HEADER TRANSCRIPTION 10-NOV-17 6BLO
TITLE POL II ELONGATION COMPLEX WITH AN ABASIC LESION AT I+1 POSITION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: RNA POLYMERASE II SUBUNIT B1,DNA-DIRECTED RNA POLYMERASE III
COMPND 5 LARGEST SUBUNIT,RNA POLYMERASE II SUBUNIT B220;
COMPND 6 EC: 2.7.7.6;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB2;
COMPND 10 CHAIN: B;
COMPND 11 SYNONYM: RNA POLYMERASE II SUBUNIT 2,B150,DNA-DIRECTED RNA POLYMERASE
COMPND 12 II 140 KDA POLYPEPTIDE;
COMPND 13 EC: 2.7.7.6;
COMPND 14 ENGINEERED: YES;
COMPND 15 MOL_ID: 3;
COMPND 16 MOLECULE: DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB3;
COMPND 17 CHAIN: C;
COMPND 18 SYNONYM: RNA POLYMERASE II SUBUNIT B3,B44.5,DNA-DIRECTED RNA
COMPND 19 POLYMERASE II 45 KDA POLYPEPTIDE;
COMPND 20 ENGINEERED: YES;
COMPND 21 MOL_ID: 4;
COMPND 22 MOLECULE: DNA-DIRECTED RNA POLYMERASES I, II, AND III SUBUNIT RPABC1;
COMPND 23 CHAIN: E;
COMPND 24 SYNONYM: RNA POLYMERASES I,II,AND III SUBUNIT ABC1,ABC27,DNA-DIRECTED
COMPND 25 RNA POLYMERASES I,AND III 27 KDA POLYPEPTIDE;
COMPND 26 ENGINEERED: YES;
COMPND 27 MOL_ID: 5;
COMPND 28 MOLECULE: DNA-DIRECTED RNA POLYMERASES I, II, AND III SUBUNIT RPABC2;
COMPND 29 CHAIN: F;
COMPND 30 SYNONYM: RNA POLYMERASES I,II,AND III SUBUNIT ABC2,ABC23,DNA-DIRECTED
COMPND 31 RNA POLYMERASES I,AND III 23 KDA POLYPEPTIDE;
COMPND 32 ENGINEERED: YES;
COMPND 33 MOL_ID: 6;
COMPND 34 MOLECULE: DNA-DIRECTED RNA POLYMERASES I, II, AND III SUBUNIT RPABC3;
COMPND 35 CHAIN: H;
COMPND 36 SYNONYM: RNA POLYMERASES I,II,AND III SUBUNIT ABC3,ABC14.4,ABC14.5,
COMPND 37 DNA-DIRECTED RNA POLYMERASES I,AND III 14.5 KDA POLYPEPTIDE;
COMPND 38 ENGINEERED: YES;
COMPND 39 MOL_ID: 7;
COMPND 40 MOLECULE: DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB9;
COMPND 41 CHAIN: I;
COMPND 42 SYNONYM: RNA POLYMERASE II SUBUNIT B9,B12.6,DNA-DIRECTED RNA
COMPND 43 POLYMERASE II 14.2 KDA POLYPEPTIDE,DNA-DIRECTED RNA POLYMERASE II
COMPND 44 SUBUNIT 9;
COMPND 45 ENGINEERED: YES;
COMPND 46 MOL_ID: 8;
COMPND 47 MOLECULE: DNA-DIRECTED RNA POLYMERASES I, II, AND III SUBUNIT RPABC5;
COMPND 48 CHAIN: J;
COMPND 49 SYNONYM: RNA POLYMERASES I,II,AND III SUBUNIT ABC5,ABC10-BETA,ABC8,
COMPND 50 DNA-DIRECTED RNA POLYMERASES I,AND III 8.3 KDA POLYPEPTIDE;
COMPND 51 ENGINEERED: YES;
COMPND 52 MOL_ID: 9;
COMPND 53 MOLECULE: DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB11;
COMPND 54 CHAIN: K;
COMPND 55 SYNONYM: RNA POLYMERASE II SUBUNIT B11,B13.6,DNA-DIRECTED RNA
COMPND 56 POLYMERASE II 13.6 KDA POLYPEPTIDE;
COMPND 57 ENGINEERED: YES;
COMPND 58 MOL_ID: 10;
COMPND 59 MOLECULE: DNA-DIRECTED RNA POLYMERASES I, II, AND III SUBUNIT RPABC4;
COMPND 60 CHAIN: L;
COMPND 61 SYNONYM: RNA POLYMERASES I,II,AND III SUBUNIT ABC4,ABC10-ALPHA;
COMPND 62 ENGINEERED: YES;
COMPND 63 MOL_ID: 11;
COMPND 64 MOLECULE: DNA (5'-D(P*AP*(3DR)P*CP*TP*CP*TP*CP*GP*AP*TP*G)-3');
COMPND 65 CHAIN: T;
COMPND 66 ENGINEERED: YES;
COMPND 67 MOL_ID: 12;
COMPND 68 MOLECULE: RNA (5'-R(P*AP*UP*CP*GP*AP*GP*AP*G)-3');
COMPND 69 CHAIN: R;
COMPND 70 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 3 S288C);
SOURCE 4 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 5 ORGANISM_TAXID: 559292;
SOURCE 6 STRAIN: ATCC 204508 / S288C;
SOURCE 7 GENE: RPO21, RPB1, RPB220, SUA8, YDL140C, D2150;
SOURCE 8 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 4932;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 12 S288C);
SOURCE 13 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 14 ORGANISM_TAXID: 559292;
SOURCE 15 STRAIN: ATCC 204508 / S288C;
SOURCE 16 GENE: RPB2, RPB150, RPO22, YOR151C;
SOURCE 17 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;
SOURCE 18 EXPRESSION_SYSTEM_TAXID: 4932;
SOURCE 19 MOL_ID: 3;
SOURCE 20 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 21 S288C);
SOURCE 22 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 23 ORGANISM_TAXID: 559292;
SOURCE 24 STRAIN: ATCC 204508 / S288C;
SOURCE 25 GENE: RPB3, YIL021W;
SOURCE 26 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;
SOURCE 27 EXPRESSION_SYSTEM_TAXID: 4932;
SOURCE 28 MOL_ID: 4;
SOURCE 29 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 30 S288C);
SOURCE 31 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 32 ORGANISM_TAXID: 559292;
SOURCE 33 STRAIN: ATCC 204508 / S288C;
SOURCE 34 GENE: RPB5, RPA7, RPC9, YBR154C, YBR1204;
SOURCE 35 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;
SOURCE 36 EXPRESSION_SYSTEM_TAXID: 4932;
SOURCE 37 MOL_ID: 5;
SOURCE 38 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 39 S288C);
SOURCE 40 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 41 ORGANISM_TAXID: 559292;
SOURCE 42 STRAIN: ATCC 204508 / S288C;
SOURCE 43 GENE: RPO26, RPB6, YPR187W, P9677.8;
SOURCE 44 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;
SOURCE 45 EXPRESSION_SYSTEM_TAXID: 4932;
SOURCE 46 MOL_ID: 6;
SOURCE 47 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 48 S288C);
SOURCE 49 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 50 ORGANISM_TAXID: 559292;
SOURCE 51 STRAIN: ATCC 204508 / S288C;
SOURCE 52 GENE: RPB8, YOR224C, YOR50-14;
SOURCE 53 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;
SOURCE 54 EXPRESSION_SYSTEM_TAXID: 4932;
SOURCE 55 MOL_ID: 7;
SOURCE 56 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 57 S288C);
SOURCE 58 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 59 ORGANISM_TAXID: 559292;
SOURCE 60 STRAIN: ATCC 204508 / S288C;
SOURCE 61 GENE: RPB9, YGL070C;
SOURCE 62 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;
SOURCE 63 EXPRESSION_SYSTEM_TAXID: 4932;
SOURCE 64 MOL_ID: 8;
SOURCE 65 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 66 S288C);
SOURCE 67 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 68 ORGANISM_TAXID: 559292;
SOURCE 69 STRAIN: ATCC 204508 / S288C;
SOURCE 70 GENE: RPB10, YOR210W;
SOURCE 71 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;
SOURCE 72 EXPRESSION_SYSTEM_TAXID: 4932;
SOURCE 73 MOL_ID: 9;
SOURCE 74 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 75 S288C);
SOURCE 76 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 77 ORGANISM_TAXID: 559292;
SOURCE 78 STRAIN: ATCC 204508 / S288C;
SOURCE 79 GENE: RPB11, YOL005C;
SOURCE 80 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;
SOURCE 81 EXPRESSION_SYSTEM_TAXID: 4932;
SOURCE 82 MOL_ID: 10;
SOURCE 83 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 84 S288C);
SOURCE 85 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 86 ORGANISM_TAXID: 559292;
SOURCE 87 STRAIN: ATCC 204508 / S288C;
SOURCE 88 GENE: RPC10, RPB12, YHR143W-A, YHR143BW;
SOURCE 89 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;
SOURCE 90 EXPRESSION_SYSTEM_TAXID: 4932;
SOURCE 91 MOL_ID: 11;
SOURCE 92 SYNTHETIC: YES;
SOURCE 93 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 94 ORGANISM_TAXID: 32630;
SOURCE 95 MOL_ID: 12;
SOURCE 96 SYNTHETIC: YES;
SOURCE 97 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 98 ORGANISM_TAXID: 32630
KEYWDS COMPLEX, DNA BINDING PROTEIN, DNA-RNA HYBRID, TRANSCRIPTION
EXPDTA X-RAY DIFFRACTION
AUTHOR W.WANG,D.WANG
REVDAT 5 13-MAR-24 6BLO 1 LINK
REVDAT 4 01-JAN-20 6BLO 1 REMARK
REVDAT 3 21-MAR-18 6BLO 1 JRNL
REVDAT 2 14-MAR-18 6BLO 1 JRNL
REVDAT 1 28-FEB-18 6BLO 0
JRNL AUTH W.WANG,C.WALMACQ,J.CHONG,M.KASHLEV,D.WANG
JRNL TITL STRUCTURAL BASIS OF TRANSCRIPTIONAL STALLING AND BYPASS OF
JRNL TITL 2 ABASIC DNA LESION BY RNA POLYMERASE II.
JRNL REF PROC. NATL. ACAD. SCI. V. 115 E2538 2018
JRNL REF 2 U.S.A.
JRNL REFN ESSN 1091-6490
JRNL PMID 29487211
JRNL DOI 10.1073/PNAS.1722050115
REMARK 2
REMARK 2 RESOLUTION. 3.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.8.4_1496
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 63.48
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 86.6
REMARK 3 NUMBER OF REFLECTIONS : 83193
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.204
REMARK 3 R VALUE (WORKING SET) : 0.203
REMARK 3 FREE R VALUE : 0.227
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.850
REMARK 3 FREE R VALUE TEST SET COUNT : 4034
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 63.4947 - 10.4337 0.99 3195 168 0.1928 0.2067
REMARK 3 2 10.4337 - 8.2874 1.00 3162 175 0.1419 0.1584
REMARK 3 3 8.2874 - 7.2415 1.00 3166 153 0.1651 0.1667
REMARK 3 4 7.2415 - 6.5801 1.00 3171 151 0.1945 0.2575
REMARK 3 5 6.5801 - 6.1089 1.00 3161 155 0.2069 0.2039
REMARK 3 6 6.1089 - 5.7490 1.00 3136 179 0.1959 0.2358
REMARK 3 7 5.7490 - 5.4612 1.00 3140 173 0.1947 0.2266
REMARK 3 8 5.4612 - 5.2236 1.00 3123 192 0.1882 0.2390
REMARK 3 9 5.2236 - 5.0226 1.00 3138 165 0.1773 0.2278
REMARK 3 10 5.0226 - 4.8494 1.00 3165 140 0.1799 0.2149
REMARK 3 11 4.8494 - 4.6978 1.00 3178 157 0.1766 0.2081
REMARK 3 12 4.6978 - 4.5635 1.00 3164 154 0.1721 0.1968
REMARK 3 13 4.5635 - 4.4434 1.00 3149 143 0.1796 0.2057
REMARK 3 14 4.4434 - 4.3350 1.00 3135 162 0.1861 0.2174
REMARK 3 15 4.3350 - 4.2365 1.00 3126 174 0.1939 0.2173
REMARK 3 16 4.2365 - 4.1464 1.00 3186 159 0.2125 0.2386
REMARK 3 17 4.1464 - 4.0634 1.00 3160 136 0.2224 0.2725
REMARK 3 18 4.0634 - 3.9868 1.00 3118 155 0.2329 0.2365
REMARK 3 19 3.9868 - 3.9156 1.00 3150 166 0.2533 0.2463
REMARK 3 20 3.9156 - 3.8492 0.95 3015 144 0.2613 0.2937
REMARK 3 21 3.8492 - 3.7871 0.88 2774 138 0.2575 0.2832
REMARK 3 22 3.7871 - 3.7289 0.81 2532 139 0.2606 0.2777
REMARK 3 23 3.7289 - 3.6740 0.75 2338 113 0.2592 0.2765
REMARK 3 24 3.6740 - 3.6223 0.67 2125 109 0.2683 0.3294
REMARK 3 25 3.6223 - 3.5734 0.59 1825 103 0.2760 0.2746
REMARK 3 26 3.5734 - 3.5269 0.52 1655 74 0.2792 0.2908
REMARK 3 27 3.5269 - 3.4829 0.44 1355 84 0.2924 0.2802
REMARK 3 28 3.4829 - 3.4409 0.33 1044 50 0.2946 0.3267
REMARK 3 29 3.4409 - 3.4009 0.18 573 23 0.3007 0.2907
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.320
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.580
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) : 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 : 0.002 28771
REMARK 3 ANGLE : 0.575 38929
REMARK 3 CHIRALITY : 0.023 4377
REMARK 3 PLANARITY : 0.002 4972
REMARK 3 DIHEDRAL : 11.925 10971
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 52
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 3 THROUGH 394 )
REMARK 3 ORIGIN FOR THE GROUP (A): 359.6615 3.5691 57.8237
REMARK 3 T TENSOR
REMARK 3 T11: 0.3801 T22: 0.9042
REMARK 3 T33: 1.1988 T12: 0.1879
REMARK 3 T13: -0.0337 T23: -0.0421
REMARK 3 L TENSOR
REMARK 3 L11: 1.1294 L22: 0.7236
REMARK 3 L33: 0.8354 L12: -0.1182
REMARK 3 L13: 0.2041 L23: -0.0264
REMARK 3 S TENSOR
REMARK 3 S11: 0.0325 S12: -0.1797 S13: 0.5159
REMARK 3 S21: 0.0371 S22: -0.0299 S23: 0.7806
REMARK 3 S31: -0.2405 S32: -0.7982 S33: -0.0548
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 395 THROUGH 889 )
REMARK 3 ORIGIN FOR THE GROUP (A): 402.5771 -18.2072 42.2353
REMARK 3 T TENSOR
REMARK 3 T11: 0.3369 T22: 0.2055
REMARK 3 T33: 0.2593 T12: 0.0480
REMARK 3 T13: -0.0634 T23: -0.0555
REMARK 3 L TENSOR
REMARK 3 L11: 0.3911 L22: 0.7387
REMARK 3 L33: 0.7634 L12: 0.0580
REMARK 3 L13: 0.1180 L23: -0.0356
REMARK 3 S TENSOR
REMARK 3 S11: 0.1343 S12: 0.0208 S13: -0.0850
REMARK 3 S21: -0.2610 S22: 0.0233 S23: 0.0948
REMARK 3 S31: 0.3352 S32: 0.0371 S33: -0.0576
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 890 THROUGH 1115 )
REMARK 3 ORIGIN FOR THE GROUP (A): 386.0544 -43.9638 30.2098
REMARK 3 T TENSOR
REMARK 3 T11: 0.9369 T22: 0.2147
REMARK 3 T33: 0.5541 T12: -0.1281
REMARK 3 T13: -0.3806 T23: -0.0216
REMARK 3 L TENSOR
REMARK 3 L11: 0.7337 L22: 1.1003
REMARK 3 L33: 0.7320 L12: 0.2859
REMARK 3 L13: 0.0455 L23: 0.8076
REMARK 3 S TENSOR
REMARK 3 S11: -0.0276 S12: 0.1638 S13: -0.1578
REMARK 3 S21: -0.1798 S22: 0.3233 S23: 0.0486
REMARK 3 S31: 0.5719 S32: 0.0034 S33: 0.0215
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1116 THROUGH 1280 )
REMARK 3 ORIGIN FOR THE GROUP (A): 377.0342 5.5747 -9.9525
REMARK 3 T TENSOR
REMARK 3 T11: 1.3465 T22: 0.3650
REMARK 3 T33: 0.6432 T12: -0.0849
REMARK 3 T13: -0.3243 T23: 0.1696
REMARK 3 L TENSOR
REMARK 3 L11: 0.5296 L22: 2.8355
REMARK 3 L33: 2.0508 L12: -0.3123
REMARK 3 L13: 0.5738 L23: -2.1296
REMARK 3 S TENSOR
REMARK 3 S11: 0.1401 S12: 0.0686 S13: 0.1342
REMARK 3 S21: -0.3352 S22: -0.2013 S23: 0.0606
REMARK 3 S31: 0.1830 S32: -0.1432 S33: 0.0650
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1281 THROUGH 1376 )
REMARK 3 ORIGIN FOR THE GROUP (A): 381.9205 -19.5191 17.5380
REMARK 3 T TENSOR
REMARK 3 T11: 0.7982 T22: 0.4059
REMARK 3 T33: 0.5160 T12: -0.2213
REMARK 3 T13: -0.3271 T23: 0.0892
REMARK 3 L TENSOR
REMARK 3 L11: 0.4224 L22: 0.9645
REMARK 3 L33: 1.2047 L12: 0.0552
REMARK 3 L13: 0.1350 L23: -0.0749
REMARK 3 S TENSOR
REMARK 3 S11: -0.0625 S12: 0.2052 S13: 0.0948
REMARK 3 S21: -0.6217 S22: -0.0013 S23: 0.1518
REMARK 3 S31: -0.1206 S32: 0.1257 S33: 0.0170
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1377 THROUGH 1448 )
REMARK 3 ORIGIN FOR THE GROUP (A): 365.9345 -13.9419 49.4271
REMARK 3 T TENSOR
REMARK 3 T11: 0.5376 T22: 0.5362
REMARK 3 T33: 0.8730 T12: -0.1334
REMARK 3 T13: -0.1857 T23: 0.0381
REMARK 3 L TENSOR
REMARK 3 L11: 1.3603 L22: 0.4248
REMARK 3 L33: 1.2798 L12: -0.3588
REMARK 3 L13: -0.0302 L23: 0.6148
REMARK 3 S TENSOR
REMARK 3 S11: -0.0367 S12: -0.2000 S13: 0.4629
REMARK 3 S21: -0.2228 S22: 0.0720 S23: 0.5180
REMARK 3 S31: -0.3125 S32: -0.6923 S33: -0.1347
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 20 THROUGH 185 )
REMARK 3 ORIGIN FOR THE GROUP (A): 403.4898 38.6307 52.7598
REMARK 3 T TENSOR
REMARK 3 T11: 0.5535 T22: 0.2625
REMARK 3 T33: 0.2825 T12: 0.1551
REMARK 3 T13: 0.1900 T23: -0.1596
REMARK 3 L TENSOR
REMARK 3 L11: 0.8371 L22: 0.8971
REMARK 3 L33: 0.7304 L12: -0.2973
REMARK 3 L13: 0.0382 L23: 0.1813
REMARK 3 S TENSOR
REMARK 3 S11: -0.2118 S12: -0.1132 S13: 0.3898
REMARK 3 S21: -0.0490 S22: 0.1824 S23: -0.0547
REMARK 3 S31: -0.5800 S32: -0.1147 S33: -0.1937
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 186 THROUGH 408 )
REMARK 3 ORIGIN FOR THE GROUP (A): 383.4322 31.4645 23.1435
REMARK 3 T TENSOR
REMARK 3 T11: 0.5611 T22: 0.4250
REMARK 3 T33: 0.5074 T12: 0.1501
REMARK 3 T13: 0.0333 T23: 0.0151
REMARK 3 L TENSOR
REMARK 3 L11: 0.7298 L22: 0.4836
REMARK 3 L33: 1.8162 L12: -0.0176
REMARK 3 L13: 0.8600 L23: -0.2052
REMARK 3 S TENSOR
REMARK 3 S11: 0.0489 S12: -0.0219 S13: 0.1064
REMARK 3 S21: -0.1935 S22: 0.0582 S23: 0.2279
REMARK 3 S31: -0.2205 S32: -0.3051 S33: -0.0329
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 409 THROUGH 487 )
REMARK 3 ORIGIN FOR THE GROUP (A): 386.2167 33.9283 54.3179
REMARK 3 T TENSOR
REMARK 3 T11: 0.3780 T22: 0.5300
REMARK 3 T33: 0.5953 T12: 0.1400
REMARK 3 T13: 0.1484 T23: -0.0406
REMARK 3 L TENSOR
REMARK 3 L11: 2.5663 L22: 2.0012
REMARK 3 L33: 0.8372 L12: -1.7104
REMARK 3 L13: 0.0232 L23: -0.2291
REMARK 3 S TENSOR
REMARK 3 S11: 0.0119 S12: -0.0111 S13: -0.3400
REMARK 3 S21: 0.1505 S22: 0.1153 S23: 0.8954
REMARK 3 S31: -0.0290 S32: -0.4370 S33: 0.0940
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 488 THROUGH 700 )
REMARK 3 ORIGIN FOR THE GROUP (A): 407.6600 31.6337 27.6411
REMARK 3 T TENSOR
REMARK 3 T11: 0.4404 T22: 0.2705
REMARK 3 T33: 0.3036 T12: -0.0115
REMARK 3 T13: 0.1257 T23: -0.0244
REMARK 3 L TENSOR
REMARK 3 L11: 1.0914 L22: 1.1841
REMARK 3 L33: 1.5133 L12: -0.2200
REMARK 3 L13: 0.1866 L23: -0.1526
REMARK 3 S TENSOR
REMARK 3 S11: 0.0351 S12: 0.1649 S13: 0.2479
REMARK 3 S21: -0.2547 S22: 0.0118 S23: 0.0654
REMARK 3 S31: -0.3451 S32: 0.1619 S33: -0.0306
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 701 THROUGH 820 )
REMARK 3 ORIGIN FOR THE GROUP (A): 417.3365 13.1704 41.5974
REMARK 3 T TENSOR
REMARK 3 T11: 0.2862 T22: 0.3292
REMARK 3 T33: 0.2344 T12: -0.0070
REMARK 3 T13: 0.1336 T23: -0.0500
REMARK 3 L TENSOR
REMARK 3 L11: 0.5103 L22: 0.7852
REMARK 3 L33: 0.3818 L12: -0.2406
REMARK 3 L13: 0.3898 L23: -0.3605
REMARK 3 S TENSOR
REMARK 3 S11: 0.0319 S12: 0.1482 S13: 0.0540
REMARK 3 S21: -0.1492 S22: -0.0487 S23: -0.1365
REMARK 3 S31: 0.1797 S32: 0.1449 S33: -0.0142
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 821 THROUGH 994 )
REMARK 3 ORIGIN FOR THE GROUP (A): 402.1405 8.3826 73.8359
REMARK 3 T TENSOR
REMARK 3 T11: 0.1727 T22: 0.5486
REMARK 3 T33: 0.3068 T12: -0.0085
REMARK 3 T13: 0.1570 T23: -0.1546
REMARK 3 L TENSOR
REMARK 3 L11: 0.4839 L22: 0.6709
REMARK 3 L33: 1.1862 L12: -0.3031
REMARK 3 L13: -0.2287 L23: 0.0302
REMARK 3 S TENSOR
REMARK 3 S11: 0.1254 S12: -0.3385 S13: -0.0132
REMARK 3 S21: 0.1039 S22: -0.1148 S23: 0.2653
REMARK 3 S31: -0.0593 S32: -0.2592 S33: 0.0131
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 995 THROUGH 1220 )
REMARK 3 ORIGIN FOR THE GROUP (A): 395.1834 -7.0190 57.7943
REMARK 3 T TENSOR
REMARK 3 T11: 0.1990 T22: 0.2978
REMARK 3 T33: 0.3293 T12: 0.0539
REMARK 3 T13: 0.0233 T23: -0.1056
REMARK 3 L TENSOR
REMARK 3 L11: 0.5912 L22: 0.7560
REMARK 3 L33: 0.6583 L12: 0.2467
REMARK 3 L13: 0.4292 L23: 0.0400
REMARK 3 S TENSOR
REMARK 3 S11: 0.0111 S12: -0.3238 S13: 0.2808
REMARK 3 S21: -0.0761 S22: -0.0023 S23: 0.3401
REMARK 3 S31: 0.2570 S32: -0.0847 S33: -0.0152
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 3 THROUGH 26 )
REMARK 3 ORIGIN FOR THE GROUP (A): 447.3173 -19.7398 64.9100
REMARK 3 T TENSOR
REMARK 3 T11: 0.3628 T22: 0.8911
REMARK 3 T33: 0.5793 T12: 0.3739
REMARK 3 T13: -0.1150 T23: -0.0384
REMARK 3 L TENSOR
REMARK 3 L11: 4.2712 L22: 3.3260
REMARK 3 L33: 3.7722 L12: 0.0847
REMARK 3 L13: 0.3423 L23: 1.8768
REMARK 3 S TENSOR
REMARK 3 S11: 0.0128 S12: 0.0291 S13: 0.1199
REMARK 3 S21: 0.0428 S22: -0.0121 S23: -0.2529
REMARK 3 S31: 0.1995 S32: 0.2375 S33: -0.0412
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 27 THROUGH 51 )
REMARK 3 ORIGIN FOR THE GROUP (A): 430.3729 -12.7204 73.2037
REMARK 3 T TENSOR
REMARK 3 T11: 0.1632 T22: 0.6682
REMARK 3 T33: 0.4117 T12: 0.2612
REMARK 3 T13: -0.1321 T23: -0.1657
REMARK 3 L TENSOR
REMARK 3 L11: 0.7790 L22: 0.1400
REMARK 3 L33: 0.3264 L12: 0.0570
REMARK 3 L13: 0.0190 L23: -0.0482
REMARK 3 S TENSOR
REMARK 3 S11: -0.0025 S12: 0.2268 S13: -0.2802
REMARK 3 S21: -0.0059 S22: -0.0612 S23: -0.0985
REMARK 3 S31: 0.1315 S32: 0.1677 S33: -0.3521
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 52 THROUGH 84 )
REMARK 3 ORIGIN FOR THE GROUP (A): 427.5966 1.1084 80.2808
REMARK 3 T TENSOR
REMARK 3 T11: 0.1597 T22: 0.5919
REMARK 3 T33: 0.2061 T12: 0.0116
REMARK 3 T13: 0.0740 T23: -0.0913
REMARK 3 L TENSOR
REMARK 3 L11: 1.2086 L22: 1.4975
REMARK 3 L33: 1.3050 L12: 0.5609
REMARK 3 L13: -0.2754 L23: -0.1901
REMARK 3 S TENSOR
REMARK 3 S11: 0.0497 S12: -0.1414 S13: 0.0415
REMARK 3 S21: 0.1660 S22: -0.1121 S23: -0.0888
REMARK 3 S31: 0.1974 S32: 0.3494 S33: -0.0065
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 85 THROUGH 190 )
REMARK 3 ORIGIN FOR THE GROUP (A): 432.4161 0.3859 76.7217
REMARK 3 T TENSOR
REMARK 3 T11: 0.3116 T22: 0.5916
REMARK 3 T33: 0.3180 T12: -0.0166
REMARK 3 T13: -0.0272 T23: -0.0491
REMARK 3 L TENSOR
REMARK 3 L11: 0.8147 L22: 0.8806
REMARK 3 L33: 0.7544 L12: -0.1870
REMARK 3 L13: 0.0327 L23: 0.1210
REMARK 3 S TENSOR
REMARK 3 S11: 0.1005 S12: -0.2221 S13: 0.0024
REMARK 3 S21: 0.1837 S22: -0.0992 S23: -0.3675
REMARK 3 S31: -0.0510 S32: 0.4758 S33: -0.0416
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 191 THROUGH 227 )
REMARK 3 ORIGIN FOR THE GROUP (A): 441.4385 -22.8941 43.5604
REMARK 3 T TENSOR
REMARK 3 T11: 0.6683 T22: 0.7832
REMARK 3 T33: 0.6545 T12: 0.3297
REMARK 3 T13: 0.0397 T23: -0.1925
REMARK 3 L TENSOR
REMARK 3 L11: 1.4219 L22: 0.7871
REMARK 3 L33: 0.4853 L12: -0.3493
REMARK 3 L13: 0.7118 L23: -0.4769
REMARK 3 S TENSOR
REMARK 3 S11: 0.0436 S12: -0.0325 S13: -0.3211
REMARK 3 S21: -0.2862 S22: 0.0098 S23: -0.6623
REMARK 3 S31: 0.1959 S32: 0.6130 S33: -0.0079
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 228 THROUGH 268 )
REMARK 3 ORIGIN FOR THE GROUP (A): 434.8533 -22.5700 75.6069
REMARK 3 T TENSOR
REMARK 3 T11: 0.4617 T22: 0.7033
REMARK 3 T33: 0.4634 T12: 0.1917
REMARK 3 T13: -0.2500 T23: 0.0458
REMARK 3 L TENSOR
REMARK 3 L11: 1.2677 L22: 1.9633
REMARK 3 L33: 0.5681 L12: 0.0596
REMARK 3 L13: 0.5550 L23: 0.5335
REMARK 3 S TENSOR
REMARK 3 S11: 0.2177 S12: -0.3455 S13: -0.0115
REMARK 3 S21: 0.2855 S22: -0.0944 S23: -0.1833
REMARK 3 S31: 0.2794 S32: 0.2308 S33: 0.0162
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 3 THROUGH 71 )
REMARK 3 ORIGIN FOR THE GROUP (A): 359.1079 -26.8989 -1.3407
REMARK 3 T TENSOR
REMARK 3 T11: 1.4957 T22: 0.9998
REMARK 3 T33: 1.0872 T12: -0.4473
REMARK 3 T13: -0.9007 T23: 0.1696
REMARK 3 L TENSOR
REMARK 3 L11: 0.9287 L22: 0.2899
REMARK 3 L33: 0.9362 L12: 0.1353
REMARK 3 L13: 0.3760 L23: 0.3350
REMARK 3 S TENSOR
REMARK 3 S11: -0.2174 S12: 0.4731 S13: -0.0139
REMARK 3 S21: -0.4043 S22: 0.1319 S23: 0.0824
REMARK 3 S31: 0.1393 S32: -0.3660 S33: -0.3440
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 72 THROUGH 89 )
REMARK 3 ORIGIN FOR THE GROUP (A): 349.3413 -22.3515 5.8675
REMARK 3 T TENSOR
REMARK 3 T11: 1.4150 T22: 1.3331
REMARK 3 T33: 1.4926 T12: -0.4692
REMARK 3 T13: -0.8550 T23: 0.4180
REMARK 3 L TENSOR
REMARK 3 L11: 1.1596 L22: 0.1554
REMARK 3 L33: 0.6180 L12: 0.4123
REMARK 3 L13: 0.2963 L23: 0.0344
REMARK 3 S TENSOR
REMARK 3 S11: -0.1777 S12: 0.3016 S13: 0.3935
REMARK 3 S21: -0.1055 S22: 0.0619 S23: 0.2205
REMARK 3 S31: -0.3165 S32: -0.0869 S33: 0.1890
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 90 THROUGH 103 )
REMARK 3 ORIGIN FOR THE GROUP (A): 340.7193 -16.8582 4.7686
REMARK 3 T TENSOR
REMARK 3 T11: 1.2956 T22: 2.0076
REMARK 3 T33: 1.9811 T12: 0.1983
REMARK 3 T13: -0.2904 T23: 0.3026
REMARK 3 L TENSOR
REMARK 3 L11: 0.3444 L22: 0.0954
REMARK 3 L33: 0.4946 L12: -0.1804
REMARK 3 L13: -0.4075 L23: 0.2175
REMARK 3 S TENSOR
REMARK 3 S11: 0.0295 S12: -0.1525 S13: 0.0623
REMARK 3 S21: 0.4005 S22: -0.1395 S23: -0.3054
REMARK 3 S31: -0.1760 S32: 0.1265 S33: 0.0796
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 104 THROUGH 122 )
REMARK 3 ORIGIN FOR THE GROUP (A): 349.2514 -14.6280 7.8841
REMARK 3 T TENSOR
REMARK 3 T11: 1.1602 T22: 1.0332
REMARK 3 T33: 1.4948 T12: -0.1456
REMARK 3 T13: -0.4254 T23: 0.2451
REMARK 3 L TENSOR
REMARK 3 L11: 0.6289 L22: 1.5898
REMARK 3 L33: 1.3920 L12: -0.9156
REMARK 3 L13: 0.0282 L23: 0.5470
REMARK 3 S TENSOR
REMARK 3 S11: 0.2078 S12: -0.2847 S13: 0.4155
REMARK 3 S21: 0.2627 S22: -0.1133 S23: 0.6002
REMARK 3 S31: -0.4044 S32: -0.0627 S33: -0.0431
REMARK 3 TLS GROUP : 24
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 123 THROUGH 215 )
REMARK 3 ORIGIN FOR THE GROUP (A): 360.1530 -25.9246 23.3731
REMARK 3 T TENSOR
REMARK 3 T11: 0.7772 T22: 0.5025
REMARK 3 T33: 0.9917 T12: -0.3897
REMARK 3 T13: -0.5706 T23: 0.0588
REMARK 3 L TENSOR
REMARK 3 L11: 0.4313 L22: 0.9028
REMARK 3 L33: 0.9052 L12: 0.2590
REMARK 3 L13: 0.0253 L23: -0.2336
REMARK 3 S TENSOR
REMARK 3 S11: 0.0614 S12: -0.0761 S13: 0.2134
REMARK 3 S21: -0.2821 S22: -0.0237 S23: 0.7137
REMARK 3 S31: 0.1516 S32: -0.4382 S33: 0.4004
REMARK 3 TLS GROUP : 25
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 72 THROUGH 103 )
REMARK 3 ORIGIN FOR THE GROUP (A): 372.6432 -36.8949 59.1504
REMARK 3 T TENSOR
REMARK 3 T11: 0.5793 T22: 0.4281
REMARK 3 T33: 0.5138 T12: -0.2837
REMARK 3 T13: -0.1362 T23: 0.0371
REMARK 3 L TENSOR
REMARK 3 L11: 1.7877 L22: 1.6446
REMARK 3 L33: 1.3248 L12: 0.1832
REMARK 3 L13: -0.2776 L23: 0.0325
REMARK 3 S TENSOR
REMARK 3 S11: 0.1980 S12: -0.2471 S13: -0.0997
REMARK 3 S21: -0.0259 S22: 0.0446 S23: 0.4494
REMARK 3 S31: 0.2730 S32: -0.2664 S33: -0.0262
REMARK 3 TLS GROUP : 26
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 104 THROUGH 126 )
REMARK 3 ORIGIN FOR THE GROUP (A): 384.4575 -39.9488 72.2608
REMARK 3 T TENSOR
REMARK 3 T11: 0.7852 T22: 0.5874
REMARK 3 T33: 0.6334 T12: -0.2064
REMARK 3 T13: -0.0474 T23: 0.0296
REMARK 3 L TENSOR
REMARK 3 L11: 4.0345 L22: 2.8311
REMARK 3 L33: 3.2380 L12: 1.6811
REMARK 3 L13: 2.4097 L23: -0.9287
REMARK 3 S TENSOR
REMARK 3 S11: 0.1461 S12: -0.3113 S13: -0.2180
REMARK 3 S21: 0.1275 S22: 0.0702 S23: -0.0293
REMARK 3 S31: 0.1422 S32: 0.2715 S33: -0.0624
REMARK 3 TLS GROUP : 27
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 127 THROUGH 137 )
REMARK 3 ORIGIN FOR THE GROUP (A): 371.3958 -39.4236 61.9469
REMARK 3 T TENSOR
REMARK 3 T11: 0.8170 T22: 0.5084
REMARK 3 T33: 0.5662 T12: -0.1497
REMARK 3 T13: -0.0161 T23: 0.0699
REMARK 3 L TENSOR
REMARK 3 L11: 1.6544 L22: 0.6850
REMARK 3 L33: 4.1633 L12: 1.0402
REMARK 3 L13: 0.5643 L23: -0.0080
REMARK 3 S TENSOR
REMARK 3 S11: 0.0934 S12: -0.1906 S13: -0.2196
REMARK 3 S21: 0.3516 S22: 0.1174 S23: 0.0320
REMARK 3 S31: 0.0610 S32: -0.2905 S33: -0.1435
REMARK 3 TLS GROUP : 28
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 138 THROUGH 155 )
REMARK 3 ORIGIN FOR THE GROUP (A): 369.5593 -39.4613 54.6675
REMARK 3 T TENSOR
REMARK 3 T11: 0.6238 T22: 0.4210
REMARK 3 T33: 0.7844 T12: -0.3167
REMARK 3 T13: 0.0603 T23: 0.0919
REMARK 3 L TENSOR
REMARK 3 L11: 7.4701 L22: 5.5686
REMARK 3 L33: 3.4596 L12: -3.4890
REMARK 3 L13: 1.8492 L23: -1.8301
REMARK 3 S TENSOR
REMARK 3 S11: 0.3139 S12: -0.1813 S13: -0.2059
REMARK 3 S21: 0.1000 S22: 0.1473 S23: 0.1761
REMARK 3 S31: 0.2707 S32: -0.2821 S33: -0.2450
REMARK 3 TLS GROUP : 29
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 3 THROUGH 60 )
REMARK 3 ORIGIN FOR THE GROUP (A): 430.2538 -46.9100 29.9358
REMARK 3 T TENSOR
REMARK 3 T11: 0.8313 T22: 0.6114
REMARK 3 T33: 0.9698 T12: 0.5922
REMARK 3 T13: 0.0011 T23: -0.3963
REMARK 3 L TENSOR
REMARK 3 L11: 0.7556 L22: 1.0394
REMARK 3 L33: 0.5764 L12: 0.0595
REMARK 3 L13: -0.2730 L23: 0.0913
REMARK 3 S TENSOR
REMARK 3 S11: -0.0142 S12: 0.3553 S13: -0.3621
REMARK 3 S21: -0.2391 S22: -0.1260 S23: -0.2128
REMARK 3 S31: 0.3560 S32: 0.1192 S33: 0.0587
REMARK 3 TLS GROUP : 30
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 61 THROUGH 82 )
REMARK 3 ORIGIN FOR THE GROUP (A): 424.4039 -52.1028 53.5163
REMARK 3 T TENSOR
REMARK 3 T11: 1.3636 T22: 0.7907
REMARK 3 T33: 0.9072 T12: 0.3715
REMARK 3 T13: -0.2262 T23: -0.0676
REMARK 3 L TENSOR
REMARK 3 L11: 1.2604 L22: 6.4676
REMARK 3 L33: 8.2552 L12: -2.5069
REMARK 3 L13: -3.0547 L23: 5.0451
REMARK 3 S TENSOR
REMARK 3 S11: -0.0962 S12: -0.1755 S13: -0.2619
REMARK 3 S21: 0.2803 S22: -0.1159 S23: -0.1488
REMARK 3 S31: 0.1113 S32: 0.0027 S33: -0.0043
REMARK 3 TLS GROUP : 31
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 83 THROUGH 92 )
REMARK 3 ORIGIN FOR THE GROUP (A): 434.6864 -54.8229 52.6750
REMARK 3 T TENSOR
REMARK 3 T11: 1.4016 T22: 0.7893
REMARK 3 T33: 1.5249 T12: 0.6009
REMARK 3 T13: 0.0937 T23: 0.1501
REMARK 3 L TENSOR
REMARK 3 L11: 7.8860 L22: 3.4385
REMARK 3 L33: 3.2333 L12: 0.1917
REMARK 3 L13: 0.1975 L23: 0.4720
REMARK 3 S TENSOR
REMARK 3 S11: 0.0567 S12: -0.6196 S13: 0.3392
REMARK 3 S21: 0.5514 S22: 0.2291 S23: -0.3160
REMARK 3 S31: -0.3913 S32: 0.3303 S33: -0.1774
REMARK 3 TLS GROUP : 32
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 93 THROUGH 106 )
REMARK 3 ORIGIN FOR THE GROUP (A): 421.5292 -50.2803 36.3900
REMARK 3 T TENSOR
REMARK 3 T11: 0.8777 T22: 0.5636
REMARK 3 T33: 0.7784 T12: 0.2211
REMARK 3 T13: -0.1733 T23: -0.4206
REMARK 3 L TENSOR
REMARK 3 L11: 1.3180 L22: 2.2546
REMARK 3 L33: 1.7489 L12: -0.5841
REMARK 3 L13: -0.4926 L23: 0.3635
REMARK 3 S TENSOR
REMARK 3 S11: 0.0077 S12: 0.0575 S13: -0.2217
REMARK 3 S21: 0.0626 S22: 0.0315 S23: -0.0263
REMARK 3 S31: 0.2698 S32: 0.0216 S33: -0.1236
REMARK 3 TLS GROUP : 33
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 107 THROUGH 118 )
REMARK 3 ORIGIN FOR THE GROUP (A): 417.0544 -53.7065 27.5002
REMARK 3 T TENSOR
REMARK 3 T11: 1.0881 T22: 0.5457
REMARK 3 T33: 0.9156 T12: 0.2058
REMARK 3 T13: -0.1298 T23: -0.3855
REMARK 3 L TENSOR
REMARK 3 L11: 4.8139 L22: 6.9874
REMARK 3 L33: 3.3141 L12: 1.2733
REMARK 3 L13: -0.1563 L23: 0.5625
REMARK 3 S TENSOR
REMARK 3 S11: -0.1475 S12: 0.5386 S13: -0.5387
REMARK 3 S21: -0.4175 S22: 0.1254 S23: -0.1824
REMARK 3 S31: 0.4161 S32: 0.0040 S33: -0.1661
REMARK 3 TLS GROUP : 34
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 119 THROUGH 146 )
REMARK 3 ORIGIN FOR THE GROUP (A): 422.7737 -53.5622 34.9087
REMARK 3 T TENSOR
REMARK 3 T11: 1.0573 T22: 0.5618
REMARK 3 T33: 0.7608 T12: 0.4136
REMARK 3 T13: -0.0965 T23: -0.2047
REMARK 3 L TENSOR
REMARK 3 L11: 0.5501 L22: 3.3575
REMARK 3 L33: 2.0091 L12: -0.0644
REMARK 3 L13: 0.9848 L23: 0.6049
REMARK 3 S TENSOR
REMARK 3 S11: 0.0205 S12: 0.1353 S13: -0.5683
REMARK 3 S21: 0.0371 S22: 0.0091 S23: 0.2782
REMARK 3 S31: 0.2689 S32: -0.1303 S33: 0.0809
REMARK 3 TLS GROUP : 35
REMARK 3 SELECTION: CHAIN 'I' AND (RESID 2 THROUGH 52 )
REMARK 3 ORIGIN FOR THE GROUP (A): 374.7737 32.5611 -9.1110
REMARK 3 T TENSOR
REMARK 3 T11: 1.2831 T22: 0.4970
REMARK 3 T33: 0.5455 T12: 0.0607
REMARK 3 T13: -0.1250 T23: 0.2165
REMARK 3 L TENSOR
REMARK 3 L11: 0.3510 L22: 1.9086
REMARK 3 L33: 0.6471 L12: -0.0609
REMARK 3 L13: -0.2776 L23: 0.2456
REMARK 3 S TENSOR
REMARK 3 S11: 0.1034 S12: -0.0095 S13: -0.1975
REMARK 3 S21: -0.2796 S22: -0.0369 S23: 0.3492
REMARK 3 S31: -0.2638 S32: -0.2605 S33: -0.0050
REMARK 3 TLS GROUP : 36
REMARK 3 SELECTION: CHAIN 'I' AND (RESID 53 THROUGH 116 )
REMARK 3 ORIGIN FOR THE GROUP (A): 407.2713 20.3692 1.2174
REMARK 3 T TENSOR
REMARK 3 T11: 0.4425 T22: 0.5084
REMARK 3 T33: 0.3165 T12: -0.0268
REMARK 3 T13: 0.1049 T23: 0.0432
REMARK 3 L TENSOR
REMARK 3 L11: 2.1246 L22: 1.8021
REMARK 3 L33: 2.5172 L12: 0.5682
REMARK 3 L13: -0.6310 L23: -0.4545
REMARK 3 S TENSOR
REMARK 3 S11: 0.2623 S12: 0.2047 S13: 0.0171
REMARK 3 S21: 0.1491 S22: -0.1185 S23: 0.0866
REMARK 3 S31: 0.0605 S32: -0.2656 S33: -0.0072
REMARK 3 TLS GROUP : 37
REMARK 3 SELECTION: CHAIN 'J' AND (RESID 1 THROUGH 17 )
REMARK 3 ORIGIN FOR THE GROUP (A): 431.1542 3.4169 65.8582
REMARK 3 T TENSOR
REMARK 3 T11: 0.1503 T22: 0.5202
REMARK 3 T33: 0.3069 T12: 0.0920
REMARK 3 T13: 0.1424 T23: -0.0874
REMARK 3 L TENSOR
REMARK 3 L11: 1.8144 L22: 2.0510
REMARK 3 L33: 0.5813 L12: -0.7258
REMARK 3 L13: -0.6176 L23: 0.3867
REMARK 3 S TENSOR
REMARK 3 S11: 0.1507 S12: -0.0597 S13: -0.0177
REMARK 3 S21: -0.0079 S22: 0.0298 S23: -0.0422
REMARK 3 S31: -0.1249 S32: 0.1488 S33: 0.1850
REMARK 3 TLS GROUP : 38
REMARK 3 SELECTION: CHAIN 'J' AND (RESID 18 THROUGH 26 )
REMARK 3 ORIGIN FOR THE GROUP (A): 438.9220 14.8419 61.1421
REMARK 3 T TENSOR
REMARK 3 T11: 0.3682 T22: 0.6313
REMARK 3 T33: 0.7045 T12: -0.1299
REMARK 3 T13: 0.1271 T23: -0.0888
REMARK 3 L TENSOR
REMARK 3 L11: 3.2145 L22: 1.3249
REMARK 3 L33: 2.9563 L12: -1.1706
REMARK 3 L13: -2.6523 L23: 0.1353
REMARK 3 S TENSOR
REMARK 3 S11: 0.0976 S12: -0.1649 S13: 0.6417
REMARK 3 S21: 0.1917 S22: -0.0059 S23: -0.3714
REMARK 3 S31: -0.9502 S32: 0.6837 S33: -0.0516
REMARK 3 TLS GROUP : 39
REMARK 3 SELECTION: CHAIN 'J' AND (RESID 27 THROUGH 31 )
REMARK 3 ORIGIN FOR THE GROUP (A): 444.8686 16.5513 54.9441
REMARK 3 T TENSOR
REMARK 3 T11: 0.6706 T22: 1.1020
REMARK 3 T33: 0.9658 T12: 0.1851
REMARK 3 T13: 0.2268 T23: 0.0097
REMARK 3 L TENSOR
REMARK 3 L11: 9.3986 L22: 8.7760
REMARK 3 L33: 4.1023 L12: -0.6352
REMARK 3 L13: 0.9519 L23: -5.8902
REMARK 3 S TENSOR
REMARK 3 S11: -0.1516 S12: -0.2631 S13: 0.5734
REMARK 3 S21: -0.0023 S22: -0.1713 S23: 0.1153
REMARK 3 S31: -0.7546 S32: -0.1654 S33: 0.2917
REMARK 3 TLS GROUP : 40
REMARK 3 SELECTION: CHAIN 'J' AND (RESID 32 THROUGH 43 )
REMARK 3 ORIGIN FOR THE GROUP (A): 440.8805 4.6168 56.7419
REMARK 3 T TENSOR
REMARK 3 T11: 0.2150 T22: 0.8579
REMARK 3 T33: 0.6038 T12: 0.0070
REMARK 3 T13: 0.1397 T23: -0.0276
REMARK 3 L TENSOR
REMARK 3 L11: 4.3552 L22: 3.7225
REMARK 3 L33: 3.9772 L12: 1.3893
REMARK 3 L13: -1.8883 L23: -2.1656
REMARK 3 S TENSOR
REMARK 3 S11: -0.1199 S12: 0.0301 S13: 0.0047
REMARK 3 S21: -0.0474 S22: -0.1781 S23: -0.3178
REMARK 3 S31: 0.0098 S32: 0.2351 S33: 0.0324
REMARK 3 TLS GROUP : 41
REMARK 3 SELECTION: CHAIN 'J' AND (RESID 44 THROUGH 56 )
REMARK 3 ORIGIN FOR THE GROUP (A): 430.4317 6.1746 57.9484
REMARK 3 T TENSOR
REMARK 3 T11: 0.1674 T22: 0.3813
REMARK 3 T33: 0.3042 T12: 0.1056
REMARK 3 T13: 0.1491 T23: -0.1423
REMARK 3 L TENSOR
REMARK 3 L11: 1.4662 L22: 0.9021
REMARK 3 L33: 0.5437 L12: -0.2071
REMARK 3 L13: 0.0864 L23: -0.5398
REMARK 3 S TENSOR
REMARK 3 S11: -0.0114 S12: -0.0479 S13: -0.0093
REMARK 3 S21: -0.0328 S22: 0.0187 S23: -0.1575
REMARK 3 S31: 0.0337 S32: 0.1235 S33: 0.0150
REMARK 3 TLS GROUP : 42
REMARK 3 SELECTION: CHAIN 'J' AND (RESID 57 THROUGH 65 )
REMARK 3 ORIGIN FOR THE GROUP (A): 422.3567 23.6543 68.1383
REMARK 3 T TENSOR
REMARK 3 T11: 0.2306 T22: 0.4527
REMARK 3 T33: 0.5435 T12: -0.1257
REMARK 3 T13: 0.0052 T23: 0.0201
REMARK 3 L TENSOR
REMARK 3 L11: 5.0713 L22: 2.6834
REMARK 3 L33: 5.7446 L12: 1.6682
REMARK 3 L13: 4.5103 L23: -0.4167
REMARK 3 S TENSOR
REMARK 3 S11: 0.3321 S12: -0.2391 S13: 0.1216
REMARK 3 S21: 0.2830 S22: 0.1683 S23: 0.1413
REMARK 3 S31: -0.0938 S32: -0.0002 S33: 0.0432
REMARK 3 TLS GROUP : 43
REMARK 3 SELECTION: CHAIN 'K' AND (RESID 1 THROUGH 39 )
REMARK 3 ORIGIN FOR THE GROUP (A): 416.2079 -27.7360 75.0206
REMARK 3 T TENSOR
REMARK 3 T11: 0.5692 T22: 0.4430
REMARK 3 T33: 0.3729 T12: 0.0800
REMARK 3 T13: -0.0606 T23: 0.0416
REMARK 3 L TENSOR
REMARK 3 L11: 0.6199 L22: 3.4737
REMARK 3 L33: 0.6247 L12: -0.8900
REMARK 3 L13: 0.0207 L23: 0.0776
REMARK 3 S TENSOR
REMARK 3 S11: 0.2818 S12: -0.3189 S13: -0.3779
REMARK 3 S21: 0.2946 S22: -0.0358 S23: 0.3851
REMARK 3 S31: 0.4342 S32: -0.0874 S33: -0.0553
REMARK 3 TLS GROUP : 44
REMARK 3 SELECTION: CHAIN 'K' AND (RESID 40 THROUGH 82 )
REMARK 3 ORIGIN FOR THE GROUP (A): 423.7873 -35.3073 66.8844
REMARK 3 T TENSOR
REMARK 3 T11: 0.5366 T22: 0.4298
REMARK 3 T33: 0.5044 T12: 0.2463
REMARK 3 T13: -0.2016 T23: 0.0632
REMARK 3 L TENSOR
REMARK 3 L11: 1.2395 L22: 2.4944
REMARK 3 L33: 0.8919 L12: -0.1484
REMARK 3 L13: -0.0307 L23: -0.3004
REMARK 3 S TENSOR
REMARK 3 S11: 0.1264 S12: -0.3081 S13: -0.4464
REMARK 3 S21: -0.1152 S22: 0.0575 S23: -0.3325
REMARK 3 S31: 0.4486 S32: 0.3046 S33: 0.0995
REMARK 3 TLS GROUP : 45
REMARK 3 SELECTION: CHAIN 'K' AND (RESID 83 THROUGH 114 )
REMARK 3 ORIGIN FOR THE GROUP (A): 442.5152 -27.5597 73.0410
REMARK 3 T TENSOR
REMARK 3 T11: 0.3874 T22: 0.7841
REMARK 3 T33: 0.6760 T12: 0.2744
REMARK 3 T13: -0.0829 T23: -0.0158
REMARK 3 L TENSOR
REMARK 3 L11: 1.0257 L22: 0.4210
REMARK 3 L33: 0.8560 L12: -0.3284
REMARK 3 L13: 0.2527 L23: 0.2378
REMARK 3 S TENSOR
REMARK 3 S11: 0.2243 S12: -0.2038 S13: -0.3295
REMARK 3 S21: 0.1070 S22: 0.0139 S23: -0.4200
REMARK 3 S31: 0.4234 S32: 0.6292 S33: 0.0728
REMARK 3 TLS GROUP : 46
REMARK 3 SELECTION: CHAIN 'L' AND (RESID 27 THROUGH 31 )
REMARK 3 ORIGIN FOR THE GROUP (A): 408.2825 25.6999 86.4069
REMARK 3 T TENSOR
REMARK 3 T11: 0.9946 T22: 1.1184
REMARK 3 T33: 1.0944 T12: -0.0863
REMARK 3 T13: -0.0370 T23: -0.2423
REMARK 3 L TENSOR
REMARK 3 L11: 2.3120 L22: 5.5433
REMARK 3 L33: 3.3538 L12: -1.2115
REMARK 3 L13: 1.0260 L23: 3.2147
REMARK 3 S TENSOR
REMARK 3 S11: 0.1290 S12: -0.2123 S13: -0.0147
REMARK 3 S21: 0.0976 S22: 0.0242 S23: 0.0634
REMARK 3 S31: -0.1276 S32: -0.0649 S33: -0.0618
REMARK 3 TLS GROUP : 47
REMARK 3 SELECTION: CHAIN 'L' AND (RESID 32 THROUGH 36 )
REMARK 3 ORIGIN FOR THE GROUP (A): 413.8315 31.6987 79.3527
REMARK 3 T TENSOR
REMARK 3 T11: 1.5431 T22: 1.3582
REMARK 3 T33: 1.4328 T12: -0.1636
REMARK 3 T13: -0.1144 T23: -0.0504
REMARK 3 L TENSOR
REMARK 3 L11: 3.6805 L22: 3.4399
REMARK 3 L33: 2.1812 L12: 3.4930
REMARK 3 L13: 1.6009 L23: 1.0930
REMARK 3 S TENSOR
REMARK 3 S11: 0.0224 S12: -0.0189 S13: -0.1400
REMARK 3 S21: 0.2534 S22: -0.0536 S23: -0.8356
REMARK 3 S31: 0.0356 S32: 1.4500 S33: 0.0152
REMARK 3 TLS GROUP : 48
REMARK 3 SELECTION: CHAIN 'L' AND (RESID 37 THROUGH 41 )
REMARK 3 ORIGIN FOR THE GROUP (A): 407.9400 29.5048 89.9156
REMARK 3 T TENSOR
REMARK 3 T11: 1.5615 T22: 1.2297
REMARK 3 T33: 1.2795 T12: 0.0096
REMARK 3 T13: 0.0538 T23: -0.5007
REMARK 3 L TENSOR
REMARK 3 L11: 6.2114 L22: 4.2840
REMARK 3 L33: 2.1284 L12: -5.0977
REMARK 3 L13: 3.2987 L23: -2.7471
REMARK 3 S TENSOR
REMARK 3 S11: -0.1296 S12: 0.0484 S13: 0.1261
REMARK 3 S21: 0.3296 S22: 0.0465 S23: 0.6296
REMARK 3 S31: 0.2401 S32: -0.7272 S33: -0.0088
REMARK 3 TLS GROUP : 49
REMARK 3 SELECTION: CHAIN 'L' AND (RESID 42 THROUGH 46 )
REMARK 3 ORIGIN FOR THE GROUP (A): 398.3513 30.5504 88.8106
REMARK 3 T TENSOR
REMARK 3 T11: 2.3041 T22: 2.1856
REMARK 3 T33: 2.2886 T12: 0.1396
REMARK 3 T13: 0.0930 T23: -0.0333
REMARK 3 L TENSOR
REMARK 3 L11: 0.0003 L22: 0.0366
REMARK 3 L33: 0.0087 L12: 0.0041
REMARK 3 L13: 0.0001 L23: 0.0007
REMARK 3 S TENSOR
REMARK 3 S11: -0.1725 S12: -0.1600 S13: -0.5411
REMARK 3 S21: 0.1383 S22: -0.0045 S23: 0.3781
REMARK 3 S31: 0.9408 S32: -0.5887 S33: 0.1560
REMARK 3 TLS GROUP : 50
REMARK 3 SELECTION: CHAIN 'L' AND (RESID 47 THROUGH 70 )
REMARK 3 ORIGIN FOR THE GROUP (A): 411.4427 20.3655 82.8940
REMARK 3 T TENSOR
REMARK 3 T11: 0.5954 T22: 0.7055
REMARK 3 T33: 0.3433 T12: -0.0904
REMARK 3 T13: 0.0255 T23: -0.2030
REMARK 3 L TENSOR
REMARK 3 L11: 2.7556 L22: 2.2475
REMARK 3 L33: 2.3486 L12: -2.1051
REMARK 3 L13: -0.4856 L23: 1.1354
REMARK 3 S TENSOR
REMARK 3 S11: -0.1926 S12: -0.3615 S13: 0.4951
REMARK 3 S21: 0.4948 S22: 0.2373 S23: -0.1428
REMARK 3 S31: -0.5077 S32: -0.1145 S33: 0.0196
REMARK 3 TLS GROUP : 51
REMARK 3 SELECTION: CHAIN 'T' AND (RESID 19 THROUGH 29 )
REMARK 3 ORIGIN FOR THE GROUP (A): 388.3912 7.3169 57.2379
REMARK 3 T TENSOR
REMARK 3 T11: 1.0498 T22: 0.9442
REMARK 3 T33: 0.7968 T12: 0.2615
REMARK 3 T13: 0.0015 T23: 0.0345
REMARK 3 L TENSOR
REMARK 3 L11: 1.8800 L22: 4.2159
REMARK 3 L33: 2.3363 L12: 0.3854
REMARK 3 L13: -0.0369 L23: -0.5840
REMARK 3 S TENSOR
REMARK 3 S11: -0.2760 S12: -0.0098 S13: 0.6048
REMARK 3 S21: 0.1414 S22: -0.0936 S23: 0.5653
REMARK 3 S31: -0.7052 S32: -0.7983 S33: 0.3568
REMARK 3 TLS GROUP : 52
REMARK 3 SELECTION: CHAIN 'R' AND (RESID 1 THROUGH 8 )
REMARK 3 ORIGIN FOR THE GROUP (A): 390.8726 8.5427 54.2398
REMARK 3 T TENSOR
REMARK 3 T11: 0.8570 T22: 0.7387
REMARK 3 T33: 0.9199 T12: -0.0007
REMARK 3 T13: 0.1447 T23: 0.0288
REMARK 3 L TENSOR
REMARK 3 L11: 1.0613 L22: 5.1171
REMARK 3 L33: 2.2553 L12: -0.3910
REMARK 3 L13: 1.5347 L23: -0.1372
REMARK 3 S TENSOR
REMARK 3 S11: -0.2681 S12: -0.1124 S13: -0.0077
REMARK 3 S21: 0.7757 S22: 0.0119 S23: 0.6450
REMARK 3 S31: -0.4368 S32: -0.5216 S33: 0.1584
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 6BLO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-NOV-17.
REMARK 100 THE DEPOSITION ID IS D_1000231068.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-SEP-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.2.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 83242
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.400
REMARK 200 RESOLUTION RANGE LOW (A) : 63.500
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: NULL
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 66.83
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.71
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 390MM (NH4)2HPO4/NAH2PO4, PH 6.5, 50MM
REMARK 280 DIOXANE, 10MM DTT, 9-12% PEG6000, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 84.27500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 111.14000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 84.27500
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 111.14000
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 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: 60480 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 136610 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -356.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, E, F, H, I, J, K, L,
REMARK 350 AND CHAINS: T, 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 MET A 1
REMARK 465 VAL A 2
REMARK 465 GLU A 149
REMARK 465 THR A 150
REMARK 465 ASP A 151
REMARK 465 VAL A 152
REMARK 465 PRO A 153
REMARK 465 SER A 154
REMARK 465 GLU A 155
REMARK 465 ASP A 156
REMARK 465 ASP A 157
REMARK 465 PRO A 158
REMARK 465 THR A 159
REMARK 465 GLN A 160
REMARK 465 LEU A 161
REMARK 465 VAL A 162
REMARK 465 SER A 163
REMARK 465 ARG A 164
REMARK 465 LYS A 186
REMARK 465 LYS A 187
REMARK 465 ASP A 188
REMARK 465 ARG A 189
REMARK 465 ALA A 190
REMARK 465 THR A 191
REMARK 465 GLY A 192
REMARK 465 ASP A 193
REMARK 465 ALA A 194
REMARK 465 ASP A 195
REMARK 465 GLU A 196
REMARK 465 PRO A 197
REMARK 465 GLU A 198
REMARK 465 LEU A 199
REMARK 465 ARG A 200
REMARK 465 SER A 251
REMARK 465 PHE A 252
REMARK 465 ASN A 253
REMARK 465 GLU A 254
REMARK 465 SER A 255
REMARK 465 GLN A 256
REMARK 465 ARG A 257
REMARK 465 GLY A 258
REMARK 465 LEU A 1081
REMARK 465 ASN A 1082
REMARK 465 THR A 1083
REMARK 465 PHE A 1084
REMARK 465 HIS A 1085
REMARK 465 PHE A 1086
REMARK 465 ALA A 1087
REMARK 465 GLY A 1088
REMARK 465 VAL A 1089
REMARK 465 ALA A 1090
REMARK 465 SER A 1091
REMARK 465 LYS A 1092
REMARK 465 LEU A 1176
REMARK 465 LEU A 1177
REMARK 465 ASP A 1178
REMARK 465 GLU A 1179
REMARK 465 GLU A 1180
REMARK 465 ALA A 1181
REMARK 465 GLU A 1182
REMARK 465 GLN A 1183
REMARK 465 SER A 1184
REMARK 465 PHE A 1185
REMARK 465 ASP A 1186
REMARK 465 ARG A 1244
REMARK 465 PRO A 1245
REMARK 465 LYS A 1246
REMARK 465 SER A 1247
REMARK 465 LEU A 1248
REMARK 465 ASP A 1249
REMARK 465 ALA A 1250
REMARK 465 GLU A 1251
REMARK 465 THR A 1252
REMARK 465 GLU A 1253
REMARK 465 GLU A 1447
REMARK 465 GLU A 1448
REMARK 465 SER A 1449
REMARK 465 LEU A 1450
REMARK 465 VAL A 1451
REMARK 465 LYS A 1452
REMARK 465 TYR A 1453
REMARK 465 MET A 1454
REMARK 465 PRO A 1455
REMARK 465 GLU A 1456
REMARK 465 GLN A 1457
REMARK 465 LYS A 1458
REMARK 465 ILE A 1459
REMARK 465 THR A 1460
REMARK 465 GLU A 1461
REMARK 465 ILE A 1462
REMARK 465 GLU A 1463
REMARK 465 ASP A 1464
REMARK 465 GLY A 1465
REMARK 465 GLN A 1466
REMARK 465 ASP A 1467
REMARK 465 GLY A 1468
REMARK 465 GLY A 1469
REMARK 465 VAL A 1470
REMARK 465 THR A 1471
REMARK 465 PRO A 1472
REMARK 465 TYR A 1473
REMARK 465 SER A 1474
REMARK 465 ASN A 1475
REMARK 465 GLU A 1476
REMARK 465 SER A 1477
REMARK 465 GLY A 1478
REMARK 465 LEU A 1479
REMARK 465 VAL A 1480
REMARK 465 ASN A 1481
REMARK 465 ALA A 1482
REMARK 465 ASP A 1483
REMARK 465 LEU A 1484
REMARK 465 ASP A 1485
REMARK 465 VAL A 1486
REMARK 465 LYS A 1487
REMARK 465 ASP A 1488
REMARK 465 GLU A 1489
REMARK 465 LEU A 1490
REMARK 465 MET A 1491
REMARK 465 PHE A 1492
REMARK 465 SER A 1493
REMARK 465 PRO A 1494
REMARK 465 LEU A 1495
REMARK 465 VAL A 1496
REMARK 465 ASP A 1497
REMARK 465 SER A 1498
REMARK 465 GLY A 1499
REMARK 465 SER A 1500
REMARK 465 ASN A 1501
REMARK 465 ASP A 1502
REMARK 465 ALA A 1503
REMARK 465 MET A 1504
REMARK 465 ALA A 1505
REMARK 465 GLY A 1506
REMARK 465 GLY A 1507
REMARK 465 PHE A 1508
REMARK 465 THR A 1509
REMARK 465 ALA A 1510
REMARK 465 TYR A 1511
REMARK 465 GLY A 1512
REMARK 465 GLY A 1513
REMARK 465 ALA A 1514
REMARK 465 ASP A 1515
REMARK 465 TYR A 1516
REMARK 465 GLY A 1517
REMARK 465 GLU A 1518
REMARK 465 ALA A 1519
REMARK 465 THR A 1520
REMARK 465 SER A 1521
REMARK 465 PRO A 1522
REMARK 465 PHE A 1523
REMARK 465 GLY A 1524
REMARK 465 ALA A 1525
REMARK 465 TYR A 1526
REMARK 465 GLY A 1527
REMARK 465 GLU A 1528
REMARK 465 ALA A 1529
REMARK 465 PRO A 1530
REMARK 465 THR A 1531
REMARK 465 SER A 1532
REMARK 465 PRO A 1533
REMARK 465 GLY A 1534
REMARK 465 PHE A 1535
REMARK 465 GLY A 1536
REMARK 465 VAL A 1537
REMARK 465 SER A 1538
REMARK 465 SER A 1539
REMARK 465 PRO A 1540
REMARK 465 GLY A 1541
REMARK 465 PHE A 1542
REMARK 465 SER A 1543
REMARK 465 PRO A 1544
REMARK 465 THR A 1545
REMARK 465 SER A 1546
REMARK 465 PRO A 1547
REMARK 465 THR A 1548
REMARK 465 TYR A 1549
REMARK 465 SER A 1550
REMARK 465 PRO A 1551
REMARK 465 THR A 1552
REMARK 465 SER A 1553
REMARK 465 PRO A 1554
REMARK 465 ALA A 1555
REMARK 465 TYR A 1556
REMARK 465 SER A 1557
REMARK 465 PRO A 1558
REMARK 465 THR A 1559
REMARK 465 SER A 1560
REMARK 465 PRO A 1561
REMARK 465 SER A 1562
REMARK 465 TYR A 1563
REMARK 465 SER A 1564
REMARK 465 PRO A 1565
REMARK 465 THR A 1566
REMARK 465 SER A 1567
REMARK 465 PRO A 1568
REMARK 465 SER A 1569
REMARK 465 TYR A 1570
REMARK 465 SER A 1571
REMARK 465 PRO A 1572
REMARK 465 THR A 1573
REMARK 465 SER A 1574
REMARK 465 PRO A 1575
REMARK 465 SER A 1576
REMARK 465 TYR A 1577
REMARK 465 SER A 1578
REMARK 465 PRO A 1579
REMARK 465 THR A 1580
REMARK 465 SER A 1581
REMARK 465 PRO A 1582
REMARK 465 SER A 1583
REMARK 465 TYR A 1584
REMARK 465 SER A 1585
REMARK 465 PRO A 1586
REMARK 465 THR A 1587
REMARK 465 SER A 1588
REMARK 465 PRO A 1589
REMARK 465 SER A 1590
REMARK 465 TYR A 1591
REMARK 465 SER A 1592
REMARK 465 PRO A 1593
REMARK 465 THR A 1594
REMARK 465 SER A 1595
REMARK 465 PRO A 1596
REMARK 465 SER A 1597
REMARK 465 TYR A 1598
REMARK 465 SER A 1599
REMARK 465 PRO A 1600
REMARK 465 THR A 1601
REMARK 465 SER A 1602
REMARK 465 PRO A 1603
REMARK 465 SER A 1604
REMARK 465 TYR A 1605
REMARK 465 SER A 1606
REMARK 465 PRO A 1607
REMARK 465 THR A 1608
REMARK 465 SER A 1609
REMARK 465 PRO A 1610
REMARK 465 SER A 1611
REMARK 465 TYR A 1612
REMARK 465 SER A 1613
REMARK 465 PRO A 1614
REMARK 465 THR A 1615
REMARK 465 SER A 1616
REMARK 465 PRO A 1617
REMARK 465 SER A 1618
REMARK 465 TYR A 1619
REMARK 465 SER A 1620
REMARK 465 PRO A 1621
REMARK 465 THR A 1622
REMARK 465 SER A 1623
REMARK 465 PRO A 1624
REMARK 465 SER A 1625
REMARK 465 TYR A 1626
REMARK 465 SER A 1627
REMARK 465 PRO A 1628
REMARK 465 THR A 1629
REMARK 465 SER A 1630
REMARK 465 PRO A 1631
REMARK 465 SER A 1632
REMARK 465 TYR A 1633
REMARK 465 SER A 1634
REMARK 465 PRO A 1635
REMARK 465 THR A 1636
REMARK 465 SER A 1637
REMARK 465 PRO A 1638
REMARK 465 SER A 1639
REMARK 465 TYR A 1640
REMARK 465 SER A 1641
REMARK 465 PRO A 1642
REMARK 465 THR A 1643
REMARK 465 SER A 1644
REMARK 465 PRO A 1645
REMARK 465 SER A 1646
REMARK 465 TYR A 1647
REMARK 465 SER A 1648
REMARK 465 PRO A 1649
REMARK 465 THR A 1650
REMARK 465 SER A 1651
REMARK 465 PRO A 1652
REMARK 465 SER A 1653
REMARK 465 TYR A 1654
REMARK 465 SER A 1655
REMARK 465 PRO A 1656
REMARK 465 THR A 1657
REMARK 465 SER A 1658
REMARK 465 PRO A 1659
REMARK 465 ALA A 1660
REMARK 465 TYR A 1661
REMARK 465 SER A 1662
REMARK 465 PRO A 1663
REMARK 465 THR A 1664
REMARK 465 SER A 1665
REMARK 465 PRO A 1666
REMARK 465 SER A 1667
REMARK 465 TYR A 1668
REMARK 465 SER A 1669
REMARK 465 PRO A 1670
REMARK 465 THR A 1671
REMARK 465 SER A 1672
REMARK 465 PRO A 1673
REMARK 465 SER A 1674
REMARK 465 TYR A 1675
REMARK 465 SER A 1676
REMARK 465 PRO A 1677
REMARK 465 THR A 1678
REMARK 465 SER A 1679
REMARK 465 PRO A 1680
REMARK 465 SER A 1681
REMARK 465 TYR A 1682
REMARK 465 SER A 1683
REMARK 465 PRO A 1684
REMARK 465 THR A 1685
REMARK 465 SER A 1686
REMARK 465 PRO A 1687
REMARK 465 SER A 1688
REMARK 465 TYR A 1689
REMARK 465 SER A 1690
REMARK 465 PRO A 1691
REMARK 465 THR A 1692
REMARK 465 SER A 1693
REMARK 465 PRO A 1694
REMARK 465 ASN A 1695
REMARK 465 TYR A 1696
REMARK 465 SER A 1697
REMARK 465 PRO A 1698
REMARK 465 THR A 1699
REMARK 465 SER A 1700
REMARK 465 PRO A 1701
REMARK 465 SER A 1702
REMARK 465 TYR A 1703
REMARK 465 SER A 1704
REMARK 465 PRO A 1705
REMARK 465 THR A 1706
REMARK 465 SER A 1707
REMARK 465 PRO A 1708
REMARK 465 GLY A 1709
REMARK 465 TYR A 1710
REMARK 465 SER A 1711
REMARK 465 PRO A 1712
REMARK 465 GLY A 1713
REMARK 465 SER A 1714
REMARK 465 PRO A 1715
REMARK 465 ALA A 1716
REMARK 465 TYR A 1717
REMARK 465 SER A 1718
REMARK 465 PRO A 1719
REMARK 465 LYS A 1720
REMARK 465 GLN A 1721
REMARK 465 ASP A 1722
REMARK 465 GLU A 1723
REMARK 465 GLN A 1724
REMARK 465 LYS A 1725
REMARK 465 HIS A 1726
REMARK 465 ASN A 1727
REMARK 465 GLU A 1728
REMARK 465 ASN A 1729
REMARK 465 GLU A 1730
REMARK 465 ASN A 1731
REMARK 465 SER A 1732
REMARK 465 ARG A 1733
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 ASP B 3
REMARK 465 LEU B 4
REMARK 465 ALA B 5
REMARK 465 ASN B 6
REMARK 465 SER B 7
REMARK 465 GLU B 8
REMARK 465 LYS B 9
REMARK 465 TYR B 10
REMARK 465 TYR B 11
REMARK 465 ASP B 12
REMARK 465 GLU B 13
REMARK 465 ASP B 14
REMARK 465 PRO B 15
REMARK 465 TYR B 16
REMARK 465 GLY B 17
REMARK 465 PHE B 18
REMARK 465 GLU B 19
REMARK 465 LEU B 71
REMARK 465 GLU B 72
REMARK 465 GLN B 73
REMARK 465 LEU B 74
REMARK 465 ALA B 75
REMARK 465 GLN B 76
REMARK 465 HIS B 77
REMARK 465 THR B 78
REMARK 465 THR B 79
REMARK 465 GLU B 80
REMARK 465 SER B 81
REMARK 465 ASP B 82
REMARK 465 ASN B 83
REMARK 465 ILE B 84
REMARK 465 SER B 85
REMARK 465 ARG B 86
REMARK 465 LYS B 87
REMARK 465 TYR B 88
REMARK 465 ARG B 135
REMARK 465 THR B 136
REMARK 465 TYR B 137
REMARK 465 GLU B 138
REMARK 465 ALA B 139
REMARK 465 ILE B 140
REMARK 465 ASP B 141
REMARK 465 VAL B 142
REMARK 465 PRO B 143
REMARK 465 GLY B 144
REMARK 465 ARG B 145
REMARK 465 GLU B 146
REMARK 465 LEU B 147
REMARK 465 LYS B 148
REMARK 465 TYR B 149
REMARK 465 GLU B 150
REMARK 465 LEU B 151
REMARK 465 ILE B 152
REMARK 465 ALA B 153
REMARK 465 GLU B 154
REMARK 465 GLU B 155
REMARK 465 SER B 156
REMARK 465 GLU B 157
REMARK 465 ASP B 158
REMARK 465 ASP B 159
REMARK 465 SER B 160
REMARK 465 GLU B 161
REMARK 465 SER B 162
REMARK 465 GLY B 163
REMARK 465 LEU B 244
REMARK 465 GLU B 245
REMARK 465 LYS B 246
REMARK 465 GLY B 247
REMARK 465 SER B 248
REMARK 465 ARG B 249
REMARK 465 PHE B 250
REMARK 465 THR B 339
REMARK 465 ALA B 340
REMARK 465 LEU B 341
REMARK 465 GLY B 342
REMARK 465 ILE B 343
REMARK 465 LYS B 344
REMARK 465 VAL B 436
REMARK 465 GLU B 437
REMARK 465 GLU B 438
REMARK 465 ALA B 439
REMARK 465 HIS B 440
REMARK 465 ASP B 441
REMARK 465 PHE B 442
REMARK 465 ASN B 443
REMARK 465 MET B 444
REMARK 465 LYS B 445
REMARK 465 GLY B 503
REMARK 465 ARG B 504
REMARK 465 ASP B 505
REMARK 465 GLY B 506
REMARK 465 LYS B 507
REMARK 465 LEU B 508
REMARK 465 ILE B 669
REMARK 465 GLU B 670
REMARK 465 GLY B 671
REMARK 465 GLY B 672
REMARK 465 PHE B 673
REMARK 465 GLU B 674
REMARK 465 ASP B 675
REMARK 465 VAL B 676
REMARK 465 GLU B 677
REMARK 465 ALA B 713
REMARK 465 GLU B 714
REMARK 465 ALA B 715
REMARK 465 ASN B 716
REMARK 465 GLU B 717
REMARK 465 GLU B 718
REMARK 465 ASN B 719
REMARK 465 ASP B 720
REMARK 465 LEU B 721
REMARK 465 SER B 919
REMARK 465 PRO B 920
REMARK 465 ASP B 921
REMARK 465 GLU B 922
REMARK 465 GLU B 923
REMARK 465 GLU B 924
REMARK 465 LEU B 925
REMARK 465 GLY B 926
REMARK 465 GLN B 927
REMARK 465 ARG B 928
REMARK 465 SER B 1221
REMARK 465 ARG B 1222
REMARK 465 ASP B 1223
REMARK 465 PHE B 1224
REMARK 465 MET C 1
REMARK 465 SER C 2
REMARK 465 LYS C 269
REMARK 465 VAL C 270
REMARK 465 ASN C 271
REMARK 465 PHE C 272
REMARK 465 ALA C 273
REMARK 465 SER C 274
REMARK 465 GLY C 275
REMARK 465 ASP C 276
REMARK 465 ASN C 277
REMARK 465 ASN C 278
REMARK 465 THR C 279
REMARK 465 ALA C 280
REMARK 465 SER C 281
REMARK 465 ASN C 282
REMARK 465 MET C 283
REMARK 465 LEU C 284
REMARK 465 GLY C 285
REMARK 465 SER C 286
REMARK 465 ASN C 287
REMARK 465 GLU C 288
REMARK 465 ASP C 289
REMARK 465 VAL C 290
REMARK 465 MET C 291
REMARK 465 MET C 292
REMARK 465 THR C 293
REMARK 465 GLY C 294
REMARK 465 ALA C 295
REMARK 465 GLU C 296
REMARK 465 GLN C 297
REMARK 465 ASP C 298
REMARK 465 PRO C 299
REMARK 465 TYR C 300
REMARK 465 SER C 301
REMARK 465 ASN C 302
REMARK 465 ALA C 303
REMARK 465 SER C 304
REMARK 465 GLN C 305
REMARK 465 MET C 306
REMARK 465 GLY C 307
REMARK 465 ASN C 308
REMARK 465 THR C 309
REMARK 465 GLY C 310
REMARK 465 SER C 311
REMARK 465 GLY C 312
REMARK 465 GLY C 313
REMARK 465 TYR C 314
REMARK 465 ASP C 315
REMARK 465 ASN C 316
REMARK 465 ALA C 317
REMARK 465 TRP C 318
REMARK 465 MET E 1
REMARK 465 ASP E 2
REMARK 465 MET F 1
REMARK 465 SER F 2
REMARK 465 ASP F 3
REMARK 465 TYR F 4
REMARK 465 GLU F 5
REMARK 465 GLU F 6
REMARK 465 ALA F 7
REMARK 465 PHE F 8
REMARK 465 ASN F 9
REMARK 465 ASP F 10
REMARK 465 GLY F 11
REMARK 465 ASN F 12
REMARK 465 GLU F 13
REMARK 465 ASN F 14
REMARK 465 PHE F 15
REMARK 465 GLU F 16
REMARK 465 ASP F 17
REMARK 465 PHE F 18
REMARK 465 ASP F 19
REMARK 465 VAL F 20
REMARK 465 GLU F 21
REMARK 465 HIS F 22
REMARK 465 PHE F 23
REMARK 465 SER F 24
REMARK 465 ASP F 25
REMARK 465 GLU F 26
REMARK 465 GLU F 27
REMARK 465 THR F 28
REMARK 465 TYR F 29
REMARK 465 GLU F 30
REMARK 465 GLU F 31
REMARK 465 LYS F 32
REMARK 465 PRO F 33
REMARK 465 GLN F 34
REMARK 465 PHE F 35
REMARK 465 LYS F 36
REMARK 465 ASP F 37
REMARK 465 GLY F 38
REMARK 465 GLU F 39
REMARK 465 THR F 40
REMARK 465 THR F 41
REMARK 465 ASP F 42
REMARK 465 ALA F 43
REMARK 465 ASN F 44
REMARK 465 GLY F 45
REMARK 465 LYS F 46
REMARK 465 THR F 47
REMARK 465 ILE F 48
REMARK 465 VAL F 49
REMARK 465 THR F 50
REMARK 465 GLY F 51
REMARK 465 GLY F 52
REMARK 465 ASN F 53
REMARK 465 GLY F 54
REMARK 465 PRO F 55
REMARK 465 GLU F 56
REMARK 465 ASP F 57
REMARK 465 PHE F 58
REMARK 465 GLN F 59
REMARK 465 GLN F 60
REMARK 465 HIS F 61
REMARK 465 GLU F 62
REMARK 465 GLN F 63
REMARK 465 ILE F 64
REMARK 465 ARG F 65
REMARK 465 ARG F 66
REMARK 465 LYS F 67
REMARK 465 THR F 68
REMARK 465 LEU F 69
REMARK 465 LYS F 70
REMARK 465 GLU F 71
REMARK 465 MET H 1
REMARK 465 SER H 2
REMARK 465 ASN H 64
REMARK 465 LEU H 65
REMARK 465 GLU H 66
REMARK 465 ASP H 67
REMARK 465 THR H 68
REMARK 465 PRO H 69
REMARK 465 ALA H 70
REMARK 465 ASN H 71
REMARK 465 ASP H 72
REMARK 465 SER H 73
REMARK 465 SER H 74
REMARK 465 ALA H 75
REMARK 465 ARG H 130
REMARK 465 ASN H 131
REMARK 465 MET I 1
REMARK 465 LYS I 117
REMARK 465 ARG I 118
REMARK 465 THR I 119
REMARK 465 GLN I 120
REMARK 465 PHE I 121
REMARK 465 SER I 122
REMARK 465 LEU J 66
REMARK 465 GLU J 67
REMARK 465 LYS J 68
REMARK 465 ARG J 69
REMARK 465 ASP J 70
REMARK 465 ALA K 115
REMARK 465 ALA K 116
REMARK 465 ASP K 117
REMARK 465 ASP K 118
REMARK 465 ALA K 119
REMARK 465 PHE K 120
REMARK 465 MET L 1
REMARK 465 SER L 2
REMARK 465 ARG L 3
REMARK 465 GLU L 4
REMARK 465 GLY L 5
REMARK 465 PHE L 6
REMARK 465 GLN L 7
REMARK 465 ILE L 8
REMARK 465 PRO L 9
REMARK 465 THR L 10
REMARK 465 ASN L 11
REMARK 465 LEU L 12
REMARK 465 ASP L 13
REMARK 465 ALA L 14
REMARK 465 ALA L 15
REMARK 465 ALA L 16
REMARK 465 ALA L 17
REMARK 465 GLY L 18
REMARK 465 THR L 19
REMARK 465 SER L 20
REMARK 465 GLN L 21
REMARK 465 ALA L 22
REMARK 465 ARG L 23
REMARK 465 THR L 24
REMARK 465 ALA L 25
REMARK 465 THR L 26
REMARK 465 DC T 1
REMARK 465 DT T 2
REMARK 465 DA T 3
REMARK 465 DC T 4
REMARK 465 DC T 5
REMARK 465 DG T 6
REMARK 465 DA T 7
REMARK 465 DT T 8
REMARK 465 DA T 9
REMARK 465 DA T 10
REMARK 465 DG T 11
REMARK 465 DC T 12
REMARK 465 DA T 13
REMARK 465 DG T 14
REMARK 465 DA T 15
REMARK 465 DG T 16
REMARK 465 DG T 17
REMARK 465 DC T 18
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 GLN A 4 -100.87 -125.71
REMARK 500 THR A 40 -89.87 -69.43
REMARK 500 ALA A 48 -155.17 -143.08
REMARK 500 ASP A 62 24.11 -159.66
REMARK 500 CYS A 67 94.46 -166.08
REMARK 500 THR A 69 -28.35 62.39
REMARK 500 GLN A 71 -126.57 59.39
REMARK 500 PRO A 78 -147.66 -71.15
REMARK 500 HIS A 109 -58.02 61.23
REMARK 500 CYS A 110 -87.71 -64.45
REMARK 500 ASP A 116 -153.94 -120.59
REMARK 500 CYS A 142 -13.27 -160.58
REMARK 500 SER A 215 -174.02 63.21
REMARK 500 LEU A 222 44.31 -146.42
REMARK 500 GLU A 226 -73.46 -72.37
REMARK 500 ASN A 282 -145.26 -95.41
REMARK 500 HIS A 287 35.86 -94.54
REMARK 500 ALA A 288 -35.49 -133.33
REMARK 500 PRO A 312 105.47 -59.34
REMARK 500 ALA A 314 76.74 51.87
REMARK 500 GLN A 316 -164.87 -111.33
REMARK 500 VAL A 322 146.36 67.43
REMARK 500 ASN A 397 -32.34 62.94
REMARK 500 TYR A 465 158.74 65.72
REMARK 500 SER A 466 42.07 -101.08
REMARK 500 ASN A 479 70.65 50.94
REMARK 500 ASP A 481 -159.27 -110.52
REMARK 500 ASP A 483 37.24 -84.75
REMARK 500 ASN A 517 42.53 35.60
REMARK 500 GLN A 525 -126.08 55.28
REMARK 500 ASP A 555 35.36 -94.06
REMARK 500 ASP A 592 -113.22 -87.59
REMARK 500 GLU A 593 -87.78 -91.78
REMARK 500 LEU A 597 -1.28 60.93
REMARK 500 SER A 599 81.74 42.82
REMARK 500 GLU A 618 -144.29 -145.68
REMARK 500 SER A 624 59.54 -92.68
REMARK 500 GLU A 636 -63.47 -98.44
REMARK 500 ALA A 763 -71.41 -114.44
REMARK 500 ILE A 775 109.37 -46.48
REMARK 500 ASP A 781 17.27 59.33
REMARK 500 ASN A 858 -155.02 -123.48
REMARK 500 ASP A 871 -21.12 -148.58
REMARK 500 HIS A 877 46.16 -93.44
REMARK 500 HIS A 906 37.01 -96.25
REMARK 500 VAL A 958 101.34 61.35
REMARK 500 GLN A 968 38.51 -80.35
REMARK 500 GLN A 969 -38.32 -149.34
REMARK 500 ASP A 980 47.17 -83.99
REMARK 500 LEU A 997 69.91 -67.41
REMARK 500
REMARK 500 THIS ENTRY HAS 175 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 A1802 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 67 SG
REMARK 620 2 CYS A 70 SG 122.8
REMARK 620 3 CYS A 77 SG 92.3 100.3
REMARK 620 4 HIS A 80 NE2 130.4 106.5 72.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A1801 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 110 SG
REMARK 620 2 CYS A 167 O 153.2
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1803 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 481 OD1
REMARK 620 2 ASP A 483 OD1 74.3
REMARK 620 3 ASP A 485 OD1 92.7 78.4
REMARK 620 4 G R 8 O3' 132.7 151.7 104.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B1301 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B1163 SG
REMARK 620 2 CYS B1166 SG 108.3
REMARK 620 3 CYS B1182 SG 84.7 143.5
REMARK 620 4 CYS B1185 SG 108.4 96.7 111.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C 401 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 86 SG
REMARK 620 2 CYS C 88 SG 96.5
REMARK 620 3 CYS C 92 SG 93.8 98.0
REMARK 620 4 CYS C 95 SG 140.7 114.4 104.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN I 201 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS I 7 SG
REMARK 620 2 CYS I 10 SG 111.5
REMARK 620 3 CYS I 29 SG 103.3 135.9
REMARK 620 4 CYS I 32 SG 95.3 100.1 102.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN I 202 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS I 75 SG
REMARK 620 2 CYS I 78 SG 119.1
REMARK 620 3 CYS I 103 SG 103.8 98.2
REMARK 620 4 CYS I 106 SG 114.8 103.2 117.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN J 101 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS J 7 SG
REMARK 620 2 CYS J 10 SG 102.4
REMARK 620 3 CYS J 45 SG 118.0 131.2
REMARK 620 4 CYS J 46 SG 105.4 96.8 97.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN L 101 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS L 31 SG
REMARK 620 2 CYS L 34 SG 85.1
REMARK 620 3 CYS L 48 SG 95.8 114.1
REMARK 620 4 CYS L 51 SG 101.7 116.5 127.4
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 1801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 1802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1803
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 1301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN I 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN I 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN J 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN L 101
DBREF 6BLO A 1 1733 UNP P04050 RPB1_YEAST 1 1733
DBREF 6BLO B 1 1224 UNP P08518 RPB2_YEAST 1 1224
DBREF 6BLO C 1 318 UNP P16370 RPB3_YEAST 1 318
DBREF 6BLO E 1 215 UNP P20434 RPAB1_YEAST 1 215
DBREF 6BLO F 1 155 UNP P20435 RPAB2_YEAST 1 155
DBREF 6BLO H 1 146 UNP P20436 RPAB3_YEAST 1 146
DBREF 6BLO I 1 122 UNP P27999 RPB9_YEAST 1 122
DBREF 6BLO J 1 70 UNP P22139 RPAB5_YEAST 1 70
DBREF 6BLO K 1 120 UNP P38902 RPB11_YEAST 1 120
DBREF 6BLO L 1 70 UNP P40422 RPAB4_YEAST 1 70
DBREF 6BLO T 1 29 PDB 6BLO 6BLO 1 29
DBREF 6BLO R 1 8 PDB 6BLO 6BLO 1 8
SEQRES 1 A 1733 MET VAL GLY GLN GLN TYR SER SER ALA PRO LEU ARG THR
SEQRES 2 A 1733 VAL LYS GLU VAL GLN PHE GLY LEU PHE SER PRO GLU GLU
SEQRES 3 A 1733 VAL ARG ALA ILE SER VAL ALA LYS ILE ARG PHE PRO GLU
SEQRES 4 A 1733 THR MET ASP GLU THR GLN THR ARG ALA LYS ILE GLY GLY
SEQRES 5 A 1733 LEU ASN ASP PRO ARG LEU GLY SER ILE ASP ARG ASN LEU
SEQRES 6 A 1733 LYS CYS GLN THR CYS GLN GLU GLY MET ASN GLU CYS PRO
SEQRES 7 A 1733 GLY HIS PHE GLY HIS ILE ASP LEU ALA LYS PRO VAL PHE
SEQRES 8 A 1733 HIS VAL GLY PHE ILE ALA LYS ILE LYS LYS VAL CYS GLU
SEQRES 9 A 1733 CYS VAL CYS MET HIS CYS GLY LYS LEU LEU LEU ASP GLU
SEQRES 10 A 1733 HIS ASN GLU LEU MET ARG GLN ALA LEU ALA ILE LYS ASP
SEQRES 11 A 1733 SER LYS LYS ARG PHE ALA ALA ILE TRP THR LEU CYS LYS
SEQRES 12 A 1733 THR LYS MET VAL CYS GLU THR ASP VAL PRO SER GLU ASP
SEQRES 13 A 1733 ASP PRO THR GLN LEU VAL SER ARG GLY GLY CYS GLY ASN
SEQRES 14 A 1733 THR GLN PRO THR ILE ARG LYS ASP GLY LEU LYS LEU VAL
SEQRES 15 A 1733 GLY SER TRP LYS LYS ASP ARG ALA THR GLY ASP ALA ASP
SEQRES 16 A 1733 GLU PRO GLU LEU ARG VAL LEU SER THR GLU GLU ILE LEU
SEQRES 17 A 1733 ASN ILE PHE LYS HIS ILE SER VAL LYS ASP PHE THR SER
SEQRES 18 A 1733 LEU GLY PHE ASN GLU VAL PHE SER ARG PRO GLU TRP MET
SEQRES 19 A 1733 ILE LEU THR CYS LEU PRO VAL PRO PRO PRO PRO VAL ARG
SEQRES 20 A 1733 PRO SER ILE SER PHE ASN GLU SER GLN ARG GLY GLU ASP
SEQRES 21 A 1733 ASP LEU THR PHE LYS LEU ALA ASP ILE LEU LYS ALA ASN
SEQRES 22 A 1733 ILE SER LEU GLU THR LEU GLU HIS ASN GLY ALA PRO HIS
SEQRES 23 A 1733 HIS ALA ILE GLU GLU ALA GLU SER LEU LEU GLN PHE HIS
SEQRES 24 A 1733 VAL ALA THR TYR MET ASP ASN ASP ILE ALA GLY GLN PRO
SEQRES 25 A 1733 GLN ALA LEU GLN LYS SER GLY ARG PRO VAL LYS SER ILE
SEQRES 26 A 1733 ARG ALA ARG LEU LYS GLY LYS GLU GLY ARG ILE ARG GLY
SEQRES 27 A 1733 ASN LEU MET GLY LYS ARG VAL ASP PHE SER ALA ARG THR
SEQRES 28 A 1733 VAL ILE SER GLY ASP PRO ASN LEU GLU LEU ASP GLN VAL
SEQRES 29 A 1733 GLY VAL PRO LYS SER ILE ALA LYS THR LEU THR TYR PRO
SEQRES 30 A 1733 GLU VAL VAL THR PRO TYR ASN ILE ASP ARG LEU THR GLN
SEQRES 31 A 1733 LEU VAL ARG ASN GLY PRO ASN GLU HIS PRO GLY ALA LYS
SEQRES 32 A 1733 TYR VAL ILE ARG ASP SER GLY ASP ARG ILE ASP LEU ARG
SEQRES 33 A 1733 TYR SER LYS ARG ALA GLY ASP ILE GLN LEU GLN TYR GLY
SEQRES 34 A 1733 TRP LYS VAL GLU ARG HIS ILE MET ASP ASN ASP PRO VAL
SEQRES 35 A 1733 LEU PHE ASN ARG GLN PRO SER LEU HIS LYS MET SER MET
SEQRES 36 A 1733 MET ALA HIS ARG VAL LYS VAL ILE PRO TYR SER THR PHE
SEQRES 37 A 1733 ARG LEU ASN LEU SER VAL THR SER PRO TYR ASN ALA ASP
SEQRES 38 A 1733 PHE ASP GLY ASP GLU MET ASN LEU HIS VAL PRO GLN SER
SEQRES 39 A 1733 GLU GLU THR ARG ALA GLU LEU SER GLN LEU CYS ALA VAL
SEQRES 40 A 1733 PRO LEU GLN ILE VAL SER PRO GLN SER ASN LYS PRO CYS
SEQRES 41 A 1733 MET GLY ILE VAL GLN ASP THR LEU CYS GLY ILE ARG LYS
SEQRES 42 A 1733 LEU THR LEU ARG ASP THR PHE ILE GLU LEU ASP GLN VAL
SEQRES 43 A 1733 LEU ASN MET LEU TYR TRP VAL PRO ASP TRP ASP GLY VAL
SEQRES 44 A 1733 ILE PRO THR PRO ALA ILE ILE LYS PRO LYS PRO LEU TRP
SEQRES 45 A 1733 SER GLY LYS GLN ILE LEU SER VAL ALA ILE PRO ASN GLY
SEQRES 46 A 1733 ILE HIS LEU GLN ARG PHE ASP GLU GLY THR THR LEU LEU
SEQRES 47 A 1733 SER PRO LYS ASP ASN GLY MET LEU ILE ILE ASP GLY GLN
SEQRES 48 A 1733 ILE ILE PHE GLY VAL VAL GLU LYS LYS THR VAL GLY SER
SEQRES 49 A 1733 SER ASN GLY GLY LEU ILE HIS VAL VAL THR ARG GLU LYS
SEQRES 50 A 1733 GLY PRO GLN VAL CYS ALA LYS LEU PHE GLY ASN ILE GLN
SEQRES 51 A 1733 LYS VAL VAL ASN PHE TRP LEU LEU HIS ASN GLY PHE SER
SEQRES 52 A 1733 THR GLY ILE GLY ASP THR ILE ALA ASP GLY PRO THR MET
SEQRES 53 A 1733 ARG GLU ILE THR GLU THR ILE ALA GLU ALA LYS LYS LYS
SEQRES 54 A 1733 VAL LEU ASP VAL THR LYS GLU ALA GLN ALA ASN LEU LEU
SEQRES 55 A 1733 THR ALA LYS HIS GLY MET THR LEU ARG GLU SER PHE GLU
SEQRES 56 A 1733 ASP ASN VAL VAL ARG PHE LEU ASN GLU ALA ARG ASP LYS
SEQRES 57 A 1733 ALA GLY ARG LEU ALA GLU VAL ASN LEU LYS ASP LEU ASN
SEQRES 58 A 1733 ASN VAL LYS GLN MET VAL MET ALA GLY SER LYS GLY SER
SEQRES 59 A 1733 PHE ILE ASN ILE ALA GLN MET SER ALA CYS VAL GLY GLN
SEQRES 60 A 1733 GLN SER VAL GLU GLY LYS ARG ILE ALA PHE GLY PHE VAL
SEQRES 61 A 1733 ASP ARG THR LEU PRO HIS PHE SER LYS ASP ASP TYR SER
SEQRES 62 A 1733 PRO GLU SER LYS GLY PHE VAL GLU ASN SER TYR LEU ARG
SEQRES 63 A 1733 GLY LEU THR PRO GLN GLU PHE PHE PHE HIS ALA MET GLY
SEQRES 64 A 1733 GLY ARG GLU GLY LEU ILE ASP THR ALA VAL LYS THR ALA
SEQRES 65 A 1733 GLU THR GLY TYR ILE GLN ARG ARG LEU VAL LYS ALA LEU
SEQRES 66 A 1733 GLU ASP ILE MET VAL HIS TYR ASP ASN THR THR ARG ASN
SEQRES 67 A 1733 SER LEU GLY ASN VAL ILE GLN PHE ILE TYR GLY GLU ASP
SEQRES 68 A 1733 GLY MET ASP ALA ALA HIS ILE GLU LYS GLN SER LEU ASP
SEQRES 69 A 1733 THR ILE GLY GLY SER ASP ALA ALA PHE GLU LYS ARG TYR
SEQRES 70 A 1733 ARG VAL ASP LEU LEU ASN THR ASP HIS THR LEU ASP PRO
SEQRES 71 A 1733 SER LEU LEU GLU SER GLY SER GLU ILE LEU GLY ASP LEU
SEQRES 72 A 1733 LYS LEU GLN VAL LEU LEU ASP GLU GLU TYR LYS GLN LEU
SEQRES 73 A 1733 VAL LYS ASP ARG LYS PHE LEU ARG GLU VAL PHE VAL ASP
SEQRES 74 A 1733 GLY GLU ALA ASN TRP PRO LEU PRO VAL ASN ILE ARG ARG
SEQRES 75 A 1733 ILE ILE GLN ASN ALA GLN GLN THR PHE HIS ILE ASP HIS
SEQRES 76 A 1733 THR LYS PRO SER ASP LEU THR ILE LYS ASP ILE VAL LEU
SEQRES 77 A 1733 GLY VAL LYS ASP LEU GLN GLU ASN LEU LEU VAL LEU ARG
SEQRES 78 A 1733 GLY LYS ASN GLU ILE ILE GLN ASN ALA GLN ARG ASP ALA
SEQRES 79 A 1733 VAL THR LEU PHE CYS CYS LEU LEU ARG SER ARG LEU ALA
SEQRES 80 A 1733 THR ARG ARG VAL LEU GLN GLU TYR ARG LEU THR LYS GLN
SEQRES 81 A 1733 ALA PHE ASP TRP VAL LEU SER ASN ILE GLU ALA GLN PHE
SEQRES 82 A 1733 LEU ARG SER VAL VAL HIS PRO GLY GLU MET VAL GLY VAL
SEQRES 83 A 1733 LEU ALA ALA GLN SER ILE GLY GLU PRO ALA THR GLN MET
SEQRES 84 A 1733 THR LEU ASN THR PHE HIS PHE ALA GLY VAL ALA SER LYS
SEQRES 85 A 1733 LYS VAL THR SER GLY VAL PRO ARG LEU LYS GLU ILE LEU
SEQRES 86 A 1733 ASN VAL ALA LYS ASN MET LYS THR PRO SER LEU THR VAL
SEQRES 87 A 1733 TYR LEU GLU PRO GLY HIS ALA ALA ASP GLN GLU GLN ALA
SEQRES 88 A 1733 LYS LEU ILE ARG SER ALA ILE GLU HIS THR THR LEU LYS
SEQRES 89 A 1733 SER VAL THR ILE ALA SER GLU ILE TYR TYR ASP PRO ASP
SEQRES 90 A 1733 PRO ARG SER THR VAL ILE PRO GLU ASP GLU GLU ILE ILE
SEQRES 91 A 1733 GLN LEU HIS PHE SER LEU LEU ASP GLU GLU ALA GLU GLN
SEQRES 92 A 1733 SER PHE ASP GLN GLN SER PRO TRP LEU LEU ARG LEU GLU
SEQRES 93 A 1733 LEU ASP ARG ALA ALA MET ASN ASP LYS ASP LEU THR MET
SEQRES 94 A 1733 GLY GLN VAL GLY GLU ARG ILE LYS GLN THR PHE LYS ASN
SEQRES 95 A 1733 ASP LEU PHE VAL ILE TRP SER GLU ASP ASN ASP GLU LYS
SEQRES 96 A 1733 LEU ILE ILE ARG CYS ARG VAL VAL ARG PRO LYS SER LEU
SEQRES 97 A 1733 ASP ALA GLU THR GLU ALA GLU GLU ASP HIS MET LEU LYS
SEQRES 98 A 1733 LYS ILE GLU ASN THR MET LEU GLU ASN ILE THR LEU ARG
SEQRES 99 A 1733 GLY VAL GLU ASN ILE GLU ARG VAL VAL MET MET LYS TYR
SEQRES 100 A 1733 ASP ARG LYS VAL PRO SER PRO THR GLY GLU TYR VAL LYS
SEQRES 101 A 1733 GLU PRO GLU TRP VAL LEU GLU THR ASP GLY VAL ASN LEU
SEQRES 102 A 1733 SER GLU VAL MET THR VAL PRO GLY ILE ASP PRO THR ARG
SEQRES 103 A 1733 ILE TYR THR ASN SER PHE ILE ASP ILE MET GLU VAL LEU
SEQRES 104 A 1733 GLY ILE GLU ALA GLY ARG ALA ALA LEU TYR LYS GLU VAL
SEQRES 105 A 1733 TYR ASN VAL ILE ALA SER ASP GLY SER TYR VAL ASN TYR
SEQRES 106 A 1733 ARG HIS MET ALA LEU LEU VAL ASP VAL MET THR THR GLN
SEQRES 107 A 1733 GLY GLY LEU THR SER VAL THR ARG HIS GLY PHE ASN ARG
SEQRES 108 A 1733 SER ASN THR GLY ALA LEU MET ARG CYS SER PHE GLU GLU
SEQRES 109 A 1733 THR VAL GLU ILE LEU PHE GLU ALA GLY ALA SER ALA GLU
SEQRES 110 A 1733 LEU ASP ASP CYS ARG GLY VAL SER GLU ASN VAL ILE LEU
SEQRES 111 A 1733 GLY GLN MET ALA PRO ILE GLY THR GLY ALA PHE ASP VAL
SEQRES 112 A 1733 MET ILE ASP GLU GLU SER LEU VAL LYS TYR MET PRO GLU
SEQRES 113 A 1733 GLN LYS ILE THR GLU ILE GLU ASP GLY GLN ASP GLY GLY
SEQRES 114 A 1733 VAL THR PRO TYR SER ASN GLU SER GLY LEU VAL ASN ALA
SEQRES 115 A 1733 ASP LEU ASP VAL LYS ASP GLU LEU MET PHE SER PRO LEU
SEQRES 116 A 1733 VAL ASP SER GLY SER ASN ASP ALA MET ALA GLY GLY PHE
SEQRES 117 A 1733 THR ALA TYR GLY GLY ALA ASP TYR GLY GLU ALA THR SER
SEQRES 118 A 1733 PRO PHE GLY ALA TYR GLY GLU ALA PRO THR SER PRO GLY
SEQRES 119 A 1733 PHE GLY VAL SER SER PRO GLY PHE SER PRO THR SER PRO
SEQRES 120 A 1733 THR TYR SER PRO THR SER PRO ALA TYR SER PRO THR SER
SEQRES 121 A 1733 PRO SER TYR SER PRO THR SER PRO SER TYR SER PRO THR
SEQRES 122 A 1733 SER PRO SER TYR SER PRO THR SER PRO SER TYR SER PRO
SEQRES 123 A 1733 THR SER PRO SER TYR SER PRO THR SER PRO SER TYR SER
SEQRES 124 A 1733 PRO THR SER PRO SER TYR SER PRO THR SER PRO SER TYR
SEQRES 125 A 1733 SER PRO THR SER PRO SER TYR SER PRO THR SER PRO SER
SEQRES 126 A 1733 TYR SER PRO THR SER PRO SER TYR SER PRO THR SER PRO
SEQRES 127 A 1733 SER TYR SER PRO THR SER PRO SER TYR SER PRO THR SER
SEQRES 128 A 1733 PRO SER TYR SER PRO THR SER PRO ALA TYR SER PRO THR
SEQRES 129 A 1733 SER PRO SER TYR SER PRO THR SER PRO SER TYR SER PRO
SEQRES 130 A 1733 THR SER PRO SER TYR SER PRO THR SER PRO SER TYR SER
SEQRES 131 A 1733 PRO THR SER PRO ASN TYR SER PRO THR SER PRO SER TYR
SEQRES 132 A 1733 SER PRO THR SER PRO GLY TYR SER PRO GLY SER PRO ALA
SEQRES 133 A 1733 TYR SER PRO LYS GLN ASP GLU GLN LYS HIS ASN GLU ASN
SEQRES 134 A 1733 GLU ASN SER ARG
SEQRES 1 B 1224 MET SER ASP LEU ALA ASN SER GLU LYS TYR TYR ASP GLU
SEQRES 2 B 1224 ASP PRO TYR GLY PHE GLU ASP GLU SER ALA PRO ILE THR
SEQRES 3 B 1224 ALA GLU ASP SER TRP ALA VAL ILE SER ALA PHE PHE ARG
SEQRES 4 B 1224 GLU LYS GLY LEU VAL SER GLN GLN LEU ASP SER PHE ASN
SEQRES 5 B 1224 GLN PHE VAL ASP TYR THR LEU GLN ASP ILE ILE CYS GLU
SEQRES 6 B 1224 ASP SER THR LEU ILE LEU GLU GLN LEU ALA GLN HIS THR
SEQRES 7 B 1224 THR GLU SER ASP ASN ILE SER ARG LYS TYR GLU ILE SER
SEQRES 8 B 1224 PHE GLY LYS ILE TYR VAL THR LYS PRO MET VAL ASN GLU
SEQRES 9 B 1224 SER ASP GLY VAL THR HIS ALA LEU TYR PRO GLN GLU ALA
SEQRES 10 B 1224 ARG LEU ARG ASN LEU THR TYR SER SER GLY LEU PHE VAL
SEQRES 11 B 1224 ASP VAL LYS LYS ARG THR TYR GLU ALA ILE ASP VAL PRO
SEQRES 12 B 1224 GLY ARG GLU LEU LYS TYR GLU LEU ILE ALA GLU GLU SER
SEQRES 13 B 1224 GLU ASP ASP SER GLU SER GLY LYS VAL PHE ILE GLY ARG
SEQRES 14 B 1224 LEU PRO ILE MET LEU ARG SER LYS ASN CYS TYR LEU SER
SEQRES 15 B 1224 GLU ALA THR GLU SER ASP LEU TYR LYS LEU LYS GLU CYS
SEQRES 16 B 1224 PRO PHE ASP MET GLY GLY TYR PHE ILE ILE ASN GLY SER
SEQRES 17 B 1224 GLU LYS VAL LEU ILE ALA GLN GLU ARG SER ALA GLY ASN
SEQRES 18 B 1224 ILE VAL GLN VAL PHE LYS LYS ALA ALA PRO SER PRO ILE
SEQRES 19 B 1224 SER HIS VAL ALA GLU ILE ARG SER ALA LEU GLU LYS GLY
SEQRES 20 B 1224 SER ARG PHE ILE SER THR LEU GLN VAL LYS LEU TYR GLY
SEQRES 21 B 1224 ARG GLU GLY SER SER ALA ARG THR ILE LYS ALA THR LEU
SEQRES 22 B 1224 PRO TYR ILE LYS GLN ASP ILE PRO ILE VAL ILE ILE PHE
SEQRES 23 B 1224 ARG ALA LEU GLY ILE ILE PRO ASP GLY GLU ILE LEU GLU
SEQRES 24 B 1224 HIS ILE CYS TYR ASP VAL ASN ASP TRP GLN MET LEU GLU
SEQRES 25 B 1224 MET LEU LYS PRO CYS VAL GLU ASP GLY PHE VAL ILE GLN
SEQRES 26 B 1224 ASP ARG GLU THR ALA LEU ASP PHE ILE GLY ARG ARG GLY
SEQRES 27 B 1224 THR ALA LEU GLY ILE LYS LYS GLU LYS ARG ILE GLN TYR
SEQRES 28 B 1224 ALA LYS ASP ILE LEU GLN LYS GLU PHE LEU PRO HIS ILE
SEQRES 29 B 1224 THR GLN LEU GLU GLY PHE GLU SER ARG LYS ALA PHE PHE
SEQRES 30 B 1224 LEU GLY TYR MET ILE ASN ARG LEU LEU LEU CYS ALA LEU
SEQRES 31 B 1224 ASP ARG LYS ASP GLN ASP ASP ARG ASP HIS PHE GLY LYS
SEQRES 32 B 1224 LYS ARG LEU ASP LEU ALA GLY PRO LEU LEU ALA GLN LEU
SEQRES 33 B 1224 PHE LYS THR LEU PHE LYS LYS LEU THR LYS ASP ILE PHE
SEQRES 34 B 1224 ARG TYR MET GLN ARG THR VAL GLU GLU ALA HIS ASP PHE
SEQRES 35 B 1224 ASN MET LYS LEU ALA ILE ASN ALA LYS THR ILE THR SER
SEQRES 36 B 1224 GLY LEU LYS TYR ALA LEU ALA THR GLY ASN TRP GLY GLU
SEQRES 37 B 1224 GLN LYS LYS ALA MET SER SER ARG ALA GLY VAL SER GLN
SEQRES 38 B 1224 VAL LEU ASN ARG TYR THR TYR SER SER THR LEU SER HIS
SEQRES 39 B 1224 LEU ARG ARG THR ASN THR PRO ILE GLY ARG ASP GLY LYS
SEQRES 40 B 1224 LEU ALA LYS PRO ARG GLN LEU HIS ASN THR HIS TRP GLY
SEQRES 41 B 1224 LEU VAL CYS PRO ALA GLU THR PRO GLU GLY GLN ALA CYS
SEQRES 42 B 1224 GLY LEU VAL LYS ASN LEU SER LEU MET SER CYS ILE SER
SEQRES 43 B 1224 VAL GLY THR ASP PRO MET PRO ILE ILE THR PHE LEU SER
SEQRES 44 B 1224 GLU TRP GLY MET GLU PRO LEU GLU ASP TYR VAL PRO HIS
SEQRES 45 B 1224 GLN SER PRO ASP ALA THR ARG VAL PHE VAL ASN GLY VAL
SEQRES 46 B 1224 TRP HIS GLY VAL HIS ARG ASN PRO ALA ARG LEU MET GLU
SEQRES 47 B 1224 THR LEU ARG THR LEU ARG ARG LYS GLY ASP ILE ASN PRO
SEQRES 48 B 1224 GLU VAL SER MET ILE ARG ASP ILE ARG GLU LYS GLU LEU
SEQRES 49 B 1224 LYS ILE PHE THR ASP ALA GLY ARG VAL TYR ARG PRO LEU
SEQRES 50 B 1224 PHE ILE VAL GLU ASP ASP GLU SER LEU GLY HIS LYS GLU
SEQRES 51 B 1224 LEU LYS VAL ARG LYS GLY HIS ILE ALA LYS LEU MET ALA
SEQRES 52 B 1224 THR GLU TYR GLN ASP ILE GLU GLY GLY PHE GLU ASP VAL
SEQRES 53 B 1224 GLU GLU TYR THR TRP SER SER LEU LEU ASN GLU GLY LEU
SEQRES 54 B 1224 VAL GLU TYR ILE ASP ALA GLU GLU GLU GLU SER ILE LEU
SEQRES 55 B 1224 ILE ALA MET GLN PRO GLU ASP LEU GLU PRO ALA GLU ALA
SEQRES 56 B 1224 ASN GLU GLU ASN ASP LEU ASP VAL ASP PRO ALA LYS ARG
SEQRES 57 B 1224 ILE ARG VAL SER HIS HIS ALA THR THR PHE THR HIS CYS
SEQRES 58 B 1224 GLU ILE HIS PRO SER MET ILE LEU GLY VAL ALA ALA SER
SEQRES 59 B 1224 ILE ILE PRO PHE PRO ASP HIS ASN GLN SER PRO ARG ASN
SEQRES 60 B 1224 THR TYR GLN SER ALA MET GLY LYS GLN ALA MET GLY VAL
SEQRES 61 B 1224 PHE LEU THR ASN TYR ASN VAL ARG MET ASP THR MET ALA
SEQRES 62 B 1224 ASN ILE LEU TYR TYR PRO GLN LYS PRO LEU GLY THR THR
SEQRES 63 B 1224 ARG ALA MET GLU TYR LEU LYS PHE ARG GLU LEU PRO ALA
SEQRES 64 B 1224 GLY GLN ASN ALA ILE VAL ALA ILE ALA CYS TYR SER GLY
SEQRES 65 B 1224 TYR ASN GLN GLU ASP SER MET ILE MET ASN GLN SER SER
SEQRES 66 B 1224 ILE ASP ARG GLY LEU PHE ARG SER LEU PHE PHE ARG SER
SEQRES 67 B 1224 TYR MET ASP GLN GLU LYS LYS TYR GLY MET SER ILE THR
SEQRES 68 B 1224 GLU THR PHE GLU LYS PRO GLN ARG THR ASN THR LEU ARG
SEQRES 69 B 1224 MET LYS HIS GLY THR TYR ASP LYS LEU ASP ASP ASP GLY
SEQRES 70 B 1224 LEU ILE ALA PRO GLY VAL ARG VAL SER GLY GLU ASP VAL
SEQRES 71 B 1224 ILE ILE GLY LYS THR THR PRO ILE SER PRO ASP GLU GLU
SEQRES 72 B 1224 GLU LEU GLY GLN ARG THR ALA TYR HIS SER LYS ARG ASP
SEQRES 73 B 1224 ALA SER THR PRO LEU ARG SER THR GLU ASN GLY ILE VAL
SEQRES 74 B 1224 ASP GLN VAL LEU VAL THR THR ASN GLN ASP GLY LEU LYS
SEQRES 75 B 1224 PHE VAL LYS VAL ARG VAL ARG THR THR LYS ILE PRO GLN
SEQRES 76 B 1224 ILE GLY ASP LYS PHE ALA SER ARG HIS GLY GLN LYS GLY
SEQRES 77 B 1224 THR ILE GLY ILE THR TYR ARG ARG GLU ASP MET PRO PHE
SEQRES 78 B 1224 THR ALA GLU GLY ILE VAL PRO ASP LEU ILE ILE ASN PRO
SEQRES 79 B 1224 HIS ALA ILE PRO SER ARG MET THR VAL ALA HIS LEU ILE
SEQRES 80 B 1224 GLU CYS LEU LEU SER LYS VAL ALA ALA LEU SER GLY ASN
SEQRES 81 B 1224 GLU GLY ASP ALA SER PRO PHE THR ASP ILE THR VAL GLU
SEQRES 82 B 1224 GLY ILE SER LYS LEU LEU ARG GLU HIS GLY TYR GLN SER
SEQRES 83 B 1224 ARG GLY PHE GLU VAL MET TYR ASN GLY HIS THR GLY LYS
SEQRES 84 B 1224 LYS LEU MET ALA GLN ILE PHE PHE GLY PRO THR TYR TYR
SEQRES 85 B 1224 GLN ARG LEU ARG HIS MET VAL ASP ASP LYS ILE HIS ALA
SEQRES 86 B 1224 ARG ALA ARG GLY PRO MET GLN VAL LEU THR ARG GLN PRO
SEQRES 87 B 1224 VAL GLU GLY ARG SER ARG ASP GLY GLY LEU ARG PHE GLY
SEQRES 88 B 1224 GLU MET GLU ARG ASP CYS MET ILE ALA HIS GLY ALA ALA
SEQRES 89 B 1224 SER PHE LEU LYS GLU ARG LEU MET GLU ALA SER ASP ALA
SEQRES 90 B 1224 PHE ARG VAL HIS ILE CYS GLY ILE CYS GLY LEU MET THR
SEQRES 91 B 1224 VAL ILE ALA LYS LEU ASN HIS ASN GLN PHE GLU CYS LYS
SEQRES 92 B 1224 GLY CYS ASP ASN LYS ILE ASP ILE TYR GLN ILE HIS ILE
SEQRES 93 B 1224 PRO TYR ALA ALA LYS LEU LEU PHE GLN GLU LEU MET ALA
SEQRES 94 B 1224 MET ASN ILE THR PRO ARG LEU TYR THR ASP ARG SER ARG
SEQRES 95 B 1224 ASP PHE
SEQRES 1 C 318 MET SER GLU GLU GLY PRO GLN VAL LYS ILE ARG GLU ALA
SEQRES 2 C 318 SER LYS ASP ASN VAL ASP PHE ILE LEU SER ASN VAL ASP
SEQRES 3 C 318 LEU ALA MET ALA ASN SER LEU ARG ARG VAL MET ILE ALA
SEQRES 4 C 318 GLU ILE PRO THR LEU ALA ILE ASP SER VAL GLU VAL GLU
SEQRES 5 C 318 THR ASN THR THR VAL LEU ALA ASP GLU PHE ILE ALA HIS
SEQRES 6 C 318 ARG LEU GLY LEU ILE PRO LEU GLN SER MET ASP ILE GLU
SEQRES 7 C 318 GLN LEU GLU TYR SER ARG ASP CYS PHE CYS GLU ASP HIS
SEQRES 8 C 318 CYS ASP LYS CYS SER VAL VAL LEU THR LEU GLN ALA PHE
SEQRES 9 C 318 GLY GLU SER GLU SER THR THR ASN VAL TYR SER LYS ASP
SEQRES 10 C 318 LEU VAL ILE VAL SER ASN LEU MET GLY ARG ASN ILE GLY
SEQRES 11 C 318 HIS PRO ILE ILE GLN ASP LYS GLU GLY ASN GLY VAL LEU
SEQRES 12 C 318 ILE CYS LYS LEU ARG LYS GLY GLN GLU LEU LYS LEU THR
SEQRES 13 C 318 CYS VAL ALA LYS LYS GLY ILE ALA LYS GLU HIS ALA LYS
SEQRES 14 C 318 TRP GLY PRO ALA ALA ALA ILE GLU PHE GLU TYR ASP PRO
SEQRES 15 C 318 TRP ASN LYS LEU LYS HIS THR ASP TYR TRP TYR GLU GLN
SEQRES 16 C 318 ASP SER ALA LYS GLU TRP PRO GLN SER LYS ASN CYS GLU
SEQRES 17 C 318 TYR GLU ASP PRO PRO ASN GLU GLY ASP PRO PHE ASP TYR
SEQRES 18 C 318 LYS ALA GLN ALA ASP THR PHE TYR MET ASN VAL GLU SER
SEQRES 19 C 318 VAL GLY SER ILE PRO VAL ASP GLN VAL VAL VAL ARG GLY
SEQRES 20 C 318 ILE ASP THR LEU GLN LYS LYS VAL ALA SER ILE LEU LEU
SEQRES 21 C 318 ALA LEU THR GLN MET ASP GLN ASP LYS VAL ASN PHE ALA
SEQRES 22 C 318 SER GLY ASP ASN ASN THR ALA SER ASN MET LEU GLY SER
SEQRES 23 C 318 ASN GLU ASP VAL MET MET THR GLY ALA GLU GLN ASP PRO
SEQRES 24 C 318 TYR SER ASN ALA SER GLN MET GLY ASN THR GLY SER GLY
SEQRES 25 C 318 GLY TYR ASP ASN ALA TRP
SEQRES 1 E 215 MET ASP GLN GLU ASN GLU ARG ASN ILE SER ARG LEU TRP
SEQRES 2 E 215 ARG ALA PHE ARG THR VAL LYS GLU MET VAL LYS ASP ARG
SEQRES 3 E 215 GLY TYR PHE ILE THR GLN GLU GLU VAL GLU LEU PRO LEU
SEQRES 4 E 215 GLU ASP PHE LYS ALA LYS TYR CYS ASP SER MET GLY ARG
SEQRES 5 E 215 PRO GLN ARG LYS MET MET SER PHE GLN ALA ASN PRO THR
SEQRES 6 E 215 GLU GLU SER ILE SER LYS PHE PRO ASP MET GLY SER LEU
SEQRES 7 E 215 TRP VAL GLU PHE CYS ASP GLU PRO SER VAL GLY VAL LYS
SEQRES 8 E 215 THR MET LYS THR PHE VAL ILE HIS ILE GLN GLU LYS ASN
SEQRES 9 E 215 PHE GLN THR GLY ILE PHE VAL TYR GLN ASN ASN ILE THR
SEQRES 10 E 215 PRO SER ALA MET LYS LEU VAL PRO SER ILE PRO PRO ALA
SEQRES 11 E 215 THR ILE GLU THR PHE ASN GLU ALA ALA LEU VAL VAL ASN
SEQRES 12 E 215 ILE THR HIS HIS GLU LEU VAL PRO LYS HIS ILE ARG LEU
SEQRES 13 E 215 SER SER ASP GLU LYS ARG GLU LEU LEU LYS ARG TYR ARG
SEQRES 14 E 215 LEU LYS GLU SER GLN LEU PRO ARG ILE GLN ARG ALA ASP
SEQRES 15 E 215 PRO VAL ALA LEU TYR LEU GLY LEU LYS ARG GLY GLU VAL
SEQRES 16 E 215 VAL LYS ILE ILE ARG LYS SER GLU THR SER GLY ARG TYR
SEQRES 17 E 215 ALA SER TYR ARG ILE CYS MET
SEQRES 1 F 155 MET SER ASP TYR GLU GLU ALA PHE ASN ASP GLY ASN GLU
SEQRES 2 F 155 ASN PHE GLU ASP PHE ASP VAL GLU HIS PHE SER ASP GLU
SEQRES 3 F 155 GLU THR TYR GLU GLU LYS PRO GLN PHE LYS ASP GLY GLU
SEQRES 4 F 155 THR THR ASP ALA ASN GLY LYS THR ILE VAL THR GLY GLY
SEQRES 5 F 155 ASN GLY PRO GLU ASP PHE GLN GLN HIS GLU GLN ILE ARG
SEQRES 6 F 155 ARG LYS THR LEU LYS GLU LYS ALA ILE PRO LYS ASP GLN
SEQRES 7 F 155 ARG ALA THR THR PRO TYR MET THR LYS TYR GLU ARG ALA
SEQRES 8 F 155 ARG ILE LEU GLY THR ARG ALA LEU GLN ILE SER MET ASN
SEQRES 9 F 155 ALA PRO VAL PHE VAL ASP LEU GLU GLY GLU THR ASP PRO
SEQRES 10 F 155 LEU ARG ILE ALA MET LYS GLU LEU ALA GLU LYS LYS ILE
SEQRES 11 F 155 PRO LEU VAL ILE ARG ARG TYR LEU PRO ASP GLY SER PHE
SEQRES 12 F 155 GLU ASP TRP SER VAL GLU GLU LEU ILE VAL ASP LEU
SEQRES 1 H 146 MET SER ASN THR LEU PHE ASP ASP ILE PHE GLN VAL SER
SEQRES 2 H 146 GLU VAL ASP PRO GLY ARG TYR ASN LYS VAL CYS ARG ILE
SEQRES 3 H 146 GLU ALA ALA SER THR THR GLN ASP GLN CYS LYS LEU THR
SEQRES 4 H 146 LEU ASP ILE ASN VAL GLU LEU PHE PRO VAL ALA ALA GLN
SEQRES 5 H 146 ASP SER LEU THR VAL THR ILE ALA SER SER LEU ASN LEU
SEQRES 6 H 146 GLU ASP THR PRO ALA ASN ASP SER SER ALA THR ARG SER
SEQRES 7 H 146 TRP ARG PRO PRO GLN ALA GLY ASP ARG SER LEU ALA ASP
SEQRES 8 H 146 ASP TYR ASP TYR VAL MET TYR GLY THR ALA TYR LYS PHE
SEQRES 9 H 146 GLU GLU VAL SER LYS ASP LEU ILE ALA VAL TYR TYR SER
SEQRES 10 H 146 PHE GLY GLY LEU LEU MET ARG LEU GLU GLY ASN TYR ARG
SEQRES 11 H 146 ASN LEU ASN ASN LEU LYS GLN GLU ASN ALA TYR LEU LEU
SEQRES 12 H 146 ILE ARG ARG
SEQRES 1 I 122 MET THR THR PHE ARG PHE CYS ARG ASP CYS ASN ASN MET
SEQRES 2 I 122 LEU TYR PRO ARG GLU ASP LYS GLU ASN ASN ARG LEU LEU
SEQRES 3 I 122 PHE GLU CYS ARG THR CYS SER TYR VAL GLU GLU ALA GLY
SEQRES 4 I 122 SER PRO LEU VAL TYR ARG HIS GLU LEU ILE THR ASN ILE
SEQRES 5 I 122 GLY GLU THR ALA GLY VAL VAL GLN ASP ILE GLY SER ASP
SEQRES 6 I 122 PRO THR LEU PRO ARG SER ASP ARG GLU CYS PRO LYS CYS
SEQRES 7 I 122 HIS SER ARG GLU ASN VAL PHE PHE GLN SER GLN GLN ARG
SEQRES 8 I 122 ARG LYS ASP THR SER MET VAL LEU PHE PHE VAL CYS LEU
SEQRES 9 I 122 SER CYS SER HIS ILE PHE THR SER ASP GLN LYS ASN LYS
SEQRES 10 I 122 ARG THR GLN PHE SER
SEQRES 1 J 70 MET ILE VAL PRO VAL ARG CYS PHE SER CYS GLY LYS VAL
SEQRES 2 J 70 VAL GLY ASP LYS TRP GLU SER TYR LEU ASN LEU LEU GLN
SEQRES 3 J 70 GLU ASP GLU LEU ASP GLU GLY THR ALA LEU SER ARG LEU
SEQRES 4 J 70 GLY LEU LYS ARG TYR CYS CYS ARG ARG MET ILE LEU THR
SEQRES 5 J 70 HIS VAL ASP LEU ILE GLU LYS PHE LEU ARG TYR ASN PRO
SEQRES 6 J 70 LEU GLU LYS ARG ASP
SEQRES 1 K 120 MET ASN ALA PRO ASP ARG PHE GLU LEU PHE LEU LEU GLY
SEQRES 2 K 120 GLU GLY GLU SER LYS LEU LYS ILE ASP PRO ASP THR LYS
SEQRES 3 K 120 ALA PRO ASN ALA VAL VAL ILE THR PHE GLU LYS GLU ASP
SEQRES 4 K 120 HIS THR LEU GLY ASN LEU ILE ARG ALA GLU LEU LEU ASN
SEQRES 5 K 120 ASP ARG LYS VAL LEU PHE ALA ALA TYR LYS VAL GLU HIS
SEQRES 6 K 120 PRO PHE PHE ALA ARG PHE LYS LEU ARG ILE GLN THR THR
SEQRES 7 K 120 GLU GLY TYR ASP PRO LYS ASP ALA LEU LYS ASN ALA CYS
SEQRES 8 K 120 ASN SER ILE ILE ASN LYS LEU GLY ALA LEU LYS THR ASN
SEQRES 9 K 120 PHE GLU THR GLU TRP ASN LEU GLN THR LEU ALA ALA ASP
SEQRES 10 K 120 ASP ALA PHE
SEQRES 1 L 70 MET SER ARG GLU GLY PHE GLN ILE PRO THR ASN LEU ASP
SEQRES 2 L 70 ALA ALA ALA ALA GLY THR SER GLN ALA ARG THR ALA THR
SEQRES 3 L 70 LEU LYS TYR ILE CYS ALA GLU CYS SER SER LYS LEU SER
SEQRES 4 L 70 LEU SER ARG THR ASP ALA VAL ARG CYS LYS ASP CYS GLY
SEQRES 5 L 70 HIS ARG ILE LEU LEU LYS ALA ARG THR LYS ARG LEU VAL
SEQRES 6 L 70 GLN PHE GLU ALA ARG
SEQRES 1 T 29 DC DT DA DC DC DG DA DT DA DA DG DC DA
SEQRES 2 T 29 DG DA DG DG DC DA 3DR DC DT DC DT DC DG
SEQRES 3 T 29 DA DT DG
SEQRES 1 R 8 A U C G A G A G
HET 3DR T 20 11
HET ZN A1801 1
HET ZN A1802 1
HET MG A1803 1
HET ZN B1301 1
HET ZN C 401 1
HET ZN I 201 1
HET ZN I 202 1
HET ZN J 101 1
HET ZN L 101 1
HETNAM 3DR 1',2'-DIDEOXYRIBOFURANOSE-5'-PHOSPHATE
HETNAM ZN ZINC ION
HETNAM MG MAGNESIUM ION
HETSYN 3DR ABASIC DIDEOXYRIBOSE
FORMUL 11 3DR C5 H11 O6 P
FORMUL 13 ZN 8(ZN 2+)
FORMUL 15 MG MG 2+
HELIX 1 AA1 SER A 23 SER A 31 1 9
HELIX 2 AA2 HIS A 92 GLY A 94 5 3
HELIX 3 AA3 PHE A 95 VAL A 106 1 12
HELIX 4 AA4 ASN A 119 LEU A 126 1 8
HELIX 5 AA5 ASP A 130 THR A 140 1 11
HELIX 6 AA6 SER A 203 LYS A 212 1 10
HELIX 7 AA7 VAL A 216 SER A 221 1 6
HELIX 8 AA8 ASP A 260 ASN A 282 1 23
HELIX 9 AA9 PRO A 285 ASP A 305 1 21
HELIX 10 AB1 SER A 324 LYS A 330 1 7
HELIX 11 AB2 GLY A 334 LEU A 340 1 7
HELIX 12 AB3 LYS A 368 LEU A 374 1 7
HELIX 13 AB4 ASN A 384 GLY A 395 1 12
HELIX 14 AB5 HIS A 451 MET A 453 5 3
HELIX 15 AB6 VAL A 474 ASN A 479 1 6
HELIX 16 AB7 SER A 494 CYS A 505 1 12
HELIX 17 AB8 ALA A 506 GLN A 510 5 5
HELIX 18 AB9 GLN A 525 THR A 535 1 11
HELIX 19 AC1 GLU A 542 VAL A 553 1 12
HELIX 20 AC2 GLY A 574 SER A 579 1 6
HELIX 21 AC3 GLU A 618 GLY A 623 1 6
HELIX 22 AC4 GLY A 628 GLY A 638 1 11
HELIX 23 AC5 GLY A 638 HIS A 659 1 22
HELIX 24 AC6 GLY A 665 ILE A 670 5 6
HELIX 25 AC7 ASP A 672 ALA A 699 1 28
HELIX 26 AC8 THR A 709 LEU A 737 1 29
HELIX 27 AC9 ASN A 741 GLY A 750 1 10
HELIX 28 AD1 SER A 754 ALA A 763 1 10
HELIX 29 AD2 THR A 809 LEU A 845 1 37
HELIX 30 AD3 ILE A 867 ASP A 871 5 5
HELIX 31 AD4 ASP A 874 ALA A 876 5 3
HELIX 32 AD5 SER A 889 ARG A 898 1 10
HELIX 33 AD6 GLY A 916 LEU A 920 5 5
HELIX 34 AD7 ASP A 922 PHE A 947 1 26
HELIX 35 AD8 ASN A 959 PHE A 971 1 13
HELIX 36 AD9 THR A 982 GLN A 994 1 13
HELIX 37 AE1 ASN A 1004 LEU A 1026 1 23
HELIX 38 AE2 ALA A 1027 GLU A 1034 1 8
HELIX 39 AE3 THR A 1038 VAL A 1057 1 20
HELIX 40 AE4 MET A 1063 GLU A 1074 1 12
HELIX 41 AE5 GLY A 1097 VAL A 1107 1 11
HELIX 42 AE6 ASP A 1127 GLU A 1139 1 13
HELIX 43 AE7 ASP A 1166 HIS A 1173 1 8
HELIX 44 AE8 ALA A 1200 LYS A 1205 1 6
HELIX 45 AE9 THR A 1208 LYS A 1221 1 14
HELIX 46 AF1 MET A 1259 GLU A 1269 1 11
HELIX 47 AF2 ASN A 1312 MET A 1317 1 6
HELIX 48 AF3 SER A 1331 LEU A 1339 1 9
HELIX 49 AF4 GLY A 1340 ASP A 1359 1 20
HELIX 50 AF5 ASN A 1364 THR A 1377 1 14
HELIX 51 AF6 GLY A 1388 SER A 1392 5 5
HELIX 52 AF7 GLY A 1395 SER A 1401 1 7
HELIX 53 AF8 THR A 1405 ALA A 1416 1 12
HELIX 54 AF9 GLY A 1423 GLY A 1431 1 9
HELIX 55 AG1 ILE A 1436 GLY A 1439 5 4
HELIX 56 AG2 GLU B 28 PHE B 37 1 10
HELIX 57 AG3 VAL B 44 TYR B 57 1 14
HELIX 58 AG4 TYR B 57 ASP B 66 1 10
HELIX 59 AG5 TYR B 113 ARG B 120 1 8
HELIX 60 AG6 THR B 185 LEU B 192 1 8
HELIX 61 AG7 ILE B 282 LEU B 289 1 8
HELIX 62 AG8 GLY B 295 CYS B 302 1 8
HELIX 63 AG9 ASP B 307 GLY B 321 1 15
HELIX 64 AH1 ASP B 326 GLY B 338 1 13
HELIX 65 AH2 GLU B 346 GLU B 359 1 14
HELIX 66 AH3 GLU B 371 LEU B 390 1 20
HELIX 67 AH4 HIS B 400 GLY B 402 5 3
HELIX 68 AH5 LEU B 408 THR B 435 1 28
HELIX 69 AH6 ALA B 450 GLY B 464 1 15
HELIX 70 AH7 THR B 487 LEU B 495 1 9
HELIX 71 AH8 HIS B 515 TRP B 519 5 5
HELIX 72 AH9 PRO B 551 GLU B 560 1 10
HELIX 73 AI1 PRO B 565 TYR B 569 5 5
HELIX 74 AI2 VAL B 570 SER B 574 5 5
HELIX 75 AI3 ASN B 592 GLY B 607 1 16
HELIX 76 AI4 ARG B 654 ASP B 668 1 15
HELIX 77 AI5 THR B 680 GLU B 687 1 8
HELIX 78 AI6 ALA B 695 GLU B 699 1 5
HELIX 79 AI7 HIS B 744 LEU B 749 5 6
HELIX 80 AI8 ALA B 752 ILE B 756 5 5
HELIX 81 AI9 PHE B 758 ASN B 762 5 5
HELIX 82 AJ1 GLN B 763 GLY B 774 1 12
HELIX 83 AJ2 LYS B 775 ALA B 777 5 3
HELIX 84 AJ3 THR B 806 TYR B 811 5 6
HELIX 85 AJ4 GLN B 843 ARG B 848 1 6
HELIX 86 AJ5 ASN B 1013 ILE B 1017 5 5
HELIX 87 AJ6 THR B 1022 GLY B 1039 1 18
HELIX 88 AJ7 THR B 1051 HIS B 1062 1 12
HELIX 89 AJ8 MET B 1098 LYS B 1102 5 5
HELIX 90 AJ9 GLY B 1131 GLY B 1142 1 12
HELIX 91 AK1 ALA B 1143 LEU B 1151 1 9
HELIX 92 AK2 PRO B 1197 ALA B 1209 1 13
HELIX 93 AK3 ASP C 26 GLU C 40 1 15
HELIX 94 AK4 ALA C 59 LEU C 69 1 11
HELIX 95 AK5 SER C 74 LEU C 80 5 7
HELIX 96 AK6 HIS C 167 GLY C 171 5 5
HELIX 97 AK7 ASP C 196 TRP C 201 1 6
HELIX 98 AK8 SER C 204 GLU C 210 5 7
HELIX 99 AK9 PRO C 239 MET C 265 1 27
HELIX 100 AL1 GLU E 4 GLY E 27 1 24
HELIX 101 AL2 THR E 31 GLU E 36 1 6
HELIX 102 AL3 PRO E 38 CYS E 47 1 10
HELIX 103 AL4 THR E 65 PHE E 72 1 8
HELIX 104 AL5 GLY E 89 ASN E 104 1 16
HELIX 105 AL6 ALA E 138 VAL E 141 5 4
HELIX 106 AL7 ASN E 143 HIS E 147 5 5
HELIX 107 AL8 SER E 157 TYR E 168 1 12
HELIX 108 AL9 ASP E 182 GLY E 189 1 8
HELIX 109 AM1 THR F 86 SER F 102 1 17
HELIX 110 AM2 ASP F 116 GLU F 127 1 12
HELIX 111 AM3 VAL I 59 ASP I 65 5 7
HELIX 112 AM4 LYS J 17 GLU J 27 1 11
HELIX 113 AM5 ASP J 31 LEU J 39 1 9
HELIX 114 AM6 ARG J 43 THR J 52 1 10
HELIX 115 AM7 LEU J 56 LEU J 61 1 6
HELIX 116 AM8 ASP K 5 PHE K 10 5 6
HELIX 117 AM9 ASP K 39 LEU K 51 1 13
HELIX 118 AN1 ASP K 82 ASN K 110 1 29
SHEET 1 AA1 3 LEU A1418 ASP A1419 0
SHEET 2 AA1 3 GLU A 16 GLN A 18 -1 N VAL A 17 O ASP A1419
SHEET 3 AA1 3 ARG B1215 TYR B1217 -1 O TYR B1217 N GLU A 16
SHEET 1 AA2 2 GLY A 82 VAL A 90 0
SHEET 2 AA2 2 LEU A 236 VAL A 241 -1 O VAL A 241 N GLY A 82
SHEET 1 AA3 2 LYS A 176 ASP A 177 0
SHEET 2 AA3 2 LYS A 180 LEU A 181 -1 O LYS A 180 N ASP A 177
SHEET 1 AA4 2 LYS A 343 VAL A 345 0
SHEET 2 AA4 2 LEU B1128 PHE B1130 -1 O PHE B1130 N LYS A 343
SHEET 1 AA5 8 HIS B1104 ARG B1106 0
SHEET 2 AA5 8 SER A 348 GLY A 355 -1 N SER A 348 O ARG B1106
SHEET 3 AA5 8 GLU A 486 HIS A 490 -1 O MET A 487 N THR A 351
SHEET 4 AA5 8 PRO A 441 ASN A 445 -1 N LEU A 443 O HIS A 490
SHEET 5 AA5 8 MET A 455 ILE A 463 -1 O MET A 456 N PHE A 444
SHEET 6 AA5 8 GLN A 363 PRO A 367 1 N VAL A 366 O ILE A 463
SHEET 7 AA5 8 PHE A 468 LEU A 470 -1 O ARG A 469 N GLY A 365
SHEET 8 AA5 8 SER A 348 GLY A 355 1 N SER A 354 O LEU A 470
SHEET 1 AA6 4 THR A 375 VAL A 379 0
SHEET 2 AA6 4 LYS A 431 HIS A 435 -1 O ARG A 434 N TYR A 376
SHEET 3 AA6 4 ALA A 402 ILE A 406 -1 N LYS A 403 O GLU A 433
SHEET 4 AA6 4 ARG A 412 ASP A 414 -1 O ILE A 413 N VAL A 405
SHEET 1 AA7 2 VAL A 512 SER A 513 0
SHEET 2 AA7 2 LYS A 518 PRO A 519 -1 O LYS A 518 N SER A 513
SHEET 1 AA8 2 PHE A 540 ILE A 541 0
SHEET 2 AA8 2 TRP A 572 SER A 573 -1 O TRP A 572 N ILE A 541
SHEET 1 AA910 ILE A 565 LYS A 567 0
SHEET 2 AA910 TYR H 95 TYR H 98 -1 O VAL H 96 N ILE A 566
SHEET 3 AA910 TYR H 141 ARG H 145 -1 O ILE H 144 N TYR H 95
SHEET 4 AA910 SER H 54 ALA H 60 -1 N THR H 58 O LEU H 143
SHEET 5 AA910 THR H 4 ASP H 16 -1 N LEU H 5 O ILE H 59
SHEET 6 AA910 VAL H 23 SER H 30 -1 O GLU H 27 N SER H 13
SHEET 7 AA910 LYS H 37 ASN H 43 -1 O LEU H 38 N ALA H 28
SHEET 8 AA910 LEU H 121 GLY H 127 -1 O GLU H 126 N LYS H 37
SHEET 9 AA910 ILE H 112 PHE H 118 -1 N ILE H 112 O GLY H 127
SHEET 10 AA910 THR H 100 GLU H 106 -1 N GLU H 105 O ALA H 113
SHEET 1 AB1 3 LEU A 588 ARG A 590 0
SHEET 2 AB1 3 MET A 605 ILE A 608 -1 O ILE A 607 N LEU A 588
SHEET 3 AB1 3 GLN A 611 PHE A 614 -1 O GLN A 611 N ILE A 608
SHEET 1 AB2 8 PHE A 662 SER A 663 0
SHEET 2 AB2 8 GLN B 821 CYS B 829 -1 O CYS B 829 N PHE A 662
SHEET 3 AB2 8 LEU B1010 ILE B1012 1 O ILE B1012 N ALA B 828
SHEET 4 AB2 8 SER B 838 ASN B 842 -1 N ILE B 840 O ILE B1011
SHEET 5 AB2 8 LYS B 987 TYR B 994 1 O GLY B 991 N MET B 839
SHEET 6 AB2 8 LYS B 979 ALA B 981 -1 N PHE B 980 O GLY B 988
SHEET 7 AB2 8 ILE B1085 ARG B1094 -1 O GLN B1093 N ALA B 981
SHEET 8 AB2 8 PHE B1069 GLU B1070 -1 N GLU B1070 O ILE B1085
SHEET 1 AB3 4 PHE A 662 SER A 663 0
SHEET 2 AB3 4 GLN B 821 CYS B 829 -1 O CYS B 829 N PHE A 662
SHEET 3 AB3 4 ILE B1085 ARG B1094 -1 O GLY B1088 N VAL B 825
SHEET 4 AB3 4 PHE B1069 GLU B1070 -1 N GLU B1070 O ILE B1085
SHEET 1 AB4 2 GLY A 766 GLN A 767 0
SHEET 2 AB4 2 PHE A 799 VAL A 800 -1 O VAL A 800 N GLY A 766
SHEET 1 AB5 3 MET A 849 VAL A 850 0
SHEET 2 AB5 3 THR A 856 ARG A 857 -1 O ARG A 857 N MET A 849
SHEET 3 AB5 3 VAL A 863 GLN A 865 -1 O ILE A 864 N THR A 856
SHEET 1 AB6 2 ILE A 878 GLN A 881 0
SHEET 2 AB6 2 TRP A 954 PRO A 957 -1 O LEU A 956 N GLU A 879
SHEET 1 AB7 4 ARG A1281 TYR A1287 0
SHEET 2 AB7 4 GLU A1303 ASP A1309 -1 O VAL A1305 N MET A1285
SHEET 3 AB7 4 LEU A1116 TYR A1119 -1 N VAL A1118 O LEU A1306
SHEET 4 AB7 4 TYR A1328 THR A1329 -1 O TYR A1328 N THR A1117
SHEET 1 AB8 2 THR A1141 THR A1142 0
SHEET 2 AB8 2 THR A1272 ARG A1274 -1 O LEU A1273 N THR A1141
SHEET 1 AB9 5 LEU A1224 TRP A1228 0
SHEET 2 AB9 5 ILE A1237 VAL A1242 -1 O ARG A1239 N ILE A1227
SHEET 3 AB9 5 TRP A1191 LEU A1197 -1 N LEU A1195 O ILE A1238
SHEET 4 AB9 5 THR A1147 TYR A1154 -1 N ALA A1149 O GLU A1196
SHEET 5 AB9 5 TYR I 44 GLU I 47 -1 O HIS I 46 N SER A1150
SHEET 1 AC1 2 LYS A1290 PRO A1292 0
SHEET 2 AC1 2 TYR A1298 LYS A1300 -1 O VAL A1299 N VAL A1291
SHEET 1 AC2 3 PHE A1441 ILE A1445 0
SHEET 2 AC2 3 LEU F 132 TYR F 137 -1 O ARG F 135 N ASP A1442
SHEET 3 AC2 3 PHE F 143 SER F 147 -1 O GLU F 144 N ARG F 136
SHEET 1 AC3 4 THR B 68 LEU B 69 0
SHEET 2 AC3 4 ILE B 90 VAL B 97 -1 O ILE B 90 N LEU B 69
SHEET 3 AC3 4 SER B 125 VAL B 132 -1 O PHE B 129 N TYR B 96
SHEET 4 AC3 4 VAL B 165 PRO B 171 -1 O GLY B 168 N LEU B 128
SHEET 1 AC4 2 MET B 101 ASN B 103 0
SHEET 2 AC4 2 THR B 109 ALA B 111 -1 O HIS B 110 N VAL B 102
SHEET 1 AC5 3 PHE B 203 ILE B 205 0
SHEET 2 AC5 3 SER B 208 LEU B 212 -1 O SER B 208 N ILE B 205
SHEET 3 AC5 3 SER B 480 VAL B 482 -1 O GLN B 481 N VAL B 211
SHEET 1 AC6 4 LYS B 404 ASP B 407 0
SHEET 2 AC6 4 ALA B 214 SER B 218 -1 N GLN B 215 O ASP B 407
SHEET 3 AC6 4 ARG B 497 ASN B 499 1 O ASN B 499 N GLU B 216
SHEET 4 AC6 4 LYS B 537 ASN B 538 -1 O LYS B 537 N THR B 498
SHEET 1 AC7 5 VAL B 223 LYS B 227 0
SHEET 2 AC7 5 ILE B 234 SER B 242 -1 O GLU B 239 N GLN B 224
SHEET 3 AC7 5 SER B 252 TYR B 259 -1 O LEU B 258 N SER B 235
SHEET 4 AC7 5 ILE B 269 THR B 272 -1 O LYS B 270 N LYS B 257
SHEET 5 AC7 5 ILE B 280 PRO B 281 -1 O ILE B 280 N ALA B 271
SHEET 1 AC8 3 CYS B 544 ILE B 545 0
SHEET 2 AC8 3 VAL B 633 GLU B 641 -1 O TYR B 634 N CYS B 544
SHEET 3 AC8 3 VAL B 690 ASP B 694 -1 O ILE B 693 N ARG B 635
SHEET 1 AC9 4 GLU B 650 LEU B 651 0
SHEET 2 AC9 4 VAL B 633 GLU B 641 -1 N GLU B 641 O GLU B 650
SHEET 3 AC9 4 HIS B 740 CYS B 741 -1 O CYS B 741 N PHE B 638
SHEET 4 AC9 4 ILE B 703 ALA B 704 1 N ALA B 704 O HIS B 740
SHEET 1 AD1 4 VAL B 585 HIS B 590 0
SHEET 2 AD1 4 THR B 578 VAL B 582 -1 N VAL B 580 O GLY B 588
SHEET 3 AD1 4 GLU B 623 PHE B 627 1 O LEU B 624 N PHE B 581
SHEET 4 AD1 4 SER B 614 ASP B 618 -1 N ILE B 616 O LYS B 625
SHEET 1 AD2 5 MET B 792 LEU B 796 0
SHEET 2 AD2 5 SER B 853 GLN B 862 -1 O LEU B 854 N ILE B 795
SHEET 3 AD2 5 LYS B 962 LYS B 972 -1 O VAL B 966 N TYR B 859
SHEET 4 AD2 5 ASN B 946 THR B 956 -1 N ILE B 948 O ARG B 969
SHEET 5 AD2 5 ARG B 904 SER B 906 -1 N VAL B 905 O GLY B 947
SHEET 1 AD3 6 MET B 792 LEU B 796 0
SHEET 2 AD3 6 SER B 853 GLN B 862 -1 O LEU B 854 N ILE B 795
SHEET 3 AD3 6 LYS B 962 LYS B 972 -1 O VAL B 966 N TYR B 859
SHEET 4 AD3 6 ASN B 946 THR B 956 -1 N ILE B 948 O ARG B 969
SHEET 5 AD3 6 LEU L 56 LYS L 58 -1 O LEU L 56 N VAL B 954
SHEET 6 AD3 6 TYR L 29 CYS L 31 -1 N ILE L 30 O LEU L 57
SHEET 1 AD4 2 GLY B 804 THR B 805 0
SHEET 2 AD4 2 GLY B1042 ASP B1043 1 O GLY B1042 N THR B 805
SHEET 1 AD5 3 THR B 873 PHE B 874 0
SHEET 2 AD5 3 LYS B 914 THR B 916 -1 O THR B 915 N THR B 873
SHEET 3 AD5 3 ARG B 935 ASP B 936 -1 O ARG B 935 N THR B 916
SHEET 1 AD6 2 VAL B 910 ILE B 912 0
SHEET 2 AD6 2 THR B 939 PRO B 940 -1 O THR B 939 N ILE B 912
SHEET 1 AD7 2 PHE B1001 THR B1002 0
SHEET 2 AD7 2 MET B1072 TYR B1073 -1 O TYR B1073 N PHE B1001
SHEET 1 AD8 2 PHE B1158 CYS B1163 0
SHEET 2 AD8 2 ILE B1191 ILE B1196 -1 O ILE B1194 N VAL B1160
SHEET 1 AD9 2 ILE B1172 LYS B1174 0
SHEET 2 AD9 2 GLN B1179 GLU B1181 -1 O GLN B1179 N LYS B1174
SHEET 1 AE1 4 GLN C 7 ALA C 13 0
SHEET 2 AE1 4 ASN C 17 SER C 23 -1 O SER C 23 N GLN C 7
SHEET 3 AE1 4 PHE C 228 SER C 234 -1 O MET C 230 N PHE C 20
SHEET 4 AE1 4 ALA C 173 TYR C 180 -1 N GLU C 177 O ASN C 231
SHEET 1 AE2 5 VAL C 119 ILE C 120 0
SHEET 2 AE2 5 SER C 96 PHE C 104 -1 N THR C 100 O VAL C 119
SHEET 3 AE2 5 GLU C 152 ILE C 163 -1 O LEU C 153 N ALA C 103
SHEET 4 AE2 5 PRO C 42 ASN C 54 -1 N THR C 53 O LYS C 154
SHEET 5 AE2 5 VAL L 65 GLU L 68 -1 O PHE L 67 N VAL C 49
SHEET 1 AE3 2 THR C 111 TYR C 114 0
SHEET 2 AE3 2 LEU C 143 LEU C 147 -1 O CYS C 145 N VAL C 113
SHEET 1 AE4 4 GLN E 61 ALA E 62 0
SHEET 2 AE4 4 LEU E 78 PHE E 82 -1 O LEU E 78 N ALA E 62
SHEET 3 AE4 4 THR E 107 TYR E 112 1 O ILE E 109 N TRP E 79
SHEET 4 AE4 4 THR E 131 ASN E 136 1 O GLU E 133 N PHE E 110
SHEET 1 AE5 2 SER E 87 VAL E 88 0
SHEET 2 AE5 2 ASN E 115 ILE E 116 1 N ASN E 115 O VAL E 88
SHEET 1 AE6 4 LYS E 152 ARG E 155 0
SHEET 2 AE6 4 VAL E 196 SER E 202 -1 O ILE E 199 N LYS E 152
SHEET 3 AE6 4 GLY E 206 CYS E 214 -1 O ARG E 212 N VAL E 196
SHEET 4 AE6 4 ARG E 177 ILE E 178 1 N ILE E 178 O ILE E 213
SHEET 1 AE7 3 TYR I 15 ASP I 19 0
SHEET 2 AE7 3 ARG I 24 GLU I 28 -1 O LEU I 26 N ARG I 17
SHEET 3 AE7 3 VAL I 35 GLU I 37 -1 O GLU I 36 N PHE I 27
SHEET 1 AE8 3 ASN I 83 GLN I 87 0
SHEET 2 AE8 3 LEU I 99 CYS I 103 -1 O PHE I 100 N PHE I 86
SHEET 3 AE8 3 ILE I 109 THR I 111 -1 O PHE I 110 N PHE I 101
SHEET 1 AE9 4 LEU K 19 PRO K 23 0
SHEET 2 AE9 4 ALA K 30 GLU K 36 -1 O VAL K 32 N ASP K 22
SHEET 3 AE9 4 ARG K 70 THR K 77 -1 O PHE K 71 N PHE K 35
SHEET 4 AE9 4 VAL K 56 LYS K 62 -1 N ALA K 60 O ARG K 74
LINK O3' DA T 19 P 3DR T 20 1555 1555 1.62
LINK O3' 3DR T 20 P DC T 21 1555 1555 1.61
LINK SG CYS A 67 ZN ZN A1802 1555 1555 2.76
LINK SG CYS A 70 ZN ZN A1802 1555 1555 2.59
LINK SG CYS A 77 ZN ZN A1802 1555 1555 2.30
LINK NE2 HIS A 80 ZN ZN A1802 1555 1555 2.22
LINK SG CYS A 110 ZN ZN A1801 1555 1555 2.46
LINK O CYS A 167 ZN ZN A1801 1555 1555 2.54
LINK OD1 ASP A 481 MG MG A1803 1555 1555 2.43
LINK OD1 ASP A 483 MG MG A1803 1555 1555 2.27
LINK OD1 ASP A 485 MG MG A1803 1555 1555 2.21
LINK MG MG A1803 O3' G R 8 1555 1555 1.89
LINK SG CYS B1163 ZN ZN B1301 1555 1555 2.51
LINK SG CYS B1166 ZN ZN B1301 1555 1555 2.44
LINK SG CYS B1182 ZN ZN B1301 1555 1555 2.79
LINK SG CYS B1185 ZN ZN B1301 1555 1555 2.73
LINK SG CYS C 86 ZN ZN C 401 1555 1555 2.45
LINK SG CYS C 88 ZN ZN C 401 1555 1555 2.36
LINK SG CYS C 92 ZN ZN C 401 1555 1555 2.39
LINK SG CYS C 95 ZN ZN C 401 1555 1555 2.53
LINK SG CYS I 7 ZN ZN I 201 1555 1555 2.68
LINK SG CYS I 10 ZN ZN I 201 1555 1555 2.51
LINK SG CYS I 29 ZN ZN I 201 1555 1555 2.40
LINK SG CYS I 32 ZN ZN I 201 1555 1555 2.39
LINK SG CYS I 75 ZN ZN I 202 1555 1555 2.42
LINK SG CYS I 78 ZN ZN I 202 1555 1555 2.27
LINK SG CYS I 103 ZN ZN I 202 1555 1555 2.50
LINK SG CYS I 106 ZN ZN I 202 1555 1555 2.36
LINK SG CYS J 7 ZN ZN J 101 1555 1555 2.44
LINK SG CYS J 10 ZN ZN J 101 1555 1555 2.40
LINK SG CYS J 45 ZN ZN J 101 1555 1555 2.33
LINK SG CYS J 46 ZN ZN J 101 1555 1555 2.36
LINK SG CYS L 31 ZN ZN L 101 1555 1555 2.88
LINK SG CYS L 34 ZN ZN L 101 1555 1555 2.42
LINK SG CYS L 48 ZN ZN L 101 1555 1555 2.53
LINK SG CYS L 51 ZN ZN L 101 1555 1555 2.48
CISPEP 1 GLY A 331 LYS A 332 0 1.75
CISPEP 2 HIS A 399 PRO A 400 0 1.24
CISPEP 3 GLN A 447 PRO A 448 0 0.12
CISPEP 4 LYS A 567 PRO A 568 0 1.27
CISPEP 5 PRO E 128 PRO E 129 0 -4.08
CISPEP 6 GLN H 83 ALA H 84 0 -0.67
CISPEP 7 ALA H 84 GLY H 85 0 0.27
CISPEP 8 GLY H 85 ASP H 86 0 0.50
CISPEP 9 VAL L 46 ARG L 47 0 3.73
SITE 1 AC1 5 CYS A 107 MET A 108 CYS A 110 CYS A 148
SITE 2 AC1 5 CYS A 167
SITE 1 AC2 4 CYS A 67 CYS A 70 CYS A 77 HIS A 80
SITE 1 AC3 4 ASP A 481 ASP A 483 ASP A 485 G R 8
SITE 1 AC4 4 CYS B1163 CYS B1166 CYS B1182 CYS B1185
SITE 1 AC5 4 CYS C 86 CYS C 88 CYS C 92 CYS C 95
SITE 1 AC6 4 CYS I 7 CYS I 10 CYS I 29 CYS I 32
SITE 1 AC7 4 CYS I 75 CYS I 78 CYS I 103 CYS I 106
SITE 1 AC8 4 CYS J 7 CYS J 10 CYS J 45 CYS J 46
SITE 1 AC9 4 CYS L 31 CYS L 34 CYS L 48 CYS L 51
CRYST1 168.550 222.280 193.770 90.00 100.62 90.00 C 1 2 1 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 0.005933 0.000000 0.001112 0.00000
SCALE2 0.000000 0.004499 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005251 0.00000
(ATOM LINES ARE NOT SHOWN.)
END