK 3 38) or (chain YH and resid 1:48) or (chain ZT and not
REMARK 3 (resid 9501 or resid 2304 or resid 6095:6100)))
REMARK 3 ORIGIN FOR THE GROUP (A): -29.9774 131.0416 171.2268
REMARK 3 T TENSOR
REMARK 3 T11: 0.5845 T22: 0.4357
REMARK 3 T33: -0.3023 T12: -0.2750
REMARK 3 T13: -0.2459 T23: -0.3820
REMARK 3 L TENSOR
REMARK 3 L11: -0.1114 L22: 0.0897
REMARK 3 L33: 0.4354 L12: -0.0036
REMARK 3 L13: -0.1654 L23: -0.0364
REMARK 3 S TENSOR
REMARK 3 S11: -0.1047 S12: -0.4462 S13: 0.0811
REMARK 3 S21: 0.2695 S22: 0.3376 S23: 0.1212
REMARK 3 S31: -0.2100 S32: 0.3553 S33: 0.2834
REMARK 3 TLS GROUP : 31
REMARK 3 SELECTION: ((chain YA and resid 1039:1115) or (chain YI and
REMARK 3 resid 1:141))
REMARK 3 ORIGIN FOR THE GROUP (A):-116.7923 71.8792 150.6018
REMARK 3 T TENSOR
REMARK 3 T11: 1.8491 T22: 1.8718
REMARK 3 T33: 1.8613 T12: -0.0079
REMARK 3 T13: 0.0058 T23: -0.0083
REMARK 3 L TENSOR
REMARK 3 L11: 0.0051 L22: 0.0011
REMARK 3 L33: 0.0017 L12: 0.0019
REMARK 3 L13: 0.0005 L23: -0.0002
REMARK 3 S TENSOR
REMARK 3 S11: 0.0066 S12: 0.0005 S13: 0.0077
REMARK 3 S21: -0.0075 S22: 0.0013 S23: 0.0020
REMARK 3 S31: 0.0021 S32: 0.0026 S33: 0.0000
REMARK 3 TLS GROUP : 32
REMARK 3 SELECTION: (chain YA and resid 1906:1929)
REMARK 3 ORIGIN FOR THE GROUP (A): -60.3188 115.4696 110.4409
REMARK 3 T TENSOR
REMARK 3 T11: 0.7494 T22: 0.7341
REMARK 3 T33: 0.7307 T12: -0.0363
REMARK 3 T13: 0.0117 T23: -0.0166
REMARK 3 L TENSOR
REMARK 3 L11: 0.0002 L22: 0.0002
REMARK 3 L33: 0.0013 L12: 0.0001
REMARK 3 L13: -0.0007 L23: -0.0001
REMARK 3 S TENSOR
REMARK 3 S11: -0.0007 S12: -0.0015 S13: 0.0029
REMARK 3 S21: 0.0006 S22: -0.0007 S23: 0.0002
REMARK 3 S31: -0.0055 S32: 0.0035 S33: 0.0000
REMARK 3 TLS GROUP : 33
REMARK 3 SELECTION: (chain YA and resid 2093:2197)
REMARK 3 ORIGIN FOR THE GROUP (A): -28.4999 193.3428 90.9371
REMARK 3 T TENSOR
REMARK 3 T11: 1.1781 T22: 1.1841
REMARK 3 T33: 1.1814 T12: 0.0055
REMARK 3 T13: 0.0229 T23: -0.0022
REMARK 3 L TENSOR
REMARK 3 L11: 0.0007 L22: -0.0001
REMARK 3 L33: 0.0006 L12: -0.0014
REMARK 3 L13: -0.0005 L23: -0.0011
REMARK 3 S TENSOR
REMARK 3 S11: -0.0061 S12: 0.0018 S13: 0.0072
REMARK 3 S21: -0.0054 S22: -0.0076 S23: 0.0095
REMARK 3 S31: -0.0027 S32: -0.0096 S33: 0.0000
REMARK 3 TLS GROUP : 34
REMARK 3 SELECTION: (chain YA and resid 877:901)
REMARK 3 ORIGIN FOR THE GROUP (A):-110.1845 124.9269 132.4728
REMARK 3 T TENSOR
REMARK 3 T11: 1.6685 T22: 1.6691
REMARK 3 T33: 1.6712 T12: 0.0002
REMARK 3 T13: -0.0001 T23: -0.0028
REMARK 3 L TENSOR
REMARK 3 L11: 0.0001 L22: 0.0001
REMARK 3 L33: 0.0002 L12: 0.0001
REMARK 3 L13: 0.0000 L23: 0.0000
REMARK 3 S TENSOR
REMARK 3 S11: -0.0003 S12: -0.0001 S13: 0.0006
REMARK 3 S21: -0.0001 S22: -0.0003 S23: -0.0004
REMARK 3 S31: -0.0002 S32: -0.0000 S33: 0.0000
REMARK 3 TLS GROUP : 35
REMARK 3 SELECTION: ((chain YA and resid 2297:2321) or (chain YF and
REMARK 3 resid 1:177) or (chain ZT and resid 2304))
REMARK 3 ORIGIN FOR THE GROUP (A):-121.2676 152.1967 116.6719
REMARK 3 T TENSOR
REMARK 3 T11: 1.5314 T22: 1.5395
REMARK 3 T33: 1.5370 T12: 0.0035
REMARK 3 T13: 0.0016 T23: 0.0020
REMARK 3 L TENSOR
REMARK 3 L11: 0.0017 L22: 0.0016
REMARK 3 L33: 0.0013 L12: 0.0002
REMARK 3 L13: -0.0003 L23: 0.0001
REMARK 3 S TENSOR
REMARK 3 S11: -0.0024 S12: 0.0011 S13: 0.0017
REMARK 3 S21: -0.0031 S22: -0.0026 S23: 0.0002
REMARK 3 S31: -0.0002 S32: 0.0002 S33: 0.0000
REMARK 3 TLS GROUP : 36
REMARK 3 SELECTION: ((chain YB and (resid 2:69 or resid 108:119)) or
REMARK 3 (chain YO and resid 2:117))
REMARK 3 ORIGIN FOR THE GROUP (A):-129.0977 170.5821 144.0762
REMARK 3 T TENSOR
REMARK 3 T11: 1.2921 T22: 1.3005
REMARK 3 T33: 1.3116 T12: 0.0557
REMARK 3 T13: 0.0122 T23: 0.0437
REMARK 3 L TENSOR
REMARK 3 L11: 0.0045 L22: 0.0020
REMARK 3 L33: 0.0003 L12: -0.0033
REMARK 3 L13: -0.0010 L23: -0.0005
REMARK 3 S TENSOR
REMARK 3 S11: -0.0019 S12: -0.0008 S13: -0.0023
REMARK 3 S21: -0.0036 S22: 0.0009 S23: 0.0066
REMARK 3 S31: -0.0019 S32: -0.0022 S33: -0.0000
REMARK 3 TLS GROUP : 37
REMARK 3 SELECTION: ((chain YB and resid 70:107) or (chain YV and resid
REMARK 3 1:94) or (chain ZT and resid 6095:6100))
REMARK 3 ORIGIN FOR THE GROUP (A):-113.4768 128.5463 177.2528
REMARK 3 T TENSOR
REMARK 3 T11: 0.7849 T22: 0.8208
REMARK 3 T33: 0.7954 T12: 0.0349
REMARK 3 T13: 0.0217 T23: 0.0512
REMARK 3 L TENSOR
REMARK 3 L11: 0.0023 L22: 0.0010
REMARK 3 L33: 0.0032 L12: 0.0006
REMARK 3 L13: -0.0021 L23: -0.0020
REMARK 3 S TENSOR
REMARK 3 S11: -0.0064 S12: 0.0086 S13: 0.0029
REMARK 3 S21: 0.0011 S22: -0.0028 S23: 0.0005
REMARK 3 S31: 0.0060 S32: -0.0055 S33: 0.0000
REMARK 3 TLS GROUP : 38
REMARK 3 SELECTION: (chain YH and resid 49:149)
REMARK 3 ORIGIN FOR THE GROUP (A): 11.7147 227.2670 88.7920
REMARK 3 T TENSOR
REMARK 3 T11: 0.9318 T22: 0.9199
REMARK 3 T33: 0.9233 T12: 0.0046
REMARK 3 T13: 0.0092 T23: 0.0027
REMARK 3 L TENSOR
REMARK 3 L11: 0.0004 L22: 0.0013
REMARK 3 L33: 0.0003 L12: -0.0005
REMARK 3 L13: -0.0001 L23: 0.0004
REMARK 3 S TENSOR
REMARK 3 S11: -0.0007 S12: 0.0040 S13: 0.0032
REMARK 3 S21: -0.0030 S22: -0.0030 S23: 0.0005
REMARK 3 S31: -0.0014 S32: -0.0010 S33: -0.0000
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 3OAR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-AUG-10.
REMARK 100 THE RCSB ID CODE IS RCSB060879.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.3.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 801811
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.250
REMARK 200 RESOLUTION RANGE LOW (A) : 100.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 91.2
REMARK 200 DATA REDUNDANCY : 2.500
REMARK 200 R MERGE (I) : 0.08300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.25
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.31
REMARK 200 COMPLETENESS FOR SHELL (%) : 81.1
REMARK 200 DATA REDUNDANCY IN SHELL : 1.80
REMARK 200 R MERGE FOR SHELL (I) : 0.45500
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: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: PDB ENTRY 3I1M, 3I1N, 3I1O, 3I1P
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG8K, MPD, PH 6.5, MICROBATCH,
REMARK 280 TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 105.37950
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 309.43150
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 216.63600
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 309.43150
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 105.37950
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 216.63600
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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 300 REMARK: THERE ARE 2 BIOLOGICAL UNITS IN THE ASSYMETRIC UNIT.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 21-MERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I,
REMARK 350 AND CHAINS: J, K, L, M, N, O, P, Q, R,
REMARK 350 AND CHAINS: S, T, U
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 ALA N 35
REMARK 465 SER N 36
REMARK 465 ASP N 37
REMARK 465 GLU N 38
REMARK 465 ASP N 39
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 O2' U A 701 OP2 A A 702 1.84
REMARK 500 O2' G A 1047 OP1 A A 1216 1.94
REMARK 500 O2' G A 1138 OP1 G A 1139 2.03
REMARK 500 O2' A A 533 OP2 A A 535 2.05
REMARK 500 O2' A A 974 OP1 A A 975 2.07
REMARK 500 O2' C A 330 O5' G A 331 2.09
REMARK 500 OP1 C A 536 O HOH A 1761 2.09
REMARK 500 O2' U A 89 O4' C A 90 2.09
REMARK 500 O2' G A 1242 O4' C A 1243 2.10
REMARK 500 O6 G A 1160 O6 G A 1181 2.11
REMARK 500 O2' G A 1242 O5' C A 1243 2.11
REMARK 500 O2' G A 86 OP2 C A 87 2.12
REMARK 500 O2' U A 1451 OP1 C A 1452 2.15
REMARK 500 O2' U A 1183 OP1 G A 1184 2.17
REMARK 500 O2' C A 1051 O5' U A 1052 2.17
REMARK 500 O GLU D 34 N ALA D 36 2.18
REMARK 500 O2' A A 1151 O5' A A 1152 2.18
REMARK 500 O2' A A 704 O5' G A 705 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 A A1396 O3' C A1397 P -0.160
REMARK 500 ARG B 107 C GLN B 108 N 0.145
REMARK 500 THR O 78 C GLN O 79 N 0.144
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 C A 210 C6 - N1 - C1' ANGL. DEV. = -7.6 DEGREES
REMARK 500 C A 210 C2 - N1 - C1' ANGL. DEV. = 8.5 DEGREES
REMARK 500 G A 251 C8 - N9 - C1' ANGL. DEV. = -8.8 DEGREES
REMARK 500 G A 251 C4 - N9 - C1' ANGL. DEV. = 10.0 DEGREES
REMARK 500 C A 316 C6 - N1 - C2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 C A 328 C6 - N1 - C2 ANGL. DEV. = -2.7 DEGREES
REMARK 500 C A 381 C2 - N1 - C1' ANGL. DEV. = 8.2 DEGREES
REMARK 500 G A 765 C4 - N9 - C1' ANGL. DEV. = 8.0 DEGREES
REMARK 500 C A 962 C6 - N1 - C2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 ARG B 107 O - C - N ANGL. DEV. = -11.9 DEGREES
REMARK 500 SER B 146 CA - C - N ANGL. DEV. = 16.5 DEGREES
REMARK 500 SER B 146 O - C - N ANGL. DEV. = -17.3 DEGREES
REMARK 500 LEU B 147 C - N - CA ANGL. DEV. = 17.5 DEGREES
REMARK 500 PRO D 167 C - N - CA ANGL. DEV. = 9.4 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 LEU B 9 -71.70 -96.45
REMARK 500 LYS B 10 -16.11 80.13
REMARK 500 ALA B 11 55.38 -91.20
REMARK 500 HIS B 17 -140.96 -114.31
REMARK 500 GLN B 18 105.09 64.67
REMARK 500 THR B 19 -75.42 -90.85
REMARK 500 ARG B 20 30.96 -99.90
REMARK 500 LYS B 25 49.48 -81.24
REMARK 500 MET B 26 2.79 -156.18
REMARK 500 LYS B 36 43.42 36.59
REMARK 500 PHE B 49 -6.73 -141.43
REMARK 500 ALA B 52 -53.83 -121.35
REMARK 500 SER B 61 37.82 -75.39
REMARK 500 LYS B 72 115.53 -34.60
REMARK 500 ARG B 73 -34.94 -35.30
REMARK 500 ASP B 81 -102.51 13.43
REMARK 500 LEU B 84 77.77 -56.18
REMARK 500 SER B 85 -52.94 -169.90
REMARK 500 CYS B 86 179.38 -57.93
REMARK 500 GLN B 88 -163.59 -163.88
REMARK 500 HIS B 93 -139.03 -85.24
REMARK 500 THR B 101 39.32 -75.34
REMARK 500 ASN B 102 18.18 170.08
REMARK 500 ARG B 107 11.38 -68.94
REMARK 500 ARG B 112 3.79 -69.51
REMARK 500 LEU B 128 92.73 49.16
REMARK 500 THR B 129 -91.94 -3.20
REMARK 500 LEU B 134 -66.55 -141.12
REMARK 500 THR B 137 -45.09 -141.15
REMARK 500 ILE B 150 -10.25 179.72
REMARK 500 PRO B 157 -178.96 -66.71
REMARK 500 ALA B 159 149.67 -175.66
REMARK 500 ILE B 163 -84.06 -78.35
REMARK 500 ASN B 177 11.53 -65.51
REMARK 500 LEU B 178 -77.21 -109.88
REMARK 500 THR B 188 -1.49 -56.65
REMARK 500 PRO B 200 98.71 -44.41
REMARK 500 ASN B 202 -154.57 -120.81
REMARK 500 ASP B 203 -3.04 -168.15
REMARK 500 ALA B 205 104.53 60.59
REMARK 500 ALA B 208 -23.30 -155.30
REMARK 500 ALA B 218 -62.13 -160.00
REMARK 500 GLU B 222 9.27 -66.19
REMARK 500 GLN C 2 -74.05 -29.94
REMARK 500 ARG C 10 35.31 -90.63
REMARK 500 LEU C 11 -73.86 -83.94
REMARK 500 LYS C 15 138.84 -172.30
REMARK 500 SER C 19 73.37 -111.28
REMARK 500 THR C 20 41.17 -85.19
REMARK 500 ASN C 24 -129.10 -76.97
REMARK 500
REMARK 500 THIS ENTRY HAS 446 RAMACHANDRAN OUTLIERS.
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 A1558 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A1697 O
REMARK 620 2 HOH A1700 O 89.8
REMARK 620 3 HOH A1699 O 87.7 90.9
REMARK 620 4 HOH A1698 O 179.8 90.2 92.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1565 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A1731 O
REMARK 620 2 HOH A1729 O 89.0
REMARK 620 3 HOH A1728 O 89.9 178.8
REMARK 620 4 HOH A1730 O 90.7 89.4 91.1
REMARK 620 5 U A 516 O4 71.6 90.4 88.8 162.3
REMARK 620 6 A A 533 OP1 152.4 69.0 111.9 105.0 91.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1538 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A1597 O
REMARK 620 2 HOH A1596 O 89.4
REMARK 620 3 HOH A1594 O 89.0 91.0
REMARK 620 4 HOH A1595 O 90.4 88.5 179.1
REMARK 620 5 A A 510 OP2 73.0 144.2 118.8 61.5
REMARK 620 6 A A 509 OP2 156.3 77.8 110.9 69.7 106.2
REMARK 620 7 A A 509 O5' 141.3 129.3 90.7 90.2 73.4 54.6
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1545 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A1628 O
REMARK 620 2 HOH A1629 O 179.7
REMARK 620 3 HOH A1631 O 91.0 89.2
REMARK 620 4 HOH A1630 O 89.0 90.7 89.5
REMARK 620 5 A A 814 OP2 85.2 95.1 75.1 163.4
REMARK 620 6 G A 577 OP2 82.9 96.8 147.0 58.1 136.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1571 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A1757 O
REMARK 620 2 HOH A1758 O 90.4
REMARK 620 3 HOH A1755 O 90.2 90.0
REMARK 620 4 HOH A1756 O 89.9 90.3 179.6
REMARK 620 5 A A 195 OP2 109.5 157.6 80.1 99.5
REMARK 620 6 U A 180 O4 164.2 90.9 74.1 105.8 67.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1569 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A1748 O
REMARK 620 2 HOH A1749 O 84.9
REMARK 620 3 HOH A1747 O 92.7 93.9
REMARK 620 4 A A1500 OP2 97.5 77.5 165.9
REMARK 620 5 G A1505 OP2 67.6 134.7 121.6 71.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1563 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH E 187 O
REMARK 620 2 HOH A1722 O 179.4
REMARK 620 3 HOH A1720 O 90.0 89.6
REMARK 620 4 HOH A1721 O 90.3 90.1 177.7
REMARK 620 5 G A 558 OP1 110.4 70.3 111.4 66.4
REMARK 620 6 G A 299 O6 94.6 85.2 123.3 59.0 119.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1561 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A1711 O
REMARK 620 2 HOH A1713 O 89.0
REMARK 620 3 HOH A1712 O 178.8 90.7
REMARK 620 4 HOH A1714 O 89.9 91.8 91.2
REMARK 620 5 G A1198 OP1 92.0 93.6 86.9 174.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1551 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A1659 O
REMARK 620 2 HOH A1656 O 90.3
REMARK 620 3 HOH A1657 O 90.2 178.9
REMARK 620 4 HOH A1658 O 89.6 91.2 89.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1572 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A1762 O
REMARK 620 2 HOH A1761 O 178.5
REMARK 620 3 HOH A1760 O 89.2 91.0
REMARK 620 4 HOH A1763 O 89.2 89.3 90.8
REMARK 620 5 HOH A1759 O 90.1 89.7 178.9 90.1
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1539 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A1601 O
REMARK 620 2 HOH A1600 O 178.6
REMARK 620 3 HOH A1599 O 92.4 88.0
REMARK 620 4 HOH A1602 O 88.2 93.1 89.0
REMARK 620 5 HOH A1598 O 88.5 91.1 178.9 91.8
REMARK 620 6 A A 547 OP1 86.6 92.0 102.8 167.3 76.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1574 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A1768 O
REMARK 620 2 HOH A1771 O 89.1
REMARK 620 3 HOH A1767 O 178.3 89.2
REMARK 620 4 HOH A1770 O 89.3 90.6 91.0
REMARK 620 5 HOH A1769 O 90.5 90.6 89.3 178.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1557 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A1694 O
REMARK 620 2 HOH A1695 O 178.3
REMARK 620 3 HOH A1696 O 91.7 90.0
REMARK 620 4 HOH A1693 O 89.4 90.9 89.8
REMARK 620 5 HOH A1692 O 90.3 89.4 89.9 179.5
REMARK 620 6 G A 21 OP1 62.3 116.1 139.6 118.2 62.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1542 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A1614 O
REMARK 620 2 HOH A1612 O 87.7
REMARK 620 3 HOH A1615 O 88.4 90.0
REMARK 620 4 HOH A1613 O 176.7 90.8 94.5
REMARK 620 5 HOH A1611 O 92.3 179.9 89.9 89.2
REMARK 620 6 C A 578 OP1 91.2 108.9 161.1 86.5 71.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1566 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A1733 O
REMARK 620 2 HOH A1735 O 89.7
REMARK 620 3 HOH A1736 O 89.4 86.3
REMARK 620 4 HOH A1732 O 178.4 91.9 90.7
REMARK 620 5 HOH A1734 O 90.3 179.9 93.8 88.1
REMARK 620 6 A A 608 OP2 121.6 57.3 128.7 59.4 122.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1548 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A1642 O
REMARK 620 2 HOH A1645 O 89.6
REMARK 620 3 HOH A1646 O 89.7 91.0
REMARK 620 4 HOH A1644 O 89.9 179.0 89.9
REMARK 620 5 HOH A1643 O 179.6 90.2 90.7 90.3
REMARK 620 6 A A 937 OP2 86.5 104.4 164.1 74.7 93.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1567 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A1738 O
REMARK 620 2 HOH A1739 O 89.7
REMARK 620 3 HOH A1740 O 89.6 178.9
REMARK 620 4 HOH A1737 O 178.3 90.7 89.9
REMARK 620 5 HOH A1741 O 91.6 89.9 90.9 90.1
REMARK 620 6 A A1110 OP2 97.0 101.8 77.4 81.3 165.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1562 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A1716 O
REMARK 620 2 HOH A1717 O 88.7
REMARK 620 3 HOH A1718 O 90.9 178.9
REMARK 620 4 HOH A1719 O 89.3 90.6 90.4
REMARK 620 5 HOH A1715 O 179.5 90.8 89.6 90.9
REMARK 620 6 A A1433 OP2 72.8 85.4 93.5 161.8 106.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1546 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A1635 O
REMARK 620 2 HOH A1633 O 90.2
REMARK 620 3 HOH A1632 O 88.7 178.9
REMARK 620 4 HOH A1634 O 178.3 90.1 91.0
REMARK 620 5 HOH A1636 O 90.8 89.9 90.4 90.8
REMARK 620 6 U A 891 OP2 78.7 112.5 67.0 99.7 155.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1570 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A1754 O
REMARK 620 2 HOH A1750 O 91.0
REMARK 620 3 HOH A1751 O 89.8 179.2
REMARK 620 4 HOH A1752 O 91.1 89.2 90.7
REMARK 620 5 HOH A1753 O 91.9 90.5 89.7 177.0
REMARK 620 6 G A 100 OP2 172.0 96.9 82.3 90.5 86.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1564 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A1725 O
REMARK 620 2 HOH A1723 O 90.0
REMARK 620 3 HOH A1727 O 90.3 90.5
REMARK 620 4 HOH A1724 O 90.1 179.3 90.2
REMARK 620 5 HOH A1726 O 178.9 89.2 90.5 90.6
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1536 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A1583 O
REMARK 620 2 HOH A1584 O 179.8
REMARK 620 3 HOH A1586 O 91.0 89.2
REMARK 620 4 HOH A1587 O 90.3 89.6 90.0
REMARK 620 5 HOH A1585 O 88.5 91.3 178.8 91.0
REMARK 620 6 G A 362 O6 72.3 107.9 81.0 160.1 97.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1540 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A1605 O
REMARK 620 2 HOH A1606 O 176.6
REMARK 620 3 HOH A1603 O 91.3 90.0
REMARK 620 4 HOH A1604 O 89.5 89.2 179.2
REMARK 620 5 HOH A1607 O 91.0 92.2 86.4 93.5
REMARK 620 6 A A 560 OP2 86.3 90.5 95.1 85.1 177.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1547 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A1637 O
REMARK 620 2 HOH A1639 O 89.9
REMARK 620 3 HOH A1638 O 179.8 90.0
REMARK 620 4 HOH A1640 O 90.2 178.4 89.9
REMARK 620 5 HOH A1641 O 89.5 90.5 90.6 91.0
REMARK 620 6 C A 934 OP1 115.2 67.8 64.7 110.8 146.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1553 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A1666 O
REMARK 620 2 HOH A1668 O 91.0
REMARK 620 3 HOH A1670 O 88.9 92.3
REMARK 620 4 HOH A1669 O 90.5 178.3 88.5
REMARK 620 5 HOH A1667 O 179.5 88.6 91.5 89.9
REMARK 620 6 G A1417 O6 113.6 84.6 157.4 94.0 66.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1560 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A1707 O
REMARK 620 2 HOH A1709 O 89.5
REMARK 620 3 HOH A1710 O 89.1 90.1
REMARK 620 4 HOH I 169 O 179.2 89.8 91.2
REMARK 620 5 HOH A1708 O 90.6 178.8 91.0 90.1
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1544 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A1624 O
REMARK 620 2 HOH A1622 O 92.3
REMARK 620 3 HOH A1625 O 178.7 88.1
REMARK 620 4 HOH A1626 O 87.2 89.7 91.5
REMARK 620 5 HOH A1623 O 87.9 179.3 91.6 90.9
REMARK 620 6 HOH A1627 O 92.8 89.1 88.5 178.8 90.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1554 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A1672 O
REMARK 620 2 HOH A1673 O 90.6
REMARK 620 3 HOH A1671 O 177.7 91.1
REMARK 620 4 G A1505 OP1 93.4 111.3 84.5
REMARK 620 5 A A1500 OP1 106.5 162.4 72.0 72.7
REMARK 620 6 A A1508 OP1 100.0 93.1 81.6 152.1 80.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1541 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A1610 O
REMARK 620 2 HOH A1609 O 89.5
REMARK 620 3 HOH A1608 O 89.9 177.3
REMARK 620 4 A A 573 OP2 132.4 105.5 73.0
REMARK 620 5 A A 574 OP2 69.1 74.1 103.3 72.3
REMARK 620 6 A A 572 OP2 127.1 108.6 73.8 90.9 162.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1573 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A1764 O
REMARK 620 2 HOH A1766 O 87.9
REMARK 620 3 HOH A1765 O 178.8 93.2
REMARK 620 4 A A 116 OP2 73.9 147.3 105.3
REMARK 620 5 G A 289 OP2 65.8 108.3 113.4 89.2
REMARK 620 6 G A 117 OP2 61.9 77.4 118.7 70.1 127.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG E 159 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A1690 O
REMARK 620 2 HOH A1686 O 90.2
REMARK 620 3 HOH A1688 O 88.7 88.6
REMARK 620 4 HOH A1687 O 90.4 179.3 91.2
REMARK 620 5 HOH A1691 O 179.7 89.7 91.6 89.7
REMARK 620 6 HOH A1689 O 90.4 90.7 178.9 89.6 89.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1537 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A1590 O
REMARK 620 2 HOH A1591 O 179.3
REMARK 620 3 HOH A1589 O 91.1 89.2
REMARK 620 4 HOH A1592 O 90.1 89.3 89.9
REMARK 620 5 HOH A1593 O 90.1 90.5 90.6 179.5
REMARK 620 6 HOH A1588 O 88.6 91.1 179.3 90.8 88.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1568 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A1746 O
REMARK 620 2 HOH A1744 O 89.5
REMARK 620 3 HOH A1742 O 89.9 90.7
REMARK 620 4 HOH A1743 O 89.4 89.3 179.3
REMARK 620 5 HOH U 218 O 178.6 89.2 90.0 90.7
REMARK 620 6 HOH A1745 O 90.3 179.2 88.5 91.5 91.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1535 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A1579 O
REMARK 620 2 HOH A1578 O 88.0
REMARK 620 3 HOH A1581 O 89.2 90.2
REMARK 620 4 HOH A1582 O 90.2 90.2 179.3
REMARK 620 5 HOH A1577 O 90.8 178.5 88.9 90.6
REMARK 620 6 HOH A1580 O 179.2 91.2 91.0 89.6 90.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1556 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A1680 O
REMARK 620 2 HOH A1684 O 90.1
REMARK 620 3 HOH A1685 O 88.3 178.3
REMARK 620 4 HOH A1682 O 90.5 88.4 91.0
REMARK 620 5 HOH A1681 O 179.6 89.5 92.1 89.3
REMARK 620 6 HOH A1683 O 89.9 91.4 89.2 179.6 90.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 1 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH T 87 O
REMARK 620 2 HOH A1575 O 90.7
REMARK 620 3 HOH A 4 O 89.8 179.3
REMARK 620 4 HOH A 2 O 90.1 89.6 89.9
REMARK 620 5 HOH A1576 O 179.3 88.6 91.0 90.0
REMARK 620 6 HOH A 3 O 89.3 90.9 89.5 179.3 90.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1550 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A1651 O
REMARK 620 2 HOH A1652 O 179.5
REMARK 620 3 HOH N 105 O 89.8 90.4
REMARK 620 4 HOH A1654 O 89.2 90.4 89.7
REMARK 620 5 HOH A1653 O 90.5 89.9 89.7 179.3
REMARK 620 6 HOH A1655 O 90.4 89.3 179.5 90.7 89.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1555 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A1678 O
REMARK 620 2 HOH A1677 O 88.6
REMARK 620 3 HOH A1679 O 178.8 90.2
REMARK 620 4 HOH A1674 O 89.6 90.4 90.2
REMARK 620 5 HOH A1675 O 90.3 89.5 90.0 179.8
REMARK 620 6 HOH A1676 O 90.8 179.4 90.4 89.7 90.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1543 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A1616 O
REMARK 620 2 HOH A1617 O 179.8
REMARK 620 3 HOH A1618 O 89.6 90.6
REMARK 620 4 HOH A1620 O 88.6 91.4 89.7
REMARK 620 5 HOH A1621 O 91.7 88.3 89.9 179.5
REMARK 620 6 HOH A1619 O 89.9 89.9 179.5 90.2 90.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1549 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH N 101 O
REMARK 620 2 HOH A1648 O 89.6
REMARK 620 3 HOH A1650 O 89.8 89.8
REMARK 620 4 HOH N 102 O 90.0 90.0 179.7
REMARK 620 5 HOH A1649 O 179.6 90.5 90.5 89.7
REMARK 620 6 HOH A1647 O 90.4 179.7 89.9 90.3 89.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1559 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A1704 O
REMARK 620 2 HOH A1703 O 179.6
REMARK 620 3 HOH A1705 O 90.8 89.2
REMARK 620 4 HOH A1702 O 90.0 89.6 90.8
REMARK 620 5 HOH A1706 O 89.3 90.8 179.4 88.6
REMARK 620 6 HOH A1701 O 89.9 90.5 89.0 179.7 91.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1552 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A1662 O
REMARK 620 2 HOH A1665 O 91.1
REMARK 620 3 HOH A1661 O 89.2 89.2
REMARK 620 4 HOH A1663 O 179.6 88.5 90.5
REMARK 620 5 HOH A1664 O 88.6 179.7 91.0 91.7
REMARK 620 6 HOH A1660 O 90.8 90.7 180.0 89.5 89.0
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1535
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1536
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1537
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1538
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1539
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1540
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1541
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1542
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1543
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1544
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1545
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1546
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1547
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1548
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1549
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1550
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1551
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1552
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1553
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1554
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1555
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1556
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1557
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1558
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1559
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1560
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1561
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1562
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1563
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1564
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1565
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1566
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1567
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1568
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1569
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1570
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1571
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1572
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1573
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1574
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG E 159
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3OAQ RELATED DB: PDB
REMARK 900 30S SUBUNIT OF 70S RIBOSOME 1
REMARK 900 RELATED ID: 3OAS RELATED DB: PDB
REMARK 900 50S SUBUNIT OF 70S RIBOSOME 2
REMARK 900 RELATED ID: 3OAT RELATED DB: PDB
REMARK 900 50S SUBUNIT OF 70S RIBOSOME 1
REMARK 900 RELATED ID: 3OFA RELATED DB: PDB
REMARK 900 RELATED ID: 3OFB RELATED DB: PDB
REMARK 900 RELATED ID: 3OFC RELATED DB: PDB
REMARK 900 RELATED ID: 3OFD RELATED DB: PDB
REMARK 900 RELATED ID: 3OFO RELATED DB: PDB
REMARK 900 RELATED ID: 3OFP RELATED DB: PDB
REMARK 900 RELATED ID: 3OFQ RELATED DB: PDB
REMARK 900 RELATED ID: 3OFR RELATED DB: PDB
REMARK 900 RELATED ID: 3OFX RELATED DB: PDB
REMARK 900 RELATED ID: 3OFY RELATED DB: PDB
REMARK 900 RELATED ID: 3OFZ RELATED DB: PDB
REMARK 900 RELATED ID: 3OG0 RELATED DB: PDB
DBREF1 3OAR A 5 1534 GB AP009048
DBREF2 3OAR A AP009048.1 3427004 3428533
DBREF 3OAR B 8 225 UNP P0A7V0 RS2_ECOLI 9 226
DBREF 3OAR C 1 206 UNP P0A7V3 RS3_ECOLI 2 207
DBREF 3OAR D 1 205 UNP P0A7V8 RS4_ECOLI 2 206
DBREF 3OAR E 9 158 UNP P0A7W1 RS5_ECOLI 10 159
DBREF 3OAR F 1 100 UNP P02358 RS6_ECOLI 1 100
DBREF 3OAR G 2 151 UNP P02359 RS7_ECOLI 3 152
DBREF 3OAR H 1 129 UNP P0A7W7 RS8_ECOLI 2 130
DBREF 3OAR I 3 129 UNP P0A7X3 RS9_ECOLI 4 130
DBREF 3OAR J 5 102 UNP P0A7R5 RS10_ECOLI 5 102
DBREF 3OAR K 12 128 UNP P0A7R9 RS11_ECOLI 13 129
DBREF 3OAR L 1 123 UNP P0A7S3 RS12_ECOLI 2 124
DBREF 3OAR M 1 113 UNP P0A7S9 RS13_ECOLI 2 114
DBREF 3OAR N 1 100 UNP P0AG59 RS14_ECOLI 2 101
DBREF 3OAR O 1 88 UNP P0ADZ4 RS15_ECOLI 2 89
DBREF 3OAR P 1 80 UNP P0A7T3 RS16_ECOLI 1 80
DBREF 3OAR Q 3 82 UNP P0AG63 RS17_ECOLI 4 83
DBREF 3OAR R 19 73 UNP P0A7T7 RS18_ECOLI 20 74
DBREF 3OAR S 2 80 UNP P0A7U3 RS19_ECOLI 3 81
DBREF 3OAR T 2 86 UNP P0A7U7 RS20_ECOLI 3 87
DBREF 3OAR U 3 53 UNP P68679 RS21_ECOLI 4 54
SEQRES 1 A 1530 U G A A G A G U U U G A U
SEQRES 2 A 1530 C A U G G C U C A G A U U
SEQRES 3 A 1530 G A A C G C U G G C G G C
SEQRES 4 A 1530 A G G C C U A A C A C A U
SEQRES 5 A 1530 G C A A G U C G A A C G G
SEQRES 6 A 1530 U A A C A G G A A G A A G
SEQRES 7 A 1530 C U U G C U U C U U U G C
SEQRES 8 A 1530 U G A C G A G U G G C G G
SEQRES 9 A 1530 A C G G G U G A G U A A U
SEQRES 10 A 1530 G U C U G G G A A A C U G
SEQRES 11 A 1530 C C U G A U G G A G G G G
SEQRES 12 A 1530 G A U A A C U A C U G G A
SEQRES 13 A 1530 A A C G G U A G C U A A U
SEQRES 14 A 1530 A C C G C A U A A C G U C
SEQRES 15 A 1530 G C A A G A C C A A A G A
SEQRES 16 A 1530 G G G G G A C C U U C G G
SEQRES 17 A 1530 G C C U C U U G C C A U C
SEQRES 18 A 1530 G G A U G U G C C C A G A
SEQRES 19 A 1530 U G G G A U U A G C U A G
SEQRES 20 A 1530 U A G G U G G G G U A A C
SEQRES 21 A 1530 G G C U C A C C U A G G C
SEQRES 22 A 1530 G A C G A U C C C U A G C
SEQRES 23 A 1530 U G G U C U G A G A G G A
SEQRES 24 A 1530 U G A C C A G C C A C A C
SEQRES 25 A 1530 U G G A A C U G A G A C A
SEQRES 26 A 1530 C G G U C C A G A C U C C
SEQRES 27 A 1530 U A C G G G A G G C A G C
SEQRES 28 A 1530 A G U G G G G A A U A U U
SEQRES 29 A 1530 G C A C A A U G G G C G C
SEQRES 30 A 1530 A A G C C U G A U G C A G
SEQRES 31 A 1530 C C A U G C C G C G U G U
SEQRES 32 A 1530 A U G A A G A A G G C C U
SEQRES 33 A 1530 U C G G G U U G U A A A G
SEQRES 34 A 1530 U A C U U U C A G C G G G
SEQRES 35 A 1530 G A G G A A G G G A G U A
SEQRES 36 A 1530 A A G U U A A U A C C U U
SEQRES 37 A 1530 U G C U C A U U G A C G U
SEQRES 38 A 1530 U A C C C G C A G A A G A
SEQRES 39 A 1530 A G C A C C G G C U A A C
SEQRES 40 A 1530 U C C G U G C C A G C A G
SEQRES 41 A 1530 C C G C G G U A A U A C G
SEQRES 42 A 1530 G A G G G U G C A A G C G
SEQRES 43 A 1530 U U A A U C G G A A U U A
SEQRES 44 A 1530 C U G G G C G U A A A G C
SEQRES 45 A 1530 G C A C G C A G G C G G U
SEQRES 46 A 1530 U U G U U A A G U C A G A
SEQRES 47 A 1530 U G U G A A A U C C C C G
SEQRES 48 A 1530 G G C U C A A C C U G G G
SEQRES 49 A 1530 A A C U G C A U C U G A U
SEQRES 50 A 1530 A C U G G C A A G C U U G
SEQRES 51 A 1530 A G U C U C G U A G A G G
SEQRES 52 A 1530 G G G G U A G A A U U C C
SEQRES 53 A 1530 A G G U G U A G C G G U G
SEQRES 54 A 1530 A A A U G C G U A G A G A
SEQRES 55 A 1530 U C U G G A G G A A U A C
SEQRES 56 A 1530 C G G U G G C G A A G G C
SEQRES 57 A 1530 G G C C C C C U G G A C G
SEQRES 58 A 1530 A A G A C U G A C G C U C
SEQRES 59 A 1530 A G G U G C G A A A G C G
SEQRES 60 A 1530 U G G G G A G C A A A C A
SEQRES 61 A 1530 G G A U U A G A U A C C C
SEQRES 62 A 1530 U G G U A G U C C A C G C
SEQRES 63 A 1530 C G U A A A C G A U G U C
SEQRES 64 A 1530 G A C U U G G A G G U U G
SEQRES 65 A 1530 U G C C C U U G A G G C G
SEQRES 66 A 1530 U G G C U U C C G G A G C
SEQRES 67 A 1530 U A A C G C G U U A A G U
SEQRES 68 A 1530 C G A C C G C C U G G G G
SEQRES 69 A 1530 A G U A C G G C C G C A A
SEQRES 70 A 1530 G G U U A A A A C U C A A
SEQRES 71 A 1530 A U G A A U U G A C G G G
SEQRES 72 A 1530 G G C C C G C A C A A G C
SEQRES 73 A 1530 G G U G G A G C A U G U G
SEQRES 74 A 1530 G U U U A A U U C G A U G
SEQRES 75 A 1530 C A A C G C G A A G A A C
SEQRES 76 A 1530 C U U A C C U G G U C U U
SEQRES 77 A 1530 G A C A U C C A C G G A A
SEQRES 78 A 1530 G U U U U C A G A G A U G
SEQRES 79 A 1530 A G A A U G U G C C U U C
SEQRES 80 A 1530 G G G A A C C G U G A G A
SEQRES 81 A 1530 C A G G U G C U G C A U G
SEQRES 82 A 1530 G C U G U C G U C A G C U
SEQRES 83 A 1530 C G U G U U G U G A A A U
SEQRES 84 A 1530 G U U G G G U U A A G U C
SEQRES 85 A 1530 C C G C A A C G A G C G C
SEQRES 86 A 1530 A A C C C U U A U C C U U
SEQRES 87 A 1530 U G U U G C C A G C G G U
SEQRES 88 A 1530 C C G G C C G G G A A C U
SEQRES 89 A 1530 C A A A G G A G A C U G C
SEQRES 90 A 1530 C A G U G A U A A A C U G
SEQRES 91 A 1530 G A G G A A G G U G G G G
SEQRES 92 A 1530 A U G A C G U C A A G U C
SEQRES 93 A 1530 A U C A U G G C C C U U A
SEQRES 94 A 1530 C G A C C A G G G C U A C
SEQRES 95 A 1530 A C A C G U G C U A C A A
SEQRES 96 A 1530 U G G C G C A U A C A A A
SEQRES 97 A 1530 G A G A A G C G A C C U C
SEQRES 98 A 1530 G C G A G A G C A A G C G
SEQRES 99 A 1530 G A C C U C A U A A A G U
SEQRES 100 A 1530 G C G U C G U A G U C C G
SEQRES 101 A 1530 G A U U G G A G U C U G C
SEQRES 102 A 1530 A A C U C G A C U C C A U
SEQRES 103 A 1530 G A A G U C G G A A U C G
SEQRES 104 A 1530 C U A G U A A U C G U G G
SEQRES 105 A 1530 A U C A G A A U G C C A C
SEQRES 106 A 1530 G G U G A A U A C G U U C
SEQRES 107 A 1530 C C G G G C C U U G U A C
SEQRES 108 A 1530 A C A C C G C C C G U C A
SEQRES 109 A 1530 C A C C A U G G G A G U G
SEQRES 110 A 1530 G G U U G C A A A A G A A
SEQRES 111 A 1530 G U A G G U A G C U U A A
SEQRES 112 A 1530 C C U U C G G G A G G G C
SEQRES 113 A 1530 G C U U A C C A C U U U G
SEQRES 114 A 1530 U G A U U C A U G A C U G
SEQRES 115 A 1530 G G G U G A A G U C G U A
SEQRES 116 A 1530 A C A A G G U A A C C G U
SEQRES 117 A 1530 A G G G G A A C C U G C G
SEQRES 118 A 1530 G U U G G A U C A
SEQRES 1 B 218 MET LEU LYS ALA GLY VAL HIS PHE GLY HIS GLN THR ARG
SEQRES 2 B 218 TYR TRP ASN PRO LYS MET LYS PRO PHE ILE PHE GLY ALA
SEQRES 3 B 218 ARG ASN LYS VAL HIS ILE ILE ASN LEU GLU LYS THR VAL
SEQRES 4 B 218 PRO MET PHE ASN GLU ALA LEU ALA GLU LEU ASN LYS ILE
SEQRES 5 B 218 ALA SER ARG LYS GLY LYS ILE LEU PHE VAL GLY THR LYS
SEQRES 6 B 218 ARG ALA ALA SER GLU ALA VAL LYS ASP ALA ALA LEU SER
SEQRES 7 B 218 CYS ASP GLN PHE PHE VAL ASN HIS ARG TRP LEU GLY GLY
SEQRES 8 B 218 MET LEU THR ASN TRP LYS THR VAL ARG GLN SER ILE LYS
SEQRES 9 B 218 ARG LEU LYS ASP LEU GLU THR GLN SER GLN ASP GLY THR
SEQRES 10 B 218 PHE ASP LYS LEU THR LYS LYS GLU ALA LEU MET ARG THR
SEQRES 11 B 218 ARG GLU LEU GLU LYS LEU GLU ASN SER LEU GLY GLY ILE
SEQRES 12 B 218 LYS ASP MET GLY GLY LEU PRO ASP ALA LEU PHE VAL ILE
SEQRES 13 B 218 ASP ALA ASP HIS GLU HIS ILE ALA ILE LYS GLU ALA ASN
SEQRES 14 B 218 ASN LEU GLY ILE PRO VAL PHE ALA ILE VAL ASP THR ASN
SEQRES 15 B 218 SER ASP PRO ASP GLY VAL ASP PHE VAL ILE PRO GLY ASN
SEQRES 16 B 218 ASP ASP ALA ILE ARG ALA VAL THR LEU TYR LEU GLY ALA
SEQRES 17 B 218 VAL ALA ALA THR VAL ARG GLU GLY ARG SER
SEQRES 1 C 206 GLY GLN LYS VAL HIS PRO ASN GLY ILE ARG LEU GLY ILE
SEQRES 2 C 206 VAL LYS PRO TRP ASN SER THR TRP PHE ALA ASN THR LYS
SEQRES 3 C 206 GLU PHE ALA ASP ASN LEU ASP SER ASP PHE LYS VAL ARG
SEQRES 4 C 206 GLN TYR LEU THR LYS GLU LEU ALA LYS ALA SER VAL SER
SEQRES 5 C 206 ARG ILE VAL ILE GLU ARG PRO ALA LYS SER ILE ARG VAL
SEQRES 6 C 206 THR ILE HIS THR ALA ARG PRO GLY ILE VAL ILE GLY LYS
SEQRES 7 C 206 LYS GLY GLU ASP VAL GLU LYS LEU ARG LYS VAL VAL ALA
SEQRES 8 C 206 ASP ILE ALA GLY VAL PRO ALA GLN ILE ASN ILE ALA GLU
SEQRES 9 C 206 VAL ARG LYS PRO GLU LEU ASP ALA LYS LEU VAL ALA ASP
SEQRES 10 C 206 SER ILE THR SER GLN LEU GLU ARG ARG VAL MET PHE ARG
SEQRES 11 C 206 ARG ALA MET LYS ARG ALA VAL GLN ASN ALA MET ARG LEU
SEQRES 12 C 206 GLY ALA LYS GLY ILE LYS VAL GLU VAL SER GLY ARG LEU
SEQRES 13 C 206 GLY GLY ALA GLU ILE ALA ARG THR GLU TRP TYR ARG GLU
SEQRES 14 C 206 GLY ARG VAL PRO LEU HIS THR LEU ARG ALA ASP ILE ASP
SEQRES 15 C 206 TYR ASN THR SER GLU ALA HIS THR THR TYR GLY VAL ILE
SEQRES 16 C 206 GLY VAL LYS VAL TRP ILE PHE LYS GLY GLU ILE
SEQRES 1 D 205 ALA ARG TYR LEU GLY PRO LYS LEU LYS LEU SER ARG ARG
SEQRES 2 D 205 GLU GLY THR ASP LEU PHE LEU LYS SER GLY VAL ARG ALA
SEQRES 3 D 205 ILE ASP THR LYS CYS LYS ILE GLU GLN ALA PRO GLY GLN
SEQRES 4 D 205 HIS GLY ALA ARG LYS PRO ARG LEU SER ASP TYR GLY VAL
SEQRES 5 D 205 GLN LEU ARG GLU LYS GLN LYS VAL ARG ARG ILE TYR GLY
SEQRES 6 D 205 VAL LEU GLU ARG GLN PHE ARG ASN TYR TYR LYS GLU ALA
SEQRES 7 D 205 ALA ARG LEU LYS GLY ASN THR GLY GLU ASN LEU LEU ALA
SEQRES 8 D 205 LEU LEU GLU GLY ARG LEU ASP ASN VAL VAL TYR ARG MET
SEQRES 9 D 205 GLY PHE GLY ALA THR ARG ALA GLU ALA ARG GLN LEU VAL
SEQRES 10 D 205 SER HIS LYS ALA ILE MET VAL ASN GLY ARG VAL VAL ASN
SEQRES 11 D 205 ILE ALA SER TYR GLN VAL SER PRO ASN ASP VAL VAL SER
SEQRES 12 D 205 ILE ARG GLU LYS ALA LYS LYS GLN SER ARG VAL LYS ALA
SEQRES 13 D 205 ALA LEU GLU LEU ALA GLU GLN ARG GLU LYS PRO THR TRP
SEQRES 14 D 205 LEU GLU VAL ASP ALA GLY LYS MET GLU GLY THR PHE LYS
SEQRES 15 D 205 ARG LYS PRO GLU ARG SER ASP LEU SER ALA ASP ILE ASN
SEQRES 16 D 205 GLU HIS LEU ILE VAL GLU LEU TYR SER LYS
SEQRES 1 E 150 GLU LEU GLN GLU LYS LEU ILE ALA VAL ASN ARG VAL SER
SEQRES 2 E 150 LYS THR VAL LYS GLY GLY ARG ILE PHE SER PHE THR ALA
SEQRES 3 E 150 LEU THR VAL VAL GLY ASP GLY ASN GLY ARG VAL GLY PHE
SEQRES 4 E 150 GLY TYR GLY LYS ALA ARG GLU VAL PRO ALA ALA ILE GLN
SEQRES 5 E 150 LYS ALA MET GLU LYS ALA ARG ARG ASN MET ILE ASN VAL
SEQRES 6 E 150 ALA LEU ASN ASN GLY THR LEU GLN HIS PRO VAL LYS GLY
SEQRES 7 E 150 VAL HIS THR GLY SER ARG VAL PHE MET GLN PRO ALA SER
SEQRES 8 E 150 GLU GLY THR GLY ILE ILE ALA GLY GLY ALA MET ARG ALA
SEQRES 9 E 150 VAL LEU GLU VAL ALA GLY VAL HIS ASN VAL LEU ALA LYS
SEQRES 10 E 150 ALA TYR GLY SER THR ASN PRO ILE ASN VAL VAL ARG ALA
SEQRES 11 E 150 THR ILE ASP GLY LEU GLU ASN MET ASN SER PRO GLU MET
SEQRES 12 E 150 VAL ALA ALA LYS ARG GLY LYS
SEQRES 1 F 100 MET ARG HIS TYR GLU ILE VAL PHE MET VAL HIS PRO ASP
SEQRES 2 F 100 GLN SER GLU GLN VAL PRO GLY MET ILE GLU ARG TYR THR
SEQRES 3 F 100 ALA ALA ILE THR GLY ALA GLU GLY LYS ILE HIS ARG LEU
SEQRES 4 F 100 GLU ASP TRP GLY ARG ARG GLN LEU ALA TYR PRO ILE ASN
SEQRES 5 F 100 LYS LEU HIS LYS ALA HIS TYR VAL LEU MET ASN VAL GLU
SEQRES 6 F 100 ALA PRO GLN GLU VAL ILE ASP GLU LEU GLU THR THR PHE
SEQRES 7 F 100 ARG PHE ASN ASP ALA VAL ILE ARG SER MET VAL MET ARG
SEQRES 8 F 100 THR LYS HIS ALA VAL THR GLU ALA SER
SEQRES 1 G 150 ARG ARG ARG VAL ILE GLY GLN ARG LYS ILE LEU PRO ASP
SEQRES 2 G 150 PRO LYS PHE GLY SER GLU LEU LEU ALA LYS PHE VAL ASN
SEQRES 3 G 150 ILE LEU MET VAL ASP GLY LYS LYS SER THR ALA GLU SER
SEQRES 4 G 150 ILE VAL TYR SER ALA LEU GLU THR LEU ALA GLN ARG SER
SEQRES 5 G 150 GLY LYS SER GLU LEU GLU ALA PHE GLU VAL ALA LEU GLU
SEQRES 6 G 150 ASN VAL ARG PRO THR VAL GLU VAL LYS SER ARG ARG VAL
SEQRES 7 G 150 GLY GLY SER THR TYR GLN VAL PRO VAL GLU VAL ARG PRO
SEQRES 8 G 150 VAL ARG ARG ASN ALA LEU ALA MET ARG TRP ILE VAL GLU
SEQRES 9 G 150 ALA ALA ARG LYS ARG GLY ASP LYS SER MET ALA LEU ARG
SEQRES 10 G 150 LEU ALA ASN GLU LEU SER ASP ALA ALA GLU ASN LYS GLY
SEQRES 11 G 150 THR ALA VAL LYS LYS ARG GLU ASP VAL HIS ARG MET ALA
SEQRES 12 G 150 GLU ALA ASN LYS ALA PHE ALA
SEQRES 1 H 129 SER MET GLN ASP PRO ILE ALA ASP MET LEU THR ARG ILE
SEQRES 2 H 129 ARG ASN GLY GLN ALA ALA ASN LYS ALA ALA VAL THR MET
SEQRES 3 H 129 PRO SER SER LYS LEU LYS VAL ALA ILE ALA ASN VAL LEU
SEQRES 4 H 129 LYS GLU GLU GLY PHE ILE GLU ASP PHE LYS VAL GLU GLY
SEQRES 5 H 129 ASP THR LYS PRO GLU LEU GLU LEU THR LEU LYS TYR PHE
SEQRES 6 H 129 GLN GLY LYS ALA VAL VAL GLU SER ILE GLN ARG VAL SER
SEQRES 7 H 129 ARG PRO GLY LEU ARG ILE TYR LYS ARG LYS ASP GLU LEU
SEQRES 8 H 129 PRO LYS VAL MET ALA GLY LEU GLY ILE ALA VAL VAL SER
SEQRES 9 H 129 THR SER LYS GLY VAL MET THR ASP ARG ALA ALA ARG GLN
SEQRES 10 H 129 ALA GLY LEU GLY GLY GLU ILE ILE CYS TYR VAL ALA
SEQRES 1 I 127 ASN GLN TYR TYR GLY THR GLY ARG ARG LYS SER SER ALA
SEQRES 2 I 127 ALA ARG VAL PHE ILE LYS PRO GLY ASN GLY LYS ILE VAL
SEQRES 3 I 127 ILE ASN GLN ARG SER LEU GLU GLN TYR PHE GLY ARG GLU
SEQRES 4 I 127 THR ALA ARG MET VAL VAL ARG GLN PRO LEU GLU LEU VAL
SEQRES 5 I 127 ASP MET VAL GLU LYS LEU ASP LEU TYR ILE THR VAL LYS
SEQRES 6 I 127 GLY GLY GLY ILE SER GLY GLN ALA GLY ALA ILE ARG HIS
SEQRES 7 I 127 GLY ILE THR ARG ALA LEU MET GLU TYR ASP GLU SER LEU
SEQRES 8 I 127 ARG SER GLU LEU ARG LYS ALA GLY PHE VAL THR ARG ASP
SEQRES 9 I 127 ALA ARG GLN VAL GLU ARG LYS LYS VAL GLY LEU ARG LYS
SEQRES 10 I 127 ALA ARG ARG ARG PRO GLN PHE SER LYS ARG
SEQRES 1 J 98 ARG ILE ARG ILE ARG LEU LYS ALA PHE ASP HIS ARG LEU
SEQRES 2 J 98 ILE ASP GLN ALA THR ALA GLU ILE VAL GLU THR ALA LYS
SEQRES 3 J 98 ARG THR GLY ALA GLN VAL ARG GLY PRO ILE PRO LEU PRO
SEQRES 4 J 98 THR ARG LYS GLU ARG PHE THR VAL LEU ILE SER PRO HIS
SEQRES 5 J 98 VAL ASN LYS ASP ALA ARG ASP GLN TYR GLU ILE ARG THR
SEQRES 6 J 98 HIS LEU ARG LEU VAL ASP ILE VAL GLU PRO THR GLU LYS
SEQRES 7 J 98 THR VAL ASP ALA LEU MET ARG LEU ASP LEU ALA ALA GLY
SEQRES 8 J 98 VAL ASP VAL GLN ILE SER LEU
SEQRES 1 K 117 ARG LYS GLN VAL SER ASP GLY VAL ALA HIS ILE HIS ALA
SEQRES 2 K 117 SER PHE ASN ASN THR ILE VAL THR ILE THR ASP ARG GLN
SEQRES 3 K 117 GLY ASN ALA LEU GLY TRP ALA THR ALA GLY GLY SER GLY
SEQRES 4 K 117 PHE ARG GLY SER ARG LYS SER THR PRO PHE ALA ALA GLN
SEQRES 5 K 117 VAL ALA ALA GLU ARG CYS ALA ASP ALA VAL LYS GLU TYR
SEQRES 6 K 117 GLY ILE LYS ASN LEU GLU VAL MET VAL LYS GLY PRO GLY
SEQRES 7 K 117 PRO GLY ARG GLU SER THR ILE ARG ALA LEU ASN ALA ALA
SEQRES 8 K 117 GLY PHE ARG ILE THR ASN ILE THR ASP VAL THR PRO ILE
SEQRES 9 K 117 PRO HIS ASN GLY CYS ARG PRO PRO LYS LYS ARG ARG VAL
SEQRES 1 L 123 ALA THR VAL ASN GLN LEU VAL ARG LYS PRO ARG ALA ARG
SEQRES 2 L 123 LYS VAL ALA LYS SER ASN VAL PRO ALA LEU GLU ALA CYS
SEQRES 3 L 123 PRO GLN LYS ARG GLY VAL CYS THR ARG VAL TYR THR THR
SEQRES 4 L 123 THR PRO LYS LYS PRO ASN SER ALA LEU ARG LYS VAL CYS
SEQRES 5 L 123 ARG VAL ARG LEU THR ASN GLY PHE GLU VAL THR SER TYR
SEQRES 6 L 123 ILE GLY GLY GLU GLY HIS ASN LEU GLN GLU HIS SER VAL
SEQRES 7 L 123 ILE LEU ILE ARG GLY GLY ARG VAL LYS ASP LEU PRO GLY
SEQRES 8 L 123 VAL ARG TYR HIS THR VAL ARG GLY ALA LEU ASP CYS SER
SEQRES 9 L 123 GLY VAL LYS ASP ARG LYS GLN ALA ARG SER LYS TYR GLY
SEQRES 10 L 123 VAL LYS ARG PRO LYS ALA
SEQRES 1 M 113 ALA ARG ILE ALA GLY ILE ASN ILE PRO ASP HIS LYS HIS
SEQRES 2 M 113 ALA VAL ILE ALA LEU THR SER ILE TYR GLY VAL GLY LYS
SEQRES 3 M 113 THR ARG SER LYS ALA ILE LEU ALA ALA ALA GLY ILE ALA
SEQRES 4 M 113 GLU ASP VAL LYS ILE SER GLU LEU SER GLU GLY GLN ILE
SEQRES 5 M 113 ASP THR LEU ARG ASP GLU VAL ALA LYS PHE VAL VAL GLU
SEQRES 6 M 113 GLY ASP LEU ARG ARG GLU ILE SER MET SER ILE LYS ARG
SEQRES 7 M 113 LEU MET ASP LEU GLY CYS TYR ARG GLY LEU ARG HIS ARG
SEQRES 8 M 113 ARG GLY LEU PRO VAL ARG GLY GLN ARG THR LYS THR ASN
SEQRES 9 M 113 ALA ARG THR ARG LYS GLY PRO ARG LYS
SEQRES 1 N 100 ALA LYS GLN SER MET LYS ALA ARG GLU VAL LYS ARG VAL
SEQRES 2 N 100 ALA LEU ALA ASP LYS TYR PHE ALA LYS ARG ALA GLU LEU
SEQRES 3 N 100 LYS ALA ILE ILE SER ASP VAL ASN ALA SER ASP GLU ASP
SEQRES 4 N 100 ARG TRP ASN ALA VAL LEU LYS LEU GLN THR LEU PRO ARG
SEQRES 5 N 100 ASP SER SER PRO SER ARG GLN ARG ASN ARG CYS ARG GLN
SEQRES 6 N 100 THR GLY ARG PRO HIS GLY PHE LEU ARG LYS PHE GLY LEU
SEQRES 7 N 100 SER ARG ILE LYS VAL ARG GLU ALA ALA MET ARG GLY GLU
SEQRES 8 N 100 ILE PRO GLY LEU LYS LYS ALA SER TRP
SEQRES 1 O 88 SER LEU SER THR GLU ALA THR ALA LYS ILE VAL SER GLU
SEQRES 2 O 88 PHE GLY ARG ASP ALA ASN ASP THR GLY SER THR GLU VAL
SEQRES 3 O 88 GLN VAL ALA LEU LEU THR ALA GLN ILE ASN HIS LEU GLN
SEQRES 4 O 88 GLY HIS PHE ALA GLU HIS LYS LYS ASP HIS HIS SER ARG
SEQRES 5 O 88 ARG GLY LEU LEU ARG MET VAL SER GLN ARG ARG LYS LEU
SEQRES 6 O 88 LEU ASP TYR LEU LYS ARG LYS ASP VAL ALA ARG TYR THR
SEQRES 7 O 88 GLN LEU ILE GLU ARG LEU GLY LEU ARG ARG
SEQRES 1 P 80 MET VAL THR ILE ARG LEU ALA ARG HIS GLY ALA LYS LYS
SEQRES 2 P 80 ARG PRO PHE TYR GLN VAL VAL VAL ALA ASP SER ARG ASN
SEQRES 3 P 80 ALA ARG ASN GLY ARG PHE ILE GLU ARG VAL GLY PHE PHE
SEQRES 4 P 80 ASN PRO ILE ALA SER GLU LYS GLU GLU GLY THR ARG LEU
SEQRES 5 P 80 ASP LEU ASP ARG ILE ALA HIS TRP VAL GLY GLN GLY ALA
SEQRES 6 P 80 THR ILE SER ASP ARG VAL ALA ALA LEU ILE LYS GLU VAL
SEQRES 7 P 80 ASN LYS
SEQRES 1 Q 80 LYS ILE ARG THR LEU GLN GLY ARG VAL VAL SER ASP LYS
SEQRES 2 Q 80 MET GLU LYS SER ILE VAL VAL ALA ILE GLU ARG PHE VAL
SEQRES 3 Q 80 LYS HIS PRO ILE TYR GLY LYS PHE ILE LYS ARG THR THR
SEQRES 4 Q 80 LYS LEU HIS VAL HIS ASP GLU ASN ASN GLU CYS GLY ILE
SEQRES 5 Q 80 GLY ASP VAL VAL GLU ILE ARG GLU CYS ARG PRO LEU SER
SEQRES 6 Q 80 LYS THR LYS SER TRP THR LEU VAL ARG VAL VAL GLU LYS
SEQRES 7 Q 80 ALA VAL
SEQRES 1 R 55 GLU ILE ASP TYR LYS ASP ILE ALA THR LEU LYS ASN TYR
SEQRES 2 R 55 ILE THR GLU SER GLY LYS ILE VAL PRO SER ARG ILE THR
SEQRES 3 R 55 GLY THR ARG ALA LYS TYR GLN ARG GLN LEU ALA ARG ALA
SEQRES 4 R 55 ILE LYS ARG ALA ARG TYR LEU SER LEU LEU PRO TYR THR
SEQRES 5 R 55 ASP ARG HIS
SEQRES 1 S 79 ARG SER LEU LYS LYS GLY PRO PHE ILE ASP LEU HIS LEU
SEQRES 2 S 79 LEU LYS LYS VAL GLU LYS ALA VAL GLU SER GLY ASP LYS
SEQRES 3 S 79 LYS PRO LEU ARG THR TRP SER ARG ARG SER THR ILE PHE
SEQRES 4 S 79 PRO ASN MET ILE GLY LEU THR ILE ALA VAL HIS ASN GLY
SEQRES 5 S 79 ARG GLN HIS VAL PRO VAL PHE VAL THR ASP GLU MET VAL
SEQRES 6 S 79 GLY HIS LYS LEU GLY GLU PHE ALA PRO THR ARG THR TYR
SEQRES 7 S 79 ARG
SEQRES 1 T 85 ASN ILE LYS SER ALA LYS LYS ARG ALA ILE GLN SER GLU
SEQRES 2 T 85 LYS ALA ARG LYS HIS ASN ALA SER ARG ARG SER MET MET
SEQRES 3 T 85 ARG THR PHE ILE LYS LYS VAL TYR ALA ALA ILE GLU ALA
SEQRES 4 T 85 GLY ASP LYS ALA ALA ALA GLN LYS ALA PHE ASN GLU MET
SEQRES 5 T 85 GLN PRO ILE VAL ASP ARG GLN ALA ALA LYS GLY LEU ILE
SEQRES 6 T 85 HIS LYS ASN LYS ALA ALA ARG HIS LYS ALA ASN LEU THR
SEQRES 7 T 85 ALA GLN ILE ASN LYS LEU ALA
SEQRES 1 U 51 ILE LYS VAL ARG GLU ASN GLU PRO PHE ASP VAL ALA LEU
SEQRES 2 U 51 ARG ARG PHE LYS ARG SER CYS GLU LYS ALA GLY VAL LEU
SEQRES 3 U 51 ALA GLU VAL ARG ARG ARG GLU PHE TYR GLU LYS PRO THR
SEQRES 4 U 51 THR GLU ARG LYS ARG ALA LYS ALA SER ALA VAL LYS
HET MG A 1 1
HET MG A1535 1
HET MG A1536 1
HET MG A1537 1
HET MG A1538 1
HET MG A1539 1
HET MG A1540 1
HET MG A1541 1
HET MG A1542 1
HET MG A1543 1
HET MG A1544 1
HET MG A1545 1
HET MG A1546 1
HET MG A1547 1
HET MG A1548 1
HET MG A1549 1
HET MG A1550 1
HET MG A1551 1
HET MG A1552 1
HET MG A1553 1
HET MG A1554 1
HET MG A1555 1
HET MG A1556 1
HET MG A1557 1
HET MG A1558 1
HET MG A1559 1
HET MG A1560 1
HET MG A1561 1
HET MG A1562 1
HET MG A1563 1
HET MG A1564 1
HET MG A1565 1
HET MG A1566 1
HET MG A1567 1
HET MG A1568 1
HET MG A1569 1
HET MG A1570 1
HET MG A1571 1
HET MG A1572 1
HET MG A1573 1
HET MG A1574 1
HET MG E 159 1
HETNAM MG MAGNESIUM ION
FORMUL 22 MG 42(MG 2+)
FORMUL 64 HOH *207(H2 O)
HELIX 1 1 ALA B 33 VAL B 37 5 5
HELIX 2 2 ASN B 41 VAL B 46 1 6
HELIX 3 3 ALA B 52 SER B 61 1 10
HELIX 4 4 SER B 76 LYS B 80 5 5
HELIX 5 5 ASN B 102 ARG B 107 1 6
HELIX 6 6 ILE B 110 ASP B 115 1 6
HELIX 7 7 THR B 137 LEU B 147 1 11
HELIX 8 8 ILE B 150 GLY B 154 5 5
HELIX 9 9 GLU B 168 ASN B 177 1 10
HELIX 10 10 ASP B 191 VAL B 195 5 5
HELIX 11 11 ALA B 205 LEU B 213 1 9
HELIX 12 12 ALA B 215 VAL B 220 1 6
HELIX 13 13 VAL B 220 SER B 225 1 6
HELIX 14 14 ALA C 29 LEU C 46 1 18
HELIX 15 15 ARG C 71 VAL C 75 5 5
HELIX 16 16 GLY C 80 ILE C 93 1 14
HELIX 17 17 LYS C 107 LEU C 110 5 4
HELIX 18 18 ASP C 111 THR C 120 1 10
HELIX 19 19 MET C 128 ARG C 142 1 15
HELIX 20 20 ARG C 155 ALA C 159 5 5
HELIX 21 21 LYS D 7 GLY D 15 1 9
HELIX 22 22 GLN D 39 ARG D 43 5 5
HELIX 23 23 SER D 48 GLY D 65 1 18
HELIX 24 24 LEU D 67 ARG D 80 1 14
HELIX 25 25 ASN D 84 GLY D 95 1 12
HELIX 26 26 ARG D 96 MET D 104 1 9
HELIX 27 27 THR D 109 HIS D 119 1 11
HELIX 28 28 GLN D 151 GLN D 163 1 13
HELIX 29 29 ASN D 195 SER D 204 1 10
HELIX 30 30 GLU E 54 ARG E 68 1 15
HELIX 31 31 GLY E 107 GLY E 118 1 12
HELIX 32 32 ASN E 131 LEU E 143 1 13
HELIX 33 33 SER E 148 ALA E 153 1 6
HELIX 34 34 PRO F 12 GLU F 16 5 5
HELIX 35 35 GLN F 17 THR F 30 1 14
HELIX 36 36 GLN F 68 PHE F 80 1 13
HELIX 37 37 SER G 19 MET G 30 1 12
HELIX 38 38 ARG G 91 LEU G 98 1 8
HELIX 39 39 ALA G 99 VAL G 104 1 6
HELIX 40 40 SER G 114 LEU G 119 1 6
HELIX 41 41 ALA G 120 ALA G 127 5 8
HELIX 42 42 VAL G 134 ASP G 139 1 6
HELIX 43 43 ASP G 139 ALA G 144 1 6
HELIX 44 44 ASP H 4 ALA H 19 1 16
HELIX 45 45 LYS H 32 GLU H 42 1 11
HELIX 46 46 THR H 111 ALA H 118 1 8
HELIX 47 47 ARG I 44 GLN I 49 1 6
HELIX 48 48 GLY I 70 ALA I 85 1 16
HELIX 49 49 ARG I 94 LYS I 99 1 6
HELIX 50 50 ASP J 14 ILE J 25 1 12
HELIX 51 51 GLY K 47 GLY K 50 5 4
HELIX 52 52 SER K 54 THR K 58 5 5
HELIX 53 53 PRO K 59 ARG K 68 1 10
HELIX 54 54 VAL K 73 GLY K 77 5 5
HELIX 55 55 PRO K 90 GLY K 103 1 14
HELIX 56 56 THR L 2 VAL L 7 1 6
HELIX 57 57 HIS M 13 THR M 19 1 7
HELIX 58 58 THR M 27 ILE M 32 1 6
HELIX 59 59 LEU M 33 ALA M 35 5 3
HELIX 60 60 LEU M 55 LYS M 61 1 7
HELIX 61 61 VAL M 64 ILE M 72 1 9
HELIX 62 62 MET M 74 LEU M 79 1 6
HELIX 63 63 MET M 80 LEU M 82 5 3
HELIX 64 64 TYR M 85 ARG M 89 5 5
HELIX 65 65 LYS N 2 LEU N 15 1 14
HELIX 66 66 LYS N 22 LYS N 27 1 6
HELIX 67 67 TRP N 41 LEU N 45 5 5
HELIX 68 68 SER N 79 MET N 88 1 10
HELIX 69 69 SER O 3 PHE O 14 1 12
HELIX 70 70 SER O 23 PHE O 42 1 20
HELIX 71 71 ASP O 48 ASP O 73 1 26
HELIX 72 72 ASP O 73 ARG O 83 1 11
HELIX 73 73 ASP P 53 GLY P 62 1 10
HELIX 74 74 SER P 68 LYS P 76 1 9
HELIX 75 75 ASP R 24 LYS R 29 1 6
HELIX 76 76 ASN R 30 ILE R 32 5 3
HELIX 77 77 PRO R 40 GLY R 45 1 6
HELIX 78 78 ARG R 47 LEU R 64 1 18
HELIX 79 79 LEU S 14 GLU S 19 1 6
HELIX 80 80 LYS S 69 ALA S 74 1 6
HELIX 81 81 LYS T 7 ALA T 40 1 34
HELIX 82 82 ALA T 45 LYS T 63 1 19
HELIX 83 83 ALA T 71 ALA T 80 1 10
HELIX 84 84 PHE U 18 CYS U 22 5 5
HELIX 85 85 ALA U 25 ARG U 33 1 9
HELIX 86 86 LYS U 39 ALA U 47 1 9
SHEET 1 A 5 PHE B 89 VAL B 91 0
SHEET 2 A 5 ILE B 66 VAL B 69 1 N PHE B 68 O VAL B 91
SHEET 3 A 5 ALA B 159 VAL B 162 1 O PHE B 161 N LEU B 67
SHEET 4 A 5 VAL B 182 ALA B 184 1 O PHE B 183 N LEU B 160
SHEET 5 A 5 PHE B 197 VAL B 198 1 O PHE B 197 N VAL B 182
SHEET 1 B 2 VAL C 51 ILE C 54 0
SHEET 2 B 2 ILE C 67 THR C 69 -1 O HIS C 68 N SER C 52
SHEET 1 C 4 ARG C 168 GLY C 170 0
SHEET 2 C 4 GLY C 147 SER C 153 -1 N ILE C 148 O GLU C 169
SHEET 3 C 4 GLY C 196 PHE C 202 -1 O PHE C 202 N GLY C 147
SHEET 4 C 4 TYR C 183 ASN C 184 -1 N ASN C 184 O VAL C 199
SHEET 1 D 5 ARG D 127 VAL D 128 0
SHEET 2 D 5 ILE D 122 VAL D 124 -1 N VAL D 124 O ARG D 127
SHEET 3 D 5 VAL D 141 ILE D 144 -1 O SER D 143 N MET D 123
SHEET 4 D 5 GLU D 178 THR D 180 -1 O GLY D 179 N VAL D 142
SHEET 5 D 5 GLU D 171 ASP D 173 -1 N ASP D 173 O GLU D 178
SHEET 1 E 3 LYS E 13 ASN E 18 0
SHEET 2 E 3 PHE E 32 VAL E 37 -1 O LEU E 35 N ALA E 16
SHEET 3 E 3 PHE E 47 ALA E 52 -1 O GLY E 48 N THR E 36
SHEET 1 F 2 THR E 23 VAL E 24 0
SHEET 2 F 2 GLY E 27 ARG E 28 -1 O GLY E 27 N VAL E 24
SHEET 1 G 2 ARG E 44 VAL E 45 0
SHEET 2 G 2 ILE E 71 ASN E 72 -1 O ILE E 71 N VAL E 45
SHEET 1 H 3 VAL E 84 HIS E 88 0
SHEET 2 H 3 SER E 91 PRO E 97 -1 O MET E 95 N VAL E 84
SHEET 3 H 3 VAL E 122 GLY E 128 -1 O LEU E 123 N GLN E 96
SHEET 1 I 4 ARG F 45 ILE F 51 0
SHEET 2 I 4 LEU F 54 LEU F 61 -1 O ALA F 57 N ARG F 45
SHEET 3 I 4 GLU F 5 VAL F 10 -1 N VAL F 10 O HIS F 58
SHEET 4 I 4 VAL F 84 MET F 90 -1 O ILE F 85 N MET F 9
SHEET 1 J 2 VAL G 72 GLU G 73 0
SHEET 2 J 2 VAL G 88 GLU G 89 -1 O VAL G 88 N GLU G 73
SHEET 1 K 3 ALA H 23 THR H 25 0
SHEET 2 K 3 GLU H 59 LEU H 62 -1 O LEU H 60 N VAL H 24
SHEET 3 K 3 ILE H 45 LYS H 49 -1 N LYS H 49 O GLU H 59
SHEET 1 L 4 TYR H 85 LYS H 86 0
SHEET 2 L 4 GLY H 122 VAL H 128 -1 O GLY H 122 N LYS H 86
SHEET 3 L 4 ILE H 100 SER H 104 -1 N SER H 104 O GLU H 123
SHEET 4 L 4 VAL H 109 MET H 110 -1 O MET H 110 N VAL H 103
SHEET 1 M 4 TYR I 5 ARG I 10 0
SHEET 2 M 4 ALA I 15 ILE I 20 -1 O ALA I 16 N GLY I 9
SHEET 3 M 4 LEU I 62 LYS I 67 -1 O TYR I 63 N PHE I 19
SHEET 4 M 4 ILE I 27 ILE I 29 1 N VAL I 28 O LEU I 62
SHEET 1 N 2 ARG J 7 LYS J 11 0
SHEET 2 N 2 ASP J 97 SER J 101 -1 O ASP J 97 N LYS J 11
SHEET 1 O 3 PHE J 49 VAL J 51 0
SHEET 2 O 3 ASP J 63 GLU J 66 -1 O TYR J 65 N PHE J 49
SHEET 3 O 3 LYS N 96 LYS N 97 -1 O LYS N 96 N GLU J 66
SHEET 1 P 5 ALA K 40 THR K 45 0
SHEET 2 P 5 THR K 29 ASP K 35 -1 N ILE K 33 O GLY K 42
SHEET 3 P 5 ASP K 17 ALA K 24 -1 N VAL K 19 O THR K 34
SHEET 4 P 5 ASN K 80 LYS K 86 1 O ASN K 80 N GLY K 18
SHEET 5 P 5 ARG K 105 ASP K 111 1 O ASN K 108 N VAL K 83
SHEET 1 Q 3 LYS L 29 GLY L 31 0
SHEET 2 Q 3 ILE L 79 ILE L 81 -1 O ILE L 81 N LYS L 29
SHEET 3 Q 3 THR L 96 LEU L 101 -1 O VAL L 97 N LEU L 80
SHEET 1 R 2 VAL L 51 ARG L 53 0
SHEET 2 R 2 THR L 63 TYR L 65 -1 O SER L 64 N CYS L 52
SHEET 1 S 4 PHE P 32 ARG P 35 0
SHEET 2 S 4 VAL P 19 ASP P 23 -1 N VAL P 21 O ILE P 33
SHEET 3 S 4 VAL P 2 LEU P 6 -1 N ARG P 5 O VAL P 20
SHEET 4 S 4 THR P 66 ILE P 67 1 O THR P 66 N ILE P 4
SHEET 1 T 2 GLY P 10 ALA P 11 0
SHEET 2 T 2 ARG P 14 PRO P 15 -1 O ARG P 14 N ALA P 11
SHEET 1 U 2 PHE P 38 PHE P 39 0
SHEET 2 U 2 THR P 50 ARG P 51 -1 O ARG P 51 N PHE P 38
SHEET 1 V 6 LEU Q 7 MET Q 16 0
SHEET 2 V 6 SER Q 19 LYS Q 29 -1 O ALA Q 23 N ARG Q 10
SHEET 3 V 6 PHE Q 36 HIS Q 46 -1 O VAL Q 45 N ILE Q 20
SHEET 4 V 6 LYS Q 70 VAL Q 77 1 O LEU Q 74 N HIS Q 46
SHEET 5 V 6 VAL Q 57 SER Q 67 -1 N LEU Q 66 O LYS Q 70
SHEET 6 V 6 LEU Q 7 MET Q 16 -1 N LEU Q 7 O ILE Q 60
SHEET 1 W 2 ILE S 48 HIS S 51 0
SHEET 2 W 2 HIS S 56 VAL S 59 -1 O VAL S 57 N VAL S 50
LINK MG MG A1558 O HOH A1697 1555 1555 2.06
LINK MG MG A1565 O HOH A1731 1555 1555 2.06
LINK MG MG A1538 O HOH A1597 1555 1555 2.06
LINK MG MG A1545 O HOH A1628 1555 1555 2.07
LINK MG MG A1538 O HOH A1596 1555 1555 2.07
LINK MG MG A1571 O HOH A1757 1555 1555 2.07
LINK MG MG A1569 O HOH A1748 1555 1555 2.07
LINK MG MG A1565 O HOH A1729 1555 1555 2.07
LINK MG MG A1565 O HOH A1728 1555 1555 2.07
LINK MG MG A1545 O HOH A1629 1555 1555 2.07
LINK MG MG A1545 O HOH A1631 1555 1555 2.07
LINK MG MG A1569 O HOH A1749 1555 1555 2.07
LINK MG MG A1563 O HOH E 187 1555 1555 2.07
LINK MG MG A1571 O HOH A1758 1555 1555 2.07
LINK MG MG A1561 O HOH A1711 1555 1555 2.07
LINK MG MG A1538 O HOH A1594 1555 1555 2.07
LINK MG MG A1571 O HOH A1755 1555 1555 2.07
LINK MG MG A1565 O HOH A1730 1555 1555 2.07
LINK MG MG A1571 O HOH A1756 1555 1555 2.07
LINK MG MG A1561 O HOH A1713 1555 1555 2.07
LINK MG MG A1551 O HOH A1659 1555 1555 2.07
LINK MG MG A1558 O HOH A1700 1555 1555 2.07
LINK MG MG A1551 O HOH A1656 1555 1555 2.07
LINK MG MG A1563 O HOH A1722 1555 1555 2.07
LINK MG MG A1545 O HOH A1630 1555 1555 2.07
LINK MG MG A1558 O HOH A1699 1555 1555 2.07
LINK MG MG A1551 O HOH A1657 1555 1555 2.07
LINK MG MG A1572 O HOH A1762 1555 1555 2.07
LINK MG MG A1561 O HOH A1712 1555 1555 2.07
LINK MG MG A1561 O HOH A1714 1555 1555 2.07
LINK MG MG A1551 O HOH A1658 1555 1555 2.07
LINK MG MG A1563 O HOH A1720 1555 1555 2.07
LINK MG MG A1538 O HOH A1595 1555 1555 2.07
LINK MG MG A1569 O HOH A1747 1555 1555 2.08
LINK MG MG A1572 O HOH A1761 1555 1555 2.08
LINK MG MG A1558 O HOH A1698 1555 1555 2.08
LINK MG MG A1539 O HOH A1601 1555 1555 2.08
LINK MG MG A1574 O HOH A1768 1555 1555 2.08
LINK MG MG A1557 O HOH A1694 1555 1555 2.08
LINK MG MG A1557 O HOH A1695 1555 1555 2.08
LINK MG MG A1542 O HOH A1614 1555 1555 2.08
LINK MG MG A1566 O HOH A1733 1555 1555 2.08
LINK MG MG A1548 O HOH A1642 1555 1555 2.08
LINK MG MG A1572 O HOH A1760 1555 1555 2.08
LINK MG MG A1572 O HOH A1763 1555 1555 2.08
LINK MG MG A1567 O HOH A1738 1555 1555 2.08
LINK MG MG A1562 O HOH A1716 1555 1555 2.08
LINK MG MG A1566 O HOH A1735 1555 1555 2.08
LINK MG MG A1566 O HOH A1736 1555 1555 2.08
LINK MG MG A1563 O HOH A1721 1555 1555 2.08
LINK MG MG A1539 O HOH A1600 1555 1555 2.08
LINK MG MG A1567 O HOH A1739 1555 1555 2.08
LINK MG MG A1562 O HOH A1717 1555 1555 2.08
LINK MG MG A1546 O HOH A1635 1555 1555 2.08
LINK MG MG A1546 O HOH A1633 1555 1555 2.08
LINK MG MG A1567 O HOH A1740 1555 1555 2.08
LINK MG MG A1572 O HOH A1759 1555 1555 2.08
LINK MG MG A1557 O HOH A1696 1555 1555 2.08
LINK MG MG A1570 O HOH A1754 1555 1555 2.08
LINK MG MG A1539 O HOH A1599 1555 1555 2.08
LINK MG MG A1562 O HOH A1718 1555 1555 2.08
LINK MG MG A1574 O HOH A1771 1555 1555 2.08
LINK MG MG A1574 O HOH A1767 1555 1555 2.08
LINK MG MG A1539 O HOH A1602 1555 1555 2.08
LINK MG MG A1548 O HOH A1645 1555 1555 2.08
LINK MG MG A1542 O HOH A1612 1555 1555 2.08
LINK MG MG A1570 O HOH A1750 1555 1555 2.08
LINK MG MG A1566 O HOH A1732 1555 1555 2.08
LINK MG MG A1564 O HOH A1725 1555 1555 2.08
LINK MG MG A1536 O HOH A1583 1555 1555 2.08
LINK MG MG A1570 O HOH A1751 1555 1555 2.08
LINK MG MG A1564 O HOH A1723 1555 1555 2.08
LINK MG MG A1548 O HOH A1646 1555 1555 2.08
LINK MG MG A1570 O HOH A1752 1555 1555 2.08
LINK MG MG A1546 O HOH A1632 1555 1555 2.08
LINK MG MG A1540 O HOH A1605 1555 1555 2.08
LINK MG MG A1536 O HOH A1584 1555 1555 2.08
LINK MG MG A1557 O HOH A1693 1555 1555 2.08
LINK MG MG A1547 O HOH A1637 1555 1555 2.08
LINK MG MG A1548 O HOH A1644 1555 1555 2.08
LINK MG MG A1553 O HOH A1666 1555 1555 2.08
LINK MG MG A1564 O HOH A1727 1555 1555 2.08
LINK MG MG A1566 O HOH A1734 1555 1555 2.08
LINK MG MG A1567 O HOH A1737 1555 1555 2.08
LINK MG MG A1574 O HOH A1770 1555 1555 2.08
LINK MG MG A1536 O HOH A1586 1555 1555 2.08
LINK MG MG A1540 O HOH A1606 1555 1555 2.08
LINK MG MG A1567 O HOH A1741 1555 1555 2.08
LINK MG MG A1548 O HOH A1643 1555 1555 2.08
LINK MG MG A1574 O HOH A1769 1555 1555 2.08
LINK MG MG A1553 O HOH A1668 1555 1555 2.08
LINK MG MG A1536 O HOH A1587 1555 1555 2.08
LINK MG MG A1553 O HOH A1670 1555 1555 2.08
LINK MG MG A1560 O HOH A1707 1555 1555 2.08
LINK MG MG A1540 O HOH A1603 1555 1555 2.08
LINK MG MG A1557 O HOH A1692 1555 1555 2.08
LINK MG MG A1562 O HOH A1719 1555 1555 2.08
LINK MG MG A1553 O HOH A1669 1555 1555 2.08
LINK MG MG A1553 O HOH A1667 1555 1555 2.08
LINK MG MG A1547 O HOH A1639 1555 1555 2.08
LINK MG MG A1547 O HOH A1638 1555 1555 2.08
LINK MG MG A1547 O HOH A1640 1555 1555 2.08
LINK MG MG A1560 O HOH A1709 1555 1555 2.08
LINK MG MG A1547 O HOH A1641 1555 1555 2.08
LINK MG MG A1564 O HOH A1724 1555 1555 2.08
LINK MG MG A1546 O HOH A1634 1555 1555 2.08
LINK MG MG A1540 O HOH A1604 1555 1555 2.08
LINK MG MG A1536 O HOH A1585 1555 1555 2.08
LINK MG MG A1562 O HOH A1715 1555 1555 2.08
LINK MG MG A1564 O HOH A1726 1555 1555 2.09
LINK MG MG A1570 O HOH A1753 1555 1555 2.09
LINK MG MG A1560 O HOH A1710 1555 1555 2.09
LINK MG MG A1542 O HOH A1615 1555 1555 2.09
LINK MG MG A1542 O HOH A1613 1555 1555 2.09
LINK MG MG A1560 O HOH I 169 1555 1555 2.09
LINK MG MG A1539 O HOH A1598 1555 1555 2.09
LINK MG MG A1542 O HOH A1611 1555 1555 2.09
LINK MG MG A1560 O HOH A1708 1555 1555 2.09
LINK MG MG A1546 O HOH A1636 1555 1555 2.09
LINK MG MG A1540 O HOH A1607 1555 1555 2.09
LINK OP2 G A 100 MG MG A1570 1555 1555 2.10
LINK MG MG A1544 O HOH A1624 1555 1555 2.17
LINK MG MG A1554 O HOH A1672 1555 1555 2.17
LINK MG MG A1541 O HOH A1610 1555 1555 2.17
LINK MG MG A1573 O HOH A1764 1555 1555 2.18
LINK MG MG A1541 O HOH A1609 1555 1555 2.18
LINK MG MG A1544 O HOH A1622 1555 1555 2.18
LINK MG MG E 159 O HOH A1690 1555 1555 2.18
LINK MG MG A1537 O HOH A1590 1555 1555 2.18
LINK MG MG A1568 O HOH A1746 1555 1555 2.18
LINK MG MG E 159 O HOH A1686 1555 1555 2.18
LINK MG MG A1535 O HOH A1579 1555 1555 2.18
LINK MG MG A1556 O HOH A1680 1555 1555 2.18
LINK MG MG A1544 O HOH A1625 1555 1555 2.18
LINK MG MG A1568 O HOH A1744 1555 1555 2.18
LINK MG MG A 1 O HOH T 87 1555 1555 2.18
LINK MG MG A1550 O HOH A1651 1555 1555 2.18
LINK MG MG A1550 O HOH A1652 1555 1555 2.18
LINK MG MG A 1 O HOH A1575 1555 1555 2.18
LINK MG MG A1550 O HOH N 105 1555 1555 2.18
LINK MG MG A1556 O HOH A1684 1555 1555 2.18
LINK MG MG A1555 O HOH A1678 1555 1555 2.18
LINK MG MG A1537 O HOH A1591 1555 1555 2.18
LINK MG MG A1537 O HOH A1589 1555 1555 2.18
LINK MG MG A1537 O HOH A1592 1555 1555 2.18
LINK MG MG A1543 O HOH A1616 1555 1555 2.18
LINK MG MG A1555 O HOH A1677 1555 1555 2.18
LINK MG MG A 1 O HOH A 4 1555 1555 2.18
LINK MG MG A1549 O HOH N 101 1555 1555 2.18
LINK MG MG A1544 O HOH A1626 1555 1555 2.18
LINK MG MG A1550 O HOH A1654 1555 1555 2.18
LINK MG MG A1550 O HOH A1653 1555 1555 2.18
LINK MG MG A1543 O HOH A1617 1555 1555 2.18
LINK MG MG A1573 O HOH A1766 1555 1555 2.18
LINK MG MG A 1 O HOH A 2 1555 1555 2.18
LINK MG MG A1543 O HOH A1618 1555 1555 2.18
LINK MG MG A1568 O HOH A1742 1555 1555 2.18
LINK MG MG A1549 O HOH A1648 1555 1555 2.18
LINK MG MG A1535 O HOH A1578 1555 1555 2.18
LINK MG MG A1535 O HOH A1581 1555 1555 2.18
LINK MG MG A1554 O HOH A1673 1555 1555 2.18
LINK MG MG A 1 O HOH A1576 1555 1555 2.18
LINK MG MG A1543 O HOH A1620 1555 1555 2.18
LINK MG MG A1537 O HOH A1593 1555 1555 2.18
LINK MG MG A1549 O HOH A1650 1555 1555 2.18
LINK MG MG A1550 O HOH A1655 1555 1555 2.18
LINK MG MG A1559 O HOH A1704 1555 1555 2.18
LINK MG MG A1555 O HOH A1679 1555 1555 2.18
LINK MG MG A1559 O HOH A1703 1555 1555 2.18
LINK MG MG A1535 O HOH A1582 1555 1555 2.18
LINK MG MG A1559 O HOH A1705 1555 1555 2.18
LINK MG MG A1552 O HOH A1662 1555 1555 2.18
LINK MG MG A1535 O HOH A1577 1555 1555 2.18
LINK MG MG A1549 O HOH N 102 1555 1555 2.18
LINK MG MG A1555 O HOH A1674 1555 1555 2.18
LINK MG MG A1549 O HOH A1649 1555 1555 2.18
LINK MG MG A1541 O HOH A1608 1555 1555 2.18
LINK MG MG E 159 O HOH A1688 1555 1555 2.18
LINK MG MG A1555 O HOH A1675 1555 1555 2.18
LINK MG MG A1543 O HOH A1621 1555 1555 2.18
LINK MG MG A1552 O HOH A1665 1555 1555 2.18
LINK MG MG A1549 O HOH A1647 1555 1555 2.18
LINK MG MG A1559 O HOH A1702 1555 1555 2.18
LINK MG MG A1556 O HOH A1685 1555 1555 2.18
LINK MG MG A1556 O HOH A1682 1555 1555 2.18
LINK MG MG A1537 O HOH A1588 1555 1555 2.18
LINK MG MG A1559 O HOH A1706 1555 1555 2.18
LINK MG MG E 159 O HOH A1687 1555 1555 2.18
LINK MG MG A1568 O HOH A1743 1555 1555 2.18
LINK MG MG A1544 O HOH A1623 1555 1555 2.18
LINK MG MG A1568 O HOH U 218 1555 1555 2.18
LINK MG MG A1552 O HOH A1661 1555 1555 2.18
LINK MG MG A 1 O HOH A 3 1555 1555 2.18
LINK MG MG A1543 O HOH A1619 1555 1555 2.18
LINK MG MG E 159 O HOH A1691 1555 1555 2.18
LINK MG MG A1552 O HOH A1663 1555 1555 2.18
LINK MG MG E 159 O HOH A1689 1555 1555 2.18
LINK MG MG A1552 O HOH A1664 1555 1555 2.18
LINK MG MG A1556 O HOH A1681 1555 1555 2.19
LINK MG MG A1573 O HOH A1765 1555 1555 2.19
LINK MG MG A1554 O HOH A1671 1555 1555 2.19
LINK MG MG A1552 O HOH A1660 1555 1555 2.19
LINK MG MG A1555 O HOH A1676 1555 1555 2.19
LINK MG MG A1544 O HOH A1627 1555 1555 2.19
LINK MG MG A1556 O HOH A1683 1555 1555 2.19
LINK MG MG A1535 O HOH A1580 1555 1555 2.19
LINK MG MG A1559 O HOH A1701 1555 1555 2.19
LINK MG MG A1568 O HOH A1745 1555 1555 2.19
LINK OP2 A A 510 MG MG A1538 1555 1555 2.23
LINK OP1 G A1505 MG MG A1554 1555 1555 2.27
LINK OP1 G A 558 MG MG A1563 1555 1555 2.27
LINK OP1 A A1500 MG MG A1554 1555 1555 2.29
LINK OP2 A A1500 MG MG A1569 1555 1555 2.31
LINK OP1 C A 578 MG MG A1542 1555 1555 2.32
LINK OP1 A A 547 MG MG A1539 1555 1555 2.34
LINK OP2 A A 116 MG MG A1573 1555 1555 2.36
LINK OP2 G A 289 MG MG A1573 1555 1555 2.37
LINK O4 U A 516 MG MG A1565 1555 1555 2.38
LINK OP2 A A1110 MG MG A1567 1555 1555 2.39
LINK OP2 A A1433 MG MG A1562 1555 1555 2.39
LINK OP1 A A 533 MG MG A1565 1555 1555 2.42
LINK OP2 G A1505 MG MG A1569 1555 1555 2.43
LINK OP1 A A1508 MG MG A1554 1555 1555 2.45
LINK OP2 A A 195 MG MG A1571 1555 1555 2.49
LINK OP1 G A 21 MG MG A1557 1555 1555 2.49
LINK OP2 A A 937 MG MG A1548 1555 1555 2.50
LINK OP2 A A 573 MG MG A1541 1555 1555 2.51
LINK OP2 A A 814 MG MG A1545 1555 1555 2.55
LINK OP2 A A 574 MG MG A1541 1555 1555 2.56
LINK OP1 G A1198 MG MG A1561 1555 1555 2.57
LINK OP2 A A 560 MG MG A1540 1555 1555 2.59
LINK OP1 C A 934 MG MG A1547 1555 1555 2.62
LINK O6 G A1417 MG MG A1553 1555 1555 2.62
LINK OP2 A A 509 MG MG A1538 1555 1555 2.63
LINK OP2 A A 572 MG MG A1541 1555 1555 2.65
LINK OP2 U A 891 MG MG A1546 1555 1555 2.65
LINK OP2 G A 117 MG MG A1573 1555 1555 2.72
LINK O4 U A 180 MG MG A1571 1555 1555 2.74
LINK OP2 A A 608 MG MG A1566 1555 1555 2.76
LINK OP2 G A 577 MG MG A1545 1555 1555 2.80
LINK O6 G A 299 MG MG A1563 1555 1555 2.81
LINK O5' A A 509 MG MG A1538 1555 1555 2.83
LINK O6 G A 362 MG MG A1536 1555 1555 2.89
SITE 1 AC1 6 HOH A 2 HOH A 3 HOH A 4 HOH A1575
SITE 2 AC1 6 HOH A1576 HOH T 87
SITE 1 AC2 6 HOH A1577 HOH A1578 HOH A1579 HOH A1580
SITE 2 AC2 6 HOH A1581 HOH A1582
SITE 1 AC3 6 G A 362 HOH A1583 HOH A1584 HOH A1585
SITE 2 AC3 6 HOH A1586 HOH A1587
SITE 1 AC4 6 HOH A1588 HOH A1589 HOH A1590 HOH A1591
SITE 2 AC4 6 HOH A1592 HOH A1593
SITE 1 AC5 7 U A 508 A A 509 A A 510 HOH A1594
SITE 2 AC5 7 HOH A1595 HOH A1596 HOH A1597
SITE 1 AC6 6 A A 547 HOH A1598 HOH A1599 HOH A1600
SITE 2 AC6 6 HOH A1601 HOH A1602
SITE 1 AC7 7 A A 560 G A 566 HOH A1603 HOH A1604
SITE 2 AC7 7 HOH A1605 HOH A1606 HOH A1607
SITE 1 AC8 6 A A 572 A A 573 A A 574 HOH A1608
SITE 2 AC8 6 HOH A1609 HOH A1610
SITE 1 AC9 6 C A 578 HOH A1611 HOH A1612 HOH A1613
SITE 2 AC9 6 HOH A1614 HOH A1615
SITE 1 BC1 6 HOH A1616 HOH A1617 HOH A1618 HOH A1619
SITE 2 BC1 6 HOH A1620 HOH A1621
SITE 1 BC2 6 HOH A1622 HOH A1623 HOH A1624 HOH A1625
SITE 2 BC2 6 HOH A1626 HOH A1627
SITE 1 BC3 6 G A 577 A A 814 HOH A1628 HOH A1629
SITE 2 BC3 6 HOH A1630 HOH A1631
SITE 1 BC4 6 U A 891 HOH A1632 HOH A1633 HOH A1634
SITE 2 BC4 6 HOH A1635 HOH A1636
SITE 1 BC5 7 G A 933 C A 934 HOH A1637 HOH A1638
SITE 2 BC5 7 HOH A1639 HOH A1640 HOH A1641
SITE 1 BC6 6 A A 937 HOH A1642 HOH A1643 HOH A1644
SITE 2 BC6 6 HOH A1645 HOH A1646
SITE 1 BC7 6 HOH A1647 HOH A1648 HOH A1649 HOH A1650
SITE 2 BC7 6 HOH N 101 HOH N 102
SITE 1 BC8 7 A A1204 HOH A1651 HOH A1652 HOH A1653
SITE 2 BC8 7 HOH A1654 HOH A1655 HOH N 105
SITE 1 BC9 5 C A1054 HOH A1656 HOH A1657 HOH A1658
SITE 2 BC9 5 HOH A1659
SITE 1 CC1 6 HOH A1660 HOH A1661 HOH A1662 HOH A1663
SITE 2 CC1 6 HOH A1664 HOH A1665
SITE 1 CC2 6 G A1417 HOH A1666 HOH A1667 HOH A1668
SITE 2 CC2 6 HOH A1669 HOH A1670
SITE 1 CC3 7 A A1500 G A1505 A A1507 A A1508
SITE 2 CC3 7 HOH A1671 HOH A1672 HOH A1673
SITE 1 CC4 6 HOH A1674 HOH A1675 HOH A1676 HOH A1677
SITE 2 CC4 6 HOH A1678 HOH A1679
SITE 1 CC5 6 HOH A1680 HOH A1681 HOH A1682 HOH A1683
SITE 2 CC5 6 HOH A1684 HOH A1685
SITE 1 CC6 6 G A 21 HOH A1692 HOH A1693 HOH A1694
SITE 2 CC6 6 HOH A1695 HOH A1696
SITE 1 CC7 6 G A 858 G A 869 HOH A1697 HOH A1698
SITE 2 CC7 6 HOH A1699 HOH A1700
SITE 1 CC8 6 HOH A1701 HOH A1702 HOH A1703 HOH A1704
SITE 2 CC8 6 HOH A1705 HOH A1706
SITE 1 CC9 6 U A1348 HOH A1707 HOH A1708 HOH A1709
SITE 2 CC9 6 HOH A1710 HOH I 169
SITE 1 DC1 6 G A1198 U A1199 HOH A1711 HOH A1712
SITE 2 DC1 6 HOH A1713 HOH A1714
SITE 1 DC2 6 A A1433 HOH A1715 HOH A1716 HOH A1717
SITE 2 DC2 6 HOH A1718 HOH A1719
SITE 1 DC3 7 G A 299 G A 557 G A 558 HOH A1720
SITE 2 DC3 7 HOH A1721 HOH A1722 HOH E 187
SITE 1 DC4 6 G A 324 HOH A1723 HOH A1724 HOH A1725
SITE 2 DC4 6 HOH A1726 HOH A1727
SITE 1 DC5 6 U A 516 A A 533 HOH A1728 HOH A1729
SITE 2 DC5 6 HOH A1730 HOH A1731
SITE 1 DC6 6 A A 608 HOH A1732 HOH A1733 HOH A1734
SITE 2 DC6 6 HOH A1735 HOH A1736
SITE 1 DC7 6 A A1110 HOH A1737 HOH A1738 HOH A1739
SITE 2 DC7 6 HOH A1740 HOH A1741
SITE 1 DC8 6 HOH A1742 HOH A1743 HOH A1744 HOH A1745
SITE 2 DC8 6 HOH A1746 HOH U 218
SITE 1 DC9 7 A A1499 A A1500 G A1504 G A1505
SITE 2 DC9 7 HOH A1747 HOH A1748 HOH A1749
SITE 1 EC1 6 G A 100 HOH A1750 HOH A1751 HOH A1752
SITE 2 EC1 6 HOH A1753 HOH A1754
SITE 1 EC2 6 U A 180 A A 195 HOH A1755 HOH A1756
SITE 2 EC2 6 HOH A1757 HOH A1758
SITE 1 EC3 6 C A 536 HOH A1759 HOH A1760 HOH A1761
SITE 2 EC3 6 HOH A1762 HOH A1763
SITE 1 EC4 6 A A 116 G A 117 G A 289 HOH A1764
SITE 2 EC4 6 HOH A1765 HOH A1766
SITE 1 EC5 7 C A 330 C A 352 HOH A1767 HOH A1768
SITE 2 EC5 7 HOH A1769 HOH A1770 HOH A1771
SITE 1 EC6 6 HOH A1686 HOH A1687 HOH A1688 HOH A1689
SITE 2 EC6 6 HOH A1690 HOH A1691
CRYST1 210.759 433.272 618.863 90.00 90.00 90.00 P 21 21 21 4
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 0.004745 0.000000 0.000000 0.00000
SCALE2 0.000000 0.002308 0.000000 0.00000
SCALE3 0.000000 0.000000 0.001616 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
