HEADER HYDROLASE, TRANSFERASE/DNA 30-APR-13 4KHN
TITLE CRYSTAL STRUCTURE OF THE TERNARY COMPLEX OF THE D714A MUTANT OF RB69
TITLE 2 DNA POLYMERASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA POLYMERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: GP43;
COMPND 5 EC: 2.7.7.7;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: DNA (5'-
COMPND 10 D(*TP*CP*AP*CP*GP*TP*AP*AP*GP*CP*AP*GP*TP*CP*CP*GP*CP*G)-3');
COMPND 11 CHAIN: C, E;
COMPND 12 ENGINEERED: YES;
COMPND 13 MOL_ID: 3;
COMPND 14 MOLECULE: DNA (5'-D(*GP*CP*GP*GP*AP*CP*TP*GP*CP*TP*TP*AP*C)-3');
COMPND 15 CHAIN: D, F;
COMPND 16 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ENTEROBACTERIA PHAGE RB69;
SOURCE 3 ORGANISM_TAXID: 12353;
SOURCE 4 GENE: 43;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 MOL_ID: 2;
SOURCE 8 SYNTHETIC: YES;
SOURCE 9 MOL_ID: 3;
SOURCE 10 SYNTHETIC: YES
KEYWDS PALM SUBDOMAIN, HYDROLASE, TRANSFERASE, TRANSFERASE-DNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR K.E.GUJA,A.JACEWICZ,A.TRZEMECKA,D.PLOCHOCKA,E.YAKUBOVSKAYA,A.BEBENEK,
AUTHOR 2 M.GARCIA-DIAZ
REVDAT 3 20-SEP-23 4KHN 1 REMARK SEQADV LINK
REVDAT 2 23-OCT-13 4KHN 1 JRNL
REVDAT 1 09-OCT-13 4KHN 0
JRNL AUTH A.JACEWICZ,A.TRZEMECKA,K.E.GUJA,D.PLOCHOCKA,E.YAKUBOVSKAYA,
JRNL AUTH 2 A.BEBENEK,M.GARCIA-DIAZ
JRNL TITL A REMOTE PALM DOMAIN RESIDUE OF RB69 DNA POLYMERASE IS
JRNL TITL 2 CRITICAL FOR ENZYME ACTIVITY AND INFLUENCES THE CONFORMATION
JRNL TITL 3 OF THE ACTIVE SITE.
JRNL REF PLOS ONE V. 8 76700 2013
JRNL REFN ESSN 1932-6203
JRNL PMID 24116139
JRNL DOI 10.1371/JOURNAL.PONE.0076700
REMARK 2
REMARK 2 RESOLUTION. 2.55 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: DEV_1363)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.55
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.33
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 83990
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.170
REMARK 3 R VALUE (WORKING SET) : 0.168
REMARK 3 FREE R VALUE : 0.211
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.940
REMARK 3 FREE R VALUE TEST SET COUNT : 4149
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 35.3376 - 7.8949 1.00 2736 147 0.1478 0.1563
REMARK 3 2 7.8949 - 6.2779 1.00 2659 166 0.1675 0.2086
REMARK 3 3 6.2779 - 5.4876 1.00 2699 139 0.1668 0.2187
REMARK 3 4 5.4876 - 4.9874 1.00 2630 164 0.1445 0.1898
REMARK 3 5 4.9874 - 4.6308 1.00 2659 129 0.1325 0.1701
REMARK 3 6 4.6308 - 4.3583 1.00 2690 137 0.1273 0.1764
REMARK 3 7 4.3583 - 4.1404 1.00 2643 140 0.1375 0.1699
REMARK 3 8 4.1404 - 3.9604 1.00 2695 124 0.1366 0.1622
REMARK 3 9 3.9604 - 3.8081 1.00 2635 150 0.1507 0.1796
REMARK 3 10 3.8081 - 3.6768 1.00 2666 150 0.1597 0.2249
REMARK 3 11 3.6768 - 3.5620 1.00 2647 135 0.1660 0.2228
REMARK 3 12 3.5620 - 3.4602 1.00 2682 154 0.1697 0.2368
REMARK 3 13 3.4602 - 3.3692 1.00 2632 128 0.1798 0.2332
REMARK 3 14 3.3692 - 3.2871 1.00 2658 140 0.1801 0.2479
REMARK 3 15 3.2871 - 3.2124 1.00 2651 132 0.1910 0.2567
REMARK 3 16 3.2124 - 3.1441 1.00 2685 145 0.2071 0.2730
REMARK 3 17 3.1441 - 3.0812 1.00 2640 116 0.2110 0.2507
REMARK 3 18 3.0812 - 3.0231 1.00 2663 152 0.2003 0.2027
REMARK 3 19 3.0231 - 2.9692 1.00 2647 124 0.1964 0.2541
REMARK 3 20 2.9692 - 2.9188 1.00 2658 166 0.2031 0.2468
REMARK 3 21 2.9188 - 2.8718 1.00 2623 122 0.1958 0.2495
REMARK 3 22 2.8718 - 2.8276 1.00 2709 133 0.2030 0.2614
REMARK 3 23 2.8276 - 2.7861 1.00 2654 131 0.2089 0.2686
REMARK 3 24 2.7861 - 2.7468 1.00 2619 126 0.2183 0.2969
REMARK 3 25 2.7468 - 2.7097 1.00 2676 149 0.2271 0.2746
REMARK 3 26 2.7097 - 2.6745 1.00 2675 127 0.2391 0.2867
REMARK 3 27 2.6745 - 2.6411 1.00 2621 133 0.2482 0.2896
REMARK 3 28 2.6411 - 2.6093 1.00 2686 120 0.2574 0.3434
REMARK 3 29 2.6093 - 2.5790 1.00 2672 132 0.2660 0.3105
REMARK 3 30 2.5790 - 2.5500 1.00 2631 138 0.2615 0.3017
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.330
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.620
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 : 0.011 15863
REMARK 3 ANGLE : 1.192 21797
REMARK 3 CHIRALITY : 0.081 2355
REMARK 3 PLANARITY : 0.005 2566
REMARK 3 DIHEDRAL : 17.240 5840
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 15
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 116 )
REMARK 3 ORIGIN FOR THE GROUP (A): -7.4858 0.7978 -26.8746
REMARK 3 T TENSOR
REMARK 3 T11: 0.5104 T22: 0.4345
REMARK 3 T33: 0.3059 T12: 0.0438
REMARK 3 T13: -0.0675 T23: 0.0036
REMARK 3 L TENSOR
REMARK 3 L11: 1.4416 L22: 5.0651
REMARK 3 L33: 0.2628 L12: -2.0023
REMARK 3 L13: -0.0700 L23: -0.4647
REMARK 3 S TENSOR
REMARK 3 S11: 0.2059 S12: 0.3761 S13: 0.0056
REMARK 3 S21: -0.8934 S22: -0.2316 S23: 0.1089
REMARK 3 S31: 0.1109 S32: -0.0048 S33: 0.0331
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 117 THROUGH 280 )
REMARK 3 ORIGIN FOR THE GROUP (A): 15.3210 -20.8817 -19.4233
REMARK 3 T TENSOR
REMARK 3 T11: 0.4133 T22: 0.3959
REMARK 3 T33: 0.3410 T12: 0.0317
REMARK 3 T13: 0.0986 T23: -0.0312
REMARK 3 L TENSOR
REMARK 3 L11: 2.9408 L22: 3.4216
REMARK 3 L33: 1.8510 L12: -0.7232
REMARK 3 L13: 0.2249 L23: -1.1047
REMARK 3 S TENSOR
REMARK 3 S11: 0.1831 S12: 0.2445 S13: 0.2553
REMARK 3 S21: -0.4916 S22: -0.1709 S23: -0.5402
REMARK 3 S31: -0.1504 S32: 0.1814 S33: -0.0221
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 281 THROUGH 571 )
REMARK 3 ORIGIN FOR THE GROUP (A): -11.3970 -15.7684 -3.1875
REMARK 3 T TENSOR
REMARK 3 T11: 0.2763 T22: 0.3232
REMARK 3 T33: 0.3523 T12: -0.0350
REMARK 3 T13: -0.0696 T23: -0.0336
REMARK 3 L TENSOR
REMARK 3 L11: 1.4206 L22: 0.6675
REMARK 3 L33: 1.3660 L12: -0.1999
REMARK 3 L13: -0.7665 L23: 0.1062
REMARK 3 S TENSOR
REMARK 3 S11: -0.0301 S12: 0.0582 S13: -0.2980
REMARK 3 S21: -0.1710 S22: -0.0273 S23: 0.2050
REMARK 3 S31: 0.2277 S32: -0.0828 S33: 0.0545
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 572 THROUGH 901 )
REMARK 3 ORIGIN FOR THE GROUP (A): -4.9376 -17.3151 16.6243
REMARK 3 T TENSOR
REMARK 3 T11: 0.2097 T22: 0.2876
REMARK 3 T33: 0.2951 T12: -0.0388
REMARK 3 T13: -0.0109 T23: -0.0613
REMARK 3 L TENSOR
REMARK 3 L11: 0.9354 L22: 1.0368
REMARK 3 L33: 1.2058 L12: -0.6063
REMARK 3 L13: 0.4428 L23: -0.3983
REMARK 3 S TENSOR
REMARK 3 S11: 0.0529 S12: -0.0461 S13: -0.1227
REMARK 3 S21: 0.0050 S22: -0.0185 S23: 0.0342
REMARK 3 S31: 0.0657 S32: 0.0995 S33: -0.0375
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 1 THROUGH 18 )
REMARK 3 ORIGIN FOR THE GROUP (A): 4.4622 -1.2974 15.5019
REMARK 3 T TENSOR
REMARK 3 T11: 0.2619 T22: 0.4284
REMARK 3 T33: 0.4000 T12: -0.0933
REMARK 3 T13: -0.0451 T23: -0.0618
REMARK 3 L TENSOR
REMARK 3 L11: 7.9661 L22: 4.1959
REMARK 3 L33: 2.8997 L12: -0.4324
REMARK 3 L13: 3.6893 L23: -2.1692
REMARK 3 S TENSOR
REMARK 3 S11: -0.1328 S12: 0.0871 S13: 0.4724
REMARK 3 S21: 0.4048 S22: -0.1120 S23: -0.4550
REMARK 3 S31: -0.3270 S32: 0.7275 S33: 0.1698
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 103 THROUGH 115 )
REMARK 3 ORIGIN FOR THE GROUP (A): 4.1951 -3.2038 19.2864
REMARK 3 T TENSOR
REMARK 3 T11: 0.4637 T22: 0.5275
REMARK 3 T33: 0.3759 T12: -0.0237
REMARK 3 T13: -0.1114 T23: -0.0043
REMARK 3 L TENSOR
REMARK 3 L11: 9.1360 L22: 5.6291
REMARK 3 L33: 9.1499 L12: 2.8236
REMARK 3 L13: 6.5822 L23: 4.1278
REMARK 3 S TENSOR
REMARK 3 S11: -0.1938 S12: -1.3146 S13: 0.4616
REMARK 3 S21: 0.6222 S22: -0.1471 S23: -0.2361
REMARK 3 S31: -0.6382 S32: -0.3302 S33: 0.1270
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 1 THROUGH 18 )
REMARK 3 ORIGIN FOR THE GROUP (A): -41.5459 3.9409 -88.6318
REMARK 3 T TENSOR
REMARK 3 T11: 0.6871 T22: 0.4349
REMARK 3 T33: 0.4665 T12: 0.1946
REMARK 3 T13: 0.0355 T23: 0.0127
REMARK 3 L TENSOR
REMARK 3 L11: 4.5772 L22: 2.9946
REMARK 3 L33: 6.1043 L12: 2.4115
REMARK 3 L13: 3.3804 L23: 3.1045
REMARK 3 S TENSOR
REMARK 3 S11: 0.0115 S12: -0.1958 S13: 0.3201
REMARK 3 S21: -0.0438 S22: 0.0625 S23: 0.4894
REMARK 3 S31: -0.8973 S32: -0.5820 S33: -0.1115
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 103 THROUGH 115 )
REMARK 3 ORIGIN FOR THE GROUP (A): -41.8126 2.4170 -92.1190
REMARK 3 T TENSOR
REMARK 3 T11: 1.0312 T22: 0.7341
REMARK 3 T33: 0.6244 T12: 0.1252
REMARK 3 T13: -0.1902 T23: -0.0603
REMARK 3 L TENSOR
REMARK 3 L11: 6.8073 L22: 5.7703
REMARK 3 L33: 7.9772 L12: -5.6383
REMARK 3 L13: 7.1427 L23: -5.7828
REMARK 3 S TENSOR
REMARK 3 S11: -0.1890 S12: 1.1743 S13: 0.1519
REMARK 3 S21: -0.3444 S22: -0.2775 S23: 0.4225
REMARK 3 S31: -0.8678 S32: 0.3347 S33: 0.6512
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 179 )
REMARK 3 ORIGIN FOR THE GROUP (A): -32.9918 -3.8546 -50.4353
REMARK 3 T TENSOR
REMARK 3 T11: 1.7389 T22: 0.7986
REMARK 3 T33: 0.4838 T12: -0.2368
REMARK 3 T13: -0.0356 T23: -0.0335
REMARK 3 L TENSOR
REMARK 3 L11: 1.1960 L22: 3.7850
REMARK 3 L33: -0.4029 L12: 1.3050
REMARK 3 L13: -0.2047 L23: 0.3879
REMARK 3 S TENSOR
REMARK 3 S11: 0.3589 S12: -0.3467 S13: 0.0878
REMARK 3 S21: 1.2516 S22: -0.2463 S23: -0.0793
REMARK 3 S31: -0.3288 S32: 0.1245 S33: -0.1023
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 180 THROUGH 338 )
REMARK 3 ORIGIN FOR THE GROUP (A): -44.7933 -14.8384 -57.2206
REMARK 3 T TENSOR
REMARK 3 T11: 1.3354 T22: 0.5875
REMARK 3 T33: 0.5213 T12: -0.1095
REMARK 3 T13: 0.0811 T23: -0.0656
REMARK 3 L TENSOR
REMARK 3 L11: 1.8363 L22: 2.8753
REMARK 3 L33: 2.2712 L12: 0.1622
REMARK 3 L13: -0.8563 L23: 0.5616
REMARK 3 S TENSOR
REMARK 3 S11: 0.2297 S12: -0.4022 S13: 0.2172
REMARK 3 S21: 0.9985 S22: -0.3026 S23: 0.4362
REMARK 3 S31: -0.7300 S32: -0.0233 S33: 0.0499
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 339 THROUGH 469 )
REMARK 3 ORIGIN FOR THE GROUP (A): -16.5019 5.4391 -75.5045
REMARK 3 T TENSOR
REMARK 3 T11: 0.8693 T22: 0.4356
REMARK 3 T33: 0.5564 T12: 0.0228
REMARK 3 T13: -0.0671 T23: -0.1025
REMARK 3 L TENSOR
REMARK 3 L11: 2.4416 L22: 1.9827
REMARK 3 L33: 1.6405 L12: 1.0502
REMARK 3 L13: 0.2039 L23: 0.1483
REMARK 3 S TENSOR
REMARK 3 S11: 0.3438 S12: -0.2702 S13: 0.0404
REMARK 3 S21: 0.7316 S22: -0.2326 S23: -0.4260
REMARK 3 S31: -0.0616 S32: -0.1204 S33: -0.1076
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 470 THROUGH 571 )
REMARK 3 ORIGIN FOR THE GROUP (A): -16.3353 -16.9061 -70.7359
REMARK 3 T TENSOR
REMARK 3 T11: 1.1822 T22: 0.6282
REMARK 3 T33: 0.6477 T12: 0.0291
REMARK 3 T13: -0.1249 T23: -0.0093
REMARK 3 L TENSOR
REMARK 3 L11: 1.0359 L22: 5.4798
REMARK 3 L33: 0.6308 L12: -0.5386
REMARK 3 L13: -0.1976 L23: -2.1048
REMARK 3 S TENSOR
REMARK 3 S11: 0.0215 S12: -0.1699 S13: -0.4003
REMARK 3 S21: 0.7449 S22: -0.2683 S23: -0.5142
REMARK 3 S31: 0.2073 S32: 0.1811 S33: 0.1869
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 572 THROUGH 715 )
REMARK 3 ORIGIN FOR THE GROUP (A): -13.1925 -6.4643 -92.1233
REMARK 3 T TENSOR
REMARK 3 T11: 0.6358 T22: 0.6385
REMARK 3 T33: 0.6929 T12: 0.1788
REMARK 3 T13: -0.0500 T23: -0.2770
REMARK 3 L TENSOR
REMARK 3 L11: 3.5405 L22: 4.3671
REMARK 3 L33: 0.7038 L12: 3.0669
REMARK 3 L13: 1.6660 L23: 1.2619
REMARK 3 S TENSOR
REMARK 3 S11: 0.0537 S12: 0.9240 S13: -0.8828
REMARK 3 S21: 0.3251 S22: 0.4970 S23: -0.9033
REMARK 3 S31: 0.2691 S32: 0.6482 S33: -0.4811
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 716 THROUGH 855 )
REMARK 3 ORIGIN FOR THE GROUP (A): -47.5571 -14.5259 -87.6698
REMARK 3 T TENSOR
REMARK 3 T11: 0.6796 T22: 0.2993
REMARK 3 T33: 0.3488 T12: 0.0287
REMARK 3 T13: -0.0214 T23: 0.0345
REMARK 3 L TENSOR
REMARK 3 L11: 7.8159 L22: 2.7299
REMARK 3 L33: 2.5935 L12: -1.1523
REMARK 3 L13: -1.2559 L23: 1.1576
REMARK 3 S TENSOR
REMARK 3 S11: 0.0203 S12: -0.1638 S13: -0.1350
REMARK 3 S21: 0.3351 S22: -0.0196 S23: 0.2457
REMARK 3 S31: 0.3244 S32: -0.0818 S33: -0.0132
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 856 THROUGH 901 )
REMARK 3 ORIGIN FOR THE GROUP (A): -46.3319 -17.8712-101.4783
REMARK 3 T TENSOR
REMARK 3 T11: 0.4482 T22: 0.3848
REMARK 3 T33: 0.4912 T12: 0.0802
REMARK 3 T13: -0.0218 T23: 0.0272
REMARK 3 L TENSOR
REMARK 3 L11: 3.6046 L22: 0.9143
REMARK 3 L33: 2.5592 L12: 0.7072
REMARK 3 L13: -0.7286 L23: 0.5179
REMARK 3 S TENSOR
REMARK 3 S11: 0.1182 S12: 0.2850 S13: -0.0121
REMARK 3 S21: 0.1546 S22: -0.0934 S23: 0.3546
REMARK 3 S31: 0.1449 S32: -0.1690 S33: -0.0891
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 4KHN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-MAY-13.
REMARK 100 THE DEPOSITION ID IS D_1000079350.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-JAN-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X25
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.1
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 84020
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.550
REMARK 200 RESOLUTION RANGE LOW (A) : 39.300
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 4.900
REMARK 200 R MERGE (I) : 0.06300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.55
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.56
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 4.80
REMARK 200 R MERGE FOR SHELL (I) : 0.61700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 3NGI
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.24
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.88
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 12% PEG 8000, 0.1 M MES, 0.2 AMMONIUM
REMARK 280 SULFATE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K, PH 6
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 59.67650
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7610 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 41150 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -119.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, D
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5580 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 41040 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -57.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, B
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 ASP A 902
REMARK 465 PHE A 903
REMARK 465 HIS B 504
REMARK 465 ASN B 505
REMARK 465 PRO B 506
REMARK 465 ASN B 507
REMARK 465 LEU B 508
REMARK 465 SER B 509
REMARK 465 VAL B 510
REMARK 465 ASP B 511
REMARK 465 GLU B 512
REMARK 465 PRO B 513
REMARK 465 LEU B 514
REMARK 465 ASP B 515
REMARK 465 VAL B 516
REMARK 465 ASP B 517
REMARK 465 TYR B 518
REMARK 465 ARG B 519
REMARK 465 PHE B 520
REMARK 465 ASP B 521
REMARK 465 PHE B 522
REMARK 465 SER B 523
REMARK 465 ASP B 524
REMARK 465 GLU B 525
REMARK 465 ILE B 526
REMARK 465 LYS B 527
REMARK 465 GLU B 528
REMARK 465 LYS B 529
REMARK 465 ILE B 530
REMARK 465 LYS B 531
REMARK 465 LYS B 532
REMARK 465 LEU B 533
REMARK 465 SER B 534
REMARK 465 ASP B 902
REMARK 465 PHE B 903
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ARG A 25 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 32 CG CD OE1 OE2
REMARK 470 GLU A 43 CG CD OE1 OE2
REMARK 470 THR A 47 OG1 CG2
REMARK 470 LYS A 60 CE NZ
REMARK 470 LYS A 73 CD CE NZ
REMARK 470 GLU A 100 CG CD OE1 OE2
REMARK 470 LYS A 102 CD CE NZ
REMARK 470 LYS A 107 NZ
REMARK 470 ASP A 121 CG OD1 OD2
REMARK 470 GLN A 128 CD OE1 NE2
REMARK 470 GLU A 165 CG CD OE1 OE2
REMARK 470 GLU A 196 CD OE1 OE2
REMARK 470 GLN A 207 CD OE1 NE2
REMARK 470 ARG A 249 NE CZ NH1 NH2
REMARK 470 LYS A 251 CE NZ
REMARK 470 GLU A 254 CG CD OE1 OE2
REMARK 470 MET A 256 CG SD CE
REMARK 470 LYS A 304 CG CD CE NZ
REMARK 470 LYS A 311 CE NZ
REMARK 470 GLU A 314 CG CD OE1 OE2
REMARK 470 GLU A 375 CG CD OE1 OE2
REMARK 470 ARG A 384 CZ NH1 NH2
REMARK 470 GLU A 448 CD OE1 OE2
REMARK 470 ASP A 452 CG OD1 OD2
REMARK 470 ASN A 505 CG OD1 ND2
REMARK 470 ASN A 507 CG OD1 ND2
REMARK 470 LEU A 508 CG CD1 CD2
REMARK 470 VAL A 510 CG1 CG2
REMARK 470 ASP A 524 CG OD1 OD2
REMARK 470 GLU A 525 CG CD OE1 OE2
REMARK 470 GLU A 528 CG CD OE1 OE2
REMARK 470 LYS A 531 CD CE NZ
REMARK 470 LYS A 532 CG CD CE NZ
REMARK 470 LYS A 536 CG CD CE NZ
REMARK 470 GLU A 607 CD OE1 OE2
REMARK 470 GLU A 612 CG CD OE1 OE2
REMARK 470 LYS A 631 NZ
REMARK 470 LYS A 640 CG CD CE NZ
REMARK 470 LYS A 653 NZ
REMARK 470 GLU A 716 CD OE1 OE2
REMARK 470 LYS A 765 CE NZ
REMARK 470 GLU A 768 CD OE1 OE2
REMARK 470 LYS A 800 CD CE NZ
REMARK 470 ASP A 856 CG OD1 OD2
REMARK 470 ASP A 860 CG OD1 OD2
REMARK 470 LEU A 897 CG CD1 CD2
REMARK 470 PHE A 898 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 PHE A 901 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 MET B 1 CG SD CE
REMARK 470 LYS B 2 CG CD CE NZ
REMARK 470 GLU B 9 CG CD OE1 OE2
REMARK 470 ASP B 13 CG OD1 OD2
REMARK 470 ARG B 18 NE CZ NH1 NH2
REMARK 470 SER B 22 OG
REMARK 470 ASN B 23 CG OD1 ND2
REMARK 470 ARG B 25 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 26 CG CD OE1 OE2
REMARK 470 ARG B 27 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 32 CG CD OE1 OE2
REMARK 470 GLU B 43 CG CD OE1 OE2
REMARK 470 GLN B 45 CG CD OE1 NE2
REMARK 470 THR B 47 OG1 CG2
REMARK 470 LYS B 48 CG CD CE NZ
REMARK 470 LYS B 55 CG CD CE NZ
REMARK 470 ARG B 66 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 76 CG CD OE1 OE2
REMARK 470 LYS B 102 CG CD CE NZ
REMARK 470 ASP B 121 CG OD1 OD2
REMARK 470 GLN B 128 CD OE1 NE2
REMARK 470 LYS B 130 CG CD CE NZ
REMARK 470 ILE B 142 CG1 CG2 CD1
REMARK 470 LEU B 152 CG CD1 CD2
REMARK 470 GLU B 160 CG CD OE1 OE2
REMARK 470 GLU B 161 CG CD OE1 OE2
REMARK 470 GLU B 165 CG CD OE1 OE2
REMARK 470 GLU B 181 CG CD OE1 OE2
REMARK 470 ASP B 184 CG OD1 OD2
REMARK 470 LYS B 195 CG CD CE NZ
REMARK 470 GLU B 196 CG CD OE1 OE2
REMARK 470 GLN B 206 CG CD OE1 NE2
REMARK 470 GLN B 207 CG CD OE1 NE2
REMARK 470 GLU B 219 CG CD OE1 OE2
REMARK 470 PHE B 234 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU B 236 CG CD OE1 OE2
REMARK 470 LYS B 240 CG CD CE NZ
REMARK 470 ARG B 241 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 246 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 247 CG CD CE NZ
REMARK 470 ARG B 249 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 251 CG CD CE NZ
REMARK 470 GLU B 254 CG CD OE1 OE2
REMARK 470 MET B 256 CG SD CE
REMARK 470 SER B 259 OG
REMARK 470 LYS B 279 CG CD CE NZ
REMARK 470 GLU B 295 CD OE1 OE2
REMARK 470 LYS B 302 CG CD CE NZ
REMARK 470 LEU B 303 CG CD1 CD2
REMARK 470 LYS B 304 CG CD CE NZ
REMARK 470 TYR B 305 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS B 311 CE NZ
REMARK 470 GLU B 314 CG CD OE1 OE2
REMARK 470 LEU B 343 CG CD1 CD2
REMARK 470 MET B 347 SD CE
REMARK 470 LYS B 374 CG CD CE NZ
REMARK 470 GLU B 375 CG CD OE1 OE2
REMARK 470 ARG B 384 NE CZ NH1 NH2
REMARK 470 GLU B 448 CG CD OE1 OE2
REMARK 470 ASP B 452 CG OD1 OD2
REMARK 470 LYS B 477 CG CD CE NZ
REMARK 470 GLN B 481 OE1 NE2
REMARK 470 LYS B 486 CE NZ
REMARK 470 LEU B 490 CG CD1 CD2
REMARK 470 GLU B 497 CG CD OE1 OE2
REMARK 470 ILE B 498 CG1 CG2 CD1
REMARK 470 GLU B 501 CG CD OE1 OE2
REMARK 470 ASN B 539 CG OD1 ND2
REMARK 470 GLU B 540 CG CD OE1 OE2
REMARK 470 ARG B 547 CG CD NE CZ NH1 NH2
REMARK 470 THR B 611 OG1 CG2
REMARK 470 GLU B 612 CG CD OE1 OE2
REMARK 470 LYS B 631 CE NZ
REMARK 470 ARG B 642 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 653 CG CD CE NZ
REMARK 470 GLU B 657 CG CD OE1 OE2
REMARK 470 GLU B 672 CG CD OE1 OE2
REMARK 470 LYS B 696 CE NZ
REMARK 470 GLU B 716 CG CD OE1 OE2
REMARK 470 LYS B 726 CE NZ
REMARK 470 LYS B 734 CE NZ
REMARK 470 LYS B 739 NZ
REMARK 470 LYS B 743 NZ
REMARK 470 LYS B 746 NZ
REMARK 470 LYS B 765 CE NZ
REMARK 470 GLU B 766 CG CD OE1 OE2
REMARK 470 GLU B 768 CD OE1 OE2
REMARK 470 LYS B 769 CG CD CE NZ
REMARK 470 LYS B 800 CD CE NZ
REMARK 470 LYS B 816 CG CD CE NZ
REMARK 470 ASN B 818 CG OD1 ND2
REMARK 470 ILE B 819 CG1 CG2 CD1
REMARK 470 ASP B 820 CG OD1 OD2
REMARK 470 GLU B 828 CG CD OE1 OE2
REMARK 470 GLU B 837 CD OE1 OE2
REMARK 470 LYS B 844 NZ
REMARK 470 LEU B 857 CG CD1 CD2
REMARK 470 LYS B 859 CG CD CE NZ
REMARK 470 ASP B 860 CG OD1 OD2
REMARK 470 LYS B 874 CE NZ
REMARK 470 GLU B 881 OE1 OE2
REMARK 470 LYS B 893 CD CE NZ
REMARK 470 LYS B 894 CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 DA C 8 O4' - C1' - N9 ANGL. DEV. = 2.8 DEGREES
REMARK 500 DG C 18 O4' - C1' - N9 ANGL. DEV. = 1.8 DEGREES
REMARK 500 DC D 108 O4' - C1' - N1 ANGL. DEV. = 2.3 DEGREES
REMARK 500 DC D 111 O4' - C1' - N1 ANGL. DEV. = 2.3 DEGREES
REMARK 500 DT D 112 O4' - C1' - N1 ANGL. DEV. = 2.0 DEGREES
REMARK 500 DC D 115 O4' - C1' - N1 ANGL. DEV. = 2.7 DEGREES
REMARK 500 DA E 8 O4' - C1' - N9 ANGL. DEV. = 2.3 DEGREES
REMARK 500 DC F 108 O4' - C1' - N1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 DC F 111 O4' - C1' - N1 ANGL. DEV. = 2.1 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 GLN A 45 24.26 -77.78
REMARK 500 ALA A 46 -131.92 39.42
REMARK 500 THR A 47 -179.78 63.08
REMARK 500 TYR A 97 65.87 -116.82
REMARK 500 ASP A 121 43.94 -107.13
REMARK 500 PRO A 179 151.56 -48.31
REMARK 500 PHE A 221 -74.16 -123.12
REMARK 500 ASN A 255 -159.52 -128.79
REMARK 500 VAL A 300 -57.89 -140.68
REMARK 500 GLN A 356 0.29 -69.93
REMARK 500 SER A 414 69.62 24.12
REMARK 500 ASN A 424 45.12 79.48
REMARK 500 ASP A 579 107.61 -164.30
REMARK 500 THR A 622 -76.31 63.81
REMARK 500 GLU A 686 -85.37 -113.86
REMARK 500 GLU A 716 -131.83 54.10
REMARK 500 LEU A 897 -5.88 72.94
REMARK 500 ASP B 21 -159.87 -93.77
REMARK 500 TYR B 97 78.12 -117.08
REMARK 500 LYS B 208 47.21 -143.71
REMARK 500 PHE B 221 -66.69 -129.19
REMARK 500 LEU B 303 14.82 -69.27
REMARK 500 LYS B 304 -115.51 66.94
REMARK 500 TYR B 305 149.07 67.83
REMARK 500 ILE B 355 -56.14 21.67
REMARK 500 SER B 414 77.12 24.70
REMARK 500 ASN B 424 51.90 70.48
REMARK 500 PRO B 458 0.72 -64.57
REMARK 500 THR B 622 -75.21 67.09
REMARK 500 GLU B 686 -74.72 -113.91
REMARK 500 GLU B 716 -122.89 57.28
REMARK 500 GLU B 755 -32.13 -132.13
REMARK 500 ARG B 772 1.39 -64.17
REMARK 500 LYS B 800 17.31 56.55
REMARK 500 ILE B 819 -116.75 63.03
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 NA A1010 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR A 619 OH
REMARK 620 2 ASP A 621 OD2 83.9
REMARK 620 3 DA D 114 O3' 167.1 96.4
REMARK 620 4 DC D 115 OP1 138.7 108.4 53.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A1002 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 623 OD2
REMARK 620 2 HOH A1126 O 80.4
REMARK 620 3 HOH A1317 O 102.8 84.1
REMARK 620 4 XG4 C 101 O2A 92.0 86.8 160.9
REMARK 620 5 XG4 C 101 O3B 153.7 115.5 99.7 69.4
REMARK 620 6 XG4 C 101 O1B 109.0 165.9 103.5 82.5 51.9
REMARK 620 7 XG4 C 101 O1G 156.0 93.4 53.3 110.9 48.9 82.0
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B1004 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 623 OD2
REMARK 620 2 XG4 B1002 O3B 145.2
REMARK 620 3 XG4 B1002 O2A 86.1 63.0
REMARK 620 4 XG4 B1002 O1B 106.4 54.7 78.5
REMARK 620 5 HOH B1126 O 79.5 114.6 141.8 72.1
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE XG4 A 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1004
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1005
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1006
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1007
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1008
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1009
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 1010
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE XG4 C 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE XG4 B 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE XG4 B 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1003
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 1004
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4I9L RELATED DB: PDB
REMARK 900 RELATED ID: 4I9Q RELATED DB: PDB
DBREF 4KHN A 1 903 UNP Q38087 DPOL_BPR69 1 903
DBREF 4KHN B 1 903 UNP Q38087 DPOL_BPR69 1 903
DBREF 4KHN C 1 18 PDB 4KHN 4KHN 1 18
DBREF 4KHN E 1 18 PDB 4KHN 4KHN 1 18
DBREF 4KHN D 103 115 PDB 4KHN 4KHN 103 115
DBREF 4KHN F 103 115 PDB 4KHN 4KHN 103 115
SEQADV 4KHN ALA A 222 UNP Q38087 ASP 222 ENGINEERED MUTATION
SEQADV 4KHN ALA A 327 UNP Q38087 ASP 327 ENGINEERED MUTATION
SEQADV 4KHN ALA A 567 UNP Q38087 TYR 567 ENGINEERED MUTATION
SEQADV 4KHN ALA A 714 UNP Q38087 ASP 714 ENGINEERED MUTATION
SEQADV 4KHN ALA B 222 UNP Q38087 ASP 222 ENGINEERED MUTATION
SEQADV 4KHN ALA B 327 UNP Q38087 ASP 327 ENGINEERED MUTATION
SEQADV 4KHN ALA B 567 UNP Q38087 TYR 567 ENGINEERED MUTATION
SEQADV 4KHN ALA B 714 UNP Q38087 ASP 714 ENGINEERED MUTATION
SEQRES 1 A 903 MET LYS GLU PHE TYR LEU THR VAL GLU GLN ILE GLY ASP
SEQRES 2 A 903 SER ILE PHE GLU ARG TYR ILE ASP SER ASN GLY ARG GLU
SEQRES 3 A 903 ARG THR ARG GLU VAL GLU TYR LYS PRO SER LEU PHE ALA
SEQRES 4 A 903 HIS CYS PRO GLU SER GLN ALA THR LYS TYR PHE ASP ILE
SEQRES 5 A 903 TYR GLY LYS PRO CYS THR ARG LYS LEU PHE ALA ASN MET
SEQRES 6 A 903 ARG ASP ALA SER GLN TRP ILE LYS ARG MET GLU ASP ILE
SEQRES 7 A 903 GLY LEU GLU ALA LEU GLY MET ASP ASP PHE LYS LEU ALA
SEQRES 8 A 903 TYR LEU SER ASP THR TYR ASN TYR GLU ILE LYS TYR ASP
SEQRES 9 A 903 HIS THR LYS ILE ARG VAL ALA ASN PHE ASP ILE GLU VAL
SEQRES 10 A 903 THR SER PRO ASP GLY PHE PRO GLU PRO SER GLN ALA LYS
SEQRES 11 A 903 HIS PRO ILE ASP ALA ILE THR HIS TYR ASP SER ILE ASP
SEQRES 12 A 903 ASP ARG PHE TYR VAL PHE ASP LEU LEU ASN SER PRO TYR
SEQRES 13 A 903 GLY ASN VAL GLU GLU TRP SER ILE GLU ILE ALA ALA LYS
SEQRES 14 A 903 LEU GLN GLU GLN GLY GLY ASP GLU VAL PRO SER GLU ILE
SEQRES 15 A 903 ILE ASP LYS ILE ILE TYR MET PRO PHE ASP ASN GLU LYS
SEQRES 16 A 903 GLU LEU LEU MET GLU TYR LEU ASN PHE TRP GLN GLN LYS
SEQRES 17 A 903 THR PRO VAL ILE LEU THR GLY TRP ASN VAL GLU SER PHE
SEQRES 18 A 903 ALA ILE PRO TYR VAL TYR ASN ARG ILE LYS ASN ILE PHE
SEQRES 19 A 903 GLY GLU SER THR ALA LYS ARG LEU SER PRO HIS ARG LYS
SEQRES 20 A 903 THR ARG VAL LYS VAL ILE GLU ASN MET TYR GLY SER ARG
SEQRES 21 A 903 GLU ILE ILE THR LEU PHE GLY ILE SER VAL LEU ASP TYR
SEQRES 22 A 903 ILE ASP LEU TYR LYS LYS PHE SER PHE THR ASN GLN PRO
SEQRES 23 A 903 SER TYR SER LEU ASP TYR ILE SER GLU PHE GLU LEU ASN
SEQRES 24 A 903 VAL GLY LYS LEU LYS TYR ASP GLY PRO ILE SER LYS LEU
SEQRES 25 A 903 ARG GLU SER ASN HIS GLN ARG TYR ILE SER TYR ASN ILE
SEQRES 26 A 903 ILE ALA VAL TYR ARG VAL LEU GLN ILE ASP ALA LYS ARG
SEQRES 27 A 903 GLN PHE ILE ASN LEU SER LEU ASP MET GLY TYR TYR ALA
SEQRES 28 A 903 LYS ILE GLN ILE GLN SER VAL PHE SER PRO ILE LYS THR
SEQRES 29 A 903 TRP ASP ALA ILE ILE PHE ASN SER LEU LYS GLU GLN ASN
SEQRES 30 A 903 LYS VAL ILE PRO GLN GLY ARG SER HIS PRO VAL GLN PRO
SEQRES 31 A 903 TYR PRO GLY ALA PHE VAL LYS GLU PRO ILE PRO ASN ARG
SEQRES 32 A 903 TYR LYS TYR VAL MET SER PHE ASP LEU THR SER LEU TYR
SEQRES 33 A 903 PRO SER ILE ILE ARG GLN VAL ASN ILE SER PRO GLU THR
SEQRES 34 A 903 ILE ALA GLY THR PHE LYS VAL ALA PRO LEU HIS ASP TYR
SEQRES 35 A 903 ILE ASN ALA VAL ALA GLU ARG PRO SER ASP VAL TYR SER
SEQRES 36 A 903 CYS SER PRO ASN GLY MET MET TYR TYR LYS ASP ARG ASP
SEQRES 37 A 903 GLY VAL VAL PRO THR GLU ILE THR LYS VAL PHE ASN GLN
SEQRES 38 A 903 ARG LYS GLU HIS LYS GLY TYR MET LEU ALA ALA GLN ARG
SEQRES 39 A 903 ASN GLY GLU ILE ILE LYS GLU ALA LEU HIS ASN PRO ASN
SEQRES 40 A 903 LEU SER VAL ASP GLU PRO LEU ASP VAL ASP TYR ARG PHE
SEQRES 41 A 903 ASP PHE SER ASP GLU ILE LYS GLU LYS ILE LYS LYS LEU
SEQRES 42 A 903 SER ALA LYS SER LEU ASN GLU MET LEU PHE ARG ALA GLN
SEQRES 43 A 903 ARG THR GLU VAL ALA GLY MET THR ALA GLN ILE ASN ARG
SEQRES 44 A 903 LYS LEU LEU ILE ASN SER LEU ALA GLY ALA LEU GLY ASN
SEQRES 45 A 903 VAL TRP PHE ARG TYR TYR ASP LEU ARG ASN ALA THR ALA
SEQRES 46 A 903 ILE THR THR PHE GLY GLN MET ALA LEU GLN TRP ILE GLU
SEQRES 47 A 903 ARG LYS VAL ASN GLU TYR LEU ASN GLU VAL CYS GLY THR
SEQRES 48 A 903 GLU GLY GLU ALA PHE VAL LEU TYR GLY ASP THR ASP SER
SEQRES 49 A 903 ILE TYR VAL SER ALA ASP LYS ILE ILE ASP LYS VAL GLY
SEQRES 50 A 903 GLU SER LYS PHE ARG ASP THR ASN HIS TRP VAL ASP PHE
SEQRES 51 A 903 LEU ASP LYS PHE ALA ARG GLU ARG MET GLU PRO ALA ILE
SEQRES 52 A 903 ASP ARG GLY PHE ARG GLU MET CYS GLU TYR MET ASN ASN
SEQRES 53 A 903 LYS GLN HIS LEU MET PHE MET ASP ARG GLU ALA ILE ALA
SEQRES 54 A 903 GLY PRO PRO LEU GLY SER LYS GLY ILE GLY GLY PHE TRP
SEQRES 55 A 903 THR GLY LYS LYS ARG TYR ALA LEU ASN VAL TRP ALA MET
SEQRES 56 A 903 GLU GLY THR ARG TYR ALA GLU PRO LYS LEU LYS ILE MET
SEQRES 57 A 903 GLY LEU GLU THR GLN LYS SER SER THR PRO LYS ALA VAL
SEQRES 58 A 903 GLN LYS ALA LEU LYS GLU CYS ILE ARG ARG MET LEU GLN
SEQRES 59 A 903 GLU GLY GLU GLU SER LEU GLN GLU TYR PHE LYS GLU PHE
SEQRES 60 A 903 GLU LYS GLU PHE ARG GLN LEU ASN TYR ILE SER ILE ALA
SEQRES 61 A 903 SER VAL SER SER ALA ASN ASN ILE ALA LYS TYR ASP VAL
SEQRES 62 A 903 GLY GLY PHE PRO GLY PRO LYS CYS PRO PHE HIS ILE ARG
SEQRES 63 A 903 GLY ILE LEU THR TYR ASN ARG ALA ILE LYS GLY ASN ILE
SEQRES 64 A 903 ASP ALA PRO GLN VAL VAL GLU GLY GLU LYS VAL TYR VAL
SEQRES 65 A 903 LEU PRO LEU ARG GLU GLY ASN PRO PHE GLY ASP LYS CYS
SEQRES 66 A 903 ILE ALA TRP PRO SER GLY THR GLU ILE THR ASP LEU ILE
SEQRES 67 A 903 LYS ASP ASP VAL LEU HIS TRP MET ASP TYR THR VAL LEU
SEQRES 68 A 903 LEU GLU LYS THR PHE ILE LYS PRO LEU GLU GLY PHE THR
SEQRES 69 A 903 SER ALA ALA LYS LEU ASP TYR GLU LYS LYS ALA SER LEU
SEQRES 70 A 903 PHE ASP MET PHE ASP PHE
SEQRES 1 C 18 DT DC DA DC DG DT DA DA DG DC DA DG DT
SEQRES 2 C 18 DC DC DG DC DG
SEQRES 1 D 13 DG DC DG DG DA DC DT DG DC DT DT DA DC
SEQRES 1 E 18 DT DC DA DC DG DT DA DA DG DC DA DG DT
SEQRES 2 E 18 DC DC DG DC DG
SEQRES 1 F 13 DG DC DG DG DA DC DT DG DC DT DT DA DC
SEQRES 1 B 903 MET LYS GLU PHE TYR LEU THR VAL GLU GLN ILE GLY ASP
SEQRES 2 B 903 SER ILE PHE GLU ARG TYR ILE ASP SER ASN GLY ARG GLU
SEQRES 3 B 903 ARG THR ARG GLU VAL GLU TYR LYS PRO SER LEU PHE ALA
SEQRES 4 B 903 HIS CYS PRO GLU SER GLN ALA THR LYS TYR PHE ASP ILE
SEQRES 5 B 903 TYR GLY LYS PRO CYS THR ARG LYS LEU PHE ALA ASN MET
SEQRES 6 B 903 ARG ASP ALA SER GLN TRP ILE LYS ARG MET GLU ASP ILE
SEQRES 7 B 903 GLY LEU GLU ALA LEU GLY MET ASP ASP PHE LYS LEU ALA
SEQRES 8 B 903 TYR LEU SER ASP THR TYR ASN TYR GLU ILE LYS TYR ASP
SEQRES 9 B 903 HIS THR LYS ILE ARG VAL ALA ASN PHE ASP ILE GLU VAL
SEQRES 10 B 903 THR SER PRO ASP GLY PHE PRO GLU PRO SER GLN ALA LYS
SEQRES 11 B 903 HIS PRO ILE ASP ALA ILE THR HIS TYR ASP SER ILE ASP
SEQRES 12 B 903 ASP ARG PHE TYR VAL PHE ASP LEU LEU ASN SER PRO TYR
SEQRES 13 B 903 GLY ASN VAL GLU GLU TRP SER ILE GLU ILE ALA ALA LYS
SEQRES 14 B 903 LEU GLN GLU GLN GLY GLY ASP GLU VAL PRO SER GLU ILE
SEQRES 15 B 903 ILE ASP LYS ILE ILE TYR MET PRO PHE ASP ASN GLU LYS
SEQRES 16 B 903 GLU LEU LEU MET GLU TYR LEU ASN PHE TRP GLN GLN LYS
SEQRES 17 B 903 THR PRO VAL ILE LEU THR GLY TRP ASN VAL GLU SER PHE
SEQRES 18 B 903 ALA ILE PRO TYR VAL TYR ASN ARG ILE LYS ASN ILE PHE
SEQRES 19 B 903 GLY GLU SER THR ALA LYS ARG LEU SER PRO HIS ARG LYS
SEQRES 20 B 903 THR ARG VAL LYS VAL ILE GLU ASN MET TYR GLY SER ARG
SEQRES 21 B 903 GLU ILE ILE THR LEU PHE GLY ILE SER VAL LEU ASP TYR
SEQRES 22 B 903 ILE ASP LEU TYR LYS LYS PHE SER PHE THR ASN GLN PRO
SEQRES 23 B 903 SER TYR SER LEU ASP TYR ILE SER GLU PHE GLU LEU ASN
SEQRES 24 B 903 VAL GLY LYS LEU LYS TYR ASP GLY PRO ILE SER LYS LEU
SEQRES 25 B 903 ARG GLU SER ASN HIS GLN ARG TYR ILE SER TYR ASN ILE
SEQRES 26 B 903 ILE ALA VAL TYR ARG VAL LEU GLN ILE ASP ALA LYS ARG
SEQRES 27 B 903 GLN PHE ILE ASN LEU SER LEU ASP MET GLY TYR TYR ALA
SEQRES 28 B 903 LYS ILE GLN ILE GLN SER VAL PHE SER PRO ILE LYS THR
SEQRES 29 B 903 TRP ASP ALA ILE ILE PHE ASN SER LEU LYS GLU GLN ASN
SEQRES 30 B 903 LYS VAL ILE PRO GLN GLY ARG SER HIS PRO VAL GLN PRO
SEQRES 31 B 903 TYR PRO GLY ALA PHE VAL LYS GLU PRO ILE PRO ASN ARG
SEQRES 32 B 903 TYR LYS TYR VAL MET SER PHE ASP LEU THR SER LEU TYR
SEQRES 33 B 903 PRO SER ILE ILE ARG GLN VAL ASN ILE SER PRO GLU THR
SEQRES 34 B 903 ILE ALA GLY THR PHE LYS VAL ALA PRO LEU HIS ASP TYR
SEQRES 35 B 903 ILE ASN ALA VAL ALA GLU ARG PRO SER ASP VAL TYR SER
SEQRES 36 B 903 CYS SER PRO ASN GLY MET MET TYR TYR LYS ASP ARG ASP
SEQRES 37 B 903 GLY VAL VAL PRO THR GLU ILE THR LYS VAL PHE ASN GLN
SEQRES 38 B 903 ARG LYS GLU HIS LYS GLY TYR MET LEU ALA ALA GLN ARG
SEQRES 39 B 903 ASN GLY GLU ILE ILE LYS GLU ALA LEU HIS ASN PRO ASN
SEQRES 40 B 903 LEU SER VAL ASP GLU PRO LEU ASP VAL ASP TYR ARG PHE
SEQRES 41 B 903 ASP PHE SER ASP GLU ILE LYS GLU LYS ILE LYS LYS LEU
SEQRES 42 B 903 SER ALA LYS SER LEU ASN GLU MET LEU PHE ARG ALA GLN
SEQRES 43 B 903 ARG THR GLU VAL ALA GLY MET THR ALA GLN ILE ASN ARG
SEQRES 44 B 903 LYS LEU LEU ILE ASN SER LEU ALA GLY ALA LEU GLY ASN
SEQRES 45 B 903 VAL TRP PHE ARG TYR TYR ASP LEU ARG ASN ALA THR ALA
SEQRES 46 B 903 ILE THR THR PHE GLY GLN MET ALA LEU GLN TRP ILE GLU
SEQRES 47 B 903 ARG LYS VAL ASN GLU TYR LEU ASN GLU VAL CYS GLY THR
SEQRES 48 B 903 GLU GLY GLU ALA PHE VAL LEU TYR GLY ASP THR ASP SER
SEQRES 49 B 903 ILE TYR VAL SER ALA ASP LYS ILE ILE ASP LYS VAL GLY
SEQRES 50 B 903 GLU SER LYS PHE ARG ASP THR ASN HIS TRP VAL ASP PHE
SEQRES 51 B 903 LEU ASP LYS PHE ALA ARG GLU ARG MET GLU PRO ALA ILE
SEQRES 52 B 903 ASP ARG GLY PHE ARG GLU MET CYS GLU TYR MET ASN ASN
SEQRES 53 B 903 LYS GLN HIS LEU MET PHE MET ASP ARG GLU ALA ILE ALA
SEQRES 54 B 903 GLY PRO PRO LEU GLY SER LYS GLY ILE GLY GLY PHE TRP
SEQRES 55 B 903 THR GLY LYS LYS ARG TYR ALA LEU ASN VAL TRP ALA MET
SEQRES 56 B 903 GLU GLY THR ARG TYR ALA GLU PRO LYS LEU LYS ILE MET
SEQRES 57 B 903 GLY LEU GLU THR GLN LYS SER SER THR PRO LYS ALA VAL
SEQRES 58 B 903 GLN LYS ALA LEU LYS GLU CYS ILE ARG ARG MET LEU GLN
SEQRES 59 B 903 GLU GLY GLU GLU SER LEU GLN GLU TYR PHE LYS GLU PHE
SEQRES 60 B 903 GLU LYS GLU PHE ARG GLN LEU ASN TYR ILE SER ILE ALA
SEQRES 61 B 903 SER VAL SER SER ALA ASN ASN ILE ALA LYS TYR ASP VAL
SEQRES 62 B 903 GLY GLY PHE PRO GLY PRO LYS CYS PRO PHE HIS ILE ARG
SEQRES 63 B 903 GLY ILE LEU THR TYR ASN ARG ALA ILE LYS GLY ASN ILE
SEQRES 64 B 903 ASP ALA PRO GLN VAL VAL GLU GLY GLU LYS VAL TYR VAL
SEQRES 65 B 903 LEU PRO LEU ARG GLU GLY ASN PRO PHE GLY ASP LYS CYS
SEQRES 66 B 903 ILE ALA TRP PRO SER GLY THR GLU ILE THR ASP LEU ILE
SEQRES 67 B 903 LYS ASP ASP VAL LEU HIS TRP MET ASP TYR THR VAL LEU
SEQRES 68 B 903 LEU GLU LYS THR PHE ILE LYS PRO LEU GLU GLY PHE THR
SEQRES 69 B 903 SER ALA ALA LYS LEU ASP TYR GLU LYS LYS ALA SER LEU
SEQRES 70 B 903 PHE ASP MET PHE ASP PHE
HET XG4 A1001 31
HET CA A1002 1
HET SO4 A1003 5
HET SO4 A1004 5
HET SO4 A1005 5
HET SO4 A1006 5
HET SO4 A1007 5
HET GOL A1008 6
HET GOL A1009 6
HET NA A1010 1
HET XG4 C 101 31
HET XG4 B1001 31
HET XG4 B1002 31
HET SO4 B1003 5
HET CA B1004 1
HETNAM XG4 2'-DEOXY-5'-O-[(R)-HYDROXY{[(R)-HYDROXY(PHOSPHONOOXY)
HETNAM 2 XG4 PHOSPHORYL]AMINO}PHOSPHORYL]GUANOSINE
HETNAM CA CALCIUM ION
HETNAM SO4 SULFATE ION
HETNAM GOL GLYCEROL
HETNAM NA SODIUM ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 7 XG4 4(C10 H17 N6 O12 P3)
FORMUL 8 CA 2(CA 2+)
FORMUL 9 SO4 6(O4 S 2-)
FORMUL 14 GOL 2(C3 H8 O3)
FORMUL 16 NA NA 1+
FORMUL 22 HOH *304(H2 O)
HELIX 1 1 ASN A 64 GLY A 79 1 16
HELIX 2 2 ASP A 87 TYR A 97 1 11
HELIX 3 3 ASP A 104 ILE A 108 5 5
HELIX 4 4 SER A 163 LYS A 169 1 7
HELIX 5 5 LEU A 170 GLY A 174 5 5
HELIX 6 6 PRO A 179 ASP A 184 1 6
HELIX 7 7 ASN A 193 LYS A 208 1 16
HELIX 8 8 PHE A 221 GLY A 235 1 15
HELIX 9 9 GLY A 235 LYS A 240 1 6
HELIX 10 10 ARG A 241 SER A 243 5 3
HELIX 11 11 ASP A 272 SER A 281 1 10
HELIX 12 12 SER A 289 ASN A 299 1 11
HELIX 13 13 PRO A 308 SER A 310 5 3
HELIX 14 14 LYS A 311 ASN A 316 1 6
HELIX 15 15 ASN A 316 GLN A 339 1 24
HELIX 16 16 GLN A 339 LYS A 352 1 14
HELIX 17 17 GLN A 354 PHE A 359 5 6
HELIX 18 18 SER A 360 GLN A 376 1 17
HELIX 19 19 SER A 414 ASN A 424 1 11
HELIX 20 20 PRO A 438 ASN A 444 1 7
HELIX 21 21 GLY A 469 LEU A 503 1 35
HELIX 22 22 SER A 523 LYS A 531 1 9
HELIX 23 23 SER A 534 LEU A 570 1 37
HELIX 24 24 ASP A 579 GLY A 610 1 32
HELIX 25 25 ALA A 629 GLY A 637 1 9
HELIX 26 26 GLU A 638 PHE A 641 5 4
HELIX 27 27 ASP A 643 ARG A 658 1 16
HELIX 28 28 ARG A 658 MET A 674 1 17
HELIX 29 29 LEU A 730 LYS A 734 5 5
HELIX 30 30 PRO A 738 GLU A 755 1 18
HELIX 31 31 GLY A 756 PHE A 771 1 16
HELIX 32 32 ARG A 772 LEU A 774 5 3
HELIX 33 33 ILE A 788 LYS A 790 5 3
HELIX 34 34 PRO A 802 LYS A 816 1 15
HELIX 35 35 ILE A 858 MET A 866 1 9
HELIX 36 36 ASP A 867 PHE A 876 1 10
HELIX 37 37 PHE A 876 ALA A 887 1 12
HELIX 38 38 ASN B 64 GLY B 79 1 16
HELIX 39 39 ASP B 87 TYR B 97 1 11
HELIX 40 40 ASP B 104 ILE B 108 5 5
HELIX 41 41 SER B 163 LYS B 169 1 7
HELIX 42 42 LEU B 170 GLY B 174 5 5
HELIX 43 43 PRO B 179 ASP B 184 1 6
HELIX 44 44 ASN B 193 LYS B 208 1 16
HELIX 45 45 PHE B 221 ASN B 232 1 12
HELIX 46 46 GLY B 235 LYS B 240 1 6
HELIX 47 47 ARG B 241 SER B 243 5 3
HELIX 48 48 ASP B 272 SER B 281 1 10
HELIX 49 49 SER B 289 ASN B 299 1 11
HELIX 50 50 PRO B 308 SER B 310 5 3
HELIX 51 51 LYS B 311 ASN B 316 1 6
HELIX 52 52 ASN B 316 GLN B 339 1 24
HELIX 53 53 GLN B 339 LYS B 352 1 14
HELIX 54 54 SER B 360 GLU B 375 1 16
HELIX 55 55 SER B 414 ASN B 424 1 11
HELIX 56 56 PRO B 438 ASN B 444 1 7
HELIX 57 57 GLY B 469 ASN B 495 1 27
HELIX 58 58 LYS B 536 LEU B 570 1 35
HELIX 59 59 ASP B 579 CYS B 609 1 31
HELIX 60 60 ALA B 629 GLY B 637 1 9
HELIX 61 61 GLU B 638 PHE B 641 5 4
HELIX 62 62 ASP B 643 ARG B 658 1 16
HELIX 63 63 ARG B 658 MET B 674 1 17
HELIX 64 64 LEU B 730 LYS B 734 5 5
HELIX 65 65 PRO B 738 GLU B 755 1 18
HELIX 66 66 GLY B 756 PHE B 771 1 16
HELIX 67 67 ARG B 772 LEU B 774 5 3
HELIX 68 68 ASN B 775 ALA B 780 1 6
HELIX 69 69 ILE B 788 LYS B 790 5 3
HELIX 70 70 PRO B 802 LYS B 816 1 15
HELIX 71 71 THR B 855 MET B 866 1 12
HELIX 72 72 ASP B 867 PHE B 876 1 10
HELIX 73 73 PHE B 876 LYS B 888 1 13
HELIX 74 74 SER B 896 PHE B 901 5 6
SHEET 1 A 3 PHE A 4 ILE A 11 0
SHEET 2 A 3 SER A 14 ILE A 20 -1 O PHE A 16 N GLU A 9
SHEET 3 A 3 GLU A 26 VAL A 31 -1 O ARG A 27 N TYR A 19
SHEET 1 B 2 SER A 36 HIS A 40 0
SHEET 2 B 2 CYS A 57 LEU A 61 -1 O LYS A 60 N LEU A 37
SHEET 1 C 2 PHE A 50 ASP A 51 0
SHEET 2 C 2 LYS A 378 VAL A 379 1 O VAL A 379 N PHE A 50
SHEET 1 D 6 ILE A 186 PHE A 191 0
SHEET 2 D 6 ARG A 145 LEU A 151 1 N VAL A 148 O ILE A 187
SHEET 3 D 6 ALA A 135 ASP A 140 -1 N ILE A 136 O PHE A 149
SHEET 4 D 6 VAL A 110 GLU A 116 -1 N ASN A 112 O TYR A 139
SHEET 5 D 6 ILE A 212 THR A 214 1 O ILE A 212 N ALA A 111
SHEET 6 D 6 SER A 269 VAL A 270 1 O SER A 269 N LEU A 213
SHEET 1 E 2 ASN A 153 SER A 154 0
SHEET 2 E 2 GLY A 157 ASN A 158 -1 O GLY A 157 N SER A 154
SHEET 1 F 2 THR A 248 GLU A 254 0
SHEET 2 F 2 SER A 259 LEU A 265 -1 O THR A 264 N ARG A 249
SHEET 1 G 7 ASN A 402 ARG A 403 0
SHEET 2 G 7 GLY A 700 GLY A 704 -1 O TRP A 702 N ASN A 402
SHEET 3 G 7 ARG A 707 MET A 715 -1 O ALA A 709 N PHE A 701
SHEET 4 G 7 MET A 683 ALA A 689 -1 N ILE A 688 O TRP A 713
SHEET 5 G 7 VAL A 407 LEU A 412 -1 N VAL A 407 O ALA A 689
SHEET 6 G 7 SER A 624 SER A 628 -1 O VAL A 627 N MET A 408
SHEET 7 G 7 VAL A 617 ASP A 621 -1 N TYR A 619 O TYR A 626
SHEET 1 H 4 ASN A 402 ARG A 403 0
SHEET 2 H 4 GLY A 700 GLY A 704 -1 O TRP A 702 N ASN A 402
SHEET 3 H 4 ARG A 707 MET A 715 -1 O ALA A 709 N PHE A 701
SHEET 4 H 4 THR A 718 MET A 728 -1 O LYS A 726 N LEU A 710
SHEET 1 I 3 ILE A 430 THR A 433 0
SHEET 2 I 3 MET A 461 TYR A 463 -1 O MET A 462 N ALA A 431
SHEET 3 I 3 SER A 455 CYS A 456 -1 N SER A 455 O TYR A 463
SHEET 1 J 3 SER A 781 SER A 784 0
SHEET 2 J 3 LYS A 829 PRO A 834 -1 O VAL A 830 N SER A 783
SHEET 3 J 3 CYS A 845 PRO A 849 -1 O ILE A 846 N LEU A 833
SHEET 1 K 2 ASP A 792 VAL A 793 0
SHEET 2 K 2 PHE A 796 PRO A 797 -1 O PHE A 796 N VAL A 793
SHEET 1 L 3 PHE B 4 ILE B 11 0
SHEET 2 L 3 SER B 14 ILE B 20 -1 O SER B 14 N ILE B 11
SHEET 3 L 3 GLU B 26 VAL B 31 -1 O ARG B 27 N TYR B 19
SHEET 1 M 5 ALA B 82 LEU B 83 0
SHEET 2 M 5 SER B 36 HIS B 40 -1 N PHE B 38 O LEU B 83
SHEET 3 M 5 PRO B 56 LEU B 61 -1 O LYS B 60 N LEU B 37
SHEET 4 M 5 TYR B 49 ASP B 51 -1 N TYR B 49 O CYS B 57
SHEET 5 M 5 LYS B 378 VAL B 379 1 O VAL B 379 N PHE B 50
SHEET 1 N 6 ILE B 186 PHE B 191 0
SHEET 2 N 6 ARG B 145 LEU B 151 1 N ASP B 150 O PHE B 191
SHEET 3 N 6 ILE B 133 ASP B 140 -1 N HIS B 138 O TYR B 147
SHEET 4 N 6 VAL B 110 VAL B 117 -1 N ASN B 112 O TYR B 139
SHEET 5 N 6 ILE B 212 THR B 214 1 O THR B 214 N ALA B 111
SHEET 6 N 6 SER B 269 VAL B 270 1 O SER B 269 N LEU B 213
SHEET 1 O 2 THR B 248 GLU B 254 0
SHEET 2 O 2 SER B 259 LEU B 265 -1 O THR B 264 N ARG B 249
SHEET 1 P 7 ASN B 402 ARG B 403 0
SHEET 2 P 7 GLY B 700 GLY B 704 -1 O TRP B 702 N ASN B 402
SHEET 3 P 7 ARG B 707 MET B 715 -1 O ARG B 707 N THR B 703
SHEET 4 P 7 MET B 683 ALA B 689 -1 N ILE B 688 O TRP B 713
SHEET 5 P 7 VAL B 407 LEU B 412 -1 N SER B 409 O GLU B 686
SHEET 6 P 7 SER B 624 SER B 628 -1 O VAL B 627 N MET B 408
SHEET 7 P 7 VAL B 617 ASP B 621 -1 N TYR B 619 O TYR B 626
SHEET 1 Q 4 ASN B 402 ARG B 403 0
SHEET 2 Q 4 GLY B 700 GLY B 704 -1 O TRP B 702 N ASN B 402
SHEET 3 Q 4 ARG B 707 MET B 715 -1 O ARG B 707 N THR B 703
SHEET 4 Q 4 THR B 718 MET B 728 -1 O LYS B 724 N VAL B 712
SHEET 1 R 3 ILE B 430 THR B 433 0
SHEET 2 R 3 MET B 461 TYR B 463 -1 O MET B 462 N ALA B 431
SHEET 3 R 3 SER B 455 CYS B 456 -1 N SER B 455 O TYR B 463
SHEET 1 S 3 SER B 781 SER B 784 0
SHEET 2 S 3 LYS B 829 PRO B 834 -1 O VAL B 830 N SER B 783
SHEET 3 S 3 CYS B 845 PRO B 849 -1 O TRP B 848 N TYR B 831
SHEET 1 T 2 ASP B 792 VAL B 793 0
SHEET 2 T 2 PHE B 796 PRO B 797 -1 O PHE B 796 N VAL B 793
LINK OH TYR A 619 NA NA A1010 1555 1555 2.68
LINK OD2 ASP A 621 NA NA A1010 1555 1555 2.44
LINK OD2 ASP A 623 CA CA A1002 1555 1555 2.33
LINK CA CA A1002 O HOH A1126 1555 1555 2.68
LINK CA CA A1002 O HOH A1317 1555 1555 2.20
LINK CA CA A1002 O2A XG4 C 101 1555 1555 2.20
LINK CA CA A1002 O3B XG4 C 101 1555 1555 2.44
LINK CA CA A1002 O1B XG4 C 101 1555 1555 3.08
LINK CA CA A1002 O1G XG4 C 101 1555 1555 3.10
LINK NA NA A1010 O3' DA D 114 1555 1555 2.84
LINK NA NA A1010 OP1 DC D 115 1555 1555 2.65
LINK OD2 ASP B 623 CA CA B1004 1555 1555 2.55
LINK O3B XG4 B1002 CA CA B1004 1555 1555 2.52
LINK O2A XG4 B1002 CA CA B1004 1555 1555 2.68
LINK O1B XG4 B1002 CA CA B1004 1555 1555 2.94
LINK CA CA B1004 O HOH B1126 1555 1555 3.11
SITE 1 AC1 13 SER A 36 PHE A 38 LYS A 48 TYR A 49
SITE 2 AC1 13 ARG A 59 GLY A 84 MET A 85 ASP A 95
SITE 3 AC1 13 PHE A 370 LYS A 374 LYS A 378 VAL A 379
SITE 4 AC1 13 ILE A 380
SITE 1 AC2 4 ASP A 623 HOH A1126 HOH A1317 XG4 C 101
SITE 1 AC3 6 THR A 413 SER A 414 ARG A 482 LYS A 486
SITE 2 AC3 6 LYS A 560 HOH A1126
SITE 1 AC4 4 TRP A 216 ASN A 217 SER A 289 LEU A 290
SITE 1 AC5 3 GLY A 637 GLU A 638 SER A 639
SITE 1 AC6 3 TYR A 49 ARG A 59 HOH A1151
SITE 1 AC7 2 HIS A 105 VAL A 110
SITE 1 AC8 4 ILE A 557 LEU A 561 ASN A 564 XG4 C 101
SITE 1 AC9 4 PHE A 650 LYS A 653 PHE A 654 ARG A 658
SITE 1 BC1 5 TYR A 619 ASP A 621 LYS A 706 DA D 114
SITE 2 BC1 5 DC D 115
SITE 1 BC2 14 LEU A 415 TYR A 416 LYS A 560 ASN A 564
SITE 2 BC2 14 THR A 622 ASP A 623 CA A1002 GOL A1008
SITE 3 BC2 14 HOH A1114 HOH A1317 DC C 4 DG C 5
SITE 4 BC2 14 HOH C 201 DC D 115
SITE 1 BC3 13 SER B 36 PHE B 38 TYR B 49 GLY B 84
SITE 2 BC3 13 MET B 85 ASP B 95 PHE B 370 LYS B 374
SITE 3 BC3 13 ASN B 377 LYS B 378 VAL B 379 ILE B 380
SITE 4 BC3 13 HOH B1101
SITE 1 BC4 11 LEU B 415 TYR B 416 LYS B 560 ASN B 564
SITE 2 BC4 11 THR B 622 ASP B 623 SO4 B1003 CA B1004
SITE 3 BC4 11 DC E 4 DG E 5 DC F 115
SITE 1 BC5 5 THR B 413 SER B 414 ARG B 482 LYS B 560
SITE 2 BC5 5 XG4 B1002
SITE 1 BC6 2 ASP B 623 XG4 B1002
CRYST1 74.258 119.353 148.031 90.00 91.64 90.00 P 1 21 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 0.013467 0.000000 0.000386 0.00000
SCALE2 0.000000 0.008379 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006758 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
