HEADER TRANSFERASE,TOXIN/IMMUNE SYSTEM 17-JAN-25 9MX1 TITLE CLOSTRIDIOIDES DIFFICILE TOXIN A WITH MCDIFA-248-25 FAB COMPND MOL_ID: 1; COMPND 2 MOLECULE: TOXIN A; COMPND 3 CHAIN: A; COMPND 4 EC: 3.4.22.-; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: MCDIFA-248-25 FAB HEAVY CHAIN; COMPND 8 CHAIN: B; COMPND 9 ENGINEERED: YES; COMPND 10 MOL_ID: 3; COMPND 11 MOLECULE: MCDIFA-248-25 FAB LIGHT CHAIN; COMPND 12 CHAIN: C; COMPND 13 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: CLOSTRIDIOIDES DIFFICILE; SOURCE 3 ORGANISM_TAXID: 1496; SOURCE 4 GENE: TCDA, TOXA; SOURCE 5 EXPRESSION_SYSTEM: CLOSTRIDIOIDES DIFFICILE; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 1496; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 9 ORGANISM_TAXID: 10090; SOURCE 10 EXPRESSION_SYSTEM: MUS MUSCULUS; SOURCE 11 EXPRESSION_SYSTEM_TAXID: 10090; SOURCE 12 MOL_ID: 3; SOURCE 13 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 14 ORGANISM_TAXID: 10090; SOURCE 15 EXPRESSION_SYSTEM: MUS MUSCULUS; SOURCE 16 EXPRESSION_SYSTEM_TAXID: 10090 KEYWDS TOXIN A, TCDA, C.DIFF, COMPLEX, TRANSFERASE, TOXIN-IMMUNE SYSTEM KEYWDS 2 COMPLEX EXPDTA ELECTRON MICROSCOPY AUTHOR K.W.HUYNH,M.AMMIRATI,H.K.KROH,D.B.LACY,S.HAN REVDAT 1 09-JUL-25 9MX1 0 JRNL AUTH H.K.KROH,J.L.JENSEN,S.WELLNITZ,J.J.PARK,A.ESADZE,K.W.HUYNH, JRNL AUTH 2 M.AMMIRATI,S.HAN,A.S.ANDERSON,D.B.LACY,A.GRIBENKO JRNL TITL MOUSE MONOCLONAL ANTIBODIES AGAINST CLOSTRIDIOIDES DIFFICILE JRNL TITL 2 TOXINS TCDA AND TCDB TARGET DIVERSE EPITOPES FOR JRNL TITL 3 NEUTRALIZATION JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 3.20 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : WARP, RELION, SERIALEM, CTFFIND, REMARK 3 RELION, RELION, PHENIX REMARK 3 RECONSTRUCTION SCHEMA : NULL REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : NULL REMARK 3 REFINEMENT SPACE : NULL REMARK 3 REFINEMENT PROTOCOL : NULL REMARK 3 REFINEMENT TARGET : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL REMARK 3 REMARK 3 FITTING PROCEDURE : NULL REMARK 3 REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 3.200 REMARK 3 NUMBER OF PARTICLES : 212265 REMARK 3 CTF CORRECTION METHOD : NONE REMARK 3 REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL REMARK 3 REMARK 3 OTHER DETAILS: NULL REMARK 4 REMARK 4 9MX1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-JAN-25. REMARK 100 THE DEPOSITION ID IS D_1000291881. REMARK 245 REMARK 245 EXPERIMENTAL DETAILS REMARK 245 RECONSTRUCTION METHOD : SINGLE PARTICLE REMARK 245 SPECIMEN TYPE : NULL REMARK 245 REMARK 245 ELECTRON MICROSCOPE SAMPLE REMARK 245 SAMPLE TYPE : PARTICLE REMARK 245 PARTICLE TYPE : POINT REMARK 245 NAME OF SAMPLE : CLOSTRIDIOIDES DIFFICILE TOXIN REMARK 245 A WITH MCDIFA-248-25 FAB REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 0.13 REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 7.50 REMARK 245 SAMPLE DETAILS : NULL REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : NULL REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : 2511 REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : TFS KRIOS REMARK 245 DETECTOR TYPE : GATAN K2 SUMMIT (4K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 1500.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 2500.00 REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 NOMINAL CS : 2.70 REMARK 245 IMAGING MODE : BRIGHT FIELD REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 5220.00 REMARK 245 ILLUMINATION MODE : FLOOD BEAM REMARK 245 NOMINAL MAGNIFICATION : 165000 REMARK 245 CALIBRATED MAGNIFICATION : NULL REMARK 245 SOURCE : FIELD EMISSION GUN REMARK 245 ACCELERATION VOLTAGE (KV) : 300 REMARK 245 IMAGING DETAILS : NULL REMARK 247 REMARK 247 ELECTRON MICROSCOPY REMARK 247 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON REMARK 247 MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE REMARK 247 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES REMARK 247 ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION REMARK 247 OF THE STRUCTURE FACTORS. 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: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C 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 SER A 2 REMARK 465 LEU A 3 REMARK 465 ALA A 2367 REMARK 465 THR A 2368 REMARK 465 GLY A 2369 REMARK 465 TRP A 2370 REMARK 465 GLN A 2371 REMARK 465 THR A 2372 REMARK 465 ILE A 2373 REMARK 465 ASP A 2374 REMARK 465 GLY A 2375 REMARK 465 LYS A 2376 REMARK 465 LYS A 2377 REMARK 465 TYR A 2378 REMARK 465 TYR A 2379 REMARK 465 PHE A 2380 REMARK 465 ASN A 2381 REMARK 465 THR A 2382 REMARK 465 ASN A 2383 REMARK 465 THR A 2384 REMARK 465 PHE A 2385 REMARK 465 ILE A 2386 REMARK 465 ALA A 2387 REMARK 465 SER A 2388 REMARK 465 THR A 2389 REMARK 465 GLY A 2390 REMARK 465 TYR A 2391 REMARK 465 THR A 2392 REMARK 465 SER A 2393 REMARK 465 ILE A 2394 REMARK 465 ASN A 2395 REMARK 465 GLY A 2396 REMARK 465 LYS A 2397 REMARK 465 HIS A 2398 REMARK 465 PHE A 2399 REMARK 465 TYR A 2400 REMARK 465 PHE A 2401 REMARK 465 ASN A 2402 REMARK 465 THR A 2403 REMARK 465 ASP A 2404 REMARK 465 GLY A 2405 REMARK 465 ILE A 2406 REMARK 465 MET A 2407 REMARK 465 GLN A 2408 REMARK 465 ILE A 2409 REMARK 465 GLY A 2410 REMARK 465 VAL A 2411 REMARK 465 PHE A 2412 REMARK 465 LYS A 2413 REMARK 465 GLY A 2414 REMARK 465 PRO A 2415 REMARK 465 ASN A 2416 REMARK 465 GLY A 2417 REMARK 465 PHE A 2418 REMARK 465 GLU A 2419 REMARK 465 TYR A 2420 REMARK 465 PHE A 2421 REMARK 465 ALA A 2422 REMARK 465 PRO A 2423 REMARK 465 ALA A 2424 REMARK 465 ASN A 2425 REMARK 465 THR A 2426 REMARK 465 HIS A 2427 REMARK 465 ASN A 2428 REMARK 465 ASN A 2429 REMARK 465 ASN A 2430 REMARK 465 ILE A 2431 REMARK 465 GLU A 2432 REMARK 465 GLY A 2433 REMARK 465 GLN A 2434 REMARK 465 ALA A 2435 REMARK 465 ILE A 2436 REMARK 465 LEU A 2437 REMARK 465 TYR A 2438 REMARK 465 GLN A 2439 REMARK 465 ASN A 2440 REMARK 465 LYS A 2441 REMARK 465 PHE A 2442 REMARK 465 LEU A 2443 REMARK 465 THR A 2444 REMARK 465 LEU A 2445 REMARK 465 ASN A 2446 REMARK 465 GLY A 2447 REMARK 465 LYS A 2448 REMARK 465 LYS A 2449 REMARK 465 TYR A 2450 REMARK 465 TYR A 2451 REMARK 465 PHE A 2452 REMARK 465 GLY A 2453 REMARK 465 SER A 2454 REMARK 465 ASP A 2455 REMARK 465 SER A 2456 REMARK 465 LYS A 2457 REMARK 465 ALA A 2458 REMARK 465 VAL A 2459 REMARK 465 THR A 2460 REMARK 465 GLY A 2461 REMARK 465 LEU A 2462 REMARK 465 ARG A 2463 REMARK 465 THR A 2464 REMARK 465 ILE A 2465 REMARK 465 ASP A 2466 REMARK 465 GLY A 2467 REMARK 465 LYS A 2468 REMARK 465 LYS A 2469 REMARK 465 TYR A 2470 REMARK 465 TYR A 2471 REMARK 465 PHE A 2472 REMARK 465 ASN A 2473 REMARK 465 THR A 2474 REMARK 465 ASN A 2475 REMARK 465 THR A 2476 REMARK 465 ALA A 2477 REMARK 465 VAL A 2478 REMARK 465 ALA A 2479 REMARK 465 VAL A 2480 REMARK 465 THR A 2481 REMARK 465 GLY A 2482 REMARK 465 TRP A 2483 REMARK 465 GLN A 2484 REMARK 465 THR A 2485 REMARK 465 ILE A 2486 REMARK 465 ASN A 2487 REMARK 465 GLY A 2488 REMARK 465 LYS A 2489 REMARK 465 LYS A 2490 REMARK 465 TYR A 2491 REMARK 465 TYR A 2492 REMARK 465 PHE A 2493 REMARK 465 ASN A 2494 REMARK 465 THR A 2495 REMARK 465 ASN A 2496 REMARK 465 THR A 2497 REMARK 465 SER A 2498 REMARK 465 ILE A 2499 REMARK 465 ALA A 2500 REMARK 465 SER A 2501 REMARK 465 THR A 2502 REMARK 465 GLY A 2503 REMARK 465 TYR A 2504 REMARK 465 THR A 2505 REMARK 465 ILE A 2506 REMARK 465 ILE A 2507 REMARK 465 SER A 2508 REMARK 465 GLY A 2509 REMARK 465 LYS A 2510 REMARK 465 HIS A 2511 REMARK 465 PHE A 2512 REMARK 465 TYR A 2513 REMARK 465 PHE A 2514 REMARK 465 ASN A 2515 REMARK 465 THR A 2516 REMARK 465 ASP A 2517 REMARK 465 GLY A 2518 REMARK 465 ILE A 2519 REMARK 465 MET A 2520 REMARK 465 GLN A 2521 REMARK 465 ILE A 2522 REMARK 465 GLY A 2523 REMARK 465 VAL A 2524 REMARK 465 PHE A 2525 REMARK 465 LYS A 2526 REMARK 465 GLY A 2527 REMARK 465 PRO A 2528 REMARK 465 ASP A 2529 REMARK 465 GLY A 2530 REMARK 465 PHE A 2531 REMARK 465 GLU A 2532 REMARK 465 TYR A 2533 REMARK 465 PHE A 2534 REMARK 465 ALA A 2535 REMARK 465 PRO A 2536 REMARK 465 ALA A 2537 REMARK 465 ASN A 2538 REMARK 465 THR A 2539 REMARK 465 ASP A 2540 REMARK 465 ALA A 2541 REMARK 465 ASN A 2542 REMARK 465 ASN A 2543 REMARK 465 ILE A 2544 REMARK 465 GLU A 2545 REMARK 465 GLY A 2546 REMARK 465 GLN A 2547 REMARK 465 ALA A 2548 REMARK 465 ILE A 2549 REMARK 465 ARG A 2550 REMARK 465 TYR A 2551 REMARK 465 GLN A 2552 REMARK 465 ASN A 2553 REMARK 465 ARG A 2554 REMARK 465 PHE A 2555 REMARK 465 LEU A 2556 REMARK 465 TYR A 2557 REMARK 465 LEU A 2558 REMARK 465 HIS A 2559 REMARK 465 ASP A 2560 REMARK 465 ASN A 2561 REMARK 465 ILE A 2562 REMARK 465 TYR A 2563 REMARK 465 TYR A 2564 REMARK 465 PHE A 2565 REMARK 465 GLY A 2566 REMARK 465 ASN A 2567 REMARK 465 ASN A 2568 REMARK 465 SER A 2569 REMARK 465 LYS A 2570 REMARK 465 ALA A 2571 REMARK 465 ALA A 2572 REMARK 465 THR A 2573 REMARK 465 GLY A 2574 REMARK 465 TRP A 2575 REMARK 465 VAL A 2576 REMARK 465 THR A 2577 REMARK 465 ILE A 2578 REMARK 465 ASP A 2579 REMARK 465 GLY A 2580 REMARK 465 ASN A 2581 REMARK 465 ARG A 2582 REMARK 465 TYR A 2583 REMARK 465 TYR A 2584 REMARK 465 PHE A 2585 REMARK 465 GLU A 2586 REMARK 465 PRO A 2587 REMARK 465 ASN A 2588 REMARK 465 THR A 2589 REMARK 465 ALA A 2590 REMARK 465 MET A 2591 REMARK 465 GLY A 2592 REMARK 465 ALA A 2593 REMARK 465 ASN A 2594 REMARK 465 GLY A 2595 REMARK 465 TYR A 2596 REMARK 465 LYS A 2597 REMARK 465 THR A 2598 REMARK 465 ILE A 2599 REMARK 465 ASP A 2600 REMARK 465 ASN A 2601 REMARK 465 LYS A 2602 REMARK 465 ASN A 2603 REMARK 465 PHE A 2604 REMARK 465 TYR A 2605 REMARK 465 PHE A 2606 REMARK 465 ARG A 2607 REMARK 465 ASN A 2608 REMARK 465 GLY A 2609 REMARK 465 LEU A 2610 REMARK 465 PRO A 2611 REMARK 465 GLN A 2612 REMARK 465 ILE A 2613 REMARK 465 GLY A 2614 REMARK 465 VAL A 2615 REMARK 465 PHE A 2616 REMARK 465 LYS A 2617 REMARK 465 GLY A 2618 REMARK 465 SER A 2619 REMARK 465 ASN A 2620 REMARK 465 GLY A 2621 REMARK 465 PHE A 2622 REMARK 465 GLU A 2623 REMARK 465 TYR A 2624 REMARK 465 PHE A 2625 REMARK 465 ALA A 2626 REMARK 465 PRO A 2627 REMARK 465 ALA A 2628 REMARK 465 ASN A 2629 REMARK 465 THR A 2630 REMARK 465 ASP A 2631 REMARK 465 ALA A 2632 REMARK 465 ASN A 2633 REMARK 465 ASN A 2634 REMARK 465 ILE A 2635 REMARK 465 GLU A 2636 REMARK 465 GLY A 2637 REMARK 465 GLN A 2638 REMARK 465 ALA A 2639 REMARK 465 ILE A 2640 REMARK 465 ARG A 2641 REMARK 465 TYR A 2642 REMARK 465 GLN A 2643 REMARK 465 ASN A 2644 REMARK 465 ARG A 2645 REMARK 465 PHE A 2646 REMARK 465 LEU A 2647 REMARK 465 HIS A 2648 REMARK 465 LEU A 2649 REMARK 465 LEU A 2650 REMARK 465 GLY A 2651 REMARK 465 LYS A 2652 REMARK 465 ILE A 2653 REMARK 465 TYR A 2654 REMARK 465 TYR A 2655 REMARK 465 PHE A 2656 REMARK 465 GLY A 2657 REMARK 465 ASN A 2658 REMARK 465 ASN A 2659 REMARK 465 SER A 2660 REMARK 465 LYS A 2661 REMARK 465 ALA A 2662 REMARK 465 VAL A 2663 REMARK 465 THR A 2664 REMARK 465 GLY A 2665 REMARK 465 TRP A 2666 REMARK 465 GLN A 2667 REMARK 465 THR A 2668 REMARK 465 ILE A 2669 REMARK 465 ASN A 2670 REMARK 465 GLY A 2671 REMARK 465 LYS A 2672 REMARK 465 VAL A 2673 REMARK 465 TYR A 2674 REMARK 465 TYR A 2675 REMARK 465 PHE A 2676 REMARK 465 MET A 2677 REMARK 465 PRO A 2678 REMARK 465 ASP A 2679 REMARK 465 THR A 2680 REMARK 465 ALA A 2681 REMARK 465 MET A 2682 REMARK 465 ALA A 2683 REMARK 465 ALA A 2684 REMARK 465 ALA A 2685 REMARK 465 GLY A 2686 REMARK 465 GLY A 2687 REMARK 465 LEU A 2688 REMARK 465 PHE A 2689 REMARK 465 GLU A 2690 REMARK 465 ILE A 2691 REMARK 465 ASP A 2692 REMARK 465 GLY A 2693 REMARK 465 VAL A 2694 REMARK 465 ILE A 2695 REMARK 465 TYR A 2696 REMARK 465 PHE A 2697 REMARK 465 PHE A 2698 REMARK 465 GLY A 2699 REMARK 465 VAL A 2700 REMARK 465 ASP A 2701 REMARK 465 GLY A 2702 REMARK 465 VAL A 2703 REMARK 465 LYS A 2704 REMARK 465 ALA A 2705 REMARK 465 PRO A 2706 REMARK 465 GLY A 2707 REMARK 465 ILE A 2708 REMARK 465 TYR A 2709 REMARK 465 GLY A 2710 REMARK 465 ALA B 124 REMARK 465 LYS B 125 REMARK 465 THR B 126 REMARK 465 THR B 127 REMARK 465 PRO B 128 REMARK 465 PRO B 129 REMARK 465 SER B 130 REMARK 465 VAL B 131 REMARK 465 TYR B 132 REMARK 465 PRO B 133 REMARK 465 LEU B 134 REMARK 465 ALA B 135 REMARK 465 PRO B 136 REMARK 465 GLY B 137 REMARK 465 SER B 138 REMARK 465 ALA B 139 REMARK 465 ALA B 140 REMARK 465 GLN B 141 REMARK 465 THR B 142 REMARK 465 ASN B 143 REMARK 465 SER B 144 REMARK 465 MET B 145 REMARK 465 VAL B 146 REMARK 465 THR B 147 REMARK 465 LEU B 148 REMARK 465 GLY B 149 REMARK 465 CYS B 150 REMARK 465 LEU B 151 REMARK 465 VAL B 152 REMARK 465 LYS B 153 REMARK 465 GLY B 154 REMARK 465 TYR B 155 REMARK 465 PHE B 156 REMARK 465 PRO B 157 REMARK 465 GLU B 158 REMARK 465 PRO B 159 REMARK 465 VAL B 160 REMARK 465 THR B 161 REMARK 465 VAL B 162 REMARK 465 THR B 163 REMARK 465 TRP B 164 REMARK 465 ASN B 165 REMARK 465 SER B 166 REMARK 465 GLY B 167 REMARK 465 SER B 168 REMARK 465 LEU B 169 REMARK 465 SER B 170 REMARK 465 SER B 171 REMARK 465 GLY B 172 REMARK 465 VAL B 173 REMARK 465 HIS B 174 REMARK 465 THR B 175 REMARK 465 PHE B 176 REMARK 465 PRO B 177 REMARK 465 ALA B 178 REMARK 465 VAL B 179 REMARK 465 LEU B 180 REMARK 465 GLU B 181 REMARK 465 SER B 182 REMARK 465 ASP B 183 REMARK 465 LEU B 184 REMARK 465 TYR B 185 REMARK 465 THR B 186 REMARK 465 LEU B 187 REMARK 465 SER B 188 REMARK 465 SER B 189 REMARK 465 SER B 190 REMARK 465 VAL B 191 REMARK 465 THR B 192 REMARK 465 VAL B 193 REMARK 465 PRO B 194 REMARK 465 SER B 195 REMARK 465 SER B 196 REMARK 465 PRO B 197 REMARK 465 ARG B 198 REMARK 465 PRO B 199 REMARK 465 SER B 200 REMARK 465 GLU B 201 REMARK 465 THR B 202 REMARK 465 VAL B 203 REMARK 465 THR B 204 REMARK 465 CYS B 205 REMARK 465 ASN B 206 REMARK 465 VAL B 207 REMARK 465 ALA B 208 REMARK 465 HIS B 209 REMARK 465 PRO B 210 REMARK 465 ALA B 211 REMARK 465 SER B 212 REMARK 465 SER B 213 REMARK 465 THR B 214 REMARK 465 LYS B 215 REMARK 465 VAL B 216 REMARK 465 ASP B 217 REMARK 465 LYS B 218 REMARK 465 LYS B 219 REMARK 465 ILE B 220 REMARK 465 ALA C 329 REMARK 465 ASP C 330 REMARK 465 ALA C 331 REMARK 465 ALA C 332 REMARK 465 PRO C 333 REMARK 465 THR C 334 REMARK 465 VAL C 335 REMARK 465 SER C 336 REMARK 465 ILE C 337 REMARK 465 PHE C 338 REMARK 465 PRO C 339 REMARK 465 PRO C 340 REMARK 465 SER C 341 REMARK 465 SER C 342 REMARK 465 GLU C 343 REMARK 465 GLN C 344 REMARK 465 LEU C 345 REMARK 465 THR C 346 REMARK 465 SER C 347 REMARK 465 GLY C 348 REMARK 465 GLY C 349 REMARK 465 ALA C 350 REMARK 465 SER C 351 REMARK 465 VAL C 352 REMARK 465 VAL C 353 REMARK 465 CYS C 354 REMARK 465 PHE C 355 REMARK 465 LEU C 356 REMARK 465 ASN C 357 REMARK 465 ASN C 358 REMARK 465 PHE C 359 REMARK 465 TYR C 360 REMARK 465 PRO C 361 REMARK 465 LYS C 362 REMARK 465 ASP C 363 REMARK 465 ILE C 364 REMARK 465 ASN C 365 REMARK 465 VAL C 366 REMARK 465 LYS C 367 REMARK 465 TRP C 368 REMARK 465 LYS C 369 REMARK 465 ILE C 370 REMARK 465 ASP C 371 REMARK 465 GLY C 372 REMARK 465 SER C 373 REMARK 465 GLU C 374 REMARK 465 ARG C 375 REMARK 465 GLN C 376 REMARK 465 ASN C 377 REMARK 465 GLY C 378 REMARK 465 VAL C 379 REMARK 465 LEU C 380 REMARK 465 ASN C 381 REMARK 465 SER C 382 REMARK 465 TRP C 383 REMARK 465 THR C 384 REMARK 465 ASP C 385 REMARK 465 GLN C 386 REMARK 465 ASP C 387 REMARK 465 SER C 388 REMARK 465 LYS C 389 REMARK 465 ASP C 390 REMARK 465 SER C 391 REMARK 465 THR C 392 REMARK 465 TYR C 393 REMARK 465 SER C 394 REMARK 465 MET C 395 REMARK 465 SER C 396 REMARK 465 SER C 397 REMARK 465 THR C 398 REMARK 465 LEU C 399 REMARK 465 THR C 400 REMARK 465 LEU C 401 REMARK 465 THR C 402 REMARK 465 LYS C 403 REMARK 465 ASP C 404 REMARK 465 GLU C 405 REMARK 465 TYR C 406 REMARK 465 GLU C 407 REMARK 465 ARG C 408 REMARK 465 HIS C 409 REMARK 465 ASN C 410 REMARK 465 SER C 411 REMARK 465 TYR C 412 REMARK 465 THR C 413 REMARK 465 CYS C 414 REMARK 465 GLU C 415 REMARK 465 ALA C 416 REMARK 465 THR C 417 REMARK 465 HIS C 418 REMARK 465 LYS C 419 REMARK 465 THR C 420 REMARK 465 SER C 421 REMARK 465 THR C 422 REMARK 465 SER C 423 REMARK 465 PRO C 424 REMARK 465 ILE C 425 REMARK 465 VAL C 426 REMARK 465 LYS C 427 REMARK 465 SER C 428 REMARK 465 PHE C 429 REMARK 465 ASN C 430 REMARK 465 ARG C 431 REMARK 465 ASN C 432 REMARK 465 GLU C 433 REMARK 465 CYS C 434 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 LEU A 507 CA - CB - CG ANGL. DEV. = 16.1 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 164 30.13 -95.47 REMARK 500 ASN A 214 52.18 -92.32 REMARK 500 ASN A 234 56.92 -95.48 REMARK 500 SER A 243 50.59 -92.15 REMARK 500 ASN A 486 61.22 60.71 REMARK 500 ASP A 522 -168.96 -102.57 REMARK 500 SER A 617 51.44 -95.64 REMARK 500 GLU A 632 53.25 -93.35 REMARK 500 SER A 736 52.27 -91.97 REMARK 500 ASP A 982 76.46 -104.56 REMARK 500 PHE A 996 -60.42 -96.07 REMARK 500 SER A 997 -168.74 -103.75 REMARK 500 GLU A1029 -31.89 -131.09 REMARK 500 ILE A1031 61.14 31.79 REMARK 500 THR A1036 22.43 -78.65 REMARK 500 ASN A1042 35.75 -90.41 REMARK 500 ALA A1045 -15.33 69.06 REMARK 500 ASP A1055 72.47 54.11 REMARK 500 ILE A1105 74.89 51.01 REMARK 500 ASP A1143 30.42 -140.77 REMARK 500 ASN A1160 -60.76 -94.78 REMARK 500 ASN A1162 60.68 61.99 REMARK 500 ILE A1199 81.54 54.62 REMARK 500 PHE A1217 50.57 -118.41 REMARK 500 VAL A1239 65.48 31.90 REMARK 500 ASP A1248 -159.20 -159.93 REMARK 500 PHE A1271 -30.89 -130.88 REMARK 500 TYR A1283 67.63 60.89 REMARK 500 ASP A1295 -165.44 -78.52 REMARK 500 ASN A1381 11.16 -140.14 REMARK 500 SER A1478 -5.51 68.72 REMARK 500 ASN A1497 55.69 -96.78 REMARK 500 ASP A1498 -13.20 68.16 REMARK 500 SER A1499 -17.67 -141.82 REMARK 500 LYS A1518 -62.40 -109.86 REMARK 500 ASP A1519 -55.89 -124.33 REMARK 500 ASN A1553 -62.85 -95.19 REMARK 500 SER A1590 68.65 61.36 REMARK 500 ASP A1605 -167.88 -126.38 REMARK 500 ASP A1624 -167.02 -128.09 REMARK 500 ASP A1817 -159.42 -146.25 REMARK 500 TYR A1823 70.93 57.31 REMARK 500 LEU A1829 70.90 58.61 REMARK 500 ASN A1838 -12.83 -140.51 REMARK 500 THR A1910 -165.68 -123.84 REMARK 500 ASN A1972 -21.56 -140.52 REMARK 500 ASP A1980 -1.36 67.33 REMARK 500 THR A2011 33.18 -99.79 REMARK 500 GLN A2081 70.53 49.00 REMARK 500 ASP A2126 48.57 36.68 REMARK 500 REMARK 500 THIS ENTRY HAS 59 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-48707 RELATED DB: EMDB REMARK 900 CLOSTRIDIOIDES DIFFICILE TOXIN A WITH MCDIFA-248-25 FAB DBREF 9MX1 A 1 2710 UNP P16154 TCDA_CLODI 1 2710 DBREF 9MX1 B 1 220 PDB 9MX1 9MX1 1 220 DBREF 9MX1 C 221 434 PDB 9MX1 9MX1 221 434 SEQADV 9MX1 ALA A 285 UNP P16154 ASP 285 CONFLICT SEQADV 9MX1 ALA A 287 UNP P16154 ASP 287 CONFLICT SEQADV 9MX1 ALA A 700 UNP P16154 CYS 700 CONFLICT SEQADV 9MX1 ILE A 1444 UNP P16154 THR 1444 CONFLICT SEQADV 9MX1 ILE A 1873 UNP P16154 THR 1873 CONFLICT SEQADV 9MX1 ASP A 1939 UNP P16154 ASN 1939 CONFLICT SEQADV 9MX1 HIS A 2427 UNP P16154 ASP 2427 CONFLICT SEQADV 9MX1 ASN A 2428 UNP P16154 ALA 2428 CONFLICT SEQRES 1 A 2710 MET SER LEU ILE SER LYS GLU GLU LEU ILE LYS LEU ALA SEQRES 2 A 2710 TYR SER ILE ARG PRO ARG GLU ASN GLU TYR LYS THR ILE SEQRES 3 A 2710 LEU THR ASN LEU ASP GLU TYR ASN LYS LEU THR THR ASN SEQRES 4 A 2710 ASN ASN GLU ASN LYS TYR LEU GLN LEU LYS LYS LEU ASN SEQRES 5 A 2710 GLU SER ILE ASP VAL PHE MET ASN LYS TYR LYS THR SER SEQRES 6 A 2710 SER ARG ASN ARG ALA LEU SER ASN LEU LYS LYS ASP ILE SEQRES 7 A 2710 LEU LYS GLU VAL ILE LEU ILE LYS ASN SER ASN THR SER SEQRES 8 A 2710 PRO VAL GLU LYS ASN LEU HIS PHE VAL TRP ILE GLY GLY SEQRES 9 A 2710 GLU VAL SER ASP ILE ALA LEU GLU TYR ILE LYS GLN TRP SEQRES 10 A 2710 ALA ASP ILE ASN ALA GLU TYR ASN ILE LYS LEU TRP TYR SEQRES 11 A 2710 ASP SER GLU ALA PHE LEU VAL ASN THR LEU LYS LYS ALA SEQRES 12 A 2710 ILE VAL GLU SER SER THR THR GLU ALA LEU GLN LEU LEU SEQRES 13 A 2710 GLU GLU GLU ILE GLN ASN PRO GLN PHE ASP ASN MET LYS SEQRES 14 A 2710 PHE TYR LYS LYS ARG MET GLU PHE ILE TYR ASP ARG GLN SEQRES 15 A 2710 LYS ARG PHE ILE ASN TYR TYR LYS SER GLN ILE ASN LYS SEQRES 16 A 2710 PRO THR VAL PRO THR ILE ASP ASP ILE ILE LYS SER HIS SEQRES 17 A 2710 LEU VAL SER GLU TYR ASN ARG ASP GLU THR VAL LEU GLU SEQRES 18 A 2710 SER TYR ARG THR ASN SER LEU ARG LYS ILE ASN SER ASN SEQRES 19 A 2710 HIS GLY ILE ASP ILE ARG ALA ASN SER LEU PHE THR GLU SEQRES 20 A 2710 GLN GLU LEU LEU ASN ILE TYR SER GLN GLU LEU LEU ASN SEQRES 21 A 2710 ARG GLY ASN LEU ALA ALA ALA SER ASP ILE VAL ARG LEU SEQRES 22 A 2710 LEU ALA LEU LYS ASN PHE GLY GLY VAL TYR LEU ALA VAL SEQRES 23 A 2710 ALA MET LEU PRO GLY ILE HIS SER ASP LEU PHE LYS THR SEQRES 24 A 2710 ILE SER ARG PRO SER SER ILE GLY LEU ASP ARG TRP GLU SEQRES 25 A 2710 MET ILE LYS LEU GLU ALA ILE MET LYS TYR LYS LYS TYR SEQRES 26 A 2710 ILE ASN ASN TYR THR SER GLU ASN PHE ASP LYS LEU ASP SEQRES 27 A 2710 GLN GLN LEU LYS ASP ASN PHE LYS LEU ILE ILE GLU SER SEQRES 28 A 2710 LYS SER GLU LYS SER GLU ILE PHE SER LYS LEU GLU ASN SEQRES 29 A 2710 LEU ASN VAL SER ASP LEU GLU ILE LYS ILE ALA PHE ALA SEQRES 30 A 2710 LEU GLY SER VAL ILE ASN GLN ALA LEU ILE SER LYS GLN SEQRES 31 A 2710 GLY SER TYR LEU THR ASN LEU VAL ILE GLU GLN VAL LYS SEQRES 32 A 2710 ASN ARG TYR GLN PHE LEU ASN GLN HIS LEU ASN PRO ALA SEQRES 33 A 2710 ILE GLU SER ASP ASN ASN PHE THR ASP THR THR LYS ILE SEQRES 34 A 2710 PHE HIS ASP SER LEU PHE ASN SER ALA THR ALA GLU ASN SEQRES 35 A 2710 SER MET PHE LEU THR LYS ILE ALA PRO TYR LEU GLN VAL SEQRES 36 A 2710 GLY PHE MET PRO GLU ALA ARG SER THR ILE SER LEU SER SEQRES 37 A 2710 GLY PRO GLY ALA TYR ALA SER ALA TYR TYR ASP PHE ILE SEQRES 38 A 2710 ASN LEU GLN GLU ASN THR ILE GLU LYS THR LEU LYS ALA SEQRES 39 A 2710 SER ASP LEU ILE GLU PHE LYS PHE PRO GLU ASN ASN LEU SEQRES 40 A 2710 SER GLN LEU THR GLU GLN GLU ILE ASN SER LEU TRP SER SEQRES 41 A 2710 PHE ASP GLN ALA SER ALA LYS TYR GLN PHE GLU LYS TYR SEQRES 42 A 2710 VAL ARG ASP TYR THR GLY GLY SER LEU SER GLU ASP ASN SEQRES 43 A 2710 GLY VAL ASP PHE ASN LYS ASN THR ALA LEU ASP LYS ASN SEQRES 44 A 2710 TYR LEU LEU ASN ASN LYS ILE PRO SER ASN ASN VAL GLU SEQRES 45 A 2710 GLU ALA GLY SER LYS ASN TYR VAL HIS TYR ILE ILE GLN SEQRES 46 A 2710 LEU GLN GLY ASP ASP ILE SER TYR GLU ALA THR CYS ASN SEQRES 47 A 2710 LEU PHE SER LYS ASN PRO LYS ASN SER ILE ILE ILE GLN SEQRES 48 A 2710 ARG ASN MET ASN GLU SER ALA LYS SER TYR PHE LEU SER SEQRES 49 A 2710 ASP ASP GLY GLU SER ILE LEU GLU LEU ASN LYS TYR ARG SEQRES 50 A 2710 ILE PRO GLU ARG LEU LYS ASN LYS GLU LYS VAL LYS VAL SEQRES 51 A 2710 THR PHE ILE GLY HIS GLY LYS ASP GLU PHE ASN THR SER SEQRES 52 A 2710 GLU PHE ALA ARG LEU SER VAL ASP SER LEU SER ASN GLU SEQRES 53 A 2710 ILE SER SER PHE LEU ASP THR ILE LYS LEU ASP ILE SER SEQRES 54 A 2710 PRO LYS ASN VAL GLU VAL ASN LEU LEU GLY ALA ASN MET SEQRES 55 A 2710 PHE SER TYR ASP PHE ASN VAL GLU GLU THR TYR PRO GLY SEQRES 56 A 2710 LYS LEU LEU LEU SER ILE MET ASP LYS ILE THR SER THR SEQRES 57 A 2710 LEU PRO ASP VAL ASN LYS ASN SER ILE THR ILE GLY ALA SEQRES 58 A 2710 ASN GLN TYR GLU VAL ARG ILE ASN SER GLU GLY ARG LYS SEQRES 59 A 2710 GLU LEU LEU ALA HIS SER GLY LYS TRP ILE ASN LYS GLU SEQRES 60 A 2710 GLU ALA ILE MET SER ASP LEU SER SER LYS GLU TYR ILE SEQRES 61 A 2710 PHE PHE ASP SER ILE ASP ASN LYS LEU LYS ALA LYS SER SEQRES 62 A 2710 LYS ASN ILE PRO GLY LEU ALA SER ILE SER GLU ASP ILE SEQRES 63 A 2710 LYS THR LEU LEU LEU ASP ALA SER VAL SER PRO ASP THR SEQRES 64 A 2710 LYS PHE ILE LEU ASN ASN LEU LYS LEU ASN ILE GLU SER SEQRES 65 A 2710 SER ILE GLY ASP TYR ILE TYR TYR GLU LYS LEU GLU PRO SEQRES 66 A 2710 VAL LYS ASN ILE ILE HIS ASN SER ILE ASP ASP LEU ILE SEQRES 67 A 2710 ASP GLU PHE ASN LEU LEU GLU ASN VAL SER ASP GLU LEU SEQRES 68 A 2710 TYR GLU LEU LYS LYS LEU ASN ASN LEU ASP GLU LYS TYR SEQRES 69 A 2710 LEU ILE SER PHE GLU ASP ILE SER LYS ASN ASN SER THR SEQRES 70 A 2710 TYR SER VAL ARG PHE ILE ASN LYS SER ASN GLY GLU SER SEQRES 71 A 2710 VAL TYR VAL GLU THR GLU LYS GLU ILE PHE SER LYS TYR SEQRES 72 A 2710 SER GLU HIS ILE THR LYS GLU ILE SER THR ILE LYS ASN SEQRES 73 A 2710 SER ILE ILE THR ASP VAL ASN GLY ASN LEU LEU ASP ASN SEQRES 74 A 2710 ILE GLN LEU ASP HIS THR SER GLN VAL ASN THR LEU ASN SEQRES 75 A 2710 ALA ALA PHE PHE ILE GLN SER LEU ILE ASP TYR SER SER SEQRES 76 A 2710 ASN LYS ASP VAL LEU ASN ASP LEU SER THR SER VAL LYS SEQRES 77 A 2710 VAL GLN LEU TYR ALA GLN LEU PHE SER THR GLY LEU ASN SEQRES 78 A 2710 THR ILE TYR ASP SER ILE GLN LEU VAL ASN LEU ILE SER SEQRES 79 A 2710 ASN ALA VAL ASN ASP THR ILE ASN VAL LEU PRO THR ILE SEQRES 80 A 2710 THR GLU GLY ILE PRO ILE VAL SER THR ILE LEU ASP GLY SEQRES 81 A 2710 ILE ASN LEU GLY ALA ALA ILE LYS GLU LEU LEU ASP GLU SEQRES 82 A 2710 HIS ASP PRO LEU LEU LYS LYS GLU LEU GLU ALA LYS VAL SEQRES 83 A 2710 GLY VAL LEU ALA ILE ASN MET SER LEU SER ILE ALA ALA SEQRES 84 A 2710 THR VAL ALA SER ILE VAL GLY ILE GLY ALA GLU VAL THR SEQRES 85 A 2710 ILE PHE LEU LEU PRO ILE ALA GLY ILE SER ALA GLY ILE SEQRES 86 A 2710 PRO SER LEU VAL ASN ASN GLU LEU ILE LEU HIS ASP LYS SEQRES 87 A 2710 ALA THR SER VAL VAL ASN TYR PHE ASN HIS LEU SER GLU SEQRES 88 A 2710 SER LYS LYS TYR GLY PRO LEU LYS THR GLU ASP ASP LYS SEQRES 89 A 2710 ILE LEU VAL PRO ILE ASP ASP LEU VAL ILE SER GLU ILE SEQRES 90 A 2710 ASP PHE ASN ASN ASN SER ILE LYS LEU GLY THR CYS ASN SEQRES 91 A 2710 ILE LEU ALA MET GLU GLY GLY SER GLY HIS THR VAL THR SEQRES 92 A 2710 GLY ASN ILE ASP HIS PHE PHE SER SER PRO SER ILE SER SEQRES 93 A 2710 SER HIS ILE PRO SER LEU SER ILE TYR SER ALA ILE GLY SEQRES 94 A 2710 ILE GLU THR GLU ASN LEU ASP PHE SER LYS LYS ILE MET SEQRES 95 A 2710 MET LEU PRO ASN ALA PRO SER ARG VAL PHE TRP TRP GLU SEQRES 96 A 2710 THR GLY ALA VAL PRO GLY LEU ARG SER LEU GLU ASN ASP SEQRES 97 A 2710 GLY THR ARG LEU LEU ASP SER ILE ARG ASP LEU TYR PRO SEQRES 98 A 2710 GLY LYS PHE TYR TRP ARG PHE TYR ALA PHE PHE ASP TYR SEQRES 99 A 2710 ALA ILE THR THR LEU LYS PRO VAL TYR GLU ASP THR ASN SEQRES 100 A 2710 ILE LYS ILE LYS LEU ASP LYS ASP THR ARG ASN PHE ILE SEQRES 101 A 2710 MET PRO THR ILE THR THR ASN GLU ILE ARG ASN LYS LEU SEQRES 102 A 2710 SER TYR SER PHE ASP GLY ALA GLY GLY THR TYR SER LEU SEQRES 103 A 2710 LEU LEU SER SER TYR PRO ILE SER THR ASN ILE ASN LEU SEQRES 104 A 2710 SER LYS ASP ASP LEU TRP ILE PHE ASN ILE ASP ASN GLU SEQRES 105 A 2710 VAL ARG GLU ILE SER ILE GLU ASN GLY THR ILE LYS LYS SEQRES 106 A 2710 GLY LYS LEU ILE LYS ASP VAL LEU SER LYS ILE ASP ILE SEQRES 107 A 2710 ASN LYS ASN LYS LEU ILE ILE GLY ASN GLN THR ILE ASP SEQRES 108 A 2710 PHE SER GLY ASP ILE ASP ASN LYS ASP ARG TYR ILE PHE SEQRES 109 A 2710 LEU THR CYS GLU LEU ASP ASP LYS ILE SER LEU ILE ILE SEQRES 110 A 2710 GLU ILE ASN LEU VAL ALA LYS SER TYR SER LEU LEU LEU SEQRES 111 A 2710 SER GLY ASP LYS ASN TYR LEU ILE SER ASN LEU SER ASN SEQRES 112 A 2710 ILE ILE GLU LYS ILE ASN THR LEU GLY LEU ASP SER LYS SEQRES 113 A 2710 ASN ILE ALA TYR ASN TYR THR ASP GLU SER ASN ASN LYS SEQRES 114 A 2710 TYR PHE GLY ALA ILE SER LYS THR SER GLN LYS SER ILE SEQRES 115 A 2710 ILE HIS TYR LYS LYS ASP SER LYS ASN ILE LEU GLU PHE SEQRES 116 A 2710 TYR ASN ASP SER THR LEU GLU PHE ASN SER LYS ASP PHE SEQRES 117 A 2710 ILE ALA GLU ASP ILE ASN VAL PHE MET LYS ASP ASP ILE SEQRES 118 A 2710 ASN THR ILE THR GLY LYS TYR TYR VAL ASP ASN ASN THR SEQRES 119 A 2710 ASP LYS SER ILE ASP PHE SER ILE SER LEU VAL SER LYS SEQRES 120 A 2710 ASN GLN VAL LYS VAL ASN GLY LEU TYR LEU ASN GLU SER SEQRES 121 A 2710 VAL TYR SER SER TYR LEU ASP PHE VAL LYS ASN SER ASP SEQRES 122 A 2710 GLY HIS HIS ASN THR SER ASN PHE MET ASN LEU PHE LEU SEQRES 123 A 2710 ASP ASN ILE SER PHE TRP LYS LEU PHE GLY PHE GLU ASN SEQRES 124 A 2710 ILE ASN PHE VAL ILE ASP LYS TYR PHE THR LEU VAL GLY SEQRES 125 A 2710 LYS THR ASN LEU GLY TYR VAL GLU PHE ILE CYS ASP ASN SEQRES 126 A 2710 ASN LYS ASN ILE ASP ILE TYR PHE GLY GLU TRP LYS THR SEQRES 127 A 2710 SER SER SER LYS SER THR ILE PHE SER GLY ASN GLY ARG SEQRES 128 A 2710 ASN VAL VAL VAL GLU PRO ILE TYR ASN PRO ASP THR GLY SEQRES 129 A 2710 GLU ASP ILE SER THR SER LEU ASP PHE SER TYR GLU PRO SEQRES 130 A 2710 LEU TYR GLY ILE ASP ARG TYR ILE ASN LYS VAL LEU ILE SEQRES 131 A 2710 ALA PRO ASP LEU TYR THR SER LEU ILE ASN ILE ASN THR SEQRES 132 A 2710 ASN TYR TYR SER ASN GLU TYR TYR PRO GLU ILE ILE VAL SEQRES 133 A 2710 LEU ASN PRO ASN THR PHE HIS LYS LYS VAL ASN ILE ASN SEQRES 134 A 2710 LEU ASP SER SER SER PHE GLU TYR LYS TRP SER THR GLU SEQRES 135 A 2710 GLY SER ASP PHE ILE LEU VAL ARG TYR LEU GLU GLU SER SEQRES 136 A 2710 ASN LYS LYS ILE LEU GLN LYS ILE ARG ILE LYS GLY ILE SEQRES 137 A 2710 LEU SER ASN THR GLN SER PHE ASN LYS MET SER ILE ASP SEQRES 138 A 2710 PHE LYS ASP ILE LYS LYS LEU SER LEU GLY TYR ILE MET SEQRES 139 A 2710 SER ASN PHE LYS SER PHE ASN SER GLU ASN GLU LEU ASP SEQRES 140 A 2710 ARG ASP HIS LEU GLY PHE LYS ILE ILE ASP ASN LYS THR SEQRES 141 A 2710 TYR TYR TYR ASP GLU ASP SER LYS LEU VAL LYS GLY LEU SEQRES 142 A 2710 ILE ASN ILE ASN ASN SER LEU PHE TYR PHE ASP PRO ILE SEQRES 143 A 2710 GLU PHE ASN LEU VAL THR GLY TRP GLN THR ILE ASN GLY SEQRES 144 A 2710 LYS LYS TYR TYR PHE ASP ILE ASN THR GLY ALA ALA LEU SEQRES 145 A 2710 ILE SER TYR LYS ILE ILE ASN GLY LYS HIS PHE TYR PHE SEQRES 146 A 2710 ASN ASN ASP GLY VAL MET GLN LEU GLY VAL PHE LYS GLY SEQRES 147 A 2710 PRO ASP GLY PHE GLU TYR PHE ALA PRO ALA ASN THR GLN SEQRES 148 A 2710 ASN ASN ASN ILE GLU GLY GLN ALA ILE VAL TYR GLN SER SEQRES 149 A 2710 LYS PHE LEU THR LEU ASN GLY LYS LYS TYR TYR PHE ASP SEQRES 150 A 2710 ASN ASP SER LYS ALA VAL THR GLY TRP ARG ILE ILE ASN SEQRES 151 A 2710 ASN GLU LYS TYR TYR PHE ASN PRO ASN ASN ALA ILE ALA SEQRES 152 A 2710 ALA VAL GLY LEU GLN VAL ILE ASP ASN ASN LYS TYR TYR SEQRES 153 A 2710 PHE ASN PRO ASP THR ALA ILE ILE SER LYS GLY TRP GLN SEQRES 154 A 2710 THR VAL ASN GLY SER ARG TYR TYR PHE ASP THR ASP THR SEQRES 155 A 2710 ALA ILE ALA PHE ASN GLY TYR LYS THR ILE ASP GLY LYS SEQRES 156 A 2710 HIS PHE TYR PHE ASP SER ASP CYS VAL VAL LYS ILE GLY SEQRES 157 A 2710 VAL PHE SER THR SER ASN GLY PHE GLU TYR PHE ALA PRO SEQRES 158 A 2710 ALA ASN THR TYR ASN ASN ASN ILE GLU GLY GLN ALA ILE SEQRES 159 A 2710 VAL TYR GLN SER LYS PHE LEU THR LEU ASN GLY LYS LYS SEQRES 160 A 2710 TYR TYR PHE ASP ASN ASN SER LYS ALA VAL THR GLY LEU SEQRES 161 A 2710 GLN THR ILE ASP SER LYS LYS TYR TYR PHE ASN THR ASN SEQRES 162 A 2710 THR ALA GLU ALA ALA THR GLY TRP GLN THR ILE ASP GLY SEQRES 163 A 2710 LYS LYS TYR TYR PHE ASN THR ASN THR ALA GLU ALA ALA SEQRES 164 A 2710 THR GLY TRP GLN THR ILE ASP GLY LYS LYS TYR TYR PHE SEQRES 165 A 2710 ASN THR ASN THR ALA ILE ALA SER THR GLY TYR THR ILE SEQRES 166 A 2710 ILE ASN GLY LYS HIS PHE TYR PHE ASN THR ASP GLY ILE SEQRES 167 A 2710 MET GLN ILE GLY VAL PHE LYS GLY PRO ASN GLY PHE GLU SEQRES 168 A 2710 TYR PHE ALA PRO ALA ASN THR ASP ALA ASN ASN ILE GLU SEQRES 169 A 2710 GLY GLN ALA ILE LEU TYR GLN ASN GLU PHE LEU THR LEU SEQRES 170 A 2710 ASN GLY LYS LYS TYR TYR PHE GLY SER ASP SER LYS ALA SEQRES 171 A 2710 VAL THR GLY TRP ARG ILE ILE ASN ASN LYS LYS TYR TYR SEQRES 172 A 2710 PHE ASN PRO ASN ASN ALA ILE ALA ALA ILE HIS LEU CYS SEQRES 173 A 2710 THR ILE ASN ASN ASP LYS TYR TYR PHE SER TYR ASP GLY SEQRES 174 A 2710 ILE LEU GLN ASN GLY TYR ILE THR ILE GLU ARG ASN ASN SEQRES 175 A 2710 PHE TYR PHE ASP ALA ASN ASN GLU SER LYS MET VAL THR SEQRES 176 A 2710 GLY VAL PHE LYS GLY PRO ASN GLY PHE GLU TYR PHE ALA SEQRES 177 A 2710 PRO ALA ASN THR HIS ASN ASN ASN ILE GLU GLY GLN ALA SEQRES 178 A 2710 ILE VAL TYR GLN ASN LYS PHE LEU THR LEU ASN GLY LYS SEQRES 179 A 2710 LYS TYR TYR PHE ASP ASN ASP SER LYS ALA VAL THR GLY SEQRES 180 A 2710 TRP GLN THR ILE ASP GLY LYS LYS TYR TYR PHE ASN LEU SEQRES 181 A 2710 ASN THR ALA GLU ALA ALA THR GLY TRP GLN THR ILE ASP SEQRES 182 A 2710 GLY LYS LYS TYR TYR PHE ASN LEU ASN THR ALA GLU ALA SEQRES 183 A 2710 ALA THR GLY TRP GLN THR ILE ASP GLY LYS LYS TYR TYR SEQRES 184 A 2710 PHE ASN THR ASN THR PHE ILE ALA SER THR GLY TYR THR SEQRES 185 A 2710 SER ILE ASN GLY LYS HIS PHE TYR PHE ASN THR ASP GLY SEQRES 186 A 2710 ILE MET GLN ILE GLY VAL PHE LYS GLY PRO ASN GLY PHE SEQRES 187 A 2710 GLU TYR PHE ALA PRO ALA ASN THR HIS ASN ASN ASN ILE SEQRES 188 A 2710 GLU GLY GLN ALA ILE LEU TYR GLN ASN LYS PHE LEU THR SEQRES 189 A 2710 LEU ASN GLY LYS LYS TYR TYR PHE GLY SER ASP SER LYS SEQRES 190 A 2710 ALA VAL THR GLY LEU ARG THR ILE ASP GLY LYS LYS TYR SEQRES 191 A 2710 TYR PHE ASN THR ASN THR ALA VAL ALA VAL THR GLY TRP SEQRES 192 A 2710 GLN THR ILE ASN GLY LYS LYS TYR TYR PHE ASN THR ASN SEQRES 193 A 2710 THR SER ILE ALA SER THR GLY TYR THR ILE ILE SER GLY SEQRES 194 A 2710 LYS HIS PHE TYR PHE ASN THR ASP GLY ILE MET GLN ILE SEQRES 195 A 2710 GLY VAL PHE LYS GLY PRO ASP GLY PHE GLU TYR PHE ALA SEQRES 196 A 2710 PRO ALA ASN THR ASP ALA ASN ASN ILE GLU GLY GLN ALA SEQRES 197 A 2710 ILE ARG TYR GLN ASN ARG PHE LEU TYR LEU HIS ASP ASN SEQRES 198 A 2710 ILE TYR TYR PHE GLY ASN ASN SER LYS ALA ALA THR GLY SEQRES 199 A 2710 TRP VAL THR ILE ASP GLY ASN ARG TYR TYR PHE GLU PRO SEQRES 200 A 2710 ASN THR ALA MET GLY ALA ASN GLY TYR LYS THR ILE ASP SEQRES 201 A 2710 ASN LYS ASN PHE TYR PHE ARG ASN GLY LEU PRO GLN ILE SEQRES 202 A 2710 GLY VAL PHE LYS GLY SER ASN GLY PHE GLU TYR PHE ALA SEQRES 203 A 2710 PRO ALA ASN THR ASP ALA ASN ASN ILE GLU GLY GLN ALA SEQRES 204 A 2710 ILE ARG TYR GLN ASN ARG PHE LEU HIS LEU LEU GLY LYS SEQRES 205 A 2710 ILE TYR TYR PHE GLY ASN ASN SER LYS ALA VAL THR GLY SEQRES 206 A 2710 TRP GLN THR ILE ASN GLY LYS VAL TYR TYR PHE MET PRO SEQRES 207 A 2710 ASP THR ALA MET ALA ALA ALA GLY GLY LEU PHE GLU ILE SEQRES 208 A 2710 ASP GLY VAL ILE TYR PHE PHE GLY VAL ASP GLY VAL LYS SEQRES 209 A 2710 ALA PRO GLY ILE TYR GLY SEQRES 1 B 220 GLU VAL LYS LEU VAL GLU SER GLY GLY GLY LEU VAL LYS SEQRES 2 B 220 PRO GLY GLY SER LEU LYS LEU SER CYS ALA ALA SER GLY SEQRES 3 B 220 PHE THR PHE SER ASN TYR ALA MET SER TRP VAL ARG GLN SEQRES 4 B 220 THR PRO GLU LYS ARG LEU GLU TRP VAL ALA ALA ILE ASN SEQRES 5 B 220 GLY ASN GLY ALA LYS ILE TYR TYR PRO ASP THR VAL LYS SEQRES 6 B 220 ASP ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN THR SEQRES 7 B 220 LEU TYR LEU GLN MET SER SER LEU ARG SER GLU ASP THR SEQRES 8 B 220 ALA LEU TYR SER CYS ALA ARG GLN TYR GLY PHE TYR ALA SEQRES 9 B 220 GLY SER PRO TYR TYR PHE ASP TYR TRP GLY LEU GLY THR SEQRES 10 B 220 THR LEU THR VAL SER SER ALA LYS THR THR PRO PRO SER SEQRES 11 B 220 VAL TYR PRO LEU ALA PRO GLY SER ALA ALA GLN THR ASN SEQRES 12 B 220 SER MET VAL THR LEU GLY CYS LEU VAL LYS GLY TYR PHE SEQRES 13 B 220 PRO GLU PRO VAL THR VAL THR TRP ASN SER GLY SER LEU SEQRES 14 B 220 SER SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLU SER SEQRES 15 B 220 ASP LEU TYR THR LEU SER SER SER VAL THR VAL PRO SER SEQRES 16 B 220 SER PRO ARG PRO SER GLU THR VAL THR CYS ASN VAL ALA SEQRES 17 B 220 HIS PRO ALA SER SER THR LYS VAL ASP LYS LYS ILE SEQRES 1 C 214 ASP ILE VAL MET THR GLN SER HIS LYS PHE MET SER THR SEQRES 2 C 214 SER ILE GLY ASP ARG VAL SER ILE THR CYS LYS ALA SER SEQRES 3 C 214 GLN ASP VAL GLY THR ALA VAL ALA TRP TYR GLN GLN LYS SEQRES 4 C 214 PRO GLY GLN SER PRO LYS LEU LEU ILE TYR TRP ALA SER SEQRES 5 C 214 THR ARG HIS THR GLY VAL PRO ASP ARG PHE THR GLY SER SEQRES 6 C 214 GLY SER GLY THR TYR PHE THR LEU SER ILE SER ASN VAL SEQRES 7 C 214 GLN SER GLU ASP LEU ALA ASP TYR PHE CYS GLN GLN TYR SEQRES 8 C 214 SER SER TYR PRO LEU THR PHE GLY ALA GLY THR LYS LEU SEQRES 9 C 214 GLU LEU LYS ARG ALA ASP ALA ALA PRO THR VAL SER ILE SEQRES 10 C 214 PHE PRO PRO SER SER GLU GLN LEU THR SER GLY GLY ALA SEQRES 11 C 214 SER VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP SEQRES 12 C 214 ILE ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN SEQRES 13 C 214 ASN GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS SEQRES 14 C 214 ASP SER THR TYR SER MET SER SER THR LEU THR LEU THR SEQRES 15 C 214 LYS ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU SEQRES 16 C 214 ALA THR HIS LYS THR SER THR SER PRO ILE VAL LYS SER SEQRES 17 C 214 PHE ASN ARG ASN GLU CYS HELIX 1 AA1 GLU A 20 LEU A 36 1 17 HELIX 2 AA2 ASN A 41 TYR A 62 1 22 HELIX 3 AA3 ARG A 67 ASN A 87 1 21 HELIX 4 AA4 SER A 107 ASN A 121 1 15 HELIX 5 AA5 LEU A 136 LEU A 156 1 21 HELIX 6 AA6 LEU A 156 GLN A 161 1 6 HELIX 7 AA7 ASP A 166 SER A 191 1 26 HELIX 8 AA8 THR A 200 TYR A 213 1 14 HELIX 9 AA9 ASP A 216 ASN A 234 1 19 HELIX 10 AB1 GLU A 247 LEU A 259 1 13 HELIX 11 AB2 ASN A 263 PHE A 279 1 17 HELIX 12 AB3 GLY A 307 LYS A 323 1 17 HELIX 13 AB4 ASP A 338 SER A 351 1 14 HELIX 14 AB5 SER A 392 SER A 419 1 28 HELIX 15 AB6 ASN A 422 ASN A 436 1 15 HELIX 16 AB7 ASN A 442 ILE A 449 1 8 HELIX 17 AB8 SER A 463 SER A 468 1 6 HELIX 18 AB9 GLY A 469 ASN A 482 1 14 HELIX 19 AC1 LYS A 493 PHE A 500 1 8 HELIX 20 AC2 PRO A 503 SER A 508 1 6 HELIX 21 AC3 THR A 511 TRP A 519 1 9 HELIX 22 AC4 ASP A 522 THR A 538 1 17 HELIX 23 AC5 ASP A 557 ASN A 564 1 8 HELIX 24 AC6 ASP A 589 ASN A 603 1 15 HELIX 25 AC7 PRO A 639 LYS A 643 5 5 HELIX 26 AC8 SER A 669 LYS A 685 1 17 HELIX 27 AC9 THR A 712 THR A 728 1 17 HELIX 28 AD1 LYS A 766 LYS A 777 1 12 HELIX 29 AD2 ASN A 795 ASP A 812 1 18 HELIX 30 AD3 SER A 816 TYR A 840 1 25 HELIX 31 AD4 ASN A 848 ASN A 878 1 31 HELIX 32 AD5 SER A 921 ASN A 936 1 16 HELIX 33 AD6 HIS A 954 TYR A 973 1 20 HELIX 34 AD7 ASP A 982 SER A 997 1 16 HELIX 35 AD8 ASP A 1005 ASP A 1019 1 15 HELIX 36 AD9 ILE A 1037 ILE A 1041 5 5 HELIX 37 AE1 ILE A 1047 ASP A 1055 1 9 HELIX 38 AE2 PRO A 1056 LYS A 1065 1 10 HELIX 39 AE3 SER A 1074 PHE A 1094 1 21 HELIX 40 AE4 LYS A 1118 SER A 1130 1 13 HELIX 41 AE5 SER A 1130 TYR A 1135 1 6 HELIX 42 AE6 ILE A 1157 ASN A 1162 1 6 HELIX 43 AE7 THR A 1250 TYR A 1260 1 11 HELIX 44 AE8 THR A 1306 ASN A 1311 1 6 HELIX 45 AE9 ASP A 1433 ASN A 1440 1 8 HELIX 46 AF1 ASN A 1440 GLY A 1452 1 13 HELIX 47 AF2 ASP A 1531 ASN A 1533 5 3 HELIX 48 AF3 ASN A 1558 SER A 1572 1 15 HELIX 49 AF4 SER A 1579 SER A 1590 1 12 HELIX 50 AF5 GLU A 1676 TYR A 1679 5 4 HELIX 51 AF6 ASN A 1771 ASN A 1776 1 6 HELIX 52 AF7 SER A 1789 PHE A 1797 1 9 HELIX 53 AF8 ASN A 1801 GLU A 1805 5 5 HELIX 54 AF9 ASP A 1824 LYS A 1828 5 5 HELIX 55 AG1 THR A 2011 LYS A 2015 5 5 SHEET 1 AA1 2 SER A 91 PRO A 92 0 SHEET 2 AA1 2 ASN A 366 VAL A 367 -1 O VAL A 367 N SER A 91 SHEET 1 AA2 6 GLY A 236 ASP A 238 0 SHEET 2 AA2 6 ASN A 125 TYR A 130 1 N LEU A 128 O ILE A 237 SHEET 3 AA2 6 ASN A 96 VAL A 100 1 N PHE A 99 O TRP A 129 SHEET 4 AA2 6 GLY A 281 TYR A 283 1 O VAL A 282 N ASN A 96 SHEET 5 AA2 6 SER A 380 SER A 388 -1 O LEU A 386 N TYR A 283 SHEET 6 AA2 6 LYS A 373 ALA A 377 -1 N ALA A 377 O SER A 380 SHEET 1 AA3 4 ILE A 608 GLN A 611 0 SHEET 2 AA3 4 TYR A 579 GLN A 585 1 N GLN A 585 O ILE A 610 SHEET 3 AA3 4 LYS A 647 GLY A 654 1 O THR A 651 N ILE A 584 SHEET 4 AA3 4 ASN A 692 GLY A 699 1 O ASN A 696 N VAL A 650 SHEET 1 AA4 2 SER A 620 LEU A 623 0 SHEET 2 AA4 2 ILE A 630 LEU A 633 -1 O LEU A 633 N SER A 620 SHEET 1 AA5 3 ILE A 739 GLY A 740 0 SHEET 2 AA5 3 TYR A 779 PHE A 782 -1 O ILE A 780 N ILE A 739 SHEET 3 AA5 3 LEU A 789 ALA A 791 -1 O LYS A 790 N PHE A 781 SHEET 1 AA6 3 VAL A 746 ILE A 748 0 SHEET 2 AA6 3 LYS A 754 LEU A 757 -1 O GLU A 755 N ARG A 747 SHEET 3 AA6 3 TRP A 763 ILE A 764 -1 O ILE A 764 N LEU A 756 SHEET 1 AA7 3 TYR A 884 ILE A 886 0 SHEET 2 AA7 3 TYR A 898 ASN A 904 -1 O ILE A 903 N LEU A 885 SHEET 3 AA7 3 SER A 910 THR A 915 -1 O THR A 915 N TYR A 898 SHEET 1 AA8 2 ILE A 938 VAL A 942 0 SHEET 2 AA8 2 ASN A 945 ASP A 948 -1 O ASN A 945 N VAL A 942 SHEET 1 AA9 6 LEU A1069 ALA A1070 0 SHEET 2 AA9 6 ASN A1514 MET A1517 -1 O MET A1517 N LEU A1069 SHEET 3 AA9 6 ASN A1522 TYR A1529 -1 O THR A1523 N PHE A1516 SHEET 4 AA9 6 SER A1537 LEU A1544 -1 O ILE A1538 N TYR A1528 SHEET 5 AA9 6 GLN A1549 LEU A1557 -1 O ASN A1553 N SER A1541 SHEET 6 AA9 6 ASN A1601 VAL A1603 1 O VAL A1603 N VAL A1552 SHEET 1 AB1 8 LEU A1069 ALA A1070 0 SHEET 2 AB1 8 ASN A1514 MET A1517 -1 O MET A1517 N LEU A1069 SHEET 3 AB1 8 ASN A1522 TYR A1529 -1 O THR A1523 N PHE A1516 SHEET 4 AB1 8 SER A1537 LEU A1544 -1 O ILE A1538 N TYR A1528 SHEET 5 AB1 8 GLN A1549 LEU A1557 -1 O ASN A1553 N SER A1541 SHEET 6 AB1 8 THR A1609 VAL A1611 1 O VAL A1611 N LEU A1555 SHEET 7 AB1 8 GLY A1617 CYS A1623 -1 O PHE A1621 N LEU A1610 SHEET 8 AB1 8 ILE A1629 TRP A1636 -1 O PHE A1633 N GLU A1620 SHEET 1 AB2 2 LYS A1139 THR A1140 0 SHEET 2 AB2 2 ILE A1145 LEU A1146 -1 O LEU A1146 N LYS A1139 SHEET 1 AB3 2 CYS A1169 ILE A1171 0 SHEET 2 AB3 2 ARG A1230 PHE A1232 1 O PHE A1232 N ASN A1170 SHEET 1 AB4 2 ALA A1173 MET A1174 0 SHEET 2 AB4 2 ILE A1195 SER A1196 -1 O SER A1196 N ALA A1173 SHEET 1 AB5 2 THR A1181 THR A1183 0 SHEET 2 AB5 2 ILE A1186 HIS A1188 -1 O HIS A1188 N THR A1181 SHEET 1 AB6 7 ILE A1221 MET A1223 0 SHEET 2 AB6 7 ASN A1298 ILE A1300 1 O ILE A1300 N MET A1222 SHEET 3 AB6 7 TYR A1324 LEU A1327 1 O LEU A1327 N PHE A1299 SHEET 4 AB6 7 TRP A1345 ASN A1348 1 O ASN A1348 N LEU A1326 SHEET 5 AB6 7 ILE A1403 GLU A1408 1 O THR A1406 N PHE A1347 SHEET 6 AB6 7 SER A1414 ASN A1420 -1 O ILE A1419 N ILE A1403 SHEET 7 AB6 7 SER A1425 LEU A1430 -1 O SER A1427 N GLU A1418 SHEET 1 AB7 2 THR A1236 GLY A1237 0 SHEET 2 AB7 2 ALA A1275 ILE A1276 -1 O ALA A1275 N GLY A1237 SHEET 1 AB8 6 THR A1286 ILE A1288 0 SHEET 2 AB8 6 LEU A1313 PHE A1317 1 O SER A1314 N ILE A1288 SHEET 3 AB8 6 SER A1334 ASN A1338 1 O ASN A1336 N TYR A1315 SHEET 4 AB8 6 GLN A1388 SER A1393 1 O ASP A1391 N ILE A1337 SHEET 5 AB8 6 LYS A1382 ILE A1385 -1 N LEU A1383 O ILE A1390 SHEET 6 AB8 6 ASP A1377 ILE A1378 -1 N ASP A1377 O ILE A1384 SHEET 1 AB9 2 ILE A1356 SER A1357 0 SHEET 2 AB9 2 LYS A1364 LYS A1365 -1 O LYS A1364 N SER A1357 SHEET 1 AC1 5 ASN A1457 THR A1463 0 SHEET 2 AC1 5 LYS A1469 SER A1475 -1 O ILE A1474 N ILE A1458 SHEET 3 AC1 5 SER A1481 LYS A1487 -1 O HIS A1484 N PHE A1471 SHEET 4 AC1 5 LYS A1490 TYR A1496 -1 O GLU A1494 N ILE A1483 SHEET 5 AC1 5 LEU A1501 SER A1505 -1 O PHE A1503 N PHE A1495 SHEET 1 AC2 8 SER A1641 THR A1644 0 SHEET 2 AC2 8 ASN A1652 PRO A1657 -1 O GLU A1656 N LYS A1642 SHEET 3 AC2 8 LYS A1687 ILE A1690 1 O LEU A1689 N VAL A1653 SHEET 4 AC2 8 ILE A1714 VAL A1716 1 O ILE A1715 N VAL A1688 SHEET 5 AC2 8 LYS A1757 ILE A1765 1 O ARG A1764 N ILE A1714 SHEET 6 AC2 8 PHE A1746 GLU A1754 -1 N ARG A1750 O GLN A1761 SHEET 7 AC2 8 TYR A1737 THR A1741 -1 N LYS A1738 O VAL A1749 SHEET 8 AC2 8 LYS A1798 SER A1799 1 O LYS A1798 N TRP A1739 SHEET 1 AC3 4 LEU A1671 SER A1674 0 SHEET 2 AC3 4 LEU A1698 ASN A1702 1 O ASN A1702 N PHE A1673 SHEET 3 AC3 4 VAL A1726 LEU A1730 1 O ASN A1729 N ILE A1699 SHEET 4 AC3 4 MET A1778 ASP A1781 1 O ASP A1781 N ILE A1728 SHEET 1 AC4 2 LEU A1833 ASN A1835 0 SHEET 2 AC4 2 LEU A1840 TYR A1842 -1 O PHE A1841 N ILE A1834 SHEET 1 AC5 2 GLY A1853 ILE A1857 0 SHEET 2 AC5 2 LYS A1860 PHE A1864 -1 O TYR A1862 N GLN A1855 SHEET 1 AC6 2 LYS A1876 ILE A1878 0 SHEET 2 AC6 2 LYS A1881 PHE A1883 -1 O LYS A1881 N ILE A1878 SHEET 1 AC7 2 GLY A1894 GLY A1898 0 SHEET 2 AC7 2 GLY A1901 PHE A1905 -1 O PHE A1905 N GLY A1894 SHEET 1 AC8 2 PHE A1926 LEU A1927 0 SHEET 2 AC8 2 TYR A1934 TYR A1935 -1 O TYR A1934 N LEU A1927 SHEET 1 AC9 2 GLY A1945 ARG A1947 0 SHEET 2 AC9 2 TYR A1954 PHE A1956 -1 O TYR A1954 N ARG A1947 SHEET 1 AD1 2 TRP A1988 VAL A1991 0 SHEET 2 AD1 2 SER A1994 TYR A1997 -1 O SER A1994 N VAL A1991 SHEET 1 AD2 2 TYR A2009 LYS A2010 0 SHEET 2 AD2 2 PHE A2017 TYR A2018 -1 O PHE A2017 N LYS A2010 SHEET 1 AD3 3 GLY A2028 SER A2031 0 SHEET 2 AD3 3 PHE A2036 ALA A2040 -1 O PHE A2039 N GLY A2028 SHEET 3 AD3 3 GLN A2052 ALA A2053 -1 O GLN A2052 N ALA A2040 SHEET 1 AD4 2 PHE A2060 LEU A2063 0 SHEET 2 AD4 2 LYS A2066 TYR A2069 -1 O TYR A2068 N LEU A2061 SHEET 1 AD5 2 GLY A2100 ILE A2104 0 SHEET 2 AD5 2 LYS A2107 PHE A2111 -1 O TYR A2109 N GLN A2102 SHEET 1 AD6 2 THR A2124 ILE A2125 0 SHEET 2 AD6 2 LYS A2128 LYS A2129 -1 O LYS A2128 N ILE A2125 SHEET 1 AD7 2 TYR A2143 ILE A2146 0 SHEET 2 AD7 2 LYS A2149 TYR A2152 -1 O LYS A2149 N ILE A2146 SHEET 1 AD8 3 GLY A2162 LYS A2165 0 SHEET 2 AD8 3 PHE A2170 ALA A2174 -1 O PHE A2173 N GLY A2162 SHEET 3 AD8 3 GLN A2186 ALA A2187 -1 O GLN A2186 N ALA A2174 SHEET 1 AD9 2 PHE A2194 LEU A2195 0 SHEET 2 AD9 2 TYR A2202 TYR A2203 -1 O TYR A2202 N LEU A2195 SHEET 1 AE1 2 GLY A2213 ILE A2216 0 SHEET 2 AE1 2 LYS A2221 PHE A2224 -1 O PHE A2224 N GLY A2213 SHEET 1 AE2 2 LEU A2235 THR A2237 0 SHEET 2 AE2 2 LYS A2242 TYR A2244 -1 O TYR A2243 N CYS A2236 SHEET 1 AE3 3 GLY A2254 ILE A2258 0 SHEET 2 AE3 3 ASN A2261 ASP A2266 -1 O ASN A2261 N ILE A2258 SHEET 3 AE3 3 LYS A2272 MET A2273 -1 O LYS A2272 N ASP A2266 SHEET 1 AE4 2 GLY A2276 LYS A2279 0 SHEET 2 AE4 2 PHE A2284 PHE A2287 -1 O PHE A2287 N GLY A2276 SHEET 1 AE5 2 PHE A2308 THR A2310 0 SHEET 2 AE5 2 LYS A2315 TYR A2317 -1 O TYR A2316 N LEU A2309 SHEET 1 AE6 2 TRP A2328 ILE A2331 0 SHEET 2 AE6 2 LYS A2334 TYR A2337 -1 O TYR A2336 N GLN A2329 SHEET 1 AE7 2 GLY A2348 ILE A2352 0 SHEET 2 AE7 2 LYS A2355 PHE A2359 -1 O PHE A2359 N GLY A2348 SHEET 1 AE8 2 LYS B 3 VAL B 5 0 SHEET 2 AE8 2 ALA B 23 SER B 25 -1 O ALA B 23 N VAL B 5 SHEET 1 AE9 6 GLY B 10 VAL B 12 0 SHEET 2 AE9 6 THR B 117 VAL B 121 1 O THR B 120 N GLY B 10 SHEET 3 AE9 6 ALA B 92 GLN B 99 -1 N TYR B 94 O THR B 117 SHEET 4 AE9 6 MET B 34 GLN B 39 -1 N GLN B 39 O LEU B 93 SHEET 5 AE9 6 LEU B 45 ILE B 51 -1 O ILE B 51 N MET B 34 SHEET 6 AE9 6 ILE B 58 TYR B 59 -1 O TYR B 59 N ALA B 50 SHEET 1 AF1 4 GLY B 10 VAL B 12 0 SHEET 2 AF1 4 THR B 117 VAL B 121 1 O THR B 120 N GLY B 10 SHEET 3 AF1 4 ALA B 92 GLN B 99 -1 N TYR B 94 O THR B 117 SHEET 4 AF1 4 PHE B 110 TRP B 113 -1 O ASP B 111 N ARG B 98 SHEET 1 AF2 2 SER B 17 LEU B 20 0 SHEET 2 AF2 2 LEU B 81 SER B 84 -1 O MET B 83 N LEU B 18 SHEET 1 AF3 2 ARG B 72 ASP B 73 0 SHEET 2 AF3 2 THR B 78 LEU B 79 -1 O THR B 78 N ASP B 73 SHEET 1 AF4 4 MET C 224 GLN C 226 0 SHEET 2 AF4 4 VAL C 239 ALA C 245 -1 O LYS C 244 N THR C 225 SHEET 3 AF4 4 TYR C 290 ILE C 295 -1 O PHE C 291 N CYS C 243 SHEET 4 AF4 4 PHE C 282 SER C 285 -1 N THR C 283 O SER C 294 SHEET 1 AF5 2 PHE C 230 THR C 233 0 SHEET 2 AF5 2 LYS C 323 LEU C 326 1 O GLU C 325 N THR C 233 SHEET 1 AF6 4 THR C 273 ARG C 274 0 SHEET 2 AF6 4 LYS C 265 TYR C 269 -1 N TYR C 269 O THR C 273 SHEET 3 AF6 4 VAL C 253 GLN C 257 -1 N TRP C 255 O LEU C 267 SHEET 4 AF6 4 CYS C 308 GLN C 310 -1 O GLN C 309 N ALA C 254 SSBOND 1 CYS B 22 CYS B 96 1555 1555 2.03 SSBOND 2 CYS C 243 CYS C 308 1555 1555 2.03 CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 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 1.000000 0.000000 0.000000 0.00000 SCALE2 0.000000 1.000000 0.000000 0.00000 SCALE3 0.000000 0.000000 1.000000 0.00000