HEADER HYDROLASE/RNA 14-DEC-12 4IFD
TITLE CRYSTAL STRUCTURE OF AN 11-SUBUNIT EUKARYOTIC EXOSOME COMPLEX BOUND TO
TITLE 2 RNA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EXOSOME COMPLEX COMPONENT RRP45;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: RIBOSOMAL RNA-PROCESSING PROTEIN 45;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: EXOSOME COMPLEX COMPONENT SKI6;
COMPND 8 CHAIN: B;
COMPND 9 SYNONYM: EXTRACELLULAR MUTANT PROTEIN 20, RIBOSOMAL RNA-PROCESSING
COMPND 10 PROTEIN 41, SUPERKILLER PROTEIN 6;
COMPND 11 ENGINEERED: YES;
COMPND 12 MOL_ID: 3;
COMPND 13 MOLECULE: EXOSOME COMPLEX COMPONENT RRP43;
COMPND 14 CHAIN: C;
COMPND 15 SYNONYM: RIBOSOMAL RNA-PROCESSING PROTEIN 43;
COMPND 16 ENGINEERED: YES;
COMPND 17 MOL_ID: 4;
COMPND 18 MOLECULE: EXOSOME COMPLEX COMPONENT RRP46;
COMPND 19 CHAIN: D;
COMPND 20 SYNONYM: RIBOSOMAL RNA-PROCESSING PROTEIN 46;
COMPND 21 ENGINEERED: YES;
COMPND 22 MOL_ID: 5;
COMPND 23 MOLECULE: EXOSOME COMPLEX COMPONENT RRP42;
COMPND 24 CHAIN: E;
COMPND 25 SYNONYM: RIBOSOMAL RNA-PROCESSING PROTEIN 42;
COMPND 26 ENGINEERED: YES;
COMPND 27 MUTATION: YES;
COMPND 28 MOL_ID: 6;
COMPND 29 MOLECULE: EXOSOME COMPLEX COMPONENT MTR3;
COMPND 30 CHAIN: F;
COMPND 31 SYNONYM: MRNA TRANSPORT REGULATOR 3;
COMPND 32 ENGINEERED: YES;
COMPND 33 MUTATION: YES;
COMPND 34 MOL_ID: 7;
COMPND 35 MOLECULE: EXOSOME COMPLEX COMPONENT RRP40;
COMPND 36 CHAIN: G;
COMPND 37 SYNONYM: RIBOSOMAL RNA-PROCESSING PROTEIN 40;
COMPND 38 ENGINEERED: YES;
COMPND 39 MOL_ID: 8;
COMPND 40 MOLECULE: EXOSOME COMPLEX COMPONENT RRP4;
COMPND 41 CHAIN: H;
COMPND 42 SYNONYM: RIBOSOMAL RNA-PROCESSING PROTEIN 4;
COMPND 43 ENGINEERED: YES;
COMPND 44 MOL_ID: 9;
COMPND 45 MOLECULE: EXOSOME COMPLEX COMPONENT CSL4;
COMPND 46 CHAIN: I;
COMPND 47 SYNONYM: CEP1 SYNTHETIC LETHAL PROTEIN 4;
COMPND 48 ENGINEERED: YES;
COMPND 49 MOL_ID: 10;
COMPND 50 MOLECULE: EXOSOME COMPLEX EXONUCLEASE DIS3;
COMPND 51 CHAIN: J;
COMPND 52 SYNONYM: CHROMOSOME DISJUNCTION PROTEIN 3, RIBOSOMAL RNA-PROCESSING
COMPND 53 PROTEIN 44;
COMPND 54 EC: 3.1.13.-, 3.1.26.-;
COMPND 55 ENGINEERED: YES;
COMPND 56 MUTATION: YES;
COMPND 57 MOL_ID: 11;
COMPND 58 MOLECULE: EXOSOME COMPLEX EXONUCLEASE RRP6;
COMPND 59 CHAIN: K;
COMPND 60 FRAGMENT: UNP RESIDUES 518-693;
COMPND 61 SYNONYM: RIBOSOMAL RNA-PROCESSING PROTEIN 6;
COMPND 62 EC: 3.1.13.-;
COMPND 63 ENGINEERED: YES;
COMPND 64 MOL_ID: 12;
COMPND 65 MOLECULE: RNA (45-MER);
COMPND 66 CHAIN: R;
COMPND 67 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 559292;
SOURCE 5 STRAIN: ATCC 204508 / S288C;
SOURCE 6 GENE: D9954.1, RRP45, YDR280W;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PETMCN;
SOURCE 12 MOL_ID: 2;
SOURCE 13 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 14 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 15 ORGANISM_TAXID: 559292;
SOURCE 16 STRAIN: ATCC 204508 / S288C;
SOURCE 17 GENE: ECM20, G7587, RRP41, SKI6, YGR195W;
SOURCE 18 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 19 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 20 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 21 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 22 EXPRESSION_SYSTEM_PLASMID: PETMCN;
SOURCE 23 MOL_ID: 3;
SOURCE 24 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 25 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 26 ORGANISM_TAXID: 559292;
SOURCE 27 STRAIN: ATCC 204508 / S288C;
SOURCE 28 GENE: RRP43, YCR035C, YCR35C, YCR522;
SOURCE 29 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 30 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 31 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 32 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 33 EXPRESSION_SYSTEM_PLASMID: PETMCN;
SOURCE 34 MOL_ID: 4;
SOURCE 35 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 36 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 37 ORGANISM_TAXID: 559292;
SOURCE 38 STRAIN: ATCC 204508 / S288C;
SOURCE 39 GENE: RRP46, YGR095C;
SOURCE 40 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 41 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 42 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 43 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 44 EXPRESSION_SYSTEM_PLASMID: PETMCN;
SOURCE 45 MOL_ID: 5;
SOURCE 46 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 47 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 48 ORGANISM_TAXID: 559292;
SOURCE 49 STRAIN: ATCC 204508 / S288C;
SOURCE 50 GENE: RRP42, YDL111C;
SOURCE 51 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 52 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 53 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 54 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 55 EXPRESSION_SYSTEM_PLASMID: PETMCN;
SOURCE 56 MOL_ID: 6;
SOURCE 57 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 58 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 59 ORGANISM_TAXID: 559292;
SOURCE 60 STRAIN: ATCC 204508 / S288C;
SOURCE 61 GENE: G6676, MTR3, YGR158C;
SOURCE 62 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 63 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 64 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 65 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 66 EXPRESSION_SYSTEM_PLASMID: PETMCN;
SOURCE 67 MOL_ID: 7;
SOURCE 68 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 69 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 70 ORGANISM_TAXID: 559292;
SOURCE 71 STRAIN: ATCC 204508 / S288C;
SOURCE 72 GENE: RRP40, YOL142W;
SOURCE 73 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 74 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 75 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 76 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 77 EXPRESSION_SYSTEM_PLASMID: PETMCN;
SOURCE 78 MOL_ID: 8;
SOURCE 79 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 80 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 81 ORGANISM_TAXID: 559292;
SOURCE 82 STRAIN: ATCC 204508 / S288C;
SOURCE 83 GENE: RRP4, YHR069C;
SOURCE 84 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 85 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 86 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 87 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 88 EXPRESSION_SYSTEM_PLASMID: PECK;
SOURCE 89 MOL_ID: 9;
SOURCE 90 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 91 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 92 ORGANISM_TAXID: 559292;
SOURCE 93 STRAIN: ATCC 204508 / S288C;
SOURCE 94 GENE: CSL4, N1154, SKI4, YNL232W;
SOURCE 95 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 96 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 97 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 98 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 99 EXPRESSION_SYSTEM_PLASMID: PETM13;
SOURCE 100 MOL_ID: 10;
SOURCE 101 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 102 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 103 ORGANISM_TAXID: 559292;
SOURCE 104 STRAIN: ATCC 204508 / S288C;
SOURCE 105 GENE: DIS3, O2197, RRP44, YOL021C;
SOURCE 106 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 107 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 108 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 109 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 110 EXPRESSION_SYSTEM_PLASMID: PETM11;
SOURCE 111 MOL_ID: 11;
SOURCE 112 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 113 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 114 ORGANISM_TAXID: 559292;
SOURCE 115 STRAIN: ATCC 204508 / S288C;
SOURCE 116 GENE: RRP6, UNC733, YOR001W;
SOURCE 117 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 118 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 119 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 120 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 121 EXPRESSION_SYSTEM_PLASMID: PECK;
SOURCE 122 MOL_ID: 12;
SOURCE 123 SYNTHETIC: YES;
SOURCE 124 OTHER_DETAILS: SEQUENCE DESIGNED BASED ON BIOCHEMICAL DATA.
KEYWDS EXOSOME, RNA, RRP44, DIS3, PIN, RRP6, EXONUCLEASE, ENDONUCLEASE,
KEYWDS 2 HYDROLASE, NUCLEASE, RIBONUCLEASE, RNA PROCESSING, HYDROLASE-RNA
KEYWDS 3 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR D.L.MAKINO,E.CONTI
REVDAT 5 08-NOV-23 4IFD 1 REMARK SEQADV LINK
REVDAT 4 15-NOV-17 4IFD 1 REMARK
REVDAT 3 13-NOV-13 4IFD 1 JRNL
REVDAT 2 13-MAR-13 4IFD 1 JRNL
REVDAT 1 06-FEB-13 4IFD 0
JRNL AUTH D.L.MAKINO,M.BAUMGARTNER,E.CONTI
JRNL TITL CRYSTAL STRUCTURE OF AN RNA-BOUND 11-SUBUNIT EUKARYOTIC
JRNL TITL 2 EXOSOME COMPLEX.
JRNL REF NATURE V. 495 70 2013
JRNL REFN ISSN 0028-0836
JRNL PMID 23376952
JRNL DOI 10.1038/NATURE11870
REMARK 2
REMARK 2 RESOLUTION. 2.81 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.1_1168)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.81
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.64
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.990
REMARK 3 COMPLETENESS FOR RANGE (%) : 87.9
REMARK 3 NUMBER OF REFLECTIONS : 99101
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.185
REMARK 3 R VALUE (WORKING SET) : 0.183
REMARK 3 FREE R VALUE : 0.224
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4956
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 49.6458 - 8.6994 1.00 3701 196 0.1590 0.1750
REMARK 3 2 8.6994 - 6.9109 1.00 3623 190 0.1584 0.1779
REMARK 3 3 6.9109 - 6.0391 1.00 3610 190 0.1814 0.2234
REMARK 3 4 6.0391 - 5.4877 1.00 3600 190 0.1712 0.2358
REMARK 3 5 5.4877 - 5.0948 1.00 3561 187 0.1577 0.2146
REMARK 3 6 5.0948 - 4.7947 1.00 3612 191 0.1433 0.1760
REMARK 3 7 4.7947 - 4.5547 1.00 3576 188 0.1365 0.1722
REMARK 3 8 4.5547 - 4.3566 1.00 3568 188 0.1432 0.1786
REMARK 3 9 4.3566 - 4.1889 1.00 3570 187 0.1505 0.1891
REMARK 3 10 4.1889 - 4.0445 1.00 3589 189 0.1593 0.2161
REMARK 3 11 4.0445 - 3.9180 1.00 3557 187 0.1698 0.1905
REMARK 3 12 3.9180 - 3.8061 1.00 3585 189 0.1700 0.2031
REMARK 3 13 3.8061 - 3.7059 1.00 3539 186 0.1760 0.2475
REMARK 3 14 3.7059 - 3.6155 1.00 3567 188 0.1853 0.2292
REMARK 3 15 3.6155 - 3.5334 1.00 3574 188 0.1948 0.2249
REMARK 3 16 3.5334 - 3.4582 1.00 3544 187 0.1959 0.2645
REMARK 3 17 3.4582 - 3.3890 1.00 3589 189 0.2142 0.2614
REMARK 3 18 3.3890 - 3.3251 1.00 3541 186 0.2190 0.2526
REMARK 3 19 3.3251 - 3.2657 1.00 3532 186 0.2330 0.3090
REMARK 3 20 3.2657 - 3.2104 0.99 3510 185 0.2401 0.2930
REMARK 3 21 3.2104 - 3.1586 0.87 3109 163 0.2524 0.3102
REMARK 3 22 3.1586 - 3.1100 0.71 2516 133 0.2539 0.2924
REMARK 3 23 3.1100 - 3.0643 0.64 2256 119 0.2602 0.3132
REMARK 3 24 3.0643 - 3.0211 0.64 2287 120 0.2636 0.3362
REMARK 3 25 3.0211 - 2.9803 0.63 2217 117 0.2787 0.3229
REMARK 3 26 2.9803 - 2.9416 0.64 2316 122 0.2869 0.3634
REMARK 3 27 2.9416 - 2.9048 0.64 2233 117 0.2924 0.3456
REMARK 3 28 2.9048 - 2.8698 0.64 2312 122 0.2938 0.3046
REMARK 3 29 2.8698 - 2.8365 0.57 2015 106 0.2932 0.3581
REMARK 3 30 2.8365 - 2.8046 0.38 1336 70 0.3046 0.3492
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.20
REMARK 3 SHRINKAGE RADIUS : 1.00
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.360
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.200
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 59.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.003 27093
REMARK 3 ANGLE : 0.542 36836
REMARK 3 CHIRALITY : 0.035 4351
REMARK 3 PLANARITY : 0.004 4662
REMARK 3 DIHEDRAL : 9.903 10175
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 12
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN G
REMARK 3 ORIGIN FOR THE GROUP (A): 141.5112 -4.2726 205.1851
REMARK 3 T TENSOR
REMARK 3 T11: 0.5673 T22: 0.2003
REMARK 3 T33: 0.3884 T12: 0.0900
REMARK 3 T13: -0.1496 T23: 0.0597
REMARK 3 L TENSOR
REMARK 3 L11: 1.9294 L22: 1.5279
REMARK 3 L33: 1.7801 L12: 0.2913
REMARK 3 L13: 0.2529 L23: -0.1525
REMARK 3 S TENSOR
REMARK 3 S11: 0.0722 S12: -0.1833 S13: -0.2761
REMARK 3 S21: 0.3481 S22: -0.0223 S23: -0.2480
REMARK 3 S31: 0.2287 S32: 0.1153 S33: 0.0477
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN H AND (RESID 50:357)
REMARK 3 ORIGIN FOR THE GROUP (A): 139.9041 42.3845 202.7967
REMARK 3 T TENSOR
REMARK 3 T11: 0.6260 T22: 0.2870
REMARK 3 T33: 0.3947 T12: -0.0229
REMARK 3 T13: -0.1034 T23: -0.0165
REMARK 3 L TENSOR
REMARK 3 L11: 0.4410 L22: 0.3590
REMARK 3 L33: 0.4692 L12: -0.2149
REMARK 3 L13: 0.0232 L23: 0.3337
REMARK 3 S TENSOR
REMARK 3 S11: -0.0776 S12: -0.1737 S13: 0.1024
REMARK 3 S21: 0.3513 S22: 0.0822 S23: -0.0766
REMARK 3 S31: -0.0651 S32: 0.1633 S33: -0.0000
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN J AND (RESID 249:399)
REMARK 3 ORIGIN FOR THE GROUP (A): 122.0603 28.4635 121.9292
REMARK 3 T TENSOR
REMARK 3 T11: 0.7377 T22: 0.8735
REMARK 3 T33: 0.5761 T12: -0.0796
REMARK 3 T13: -0.0266 T23: 0.0124
REMARK 3 L TENSOR
REMARK 3 L11: 0.4703 L22: 0.3109
REMARK 3 L33: 0.2861 L12: -0.2415
REMARK 3 L13: 0.0899 L23: 0.0945
REMARK 3 S TENSOR
REMARK 3 S11: 0.1583 S12: 0.0681 S13: -0.1864
REMARK 3 S21: -0.3683 S22: -0.1263 S23: 0.2446
REMARK 3 S31: 0.3973 S32: -0.1936 S33: -0.0000
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN J AND (RESID 491:910 )) OR (CHAIN R AND
REMARK 3 (RESSEQ -6:-1))
REMARK 3 ORIGIN FOR THE GROUP (A): 161.7901 9.3733 129.7451
REMARK 3 T TENSOR
REMARK 3 T11: 0.4432 T22: 1.2502
REMARK 3 T33: 0.5646 T12: 0.0766
REMARK 3 T13: 0.1465 T23: -0.1380
REMARK 3 L TENSOR
REMARK 3 L11: 0.9169 L22: 1.4812
REMARK 3 L33: 1.0524 L12: 0.0788
REMARK 3 L13: 0.2347 L23: 0.1477
REMARK 3 S TENSOR
REMARK 3 S11: -0.1323 S12: 0.4658 S13: -0.1995
REMARK 3 S21: -0.2193 S22: 0.2190 S23: -0.1596
REMARK 3 S31: 0.2157 S32: 0.2661 S33: 0.0205
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: (CHAIN I AND (RESSEQ 1:113)) OR (CHAIN K AND (RESID
REMARK 3 532:557 ))
REMARK 3 ORIGIN FOR THE GROUP (A): 77.2820 35.5149 208.1468
REMARK 3 T TENSOR
REMARK 3 T11: 0.8065 T22: 1.0190
REMARK 3 T33: 0.8602 T12: 0.2503
REMARK 3 T13: 0.1967 T23: -0.1271
REMARK 3 L TENSOR
REMARK 3 L11: 0.2801 L22: 0.1185
REMARK 3 L33: 0.1535 L12: 0.1174
REMARK 3 L13: -0.1817 L23: -0.0015
REMARK 3 S TENSOR
REMARK 3 S11: -0.3637 S12: -0.2651 S13: 0.2563
REMARK 3 S21: 0.0829 S22: 0.1678 S23: 0.3363
REMARK 3 S31: -0.2102 S32: -0.3553 S33: 0.0001
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN R AND (RESSEQ -44:-30 )
REMARK 3 ORIGIN FOR THE GROUP (A): 132.0747 29.1686 222.8311
REMARK 3 T TENSOR
REMARK 3 T11: 1.9546 T22: 1.6295
REMARK 3 T33: 1.4118 T12: 0.0608
REMARK 3 T13: 0.0382 T23: -0.0045
REMARK 3 L TENSOR
REMARK 3 L11: 0.0250 L22: -0.0005
REMARK 3 L33: 0.0175 L12: -0.0119
REMARK 3 L13: 0.0080 L23: 0.0004
REMARK 3 S TENSOR
REMARK 3 S11: 0.0574 S12: -0.4636 S13: -0.0275
REMARK 3 S21: 0.4583 S22: -0.0200 S23: -0.0701
REMARK 3 S31: -0.2034 S32: 0.2008 S33: -0.0000
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN A OR CHAIN B OR CHAIN C OR CHAIN D OR CHAIN E
REMARK 3 OR CHAIN F OR (CHAIN H AND RESSEQ 2:17) OR (CHAIN K
REMARK 3 AND RESSEQ 565:619)
REMARK 3 ORIGIN FOR THE GROUP (A): 116.8655 16.7855 173.9893
REMARK 3 T TENSOR
REMARK 3 T11: 0.3539 T22: 0.3151
REMARK 3 T33: 0.3309 T12: -0.0121
REMARK 3 T13: 0.0070 T23: 0.0051
REMARK 3 L TENSOR
REMARK 3 L11: 0.5842 L22: 0.5846
REMARK 3 L33: 0.6283 L12: 0.1924
REMARK 3 L13: 0.1899 L23: -0.0163
REMARK 3 S TENSOR
REMARK 3 S11: -0.0134 S12: 0.1068 S13: 0.0110
REMARK 3 S21: 0.0316 S22: 0.0498 S23: 0.0597
REMARK 3 S31: 0.0418 S32: -0.0889 S33: 0.0000
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN J AND (RESID 400:490)
REMARK 3 ORIGIN FOR THE GROUP (A): 146.8575 40.4667 111.2989
REMARK 3 T TENSOR
REMARK 3 T11: 0.5106 T22: 1.2664
REMARK 3 T33: 0.4452 T12: -0.1333
REMARK 3 T13: 0.0948 T23: 0.1216
REMARK 3 L TENSOR
REMARK 3 L11: 0.2476 L22: 0.5916
REMARK 3 L33: 0.1656 L12: 0.2809
REMARK 3 L13: 0.1481 L23: 0.2998
REMARK 3 S TENSOR
REMARK 3 S11: -0.0598 S12: 0.3325 S13: 0.2730
REMARK 3 S21: -0.4012 S22: -0.0001 S23: -0.0677
REMARK 3 S31: -0.1735 S32: 0.5582 S33: -0.0567
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN J AND RESID 911:1001
REMARK 3 ORIGIN FOR THE GROUP (A): 145.7982 11.0270 95.2145
REMARK 3 T TENSOR
REMARK 3 T11: 1.1275 T22: 1.8881
REMARK 3 T33: 0.7299 T12: -0.0864
REMARK 3 T13: 0.0894 T23: -0.3012
REMARK 3 L TENSOR
REMARK 3 L11: 0.0612 L22: 0.0338
REMARK 3 L33: 0.0404 L12: -0.0153
REMARK 3 L13: 0.0147 L23: -0.0040
REMARK 3 S TENSOR
REMARK 3 S11: -0.0090 S12: 0.1468 S13: 0.1318
REMARK 3 S21: -0.2223 S22: 0.0232 S23: 0.4688
REMARK 3 S31: 0.2068 S32: -0.4299 S33: 0.0001
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN R AND (RESSEQ -15:-7)
REMARK 3 ORIGIN FOR THE GROUP (A): 135.5706 24.7207 143.4691
REMARK 3 T TENSOR
REMARK 3 T11: 1.8674 T22: 1.7902
REMARK 3 T33: 1.9529 T12: -0.0001
REMARK 3 T13: -0.0878 T23: -0.1395
REMARK 3 L TENSOR
REMARK 3 L11: 0.0095 L22: 0.0028
REMARK 3 L33: 0.0012 L12: -0.0127
REMARK 3 L13: -0.0107 L23: 0.0093
REMARK 3 S TENSOR
REMARK 3 S11: 0.1189 S12: 0.1814 S13: 0.0253
REMARK 3 S21: 0.2413 S22: -0.1109 S23: -0.1615
REMARK 3 S31: -0.0832 S32: 0.1787 S33: 0.0000
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: (CHAIN J AND RESID 9:237 )
REMARK 3 ORIGIN FOR THE GROUP (A): 148.5578 55.0109 139.8855
REMARK 3 T TENSOR
REMARK 3 T11: 0.5625 T22: 0.7906
REMARK 3 T33: 0.5333 T12: -0.1399
REMARK 3 T13: 0.0266 T23: 0.1916
REMARK 3 L TENSOR
REMARK 3 L11: 0.8798 L22: 0.6098
REMARK 3 L33: 1.0774 L12: 0.4595
REMARK 3 L13: -0.0884 L23: 0.1362
REMARK 3 S TENSOR
REMARK 3 S11: -0.0174 S12: 0.2973 S13: 0.2703
REMARK 3 S21: -0.0327 S22: 0.0606 S23: -0.0086
REMARK 3 S31: -0.1460 S32: 0.1904 S33: -0.0001
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN I AND RESID 126:291
REMARK 3 ORIGIN FOR THE GROUP (A): 106.7710 7.4440 211.4245
REMARK 3 T TENSOR
REMARK 3 T11: 0.9328 T22: 0.6011
REMARK 3 T33: 0.5565 T12: -0.0185
REMARK 3 T13: -0.0152 T23: -0.0061
REMARK 3 L TENSOR
REMARK 3 L11: 0.5705 L22: 0.8719
REMARK 3 L33: 0.3109 L12: 0.2597
REMARK 3 L13: -0.1636 L23: 0.0254
REMARK 3 S TENSOR
REMARK 3 S11: -0.0892 S12: -0.3745 S13: 0.0388
REMARK 3 S21: 0.5398 S22: -0.0187 S23: -0.0772
REMARK 3 S31: -0.1074 S32: -0.2593 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 4IFD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 20-DEC-12.
REMARK 100 THE DEPOSITION ID IS D_1000076682.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-OCT-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 10
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X10SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9199
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 99137
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.805
REMARK 200 RESOLUTION RANGE LOW (A) : 49.640
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 87.4
REMARK 200 DATA REDUNDANCY : 12.80
REMARK 200 R MERGE (I) : 0.17600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.2500
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 56.5
REMARK 200 DATA REDUNDANCY IN SHELL : 2.50
REMARK 200 R MERGE FOR SHELL (I) : 0.54800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.890
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 2NN6, 2WP8, 2JA9, 2JE6
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.93
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.67
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.02M TRIS PH7.5, 0.05M NACL, 0.001M
REMARK 280 MNCL2, 0.002M MGCL2, 1MM TCEP, 0.15M MES PH6.5, 0.27M NABR, 11.4-
REMARK 280 12.2% PEG 3350, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 292K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 53.72000
REMARK 290 SMTRY3 2 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 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: DODECAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DODECAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 54990 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 138770 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -266.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J,
REMARK 350 AND CHAINS: K, R
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 A 302
REMARK 465 ARG A 303
REMARK 465 GLU A 304
REMARK 465 ILE A 305
REMARK 465 GLY B -1
REMARK 465 HIS B 0
REMARK 465 ALA B 243
REMARK 465 SER B 244
REMARK 465 ALA B 245
REMARK 465 ARG B 246
REMARK 465 ALA C 2
REMARK 465 GLU C 3
REMARK 465 SER C 4
REMARK 465 THR C 5
REMARK 465 THR C 6
REMARK 465 SER C 100
REMARK 465 ALA C 101
REMARK 465 SER C 102
REMARK 465 ILE C 103
REMARK 465 LYS C 104
REMARK 465 ASP C 105
REMARK 465 LEU C 106
REMARK 465 ASP C 107
REMARK 465 ASP C 108
REMARK 465 PHE C 109
REMARK 465 GLY C 110
REMARK 465 GLU C 111
REMARK 465 GLU C 112
REMARK 465 GLU C 113
REMARK 465 LEU C 114
REMARK 465 PHE C 115
REMARK 465 GLU C 116
REMARK 465 VAL C 117
REMARK 465 THR C 118
REMARK 465 LYS C 119
REMARK 465 GLU C 120
REMARK 465 GLU C 194
REMARK 465 ASP C 195
REMARK 465 ASP C 196
REMARK 465 THR C 197
REMARK 465 LEU C 198
REMARK 465 ASN C 199
REMARK 465 GLU C 200
REMARK 465 THR C 201
REMARK 465 ASN C 202
REMARK 465 LEU C 203
REMARK 465 LYS C 204
REMARK 465 MET C 205
REMARK 465 ASN C 310
REMARK 465 SER C 311
REMARK 465 ASP C 312
REMARK 465 ASN C 313
REMARK 465 SER C 314
REMARK 465 GLU C 315
REMARK 465 GLU C 316
REMARK 465 GLU C 317
REMARK 465 GLU C 318
REMARK 465 VAL C 319
REMARK 465 ASP C 320
REMARK 465 ILE C 321
REMARK 465 ASP C 322
REMARK 465 MET C 323
REMARK 465 ASP C 324
REMARK 465 LYS C 325
REMARK 465 LEU C 326
REMARK 465 GLY D -21
REMARK 465 HIS D -20
REMARK 465 GLY D -19
REMARK 465 ASN D -18
REMARK 465 ASN D -17
REMARK 465 LYS D -16
REMARK 465 GLU D -15
REMARK 465 PRO D -14
REMARK 465 ASN D -13
REMARK 465 THR D -12
REMARK 465 LYS D -11
REMARK 465 ASN D -10
REMARK 465 ARG D -9
REMARK 465 LEU D -8
REMARK 465 ASP D -7
REMARK 465 SER D -6
REMARK 465 ALA D -5
REMARK 465 GLU D -4
REMARK 465 LYS D -3
REMARK 465 LYS D -2
REMARK 465 LYS D -1
REMARK 465 LYS D 0
REMARK 465 MET F 1
REMARK 465 ASN F 2
REMARK 465 VAL F 3
REMARK 465 THR F 23
REMARK 465 THR F 24
REMARK 465 THR F 25
REMARK 465 HIS F 26
REMARK 465 VAL F 27
REMARK 465 PRO F 28
REMARK 465 GLU F 29
REMARK 465 LYS F 30
REMARK 465 LYS F 31
REMARK 465 SER F 32
REMARK 465 THR F 33
REMARK 465 ASP F 34
REMARK 465 LEU F 35
REMARK 465 THR F 36
REMARK 465 PRO F 37
REMARK 465 LYS F 38
REMARK 465 GLY F 39
REMARK 465 ASN F 40
REMARK 465 GLU F 41
REMARK 465 ASN F 150
REMARK 465 PRO F 151
REMARK 465 GLN F 152
REMARK 465 ASP F 153
REMARK 465 ASP F 154
REMARK 465 ASP F 155
REMARK 465 SER F 156
REMARK 465 GLN F 157
REMARK 465 SER F 158
REMARK 465 LYS F 159
REMARK 465 MET F 160
REMARK 465 THR F 161
REMARK 465 SER F 162
REMARK 465 GLU F 249
REMARK 465 THR F 250
REMARK 465 GLY G -1
REMARK 465 HIS G 0
REMARK 465 VAL G 237
REMARK 465 LYS G 238
REMARK 465 GLU G 239
REMARK 465 GLU G 240
REMARK 465 ARG H -1
REMARK 465 SER H 0
REMARK 465 MET H 1
REMARK 465 SER H 18
REMARK 465 ASN H 19
REMARK 465 LEU H 20
REMARK 465 SER H 21
REMARK 465 TYR H 22
REMARK 465 ASN H 23
REMARK 465 ASN H 24
REMARK 465 THR H 25
REMARK 465 GLY H 26
REMARK 465 ILE H 27
REMARK 465 SER H 28
REMARK 465 ASP H 29
REMARK 465 ASP H 30
REMARK 465 GLU H 31
REMARK 465 ASN H 32
REMARK 465 ASP H 33
REMARK 465 GLU H 34
REMARK 465 GLU H 35
REMARK 465 ASP H 36
REMARK 465 ILE H 37
REMARK 465 TYR H 38
REMARK 465 MET H 39
REMARK 465 HIS H 40
REMARK 465 ASP H 41
REMARK 465 VAL H 42
REMARK 465 ASN H 43
REMARK 465 SER H 44
REMARK 465 ALA H 45
REMARK 465 SER H 46
REMARK 465 LYS H 47
REMARK 465 SER H 48
REMARK 465 GLU H 49
REMARK 465 PRO H 246
REMARK 465 SER H 247
REMARK 465 ALA H 248
REMARK 465 ASN H 249
REMARK 465 ASN H 250
REMARK 465 SER H 251
REMARK 465 SER H 252
REMARK 465 SER H 253
REMARK 465 ILE H 254
REMARK 465 LYS H 255
REMARK 465 SER H 256
REMARK 465 THR H 257
REMARK 465 GLY H 258
REMARK 465 PRO H 259
REMARK 465 THR H 260
REMARK 465 GLY H 261
REMARK 465 ALA H 262
REMARK 465 VAL H 263
REMARK 465 SER H 264
REMARK 465 LEU H 265
REMARK 465 ASN H 266
REMARK 465 PRO H 267
REMARK 465 SER H 268
REMARK 465 ILE H 269
REMARK 465 THR H 270
REMARK 465 ARG H 271
REMARK 465 LEU H 272
REMARK 465 GLU H 273
REMARK 465 GLU H 274
REMARK 465 GLY H 358
REMARK 465 ASN H 359
REMARK 465 MET I -8
REMARK 465 LYS I -7
REMARK 465 HIS I -6
REMARK 465 HIS I -5
REMARK 465 HIS I -4
REMARK 465 HIS I -3
REMARK 465 HIS I -2
REMARK 465 HIS I -1
REMARK 465 PRO I 0
REMARK 465 THR I 72
REMARK 465 ASP I 73
REMARK 465 GLN I 74
REMARK 465 GLU I 75
REMARK 465 GLU I 76
REMARK 465 GLU I 77
REMARK 465 ARG I 78
REMARK 465 GLU I 79
REMARK 465 GLY I 80
REMARK 465 THR I 81
REMARK 465 ASP I 82
REMARK 465 GLN I 83
REMARK 465 SER I 84
REMARK 465 THR I 85
REMARK 465 GLU I 86
REMARK 465 GLU I 87
REMARK 465 GLU I 88
REMARK 465 LYS I 89
REMARK 465 SER I 90
REMARK 465 VAL I 91
REMARK 465 ASP I 92
REMARK 465 ALA I 93
REMARK 465 SER I 94
REMARK 465 PRO I 95
REMARK 465 ASN I 96
REMARK 465 ASP I 97
REMARK 465 VAL I 98
REMARK 465 THR I 114
REMARK 465 GLU I 115
REMARK 465 LYS I 116
REMARK 465 GLY I 117
REMARK 465 ARG I 118
REMARK 465 LYS I 119
REMARK 465 THR I 120
REMARK 465 ASN I 121
REMARK 465 LYS I 122
REMARK 465 TYR I 123
REMARK 465 ALA I 124
REMARK 465 ASN I 125
REMARK 465 SER I 163
REMARK 465 PRO I 164
REMARK 465 ILE I 165
REMARK 465 ASP I 166
REMARK 465 SER I 167
REMARK 465 GLY I 168
REMARK 465 ILE I 169
REMARK 465 GLY I 170
REMARK 465 SER I 171
REMARK 465 ASN I 172
REMARK 465 GLY I 173
REMARK 465 SER I 174
REMARK 465 GLY I 175
REMARK 465 ILE I 176
REMARK 465 VAL I 177
REMARK 465 ALA I 178
REMARK 465 ALA I 179
REMARK 465 GLY I 180
REMARK 465 GLY I 181
REMARK 465 GLY I 182
REMARK 465 SER I 183
REMARK 465 GLY I 184
REMARK 465 PHE I 292
REMARK 465 GLY J -1
REMARK 465 ALA J 0
REMARK 465 MET J 1
REMARK 465 SER J 2
REMARK 465 VAL J 3
REMARK 465 PRO J 4
REMARK 465 ALA J 5
REMARK 465 ILE J 6
REMARK 465 ALA J 7
REMARK 465 PRO J 8
REMARK 465 MET J 238
REMARK 465 ASP J 239
REMARK 465 SER J 240
REMARK 465 PHE J 241
REMARK 465 ASP J 242
REMARK 465 LYS J 243
REMARK 465 ASP J 244
REMARK 465 LEU J 245
REMARK 465 GLU J 246
REMARK 465 ARG J 247
REMARK 465 ASP J 248
REMARK 465 SER J 330
REMARK 465 SER J 331
REMARK 465 ILE J 332
REMARK 465 VAL J 333
REMARK 465 LEU J 334
REMARK 465 ASP J 335
REMARK 465 SER J 336
REMARK 465 GLU J 337
REMARK 465 HIS J 338
REMARK 465 PHE J 339
REMARK 465 ASP J 340
REMARK 465 VAL J 341
REMARK 465 ASN J 342
REMARK 465 ASP J 343
REMARK 465 ASN J 344
REMARK 465 PRO J 345
REMARK 465 ASP J 346
REMARK 465 ILE J 347
REMARK 465 GLU J 348
REMARK 465 ALA J 349
REMARK 465 GLY J 350
REMARK 465 ASP J 351
REMARK 465 ASP J 352
REMARK 465 ASP J 353
REMARK 465 ASP J 354
REMARK 465 ASN J 355
REMARK 465 ASN J 356
REMARK 465 GLU J 357
REMARK 465 SER J 358
REMARK 465 SER J 359
REMARK 465 SER J 360
REMARK 465 ASN J 361
REMARK 465 THR J 362
REMARK 465 THR J 363
REMARK 465 ARG K 515
REMARK 465 SER K 516
REMARK 465 MET K 517
REMARK 465 GLU K 518
REMARK 465 ALA K 519
REMARK 465 THR K 520
REMARK 465 PRO K 521
REMARK 465 ILE K 522
REMARK 465 PRO K 523
REMARK 465 SER K 524
REMARK 465 SER K 525
REMARK 465 GLU K 526
REMARK 465 THR K 527
REMARK 465 LYS K 528
REMARK 465 ALA K 529
REMARK 465 ASP K 530
REMARK 465 GLY K 531
REMARK 465 SER K 558
REMARK 465 LYS K 559
REMARK 465 SER K 560
REMARK 465 ARG K 561
REMARK 465 ALA K 562
REMARK 465 LYS K 563
REMARK 465 PRO K 564
REMARK 465 ILE K 620
REMARK 465 GLU K 621
REMARK 465 LYS K 622
REMARK 465 PRO K 623
REMARK 465 LEU K 624
REMARK 465 VAL K 625
REMARK 465 VAL K 626
REMARK 465 PRO K 627
REMARK 465 VAL K 628
REMARK 465 LYS K 629
REMARK 465 LEU K 630
REMARK 465 GLU K 631
REMARK 465 GLU K 632
REMARK 465 ILE K 633
REMARK 465 LYS K 634
REMARK 465 THR K 635
REMARK 465 VAL K 636
REMARK 465 ASP K 637
REMARK 465 PRO K 638
REMARK 465 ALA K 639
REMARK 465 SER K 640
REMARK 465 ALA K 641
REMARK 465 PRO K 642
REMARK 465 ASN K 643
REMARK 465 HIS K 644
REMARK 465 SER K 645
REMARK 465 PRO K 646
REMARK 465 GLU K 647
REMARK 465 ILE K 648
REMARK 465 ASP K 649
REMARK 465 ASN K 650
REMARK 465 LEU K 651
REMARK 465 ASP K 652
REMARK 465 ASP K 653
REMARK 465 LEU K 654
REMARK 465 VAL K 655
REMARK 465 VAL K 656
REMARK 465 LEU K 657
REMARK 465 LYS K 658
REMARK 465 LYS K 659
REMARK 465 LYS K 660
REMARK 465 ASN K 661
REMARK 465 ILE K 662
REMARK 465 GLN K 663
REMARK 465 LYS K 664
REMARK 465 LYS K 665
REMARK 465 GLN K 666
REMARK 465 PRO K 667
REMARK 465 ALA K 668
REMARK 465 LYS K 669
REMARK 465 GLU K 670
REMARK 465 LYS K 671
REMARK 465 GLY K 672
REMARK 465 VAL K 673
REMARK 465 THR K 674
REMARK 465 GLU K 675
REMARK 465 LYS K 676
REMARK 465 ASP K 677
REMARK 465 ALA K 678
REMARK 465 VAL K 679
REMARK 465 ASP K 680
REMARK 465 TYR K 681
REMARK 465 SER K 682
REMARK 465 LYS K 683
REMARK 465 ILE K 684
REMARK 465 PRO K 685
REMARK 465 ASN K 686
REMARK 465 ILE K 687
REMARK 465 LEU K 688
REMARK 465 SER K 689
REMARK 465 ASN K 690
REMARK 465 LYS K 691
REMARK 465 PRO K 692
REMARK 465 GLY K 693
REMARK 465 C R -45
REMARK 465 U R -29
REMARK 465 U R -28
REMARK 465 U R -27
REMARK 465 U R -26
REMARK 465 U R -25
REMARK 465 U R -24
REMARK 465 U R -23
REMARK 465 U R -22
REMARK 465 U R -21
REMARK 465 U R -20
REMARK 465 U R -19
REMARK 465 U R -18
REMARK 465 U R -17
REMARK 465 U R -16
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLU A 69 CG CD OE1 OE2
REMARK 470 ILE A 96 CG1 CG2 CD1
REMARK 470 GLN A 173 CG CD OE1 NE2
REMARK 470 GLU A 181 CG CD OE1 OE2
REMARK 470 LYS A 274 CG CD CE NZ
REMARK 470 LYS A 292 CG CD CE NZ
REMARK 470 MET A 296 CG SD CE
REMARK 470 LEU A 297 CG CD1 CD2
REMARK 470 GLU A 300 CG CD OE1 OE2
REMARK 470 MET B 1 CG SD CE
REMARK 470 GLN B 64 CG CD OE1 NE2
REMARK 470 GLU B 85 CG CD OE1 OE2
REMARK 470 LYS B 88 CG CD CE NZ
REMARK 470 LYS B 238 CG CD CE NZ
REMARK 470 ASN B 242 CG OD1 ND2
REMARK 470 LEU C 7 CG CD1 CD2
REMARK 470 GLU C 8 CG CD OE1 OE2
REMARK 470 ASN C 67 CG OD1 ND2
REMARK 470 LYS C 168 CG CD CE NZ
REMARK 470 GLU C 181 CG CD OE1 OE2
REMARK 470 ASP C 182 CG OD1 OD2
REMARK 470 SER C 186 OG
REMARK 470 LEU C 193 CG CD1 CD2
REMARK 470 ARG C 260 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 264 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 140 CG CD CE NZ
REMARK 470 ASP E 110 CG OD1 OD2
REMARK 470 LYS E 113 CG CD CE NZ
REMARK 470 LYS E 118 CG CD CE NZ
REMARK 470 GLU E 165 CG CD OE1 OE2
REMARK 470 GLU E 167 CG CD OE1 OE2
REMARK 470 LEU F 147 CG CD1 CD2
REMARK 470 MET G 1 CG SD CE
REMARK 470 LYS G 47 CG CD CE NZ
REMARK 470 LYS G 49 CG CD CE NZ
REMARK 470 LYS G 107 CG CD CE NZ
REMARK 470 LYS G 108 CG CD CE NZ
REMARK 470 GLU G 199 CG CD OE1 OE2
REMARK 470 LYS G 224 CG CD CE NZ
REMARK 470 GLU H 3 CG CD OE1 OE2
REMARK 470 SER H 50 OG
REMARK 470 LYS H 122 CG CD CE NZ
REMARK 470 ILE H 147 CG1 CG2 CD1
REMARK 470 LEU H 148 CG CD1 CD2
REMARK 470 ARG H 150 CG CD NE CZ NH1 NH2
REMARK 470 LYS H 151 CG CD CE NZ
REMARK 470 GLN H 178 CG CD OE1 NE2
REMARK 470 LYS H 211 CG CD CE NZ
REMARK 470 THR H 245 OG1 CG2
REMARK 470 GLU H 275 CG CD OE1 OE2
REMARK 470 ASN H 331 CG OD1 ND2
REMARK 470 MET I 1 CG SD CE
REMARK 470 PHE I 5 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLN I 6 CG CD OE1 NE2
REMARK 470 LYS I 26 CG CD CE NZ
REMARK 470 ASP I 27 CG OD1 OD2
REMARK 470 GLU I 68 CG CD OE1 OE2
REMARK 470 GLU I 69 CG CD OE1 OE2
REMARK 470 LYS I 70 CG CD CE NZ
REMARK 470 THR I 99 OG1 CG2
REMARK 470 ARG I 100 CG CD NE CZ NH1 NH2
REMARK 470 GLN I 192 CG CD OE1 NE2
REMARK 470 ASP I 216 CG OD1 OD2
REMARK 470 ARG I 217 CG CD NE CZ NH1 NH2
REMARK 470 THR I 276 OG1 CG2
REMARK 470 LYS I 290 CG CD CE NZ
REMARK 470 ARG J 9 CG CD NE CZ NH1 NH2
REMARK 470 LYS J 124 CG CD CE NZ
REMARK 470 ASP J 189 CG OD1 OD2
REMARK 470 ARG J 199 CG CD NE CZ NH1 NH2
REMARK 470 LEU J 200 CG CD1 CD2
REMARK 470 LYS J 207 CG CD CE NZ
REMARK 470 VAL J 209 CG1 CG2
REMARK 470 GLU J 282 CG CD OE1 OE2
REMARK 470 TYR J 283 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS J 384 CG CD CE NZ
REMARK 470 ILE J 386 CG1 CG2 CD1
REMARK 470 GLN J 415 CG CD OE1 NE2
REMARK 470 LYS J 429 CG CD CE NZ
REMARK 470 LYS J 511 CG CD CE NZ
REMARK 470 LYS J 515 CG CD CE NZ
REMARK 470 LYS J 524 CG CD CE NZ
REMARK 470 LYS J 532 CG CD CE NZ
REMARK 470 LYS J 664 CG CD CE NZ
REMARK 470 LYS J 702 CG CD CE NZ
REMARK 470 HIS J 704 CG ND1 CD2 CE1 NE2
REMARK 470 ASP J 706 CG OD1 OD2
REMARK 470 GLU J 708 CG CD OE1 OE2
REMARK 470 ASP J 711 CG OD1 OD2
REMARK 470 GLU J 716 CG CD OE1 OE2
REMARK 470 GLU J 781 CG CD OE1 OE2
REMARK 470 GLU J 797 CG CD OE1 OE2
REMARK 470 PHE J 922 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS J 932 CG CD CE NZ
REMARK 470 THR J 945 OG1 CG2
REMARK 470 GLU J 946 CG CD OE1 OE2
REMARK 470 ASP J 947 CG OD1 OD2
REMARK 470 ASN J 949 CG OD1 ND2
REMARK 470 PHE J 962 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASN J 966 CG OD1 ND2
REMARK 470 LYS J 969 CG CD CE NZ
REMARK 470 ARG J 984 CG CD NE CZ NH1 NH2
REMARK 470 ILE J 990 CG1 CG2 CD1
REMARK 470 LYS J 993 CG CD CE NZ
REMARK 470 LYS J 995 CG CD CE NZ
REMARK 470 LYS J1001 CG CD CE NZ
REMARK 470 ILE K 532 CG1 CG2 CD1
REMARK 470 GLU K 535 CG CD OE1 OE2
REMARK 470 LYS K 587 CG CD CE NZ
REMARK 470 LEU K 613 CG CD1 CD2
REMARK 470 GLU K 614 CG CD OE1 OE2
REMARK 470 GLU K 619 CG CD OE1 OE2
REMARK 470 A R -39 N9 C8 N7 C5 C6 N6 N1
REMARK 470 A R -39 C2 N3 C4
REMARK 470 G R -38 N9 C8 N7 C5 C6 O6 N1
REMARK 470 G R -38 C2 N2 N3 C4
REMARK 470 U R -14 N1 C2 O2 N3 C4 O4 C5
REMARK 470 U R -14 C6
REMARK 470 U R -13 N1 C2 O2 N3 C4 O4 C5
REMARK 470 U R -13 C6
REMARK 470 U R -12 N1 C2 O2 N3 C4 O4 C5
REMARK 470 U R -12 C6
REMARK 470 U R -11 N1 C2 O2 N3 C4 O4 C5
REMARK 470 U R -11 C6
REMARK 470 U R -10 N1 C2 O2 N3 C4 O4 C5
REMARK 470 U R -10 C6
REMARK 470 U R -9 N1 C2 O2 N3 C4 O4 C5
REMARK 470 U R -9 C6
REMARK 470 U R -8 N1 C2 O2 N3 C4 O4 C5
REMARK 470 U R -8 C6
REMARK 470 U R -7 N1 C2 O2 N3 C4 O4 C5
REMARK 470 U R -7 C6
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 ASN A 95 90.62 -68.08
REMARK 500 SER A 129 -70.17 -128.82
REMARK 500 HIS A 170 78.94 -113.86
REMARK 500 GLU A 181 -75.82 -74.11
REMARK 500 GLN A 204 -146.11 -113.68
REMARK 500 ASP A 222 74.74 55.60
REMARK 500 LYS A 250 79.58 -111.18
REMARK 500 ASP B 132 55.06 -159.10
REMARK 500 ASP B 167 -83.77 56.93
REMARK 500 ASP B 173 87.88 55.98
REMARK 500 LYS C 71 44.08 -100.96
REMARK 500 LEU C 255 -155.45 -107.59
REMARK 500 THR C 261 -160.38 -104.11
REMARK 500 THR C 279 -56.50 -121.68
REMARK 500 ASN C 287 88.59 -67.32
REMARK 500 ASP C 333 81.36 56.06
REMARK 500 THR C 336 147.48 68.19
REMARK 500 HIS D 12 31.73 -97.38
REMARK 500 GLN D 22 -108.07 58.45
REMARK 500 THR D 60 -162.79 -116.05
REMARK 500 SER D 105 22.47 -140.87
REMARK 500 LYS D 140 -79.53 -58.17
REMARK 500 HIS E 0 -60.18 -102.69
REMARK 500 PRO E 28 4.73 -58.50
REMARK 500 SER E 107 -59.21 -139.33
REMARK 500 THR E 117 -165.72 -126.84
REMARK 500 GLU E 165 -83.16 -97.74
REMARK 500 PRO E 170 109.94 -57.03
REMARK 500 TYR E 175 -40.04 -135.66
REMARK 500 ASP E 200 76.54 52.37
REMARK 500 SER F 21 -148.41 -92.64
REMARK 500 CYS F 56 -168.64 -119.68
REMARK 500 LEU F 67 -112.72 55.03
REMARK 500 HIS F 69 118.61 -162.16
REMARK 500 SER F 86 -129.89 55.71
REMARK 500 LEU F 102 -95.38 -83.03
REMARK 500 LYS F 132 42.35 38.48
REMARK 500 THR F 148 24.02 -72.25
REMARK 500 ASP F 217 -118.53 54.96
REMARK 500 MET F 246 -67.64 -93.55
REMARK 500 PHE G 91 -4.43 69.39
REMARK 500 ALA G 101 40.26 -92.48
REMARK 500 ASP G 152 -142.76 56.12
REMARK 500 ALA G 222 -0.60 -160.16
REMARK 500 ASP H 77 -113.84 59.08
REMARK 500 ASN H 92 -114.88 57.24
REMARK 500 ASN H 121 -103.04 40.09
REMARK 500 PHE H 162 -66.51 -104.23
REMARK 500 VAL H 173 98.39 -69.01
REMARK 500 ASN I 49 10.92 59.13
REMARK 500
REMARK 500 THIS ENTRY HAS 80 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN J1106 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS J 47 SG
REMARK 620 2 CYS J 52 SG 97.3
REMARK 620 3 CYS J 55 SG 96.6 93.6
REMARK 620 4 HIS J 184 NE2 135.6 116.5 108.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG J1105 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP J 543 OD1
REMARK 620 2 ASP J 552 OD1 167.6
REMARK 620 3 ASP J 552 OD2 120.4 60.3
REMARK 620 4 U R -2 O3' 79.3 91.3 130.4
REMARK 620 5 U R -1 OP1 81.7 102.0 152.2 66.2
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR E 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR F 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL G 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES G 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR H 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL H 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL H 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL H 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR I 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR J 1101
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR J 1102
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR J 1103
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR J 1104
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG J 1105
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN J 1106
DBREF 4IFD A 2 305 UNP Q05636 RRP45_YEAST 2 305
DBREF 4IFD B 1 246 UNP P46948 RRP41_YEAST 1 246
DBREF 4IFD C 2 394 UNP P25359 RRP43_YEAST 2 394
DBREF 4IFD D 1 223 UNP P53256 RRP46_YEAST 1 223
DBREF 4IFD E 1 265 UNP Q12277 RRP42_YEAST 1 265
DBREF 4IFD F 1 250 UNP P48240 MTR3_YEAST 1 250
DBREF 4IFD G 1 240 UNP Q08285 RRP40_YEAST 1 240
DBREF 4IFD H 1 359 UNP P38792 RRP4_YEAST 1 359
DBREF 4IFD I 1 292 UNP P53859 CSL4_YEAST 1 292
DBREF 4IFD J 1 1001 UNP Q08162 RRP44_YEAST 1 1001
DBREF 4IFD K 518 693 UNP Q12149 RRP6_YEAST 518 693
DBREF 4IFD R -45 -1 PDB 4IFD 4IFD -45 -1
SEQADV 4IFD GLY B -1 UNP P46948 EXPRESSION TAG
SEQADV 4IFD HIS B 0 UNP P46948 EXPRESSION TAG
SEQADV 4IFD SER C 102 UNP P25359 ALA 102 ENGINEERED MUTATION
SEQADV 4IFD MET C 363 UNP P25359 VAL 363 ENGINEERED MUTATION
SEQADV 4IFD GLY D -21 UNP P53256 EXPRESSION TAG
SEQADV 4IFD HIS D -20 UNP P53256 EXPRESSION TAG
SEQADV 4IFD GLY D -19 UNP P53256 EXPRESSION TAG
SEQADV 4IFD ASN D -18 UNP P53256 EXPRESSION TAG
SEQADV 4IFD ASN D -17 UNP P53256 EXPRESSION TAG
SEQADV 4IFD LYS D -16 UNP P53256 EXPRESSION TAG
SEQADV 4IFD GLU D -15 UNP P53256 EXPRESSION TAG
SEQADV 4IFD PRO D -14 UNP P53256 EXPRESSION TAG
SEQADV 4IFD ASN D -13 UNP P53256 EXPRESSION TAG
SEQADV 4IFD THR D -12 UNP P53256 EXPRESSION TAG
SEQADV 4IFD LYS D -11 UNP P53256 EXPRESSION TAG
SEQADV 4IFD ASN D -10 UNP P53256 EXPRESSION TAG
SEQADV 4IFD ARG D -9 UNP P53256 EXPRESSION TAG
SEQADV 4IFD LEU D -8 UNP P53256 EXPRESSION TAG
SEQADV 4IFD ASP D -7 UNP P53256 EXPRESSION TAG
SEQADV 4IFD SER D -6 UNP P53256 EXPRESSION TAG
SEQADV 4IFD ALA D -5 UNP P53256 EXPRESSION TAG
SEQADV 4IFD GLU D -4 UNP P53256 EXPRESSION TAG
SEQADV 4IFD LYS D -3 UNP P53256 EXPRESSION TAG
SEQADV 4IFD LYS D -2 UNP P53256 EXPRESSION TAG
SEQADV 4IFD LYS D -1 UNP P53256 EXPRESSION TAG
SEQADV 4IFD LYS D 0 UNP P53256 EXPRESSION TAG
SEQADV 4IFD GLY E -1 UNP Q12277 EXPRESSION TAG
SEQADV 4IFD HIS E 0 UNP Q12277 EXPRESSION TAG
SEQADV 4IFD ILE E 138 UNP Q12277 VAL 138 ENGINEERED MUTATION
SEQADV 4IFD SER F 75 UNP P48240 THR 75 ENGINEERED MUTATION
SEQADV 4IFD THR F 161 UNP P48240 MET 161 ENGINEERED MUTATION
SEQADV 4IFD GLY G -1 UNP Q08285 EXPRESSION TAG
SEQADV 4IFD HIS G 0 UNP Q08285 EXPRESSION TAG
SEQADV 4IFD ARG H -1 UNP P38792 EXPRESSION TAG
SEQADV 4IFD SER H 0 UNP P38792 EXPRESSION TAG
SEQADV 4IFD MET I -8 UNP P53859 EXPRESSION TAG
SEQADV 4IFD LYS I -7 UNP P53859 EXPRESSION TAG
SEQADV 4IFD HIS I -6 UNP P53859 EXPRESSION TAG
SEQADV 4IFD HIS I -5 UNP P53859 EXPRESSION TAG
SEQADV 4IFD HIS I -4 UNP P53859 EXPRESSION TAG
SEQADV 4IFD HIS I -3 UNP P53859 EXPRESSION TAG
SEQADV 4IFD HIS I -2 UNP P53859 EXPRESSION TAG
SEQADV 4IFD HIS I -1 UNP P53859 EXPRESSION TAG
SEQADV 4IFD PRO I 0 UNP P53859 EXPRESSION TAG
SEQADV 4IFD GLY J -1 UNP Q08162 EXPRESSION TAG
SEQADV 4IFD ALA J 0 UNP Q08162 EXPRESSION TAG
SEQADV 4IFD ASN J 171 UNP Q08162 ASP 171 ENGINEERED MUTATION
SEQADV 4IFD ASN J 551 UNP Q08162 ASP 551 ENGINEERED MUTATION
SEQADV 4IFD ARG K 515 UNP Q12149 EXPRESSION TAG
SEQADV 4IFD SER K 516 UNP Q12149 EXPRESSION TAG
SEQADV 4IFD MET K 517 UNP Q12149 EXPRESSION TAG
SEQRES 1 A 304 ALA LYS ASP ILE GLU ILE SER ALA SER GLU SER LYS PHE
SEQRES 2 A 304 ILE LEU GLU ALA LEU ARG GLN ASN TYR ARG LEU ASP GLY
SEQRES 3 A 304 ARG SER PHE ASP GLN PHE ARG ASP VAL GLU ILE THR PHE
SEQRES 4 A 304 GLY LYS GLU PHE GLY ASP VAL SER VAL LYS MET GLY ASN
SEQRES 5 A 304 THR LYS VAL HIS CYS ARG ILE SER CYS GLN ILE ALA GLN
SEQRES 6 A 304 PRO TYR GLU ASP ARG PRO PHE GLU GLY LEU PHE VAL ILE
SEQRES 7 A 304 SER THR GLU ILE SER PRO MET ALA GLY SER GLN PHE GLU
SEQRES 8 A 304 ASN GLY ASN ILE THR GLY GLU ASP GLU VAL LEU CYS SER
SEQRES 9 A 304 ARG ILE ILE GLU LYS SER VAL ARG ARG SER GLY ALA LEU
SEQRES 10 A 304 ASP VAL GLU GLY LEU CYS ILE VAL ALA GLY SER LYS CYS
SEQRES 11 A 304 TRP ALA VAL ARG ALA ASP VAL HIS PHE LEU ASP CYS ASP
SEQRES 12 A 304 GLY GLY PHE ILE ASP ALA SER CYS ILE ALA VAL MET ALA
SEQRES 13 A 304 GLY LEU MET HIS PHE LYS LYS PRO ASP ILE THR VAL HIS
SEQRES 14 A 304 GLY GLU GLN ILE ILE VAL HIS PRO VAL ASN GLU ARG GLU
SEQRES 15 A 304 PRO VAL PRO LEU GLY ILE LEU HIS ILE PRO ILE CYS VAL
SEQRES 16 A 304 THR PHE SER PHE PHE ASN PRO GLN ASP THR GLU GLU ASN
SEQRES 17 A 304 ILE LYS GLY GLU THR ASN SER GLU ILE SER ILE ILE ASP
SEQRES 18 A 304 ALA THR LEU LYS GLU GLU LEU LEU ARG ASP GLY VAL LEU
SEQRES 19 A 304 THR VAL THR LEU ASN LYS ASN ARG GLU VAL VAL GLN VAL
SEQRES 20 A 304 SER LYS ALA GLY GLY LEU PRO MET ASP ALA LEU THR LEU
SEQRES 21 A 304 MET LYS CYS CYS HIS GLU ALA TYR SER ILE ILE GLU LYS
SEQRES 22 A 304 ILE THR ASP GLN ILE LEU GLN LEU LEU LYS GLU ASP SER
SEQRES 23 A 304 GLU LYS ARG ASN LYS TYR ALA ALA MET LEU THR SER GLU
SEQRES 24 A 304 ASN ALA ARG GLU ILE
SEQRES 1 B 248 GLY HIS MET SER ARG LEU GLU ILE TYR SER PRO GLU GLY
SEQRES 2 B 248 LEU ARG LEU ASP GLY ARG ARG TRP ASN GLU LEU ARG ARG
SEQRES 3 B 248 PHE GLU SER SER ILE ASN THR HIS PRO HIS ALA ALA ASP
SEQRES 4 B 248 GLY SER SER TYR MET GLU GLN GLY ASN ASN LYS ILE ILE
SEQRES 5 B 248 THR LEU VAL LYS GLY PRO LYS GLU PRO ARG LEU LYS SER
SEQRES 6 B 248 GLN MET ASP THR SER LYS ALA LEU LEU ASN VAL SER VAL
SEQRES 7 B 248 ASN ILE THR LYS PHE SER LYS PHE GLU ARG SER LYS SER
SEQRES 8 B 248 SER HIS LYS ASN GLU ARG ARG VAL LEU GLU ILE GLN THR
SEQRES 9 B 248 SER LEU VAL ARG MET PHE GLU LYS ASN VAL MET LEU ASN
SEQRES 10 B 248 ILE TYR PRO ARG THR VAL ILE ASP ILE GLU ILE HIS VAL
SEQRES 11 B 248 LEU GLU GLN ASP GLY GLY ILE MET GLY SER LEU ILE ASN
SEQRES 12 B 248 GLY ILE THR LEU ALA LEU ILE ASP ALA GLY ILE SER MET
SEQRES 13 B 248 PHE ASP TYR ILE SER GLY ILE SER VAL GLY LEU TYR ASP
SEQRES 14 B 248 THR THR PRO LEU LEU ASP THR ASN SER LEU GLU GLU ASN
SEQRES 15 B 248 ALA MET SER THR VAL THR LEU GLY VAL VAL GLY LYS SER
SEQRES 16 B 248 GLU LYS LEU SER LEU LEU LEU VAL GLU ASP LYS ILE PRO
SEQRES 17 B 248 LEU ASP ARG LEU GLU ASN VAL LEU ALA ILE GLY ILE ALA
SEQRES 18 B 248 GLY ALA HIS ARG VAL ARG ASP LEU MET ASP GLU GLU LEU
SEQRES 19 B 248 ARG LYS HIS ALA GLN LYS ARG VAL SER ASN ALA SER ALA
SEQRES 20 B 248 ARG
SEQRES 1 C 393 ALA GLU SER THR THR LEU GLU THR ILE GLU ILE HIS PRO
SEQRES 2 C 393 ILE THR PHE PRO PRO GLU VAL LEU ALA ARG ILE SER PRO
SEQRES 3 C 393 GLU LEU SER LEU GLN ARG HIS LEU SER LEU GLY ILE ARG
SEQRES 4 C 393 PRO CYS LEU ARG LYS TYR GLU GLU PHE ARG ASP VAL ALA
SEQRES 5 C 393 ILE GLU ASN ASN THR LEU SER ARG TYR ALA ASP ALA GLY
SEQRES 6 C 393 ASN ILE ASP THR LYS ASN ASN ILE LEU GLY SER ASN VAL
SEQRES 7 C 393 LEU LYS SER GLY LYS THR ILE VAL ILE THR SER ILE THR
SEQRES 8 C 393 GLY GLY ILE ILE GLU GLU THR SER ALA SER ILE LYS ASP
SEQRES 9 C 393 LEU ASP ASP PHE GLY GLU GLU GLU LEU PHE GLU VAL THR
SEQRES 10 C 393 LYS GLU GLU ASP ILE ILE ALA ASN TYR ALA SER VAL TYR
SEQRES 11 C 393 PRO VAL VAL GLU VAL GLU ARG GLY ARG VAL GLY ALA CYS
SEQRES 12 C 393 THR ASP GLU GLU MET THR ILE SER GLN LYS LEU HIS ASP
SEQRES 13 C 393 SER ILE LEU HIS SER ARG ILE LEU PRO LYS LYS ALA LEU
SEQRES 14 C 393 LYS VAL LYS ALA GLY VAL ARG SER ALA ASN GLU ASP GLY
SEQRES 15 C 393 THR PHE SER VAL LEU TYR PRO ASP GLU LEU GLU ASP ASP
SEQRES 16 C 393 THR LEU ASN GLU THR ASN LEU LYS MET LYS ARG LYS TRP
SEQRES 17 C 393 SER TYR VAL LEU TYR ALA LYS ILE VAL VAL LEU SER ARG
SEQRES 18 C 393 THR GLY PRO VAL PHE ASP LEU CYS TRP ASN SER LEU MET
SEQRES 19 C 393 TYR ALA LEU GLN SER VAL LYS LEU PRO ARG ALA PHE ILE
SEQRES 20 C 393 ASP GLU ARG ALA SER ASP LEU ARG MET THR ILE ARG THR
SEQRES 21 C 393 ARG GLY ARG SER ALA THR ILE ARG GLU THR TYR GLU ILE
SEQRES 22 C 393 ILE CYS ASP GLN THR LYS SER VAL PRO LEU MET ILE ASN
SEQRES 23 C 393 ALA LYS ASN ILE ALA PHE ALA SER ASN TYR GLY ILE VAL
SEQRES 24 C 393 GLU LEU ASP PRO GLU CYS GLN LEU GLN ASN SER ASP ASN
SEQRES 25 C 393 SER GLU GLU GLU GLU VAL ASP ILE ASP MET ASP LYS LEU
SEQRES 26 C 393 ASN THR VAL LEU ILE ALA ASP LEU ASP THR GLU ALA GLU
SEQRES 27 C 393 GLU THR SER ILE HIS SER THR ILE SER ILE LEU ALA ALA
SEQRES 28 C 393 PRO SER GLY ASN TYR LYS GLN LEU THR LEU MET GLY GLY
SEQRES 29 C 393 GLY ALA LYS ILE THR PRO GLU MET ILE LYS ARG SER LEU
SEQRES 30 C 393 LEU LEU SER ARG VAL ARG ALA ASP ASP LEU SER THR ARG
SEQRES 31 C 393 PHE ASN ILE
SEQRES 1 D 245 GLY HIS GLY ASN ASN LYS GLU PRO ASN THR LYS ASN ARG
SEQRES 2 D 245 LEU ASP SER ALA GLU LYS LYS LYS LYS MET SER VAL GLN
SEQRES 3 D 245 ALA GLU ILE GLY ILE LEU ASP HIS VAL ASP GLY SER SER
SEQRES 4 D 245 GLU PHE VAL SER GLN ASP THR LYS VAL ILE CYS SER VAL
SEQRES 5 D 245 THR GLY PRO ILE GLU PRO LYS ALA ARG GLN GLU LEU PRO
SEQRES 6 D 245 THR GLN LEU ALA LEU GLU ILE ILE VAL ARG PRO ALA LYS
SEQRES 7 D 245 GLY VAL ALA THR THR ARG GLU LYS VAL LEU GLU ASP LYS
SEQRES 8 D 245 LEU ARG ALA VAL LEU THR PRO LEU ILE THR ARG HIS CYS
SEQRES 9 D 245 TYR PRO ARG GLN LEU CYS GLN ILE THR CYS GLN ILE LEU
SEQRES 10 D 245 GLU SER GLY GLU ASP GLU ALA GLU PHE SER LEU ARG GLU
SEQRES 11 D 245 LEU SER CYS CYS ILE ASN ALA ALA PHE LEU ALA LEU VAL
SEQRES 12 D 245 ASP ALA GLY ILE ALA LEU ASN SER MET CYS ALA SER ILE
SEQRES 13 D 245 PRO ILE ALA ILE ILE LYS ASP THR SER ASP ILE ILE VAL
SEQRES 14 D 245 ASP PRO THR ALA GLU GLN LEU LYS ILE SER LEU SER VAL
SEQRES 15 D 245 HIS THR LEU ALA LEU GLU PHE VAL ASN GLY GLY LYS VAL
SEQRES 16 D 245 VAL LYS ASN VAL LEU LEU LEU ASP SER ASN GLY ASP PHE
SEQRES 17 D 245 ASN GLU ASP GLN LEU PHE SER LEU LEU GLU LEU GLY GLU
SEQRES 18 D 245 GLN LYS CYS GLN GLU LEU VAL THR ASN ILE ARG ARG ILE
SEQRES 19 D 245 ILE GLN ASP ASN ILE SER PRO ARG LEU VAL VAL
SEQRES 1 E 267 GLY HIS MET SER LEU SER VAL ALA GLU LYS SER TYR LEU
SEQRES 2 E 267 TYR ASP SER LEU ALA SER THR PRO SER ILE ARG PRO ASP
SEQRES 3 E 267 GLY ARG LEU PRO HIS GLN PHE ARG PRO ILE GLU ILE PHE
SEQRES 4 E 267 THR ASP PHE LEU PRO SER SER ASN GLY SER SER ARG ILE
SEQRES 5 E 267 ILE ALA SER ASP GLY SER GLU CYS ILE VAL SER ILE LYS
SEQRES 6 E 267 SER LYS VAL VAL ASP HIS HIS VAL GLU ASN GLU LEU LEU
SEQRES 7 E 267 GLN VAL ASP VAL ASP ILE ALA GLY GLN ARG ASP ASP ALA
SEQRES 8 E 267 LEU VAL VAL GLU THR ILE THR SER LEU LEU ASN LYS VAL
SEQRES 9 E 267 LEU LYS SER GLY SER GLY VAL ASP SER SER LYS LEU GLN
SEQRES 10 E 267 LEU THR LYS LYS TYR SER PHE LYS ILE PHE VAL ASP VAL
SEQRES 11 E 267 LEU VAL ILE SER SER HIS SER HIS PRO ILE SER LEU ILE
SEQRES 12 E 267 SER PHE ALA ILE TYR SER ALA LEU ASN SER THR TYR LEU
SEQRES 13 E 267 PRO LYS LEU ILE SER ALA PHE ASP ASP LEU GLU VAL GLU
SEQRES 14 E 267 GLU LEU PRO THR PHE HIS ASP TYR ASP MET VAL LYS LEU
SEQRES 15 E 267 ASP ILE ASN PRO PRO LEU VAL PHE ILE LEU ALA VAL VAL
SEQRES 16 E 267 GLY ASN ASN MET LEU LEU ASP PRO ALA ALA ASN GLU SER
SEQRES 17 E 267 GLU VAL ALA ASN ASN GLY LEU ILE ILE SER TRP SER ASN
SEQRES 18 E 267 GLY LYS ILE THR SER PRO ILE ARG SER VAL ALA LEU ASN
SEQRES 19 E 267 ASP SER ASN VAL LYS SER PHE LYS PRO HIS LEU LEU LYS
SEQRES 20 E 267 GLN GLY LEU ALA MET VAL GLU LYS TYR ALA PRO ASP VAL
SEQRES 21 E 267 VAL ARG SER LEU GLU ASN LEU
SEQRES 1 F 250 MET ASN VAL GLN ASP ARG ARG ARG LEU LEU GLY PRO ALA
SEQRES 2 F 250 ALA ALA LYS PRO MET ALA PHE SER ASN THR THR THR HIS
SEQRES 3 F 250 VAL PRO GLU LYS LYS SER THR ASP LEU THR PRO LYS GLY
SEQRES 4 F 250 ASN GLU SER GLU GLN GLU LEU SER LEU HIS THR GLY PHE
SEQRES 5 F 250 ILE GLU ASN CYS ASN GLY SER ALA LEU VAL GLU ALA ARG
SEQRES 6 F 250 SER LEU GLY HIS GLN THR SER LEU ILE SER ALA VAL TYR
SEQRES 7 F 250 GLY PRO ARG SER ILE ARG GLY SER PHE THR SER GLN GLY
SEQRES 8 F 250 THR ILE SER ILE GLN LEU LYS ASN GLY LEU LEU GLU LYS
SEQRES 9 F 250 TYR ASN THR ASN GLU LEU LYS GLU VAL SER SER PHE LEU
SEQRES 10 F 250 MET GLY ILE PHE ASN SER VAL VAL ASN LEU SER ARG TYR
SEQRES 11 F 250 PRO LYS SER GLY ILE ASP ILE PHE VAL TYR LEU THR TYR
SEQRES 12 F 250 ASP LYS ASP LEU THR ASN ASN PRO GLN ASP ASP ASP SER
SEQRES 13 F 250 GLN SER LYS MET THR SER SER GLN ILE SER SER LEU ILE
SEQRES 14 F 250 PRO HIS CYS ILE THR SER ILE THR LEU ALA LEU ALA ASP
SEQRES 15 F 250 ALA GLY ILE GLU LEU VAL ASP MET ALA GLY ALA GLY GLU
SEQRES 16 F 250 ALA ASN GLY THR VAL VAL SER PHE ILE LYS ASN GLY GLU
SEQRES 17 F 250 GLU ILE VAL GLY PHE TRP LYS ASP ASP GLY ASP ASP GLU
SEQRES 18 F 250 ASP LEU LEU GLU CYS LEU ASP ARG CYS LYS GLU GLN TYR
SEQRES 19 F 250 ASN ARG TYR ARG ASP LEU MET ILE SER CYS LEU MET ASN
SEQRES 20 F 250 GLN GLU THR
SEQRES 1 G 242 GLY HIS MET SER THR PHE ILE PHE PRO GLY ASP SER PHE
SEQRES 2 G 242 PRO VAL ASP PRO THR THR PRO VAL LYS LEU GLY PRO GLY
SEQRES 3 G 242 ILE TYR CYS ASP PRO ASN THR GLN GLU ILE ARG PRO VAL
SEQRES 4 G 242 ASN THR GLY VAL LEU HIS VAL SER ALA LYS GLY LYS SER
SEQRES 5 G 242 GLY VAL GLN THR ALA TYR ILE ASP TYR SER SER LYS ARG
SEQRES 6 G 242 TYR ILE PRO SER VAL ASN ASP PHE VAL ILE GLY VAL ILE
SEQRES 7 G 242 ILE GLY THR PHE SER ASP SER TYR LYS VAL SER LEU GLN
SEQRES 8 G 242 ASN PHE SER SER SER VAL SER LEU SER TYR MET ALA PHE
SEQRES 9 G 242 PRO ASN ALA SER LYS LYS ASN ARG PRO THR LEU GLN VAL
SEQRES 10 G 242 GLY ASP LEU VAL TYR ALA ARG VAL CYS THR ALA GLU LYS
SEQRES 11 G 242 GLU LEU GLU ALA GLU ILE GLU CYS PHE ASP SER THR THR
SEQRES 12 G 242 GLY ARG ASP ALA GLY PHE GLY ILE LEU GLU ASP GLY MET
SEQRES 13 G 242 ILE ILE ASP VAL ASN LEU ASN PHE ALA ARG GLN LEU LEU
SEQRES 14 G 242 PHE ASN ASN ASP PHE PRO LEU LEU LYS VAL LEU ALA ALA
SEQRES 15 G 242 HIS THR LYS PHE GLU VAL ALA ILE GLY LEU ASN GLY LYS
SEQRES 16 G 242 ILE TRP VAL LYS CYS GLU GLU LEU SER ASN THR LEU ALA
SEQRES 17 G 242 CYS TYR ARG THR ILE MET GLU CYS CYS GLN LYS ASN ASP
SEQRES 18 G 242 THR ALA ALA PHE LYS ASP ILE ALA LYS ARG GLN PHE LYS
SEQRES 19 G 242 GLU ILE LEU THR VAL LYS GLU GLU
SEQRES 1 H 361 ARG SER MET SER GLU VAL ILE THR ILE THR LYS ARG ASN
SEQRES 2 H 361 GLY ALA PHE GLN ASN SER SER ASN LEU SER TYR ASN ASN
SEQRES 3 H 361 THR GLY ILE SER ASP ASP GLU ASN ASP GLU GLU ASP ILE
SEQRES 4 H 361 TYR MET HIS ASP VAL ASN SER ALA SER LYS SER GLU SER
SEQRES 5 H 361 ASP SER GLN ILE VAL THR PRO GLY GLU LEU VAL THR ASP
SEQRES 6 H 361 ASP PRO ILE TRP MET ARG GLY HIS GLY THR TYR PHE LEU
SEQRES 7 H 361 ASP ASN MET THR TYR SER SER VAL ALA GLY THR VAL SER
SEQRES 8 H 361 ARG VAL ASN ARG LEU LEU SER VAL ILE PRO LEU LYS GLY
SEQRES 9 H 361 ARG TYR ALA PRO GLU THR GLY ASP HIS VAL VAL GLY ARG
SEQRES 10 H 361 ILE ALA GLU VAL GLY ASN LYS ARG TRP LYS VAL ASP ILE
SEQRES 11 H 361 GLY GLY LYS GLN HIS ALA VAL LEU MET LEU GLY SER VAL
SEQRES 12 H 361 ASN LEU PRO GLY GLY ILE LEU ARG ARG LYS SER GLU SER
SEQRES 13 H 361 ASP GLU LEU GLN MET ARG SER PHE LEU LYS GLU GLY ASP
SEQRES 14 H 361 LEU LEU ASN ALA GLU VAL GLN SER LEU PHE GLN ASP GLY
SEQRES 15 H 361 SER ALA SER LEU HIS THR ARG SER LEU LYS TYR GLY LYS
SEQRES 16 H 361 LEU ARG ASN GLY MET PHE CYS GLN VAL PRO SER SER LEU
SEQRES 17 H 361 ILE VAL ARG ALA LYS ASN HIS THR HIS ASN LEU PRO GLY
SEQRES 18 H 361 ASN ILE THR VAL VAL LEU GLY VAL ASN GLY TYR ILE TRP
SEQRES 19 H 361 LEU ARG LYS THR SER GLN MET ASP LEU ALA ARG ASP THR
SEQRES 20 H 361 PRO SER ALA ASN ASN SER SER SER ILE LYS SER THR GLY
SEQRES 21 H 361 PRO THR GLY ALA VAL SER LEU ASN PRO SER ILE THR ARG
SEQRES 22 H 361 LEU GLU GLU GLU SER SER TRP GLN ILE TYR SER ASP GLU
SEQRES 23 H 361 ASN ASP PRO SER ILE SER ASN ASN ILE ARG GLN ALA ILE
SEQRES 24 H 361 CYS ARG TYR ALA ASN VAL ILE LYS ALA LEU ALA PHE CYS
SEQRES 25 H 361 GLU ILE GLY ILE THR GLN GLN ARG ILE VAL SER ALA TYR
SEQRES 26 H 361 GLU ALA SER MET VAL TYR SER ASN VAL GLY GLU LEU ILE
SEQRES 27 H 361 GLU LYS ASN VAL MET GLU SER ILE GLY SER ASP ILE LEU
SEQRES 28 H 361 THR ALA GLU LYS MET ARG GLY ASN GLY ASN
SEQRES 1 I 301 MET LYS HIS HIS HIS HIS HIS HIS PRO MET ALA CYS ASN
SEQRES 2 I 301 PHE GLN PHE PRO GLU ILE ALA TYR PRO GLY LYS LEU ILE
SEQRES 3 I 301 CYS PRO GLN TYR GLY THR GLU ASN LYS ASP GLY GLU ASP
SEQRES 4 I 301 ILE ILE PHE ASN TYR VAL PRO GLY PRO GLY THR LYS LEU
SEQRES 5 I 301 ILE GLN TYR GLU HIS ASN GLY ARG THR LEU GLU ALA ILE
SEQRES 6 I 301 THR ALA THR LEU VAL GLY THR VAL ARG CYS GLU GLU GLU
SEQRES 7 I 301 LYS LYS THR ASP GLN GLU GLU GLU ARG GLU GLY THR ASP
SEQRES 8 I 301 GLN SER THR GLU GLU GLU LYS SER VAL ASP ALA SER PRO
SEQRES 9 I 301 ASN ASP VAL THR ARG ARG THR VAL LYS ASN ILE LEU VAL
SEQRES 10 I 301 SER VAL LEU PRO GLY THR GLU LYS GLY ARG LYS THR ASN
SEQRES 11 I 301 LYS TYR ALA ASN ASN ASP PHE ALA ASN ASN LEU PRO LYS
SEQRES 12 I 301 GLU GLY ASP ILE VAL LEU THR ARG VAL THR ARG LEU SER
SEQRES 13 I 301 LEU GLN ARG ALA ASN VAL GLU ILE LEU ALA VAL GLU ASP
SEQRES 14 I 301 LYS PRO SER PRO ILE ASP SER GLY ILE GLY SER ASN GLY
SEQRES 15 I 301 SER GLY ILE VAL ALA ALA GLY GLY GLY SER GLY ALA ALA
SEQRES 16 I 301 THR PHE SER VAL SER GLN ALA SER SER ASP LEU GLY GLU
SEQRES 17 I 301 THR PHE ARG GLY ILE ILE ARG SER GLN ASP VAL ARG SER
SEQRES 18 I 301 THR ASP ARG ASP ARG VAL LYS VAL ILE GLU CYS PHE LYS
SEQRES 19 I 301 PRO GLY ASP ILE VAL ARG ALA GLN VAL LEU SER LEU GLY
SEQRES 20 I 301 ASP GLY THR ASN TYR TYR LEU THR THR ALA ARG ASN ASP
SEQRES 21 I 301 LEU GLY VAL VAL PHE ALA ARG ALA ALA ASN GLY ALA GLY
SEQRES 22 I 301 GLY LEU MET TYR ALA THR ASP TRP GLN MET MET THR SER
SEQRES 23 I 301 PRO VAL THR GLY ALA THR GLU LYS ARG LYS CYS ALA LYS
SEQRES 24 I 301 PRO PHE
SEQRES 1 J 1003 GLY ALA MET SER VAL PRO ALA ILE ALA PRO ARG ARG LYS
SEQRES 2 J 1003 ARG LEU ALA ASP GLY LEU SER VAL THR GLN LYS VAL PHE
SEQRES 3 J 1003 VAL ARG SER ARG ASN GLY GLY ALA THR LYS ILE VAL ARG
SEQRES 4 J 1003 GLU HIS TYR LEU ARG SER ASP ILE PRO CYS LEU SER ARG
SEQRES 5 J 1003 SER CYS THR LYS CYS PRO GLN ILE VAL VAL PRO ASP ALA
SEQRES 6 J 1003 GLN ASN GLU LEU PRO LYS PHE ILE LEU SER ASP SER PRO
SEQRES 7 J 1003 LEU GLU LEU SER ALA PRO ILE GLY LYS HIS TYR VAL VAL
SEQRES 8 J 1003 LEU ASP THR ASN VAL VAL LEU GLN ALA ILE ASP LEU LEU
SEQRES 9 J 1003 GLU ASN PRO ASN CYS PHE PHE ASP VAL ILE VAL PRO GLN
SEQRES 10 J 1003 ILE VAL LEU ASP GLU VAL ARG ASN LYS SER TYR PRO VAL
SEQRES 11 J 1003 TYR THR ARG LEU ARG THR LEU CYS ARG ASP SER ASP ASP
SEQRES 12 J 1003 HIS LYS ARG PHE ILE VAL PHE HIS ASN GLU PHE SER GLU
SEQRES 13 J 1003 HIS THR PHE VAL GLU ARG LEU PRO ASN GLU THR ILE ASN
SEQRES 14 J 1003 ASP ARG ASN ASN ARG ALA ILE ARG LYS THR CYS GLN TRP
SEQRES 15 J 1003 TYR SER GLU HIS LEU LYS PRO TYR ASP ILE ASN VAL VAL
SEQRES 16 J 1003 LEU VAL THR ASN ASP ARG LEU ASN ARG GLU ALA ALA THR
SEQRES 17 J 1003 LYS GLU VAL GLU SER ASN ILE ILE THR LYS SER LEU VAL
SEQRES 18 J 1003 GLN TYR ILE GLU LEU LEU PRO ASN ALA ASP ASP ILE ARG
SEQRES 19 J 1003 ASP SER ILE PRO GLN MET ASP SER PHE ASP LYS ASP LEU
SEQRES 20 J 1003 GLU ARG ASP THR PHE SER ASP PHE THR PHE PRO GLU TYR
SEQRES 21 J 1003 TYR SER THR ALA ARG VAL MET GLY GLY LEU LYS ASN GLY
SEQRES 22 J 1003 VAL LEU TYR GLN GLY ASN ILE GLN ILE SER GLU TYR ASN
SEQRES 23 J 1003 PHE LEU GLU GLY SER VAL SER LEU PRO ARG PHE SER LYS
SEQRES 24 J 1003 PRO VAL LEU ILE VAL GLY GLN LYS ASN LEU ASN ARG ALA
SEQRES 25 J 1003 PHE ASN GLY ASP GLN VAL ILE VAL GLU LEU LEU PRO GLN
SEQRES 26 J 1003 SER GLU TRP LYS ALA PRO SER SER ILE VAL LEU ASP SER
SEQRES 27 J 1003 GLU HIS PHE ASP VAL ASN ASP ASN PRO ASP ILE GLU ALA
SEQRES 28 J 1003 GLY ASP ASP ASP ASP ASN ASN GLU SER SER SER ASN THR
SEQRES 29 J 1003 THR VAL ILE SER ASP LYS GLN ARG ARG LEU LEU ALA LYS
SEQRES 30 J 1003 ASP ALA MET ILE ALA GLN ARG SER LYS LYS ILE GLN PRO
SEQRES 31 J 1003 THR ALA LYS VAL VAL TYR ILE GLN ARG ARG SER TRP ARG
SEQRES 32 J 1003 GLN TYR VAL GLY GLN LEU ALA PRO SER SER VAL ASP PRO
SEQRES 33 J 1003 GLN SER SER SER THR GLN ASN VAL PHE VAL ILE LEU MET
SEQRES 34 J 1003 ASP LYS CYS LEU PRO LYS VAL ARG ILE ARG THR ARG ARG
SEQRES 35 J 1003 ALA ALA GLU LEU LEU ASP LYS ARG ILE VAL ILE SER ILE
SEQRES 36 J 1003 ASP SER TRP PRO THR THR HIS LYS TYR PRO LEU GLY HIS
SEQRES 37 J 1003 PHE VAL ARG ASP LEU GLY THR ILE GLU SER ALA GLN ALA
SEQRES 38 J 1003 GLU THR GLU ALA LEU LEU LEU GLU HIS ASP VAL GLU TYR
SEQRES 39 J 1003 ARG PRO PHE SER LYS LYS VAL LEU GLU CYS LEU PRO ALA
SEQRES 40 J 1003 GLU GLY HIS ASP TRP LYS ALA PRO THR LYS LEU ASP ASP
SEQRES 41 J 1003 PRO GLU ALA VAL SER LYS ASP PRO LEU LEU THR LYS ARG
SEQRES 42 J 1003 LYS ASP LEU ARG ASP LYS LEU ILE CYS SER ILE ASP PRO
SEQRES 43 J 1003 PRO GLY CYS VAL ASP ILE ASN ASP ALA LEU HIS ALA LYS
SEQRES 44 J 1003 LYS LEU PRO ASN GLY ASN TRP GLU VAL GLY VAL HIS ILE
SEQRES 45 J 1003 ALA ASP VAL THR HIS PHE VAL LYS PRO GLY THR ALA LEU
SEQRES 46 J 1003 ASP ALA GLU GLY ALA ALA ARG GLY THR SER VAL TYR LEU
SEQRES 47 J 1003 VAL ASP LYS ARG ILE ASP MET LEU PRO MET LEU LEU GLY
SEQRES 48 J 1003 THR ASP LEU CYS SER LEU LYS PRO TYR VAL ASP ARG PHE
SEQRES 49 J 1003 ALA PHE SER VAL ILE TRP GLU LEU ASP ASP SER ALA ASN
SEQRES 50 J 1003 ILE VAL ASN VAL ASN PHE MET LYS SER VAL ILE ARG SER
SEQRES 51 J 1003 ARG GLU ALA PHE SER TYR GLU GLN ALA GLN LEU ARG ILE
SEQRES 52 J 1003 ASP ASP LYS THR GLN ASN ASP GLU LEU THR MET GLY MET
SEQRES 53 J 1003 ARG ALA LEU LEU LYS LEU SER VAL LYS LEU LYS GLN LYS
SEQRES 54 J 1003 ARG LEU GLU ALA GLY ALA LEU ASN LEU ALA SER PRO GLU
SEQRES 55 J 1003 VAL LYS VAL HIS MET ASP SER GLU THR SER ASP PRO ASN
SEQRES 56 J 1003 GLU VAL GLU ILE LYS LYS LEU LEU ALA THR ASN SER LEU
SEQRES 57 J 1003 VAL GLU GLU PHE MET LEU LEU ALA ASN ILE SER VAL ALA
SEQRES 58 J 1003 ARG LYS ILE TYR ASP ALA PHE PRO GLN THR ALA MET LEU
SEQRES 59 J 1003 ARG ARG HIS ALA ALA PRO PRO SER THR ASN PHE GLU ILE
SEQRES 60 J 1003 LEU ASN GLU MET LEU ASN THR ARG LYS ASN MET SER ILE
SEQRES 61 J 1003 SER LEU GLU SER SER LYS ALA LEU ALA ASP SER LEU ASP
SEQRES 62 J 1003 ARG CYS VAL ASP PRO GLU ASP PRO TYR PHE ASN THR LEU
SEQRES 63 J 1003 VAL ARG ILE MET SER THR ARG CYS MET MET ALA ALA GLN
SEQRES 64 J 1003 TYR PHE TYR SER GLY ALA TYR SER TYR PRO ASP PHE ARG
SEQRES 65 J 1003 HIS TYR GLY LEU ALA VAL ASP ILE TYR THR HIS PHE THR
SEQRES 66 J 1003 SER PRO ILE ARG ARG TYR CYS ASP VAL VAL ALA HIS ARG
SEQRES 67 J 1003 GLN LEU ALA GLY ALA ILE GLY TYR GLU PRO LEU SER LEU
SEQRES 68 J 1003 THR HIS ARG ASP LYS ASN LYS MET ASP MET ILE CYS ARG
SEQRES 69 J 1003 ASN ILE ASN ARG LYS HIS ARG ASN ALA GLN PHE ALA GLY
SEQRES 70 J 1003 ARG ALA SER ILE GLU TYR TYR VAL GLY GLN VAL MET ARG
SEQRES 71 J 1003 ASN ASN GLU SER THR GLU THR GLY TYR VAL ILE LYS VAL
SEQRES 72 J 1003 PHE ASN ASN GLY ILE VAL VAL LEU VAL PRO LYS PHE GLY
SEQRES 73 J 1003 VAL GLU GLY LEU ILE ARG LEU ASP ASN LEU THR GLU ASP
SEQRES 74 J 1003 PRO ASN SER ALA ALA PHE ASP GLU VAL GLU TYR LYS LEU
SEQRES 75 J 1003 THR PHE VAL PRO THR ASN SER ASP LYS PRO ARG ASP VAL
SEQRES 76 J 1003 TYR VAL PHE ASP LYS VAL GLU VAL GLN VAL ARG SER VAL
SEQRES 77 J 1003 MET ASP PRO ILE THR SER LYS ARG LYS ALA GLU LEU LEU
SEQRES 78 J 1003 LEU LYS
SEQRES 1 K 179 ARG SER MET GLU ALA THR PRO ILE PRO SER SER GLU THR
SEQRES 2 K 179 LYS ALA ASP GLY ILE LEU LEU GLU THR ILE SER VAL PRO
SEQRES 3 K 179 GLN ILE ARG ASP VAL MET GLU ARG PHE SER VAL LEU CYS
SEQRES 4 K 179 ASN SER ASN ILE SER LYS SER ARG ALA LYS PRO VAL THR
SEQRES 5 K 179 ASN SER SER ILE LEU LEU GLY LYS ILE LEU PRO ARG GLU
SEQRES 6 K 179 GLU HIS ASP ILE ALA TYR SER LYS ASP GLY LEU PRO ASN
SEQRES 7 K 179 LYS VAL LYS THR GLU ASP ILE ARG ILE ARG ALA GLN ASN
SEQRES 8 K 179 PHE LYS SER ALA LEU ALA ASN LEU GLU ASP ILE ILE PHE
SEQRES 9 K 179 GLU ILE GLU LYS PRO LEU VAL VAL PRO VAL LYS LEU GLU
SEQRES 10 K 179 GLU ILE LYS THR VAL ASP PRO ALA SER ALA PRO ASN HIS
SEQRES 11 K 179 SER PRO GLU ILE ASP ASN LEU ASP ASP LEU VAL VAL LEU
SEQRES 12 K 179 LYS LYS LYS ASN ILE GLN LYS LYS GLN PRO ALA LYS GLU
SEQRES 13 K 179 LYS GLY VAL THR GLU LYS ASP ALA VAL ASP TYR SER LYS
SEQRES 14 K 179 ILE PRO ASN ILE LEU SER ASN LYS PRO GLY
SEQRES 1 R 45 C C C C C G A G A G G G G
SEQRES 2 R 45 G U U U U U U U U U U U U
SEQRES 3 R 45 U U U U U U U U U U U U U
SEQRES 4 R 45 U U U U U U
HET BR A 401 1
HET BR A 402 1
HET GOL C 401 6
HET BR E 301 1
HET BR F 301 1
HET GOL G 301 6
HET MES G 302 12
HET BR H 401 1
HET GOL H 402 6
HET GOL H 403 6
HET GOL H 404 6
HET BR I 301 1
HET BR J1101 1
HET BR J1102 1
HET BR J1103 1
HET BR J1104 1
HET MG J1105 1
HET ZN J1106 1
HETNAM BR BROMIDE ION
HETNAM GOL GLYCEROL
HETNAM MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID
HETNAM MG MAGNESIUM ION
HETNAM ZN ZINC ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 13 BR 10(BR 1-)
FORMUL 15 GOL 5(C3 H8 O3)
FORMUL 19 MES C6 H13 N O4 S
FORMUL 29 MG MG 2+
FORMUL 30 ZN ZN 2+
FORMUL 31 HOH *244(H2 O)
HELIX 1 1 SER A 8 GLN A 21 1 14
HELIX 2 2 SER A 84 GLY A 88 5 5
HELIX 3 3 GLY A 98 VAL A 112 1 15
HELIX 4 4 ASP A 119 GLY A 122 5 4
HELIX 5 5 GLY A 146 PHE A 162 1 17
HELIX 6 6 ASP A 205 LYS A 211 1 7
HELIX 7 7 THR A 224 LEU A 229 1 6
HELIX 8 8 ALA A 258 GLU A 300 1 43
HELIX 9 9 GLU B 94 GLU B 109 1 16
HELIX 10 10 MET B 113 TYR B 117 5 5
HELIX 11 11 GLY B 134 ALA B 150 1 17
HELIX 12 12 ASN B 175 ASN B 180 1 6
HELIX 13 13 LEU B 207 SER B 241 1 35
HELIX 14 14 PRO C 18 SER C 26 1 9
HELIX 15 15 SER C 26 SER C 36 1 11
HELIX 16 16 ILE C 123 ALA C 125 5 3
HELIX 17 17 THR C 145 SER C 162 1 18
HELIX 18 18 VAL C 226 GLN C 239 1 14
HELIX 19 19 ASP C 303 GLN C 307 5 5
HELIX 20 20 ASP C 335 ILE C 343 1 9
HELIX 21 21 THR C 370 PHE C 392 1 23
HELIX 22 22 THR D 60 ILE D 78 1 19
HELIX 23 23 THR D 79 TYR D 83 5 5
HELIX 24 24 SER D 105 GLY D 124 1 20
HELIX 25 25 THR D 150 ILE D 156 1 7
HELIX 26 26 ASN D 187 SER D 218 1 32
HELIX 27 27 SER E 4 SER E 17 1 14
HELIX 28 28 ALA E 89 LEU E 103 1 15
HELIX 29 29 ASP E 110 GLN E 115 5 6
HELIX 30 30 PRO E 137 ASN E 150 1 14
HELIX 31 31 ALA E 202 ALA E 209 1 8
HELIX 32 32 LYS E 240 GLU E 263 1 24
HELIX 33 33 ASN F 106 ASN F 122 1 17
HELIX 34 34 ASN F 126 TYR F 130 5 5
HELIX 35 35 SER F 163 SER F 167 5 5
HELIX 36 36 LEU F 168 GLY F 184 1 17
HELIX 37 37 LYS F 205 GLU F 208 5 4
HELIX 38 38 ASP F 222 GLN F 248 1 27
HELIX 39 39 ASN G 159 ASN G 169 1 11
HELIX 40 40 PRO G 173 ALA G 180 1 8
HELIX 41 41 GLU G 200 ASN G 218 1 19
HELIX 42 42 ALA G 222 THR G 236 1 15
HELIX 43 43 GLY H 139 VAL H 141 5 3
HELIX 44 44 GLY H 145 ARG H 149 5 5
HELIX 45 45 GLN H 158 PHE H 162 5 5
HELIX 46 46 PRO H 203 ILE H 207 5 5
HELIX 47 47 SER H 237 ARG H 243 1 7
HELIX 48 48 GLU H 275 GLN H 279 5 5
HELIX 49 49 SER H 290 CYS H 310 1 21
HELIX 50 50 THR H 315 SER H 326 1 12
HELIX 51 51 MET H 327 TYR H 329 5 3
HELIX 52 52 ASN H 331 ILE H 336 5 6
HELIX 53 53 GLU H 337 ASN H 357 1 21
HELIX 54 54 GLN I 208 VAL I 210 5 3
HELIX 55 55 LYS I 219 CYS I 223 5 5
HELIX 56 56 LYS J 54 ILE J 58 5 5
HELIX 57 57 ASP J 91 ALA J 98 1 8
HELIX 58 58 GLN J 115 SER J 125 1 11
HELIX 59 59 SER J 125 ASP J 138 1 14
HELIX 60 60 THR J 165 LEU J 185 1 21
HELIX 61 61 LYS J 186 TYR J 188 5 3
HELIX 62 62 ASP J 198 LYS J 207 1 10
HELIX 63 63 SER J 217 GLU J 223 1 7
HELIX 64 64 ASN J 227 ARG J 232 1 6
HELIX 65 65 ASP J 233 ILE J 235 5 3
HELIX 66 66 SER J 260 ASN J 270 1 11
HELIX 67 67 GLY J 303 ASN J 308 1 6
HELIX 68 68 PRO J 322 TRP J 326 5 5
HELIX 69 69 SER J 366 LYS J 384 1 19
HELIX 70 70 SER J 476 HIS J 488 1 13
HELIX 71 71 SER J 496 GLU J 501 1 6
HELIX 72 72 GLU J 506 TRP J 510 5 5
HELIX 73 73 ASP J 518 ASP J 525 1 8
HELIX 74 74 PRO J 526 ARG J 531 5 6
HELIX 75 75 VAL J 573 PHE J 576 5 4
HELIX 76 76 THR J 581 GLY J 591 1 11
HELIX 77 77 PRO J 605 THR J 610 1 6
HELIX 78 78 SER J 653 ASP J 663 1 11
HELIX 79 79 ASP J 668 GLY J 692 1 25
HELIX 80 80 LEU J 721 PHE J 746 1 26
HELIX 81 81 PRO J 759 ARG J 773 1 15
HELIX 82 82 SER J 782 ARG J 792 1 11
HELIX 83 83 PRO J 799 THR J 810 1 12
HELIX 84 84 SER J 825 ARG J 830 5 6
HELIX 85 85 ARG J 848 ILE J 862 1 15
HELIX 86 86 SER J 868 ARG J 872 5 5
HELIX 87 87 ASP J 873 MET J 907 1 35
HELIX 88 88 LEU J 941 THR J 945 1 5
HELIX 89 89 SER K 538 ASN K 554 1 17
HELIX 90 90 LYS K 595 ASN K 612 1 18
HELIX 91 91 LEU K 613 ASP K 615 5 3
SHEET 1 A 5 VAL A 36 PHE A 40 0
SHEET 2 A 5 ASP A 46 MET A 51 -1 O SER A 48 N THR A 39
SHEET 3 A 5 THR A 54 ALA A 65 -1 O VAL A 56 N VAL A 49
SHEET 4 A 5 LYS A 130 ASP A 142 -1 O HIS A 139 N HIS A 57
SHEET 5 A 5 LEU A 76 SER A 80 1 N SER A 80 O VAL A 138
SHEET 1 B 5 VAL A 36 PHE A 40 0
SHEET 2 B 5 ASP A 46 MET A 51 -1 O SER A 48 N THR A 39
SHEET 3 B 5 THR A 54 ALA A 65 -1 O VAL A 56 N VAL A 49
SHEET 4 B 5 LYS A 130 ASP A 142 -1 O HIS A 139 N HIS A 57
SHEET 5 B 5 CYS A 124 VAL A 126 -1 N VAL A 126 O LYS A 130
SHEET 1 C 2 LYS A 163 LYS A 164 0
SHEET 2 C 2 VAL A 185 PRO A 186 -1 O VAL A 185 N LYS A 164
SHEET 1 D 2 ILE A 167 HIS A 170 0
SHEET 2 D 2 GLN A 173 VAL A 176 -1 O ILE A 175 N THR A 168
SHEET 1 E 8 ILE A 218 ILE A 221 0
SHEET 2 E 8 ILE A 194 PHE A 201 -1 N PHE A 201 O ILE A 218
SHEET 3 E 8 GLY A 233 ASN A 240 -1 O LEU A 235 N PHE A 198
SHEET 4 E 8 GLU A 244 LYS A 250 -1 O GLN A 247 N THR A 238
SHEET 5 E 8 LYS B 195 VAL B 201 -1 O VAL B 201 N VAL A 248
SHEET 6 E 8 SER B 183 VAL B 190 -1 N GLY B 188 O SER B 197
SHEET 7 E 8 ILE B 158 TYR B 166 -1 N ILE B 161 O LEU B 187
SHEET 8 E 8 THR B 169 LEU B 172 -1 O THR B 169 N TYR B 166
SHEET 1 F 4 MET A 256 ASP A 257 0
SHEET 2 F 4 LYS B 195 VAL B 201 -1 O LEU B 196 N MET A 256
SHEET 3 F 4 GLU A 244 LYS A 250 -1 N VAL A 248 O VAL B 201
SHEET 4 F 4 ILE B 205 PRO B 206 -1 O ILE B 205 N VAL A 245
SHEET 1 G 5 PHE B 25 GLU B 26 0
SHEET 2 G 5 GLY B 38 GLN B 44 -1 O GLU B 43 N GLU B 26
SHEET 3 G 5 ASN B 47 LYS B 57 -1 O VAL B 53 N GLY B 38
SHEET 4 G 5 VAL B 121 GLU B 130 -1 O GLU B 125 N LEU B 52
SHEET 5 G 5 LEU B 71 ILE B 78 1 N LEU B 71 O ILE B 122
SHEET 1 H 2 ILE C 10 ILE C 12 0
SHEET 2 H 2 ILE K 617 GLU K 619 -1 O ILE K 617 N ILE C 12
SHEET 1 I 3 GLU C 48 ARG C 50 0
SHEET 2 I 3 ASP K 582 TYR K 585 -1 O ILE K 583 N PHE C 49
SHEET 3 I 3 PRO K 591 VAL K 594 -1 O VAL K 594 N ASP K 582
SHEET 1 J 5 ALA C 53 ASN C 56 0
SHEET 2 J 5 GLY C 76 SER C 82 -1 O LYS C 81 N ALA C 53
SHEET 3 J 5 THR C 85 GLU C 98 -1 O ILE C 91 N GLY C 76
SHEET 4 J 5 LYS C 208 LEU C 220 -1 O LYS C 208 N GLU C 98
SHEET 5 J 5 LYS C 171 VAL C 172 -1 N VAL C 172 O TRP C 209
SHEET 1 K 4 TYR C 131 VAL C 136 0
SHEET 2 K 4 LYS C 208 LEU C 220 1 O VAL C 219 N GLU C 135
SHEET 3 K 4 THR C 85 GLU C 98 -1 N GLU C 98 O LYS C 208
SHEET 4 K 4 LYS F 16 PRO F 17 -1 O LYS F 16 N ILE C 95
SHEET 1 L 2 TYR C 127 ALA C 128 0
SHEET 2 L 2 LEU C 165 PRO C 166 -1 O LEU C 165 N ALA C 128
SHEET 1 M 4 THR C 184 LEU C 188 0
SHEET 2 M 4 GLY C 175 ASN C 180 -1 N VAL C 176 O LEU C 188
SHEET 3 M 4 LYS C 242 ASP C 249 1 O ILE C 248 N ARG C 177
SHEET 4 M 4 ILE C 275 PRO C 283 -1 O ASP C 277 N ARG C 245
SHEET 1 N 2 MET C 257 ARG C 260 0
SHEET 2 N 2 SER C 265 ILE C 268 -1 O ALA C 266 N ILE C 259
SHEET 1 O 8 THR C 328 ALA C 332 0
SHEET 2 O 8 PHE C 293 GLU C 301 -1 N GLY C 298 O ILE C 331
SHEET 3 O 8 SER C 345 ALA C 351 -1 O ILE C 347 N TYR C 297
SHEET 4 O 8 TYR C 357 GLY C 364 -1 O LYS C 358 N LEU C 350
SHEET 5 O 8 VAL D 173 PHE D 186 -1 O PHE D 186 N TYR C 357
SHEET 6 O 8 SER D 157 VAL D 168 -1 N GLU D 166 O ASN D 176
SHEET 7 O 8 MET D 130 ILE D 139 -1 N ILE D 138 O LEU D 158
SHEET 8 O 8 ILE D 145 VAL D 147 -1 O ILE D 146 N ALA D 137
SHEET 1 P 5 GLN D 4 ILE D 7 0
SHEET 2 P 5 GLY D 15 SER D 21 -1 O VAL D 20 N GLN D 4
SHEET 3 P 5 THR D 24 ILE D 34 -1 O VAL D 30 N GLY D 15
SHEET 4 P 5 GLN D 86 GLU D 96 -1 O GLN D 93 N ILE D 27
SHEET 5 P 5 LEU D 46 ARG D 53 1 N GLU D 49 O ILE D 90
SHEET 1 Q 6 LEU E 76 ILE E 82 0
SHEET 2 Q 6 TYR E 120 SER E 132 1 O VAL E 128 N ASP E 79
SHEET 3 Q 6 GLU E 57 ASP E 68 -1 N LYS E 65 O LYS E 123
SHEET 4 Q 6 GLY E 46 ILE E 51 -1 N GLY E 46 O ILE E 62
SHEET 5 Q 6 ILE E 34 THR E 38 -1 N GLU E 35 O ILE E 51
SHEET 6 Q 6 ILE H 7 ASN H 11 1 O THR H 8 N ILE E 36
SHEET 1 R 2 TYR E 153 LEU E 157 0
SHEET 2 R 2 PHE E 172 LYS E 179 -1 O HIS E 173 N LYS E 156
SHEET 1 S 7 ASN E 196 LEU E 199 0
SHEET 2 S 7 LEU E 186 VAL E 193 -1 N ALA E 191 O LEU E 198
SHEET 3 S 7 ASN E 211 SER E 218 -1 O ASN E 211 N VAL E 192
SHEET 4 S 7 LYS E 221 SER E 228 -1 O ARG E 227 N ILE E 214
SHEET 5 S 7 GLU F 209 LYS F 215 -1 O PHE F 213 N SER E 228
SHEET 6 S 7 THR F 199 ILE F 204 -1 N VAL F 200 O TRP F 214
SHEET 7 S 7 GLY F 192 ALA F 196 -1 N ALA F 196 O THR F 199
SHEET 1 T 5 GLU F 45 THR F 50 0
SHEET 2 T 5 GLY F 58 SER F 66 -1 O LEU F 61 N HIS F 49
SHEET 3 T 5 HIS F 69 SER F 82 -1 O VAL F 77 N GLY F 58
SHEET 4 T 5 SER F 133 ASP F 146 -1 O TYR F 140 N ILE F 74
SHEET 5 T 5 THR F 92 ASN F 99 1 N SER F 94 O ILE F 137
SHEET 1 U 4 PHE G 4 ILE G 5 0
SHEET 2 U 4 GLY G 40 VAL G 44 -1 O GLY G 40 N ILE G 5
SHEET 3 U 4 GLN G 53 TYR G 59 -1 O TYR G 56 N HIS G 43
SHEET 4 U 4 VAL G 19 LEU G 21 1 N LYS G 20 O GLN G 53
SHEET 1 V 2 ILE G 25 CYS G 27 0
SHEET 2 V 2 ILE G 34 PRO G 36 -1 O ARG G 35 N TYR G 26
SHEET 1 W 7 GLY G 148 ILE G 149 0
SHEET 2 W 7 LEU G 118 THR G 125 -1 N TYR G 120 O GLY G 148
SHEET 3 W 7 GLU G 133 GLU G 135 -1 O GLU G 133 N THR G 125
SHEET 4 W 7 VAL G 95 SER G 98 1 N SER G 96 O ILE G 134
SHEET 5 W 7 SER G 83 SER G 87 -1 N TYR G 84 O LEU G 97
SHEET 6 W 7 PHE G 71 THR G 79 -1 N ILE G 77 O LYS G 85
SHEET 7 W 7 LEU G 118 THR G 125 -1 O VAL G 119 N GLY G 74
SHEET 1 X 3 MET G 154 ASP G 157 0
SHEET 2 X 3 LYS G 193 LYS G 197 -1 O VAL G 196 N MET G 154
SHEET 3 X 3 GLU G 185 GLY G 189 -1 N GLY G 189 O LYS G 193
SHEET 1 Y 4 ILE H 54 VAL H 55 0
SHEET 2 Y 4 GLY H 86 VAL H 91 -1 O GLY H 86 N VAL H 55
SHEET 3 Y 4 LEU H 94 PRO H 99 -1 O SER H 96 N SER H 89
SHEET 4 Y 4 MET H 68 ARG H 69 1 N MET H 68 O LEU H 95
SHEET 1 Z 3 LEU H 60 THR H 62 0
SHEET 2 Z 3 MET H 79 SER H 82 -1 O THR H 80 N VAL H 61
SHEET 3 Z 3 THR H 73 LEU H 76 -1 N TYR H 74 O TYR H 81
SHEET 1 AA 7 GLY H 192 LYS H 193 0
SHEET 2 AA 7 LEU H 168 LEU H 176 -1 N ASN H 170 O GLY H 192
SHEET 3 AA 7 ALA H 182 HIS H 185 -1 O SER H 183 N SER H 175
SHEET 4 AA 7 ALA H 134 MET H 137 1 N VAL H 135 O LEU H 184
SHEET 5 AA 7 ARG H 123 ASP H 127 -1 N TRP H 124 O LEU H 136
SHEET 6 AA 7 HIS H 111 GLY H 120 -1 N ARG H 115 O ASP H 127
SHEET 7 AA 7 LEU H 168 LEU H 176 -1 O ALA H 171 N VAL H 112
SHEET 1 AB 4 GLY H 197 GLN H 201 0
SHEET 2 AB 4 TYR H 230 LYS H 235 -1 O LEU H 233 N MET H 198
SHEET 3 AB 4 ILE H 221 LEU H 225 -1 N THR H 222 O ARG H 234
SHEET 4 AB 4 THR H 214 LEU H 217 -1 N LEU H 217 O ILE H 221
SHEET 1 AC 5 ILE I 10 ALA I 11 0
SHEET 2 AC 5 GLY I 62 GLU I 68 -1 O GLY I 62 N ALA I 11
SHEET 3 AC 5 VAL I 103 LEU I 111 -1 O LEU I 107 N GLU I 67
SHEET 4 AC 5 GLU I 29 PRO I 37 1 N ILE I 32 O LYS I 104
SHEET 5 AC 5 TYR I 21 LYS I 26 -1 N GLY I 22 O PHE I 33
SHEET 1 AD 3 LEU I 16 PRO I 19 0
SHEET 2 AD 3 ARG I 51 ALA I 58 -1 O ILE I 56 N CYS I 18
SHEET 3 AD 3 THR I 41 HIS I 48 -1 N TYR I 46 O LEU I 53
SHEET 1 AE 8 PHE I 188 VAL I 190 0
SHEET 2 AE 8 ARG I 150 GLU I 159 -1 N VAL I 158 O SER I 189
SHEET 3 AE 8 ILE I 138 LEU I 146 -1 N ILE I 138 O GLU I 159
SHEET 4 AE 8 ILE I 229 SER I 236 -1 O ALA I 232 N VAL I 139
SHEET 5 AE 8 GLY I 253 ARG I 258 -1 O VAL I 255 N ILE I 229
SHEET 6 AE 8 LEU I 266 ALA I 269 -1 O MET I 267 N ALA I 257
SHEET 7 AE 8 MET I 274 THR I 276 -1 O THR I 276 N TYR I 268
SHEET 8 AE 8 THR I 283 LYS I 285 -1 O GLU I 284 N MET I 275
SHEET 1 AF 9 PHE I 188 VAL I 190 0
SHEET 2 AF 9 ARG I 150 GLU I 159 -1 N VAL I 158 O SER I 189
SHEET 3 AF 9 ARG I 202 ARG I 206 -1 O GLY I 203 N VAL I 153
SHEET 4 AF 9 ASN I 242 THR I 246 1 O TYR I 243 N ARG I 202
SHEET 5 AF 9 ILE I 229 SER I 236 -1 N LEU I 235 O TYR I 244
SHEET 6 AF 9 GLY I 253 ARG I 258 -1 O VAL I 255 N ILE I 229
SHEET 7 AF 9 LEU I 266 ALA I 269 -1 O MET I 267 N ALA I 257
SHEET 8 AF 9 MET I 274 THR I 276 -1 O THR I 276 N TYR I 268
SHEET 9 AF 9 THR I 283 LYS I 285 -1 O GLU I 284 N MET I 275
SHEET 1 AG 3 LYS J 11 ARG J 12 0
SHEET 2 AG 3 SER J 18 ARG J 28 -1 O VAL J 19 N LYS J 11
SHEET 3 AG 3 GLY J 31 LEU J 41 -1 O HIS J 39 N THR J 20
SHEET 1 AH 4 GLU J 78 LEU J 79 0
SHEET 2 AH 4 GLY J 84 LEU J 90 -1 O GLY J 84 N LEU J 79
SHEET 3 AH 4 ASP J 110 PRO J 114 1 O ILE J 112 N VAL J 88
SHEET 4 AH 4 ARG J 144 PHE J 148 1 O ARG J 144 N VAL J 111
SHEET 1 AI 4 GLU J 78 LEU J 79 0
SHEET 2 AI 4 GLY J 84 LEU J 90 -1 O GLY J 84 N LEU J 79
SHEET 3 AI 4 ILE J 190 VAL J 195 -1 O VAL J 193 N TYR J 87
SHEET 4 AI 4 ILE J 214 LYS J 216 1 O ILE J 214 N LEU J 194
SHEET 1 AJ 5 VAL J 299 VAL J 302 0
SHEET 2 AJ 5 GLU J 287 VAL J 290 -1 N GLY J 288 O ILE J 301
SHEET 3 AJ 5 TYR J 274 ILE J 280 -1 N GLN J 279 O SER J 289
SHEET 4 AJ 5 GLN J 315 LEU J 320 -1 O VAL J 318 N TYR J 274
SHEET 5 AJ 5 ALA J 390 ARG J 397 -1 O VAL J 393 N ILE J 317
SHEET 1 AK 6 GLN J 402 LEU J 407 0
SHEET 2 AK 6 GLN J 420 LEU J 426 -1 O ILE J 425 N GLN J 406
SHEET 3 AK 6 VAL J 434 THR J 438 -1 O ILE J 436 N VAL J 422
SHEET 4 AK 6 LEU J 464 THR J 473 1 O GLY J 465 N ARG J 435
SHEET 5 AK 6 LYS J 447 SER J 455 -1 N SER J 455 O LEU J 464
SHEET 6 AK 6 GLN J 402 LEU J 407 -1 N GLY J 405 O ILE J 449
SHEET 1 AL 7 LYS J 532 ASP J 533 0
SHEET 2 AL 7 ILE J 636 PHE J 652 1 O LYS J 643 N LYS J 532
SHEET 3 AL 7 ASP J 620 LEU J 630 -1 N ALA J 623 O SER J 644
SHEET 4 AL 7 TRP J 564 ALA J 571 -1 N TRP J 564 O LEU J 630
SHEET 5 AL 7 ASP J 552 LYS J 558 -1 N LYS J 557 O GLU J 565
SHEET 6 AL 7 ILE J 539 ILE J 542 -1 N CYS J 540 O LEU J 554
SHEET 7 AL 7 ILE J 636 PHE J 652 1 O ARG J 649 N ILE J 539
SHEET 1 AM 2 VAL J 594 TYR J 595 0
SHEET 2 AM 2 ARG J 600 ILE J 601 -1 O ILE J 601 N VAL J 594
SHEET 1 AN 2 VAL J 701 MET J 705 0
SHEET 2 AN 2 PRO J 712 ILE J 717 -1 O GLU J 716 N LYS J 702
SHEET 1 AO 2 MET J 751 ARG J 754 0
SHEET 2 AO 2 GLN J 817 TYR J 820 -1 O PHE J 819 N LEU J 752
SHEET 1 AP 5 VAL J 935 ARG J 940 0
SHEET 2 AP 5 GLY J 925 VAL J 930 -1 N ILE J 926 O ILE J 939
SHEET 3 AP 5 THR J 913 VAL J 921 -1 N TYR J 917 O LEU J 929
SHEET 4 AP 5 LYS J 978 GLN J 982 -1 O VAL J 981 N GLU J 914
SHEET 5 AP 5 LEU J 999 LEU J1000 -1 O LEU J 999 N GLN J 982
SHEET 1 AQ 3 ALA J 952 ASP J 954 0
SHEET 2 AQ 3 LYS J 959 PHE J 962 -1 O LYS J 959 N ASP J 954
SHEET 3 AQ 3 ARG J 971 VAL J 973 -1 O ARG J 971 N PHE J 962
SHEET 1 AR 2 SER J 985 MET J 987 0
SHEET 2 AR 2 ARG J 994 ALA J 996 -1 O LYS J 995 N VAL J 986
SSBOND 1 CYS I 3 CYS I 66 1555 1555 2.03
LINK SG CYS J 47 ZN ZN J1106 1555 1555 2.33
LINK SG CYS J 52 ZN ZN J1106 1555 1555 2.29
LINK SG CYS J 55 ZN ZN J1106 1555 1555 2.27
LINK NE2 HIS J 184 ZN ZN J1106 1555 1555 2.03
LINK OD1 ASP J 543 MG MG J1105 1555 1555 2.14
LINK OD1 ASP J 552 MG MG J1105 1555 1555 2.12
LINK OD2 ASP J 552 MG MG J1105 1555 1555 2.21
LINK MG MG J1105 O3' U R -2 1555 1555 2.10
LINK MG MG J1105 OP1 U R -1 1555 1555 2.42
CISPEP 1 GLY B 55 PRO B 56 0 -0.38
CISPEP 2 GLY D 32 PRO D 33 0 -0.61
CISPEP 3 SER E 224 PRO E 225 0 0.80
CISPEP 4 GLY F 79 PRO F 80 0 -0.40
CISPEP 5 ALA J 81 PRO J 82 0 -0.03
SITE 1 AC1 1 THR A 224
SITE 1 AC2 4 ARG A 71 PRO A 72 PHE A 73 GLU A 74
SITE 1 AC3 4 ILE C 54 GLU C 55 ASN C 56 PHE C 392
SITE 1 AC4 1 TRP E 217
SITE 1 AC5 1 GLY F 11
SITE 1 AC6 4 ASP A 26 ARG G 209 GLN G 230 GLU G 233
SITE 1 AC7 7 ASP G 152 GLY G 153 LYS G 197 CYS G 198
SITE 2 AC7 7 GLU G 199 LEU G 201 THR G 204
SITE 1 AC8 2 LYS H 131 GLN H 132
SITE 1 AC9 6 TYR H 104 ALA H 105 SER H 204 ILE H 207
SITE 2 AC9 6 ARG H 209 VAL H 227
SITE 1 BC1 4 ARG H 115 ASP H 127 GLN H 201 TYR H 230
SITE 1 BC2 5 MET B 113 HIS H 71 GLY H 72 THR H 73
SITE 2 BC2 5 SER H 83
SITE 1 BC3 3 SER I 212 ALA I 248 ARG I 249
SITE 1 BC4 2 PRO J 293 ARG J 294
SITE 1 BC5 1 MET J 606
SITE 1 BC6 1 ARG J 137
SITE 1 BC7 1 TYR J 618
SITE 1 BC8 4 ASP J 543 ASP J 552 U R -1 U R -2
SITE 1 BC9 4 CYS J 47 CYS J 52 CYS J 55 HIS J 184
CRYST1 154.090 107.440 150.460 90.00 110.63 90.00 P 1 21 1 2
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 0.006490 0.000000 0.002443 0.00000
SCALE2 0.000000 0.009308 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007102 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
