HEADER RIBOSOME 14-AUG-10 3OFB
TITLE CRYSTAL STRUCTURE OF THE E. COLI RIBOSOME BOUND TO CHLORAMPHENICOL.
TITLE 2 THIS FILE CONTAINS THE 30S SUBUNIT OF THE SECOND 70S RIBOSOME.
SPLIT 3OFA 3OFB 3OFC 3OFD
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,
KEYWDS 2 CHLORAMPHENICOL, ANTIBIOTIC, EXIT, PEPTIDYL, 30S, 70S, 16S,
KEYWDS 3 RIBOSOMAL SUBUNIT, SMALL, RIBOSOME
EXPDTA X-RAY DIFFRACTION
AUTHOR J.A.DUNKLE,L.XIONG,A.S.MANKIN,J.H.D.CATE
REVDAT 1 20-OCT-10 3OFB 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. 3.19 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
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) : 3.19
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 82.15
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.060
REMARK 3 COMPLETENESS FOR RANGE (%) : 75.8
REMARK 3 NUMBER OF REFLECTIONS : 708760
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.192
REMARK 3 R VALUE (WORKING SET) : 0.191
REMARK 3 FREE R VALUE : 0.252
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.020
REMARK 3 FREE R VALUE TEST SET COUNT : 14298
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 82.1728 - 6.8805 0.92 86487 1773 0.1914 0.2329
REMARK 3 2 6.8805 - 5.4616 0.91 84047 1759 0.1631 0.2431
REMARK 3 3 5.4616 - 4.7713 0.86 78754 1588 0.1654 0.2292
REMARK 3 4 4.7713 - 4.3351 0.83 75864 1585 0.1736 0.2399
REMARK 3 5 4.3351 - 4.0244 0.80 72679 1511 0.1769 0.2373
REMARK 3 6 4.0244 - 3.7871 0.76 69007 1409 0.1853 0.2463
REMARK 3 7 3.7871 - 3.5975 0.70 64203 1323 0.2010 0.2661
REMARK 3 8 3.5975 - 3.4409 0.65 59546 1252 0.2296 0.2990
REMARK 3 9 3.4409 - 3.3084 0.60 55014 1106 0.2524 0.3142
REMARK 3 10 3.3084 - 3.1942 0.54 48861 992 0.2897 0.3615
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 : 41.10
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 3.620
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.140
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) : -2.33100
REMARK 3 B22 (A**2) : -7.60010
REMARK 3 B33 (A**2) : 7.00780
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 308513
REMARK 3 ANGLE : 1.427 462189
REMARK 3 CHIRALITY : 0.077 58597
REMARK 3 PLANARITY : 0.005 24721
REMARK 3 DIHEDRAL : 28.169 160833
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): -62.7325 12.5588 -76.1069
REMARK 3 T TENSOR
REMARK 3 T11: 0.3227 T22: 0.1064
REMARK 3 T33: 0.1116 T12: 0.1060
REMARK 3 T13: 0.1580 T23: 0.2957
REMARK 3 L TENSOR
REMARK 3 L11: 0.1002 L22: 0.3294
REMARK 3 L33: 0.1612 L12: -0.0831
REMARK 3 L13: -0.2117 L23: -0.1699
REMARK 3 S TENSOR
REMARK 3 S11: 0.0008 S12: 0.0863 S13: 0.0829
REMARK 3 S21: -0.4063 S22: -0.1040 S23: -0.1384
REMARK 3 S31: -0.1816 S32: -0.0984 S33: -0.1880
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): -86.0624 36.4537 -31.0855
REMARK 3 T TENSOR
REMARK 3 T11: 0.3708 T22: 0.1295
REMARK 3 T33: 0.3304 T12: 0.1120
REMARK 3 T13: 0.0222 T23: 0.1123
REMARK 3 L TENSOR
REMARK 3 L11: -0.0011 L22: 0.0184
REMARK 3 L33: 0.0053 L12: -0.0138
REMARK 3 L13: 0.0036 L23: -0.0273
REMARK 3 S TENSOR
REMARK 3 S11: -0.0221 S12: 0.0366 S13: 0.0635
REMARK 3 S21: 0.0096 S22: -0.0753 S23: 0.0015
REMARK 3 S31: -0.0570 S32: 0.0340 S33: 0.0000
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN QE AND RESID 9:73)
REMARK 3 ORIGIN FOR THE GROUP (A): -98.6415 57.1918 -39.9847
REMARK 3 T TENSOR
REMARK 3 T11: 0.7568 T22: 0.6397
REMARK 3 T33: 0.8382 T12: 0.2407
REMARK 3 T13: -0.0237 T23: 0.2364
REMARK 3 L TENSOR
REMARK 3 L11: 0.0036 L22: 0.0072
REMARK 3 L33: 0.0001 L12: -0.0108
REMARK 3 L13: -0.0003 L23: -0.0028
REMARK 3 S TENSOR
REMARK 3 S11: 0.0092 S12: -0.0031 S13: 0.0085
REMARK 3 S21: -0.0226 S22: -0.0157 S23: 0.0047
REMARK 3 S31: -0.0199 S32: -0.0091 S33: 0.0000
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN QE AND RESID 74:149)
REMARK 3 ORIGIN FOR THE GROUP (A): -80.0601 55.3712 -47.4684
REMARK 3 T TENSOR
REMARK 3 T11: 0.7169 T22: 0.6810
REMARK 3 T33: 0.7372 T12: 0.1803
REMARK 3 T13: 0.0306 T23: 0.2648
REMARK 3 L TENSOR
REMARK 3 L11: 0.0022 L22: 0.0038
REMARK 3 L33: 0.0009 L12: -0.0041
REMARK 3 L13: -0.0007 L23: -0.0019
REMARK 3 S TENSOR
REMARK 3 S11: -0.0256 S12: 0.0183 S13: -0.0048
REMARK 3 S21: -0.0153 S22: -0.0077 S23: -0.0042
REMARK 3 S31: -0.0126 S32: 0.0066 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): -86.4231 85.8030 -20.1709
REMARK 3 T TENSOR
REMARK 3 T11: 1.5725 T22: 1.3724
REMARK 3 T33: 1.6656 T12: 0.0262
REMARK 3 T13: -0.0390 T23: 0.1432
REMARK 3 L TENSOR
REMARK 3 L11: 0.0080 L22: 0.0157
REMARK 3 L33: 0.0045 L12: 0.0010
REMARK 3 L13: -0.0010 L23: -0.0003
REMARK 3 S TENSOR
REMARK 3 S11: -0.0069 S12: 0.0001 S13: -0.0035
REMARK 3 S21: 0.0225 S22: -0.0048 S23: -0.0221
REMARK 3 S31: -0.0133 S32: 0.0152 S33: 0.0000
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: (CHAIN QB AND RESID 108:146)
REMARK 3 ORIGIN FOR THE GROUP (A):-118.2881 84.5026 -17.7748
REMARK 3 T TENSOR
REMARK 3 T11: 1.4326 T22: 1.4156
REMARK 3 T33: 1.4535 T12: 0.0430
REMARK 3 T13: -0.0044 T23: 0.0004
REMARK 3 L TENSOR
REMARK 3 L11: 0.0005 L22: 0.0011
REMARK 3 L33: 0.0006 L12: -0.0002
REMARK 3 L13: 0.0001 L23: -0.0004
REMARK 3 S TENSOR
REMARK 3 S11: 0.0043 S12: -0.0022 S13: 0.0035
REMARK 3 S21: -0.0036 S22: -0.0028 S23: -0.0005
REMARK 3 S31: 0.0007 S32: -0.0032 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):-146.4429 44.3083 -3.5667
REMARK 3 T TENSOR
REMARK 3 T11: 0.5669 T22: 0.4907
REMARK 3 T33: 0.9414 T12: 0.2679
REMARK 3 T13: 0.2509 T23: 0.4130
REMARK 3 L TENSOR
REMARK 3 L11: 0.3011 L22: -0.0157
REMARK 3 L33: 0.1430 L12: 0.0204
REMARK 3 L13: 0.0677 L23: -0.2072
REMARK 3 S TENSOR
REMARK 3 S11: 0.0163 S12: -0.1020 S13: -0.1064
REMARK 3 S21: 0.0788 S22: 0.2315 S23: 0.1199
REMARK 3 S31: -0.0493 S32: -0.1833 S33: -0.0000
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: (CHAIN QA AND RESID 987:1047)
REMARK 3 ORIGIN FOR THE GROUP (A):-168.3833 20.5995 -45.5516
REMARK 3 T TENSOR
REMARK 3 T11: 1.4238 T22: 1.3699
REMARK 3 T33: 1.4360 T12: -0.0079
REMARK 3 T13: -0.0998 T23: 0.1531
REMARK 3 L TENSOR
REMARK 3 L11: 0.0118 L22: 0.0125
REMARK 3 L33: -0.0011 L12: 0.0055
REMARK 3 L13: 0.0061 L23: 0.0024
REMARK 3 S TENSOR
REMARK 3 S11: 0.0339 S12: 0.0025 S13: -0.0257
REMARK 3 S21: 0.0110 S22: -0.0010 S23: -0.0038
REMARK 3 S31: 0.0108 S32: -0.0419 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): -64.8076 38.7281 -2.7265
REMARK 3 T TENSOR
REMARK 3 T11: 0.4098 T22: 0.0665
REMARK 3 T33: 0.4041 T12: 0.0518
REMARK 3 T13: -0.0738 T23: 0.0170
REMARK 3 L TENSOR
REMARK 3 L11: 0.1031 L22: 0.2832
REMARK 3 L33: 0.1261 L12: -0.1310
REMARK 3 L13: 0.0327 L23: -0.0170
REMARK 3 S TENSOR
REMARK 3 S11: -0.0765 S12: -0.0278 S13: 0.2114
REMARK 3 S21: 0.1664 S22: 0.0850 S23: -0.0832
REMARK 3 S31: -0.1840 S32: -0.0136 S33: 0.0052
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): -56.3088 -6.6354 -41.8744
REMARK 3 T TENSOR
REMARK 3 T11: 0.0876 T22: 0.1466
REMARK 3 T33: 0.2638 T12: -0.0037
REMARK 3 T13: 0.2201 T23: 0.1932
REMARK 3 L TENSOR
REMARK 3 L11: 0.0104 L22: 0.2153
REMARK 3 L33: 0.1076 L12: 0.0562
REMARK 3 L13: -0.0411 L23: -0.1639
REMARK 3 S TENSOR
REMARK 3 S11: -0.1663 S12: -0.0033 S13: 0.0690
REMARK 3 S21: -0.1052 S22: -0.0994 S23: -0.0751
REMARK 3 S31: -0.0776 S32: 0.0221 S33: -0.0756
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): -29.3714 34.7217 104.2371
REMARK 3 T TENSOR
REMARK 3 T11: 0.8783 T22: 0.2137
REMARK 3 T33: 0.6061 T12: -0.0223
REMARK 3 T13: -0.2842 T23: 0.1244
REMARK 3 L TENSOR
REMARK 3 L11: 0.2913 L22: -0.1028
REMARK 3 L33: 0.3316 L12: -0.0356
REMARK 3 L13: -0.0675 L23: 0.0410
REMARK 3 S TENSOR
REMARK 3 S11: -0.0744 S12: -0.1129 S13: -0.2546
REMARK 3 S21: 0.1066 S22: 0.0156 S23: -0.0063
REMARK 3 S31: -0.0019 S32: 0.1031 S33: -0.0000
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): -41.1813 81.7139 75.7999
REMARK 3 T TENSOR
REMARK 3 T11: 1.0708 T22: 0.3304
REMARK 3 T33: 0.4220 T12: -0.3693
REMARK 3 T13: -0.4468 T23: 0.1302
REMARK 3 L TENSOR
REMARK 3 L11: 0.0020 L22: 0.0188
REMARK 3 L33: 0.0208 L12: 0.0117
REMARK 3 L13: 0.0224 L23: 0.0263
REMARK 3 S TENSOR
REMARK 3 S11: 0.0784 S12: -0.0098 S13: -0.1144
REMARK 3 S21: -0.0347 S22: 0.0190 S23: -0.0498
REMARK 3 S31: -0.0389 S32: -0.0450 S33: -0.0000
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: (CHAIN XE AND RESID 9:73)
REMARK 3 ORIGIN FOR THE GROUP (A): -51.2334 73.7542 53.1019
REMARK 3 T TENSOR
REMARK 3 T11: 0.9415 T22: 0.7922
REMARK 3 T33: 0.7117 T12: -0.1146
REMARK 3 T13: -0.4453 T23: -0.0989
REMARK 3 L TENSOR
REMARK 3 L11: 0.0019 L22: 0.0016
REMARK 3 L33: 0.0058 L12: 0.0001
REMARK 3 L13: 0.0098 L23: 0.0012
REMARK 3 S TENSOR
REMARK 3 S11: 0.0234 S12: 0.0148 S13: -0.0094
REMARK 3 S21: 0.0146 S22: 0.0287 S23: 0.0073
REMARK 3 S31: -0.0137 S32: 0.0074 S33: -0.0000
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: (CHAIN XE AND RESID 74:149)
REMARK 3 ORIGIN FOR THE GROUP (A): -34.5283 63.6736 58.7067
REMARK 3 T TENSOR
REMARK 3 T11: 0.9915 T22: 0.7112
REMARK 3 T33: 0.8578 T12: -0.2246
REMARK 3 T13: -0.2816 T23: -0.0521
REMARK 3 L TENSOR
REMARK 3 L11: 0.0009 L22: 0.0022
REMARK 3 L33: 0.0029 L12: 0.0021
REMARK 3 L13: 0.0041 L23: -0.0017
REMARK 3 S TENSOR
REMARK 3 S11: -0.0177 S12: -0.0082 S13: -0.0003
REMARK 3 S21: -0.0045 S22: 0.0099 S23: -0.0151
REMARK 3 S31: 0.0172 S32: 0.0305 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): -30.7605 90.0037 26.8703
REMARK 3 T TENSOR
REMARK 3 T11: 1.6383 T22: 1.5341
REMARK 3 T33: 1.3687 T12: -0.1129
REMARK 3 T13: -0.0491 T23: -0.1029
REMARK 3 L TENSOR
REMARK 3 L11: 0.0045 L22: 0.0037
REMARK 3 L33: 0.0094 L12: 0.0017
REMARK 3 L13: -0.0028 L23: -0.0012
REMARK 3 S TENSOR
REMARK 3 S11: 0.0186 S12: 0.0315 S13: 0.0124
REMARK 3 S21: -0.0085 S22: 0.0086 S23: -0.0321
REMARK 3 S31: 0.0066 S32: 0.0033 S33: -0.0000
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: (CHAIN XB AND RESID 108:146)
REMARK 3 ORIGIN FOR THE GROUP (A): -61.6105 96.7913 22.0380
REMARK 3 T TENSOR
REMARK 3 T11: 1.6282 T22: 1.6322
REMARK 3 T33: 1.5931 T12: 0.0102
REMARK 3 T13: -0.0528 T23: 0.0224
REMARK 3 L TENSOR
REMARK 3 L11: 0.0012 L22: 0.0010
REMARK 3 L33: 0.0017 L12: 0.0012
REMARK 3 L13: 0.0008 L23: -0.0001
REMARK 3 S TENSOR
REMARK 3 S11: 0.0036 S12: 0.0025 S13: 0.0026
REMARK 3 S21: 0.0042 S22: 0.0010 S23: 0.0034
REMARK 3 S31: 0.0001 S32: -0.0014 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): -95.3402 114.9150 55.5724
REMARK 3 T TENSOR
REMARK 3 T11: 0.8230 T22: 0.4892
REMARK 3 T33: 0.7978 T12: -0.1370
REMARK 3 T13: -0.3583 T23: 0.2943
REMARK 3 L TENSOR
REMARK 3 L11: 0.2273 L22: 0.0392
REMARK 3 L33: 0.0338 L12: -0.1179
REMARK 3 L13: 0.0882 L23: 0.0554
REMARK 3 S TENSOR
REMARK 3 S11: -0.2602 S12: -0.0404 S13: 0.1670
REMARK 3 S21: 0.1102 S22: 0.2139 S23: 0.2561
REMARK 3 S31: 0.0535 S32: -0.1508 S33: 0.0000
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: (CHAIN XA AND RESID 987:1047)
REMARK 3 ORIGIN FOR THE GROUP (A):-125.5708 75.1686 73.9037
REMARK 3 T TENSOR
REMARK 3 T11: 2.5035 T22: 2.5311
REMARK 3 T33: 2.4852 T12: -0.0732
REMARK 3 T13: -0.0114 T23: 0.0725
REMARK 3 L TENSOR
REMARK 3 L11: 0.0039 L22: -0.0006
REMARK 3 L33: 0.0046 L12: -0.0010
REMARK 3 L13: -0.0048 L23: -0.0113
REMARK 3 S TENSOR
REMARK 3 S11: 0.0256 S12: 0.0292 S13: -0.0367
REMARK 3 S21: -0.0135 S22: -0.0254 S23: 0.0597
REMARK 3 S31: 0.0023 S32: -0.0158 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): -15.2156 106.3592 76.4895
REMARK 3 T TENSOR
REMARK 3 T11: 0.8358 T22: 0.1756
REMARK 3 T33: 0.0997 T12: -0.3504
REMARK 3 T13: -0.2922 T23: 0.0495
REMARK 3 L TENSOR
REMARK 3 L11: 0.5987 L22: 0.2558
REMARK 3 L33: -0.0369 L12: 0.2128
REMARK 3 L13: 0.0056 L23: -0.0146
REMARK 3 S TENSOR
REMARK 3 S11: 0.1932 S12: -0.0341 S13: -0.0390
REMARK 3 S21: 0.0949 S22: -0.2623 S23: -0.3664
REMARK 3 S31: -0.0813 S32: 0.0752 S33: -0.0303
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): -22.9389 69.1716 123.9538
REMARK 3 T TENSOR
REMARK 3 T11: 1.1856 T22: 0.7245
REMARK 3 T33: 0.6198 T12: -0.1696
REMARK 3 T13: -0.4402 T23: 0.2736
REMARK 3 L TENSOR
REMARK 3 L11: 0.0622 L22: 0.1273
REMARK 3 L33: 0.0726 L12: 0.1310
REMARK 3 L13: 0.0015 L23: 0.0970
REMARK 3 S TENSOR
REMARK 3 S11: -0.1021 S12: -0.0004 S13: -0.1233
REMARK 3 S21: -0.0401 S22: 0.1359 S23: -0.1590
REMARK 3 S31: -0.0573 S32: 0.1670 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): -65.6485 -59.7158 15.2851
REMARK 3 T TENSOR
REMARK 3 T11: 0.0169 T22: 0.0866
REMARK 3 T33: 0.0930 T12: -0.0016
REMARK 3 T13: -0.0491 T23: -0.0174
REMARK 3 L TENSOR
REMARK 3 L11: 0.1210 L22: 0.1265
REMARK 3 L33: 0.0611 L12: -0.0109
REMARK 3 L13: -0.0386 L23: -0.0029
REMARK 3 S TENSOR
REMARK 3 S11: -0.0113 S12: -0.0138 S13: 0.0340
REMARK 3 S21: 0.0490 S22: 0.0037 S23: -0.0477
REMARK 3 S31: -0.0143 S32: 0.0135 S33: 0.0493
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):-139.5239 -50.6080 -62.9387
REMARK 3 T TENSOR
REMARK 3 T11: 0.2341 T22: 0.3002
REMARK 3 T33: 0.6864 T12: 0.0144
REMARK 3 T13: -0.2382 T23: 0.2485
REMARK 3 L TENSOR
REMARK 3 L11: 0.0266 L22: 0.0159
REMARK 3 L33: -0.0016 L12: 0.0290
REMARK 3 L13: 0.0342 L23: -0.0385
REMARK 3 S TENSOR
REMARK 3 S11: 0.0934 S12: -0.0703 S13: 0.1199
REMARK 3 S21: -0.1164 S22: 0.0681 S23: -0.1027
REMARK 3 S31: -0.1611 S32: -0.0147 S33: 0.0020
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: (CHAIN RA AND RESID 1906:1929)
REMARK 3 ORIGIN FOR THE GROUP (A):-103.3699 -3.9086 -3.1772
REMARK 3 T TENSOR
REMARK 3 T11: 0.3295 T22: 0.5105
REMARK 3 T33: 0.2271 T12: 0.0070
REMARK 3 T13: 0.0455 T23: 0.0278
REMARK 3 L TENSOR
REMARK 3 L11: 0.0083 L22: -0.0029
REMARK 3 L33: 0.0009 L12: -0.0051
REMARK 3 L13: -0.0009 L23: -0.0028
REMARK 3 S TENSOR
REMARK 3 S11: -0.0304 S12: -0.0352 S13: 0.0223
REMARK 3 S21: -0.0308 S22: 0.0461 S23: 0.0383
REMARK 3 S31: 0.0001 S32: -0.0136 S33: 0.0000
REMARK 3 TLS GROUP : 24
REMARK 3 SELECTION: (CHAIN RA AND RESID 2093:2197)
REMARK 3 ORIGIN FOR THE GROUP (A): -95.4065 18.9356 79.1870
REMARK 3 T TENSOR
REMARK 3 T11: 0.4706 T22: 0.4158
REMARK 3 T33: 0.5673 T12: 0.0349
REMARK 3 T13: 0.0508 T23: -0.1244
REMARK 3 L TENSOR
REMARK 3 L11: 0.0181 L22: 0.0260
REMARK 3 L33: 0.0025 L12: 0.0325
REMARK 3 L13: -0.0007 L23: 0.0231
REMARK 3 S TENSOR
REMARK 3 S11: 0.0033 S12: -0.0042 S13: -0.0689
REMARK 3 S21: 0.0030 S22: 0.0982 S23: -0.0068
REMARK 3 S31: -0.0684 S32: -0.1728 S33: -0.0000
REMARK 3 TLS GROUP : 25
REMARK 3 SELECTION: (CHAIN RA AND RESID 877:901)
REMARK 3 ORIGIN FOR THE GROUP (A):-148.5882 -27.4458 -12.0550
REMARK 3 T TENSOR
REMARK 3 T11: 1.6086 T22: 1.5208
REMARK 3 T33: 1.5976 T12: -0.0035
REMARK 3 T13: 0.0650 T23: -0.0135
REMARK 3 L TENSOR
REMARK 3 L11: -0.0006 L22: 0.0007
REMARK 3 L33: 0.0007 L12: -0.0010
REMARK 3 L13: -0.0019 L23: -0.0011
REMARK 3 S TENSOR
REMARK 3 S11: -0.0136 S12: 0.0287 S13: 0.0301
REMARK 3 S21: 0.0006 S22: -0.0145 S23: 0.0125
REMARK 3 S31: -0.0102 S32: -0.0069 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):-166.0794 -23.7566 16.2755
REMARK 3 T TENSOR
REMARK 3 T11: 0.0823 T22: 0.3289
REMARK 3 T33: 0.6670 T12: -0.0530
REMARK 3 T13: 0.0234 T23: 0.1544
REMARK 3 L TENSOR
REMARK 3 L11: 0.0197 L22: 0.0329
REMARK 3 L33: 0.0180 L12: -0.0015
REMARK 3 L13: 0.0173 L23: -0.0200
REMARK 3 S TENSOR
REMARK 3 S11: -0.0044 S12: 0.0792 S13: 0.0552
REMARK 3 S21: 0.0010 S22: 0.0364 S23: 0.0433
REMARK 3 S31: -0.1403 S32: 0.2124 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):-174.5116 -53.9240 30.3466
REMARK 3 T TENSOR
REMARK 3 T11: 0.0558 T22: 0.3050
REMARK 3 T33: 0.5634 T12: 0.0484
REMARK 3 T13: 0.1408 T23: -0.0145
REMARK 3 L TENSOR
REMARK 3 L11: 0.0519 L22: 0.0151
REMARK 3 L33: 0.0247 L12: -0.0113
REMARK 3 L13: 0.0228 L23: 0.0084
REMARK 3 S TENSOR
REMARK 3 S11: 0.0667 S12: 0.0306 S13: -0.0207
REMARK 3 S21: 0.0614 S22: -0.1741 S23: 0.2121
REMARK 3 S31: 0.0431 S32: -0.0449 S33: 0.0007
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):-143.5929 -80.2747 -7.7201
REMARK 3 T TENSOR
REMARK 3 T11: 0.0228 T22: 0.2117
REMARK 3 T33: 0.3355 T12: -0.0239
REMARK 3 T13: -0.0096 T23: -0.0615
REMARK 3 L TENSOR
REMARK 3 L11: 0.0184 L22: 0.0259
REMARK 3 L33: 0.0227 L12: 0.0138
REMARK 3 L13: 0.0235 L23: 0.0045
REMARK 3 S TENSOR
REMARK 3 S11: -0.0346 S12: 0.0391 S13: 0.0470
REMARK 3 S21: -0.0337 S22: -0.0421 S23: 0.1258
REMARK 3 S31: 0.0756 S32: -0.0980 S33: 0.0003
REMARK 3 TLS GROUP : 29
REMARK 3 SELECTION: (CHAIN RH AND RESID 49:149)
REMARK 3 ORIGIN FOR THE GROUP (A): -65.1817 20.2763 122.4195
REMARK 3 T TENSOR
REMARK 3 T11: 1.9051 T22: 1.8657
REMARK 3 T33: 1.8102 T12: -0.0427
REMARK 3 T13: -0.0523 T23: -0.0630
REMARK 3 L TENSOR
REMARK 3 L11: -0.0004 L22: 0.0028
REMARK 3 L33: 0.0087 L12: 0.0004
REMARK 3 L13: -0.0017 L23: -0.0066
REMARK 3 S TENSOR
REMARK 3 S11: 0.0090 S12: -0.0200 S13: 0.0550
REMARK 3 S21: 0.0150 S22: 0.0058 S23: 0.0258
REMARK 3 S31: -0.0340 S32: -0.0218 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 (CHAINY
REMARK 3 ORIGIN FOR THE GROUP (A): -30.0769 131.2368 171.5278
REMARK 3 T TENSOR
REMARK 3 T11: 0.7601 T22: 0.6002
REMARK 3 T33: -0.2239 T12: -0.3242
REMARK 3 T13: -0.3308 T23: -0.3444
REMARK 3 L TENSOR
REMARK 3 L11: 0.0624 L22: 0.1065
REMARK 3 L33: 0.5045 L12: 0.0761
REMARK 3 L13: -0.3333 L23: -0.0600
REMARK 3 S TENSOR
REMARK 3 S11: -0.0459 S12: -0.4413 S13: -0.0567
REMARK 3 S21: 0.3060 S22: 0.2835 S23: 0.2282
REMARK 3 S31: -0.2112 S32: 0.3269 S33: 0.2712
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):-116.9094 72.6313 150.9392
REMARK 3 T TENSOR
REMARK 3 T11: 2.7029 T22: 2.8662
REMARK 3 T33: 2.7659 T12: -0.0878
REMARK 3 T13: 0.0343 T23: -0.0894
REMARK 3 L TENSOR
REMARK 3 L11: 0.0274 L22: 0.0057
REMARK 3 L33: 0.0107 L12: 0.0200
REMARK 3 L13: 0.0024 L23: 0.0039
REMARK 3 S TENSOR
REMARK 3 S11: 0.0698 S12: -0.0176 S13: 0.0450
REMARK 3 S21: -0.0571 S22: 0.0093 S23: 0.0117
REMARK 3 S31: 0.0299 S32: 0.0116 S33: -0.0000
REMARK 3 TLS GROUP : 32
REMARK 3 SELECTION: (CHAIN YA AND RESID 1906:1929)
REMARK 3 ORIGIN FOR THE GROUP (A): -60.4667 115.7123 110.7637
REMARK 3 T TENSOR
REMARK 3 T11: 1.1923 T22: 1.0682
REMARK 3 T33: 1.0388 T12: -0.3615
REMARK 3 T13: 0.0223 T23: -0.0332
REMARK 3 L TENSOR
REMARK 3 L11: -0.0023 L22: 0.0005
REMARK 3 L33: 0.0085 L12: 0.0043
REMARK 3 L13: -0.0005 L23: -0.0029
REMARK 3 S TENSOR
REMARK 3 S11: -0.0236 S12: 0.0005 S13: -0.0017
REMARK 3 S21: 0.0104 S22: -0.0393 S23: 0.0163
REMARK 3 S31: -0.0310 S32: 0.0240 S33: 0.0000
REMARK 3 TLS GROUP : 33
REMARK 3 SELECTION: (CHAIN YA AND RESID 2093:2197)
REMARK 3 ORIGIN FOR THE GROUP (A): -28.7671 193.5812 91.1900
REMARK 3 T TENSOR
REMARK 3 T11: 1.1583 T22: 1.2262
REMARK 3 T33: 1.1937 T12: 0.0553
REMARK 3 T13: 0.1488 T23: 0.0089
REMARK 3 L TENSOR
REMARK 3 L11: 0.0062 L22: -0.0058
REMARK 3 L33: -0.0028 L12: -0.0160
REMARK 3 L13: -0.0066 L23: -0.0172
REMARK 3 S TENSOR
REMARK 3 S11: -0.0371 S12: 0.0190 S13: 0.0376
REMARK 3 S21: -0.0243 S22: -0.0734 S23: 0.0812
REMARK 3 S31: -0.0202 S32: -0.1148 S33: 0.0000
REMARK 3 TLS GROUP : 34
REMARK 3 SELECTION: (CHAIN YA AND RESID 877:901)
REMARK 3 ORIGIN FOR THE GROUP (A):-110.3630 125.1396 133.0175
REMARK 3 T TENSOR
REMARK 3 T11: 1.7489 T22: 1.7629
REMARK 3 T33: 1.7686 T12: 0.0054
REMARK 3 T13: -0.0132 T23: -0.0225
REMARK 3 L TENSOR
REMARK 3 L11: 0.0007 L22: 0.0008
REMARK 3 L33: 0.0002 L12: -0.0003
REMARK 3 L13: -0.0003 L23: 0.0002
REMARK 3 S TENSOR
REMARK 3 S11: -0.0037 S12: -0.0006 S13: 0.0076
REMARK 3 S21: -0.0014 S22: -0.0016 S23: -0.0019
REMARK 3 S31: -0.0009 S32: -0.0022 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):-121.3874 152.3692 117.0347
REMARK 3 T TENSOR
REMARK 3 T11: 2.3357 T22: 2.4137
REMARK 3 T33: 2.3866 T12: 0.0466
REMARK 3 T13: -0.0059 T23: 0.0080
REMARK 3 L TENSOR
REMARK 3 L11: 0.0098 L22: 0.0077
REMARK 3 L33: 0.0064 L12: 0.0029
REMARK 3 L13: -0.0004 L23: 0.0015
REMARK 3 S TENSOR
REMARK 3 S11: -0.0148 S12: 0.0257 S13: 0.0152
REMARK 3 S21: -0.0381 S22: 0.0001 S23: 0.0095
REMARK 3 S31: -0.0052 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):-129.3912 170.7844 144.2357
REMARK 3 T TENSOR
REMARK 3 T11: 1.5503 T22: 1.6567
REMARK 3 T33: 1.6898 T12: 0.2663
REMARK 3 T13: 0.0686 T23: 0.2346
REMARK 3 L TENSOR
REMARK 3 L11: 0.0334 L22: 0.0114
REMARK 3 L33: 0.0041 L12: -0.0199
REMARK 3 L13: -0.0063 L23: -0.0067
REMARK 3 S TENSOR
REMARK 3 S11: -0.0073 S12: -0.0096 S13: -0.0644
REMARK 3 S21: 0.0016 S22: 0.0119 S23: 0.0459
REMARK 3 S31: -0.0309 S32: -0.0082 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):-113.7384 128.7140 177.5545
REMARK 3 T TENSOR
REMARK 3 T11: 1.1749 T22: 1.5042
REMARK 3 T33: 1.3490 T12: 0.1898
REMARK 3 T13: 0.0824 T23: 0.2509
REMARK 3 L TENSOR
REMARK 3 L11: 0.0147 L22: 0.0108
REMARK 3 L33: 0.0200 L12: 0.0070
REMARK 3 L13: -0.0108 L23: -0.0055
REMARK 3 S TENSOR
REMARK 3 S11: -0.0616 S12: 0.0582 S13: 0.0173
REMARK 3 S21: -0.0156 S22: -0.0078 S23: -0.0035
REMARK 3 S31: 0.0328 S32: -0.0181 S33: 0.0000
REMARK 3 TLS GROUP : 38
REMARK 3 SELECTION: (CHAIN YH AND RESID 49:149)
REMARK 3 ORIGIN FOR THE GROUP (A): 11.0099 227.6656 88.9835
REMARK 3 T TENSOR
REMARK 3 T11: 1.6960 T22: 1.6550
REMARK 3 T33: 1.6404 T12: 0.0453
REMARK 3 T13: 0.0841 T23: 0.0662
REMARK 3 L TENSOR
REMARK 3 L11: 0.0053 L22: 0.0067
REMARK 3 L33: 0.0016 L12: -0.0007
REMARK 3 L13: 0.0032 L23: 0.0013
REMARK 3 S TENSOR
REMARK 3 S11: -0.0014 S12: 0.0354 S13: 0.0372
REMARK 3 S21: -0.0291 S22: -0.0410 S23: 0.0133
REMARK 3 S31: -0.0181 S32: -0.0261 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 3OFB COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-AUG-10.
REMARK 100 THE RCSB ID CODE IS RCSB061043.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-OCT-09
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) : 1.1158
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 : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 708760
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.194
REMARK 200 RESOLUTION RANGE LOW (A) : 100.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.800
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 82.6
REMARK 200 DATA REDUNDANCY : 2.000
REMARK 200 R MERGE (I) : 0.07200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.19
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.42
REMARK 200 COMPLETENESS FOR SHELL (%) : 69.7
REMARK 200 DATA REDUNDANCY IN SHELL : 1.50
REMARK 200 R MERGE FOR SHELL (I) : 0.43500
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 105.72800
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 310.61650
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 217.04200
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 310.61650
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 105.72800
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 217.04200
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: THE COMPLETE ASYMMETRIC UNIT CONTAINS TWO RIBOSOMES, WHICH
REMARK 300 ARE SPLIT INTO FOUR PDB ENTRIES 3OFA, 3OFB, 3OFC, AND 3OFD DUE TO
REMARK 300 PDB FORMAT LIMITATIONS. THE FIRST BIOLOGICAL ASSEMBLY IS COMPOSED
REMARK 300 OF PDB ENTRIES 3OFA (30S) AND 3OFC (50S). THE SECOND BIOLOGICAL
REMARK 300 ASSEMBLY IS COMPOSED OF PDB ENTRIES 3OFB (30S) AND 3OFD (50S).
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' C A 513 O4' C A 514 2.05
REMARK 500 O2' C A 1051 O5' U A 1052 2.07
REMARK 500 O2' A A 366 N2 G A 394 2.09
REMARK 500 O2' C A 1200 OP2 A A 1201 2.12
REMARK 500 O2' C A 1217 O4' C A 1218 2.13
REMARK 500 OP2 A A 608 O HOH A 1735 2.16
REMARK 500 O2' U A 992 OP2 G A 993 2.17
REMARK 500 O2' G A 1181 O4' G A 1182 2.17
REMARK 500 N7 G A 858 O HOH A 1698 2.18
REMARK 500 O2' A A 792 N7 A A 794 2.18
REMARK 500 O2' A A 1447 OP1 C A 1448 2.18
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 A 8 O3' G A 9 P -0.104
REMARK 500 A A 26 O3' G A 27 P -0.106
REMARK 500 U A 562 O3' A A 563 P -0.113
REMARK 500 G A1047 O3' G A1048 P 0.088
REMARK 500 A A1396 O3' C A1397 P -0.135
REMARK 500 ARG B 107 C GLN B 108 N 0.148
REMARK 500 SER B 146 C LEU B 147 N 0.233
REMARK 500 PRO L 21 C ALA L 22 N 0.197
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 U A 14 N1 - C1' - C2' ANGL. DEV. = -13.8 DEGREES
REMARK 500 U A 13 C3' - O3' - P ANGL. DEV. = 9.4 DEGREES
REMARK 500 U A 14 C3' - O3' - P ANGL. DEV. = -7.9 DEGREES
REMARK 500 G A 15 C3' - O3' - P ANGL. DEV. = -8.4 DEGREES
REMARK 500 A A 32 C3' - O3' - P ANGL. DEV. = -10.4 DEGREES
REMARK 500 U A 37 O4' - C1' - N1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 C A 52 N1 - C1' - C2' ANGL. DEV. = -8.3 DEGREES
REMARK 500 A A 60 C3' - O3' - P ANGL. DEV. = 10.0 DEGREES
REMARK 500 C A 63 O4' - C1' - N1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 A A 65 C3' - O3' - P ANGL. DEV. = 13.9 DEGREES
REMARK 500 C A 67 O4' - C1' - N1 ANGL. DEV. = 5.3 DEGREES
REMARK 500 A A 66 C3' - O3' - P ANGL. DEV. = -16.8 DEGREES
REMARK 500 G A 68 N9 - C1' - C2' ANGL. DEV. = -7.0 DEGREES
REMARK 500 G A 68 C3' - O3' - P ANGL. DEV. = -9.1 DEGREES
REMARK 500 U A 70 O4' - C1' - N1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 A A 71 C3' - C2' - C1' ANGL. DEV. = 4.8 DEGREES
REMARK 500 U A 70 C3' - O3' - P ANGL. DEV. = 8.5 DEGREES
REMARK 500 C A 73 N1 - C1' - C2' ANGL. DEV. = -11.5 DEGREES
REMARK 500 C A 73 O4' - C1' - N1 ANGL. DEV. = 7.1 DEGREES
REMARK 500 A A 72 C3' - O3' - P ANGL. DEV. = -7.8 DEGREES
REMARK 500 A A 81 C3' - O3' - P ANGL. DEV. = 7.5 DEGREES
REMARK 500 C A 83 O4' - C1' - N1 ANGL. DEV. = 4.6 DEGREES
REMARK 500 U A 85 C3' - O3' - P ANGL. DEV. = 10.9 DEGREES
REMARK 500 C A 87 N1 - C1' - C2' ANGL. DEV. = -8.1 DEGREES
REMARK 500 C A 87 O4' - C1' - N1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 G A 86 C3' - O3' - P ANGL. DEV. = 9.0 DEGREES
REMARK 500 U A 89 N1 - C1' - C2' ANGL. DEV. = -9.7 DEGREES
REMARK 500 U A 92 N1 - C1' - C2' ANGL. DEV. = -13.3 DEGREES
REMARK 500 U A 92 C3' - O3' - P ANGL. DEV. = -8.7 DEGREES
REMARK 500 C A 95 N1 - C1' - C2' ANGL. DEV. = -10.1 DEGREES
REMARK 500 G A 94 C3' - O3' - P ANGL. DEV. = 8.0 DEGREES
REMARK 500 U A 96 N1 - C1' - C2' ANGL. DEV. = -10.8 DEGREES
REMARK 500 C A 95 C3' - O3' - P ANGL. DEV. = -7.9 DEGREES
REMARK 500 U A 96 C3' - O3' - P ANGL. DEV. = -9.0 DEGREES
REMARK 500 C A 110 N1 - C1' - C2' ANGL. DEV. = -8.6 DEGREES
REMARK 500 A A 109 C3' - O3' - P ANGL. DEV. = 12.0 DEGREES
REMARK 500 C A 110 C3' - O3' - P ANGL. DEV. = -11.4 DEGREES
REMARK 500 A A 116 N9 - C1' - C2' ANGL. DEV. = -7.4 DEGREES
REMARK 500 G A 115 C3' - O3' - P ANGL. DEV. = 9.7 DEGREES
REMARK 500 A A 116 C3' - O3' - P ANGL. DEV. = -12.6 DEGREES
REMARK 500 G A 122 C3' - O3' - P ANGL. DEV. = -9.0 DEGREES
REMARK 500 A A 129 C3' - O3' - P ANGL. DEV. = 7.5 DEGREES
REMARK 500 C A 132 N1 - C1' - C2' ANGL. DEV. = -15.8 DEGREES
REMARK 500 C A 132 O4' - C1' - N1 ANGL. DEV. = 6.4 DEGREES
REMARK 500 C A 132 C3' - O3' - P ANGL. DEV. = -8.6 DEGREES
REMARK 500 U A 170 O4' - C1' - N1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 U A 173 O4' - C1' - N1 ANGL. DEV. = 7.5 DEGREES
REMARK 500 U A 173 C3' - O3' - P ANGL. DEV. = 8.7 DEGREES
REMARK 500 A A 174 C3' - O3' - P ANGL. DEV. = -8.5 DEGREES
REMARK 500 C A 183 O4' - C1' - N1 ANGL. DEV. = 7.0 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 286 ANGLE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 LEU B 9 -74.14 -100.10
REMARK 500 LYS B 10 -15.76 81.74
REMARK 500 ALA B 11 46.49 -88.29
REMARK 500 HIS B 17 -140.51 -117.21
REMARK 500 GLN B 18 109.26 63.03
REMARK 500 THR B 19 -72.27 -93.86
REMARK 500 ARG B 20 40.11 -103.89
REMARK 500 TRP B 22 -156.22 -72.22
REMARK 500 MET B 26 -3.72 -176.10
REMARK 500 PHE B 29 35.50 -84.54
REMARK 500 LYS B 36 51.89 37.81
REMARK 500 ASN B 41 88.37 -65.72
REMARK 500 PHE B 49 -2.88 -144.46
REMARK 500 SER B 61 35.16 -72.52
REMARK 500 LYS B 72 114.69 -37.34
REMARK 500 ARG B 73 -36.30 -31.55
REMARK 500 ASP B 81 -103.63 5.61
REMARK 500 LEU B 84 83.46 -52.39
REMARK 500 SER B 85 -56.86 -175.47
REMARK 500 CYS B 86 176.19 -59.09
REMARK 500 GLN B 88 -162.30 -167.00
REMARK 500 HIS B 93 -140.38 -91.88
REMARK 500 LEU B 100 -63.78 -106.30
REMARK 500 THR B 101 40.67 -70.38
REMARK 500 ASN B 102 32.03 163.98
REMARK 500 ARG B 112 4.11 -68.84
REMARK 500 PHE B 125 4.25 -69.55
REMARK 500 LEU B 128 96.09 47.59
REMARK 500 THR B 129 -92.97 -6.44
REMARK 500 LEU B 134 -73.03 -135.36
REMARK 500 THR B 137 -46.34 -139.32
REMARK 500 LEU B 147 42.40 -95.53
REMARK 500 ILE B 150 -9.34 -178.94
REMARK 500 PRO B 157 -168.18 -70.17
REMARK 500 ALA B 159 149.11 -175.53
REMARK 500 ILE B 163 -79.76 -89.65
REMARK 500 ASN B 177 28.30 -70.36
REMARK 500 LEU B 178 -79.83 -123.88
REMARK 500 THR B 188 -6.02 -51.92
REMARK 500 PRO B 200 102.17 -45.33
REMARK 500 ASN B 202 -158.58 -116.95
REMARK 500 ASP B 203 -7.17 -160.67
REMARK 500 ALA B 205 103.82 55.32
REMARK 500 ARG B 207 25.27 -76.48
REMARK 500 ALA B 208 -28.78 -155.36
REMARK 500 ALA B 218 -66.20 -159.61
REMARK 500 GLN C 2 -58.35 -29.96
REMARK 500 LYS C 15 138.90 -174.90
REMARK 500 SER C 19 71.91 -107.93
REMARK 500 THR C 20 38.73 -86.57
REMARK 500
REMARK 500 THIS ENTRY HAS 473 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 ARG B 107 -13.16
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 C A 132 -45.1 D D OUTSIDE RANGE
REMARK 500 TRP C 166 24.5 L L OUTSIDE RANGE
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 A1559 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A1700 O
REMARK 620 2 HOH A1698 O 89.2
REMARK 620 3 HOH A1697 O 90.4 179.6
REMARK 620 4 HOH A1699 O 87.7 90.4 89.6
REMARK 620 N 1 2 3
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 A1748 O
REMARK 620 2 HOH A1749 O 83.6
REMARK 620 3 HOH A1747 O 90.6 94.7
REMARK 620 4 A A1500 OP2 90.9 70.2 164.6
REMARK 620 5 G A1505 OP2 59.6 134.4 110.3 83.5
REMARK 620 6 G A1504 O2' 153.9 120.9 95.7 89.6 94.5
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 A1731 O
REMARK 620 2 HOH A1729 O 89.0
REMARK 620 3 HOH A1730 O 89.9 89.5
REMARK 620 4 HOH A1728 O 89.6 177.8 92.2
REMARK 620 5 U A 516 O4 64.8 88.2 154.7 89.6
REMARK 620 6 A A 533 OP1 146.0 64.8 109.9 115.9 91.9
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 89.0
REMARK 620 3 HOH A1595 O 91.5 179.5
REMARK 620 4 HOH A1598 O 87.9 91.7 88.5
REMARK 620 5 A A 510 OP2 151.0 66.7 112.9 77.8
REMARK 620 6 A A 509 OP2 81.8 63.7 116.1 153.3 99.9
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 E 187 O
REMARK 620 2 HOH A1721 O 89.4
REMARK 620 3 HOH A1720 O 90.7 177.6
REMARK 620 4 HOH A1722 O 179.7 90.4 89.6
REMARK 620 5 G A 558 OP1 106.0 76.2 101.5 73.8
REMARK 620 6 G A 299 O6 96.3 53.7 128.7 83.6 124.6
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 A1711 O
REMARK 620 2 HOH A1714 O 90.2
REMARK 620 3 HOH A1712 O 179.3 90.5
REMARK 620 4 HOH A1713 O 90.1 90.9 89.7
REMARK 620 5 G A1198 OP1 90.9 160.6 88.5 108.4
REMARK 620 N 1 2 3 4
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 A1758 O
REMARK 620 2 HOH A1756 O 90.5
REMARK 620 3 HOH A1757 O 91.1 89.8
REMARK 620 4 HOH A1755 O 89.7 179.6 90.5
REMARK 620 5 A A 195 OP2 143.3 106.5 120.5 73.2
REMARK 620 6 U A 180 O4 80.5 113.2 155.4 66.6 63.0
REMARK 620 7 A A 195 OP1 153.0 62.8 85.1 117.0 56.7 112.5
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 A1631 O
REMARK 620 2 HOH A1632 O 87.5
REMARK 620 3 HOH A1629 O 90.5 90.2
REMARK 620 4 HOH A1630 O 91.2 89.7 178.3
REMARK 620 5 A A 814 OP2 165.1 90.6 74.7 103.5
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 A1657 O
REMARK 620 2 HOH A1658 O 89.8
REMARK 620 3 HOH A1656 O 179.7 90.2
REMARK 620 4 HOH A1659 O 89.8 90.7 89.9
REMARK 620 N 1 2 3
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 A1586 O
REMARK 620 2 HOH A1584 O 89.7
REMARK 620 3 HOH A1588 O 89.4 89.2
REMARK 620 4 HOH A1587 O 179.9 90.2 90.6
REMARK 620 5 HOH A1585 O 90.1 179.5 90.4 90.0
REMARK 620 6 G A 362 O6 89.8 76.3 165.5 90.1 104.1
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 A1612 O
REMARK 620 2 HOH A1615 O 89.6
REMARK 620 3 HOH A1614 O 89.1 177.0
REMARK 620 4 HOH A1613 O 179.6 90.1 91.2
REMARK 620 5 HOH A1616 O 89.8 91.5 91.2 90.4
REMARK 620 6 C A 578 OP1 73.9 89.8 87.2 105.8 163.7
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 A1668 O
REMARK 620 2 HOH A1670 O 90.0
REMARK 620 3 HOH A1666 O 90.3 90.0
REMARK 620 4 HOH A1669 O 179.1 90.8 90.2
REMARK 620 5 HOH A1667 O 89.6 90.3 179.7 90.0
REMARK 620 6 G A1417 O6 94.3 156.9 112.7 84.8 67.0
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 A1734 O
REMARK 620 2 HOH A1735 O 178.9
REMARK 620 3 HOH A1733 O 88.9 90.0
REMARK 620 4 HOH A1736 O 91.6 88.5 90.9
REMARK 620 5 HOH A1732 O 90.7 90.4 179.5 89.4
REMARK 620 6 A A 608 OP2 126.8 53.7 115.7 131.1 64.4
REMARK 620 N 1 2 3 4 5
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 A1602 O
REMARK 620 2 HOH A1601 O 179.1
REMARK 620 3 HOH A1599 O 90.2 89.3
REMARK 620 4 HOH A1603 O 88.7 92.0 89.6
REMARK 620 5 HOH A1600 O 90.2 90.3 179.2 91.1
REMARK 620 6 A A 547 OP1 85.8 93.3 72.1 160.9 107.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1575 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A1768 O
REMARK 620 2 HOH A1771 O 91.0
REMARK 620 3 HOH A1769 O 89.3 90.7
REMARK 620 4 HOH A1767 O 179.2 88.7 90.0
REMARK 620 5 HOH A1770 O 90.3 89.2 179.6 90.4
REMARK 620 N 1 2 3 4
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 A1608 O 90.3
REMARK 620 3 HOH A1604 O 179.7 90.0
REMARK 620 4 HOH A1607 O 89.9 89.9 90.1
REMARK 620 5 HOH A1606 O 89.8 90.0 90.3 179.6
REMARK 620 6 A A 560 OP2 64.4 153.7 115.3 96.8 83.2
REMARK 620 N 1 2 3 4 5
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 A1695 O
REMARK 620 2 HOH A1696 O 90.8
REMARK 620 3 HOH A1693 O 90.0 90.9
REMARK 620 4 HOH A1694 O 179.3 89.6 89.5
REMARK 620 5 HOH A1692 O 89.2 88.8 179.1 91.4
REMARK 620 6 G A 21 OP1 113.0 142.9 115.9 66.9 64.7
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 A1646 O
REMARK 620 2 HOH A1643 O 89.8
REMARK 620 3 HOH A1644 O 89.9 179.7
REMARK 620 4 HOH A1647 O 90.5 89.8 90.1
REMARK 620 5 HOH A1645 O 179.5 90.2 90.1 90.0
REMARK 620 6 A A 937 OP2 100.8 96.7 83.4 166.9 78.7
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 A1754 O
REMARK 620 2 HOH A1750 O 90.4
REMARK 620 3 HOH A1752 O 90.3 89.2
REMARK 620 4 HOH A1753 O 91.0 90.2 178.5
REMARK 620 5 HOH A1751 O 89.5 179.3 91.4 89.2
REMARK 620 6 G A 100 OP2 161.5 92.5 108.0 70.7 87.4
REMARK 620 N 1 2 3 4 5
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 A1723 O
REMARK 620 2 HOH A1725 O 90.1
REMARK 620 3 HOH A1727 O 90.3 89.9
REMARK 620 4 HOH A1724 O 179.3 90.1 90.4
REMARK 620 5 HOH A1726 O 89.7 179.3 89.4 90.1
REMARK 620 N 1 2 3 4
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 A1763 O
REMARK 620 2 HOH A1760 O 90.5
REMARK 620 3 HOH A1759 O 90.7 178.8
REMARK 620 4 HOH A1762 O 89.7 89.3 90.4
REMARK 620 5 HOH A1761 O 88.8 90.8 89.5 178.4
REMARK 620 N 1 2 3 4
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 A1707 O
REMARK 620 2 HOH A1710 O 89.5
REMARK 620 3 HOH I 169 O 179.6 90.5
REMARK 620 4 HOH A1708 O 90.3 89.9 90.1
REMARK 620 5 HOH A1709 O 89.6 90.0 90.0 179.9
REMARK 620 N 1 2 3 4
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 A1636 O
REMARK 620 2 HOH A1633 O 89.7
REMARK 620 3 HOH A1634 O 89.7 179.2
REMARK 620 4 HOH A1637 O 89.6 89.6 89.8
REMARK 620 5 HOH A1635 O 178.2 90.1 90.5 92.2
REMARK 620 6 U A 891 OP2 82.0 64.5 115.9 152.7 96.4
REMARK 620 N 1 2 3 4 5
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 A1718 O
REMARK 620 2 HOH A1716 O 90.0
REMARK 620 3 HOH A1717 O 179.7 89.9
REMARK 620 4 HOH A1719 O 90.2 89.6 90.0
REMARK 620 5 HOH A1715 O 90.1 179.4 90.0 91.0
REMARK 620 6 A A1433 OP2 86.5 65.8 93.3 155.1 113.6
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 A1738 O
REMARK 620 2 HOH A1739 O 90.7
REMARK 620 3 HOH A1741 O 89.9 89.9
REMARK 620 4 HOH A1740 O 89.6 179.0 91.1
REMARK 620 5 HOH A1737 O 178.6 89.9 91.4 89.9
REMARK 620 6 A A1110 OP2 105.3 88.9 164.8 90.1 73.4
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 A1642 O
REMARK 620 2 HOH A1638 O 89.8
REMARK 620 3 HOH A1639 O 90.0 179.7
REMARK 620 4 HOH A1640 O 90.3 89.7 90.0
REMARK 620 5 HOH A1641 O 90.4 90.4 89.9 179.3
REMARK 620 6 C A 934 OP1 146.5 116.8 63.2 71.1 108.2
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 A1746 O
REMARK 620 2 HOH A1742 O 89.7
REMARK 620 3 HOH U 218 O 179.5 90.0
REMARK 620 4 HOH A1743 O 89.7 179.5 90.5
REMARK 620 5 HOH A1745 O 89.2 89.6 90.3 90.6
REMARK 620 6 HOH A1744 O 90.3 89.8 90.2 90.0 179.2
REMARK 620 N 1 2 3 4 5
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 A1625 O
REMARK 620 2 HOH A1627 O 88.6
REMARK 620 3 HOH A1624 O 88.9 89.1
REMARK 620 4 HOH A1623 O 90.6 90.7 179.5
REMARK 620 5 HOH A1628 O 90.6 179.2 91.0 89.1
REMARK 620 6 HOH A1626 O 178.6 90.5 90.0 90.4 90.3
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 178.6
REMARK 620 3 HOH A1611 O 90.8 90.5
REMARK 620 4 A A 572 OP2 100.8 77.9 131.8
REMARK 620 5 A A 573 OP2 86.7 92.7 138.9 88.7
REMARK 620 6 A A 574 OP2 73.7 107.4 68.6 159.5 71.4
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 A1764 O
REMARK 620 2 HOH A1766 O 89.9
REMARK 620 3 HOH A1765 O 178.7 90.9
REMARK 620 4 G A 117 OP2 68.7 83.5 112.4
REMARK 620 5 G A 289 OP2 70.1 98.4 108.8 138.8
REMARK 620 6 A A 116 OP2 65.7 154.3 113.7 80.4 81.3
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 A 4 O 90.0
REMARK 620 3 HOH A1576 O 90.0 179.9
REMARK 620 4 HOH A 2 O 89.3 89.7 90.2
REMARK 620 5 HOH A1577 O 179.5 90.4 89.5 90.5
REMARK 620 6 HOH A 3 O 90.3 89.7 90.4 179.3 89.8
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 90.2
REMARK 620 3 HOH A1675 O 90.5 89.0
REMARK 620 4 HOH A1679 O 179.7 89.6 89.6
REMARK 620 5 HOH A1674 O 89.3 90.5 179.5 90.6
REMARK 620 6 HOH A1676 O 89.7 179.8 90.9 90.5 89.6
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 91.3
REMARK 620 3 HOH A1671 O 178.9 89.7
REMARK 620 4 G A1505 OP1 106.8 133.4 72.7
REMARK 620 5 A A1500 OP1 114.1 143.5 64.8 65.8
REMARK 620 6 A A1508 OP1 91.8 90.4 87.8 130.2 64.4
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 A1580 O
REMARK 620 2 HOH A1583 O 89.6
REMARK 620 3 HOH A1578 O 90.4 90.4
REMARK 620 4 HOH A1579 O 89.4 89.8 179.8
REMARK 620 5 HOH A1582 O 90.4 180.0 89.6 90.2
REMARK 620 6 HOH A1581 O 179.7 90.1 89.6 90.6 89.9
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 A1652 O
REMARK 620 2 HOH N 105 O 90.2
REMARK 620 3 HOH A1654 O 90.8 89.8
REMARK 620 4 HOH A1653 O 89.3 89.5 179.4
REMARK 620 5 HOH A1651 O 179.5 90.1 89.7 90.2
REMARK 620 6 HOH A1655 O 89.4 179.5 89.9 90.8 90.3
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 A1618 O
REMARK 620 2 HOH A1621 O 89.6
REMARK 620 3 HOH A1617 O 180.0 90.4
REMARK 620 4 HOH A1622 O 90.1 179.6 89.9
REMARK 620 5 HOH A1620 O 89.8 90.0 90.2 90.2
REMARK 620 6 HOH A1619 O 90.2 89.8 89.8 90.0 179.8
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 A1649 O
REMARK 620 2 HOH N 102 O 89.9
REMARK 620 3 HOH A1650 O 90.0 89.9
REMARK 620 4 HOH A1648 O 179.9 90.0 90.0
REMARK 620 5 HOH N 101 O 90.2 179.9 90.1 89.9
REMARK 620 6 HOH N 103 O 90.0 90.1 179.9 90.1 89.8
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 A1706 O
REMARK 620 2 HOH A1704 O 89.8
REMARK 620 3 HOH A1703 O 89.9 179.5
REMARK 620 4 HOH A1702 O 90.1 89.7 89.9
REMARK 620 5 HOH A1705 O 179.7 89.9 90.4 89.8
REMARK 620 6 HOH A1701 O 90.0 90.5 89.8 179.7 90.1
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 A1661 O
REMARK 620 2 HOH A1665 O 89.9
REMARK 620 3 HOH A1664 O 89.9 179.8
REMARK 620 4 HOH A1663 O 90.4 89.8 90.1
REMARK 620 5 HOH A1662 O 89.4 90.2 89.9 179.8
REMARK 620 6 HOH A1660 O 179.6 89.9 90.2 89.3 90.9
REMARK 620 N 1 2 3 4 5
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 A1686 O
REMARK 620 2 HOH A1690 O 89.6
REMARK 620 3 HOH A1691 O 90.4 179.9
REMARK 620 4 HOH A1689 O 89.9 90.3 89.6
REMARK 620 5 HOH A1688 O 89.8 89.7 90.4 179.7
REMARK 620 6 HOH A1687 O 179.8 90.2 89.8 90.1 90.2
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 A1684 O
REMARK 620 2 HOH A1685 O 179.3
REMARK 620 3 HOH A1683 O 90.2 89.3
REMARK 620 4 HOH A1680 O 90.6 88.9 90.1
REMARK 620 5 HOH A1682 O 89.9 90.7 179.8 89.7
REMARK 620 6 HOH A1681 O 89.0 91.5 90.5 179.3 89.7
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 A1591 O
REMARK 620 2 HOH A1590 O 90.0
REMARK 620 3 HOH A1589 O 89.3 179.2
REMARK 620 4 HOH A1593 O 89.7 90.2 89.7
REMARK 620 5 HOH A1592 O 179.2 89.5 91.2 89.7
REMARK 620 6 HOH A1594 O 90.2 90.0 90.2 179.8 90.4
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 A 1575
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3OFA RELATED DB: PDB
REMARK 900 30S SUBUNIT OF 70S RIBOSOME 1
REMARK 900 RELATED ID: 3OFC RELATED DB: PDB
REMARK 900 50S SUBUNIT OF 70S RIBOSOME 1
REMARK 900 RELATED ID: 3OFD RELATED DB: PDB
REMARK 900 50S SUBUNIT OF 70S RIBOSOME 2
REMARK 900 RELATED ID: 3OAQ RELATED DB: PDB
REMARK 900 RELATED ID: 3OAR RELATED DB: PDB
REMARK 900 RELATED ID: 3OAS RELATED DB: PDB
REMARK 900 RELATED ID: 3OAT 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 3OFB A 5 1534 GB AP009048.1
DBREF2 3OFB A AP009048 3427004 3428533
DBREF 3OFB B 8 225 UNP P0A7V0 RS2_ECOLI 9 226
DBREF 3OFB C 1 206 UNP P0A7V3 RS3_ECOLI 2 207
DBREF 3OFB D 1 205 UNP P0A7V8 RS4_ECOLI 2 206
DBREF 3OFB E 9 158 UNP P0A7W1 RS5_ECOLI 10 159
DBREF 3OFB F 1 100 UNP P02358 RS6_ECOLI 1 100
DBREF 3OFB G 2 151 UNP P02359 RS7_ECOLI 3 152
DBREF 3OFB H 1 129 UNP P0A7W7 RS8_ECOLI 2 130
DBREF 3OFB I 3 129 UNP P0A7X3 RS9_ECOLI 4 130
DBREF 3OFB J 5 102 UNP P0A7R5 RS10_ECOLI 5 102
DBREF 3OFB K 12 128 UNP P0A7R9 RS11_ECOLI 13 129
DBREF 3OFB L 1 123 UNP P0A7S3 RS12_ECOLI 2 124
DBREF 3OFB M 1 113 UNP P0A7S9 RS13_ECOLI 2 114
DBREF 3OFB N 1 100 UNP P0AG59 RS14_ECOLI 2 101
DBREF 3OFB O 1 88 UNP P0ADZ4 RS15_ECOLI 2 89
DBREF 3OFB P 1 80 UNP P0A7T3 RS16_ECOLI 1 80
DBREF 3OFB Q 3 82 UNP P0AG63 RS17_ECOLI 4 83
DBREF 3OFB R 19 73 UNP P0A7T7 RS18_ECOLI 20 74
DBREF 3OFB S 2 80 UNP P0A7U3 RS19_ECOLI 3 81
DBREF 3OFB T 2 86 UNP P0A7U7 RS20_ECOLI 3 87
DBREF 3OFB 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 A1575 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 ASN B 102 ARG B 107 1 6
HELIX 5 5 ILE B 110 ASP B 115 1 6
HELIX 6 6 THR B 137 LEU B 147 1 11
HELIX 7 7 ILE B 150 GLY B 154 5 5
HELIX 8 8 GLU B 168 ASN B 177 1 10
HELIX 9 9 ASP B 191 VAL B 195 5 5
HELIX 10 10 ALA B 205 GLY B 214 1 10
HELIX 11 11 ALA B 215 VAL B 220 1 6
HELIX 12 12 ASN C 7 LEU C 11 5 5
HELIX 13 13 ALA C 29 SER C 34 1 6
HELIX 14 14 SER C 34 LEU C 46 1 13
HELIX 15 15 ARG C 71 VAL C 75 5 5
HELIX 16 16 GLY C 80 ALA C 91 1 12
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 LEU D 202 1 8
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 LYS E 155 1 8
HELIX 34 34 HIS F 11 GLU F 16 5 6
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 LEU G 98 VAL G 104 1 7
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 SER H 29 LEU H 31 5 3
HELIX 46 46 LYS H 32 GLU H 42 1 11
HELIX 47 47 THR H 111 ALA H 118 1 8
HELIX 48 48 SER I 33 PHE I 38 1 6
HELIX 49 49 ARG I 44 GLN I 49 1 6
HELIX 50 50 ILE I 71 ALA I 85 1 15
HELIX 51 51 ARG I 94 LYS I 99 1 6
HELIX 52 52 ASP J 14 ILE J 25 1 12
HELIX 53 53 SER K 54 THR K 58 5 5
HELIX 54 54 PRO K 59 ARG K 68 1 10
HELIX 55 55 VAL K 73 GLY K 77 5 5
HELIX 56 56 ARG K 92 GLY K 103 1 12
HELIX 57 57 THR L 2 VAL L 7 1 6
HELIX 58 58 HIS M 13 THR M 19 1 7
HELIX 59 59 THR M 27 ILE M 32 1 6
HELIX 60 60 LEU M 33 ALA M 35 5 3
HELIX 61 61 LEU M 55 LYS M 61 1 7
HELIX 62 62 VAL M 64 ILE M 72 1 9
HELIX 63 63 MET M 74 LEU M 79 1 6
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 SER N 79 MET N 88 1 10
HELIX 68 68 SER O 3 PHE O 14 1 12
HELIX 69 69 SER O 23 GLU O 44 1 22
HELIX 70 70 ASP O 48 ASP O 73 1 26
HELIX 71 71 ASP O 73 ARG O 83 1 11
HELIX 72 72 ASP P 53 GLY P 62 1 10
HELIX 73 73 SER P 68 LYS P 76 1 9
HELIX 74 74 ASP R 24 LYS R 29 1 6
HELIX 75 75 ASN R 30 ILE R 32 5 3
HELIX 76 76 PRO R 40 GLY R 45 1 6
HELIX 77 77 ARG R 47 LEU R 64 1 18
HELIX 78 78 LEU S 14 GLU S 19 1 6
HELIX 79 79 LYS S 69 ALA S 74 1 6
HELIX 80 80 LYS T 7 PHE T 30 1 24
HELIX 81 81 TYR T 35 GLU T 39 5 5
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 GLU U 23 ARG U 33 1 11
HELIX 85 85 GLU U 38 ALA U 47 1 10
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 VAL B 69
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 4 ARG C 168 GLY C 170 0
SHEET 2 B 4 GLY C 147 SER C 153 -1 N ILE C 148 O GLU C 169
SHEET 3 B 4 GLY C 196 PHE C 202 -1 O TRP C 200 N LYS C 149
SHEET 4 B 4 ILE C 181 ASN C 184 -1 N ASP C 182 O ILE C 201
SHEET 1 C 2 HIS C 189 THR C 190 0
SHEET 2 C 2 GLY C 193 VAL C 194 -1 N GLY C 193 O THR C 190
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 PHE D 181 -1 O GLY D 179 N VAL D 142
SHEET 5 D 5 LEU D 170 ASP D 173 -1 N GLU D 171 O THR D 180
SHEET 1 E 3 LYS E 13 ARG E 19 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 ARG E 44 VAL E 45 0
SHEET 2 F 2 ILE E 71 ASN E 72 -1 O ILE E 71 N VAL E 45
SHEET 1 G 3 VAL E 84 HIS E 88 0
SHEET 2 G 3 SER E 91 PRO E 97 -1 O VAL E 93 N GLY E 86
SHEET 3 G 3 VAL E 122 LYS E 125 -1 O LEU E 123 N GLN E 96
SHEET 1 H 4 ARG F 45 ILE F 51 0
SHEET 2 H 4 LEU F 54 LEU F 61 -1 O HIS F 55 N LEU F 47
SHEET 3 H 4 GLU F 5 VAL F 10 -1 N VAL F 10 O HIS F 58
SHEET 4 H 4 MET F 88 MET F 90 -1 O MET F 88 N VAL F 7
SHEET 1 I 3 VAL H 24 THR H 25 0
SHEET 2 I 3 GLU H 59 LEU H 62 -1 O LEU H 60 N VAL H 24
SHEET 3 I 3 ILE H 45 LYS H 49 -1 N GLU H 46 O THR H 61
SHEET 1 J 3 TYR H 85 LYS H 86 0
SHEET 2 J 3 GLY H 122 VAL H 128 -1 O GLY H 122 N LYS H 86
SHEET 3 J 3 ILE H 100 SER H 104 -1 N SER H 104 O GLU H 123
SHEET 1 K 4 TYR I 5 ARG I 10 0
SHEET 2 K 4 ALA I 15 ILE I 20 -1 O ALA I 16 N GLY I 9
SHEET 3 K 4 LEU I 62 ILE I 64 -1 O TYR I 63 N PHE I 19
SHEET 4 K 4 ILE I 27 ILE I 29 1 N VAL I 28 O ILE I 64
SHEET 1 L 2 ARG J 7 LYS J 11 0
SHEET 2 L 2 ASP J 97 SER J 101 -1 N GLN J 99 O ARG J 9
SHEET 1 M 3 PHE J 49 VAL J 51 0
SHEET 2 M 3 ASP J 63 GLU J 66 -1 O TYR J 65 N PHE J 49
SHEET 3 M 3 LYS N 96 LYS N 97 -1 O LYS N 96 N GLU J 66
SHEET 1 N 5 ALA K 40 THR K 45 0
SHEET 2 N 5 ILE K 30 ASP K 35 -1 N ILE K 33 O GLY K 42
SHEET 3 N 5 ASP K 17 HIS K 23 -1 N HIS K 23 O ILE K 30
SHEET 4 N 5 ASN K 80 LYS K 86 1 O GLU K 82 N ALA K 20
SHEET 5 N 5 ARG K 105 ASP K 111 1 O ASN K 108 N VAL K 83
SHEET 1 O 2 LYS L 29 GLY L 31 0
SHEET 2 O 2 ILE L 79 ILE L 81 -1 O ILE L 79 N GLY L 31
SHEET 1 P 2 VAL L 51 ARG L 55 0
SHEET 2 P 2 GLU L 61 TYR L 65 -1 O SER L 64 N CYS L 52
SHEET 1 Q 4 PHE P 32 ARG P 35 0
SHEET 2 Q 4 VAL P 19 ASP P 23 -1 N VAL P 21 O ILE P 33
SHEET 3 Q 4 VAL P 2 LEU P 6 -1 N ARG P 5 O VAL P 20
SHEET 4 Q 4 THR P 66 ILE P 67 1 O THR P 66 N ILE P 4
SHEET 1 R 2 HIS P 9 ALA P 11 0
SHEET 2 R 2 ARG P 14 PHE P 16 -1 O ARG P 14 N ALA P 11
SHEET 1 S 2 PHE P 38 PHE P 39 0
SHEET 2 S 2 THR P 50 ARG P 51 -1 O ARG P 51 N PHE P 38
SHEET 1 T 6 LEU Q 7 VAL Q 11 0
SHEET 2 T 6 SER Q 19 ALA Q 23 -1 O ALA Q 23 N ARG Q 10
SHEET 3 T 6 LYS Q 42 HIS Q 46 -1 O VAL Q 45 N ILE Q 20
SHEET 4 T 6 LYS Q 70 VAL Q 77 1 O LEU Q 74 N HIS Q 46
SHEET 5 T 6 VAL Q 57 SER Q 67 -1 N LEU Q 66 O LYS Q 70
SHEET 6 T 6 LEU Q 7 VAL Q 11 -1 N GLY Q 9 O VAL Q 58
SHEET 1 U 2 ARG Q 26 LYS Q 29 0
SHEET 2 U 2 PHE Q 36 ARG Q 39 -1 O ARG Q 39 N ARG Q 26
SHEET 1 V 2 ILE S 48 HIS S 51 0
SHEET 2 V 2 HIS S 56 VAL S 59 -1 O VAL S 57 N VAL S 50
LINK MG MG A1559 O HOH A1700 1555 1555 2.06
LINK MG MG A1570 O HOH A1748 1555 1555 2.06
LINK MG MG A1566 O HOH A1731 1555 1555 2.06
LINK MG MG A1538 O HOH A1597 1555 1555 2.07
LINK MG MG A1564 O HOH E 187 1555 1555 2.07
LINK MG MG A1562 O HOH A1711 1555 1555 2.07
LINK MG MG A1559 O HOH A1698 1555 1555 2.07
LINK MG MG A1566 O HOH A1729 1555 1555 2.07
LINK MG MG A1538 O HOH A1596 1555 1555 2.07
LINK MG MG A1559 O HOH A1697 1555 1555 2.07
LINK MG MG A1572 O HOH A1758 1555 1555 2.07
LINK MG MG A1559 O HOH A1699 1555 1555 2.07
LINK MG MG A1545 O HOH A1631 1555 1555 2.07
LINK MG MG A1562 O HOH A1714 1555 1555 2.07
LINK MG MG A1562 O HOH A1712 1555 1555 2.07
LINK MG MG A1545 O HOH A1632 1555 1555 2.07
LINK MG MG A1564 O HOH A1721 1555 1555 2.07
LINK MG MG A1538 O HOH A1595 1555 1555 2.07
LINK MG MG A1562 O HOH A1713 1555 1555 2.07
LINK MG MG A1551 O HOH A1657 1555 1555 2.07
LINK MG MG A1572 O HOH A1756 1555 1555 2.07
LINK MG MG A1551 O HOH A1658 1555 1555 2.07
LINK MG MG A1570 O HOH A1749 1555 1555 2.07
LINK MG MG A1551 O HOH A1656 1555 1555 2.07
LINK MG MG A1572 O HOH A1757 1555 1555 2.07
LINK MG MG A1566 O HOH A1730 1555 1555 2.07
LINK MG MG A1564 O HOH A1720 1555 1555 2.07
LINK MG MG A1538 O HOH A1598 1555 1555 2.07
LINK MG MG A1551 O HOH A1659 1555 1555 2.07
LINK MG MG A1566 O HOH A1728 1555 1555 2.07
LINK MG MG A1564 O HOH A1722 1555 1555 2.07
LINK MG MG A1572 O HOH A1755 1555 1555 2.07
LINK MG MG A1536 O HOH A1586 1555 1555 2.07
LINK MG MG A1545 O HOH A1629 1555 1555 2.07
LINK MG MG A1545 O HOH A1630 1555 1555 2.07
LINK MG MG A1570 O HOH A1747 1555 1555 2.07
LINK MG MG A1542 O HOH A1612 1555 1555 2.07
LINK MG MG A1553 O HOH A1668 1555 1555 2.08
LINK MG MG A1567 O HOH A1734 1555 1555 2.08
LINK MG MG A1539 O HOH A1602 1555 1555 2.08
LINK MG MG A1575 O HOH A1768 1555 1555 2.08
LINK MG MG A1540 O HOH A1605 1555 1555 2.08
LINK MG MG A1539 O HOH A1601 1555 1555 2.08
LINK MG MG A1567 O HOH A1735 1555 1555 2.08
LINK MG MG A1558 O HOH A1695 1555 1555 2.08
LINK MG MG A1575 O HOH A1771 1555 1555 2.08
LINK MG MG A1548 O HOH A1646 1555 1555 2.08
LINK MG MG A1558 O HOH A1696 1555 1555 2.08
LINK MG MG A1567 O HOH A1733 1555 1555 2.08
LINK MG MG A1539 O HOH A1599 1555 1555 2.08
LINK MG MG A1536 O HOH A1584 1555 1555 2.08
LINK MG MG A1571 O HOH A1754 1555 1555 2.08
LINK MG MG A1536 O HOH A1588 1555 1555 2.08
LINK MG MG A1553 O HOH A1670 1555 1555 2.08
LINK MG MG A1565 O HOH A1723 1555 1555 2.08
LINK MG MG A1536 O HOH A1587 1555 1555 2.08
LINK MG MG A1573 O HOH A1763 1555 1555 2.08
LINK MG MG A1561 O HOH A1707 1555 1555 2.08
LINK MG MG A1561 O HOH A1710 1555 1555 2.08
LINK MG MG A1565 O HOH A1725 1555 1555 2.08
LINK MG MG A1546 O HOH A1636 1555 1555 2.08
LINK MG MG A1553 O HOH A1666 1555 1555 2.08
LINK MG MG A1565 O HOH A1727 1555 1555 2.08
LINK MG MG A1571 O HOH A1750 1555 1555 2.08
LINK MG MG A1571 O HOH A1752 1555 1555 2.08
LINK MG MG A1573 O HOH A1760 1555 1555 2.08
LINK MG MG A1563 O HOH A1718 1555 1555 2.08
LINK MG MG A1542 O HOH A1615 1555 1555 2.08
LINK MG MG A1542 O HOH A1614 1555 1555 2.08
LINK MG MG A1546 O HOH A1633 1555 1555 2.08
LINK MG MG A1567 O HOH A1736 1555 1555 2.08
LINK MG MG A1548 O HOH A1643 1555 1555 2.08
LINK MG MG A1548 O HOH A1644 1555 1555 2.08
LINK MG MG A1571 O HOH A1753 1555 1555 2.08
LINK MG MG A1539 O HOH A1603 1555 1555 2.08
LINK MG MG A1540 O HOH A1608 1555 1555 2.08
LINK MG MG A1561 O HOH I 169 1555 1555 2.08
LINK MG MG A1548 O HOH A1647 1555 1555 2.08
LINK MG MG A1568 O HOH A1738 1555 1555 2.08
LINK MG MG A1547 O HOH A1642 1555 1555 2.08
LINK MG MG A1561 O HOH A1708 1555 1555 2.08
LINK MG MG A1573 O HOH A1759 1555 1555 2.08
LINK MG MG A1540 O HOH A1604 1555 1555 2.08
LINK MG MG A1568 O HOH A1739 1555 1555 2.08
LINK MG MG A1558 O HOH A1693 1555 1555 2.08
LINK MG MG A1542 O HOH A1613 1555 1555 2.08
LINK MG MG A1563 O HOH A1716 1555 1555 2.08
LINK MG MG A1565 O HOH A1724 1555 1555 2.08
LINK MG MG A1565 O HOH A1726 1555 1555 2.08
LINK MG MG A1561 O HOH A1709 1555 1555 2.08
LINK MG MG A1553 O HOH A1669 1555 1555 2.08
LINK MG MG A1573 O HOH A1762 1555 1555 2.08
LINK MG MG A1540 O HOH A1607 1555 1555 2.08
LINK MG MG A1568 O HOH A1741 1555 1555 2.08
LINK MG MG A1563 O HOH A1717 1555 1555 2.08
LINK MG MG A1558 O HOH A1694 1555 1555 2.08
LINK MG MG A1575 O HOH A1769 1555 1555 2.08
LINK MG MG A1546 O HOH A1634 1555 1555 2.08
LINK MG MG A1553 O HOH A1667 1555 1555 2.08
LINK MG MG A1567 O HOH A1732 1555 1555 2.08
LINK MG MG A1575 O HOH A1767 1555 1555 2.08
LINK MG MG A1548 O HOH A1645 1555 1555 2.08
LINK MG MG A1568 O HOH A1740 1555 1555 2.08
LINK MG MG A1540 O HOH A1606 1555 1555 2.08
LINK MG MG A1568 O HOH A1737 1555 1555 2.08
LINK MG MG A1542 O HOH A1616 1555 1555 2.08
LINK MG MG A1563 O HOH A1719 1555 1555 2.08
LINK MG MG A1536 O HOH A1585 1555 1555 2.08
LINK MG MG A1539 O HOH A1600 1555 1555 2.08
LINK MG MG A1575 O HOH A1770 1555 1555 2.08
LINK MG MG A1547 O HOH A1638 1555 1555 2.08
LINK MG MG A1547 O HOH A1639 1555 1555 2.08
LINK MG MG A1571 O HOH A1751 1555 1555 2.08
LINK MG MG A1573 O HOH A1761 1555 1555 2.08
LINK MG MG A1558 O HOH A1692 1555 1555 2.08
LINK MG MG A1547 O HOH A1640 1555 1555 2.08
LINK MG MG A1547 O HOH A1641 1555 1555 2.08
LINK MG MG A1563 O HOH A1715 1555 1555 2.08
LINK MG MG A1546 O HOH A1637 1555 1555 2.09
LINK MG MG A1546 O HOH A1635 1555 1555 2.09
LINK MG MG A1569 O HOH A1746 1555 1555 2.17
LINK MG MG A1544 O HOH A1625 1555 1555 2.17
LINK MG MG A1541 O HOH A1610 1555 1555 2.17
LINK MG MG A1574 O HOH A1764 1555 1555 2.18
LINK MG MG A1544 O HOH A1627 1555 1555 2.18
LINK MG MG A 1 O HOH T 87 1555 1555 2.18
LINK MG MG A1555 O HOH A1678 1555 1555 2.18
LINK MG MG A1554 O HOH A1672 1555 1555 2.18
LINK MG MG A1569 O HOH A1742 1555 1555 2.18
LINK MG MG A1535 O HOH A1580 1555 1555 2.18
LINK MG MG A1550 O HOH A1652 1555 1555 2.18
LINK MG MG A 1 O HOH A 4 1555 1555 2.18
LINK MG MG A1535 O HOH A1583 1555 1555 2.18
LINK MG MG A1550 O HOH N 105 1555 1555 2.18
LINK MG MG A1555 O HOH A1677 1555 1555 2.18
LINK MG MG A1543 O HOH A1618 1555 1555 2.18
LINK MG MG A1544 O HOH A1624 1555 1555 2.18
LINK MG MG A1549 O HOH A1649 1555 1555 2.18
LINK MG MG A1560 O HOH A1706 1555 1555 2.18
LINK MG MG A1560 O HOH A1704 1555 1555 2.18
LINK MG MG A1552 O HOH A1661 1555 1555 2.18
LINK MG MG A1557 O HOH A1686 1555 1555 2.18
LINK MG MG A1550 O HOH A1654 1555 1555 2.18
LINK MG MG A1560 O HOH A1703 1555 1555 2.18
LINK MG MG A1535 O HOH A1578 1555 1555 2.18
LINK MG MG A 1 O HOH A1576 1555 1555 2.18
LINK MG MG A1574 O HOH A1766 1555 1555 2.18
LINK MG MG A 1 O HOH A 2 1555 1555 2.18
LINK MG MG A 1 O HOH A1577 1555 1555 2.18
LINK MG MG A1549 O HOH N 102 1555 1555 2.18
LINK MG MG A1556 O HOH A1684 1555 1555 2.18
LINK MG MG A1537 O HOH A1591 1555 1555 2.18
LINK MG MG A1552 O HOH A1665 1555 1555 2.18
LINK MG MG A1550 O HOH A1653 1555 1555 2.18
LINK MG MG A1549 O HOH A1650 1555 1555 2.18
LINK MG MG A1537 O HOH A1590 1555 1555 2.18
LINK MG MG A1535 O HOH A1579 1555 1555 2.18
LINK MG MG A1556 O HOH A1685 1555 1555 2.18
LINK MG MG A1554 O HOH A1673 1555 1555 2.18
LINK MG MG A1543 O HOH A1621 1555 1555 2.18
LINK MG MG A1560 O HOH A1702 1555 1555 2.18
LINK MG MG A1555 O HOH A1675 1555 1555 2.18
LINK MG MG A1543 O HOH A1617 1555 1555 2.18
LINK MG MG A1556 O HOH A1683 1555 1555 2.18
LINK MG MG A1569 O HOH U 218 1555 1555 2.18
LINK MG MG A1550 O HOH A1651 1555 1555 2.18
LINK MG MG A1535 O HOH A1582 1555 1555 2.18
LINK MG MG A1537 O HOH A1589 1555 1555 2.18
LINK MG MG A1555 O HOH A1679 1555 1555 2.18
LINK MG MG A1549 O HOH A1648 1555 1555 2.18
LINK MG MG A1549 O HOH N 101 1555 1555 2.18
LINK MG MG A1556 O HOH A1680 1555 1555 2.18
LINK MG MG A1557 O HOH A1690 1555 1555 2.18
LINK MG MG A1552 O HOH A1664 1555 1555 2.18
LINK MG MG A1537 O HOH A1593 1555 1555 2.18
LINK MG MG A1535 O HOH A1581 1555 1555 2.18
LINK MG MG A1557 O HOH A1691 1555 1555 2.18
LINK MG MG A1549 O HOH N 103 1555 1555 2.18
LINK MG MG A1544 O HOH A1623 1555 1555 2.18
LINK MG MG A1554 O HOH A1671 1555 1555 2.18
LINK MG MG A1550 O HOH A1655 1555 1555 2.18
LINK MG MG A1543 O HOH A1622 1555 1555 2.18
LINK MG MG A1555 O HOH A1674 1555 1555 2.18
LINK MG MG A1552 O HOH A1663 1555 1555 2.18
LINK MG MG A1557 O HOH A1689 1555 1555 2.18
LINK MG MG A1560 O HOH A1705 1555 1555 2.18
LINK MG MG A1560 O HOH A1701 1555 1555 2.18
LINK MG MG A1574 O HOH A1765 1555 1555 2.18
LINK MG MG A1552 O HOH A1662 1555 1555 2.18
LINK MG MG A1569 O HOH A1743 1555 1555 2.18
LINK MG MG A1557 O HOH A1688 1555 1555 2.18
LINK MG MG A1555 O HOH A1676 1555 1555 2.18
LINK MG MG A1544 O HOH A1628 1555 1555 2.18
LINK MG MG A1552 O HOH A1660 1555 1555 2.18
LINK MG MG A1556 O HOH A1682 1555 1555 2.18
LINK MG MG A1569 O HOH A1745 1555 1555 2.18
LINK MG MG A1537 O HOH A1592 1555 1555 2.18
LINK MG MG A1544 O HOH A1626 1555 1555 2.18
LINK MG MG A1557 O HOH A1687 1555 1555 2.18
LINK MG MG A 1 O HOH A 3 1555 1555 2.18
LINK MG MG A1569 O HOH A1744 1555 1555 2.18
LINK MG MG A1541 O HOH A1609 1555 1555 2.18
LINK MG MG A1543 O HOH A1620 1555 1555 2.18
LINK MG MG A1543 O HOH A1619 1555 1555 2.19
LINK MG MG A1537 O HOH A1594 1555 1555 2.19
LINK MG MG A1556 O HOH A1681 1555 1555 2.19
LINK MG MG A1541 O HOH A1611 1555 1555 2.19
LINK OP1 C A 578 MG MG A1542 1555 1555 2.20
LINK OP2 G A 100 MG MG A1571 1555 1555 2.27
LINK OP1 G A 558 MG MG A1564 1555 1555 2.28
LINK OP1 A A 547 MG MG A1539 1555 1555 2.30
LINK OP1 G A1505 MG MG A1554 1555 1555 2.32
LINK OP2 A A1500 MG MG A1570 1555 1555 2.34
LINK OP2 A A 510 MG MG A1538 1555 1555 2.36
LINK O4 U A 516 MG MG A1566 1555 1555 2.36
LINK OP2 A A1110 MG MG A1568 1555 1555 2.37
LINK OP1 A A1500 MG MG A1554 1555 1555 2.37
LINK OP2 A A 814 MG MG A1545 1555 1555 2.42
LINK O6 G A1417 MG MG A1553 1555 1555 2.42
LINK OP2 A A1433 MG MG A1563 1555 1555 2.42
LINK OP1 A A 533 MG MG A1566 1555 1555 2.43
LINK OP2 A A 572 MG MG A1541 1555 1555 2.45
LINK OP1 G A1198 MG MG A1562 1555 1555 2.50
LINK OP2 G A 117 MG MG A1574 1555 1555 2.50
LINK OP2 G A 289 MG MG A1574 1555 1555 2.50
LINK OP1 G A 21 MG MG A1558 1555 1555 2.54
LINK OP2 A A 195 MG MG A1572 1555 1555 2.54
LINK OP1 A A1508 MG MG A1554 1555 1555 2.56
LINK OP2 A A 116 MG MG A1574 1555 1555 2.56
LINK OP2 U A 891 MG MG A1546 1555 1555 2.57
LINK OP2 A A 608 MG MG A1567 1555 1555 2.59
LINK OP2 A A 560 MG MG A1540 1555 1555 2.62
LINK OP2 A A 573 MG MG A1541 1555 1555 2.62
LINK OP2 G A1505 MG MG A1570 1555 1555 2.63
LINK OP2 A A 574 MG MG A1541 1555 1555 2.64
LINK OP2 A A 509 MG MG A1538 1555 1555 2.67
LINK OP1 C A 934 MG MG A1547 1555 1555 2.68
LINK OP2 A A 937 MG MG A1548 1555 1555 2.71
LINK O4 U A 180 MG MG A1572 1555 1555 2.76
LINK O6 G A 299 MG MG A1564 1555 1555 2.81
LINK O2' G A1504 MG MG A1570 1555 1555 2.83
LINK OP1 A A 195 MG MG A1572 1555 1555 2.85
LINK O6 G A 362 MG MG A1536 1555 1555 2.95
SITE 1 AC1 6 HOH A 2 HOH A 3 HOH A 4 HOH A1576
SITE 2 AC1 6 HOH A1577 HOH T 87
SITE 1 AC2 7 G A 319 HOH A1578 HOH A1579 HOH A1580
SITE 2 AC2 7 HOH A1581 HOH A1582 HOH A1583
SITE 1 AC3 6 G A 362 HOH A1584 HOH A1585 HOH A1586
SITE 2 AC3 6 HOH A1587 HOH A1588
SITE 1 AC4 6 HOH A1589 HOH A1590 HOH A1591 HOH A1592
SITE 2 AC4 6 HOH A1593 HOH A1594
SITE 1 AC5 7 U A 508 A A 509 A A 510 HOH A1595
SITE 2 AC5 7 HOH A1596 HOH A1597 HOH A1598
SITE 1 AC6 6 A A 547 HOH A1599 HOH A1600 HOH A1601
SITE 2 AC6 6 HOH A1602 HOH A1603
SITE 1 AC7 7 A A 560 G A 566 HOH A1604 HOH A1605
SITE 2 AC7 7 HOH A1606 HOH A1607 HOH A1608
SITE 1 AC8 6 A A 572 A A 573 A A 574 HOH A1609
SITE 2 AC8 6 HOH A1610 HOH A1611
SITE 1 AC9 7 G A 577 C A 578 HOH A1612 HOH A1613
SITE 2 AC9 7 HOH A1614 HOH A1615 HOH A1616
SITE 1 BC1 6 HOH A1617 HOH A1618 HOH A1619 HOH A1620
SITE 2 BC1 6 HOH A1621 HOH A1622
SITE 1 BC2 6 HOH A1623 HOH A1624 HOH A1625 HOH A1626
SITE 2 BC2 6 HOH A1627 HOH A1628
SITE 1 BC3 6 G A 577 A A 814 HOH A1629 HOH A1630
SITE 2 BC3 6 HOH A1631 HOH A1632
SITE 1 BC4 6 U A 891 HOH A1633 HOH A1634 HOH A1635
SITE 2 BC4 6 HOH A1636 HOH A1637
SITE 1 BC5 7 G A 933 C A 934 HOH A1638 HOH A1639
SITE 2 BC5 7 HOH A1640 HOH A1641 HOH A1642
SITE 1 BC6 6 A A 937 HOH A1643 HOH A1644 HOH A1645
SITE 2 BC6 6 HOH A1646 HOH A1647
SITE 1 BC7 6 HOH A1648 HOH A1649 HOH A1650 HOH N 101
SITE 2 BC7 6 HOH N 102 HOH N 103
SITE 1 BC8 6 HOH A1651 HOH A1652 HOH A1653 HOH A1654
SITE 2 BC8 6 HOH A1655 HOH N 105
SITE 1 BC9 7 G A1053 C A1054 A A1197 HOH A1656
SITE 2 BC9 7 HOH A1657 HOH A1658 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 8 A A1500 G A1504 G A1505 A A1507
SITE 2 CC3 8 A A1508 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 HOH A1686 HOH A1687 HOH A1688 HOH A1689
SITE 2 CC6 6 HOH A1690 HOH A1691
SITE 1 CC7 6 G A 21 HOH A1692 HOH A1693 HOH A1694
SITE 2 CC7 6 HOH A1695 HOH A1696
SITE 1 CC8 6 G A 858 G A 869 HOH A1697 HOH A1698
SITE 2 CC8 6 HOH A1699 HOH A1700
SITE 1 CC9 6 HOH A1701 HOH A1702 HOH A1703 HOH A1704
SITE 2 CC9 6 HOH A1705 HOH A1706
SITE 1 DC1 5 HOH A1707 HOH A1708 HOH A1709 HOH A1710
SITE 2 DC1 5 HOH I 169
SITE 1 DC2 5 G A1198 HOH A1711 HOH A1712 HOH A1713
SITE 2 DC2 5 HOH A1714
SITE 1 DC3 6 A A1433 HOH A1715 HOH A1716 HOH A1717
SITE 2 DC3 6 HOH A1718 HOH A1719
SITE 1 DC4 7 G A 299 G A 557 G A 558 HOH A1720
SITE 2 DC4 7 HOH A1721 HOH A1722 HOH E 187
SITE 1 DC5 6 G A 324 HOH A1723 HOH A1724 HOH A1725
SITE 2 DC5 6 HOH A1726 HOH A1727
SITE 1 DC6 6 U A 516 A A 533 HOH A1728 HOH A1729
SITE 2 DC6 6 HOH A1730 HOH A1731
SITE 1 DC7 6 A A 608 HOH A1732 HOH A1733 HOH A1734
SITE 2 DC7 6 HOH A1735 HOH A1736
SITE 1 DC8 7 A A1110 U A1189 HOH A1737 HOH A1738
SITE 2 DC8 7 HOH A1739 HOH A1740 HOH A1741
SITE 1 DC9 6 HOH A1742 HOH A1743 HOH A1744 HOH A1745
SITE 2 DC9 6 HOH A1746 HOH U 218
SITE 1 EC1 6 A A1500 G A1504 G A1505 HOH A1747
SITE 2 EC1 6 HOH A1748 HOH A1749
SITE 1 EC2 6 G A 100 HOH A1750 HOH A1751 HOH A1752
SITE 2 EC2 6 HOH A1753 HOH A1754
SITE 1 EC3 7 A A 179 U A 180 A A 195 HOH A1755
SITE 2 EC3 7 HOH A1756 HOH A1757 HOH A1758
SITE 1 EC4 6 G A 537 HOH A1759 HOH A1760 HOH A1761
SITE 2 EC4 6 HOH A1762 HOH A1763
SITE 1 EC5 7 G A 115 A A 116 G A 117 G A 289
SITE 2 EC5 7 HOH A1764 HOH A1765 HOH A1766
SITE 1 EC6 7 C A 330 C A 352 HOH A1767 HOH A1768
SITE 2 EC6 7 HOH A1769 HOH A1770 HOH A1771
CRYST1 211.456 434.084 621.233 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 0.004729 0.000000 0.000000 0.00000
SCALE2 0.000000 0.002304 0.000000 0.00000
SCALE3 0.000000 0.000000 0.001610 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
