HEADER DNA BINDING PROTEIN 04-JUN-17 5W1R
TITLE CRYO-EM STRUCTURE OF DNAPKCS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA-DEPENDENT PROTEIN KINASE CATALYTIC SUBUNIT;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: DNA-PKCS,DNPK1,P460;
COMPND 5 EC: 2.7.11.1
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 CELL_LINE: HELA S3;
SOURCE 6 ATCC: CCL-2.2;
SOURCE 7 ORGAN: CERVIX
KEYWDS DNAP, PIKK, NHEJ, V(D)J RECOMBINATION, DNA BINDING PROTEIN
EXPDTA ELECTRON MICROSCOPY
AUTHOR H.SHARIF,Y.LI,H.WU
REVDAT 4 18-DEC-19 5W1R 1 CRYST1 SCALE
REVDAT 3 11-DEC-19 5W1R 1 REMARK
REVDAT 2 20-SEP-17 5W1R 1 REMARK
REVDAT 1 19-JUL-17 5W1R 0
JRNL AUTH H.SHARIF,Y.LI,Y.DONG,L.DONG,W.L.WANG,Y.MAO,H.WU
JRNL TITL CRYO-EM STRUCTURE OF THE DNA-PK HOLOENZYME.
JRNL REF PROC. NATL. ACAD. SCI. V. 114 7367 2017
JRNL REF 2 U.S.A.
JRNL REFN ESSN 1091-6490
JRNL PMID 28652322
JRNL DOI 10.1073/PNAS.1707386114
REMARK 2
REMARK 2 RESOLUTION. 4.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 SOFTWARE PACKAGES : NULL
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) : 4.400
REMARK 3 NUMBER OF PARTICLES : 289798
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 5W1R COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-JUN-17.
REMARK 100 THE DEPOSITION ID IS D_1000228270.
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 : DNA-PKCS
REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 0.60
REMARK 245 SAMPLE SUPPORT DETAILS : NULL
REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL
REMARK 245 SAMPLE BUFFER : NULL
REMARK 245 PH : 7.40
REMARK 245 SAMPLE DETAILS : NULL
REMARK 245
REMARK 245 DATA ACQUISITION
REMARK 245 DATE OF EXPERIMENT : NULL
REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL
REMARK 245 TEMPERATURE (KELVIN) : NULL
REMARK 245 MICROSCOPE MODEL : FEI TECNAI ARCTICA
REMARK 245 DETECTOR TYPE : GATAN K2 SUMMIT (4K X 4K)
REMARK 245 MINIMUM DEFOCUS (NM) : NULL
REMARK 245 MAXIMUM DEFOCUS (NM) : NULL
REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 NOMINAL CS : NULL
REMARK 245 IMAGING MODE : BRIGHT FIELD
REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 40.00
REMARK 245 ILLUMINATION MODE : FLOOD BEAM
REMARK 245 NOMINAL MAGNIFICATION : NULL
REMARK 245 CALIBRATED MAGNIFICATION : NULL
REMARK 245 SOURCE : FIELD EMISSION GUN
REMARK 245 ACCELERATION VOLTAGE (KV) : 200
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 0 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 202330 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 ALA A 2
REMARK 465 GLY A 3
REMARK 465 SER A 4
REMARK 465 GLY A 5
REMARK 465 ALA A 6
REMARK 465 GLY A 7
REMARK 465 SER A 46
REMARK 465 SER A 47
REMARK 465 PRO A 48
REMARK 465 ALA A 120
REMARK 465 ALA A 121
REMARK 465 LYS A 122
REMARK 465 CYS A 123
REMARK 465 LYS A 124
REMARK 465 ILE A 125
REMARK 465 PRO A 126
REMARK 465 PRO A 498
REMARK 465 LYS A 499
REMARK 465 GLY A 500
REMARK 465 PRO A 501
REMARK 465 GLU A 502
REMARK 465 SER A 503
REMARK 465 GLU A 504
REMARK 465 SER A 505
REMARK 465 GLU A 506
REMARK 465 ASP A 507
REMARK 465 HIS A 508
REMARK 465 ARG A 509
REMARK 465 ALA A 510
REMARK 465 SER A 511
REMARK 465 GLY A 512
REMARK 465 GLU A 513
REMARK 465 VAL A 514
REMARK 465 ARG A 515
REMARK 465 THR A 516
REMARK 465 GLY A 517
REMARK 465 LYS A 518
REMARK 465 TRP A 519
REMARK 465 LYS A 520
REMARK 465 VAL A 521
REMARK 465 PRO A 522
REMARK 465 THR A 523
REMARK 465 TYR A 524
REMARK 465 MET A 541
REMARK 465 ASP A 542
REMARK 465 SER A 543
REMARK 465 ILE A 544
REMARK 465 LEU A 545
REMARK 465 TRP A 601
REMARK 465 MET A 602
REMARK 465 ILE A 603
REMARK 465 PRO A 604
REMARK 465 PHE A 683
REMARK 465 GLU A 684
REMARK 465 GLY A 685
REMARK 465 VAL A 686
REMARK 465 SER A 687
REMARK 465 PRO A 688
REMARK 465 LYS A 689
REMARK 465 SER A 690
REMARK 465 LEU A 691
REMARK 465 LYS A 692
REMARK 465 HIS A 693
REMARK 465 SER A 694
REMARK 465 PRO A 695
REMARK 465 GLU A 696
REMARK 465 ASP A 807
REMARK 465 GLU A 808
REMARK 465 THR A 809
REMARK 465 LYS A 810
REMARK 465 ASN A 811
REMARK 465 ASN A 812
REMARK 465 TRP A 813
REMARK 465 GLU A 814
REMARK 465 VAL A 815
REMARK 465 SER A 816
REMARK 465 ALA A 817
REMARK 465 LEU A 818
REMARK 465 SER A 819
REMARK 465 ARG A 820
REMARK 465 ALA A 821
REMARK 465 ALA A 822
REMARK 465 GLN A 823
REMARK 465 LYS A 824
REMARK 465 GLY A 825
REMARK 465 PHE A 826
REMARK 465 ASN A 827
REMARK 465 LYS A 828
REMARK 465 VAL A 829
REMARK 465 VAL A 830
REMARK 465 LEU A 831
REMARK 465 LYS A 832
REMARK 465 HIS A 833
REMARK 465 LEU A 834
REMARK 465 LYS A 835
REMARK 465 LYS A 836
REMARK 465 THR A 837
REMARK 465 LYS A 838
REMARK 465 ASN A 839
REMARK 465 LEU A 840
REMARK 465 SER A 841
REMARK 465 SER A 842
REMARK 465 ASN A 843
REMARK 465 GLU A 844
REMARK 465 ALA A 845
REMARK 465 ARG A 888
REMARK 465 GLU A 889
REMARK 465 LYS A 890
REMARK 465 ARG A 891
REMARK 465 LEU A 892
REMARK 465 SER A 893
REMARK 465 PHE A 894
REMARK 465 ALA A 895
REMARK 465 VAL A 896
REMARK 465 PRO A 897
REMARK 465 PHE A 898
REMARK 465 THR A 1181
REMARK 465 GLU A 1182
REMARK 465 CYS A 1183
REMARK 465 ARG A 1184
REMARK 465 HIS A 1185
REMARK 465 LYS A 1186
REMARK 465 SER A 1187
REMARK 465 ILE A 1188
REMARK 465 GLU A 1189
REMARK 465 LEU A 1190
REMARK 465 PHE A 1191
REMARK 465 TYR A 1192
REMARK 465 LYS A 1193
REMARK 465 PHE A 1194
REMARK 465 VAL A 1195
REMARK 465 PRO A 1196
REMARK 465 LEU A 1197
REMARK 465 LEU A 1198
REMARK 465 PRO A 1199
REMARK 465 GLY A 1200
REMARK 465 ASN A 1201
REMARK 465 ARG A 1202
REMARK 465 SER A 1203
REMARK 465 PRO A 1204
REMARK 465 ASN A 1205
REMARK 465 LEU A 1206
REMARK 465 TRP A 1207
REMARK 465 LEU A 1208
REMARK 465 LYS A 1209
REMARK 465 ASP A 1210
REMARK 465 VAL A 1211
REMARK 465 LEU A 1212
REMARK 465 ALA A 1308
REMARK 465 ALA A 1309
REMARK 465 GLU A 1310
REMARK 465 LYS A 1311
REMARK 465 CYS A 1312
REMARK 465 PHE A 1313
REMARK 465 GLY A 1314
REMARK 465 THR A 1315
REMARK 465 GLY A 1316
REMARK 465 ALA A 1317
REMARK 465 ALA A 1318
REMARK 465 GLY A 1319
REMARK 465 ASN A 1320
REMARK 465 ARG A 1321
REMARK 465 THR A 1322
REMARK 465 ARG A 1527
REMARK 465 LEU A 1528
REMARK 465 VAL A 1529
REMARK 465 SER A 1530
REMARK 465 LEU A 1531
REMARK 465 LEU A 1532
REMARK 465 LEU A 1533
REMARK 465 ASN A 1534
REMARK 465 PRO A 1535
REMARK 465 ALA A 1536
REMARK 465 VAL A 1537
REMARK 465 LEU A 1538
REMARK 465 SER A 1539
REMARK 465 THR A 1540
REMARK 465 ALA A 1541
REMARK 465 SER A 1542
REMARK 465 LEU A 1543
REMARK 465 GLY A 1544
REMARK 465 SER A 1545
REMARK 465 SER A 1546
REMARK 465 GLN A 1547
REMARK 465 ASN A 1610
REMARK 465 GLN A 1611
REMARK 465 LYS A 1612
REMARK 465 HIS A 1613
REMARK 465 GLN A 1614
REMARK 465 GLY A 1615
REMARK 465 LEU A 1616
REMARK 465 LYS A 1617
REMARK 465 LEU A 1618
REMARK 465 ALA A 1619
REMARK 465 THR A 1620
REMARK 465 THR A 1621
REMARK 465 ILE A 1622
REMARK 465 LEU A 1623
REMARK 465 GLN A 1624
REMARK 465 HIS A 1625
REMARK 465 TRP A 1626
REMARK 465 LYS A 1627
REMARK 465 LYS A 1628
REMARK 465 CYS A 1629
REMARK 465 VAL A 1659
REMARK 465 SER A 1660
REMARK 465 PHE A 1661
REMARK 465 ASN A 1662
REMARK 465 THR A 1663
REMARK 465 SER A 1664
REMARK 465 HIS A 1665
REMARK 465 GLY A 1666
REMARK 465 SER A 1667
REMARK 465 PHE A 1668
REMARK 465 PRO A 1669
REMARK 465 GLU A 1670
REMARK 465 VAL A 1671
REMARK 465 PHE A 1672
REMARK 465 THR A 1673
REMARK 465 THR A 1674
REMARK 465 TYR A 1675
REMARK 465 GLU A 1764
REMARK 465 VAL A 1765
REMARK 465 LEU A 1766
REMARK 465 CYS A 1767
REMARK 465 ARG A 1768
REMARK 465 GLU A 1769
REMARK 465 GLN A 1770
REMARK 465 GLN A 1771
REMARK 465 HIS A 1772
REMARK 465 VAL A 1773
REMARK 465 MET A 1774
REMARK 465 GLU A 1775
REMARK 465 GLU A 1776
REMARK 465 LEU A 1777
REMARK 465 PHE A 1778
REMARK 465 GLN A 1779
REMARK 465 SER A 1780
REMARK 465 SER A 1781
REMARK 465 PHE A 1782
REMARK 465 ARG A 1783
REMARK 465 ARG A 1784
REMARK 465 ILE A 1785
REMARK 465 ALA A 1786
REMARK 465 ARG A 1787
REMARK 465 ARG A 1788
REMARK 465 GLY A 1789
REMARK 465 SER A 1790
REMARK 465 CYS A 1791
REMARK 465 VAL A 1792
REMARK 465 THR A 1793
REMARK 465 GLN A 1794
REMARK 465 VAL A 1795
REMARK 465 GLY A 1796
REMARK 465 LEU A 1797
REMARK 465 PHE A 1819
REMARK 465 VAL A 1820
REMARK 465 ASP A 1821
REMARK 465 ARG A 1822
REMARK 465 SER A 1823
REMARK 465 LEU A 1824
REMARK 465 LEU A 1825
REMARK 465 THR A 1826
REMARK 465 LEU A 1827
REMARK 465 LEU A 1828
REMARK 465 TRP A 1829
REMARK 465 HIS A 1830
REMARK 465 CYS A 1831
REMARK 465 SER A 1832
REMARK 465 LEU A 1833
REMARK 465 ASP A 1834
REMARK 465 ALA A 1835
REMARK 465 LEU A 1836
REMARK 465 ARG A 1837
REMARK 465 GLU A 1838
REMARK 465 PHE A 1839
REMARK 465 PHE A 1840
REMARK 465 SER A 1841
REMARK 465 THR A 1842
REMARK 465 ILE A 1843
REMARK 465 VAL A 1844
REMARK 465 VAL A 1845
REMARK 465 ASP A 1846
REMARK 465 ALA A 1847
REMARK 465 ILE A 1848
REMARK 465 ASP A 1849
REMARK 465 VAL A 1850
REMARK 465 LEU A 1851
REMARK 465 LYS A 1852
REMARK 465 SER A 1853
REMARK 465 ARG A 1854
REMARK 465 PHE A 1855
REMARK 465 THR A 1856
REMARK 465 PRO A 2110
REMARK 465 PRO A 2111
REMARK 465 GLN A 2112
REMARK 465 GLY A 2113
REMARK 465 GLU A 2114
REMARK 465 GLU A 2115
REMARK 465 ASP A 2116
REMARK 465 PHE A 2389
REMARK 465 HIS A 2390
REMARK 465 GLY A 2391
REMARK 465 PRO A 2575
REMARK 465 MET A 2576
REMARK 465 PHE A 2577
REMARK 465 GLU A 2578
REMARK 465 HIS A 2579
REMARK 465 PRO A 2580
REMARK 465 LEU A 2581
REMARK 465 SER A 2582
REMARK 465 GLU A 2583
REMARK 465 CYS A 2584
REMARK 465 GLU A 2585
REMARK 465 PHE A 2586
REMARK 465 GLN A 2587
REMARK 465 GLU A 2588
REMARK 465 TYR A 2589
REMARK 465 THR A 2590
REMARK 465 ILE A 2591
REMARK 465 ASP A 2592
REMARK 465 SER A 2593
REMARK 465 ASP A 2594
REMARK 465 TRP A 2595
REMARK 465 ARG A 2596
REMARK 465 PHE A 2597
REMARK 465 ARG A 2598
REMARK 465 SER A 2599
REMARK 465 THR A 2600
REMARK 465 VAL A 2601
REMARK 465 LEU A 2602
REMARK 465 THR A 2603
REMARK 465 PRO A 2604
REMARK 465 MET A 2605
REMARK 465 PHE A 2606
REMARK 465 VAL A 2607
REMARK 465 GLU A 2608
REMARK 465 THR A 2609
REMARK 465 GLN A 2610
REMARK 465 ALA A 2611
REMARK 465 SER A 2612
REMARK 465 GLN A 2613
REMARK 465 GLY A 2614
REMARK 465 THR A 2615
REMARK 465 LEU A 2616
REMARK 465 GLN A 2617
REMARK 465 THR A 2618
REMARK 465 ARG A 2619
REMARK 465 THR A 2620
REMARK 465 GLN A 2621
REMARK 465 GLU A 2622
REMARK 465 GLY A 2623
REMARK 465 SER A 2624
REMARK 465 LEU A 2625
REMARK 465 SER A 2626
REMARK 465 ALA A 2627
REMARK 465 ARG A 2628
REMARK 465 TRP A 2629
REMARK 465 PRO A 2630
REMARK 465 VAL A 2631
REMARK 465 ALA A 2632
REMARK 465 GLY A 2633
REMARK 465 GLN A 2634
REMARK 465 ILE A 2635
REMARK 465 ARG A 2636
REMARK 465 ALA A 2637
REMARK 465 THR A 2638
REMARK 465 GLN A 2639
REMARK 465 GLN A 2640
REMARK 465 GLN A 2641
REMARK 465 HIS A 2642
REMARK 465 ASP A 2643
REMARK 465 PHE A 2644
REMARK 465 THR A 2645
REMARK 465 LEU A 2646
REMARK 465 THR A 2647
REMARK 465 GLN A 2648
REMARK 465 THR A 2649
REMARK 465 ALA A 2650
REMARK 465 ASP A 2651
REMARK 465 GLY A 2652
REMARK 465 ARG A 2653
REMARK 465 SER A 2654
REMARK 465 SER A 2655
REMARK 465 PHE A 2656
REMARK 465 ASP A 2657
REMARK 465 TRP A 2658
REMARK 465 LEU A 2659
REMARK 465 THR A 2660
REMARK 465 GLY A 2661
REMARK 465 SER A 2662
REMARK 465 SER A 2663
REMARK 465 THR A 2664
REMARK 465 ASP A 2665
REMARK 465 PRO A 2666
REMARK 465 LEU A 2667
REMARK 465 VAL A 2668
REMARK 465 ASP A 2669
REMARK 465 HIS A 2670
REMARK 465 THR A 2671
REMARK 465 SER A 2672
REMARK 465 PRO A 2673
REMARK 465 SER A 2674
REMARK 465 SER A 2675
REMARK 465 ASP A 2676
REMARK 465 SER A 2677
REMARK 465 LEU A 2678
REMARK 465 LEU A 2679
REMARK 465 PHE A 2680
REMARK 465 ALA A 2681
REMARK 465 HIS A 2682
REMARK 465 LYS A 2683
REMARK 465 ARG A 2684
REMARK 465 SER A 2685
REMARK 465 GLU A 2686
REMARK 465 ARG A 2687
REMARK 465 LEU A 2688
REMARK 465 GLN A 2689
REMARK 465 ARG A 2690
REMARK 465 ALA A 2691
REMARK 465 PRO A 2692
REMARK 465 LEU A 2693
REMARK 465 LYS A 2694
REMARK 465 SER A 2695
REMARK 465 VAL A 2696
REMARK 465 GLY A 2697
REMARK 465 PRO A 2698
REMARK 465 ASP A 2699
REMARK 465 PHE A 2700
REMARK 465 GLY A 2701
REMARK 465 LYS A 2702
REMARK 465 LYS A 2703
REMARK 465 ARG A 2704
REMARK 465 LEU A 2705
REMARK 465 GLY A 2706
REMARK 465 LEU A 2707
REMARK 465 PRO A 2708
REMARK 465 GLY A 2709
REMARK 465 ASP A 2710
REMARK 465 GLU A 2711
REMARK 465 VAL A 2712
REMARK 465 ASP A 2713
REMARK 465 ASN A 2714
REMARK 465 LYS A 2715
REMARK 465 VAL A 2716
REMARK 465 LYS A 2717
REMARK 465 GLY A 2718
REMARK 465 ALA A 2719
REMARK 465 ALA A 2720
REMARK 465 GLY A 2721
REMARK 465 ARG A 2722
REMARK 465 THR A 2723
REMARK 465 ASP A 2724
REMARK 465 LEU A 2725
REMARK 465 LEU A 2726
REMARK 465 ARG A 2727
REMARK 465 LEU A 2728
REMARK 465 ARG A 2729
REMARK 465 ARG A 2730
REMARK 465 ARG A 2731
REMARK 465 PHE A 2732
REMARK 465 MET A 2733
REMARK 465 ARG A 2734
REMARK 465 ASP A 2735
REMARK 465 GLN A 2736
REMARK 465 GLU A 2737
REMARK 465 LYS A 2738
REMARK 465 LEU A 2739
REMARK 465 SER A 2740
REMARK 465 LEU A 2741
REMARK 465 MET A 2742
REMARK 465 TYR A 2743
REMARK 465 ALA A 2744
REMARK 465 ARG A 2745
REMARK 465 LYS A 2746
REMARK 465 GLY A 2747
REMARK 465 VAL A 2748
REMARK 465 ALA A 2749
REMARK 465 GLU A 2750
REMARK 465 GLN A 2751
REMARK 465 LYS A 2752
REMARK 465 ARG A 2753
REMARK 465 GLU A 2754
REMARK 465 LYS A 2755
REMARK 465 GLU A 2756
REMARK 465 ILE A 2757
REMARK 465 LYS A 2758
REMARK 465 SER A 2759
REMARK 465 GLU A 2760
REMARK 465 LEU A 2761
REMARK 465 LYS A 2762
REMARK 465 MET A 2763
REMARK 465 LYS A 2764
REMARK 465 GLN A 2765
REMARK 465 ASP A 2766
REMARK 465 ALA A 2767
REMARK 465 GLN A 2768
REMARK 465 VAL A 2769
REMARK 465 VAL A 2770
REMARK 465 LEU A 2771
REMARK 465 TYR A 2772
REMARK 465 ARG A 2773
REMARK 465 SER A 2774
REMARK 465 LEU A 2901
REMARK 465 PRO A 2902
REMARK 465 ALA A 2903
REMARK 465 GLU A 2904
REMARK 465 LEU A 2905
REMARK 465 PRO A 2906
REMARK 465 ALA A 2927
REMARK 465 LYS A 2928
REMARK 465 THR A 3198
REMARK 465 PRO A 3199
REMARK 465 LEU A 3200
REMARK 465 PRO A 3201
REMARK 465 GLU A 3202
REMARK 465 ASP A 3203
REMARK 465 ASN A 3204
REMARK 465 SER A 3205
REMARK 465 MET A 3206
REMARK 465 ASN A 3207
REMARK 465 VAL A 3208
REMARK 465 ASP A 3209
REMARK 465 GLN A 3210
REMARK 465 ASP A 3211
REMARK 465 GLY A 3212
REMARK 465 ASP A 3213
REMARK 465 PRO A 3214
REMARK 465 SER A 3215
REMARK 465 ASP A 3216
REMARK 465 ARG A 3217
REMARK 465 MET A 3218
REMARK 465 GLU A 3219
REMARK 465 VAL A 3220
REMARK 465 GLN A 3221
REMARK 465 GLU A 3222
REMARK 465 GLN A 3223
REMARK 465 GLU A 3224
REMARK 465 GLU A 3225
REMARK 465 ASP A 3226
REMARK 465 LEU A 3360
REMARK 465 GLU A 3361
REMARK 465 LEU A 3362
REMARK 465 SER A 3363
REMARK 465 GLY A 3364
REMARK 465 SER A 3365
REMARK 465 SER A 3366
REMARK 465 SER A 3367
REMARK 465 GLU A 3368
REMARK 465 ASP A 3369
REMARK 465 SER A 3370
REMARK 465 GLU A 3371
REMARK 465 LYS A 3372
REMARK 465 SER A 3489
REMARK 465 VAL A 3490
REMARK 465 PRO A 3491
REMARK 465 LYS A 3650
REMARK 465 LEU A 3651
REMARK 465 LEU A 3652
REMARK 465 GLU A 3698
REMARK 465 LEU A 3699
REMARK 465 GLU A 3700
REMARK 465 ILE A 3701
REMARK 465 MET A 4128
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 9 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 12 CG CD1 CD2
REMARK 470 HIS A 32 CG ND1 CD2 CE1 NE2
REMARK 470 CYS A 42 SG
REMARK 470 VAL A 43 CG1 CG2
REMARK 470 LEU A 44 CG CD1 CD2
REMARK 470 VAL A 50 CG1 CG2
REMARK 470 LEU A 51 CG CD1 CD2
REMARK 470 LEU A 53 CG CD1 CD2
REMARK 470 GLN A 54 CG CD OE1 NE2
REMARK 470 THR A 55 OG1 CG2
REMARK 470 LEU A 57 CG CD1 CD2
REMARK 470 ARG A 61 CG CD NE CZ NH1 NH2
REMARK 470 SER A 75 OG
REMARK 470 ILE A 76 CG1 CG2 CD1
REMARK 470 PHE A 78 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG A 79 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 80 CG CD OE1 OE2
REMARK 470 ARG A 82 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 84 CG CD OE1 OE2
REMARK 470 PHE A 92 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU A 94 CG CD OE1 OE2
REMARK 470 LYS A 95 CG CD CE NZ
REMARK 470 MET A 96 CG SD CE
REMARK 470 GLN A 98 CG CD OE1 NE2
REMARK 470 LYS A 99 CG CD CE NZ
REMARK 470 ILE A 100 CG1 CG2 CD1
REMARK 470 TYR A 103 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU A 106 CG CD OE1 OE2
REMARK 470 LYS A 117 CG CD CE NZ
REMARK 470 LYS A 133 CG CD CE NZ
REMARK 470 GLN A 136 CG CD OE1 NE2
REMARK 470 ARG A 142 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 143 CG CD1 CD2
REMARK 470 MET A 144 CG SD CE
REMARK 470 ASP A 145 CG OD1 OD2
REMARK 470 PHE A 147 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS A 148 CG CD CE NZ
REMARK 470 GLU A 151 CG CD OE1 OE2
REMARK 470 LYS A 155 CG CD CE NZ
REMARK 470 LYS A 164 CG CD CE NZ
REMARK 470 VAL A 170 CG1 CG2
REMARK 470 VAL A 174 CG1 CG2
REMARK 470 TYR A 175 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LEU A 180 CG CD1 CD2
REMARK 470 LEU A 181 CG CD1 CD2
REMARK 470 GLU A 183 CG CD OE1 OE2
REMARK 470 VAL A 184 CG1 CG2
REMARK 470 HIS A 185 CG ND1 CD2 CE1 NE2
REMARK 470 GLU A 188 CG CD OE1 OE2
REMARK 470 MET A 189 CG SD CE
REMARK 470 GLU A 194 CG CD OE1 OE2
REMARK 470 LEU A 201 CG CD1 CD2
REMARK 470 GLU A 203 CG CD OE1 OE2
REMARK 470 MET A 208 CG SD CE
REMARK 470 ARG A 213 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 214 CG CD OE1 OE2
REMARK 470 ILE A 256 CG1 CG2 CD1
REMARK 470 SER A 280 OG
REMARK 470 PHE A 282 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU A 317 CG CD OE1 OE2
REMARK 470 LYS A 321 CG CD CE NZ
REMARK 470 LYS A 337 CG CD CE NZ
REMARK 470 PHE A 345 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASN A 356 CG OD1 ND2
REMARK 470 TYR A 366 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 PHE A 369 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS A 374 CG CD CE NZ
REMARK 470 ILE A 376 CG1 CG2 CD1
REMARK 470 LYS A 379 CG CD CE NZ
REMARK 470 THR A 402 OG1 CG2
REMARK 470 ASP A 404 CG OD1 OD2
REMARK 470 ASP A 425 CG OD1 OD2
REMARK 470 TYR A 449 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS A 452 CG CD CE NZ
REMARK 470 LEU A 468 CG CD1 CD2
REMARK 470 LYS A 471 CG CD CE NZ
REMARK 470 ARG A 476 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 489 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 493 CG CD CE NZ
REMARK 470 LEU A 497 CG CD1 CD2
REMARK 470 LYS A 525 CG CD CE NZ
REMARK 470 ASP A 526 CG OD1 OD2
REMARK 470 LEU A 530 CG CD1 CD2
REMARK 470 PHE A 531 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG A 532 CG CD NE CZ NH1 NH2
REMARK 470 HIS A 533 CG ND1 CD2 CE1 NE2
REMARK 470 ASP A 538 CG OD1 OD2
REMARK 470 GLN A 539 CG CD OE1 NE2
REMARK 470 MET A 540 CG SD CE
REMARK 470 ASP A 547 CG OD1 OD2
REMARK 470 GLU A 548 CG CD OE1 OE2
REMARK 470 PHE A 550 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 PHE A 551 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU A 567 CG CD OE1 OE2
REMARK 470 PHE A 568 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS A 570 CG CD CE NZ
REMARK 470 VAL A 572 CG1 CG2
REMARK 470 LYS A 574 CG CD CE NZ
REMARK 470 ILE A 575 CG1 CG2 CD1
REMARK 470 LYS A 578 CG CD CE NZ
REMARK 470 ASN A 593 CG OD1 ND2
REMARK 470 VAL A 600 CG1 CG2
REMARK 470 THR A 605 OG1 CG2
REMARK 470 SER A 606 OG
REMARK 470 LEU A 612 CG CD1 CD2
REMARK 470 LYS A 618 CG CD CE NZ
REMARK 470 PHE A 620 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LEU A 626 CG CD1 CD2
REMARK 470 GLU A 628 CG CD OE1 OE2
REMARK 470 PHE A 629 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 CYS A 630 SG
REMARK 470 ARG A 631 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 632 CG CD OE1 OE2
REMARK 470 LEU A 634 CG CD1 CD2
REMARK 470 LYS A 637 CG CD CE NZ
REMARK 470 GLN A 638 CG CD OE1 NE2
REMARK 470 GLU A 640 CG CD OE1 OE2
REMARK 470 PHE A 642 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 TRP A 645 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP A 645 CZ3 CH2
REMARK 470 SER A 648 OG
REMARK 470 PHE A 649 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG A 659 CG CD NE CZ NH1 NH2
REMARK 470 PHE A 666 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 TYR A 667 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS A 668 CG CD CE NZ
REMARK 470 LEU A 670 CG CD1 CD2
REMARK 470 ILE A 672 CG1 CG2 CD1
REMARK 470 ARG A 675 CG CD NE CZ NH1 NH2
REMARK 470 ASN A 676 CG OD1 ND2
REMARK 470 LYS A 679 CG CD CE NZ
REMARK 470 ILE A 680 CG1 CG2 CD1
REMARK 470 TYR A 682 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ASP A 697 CG OD1 OD2
REMARK 470 MET A 718 CG SD CE
REMARK 470 LYS A 719 CG CD CE NZ
REMARK 470 TYR A 721 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS A 722 CG CD CE NZ
REMARK 470 ASP A 723 CG OD1 OD2
REMARK 470 LEU A 726 CG CD1 CD2
REMARK 470 LEU A 730 CG CD1 CD2
REMARK 470 HIS A 738 CG ND1 CD2 CE1 NE2
REMARK 470 ASN A 739 CG OD1 ND2
REMARK 470 ILE A 740 CG1 CG2 CD1
REMARK 470 ILE A 741 CG1 CG2 CD1
REMARK 470 GLU A 742 CG CD OE1 OE2
REMARK 470 LEU A 743 CG CD1 CD2
REMARK 470 ARG A 746 CG CD NE CZ NH1 NH2
REMARK 470 TYR A 748 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLN A 753 CG CD OE1 NE2
REMARK 470 MET A 754 CG SD CE
REMARK 470 PHE A 756 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LEU A 770 CG CD1 CD2
REMARK 470 ILE A 792 CG1 CG2 CD1
REMARK 470 LYS A 801 CG CD CE NZ
REMARK 470 GLU A 878 CG CD OE1 OE2
REMARK 470 TRP A 886 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP A 886 CZ3 CH2
REMARK 470 ASP A 887 CG OD1 OD2
REMARK 470 ARG A 899 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 900 CG CD OE1 OE2
REMARK 470 MET A 901 CG SD CE
REMARK 470 LYS A 902 CG CD CE NZ
REMARK 470 ILE A 905 CG1 CG2 CD1
REMARK 470 LEU A 907 CG CD1 CD2
REMARK 470 ASP A 908 CG OD1 OD2
REMARK 470 PHE A 910 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG A 913 CG CD NE CZ NH1 NH2
REMARK 470 SER A 922 OG
REMARK 470 ASP A 923 CG OD1 OD2
REMARK 470 ARG A 924 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 925 CG CD OE1 NE2
REMARK 470 THR A 926 OG1 CG2
REMARK 470 LYS A 927 CG CD CE NZ
REMARK 470 PHE A 940 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 MET A 958 CG SD CE
REMARK 470 TYR A 962 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ARG A 964 CG CD NE CZ NH1 NH2
REMARK 470 ARG A1026 CG CD NE CZ NH1 NH2
REMARK 470 TYR A1064 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 HIS A1069 CG ND1 CD2 CE1 NE2
REMARK 470 ASN A1071 CG OD1 ND2
REMARK 470 PHE A1073 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS A1074 CG CD CE NZ
REMARK 470 ARG A1075 CG CD NE CZ NH1 NH2
REMARK 470 LEU A1076 CG CD1 CD2
REMARK 470 LEU A1080 CG CD1 CD2
REMARK 470 PHE A1082 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU A1093 CG CD OE1 OE2
REMARK 470 LEU A1095 CG CD1 CD2
REMARK 470 VAL A1096 CG1 CG2
REMARK 470 GLU A1097 CG CD OE1 OE2
REMARK 470 GLN A1098 CG CD OE1 NE2
REMARK 470 PHE A1099 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 PHE A1101 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU A1102 CG CD OE1 OE2
REMARK 470 MET A1108 CG SD CE
REMARK 470 GLU A1109 CG CD OE1 OE2
REMARK 470 LEU A1111 CG CD1 CD2
REMARK 470 LEU A1113 CG CD1 CD2
REMARK 470 HIS A1115 CG ND1 CD2 CE1 NE2
REMARK 470 LYS A1119 CG CD CE NZ
REMARK 470 GLN A1125 CG CD OE1 NE2
REMARK 470 ARG A1136 CG CD NE CZ NH1 NH2
REMARK 470 GLU A1139 CG CD OE1 OE2
REMARK 470 LYS A1141 CG CD CE NZ
REMARK 470 ASN A1146 CG OD1 ND2
REMARK 470 LYS A1147 CG CD CE NZ
REMARK 470 LYS A1149 CG CD CE NZ
REMARK 470 LYS A1150 CG CD CE NZ
REMARK 470 ARG A1155 CG CD NE CZ NH1 NH2
REMARK 470 LEU A1163 CG CD1 CD2
REMARK 470 LEU A1166 CG CD1 CD2
REMARK 470 LYS A1170 CG CD CE NZ
REMARK 470 ARG A1178 CG CD NE CZ NH1 NH2
REMARK 470 GLN A1180 CG CD OE1 NE2
REMARK 470 LYS A1213 CG CD CE NZ
REMARK 470 ILE A1235 CG1 CG2 CD1
REMARK 470 LEU A1242 CG CD1 CD2
REMARK 470 TYR A1243 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LEU A1244 CG CD1 CD2
REMARK 470 ARG A1245 CG CD NE CZ NH1 NH2
REMARK 470 PHE A1248 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLN A1251 CG CD OE1 NE2
REMARK 470 TRP A1256 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP A1256 CZ3 CH2
REMARK 470 LEU A1260 CG CD1 CD2
REMARK 470 LEU A1264 CG CD1 CD2
REMARK 470 GLU A1265 CG CD OE1 OE2
REMARK 470 TYR A1267 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ASN A1268 CG OD1 ND2
REMARK 470 THR A1269 OG1 CG2
REMARK 470 PHE A1270 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ILE A1271 CG1 CG2 CD1
REMARK 470 GLU A1273 CG CD OE1 OE2
REMARK 470 ARG A1274 CG CD NE CZ NH1 NH2
REMARK 470 LEU A1279 CG CD1 CD2
REMARK 470 GLN A1280 CG CD OE1 NE2
REMARK 470 LEU A1282 CG CD1 CD2
REMARK 470 THR A1284 OG1 CG2
REMARK 470 GLU A1285 CG CD OE1 OE2
REMARK 470 GLN A1287 CG CD OE1 NE2
REMARK 470 LEU A1290 CG CD1 CD2
REMARK 470 GLU A1299 CG CD OE1 OE2
REMARK 470 ILE A1301 CG1 CG2 CD1
REMARK 470 MET A1303 CG SD CE
REMARK 470 HIS A1304 CG ND1 CD2 CE1 NE2
REMARK 470 ASP A1305 CG OD1 OD2
REMARK 470 ILE A1306 CG1 CG2 CD1
REMARK 470 ILE A1307 CG1 CG2 CD1
REMARK 470 TYR A1330 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LEU A1349 CG CD1 CD2
REMARK 470 GLU A1354 CG CD OE1 OE2
REMARK 470 LYS A1357 CG CD CE NZ
REMARK 470 LEU A1359 CG CD1 CD2
REMARK 470 LYS A1360 CG CD CE NZ
REMARK 470 LYS A1361 CG CD CE NZ
REMARK 470 PHE A1384 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASN A1385 CG OD1 ND2
REMARK 470 GLN A1390 CG CD OE1 NE2
REMARK 470 MET A1392 CG SD CE
REMARK 470 LYS A1404 CG CD CE NZ
REMARK 470 LYS A1407 CG CD CE NZ
REMARK 470 MET A1408 CG SD CE
REMARK 470 SER A1409 OG
REMARK 470 TYR A1411 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS A1412 CG CD CE NZ
REMARK 470 ASP A1413 CG OD1 OD2
REMARK 470 LEU A1415 CG CD1 CD2
REMARK 470 GLU A1416 CG CD OE1 OE2
REMARK 470 ARG A1420 CG CD NE CZ NH1 NH2
REMARK 470 LYS A1422 CG CD CE NZ
REMARK 470 GLN A1426 CG CD OE1 NE2
REMARK 470 TYR A1437 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS A1456 CG CD CE NZ
REMARK 470 LEU A1458 CG CD1 CD2
REMARK 470 HIS A1459 CG ND1 CD2 CE1 NE2
REMARK 470 ARG A1460 CG CD NE CZ NH1 NH2
REMARK 470 SER A1472 OG
REMARK 470 HIS A1477 CG ND1 CD2 CE1 NE2
REMARK 470 SER A1485 OG
REMARK 470 LYS A1489 CG CD CE NZ
REMARK 470 ARG A1497 CG CD NE CZ NH1 NH2
REMARK 470 SER A1502 OG
REMARK 470 LYS A1508 CG CD CE NZ
REMARK 470 PHE A1521 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 MET A1583 CG SD CE
REMARK 470 LYS A1591 CG CD CE NZ
REMARK 470 MET A1592 CG SD CE
REMARK 470 MET A1600 CG SD CE
REMARK 470 ARG A1606 CG CD NE CZ NH1 NH2
REMARK 470 ARG A1608 CG CD NE CZ NH1 NH2
REMARK 470 ASP A1630 CG OD1 OD2
REMARK 470 TRP A1633 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP A1633 CZ3 CH2
REMARK 470 GLU A1640 CG CD OE1 OE2
REMARK 470 THR A1641 OG1 CG2
REMARK 470 LYS A1642 CG CD CE NZ
REMARK 470 MET A1643 CG SD CE
REMARK 470 LEU A1648 CG CD1 CD2
REMARK 470 ILE A1652 CG1 CG2 CD1
REMARK 470 GLN A1654 CG CD OE1 NE2
REMARK 470 SER A1677 OG
REMARK 470 LYS A1689 CG CD CE NZ
REMARK 470 PHE A1698 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 PHE A1699 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 THR A1700 OG1 CG2
REMARK 470 SER A1701 OG
REMARK 470 SER A1706 OG
REMARK 470 LEU A1707 CG CD1 CD2
REMARK 470 ILE A1718 CG1 CG2 CD1
REMARK 470 PHE A1722 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 MET A1724 CG SD CE
REMARK 470 GLN A1725 CG CD OE1 NE2
REMARK 470 GLU A1728 CG CD OE1 OE2
REMARK 470 ARG A1735 CG CD NE CZ NH1 NH2
REMARK 470 GLN A1754 CG CD OE1 NE2
REMARK 470 MET A1762 CG SD CE
REMARK 470 GLU A1803 CG CD OE1 OE2
REMARK 470 ARG A1806 CG CD NE CZ NH1 NH2
REMARK 470 LYS A1807 CG CD CE NZ
REMARK 470 ARG A1811 CG CD NE CZ NH1 NH2
REMARK 470 PHE A1814 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLN A1817 CG CD OE1 NE2
REMARK 470 LYS A1857 CG CD CE NZ
REMARK 470 GLU A1860 CG CD OE1 OE2
REMARK 470 TYR A1873 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS A1875 CG CD CE NZ
REMARK 470 LEU A1877 CG CD1 CD2
REMARK 470 ASP A1878 CG OD1 OD2
REMARK 470 TYR A1881 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ILE A1896 CG1 CG2 CD1
REMARK 470 TYR A1920 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 MET A1927 CG SD CE
REMARK 470 GLN A1932 CG CD OE1 NE2
REMARK 470 GLN A1963 CG CD OE1 NE2
REMARK 470 LYS A1970 CG CD CE NZ
REMARK 470 ASN A1974 CG OD1 ND2
REMARK 470 LEU A1975 CG CD1 CD2
REMARK 470 LEU A1976 CG CD1 CD2
REMARK 470 ILE A1977 CG1 CG2 CD1
REMARK 470 PHE A1978 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU A1979 CG CD OE1 OE2
REMARK 470 ASN A1980 CG OD1 ND2
REMARK 470 MET A1998 CG SD CE
REMARK 470 GLU A1999 CG CD OE1 OE2
REMARK 470 ARG A2000 CG CD NE CZ NH1 NH2
REMARK 470 LYS A2001 CG CD CE NZ
REMARK 470 LYS A2002 CG CD CE NZ
REMARK 470 LYS A2003 CG CD CE NZ
REMARK 470 TYR A2004 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ILE A2005 CG1 CG2 CD1
REMARK 470 GLU A2006 CG CD OE1 OE2
REMARK 470 ILE A2007 CG1 CG2 CD1
REMARK 470 ARG A2008 CG CD NE CZ NH1 NH2
REMARK 470 LYS A2009 CG CD CE NZ
REMARK 470 GLU A2010 CG CD OE1 OE2
REMARK 470 ARG A2012 CG CD NE CZ NH1 NH2
REMARK 470 MET A2025 CG SD CE
REMARK 470 SER A2027 OG
REMARK 470 MET A2040 CG SD CE
REMARK 470 PHE A2043 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 TYR A2052 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 TYR A2054 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ARG A2065 CG CD NE CZ NH1 NH2
REMARK 470 PHE A2066 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG A2067 CG CD NE CZ NH1 NH2
REMARK 470 GLU A2070 CG CD OE1 OE2
REMARK 470 GLN A2071 CG CD OE1 NE2
REMARK 470 ARG A2072 CG CD NE CZ NH1 NH2
REMARK 470 HIS A2077 CG ND1 CD2 CE1 NE2
REMARK 470 ASP A2078 CG OD1 OD2
REMARK 470 ASP A2079 CG OD1 OD2
REMARK 470 VAL A2080 CG1 CG2
REMARK 470 LEU A2081 CG CD1 CD2
REMARK 470 GLU A2082 CG CD OE1 OE2
REMARK 470 LEU A2083 CG CD1 CD2
REMARK 470 GLU A2084 CG CD OE1 OE2
REMARK 470 MET A2085 CG SD CE
REMARK 470 ASP A2086 CG OD1 OD2
REMARK 470 GLU A2087 CG CD OE1 OE2
REMARK 470 LEU A2088 CG CD1 CD2
REMARK 470 ASN A2089 CG OD1 ND2
REMARK 470 ARG A2090 CG CD NE CZ NH1 NH2
REMARK 470 HIS A2091 CG ND1 CD2 CE1 NE2
REMARK 470 GLU A2092 CG CD OE1 OE2
REMARK 470 MET A2094 CG SD CE
REMARK 470 SER A2117 OG
REMARK 470 ARG A2120 CG CD NE CZ NH1 NH2
REMARK 470 ASP A2121 CG OD1 OD2
REMARK 470 LEU A2122 CG CD1 CD2
REMARK 470 TRP A2125 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP A2125 CZ3 CH2
REMARK 470 LYS A2127 CG CD CE NZ
REMARK 470 PHE A2128 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS A2132 CG CD CE NZ
REMARK 470 LEU A2133 CG CD1 CD2
REMARK 470 PHE A2145 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU A2154 CG CD OE1 OE2
REMARK 470 GLU A2155 CG CD OE1 OE2
REMARK 470 PHE A2157 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG A2158 CG CD NE CZ NH1 NH2
REMARK 470 TYR A2160 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS A2162 CG CD CE NZ
REMARK 470 HIS A2163 CG ND1 CD2 CE1 NE2
REMARK 470 TRP A2164 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP A2164 CZ3 CH2
REMARK 470 LEU A2165 CG CD1 CD2
REMARK 470 LEU A2168 CG CD1 CD2
REMARK 470 GLN A2170 CG CD OE1 NE2
REMARK 470 LEU A2171 CG CD1 CD2
REMARK 470 SER A2174 OG
REMARK 470 ASN A2176 CG OD1 ND2
REMARK 470 ASN A2177 CG OD1 ND2
REMARK 470 TRP A2196 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP A2196 CZ3 CH2
REMARK 470 LEU A2199 CG CD1 CD2
REMARK 470 ASP A2208 CG OD1 OD2
REMARK 470 LEU A2211 CG CD1 CD2
REMARK 470 ARG A2214 CG CD NE CZ NH1 NH2
REMARK 470 LYS A2227 CG CD CE NZ
REMARK 470 ILE A2251 CG1 CG2 CD1
REMARK 470 TYR A2253 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ARG A2254 CG CD NE CZ NH1 NH2
REMARK 470 PHE A2257 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS A2263 CG CD CE NZ
REMARK 470 LYS A2268 CG CD CE NZ
REMARK 470 ASN A2270 CG OD1 ND2
REMARK 470 VAL A2272 CG1 CG2
REMARK 470 ILE A2274 CG1 CG2 CD1
REMARK 470 LEU A2276 CG CD1 CD2
REMARK 470 LEU A2277 CG CD1 CD2
REMARK 470 ASP A2284 CG OD1 OD2
REMARK 470 LEU A2285 CG CD1 CD2
REMARK 470 TYR A2288 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ASP A2289 CG OD1 OD2
REMARK 470 GLN A2291 CG CD OE1 NE2
REMARK 470 CYS A2292 SG
REMARK 470 ILE A2294 CG1 CG2 CD1
REMARK 470 GLN A2295 CG CD OE1 NE2
REMARK 470 SER A2297 OG
REMARK 470 TYR A2299 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 PHE A2309 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG A2311 CG CD NE CZ NH1 NH2
REMARK 470 GLU A2321 CG CD OE1 OE2
REMARK 470 ARG A2328 CG CD NE CZ NH1 NH2
REMARK 470 MET A2331 CG SD CE
REMARK 470 ARG A2333 CG CD NE CZ NH1 NH2
REMARK 470 LYS A2334 CG CD CE NZ
REMARK 470 ASN A2335 CG OD1 ND2
REMARK 470 ASN A2354 CG OD1 ND2
REMARK 470 THR A2355 OG1 CG2
REMARK 470 MET A2356 CG SD CE
REMARK 470 GLU A2357 CG CD OE1 OE2
REMARK 470 LYS A2366 CG CD CE NZ
REMARK 470 LYS A2369 CG CD CE NZ
REMARK 470 PHE A2371 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASP A2376 CG OD1 OD2
REMARK 470 ARG A2377 CG CD NE CZ NH1 NH2
REMARK 470 LYS A2394 CG CD CE NZ
REMARK 470 LEU A2396 CG CD1 CD2
REMARK 470 ARG A2404 CG CD NE CZ NH1 NH2
REMARK 470 MET A2408 CG SD CE
REMARK 470 TYR A2412 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS A2416 CG CD CE NZ
REMARK 470 HIS A2426 CG ND1 CD2 CE1 NE2
REMARK 470 ASP A2428 CG OD1 OD2
REMARK 470 GLU A2430 CG CD OE1 OE2
REMARK 470 ARG A2431 CG CD NE CZ NH1 NH2
REMARK 470 GLN A2432 CG CD OE1 NE2
REMARK 470 LEU A2436 CG CD1 CD2
REMARK 470 MET A2442 CG SD CE
REMARK 470 LEU A2446 CG CD1 CD2
REMARK 470 LYS A2447 CG CD CE NZ
REMARK 470 GLU A2471 CG CD OE1 OE2
REMARK 470 MET A2473 CG SD CE
REMARK 470 LYS A2500 CG CD CE NZ
REMARK 470 ASP A2512 CG OD1 OD2
REMARK 470 ARG A2538 CG CD NE CZ NH1 NH2
REMARK 470 MET A2568 CG SD CE
REMARK 470 TYR A2775 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ARG A2776 CG CD NE CZ NH1 NH2
REMARK 470 ILE A2785 CG1 CG2 CD1
REMARK 470 LYS A2786 CG CD CE NZ
REMARK 470 HIS A2787 CG ND1 CD2 CE1 NE2
REMARK 470 ILE A2791 CG1 CG2 CD1
REMARK 470 GLN A2807 CG CD OE1 NE2
REMARK 470 THR A2846 OG1 CG2
REMARK 470 THR A2847 OG1 CG2
REMARK 470 PHE A2848 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 SER A2849 OG
REMARK 470 PHE A2851 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 PHE A2854 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LEU A2869 CG CD1 CD2
REMARK 470 SER A2883 OG
REMARK 470 LEU A2884 CG CD1 CD2
REMARK 470 GLN A2885 CG CD OE1 NE2
REMARK 470 GLN A2886 CG CD OE1 NE2
REMARK 470 ARG A2891 CG CD NE CZ NH1 NH2
REMARK 470 GLU A2894 CG CD OE1 OE2
REMARK 470 ARG A2899 CG CD NE CZ NH1 NH2
REMARK 470 LEU A2900 CG CD1 CD2
REMARK 470 ARG A2909 CG CD NE CZ NH1 NH2
REMARK 470 ARG A2911 CG CD NE CZ NH1 NH2
REMARK 470 LYS A2913 CG CD CE NZ
REMARK 470 GLU A2935 CG CD OE1 OE2
REMARK 470 TYR A2936 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LEU A2939 CG CD1 CD2
REMARK 470 ARG A2940 CG CD NE CZ NH1 NH2
REMARK 470 PHE A2943 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS A2950 CG CD CE NZ
REMARK 470 GLN A2951 CG CD OE1 NE2
REMARK 470 GLN A2954 CG CD OE1 NE2
REMARK 470 LEU A2957 CG CD1 CD2
REMARK 470 LEU A2958 CG CD1 CD2
REMARK 470 GLU A2960 CG CD OE1 OE2
REMARK 470 ARG A2962 CG CD NE CZ NH1 NH2
REMARK 470 ASP A2964 CG OD1 OD2
REMARK 470 TYR A2965 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS A2978 CG CD CE NZ
REMARK 470 GLN A2979 CG CD OE1 NE2
REMARK 470 ASP A2980 CG OD1 OD2
REMARK 470 TRP A2981 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP A2981 CZ3 CH2
REMARK 470 ASP A2983 CG OD1 OD2
REMARK 470 GLU A2985 CG CD OE1 OE2
REMARK 470 THR A2987 OG1 CG2
REMARK 470 GLU A2988 CG CD OE1 OE2
REMARK 470 LYS A3009 CG CD CE NZ
REMARK 470 ILE A3019 CG1 CG2 CD1
REMARK 470 GLU A3022 CG CD OE1 OE2
REMARK 470 LEU A3027 CG CD1 CD2
REMARK 470 LYS A3029 CG CD CE NZ
REMARK 470 TRP A3031 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP A3031 CZ3 CH2
REMARK 470 GLU A3056 CG CD OE1 OE2
REMARK 470 ASP A3058 CG OD1 OD2
REMARK 470 GLN A3059 CG CD OE1 NE2
REMARK 470 HIS A3070 CG ND1 CD2 CE1 NE2
REMARK 470 ARG A3098 CG CD NE CZ NH1 NH2
REMARK 470 LEU A3120 CG CD1 CD2
REMARK 470 HIS A3122 CG ND1 CD2 CE1 NE2
REMARK 470 GLN A3123 CG CD OE1 NE2
REMARK 470 LYS A3128 CG CD CE NZ
REMARK 470 LYS A3147 CG CD CE NZ
REMARK 470 GLN A3148 CG CD OE1 NE2
REMARK 470 ASN A3150 CG OD1 ND2
REMARK 470 LEU A3151 CG CD1 CD2
REMARK 470 SER A3152 OG
REMARK 470 SER A3153 OG
REMARK 470 GLN A3154 CG CD OE1 NE2
REMARK 470 VAL A3155 CG1 CG2
REMARK 470 LYS A3158 CG CD CE NZ
REMARK 470 ARG A3159 CG CD NE CZ NH1 NH2
REMARK 470 LYS A3172 CG CD CE NZ
REMARK 470 MET A3173 CG SD CE
REMARK 470 LYS A3192 CG CD CE NZ
REMARK 470 LYS A3196 CG CD CE NZ
REMARK 470 ILE A3227 CG1 CG2 CD1
REMARK 470 GLN A3249 CG CD OE1 NE2
REMARK 470 ARG A3269 CG CD NE CZ NH1 NH2
REMARK 470 TRP A3276 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP A3276 CZ3 CH2
REMARK 470 ARG A3289 CG CD NE CZ NH1 NH2
REMARK 470 CYS A3293 SG
REMARK 470 GLN A3296 CG CD OE1 NE2
REMARK 470 LEU A3307 CG CD1 CD2
REMARK 470 GLU A3309 CG CD OE1 OE2
REMARK 470 ASN A3311 CG OD1 ND2
REMARK 470 VAL A3312 CG1 CG2
REMARK 470 TYR A3315 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LEU A3316 CG CD1 CD2
REMARK 470 SER A3317 OG
REMARK 470 LYS A3318 CG CD CE NZ
REMARK 470 ASN A3319 CG OD1 ND2
REMARK 470 ILE A3320 CG1 CG2 CD1
REMARK 470 LEU A3321 CG CD1 CD2
REMARK 470 PHE A3323 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG A3324 CG CD NE CZ NH1 NH2
REMARK 470 GLN A3326 CG CD OE1 NE2
REMARK 470 LEU A3348 CG CD1 CD2
REMARK 470 ARG A3358 CG CD NE CZ NH1 NH2
REMARK 470 ILE A3359 CG1 CG2 CD1
REMARK 470 GLU A3394 CG CD OE1 OE2
REMARK 470 TRP A3401 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP A3401 CZ3 CH2
REMARK 470 LYS A3449 CG CD CE NZ
REMARK 470 LYS A3452 CG CD CE NZ
REMARK 470 LYS A3455 CG CD CE NZ
REMARK 470 LEU A3456 CG CD1 CD2
REMARK 470 GLU A3460 CG CD OE1 OE2
REMARK 470 ARG A3462 CG CD NE CZ NH1 NH2
REMARK 470 ARG A3474 CG CD NE CZ NH1 NH2
REMARK 470 LEU A3480 CG CD1 CD2
REMARK 470 CYS A3492 SG
REMARK 470 ASP A3507 CG OD1 OD2
REMARK 470 LYS A3508 CG CD CE NZ
REMARK 470 ASP A3509 CG OD1 OD2
REMARK 470 GLN A3510 CG CD OE1 NE2
REMARK 470 VAL A3514 CG1 CG2
REMARK 470 ILE A3529 CG1 CG2 CD1
REMARK 470 TYR A3531 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 PHE A3542 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS A3543 CG CD CE NZ
REMARK 470 ASP A3544 CG OD1 OD2
REMARK 470 HIS A3549 CG ND1 CD2 CE1 NE2
REMARK 470 LYS A3550 CG CD CE NZ
REMARK 470 LYS A3552 CG CD CE NZ
REMARK 470 GLU A3553 CG CD OE1 OE2
REMARK 470 ARG A3557 CG CD NE CZ NH1 NH2
REMARK 470 GLN A3569 CG CD OE1 NE2
REMARK 470 PHE A3571 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LEU A3575 CG CD1 CD2
REMARK 470 ASP A3576 CG OD1 OD2
REMARK 470 GLN A3577 CG CD OE1 NE2
REMARK 470 LEU A3578 CG CD1 CD2
REMARK 470 ASN A3580 CG OD1 ND2
REMARK 470 GLU A3582 CG CD OE1 OE2
REMARK 470 LEU A3583 CG CD1 CD2
REMARK 470 LYS A3586 CG CD CE NZ
REMARK 470 LYS A3603 CG CD CE NZ
REMARK 470 LYS A3604 CG CD CE NZ
REMARK 470 MET A3609 CG SD CE
REMARK 470 GLU A3611 CG CD OE1 OE2
REMARK 470 ARG A3612 CG CD NE CZ NH1 NH2
REMARK 470 MET A3613 CG SD CE
REMARK 470 LEU A3617 CG CD1 CD2
REMARK 470 ASP A3619 CG OD1 OD2
REMARK 470 LYS A3621 CG CD CE NZ
REMARK 470 PHE A3628 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG A3630 CG CD NE CZ NH1 NH2
REMARK 470 PHE A3636 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU A3639 CG CD OE1 OE2
REMARK 470 LYS A3642 CG CD CE NZ
REMARK 470 ARG A3653 CG CD NE CZ NH1 NH2
REMARK 470 MET A3654 CG SD CE
REMARK 470 LYS A3655 CG CD CE NZ
REMARK 470 LEU A3656 CG CD1 CD2
REMARK 470 PHE A3659 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS A3672 CG CD CE NZ
REMARK 470 MET A3687 CG SD CE
REMARK 470 LYS A3691 CG CD CE NZ
REMARK 470 GLU A3693 CG CD OE1 OE2
REMARK 470 PHE A3694 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LEU A3695 CG CD1 CD2
REMARK 470 ARG A3696 CG CD NE CZ NH1 NH2
REMARK 470 ASN A3697 CG OD1 ND2
REMARK 470 PRO A3702 CG CD
REMARK 470 GLN A3704 CG CD OE1 NE2
REMARK 470 TYR A3705 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ASP A3706 CG OD1 OD2
REMARK 470 ARG A3708 CG CD NE CZ NH1 NH2
REMARK 470 LYS A3710 CG CD CE NZ
REMARK 470 LEU A3712 CG CD1 CD2
REMARK 470 HIS A3716 CG ND1 CD2 CE1 NE2
REMARK 470 GLN A3777 CG CD OE1 NE2
REMARK 470 ASP A3778 CG OD1 OD2
REMARK 470 GLN A3783 CG CD OE1 NE2
REMARK 470 ARG A3784 CG CD NE CZ NH1 NH2
REMARK 470 THR A3797 OG1 CG2
REMARK 470 SER A3798 OG
REMARK 470 ASN A3808 CG OD1 ND2
REMARK 470 MET A3820 CG SD CE
REMARK 470 GLN A3822 CG CD OE1 NE2
REMARK 470 GLU A3823 CG CD OE1 OE2
REMARK 470 GLU A3824 CG CD OE1 OE2
REMARK 470 LYS A3825 CG CD CE NZ
REMARK 470 LYS A3845 CG CD CE NZ
REMARK 470 MET A3846 CG SD CE
REMARK 470 SER A3847 OG
REMARK 470 LYS A3849 CG CD CE NZ
REMARK 470 HIS A3850 CG ND1 CD2 CE1 NE2
REMARK 470 TYR A3855 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 MET A3856 CG SD CE
REMARK 470 MET A3858 CG SD CE
REMARK 470 TYR A3859 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS A3860 CG CD CE NZ
REMARK 470 ARG A3872 CG CD NE CZ NH1 NH2
REMARK 470 ARG A3874 CG CD NE CZ NH1 NH2
REMARK 470 LYS A3884 CG CD CE NZ
REMARK 470 ARG A3923 CG CD NE CZ NH1 NH2
REMARK 470 MET A3929 CG SD CE
REMARK 470 MET A3932 CG SD CE
REMARK 470 ASP A3941 CG OD1 OD2
REMARK 470 GLU A3957 CG CD OE1 OE2
REMARK 470 MET A3959 CG SD CE
REMARK 470 PHE A3961 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG A3965 CG CD NE CZ NH1 NH2
REMARK 470 LEU A3972 CG CD1 CD2
REMARK 470 MET A3974 CG SD CE
REMARK 470 LYS A3975 CG CD CE NZ
REMARK 470 GLU A3976 CG CD OE1 OE2
REMARK 470 MET A3980 CG SD CE
REMARK 470 TYR A3981 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ILE A3983 CG1 CG2 CD1
REMARK 470 MET A3984 CG SD CE
REMARK 470 VAL A3985 CG1 CG2
REMARK 470 ARG A3989 CG CD NE CZ NH1 NH2
REMARK 470 LYS A4007 CG CD CE NZ
REMARK 470 TRP A4013 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP A4013 CZ3 CH2
REMARK 470 LYS A4014 CG CD CE NZ
REMARK 470 LYS A4019 CG CD CE NZ
REMARK 470 ILE A4059 CG1 CG2 CD1
REMARK 470 GLU A4063 CG CD OE1 OE2
REMARK 470 GLU A4069 CG CD OE1 OE2
REMARK 470 LYS A4070 CG CD CE NZ
REMARK 470 PHE A4074 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG A4075 CG CD NE CZ NH1 NH2
REMARK 470 TYR A4077 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ARG A4082 CG CD NE CZ NH1 NH2
REMARK 470 SER A4084 OG
REMARK 470 LYS A4085 CG CD CE NZ
REMARK 470 ASP A4086 CG OD1 OD2
REMARK 470 HIS A4087 CG ND1 CD2 CE1 NE2
REMARK 470 ASN A4088 CG OD1 ND2
REMARK 470 ILE A4089 CG1 CG2 CD1
REMARK 470 ARG A4090 CG CD NE CZ NH1 NH2
REMARK 470 GLN A4092 CG CD OE1 NE2
REMARK 470 MET A4108 CG SD CE
REMARK 470 ILE A4116 CG1 CG2 CD1
REMARK 470 ARG A4119 CG CD NE CZ NH1 NH2
REMARK 470 GLU A4122 CG CD OE1 OE2
REMARK 470 GLU A4125 CG CD OE1 OE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O ALA A 4081 NE2 GLN A 4110 1.57
REMARK 500 O GLY A 3978 N MET A 3980 1.61
REMARK 500 CZ PHE A 995 N SER A 1003 1.69
REMARK 500 OH TYR A 1874 CG PRO A 1885 1.70
REMARK 500 O HIS A 3501 CD1 LEU A 3505 1.79
REMARK 500 CB SER A 882 OG1 THR A 3892 1.79
REMARK 500 CD1 TYR A 2546 CE1 PHE A 2554 1.81
REMARK 500 O ASP A 3509 CB VAL A 3514 1.82
REMARK 500 O ASP A 3576 OG SER A 3579 1.90
REMARK 500 O ALA A 1520 CD1 LEU A 1524 1.90
REMARK 500 O PRO A 3832 CD PRO A 3835 1.90
REMARK 500 CD1 LEU A 3506 O VAL A 3514 1.91
REMARK 500 O ALA A 3461 CD2 PHE A 3465 1.92
REMARK 500 CE2 PHE A 995 N SER A 1003 1.93
REMARK 500 CG2 ILE A 488 CE LYS A 616 1.93
REMARK 500 OE1 GLU A 2564 OD2 ASP A 2571 1.94
REMARK 500 O PHE A 2561 CE MET A 2565 1.95
REMARK 500 O PRO A 1501 N SER A 1506 1.96
REMARK 500 O ALA A 610 CD PRO A 614 1.96
REMARK 500 O LEU A 706 N PHE A 710 1.97
REMARK 500 O PHE A 707 N GLY A 711 1.98
REMARK 500 CE2 PHE A 995 CA SER A 1003 1.99
REMARK 500 CE2 PHE A 995 CB SER A 1003 1.99
REMARK 500 O LYS A 4085 N ILE A 4089 2.01
REMARK 500 OH TYR A 1874 CB PRO A 1885 2.01
REMARK 500 O LEU A 534 N ASP A 538 2.02
REMARK 500 O HIS A 1552 ND1 HIS A 1555 2.04
REMARK 500 O LEU A 3910 OG SER A 3914 2.04
REMARK 500 O SER A 556 OG SER A 559 2.04
REMARK 500 O THR A 658 CD PRO A 661 2.05
REMARK 500 O ASP A 2033 OG SER A 2037 2.06
REMARK 500 O LEU A 706 CB PHE A 710 2.06
REMARK 500 CZ PHE A 995 C GLU A 1002 2.07
REMARK 500 O ALA A 2095 OG1 THR A 2098 2.07
REMARK 500 O ALA A 715 N LYS A 719 2.09
REMARK 500 OH TYR A 3525 O LYS A 3561 2.09
REMARK 500 O VAL A 1294 N LEU A 1298 2.12
REMARK 500 O PHE A 1073 N ARG A 1075 2.12
REMARK 500 O LEU A 1500 N ASP A 1504 2.13
REMARK 500 O PHE A 531 CD1 LEU A 534 2.13
REMARK 500 O PHE A 2231 ND2 ASN A 2234 2.13
REMARK 500 NE2 GLN A 3515 CB ASN A 3551 2.13
REMARK 500 O GLY A 864 NZ LYS A 868 2.14
REMARK 500 CB ASN A 1974 CD2 LEU A 1984 2.14
REMARK 500 O ASP A 1019 N VAL A 1021 2.14
REMARK 500 O GLU A 724 OG SER A 728 2.14
REMARK 500 O PHE A 620 O PHE A 623 2.15
REMARK 500 O ILE A 2952 OG SER A 2955 2.15
REMARK 500 CZ PHE A 3236 OG1 THR A 3268 2.15
REMARK 500 O ARG A 4082 CB ASP A 4086 2.15
REMARK 500
REMARK 500 THIS ENTRY HAS 69 CLOSE CONTACTS
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 LEU A 560 CA - CB - CG ANGL. DEV. = 17.0 DEGREES
REMARK 500 LEU A 564 CA - CB - CG ANGL. DEV. = 13.9 DEGREES
REMARK 500 PRO A 644 C - N - CD ANGL. DEV. = 17.9 DEGREES
REMARK 500 PRO A 644 CA - N - CD ANGL. DEV. = -9.8 DEGREES
REMARK 500 LEU A 752 CA - CB - CG ANGL. DEV. = 14.2 DEGREES
REMARK 500 LEU A 758 CA - CB - CG ANGL. DEV. = 15.1 DEGREES
REMARK 500 PRO A1070 CA - N - CD ANGL. DEV. = -10.5 DEGREES
REMARK 500 LEU A1812 CA - CB - CG ANGL. DEV. = 15.4 DEGREES
REMARK 500 VAL A3119 N - CA - C ANGL. DEV. = -16.5 DEGREES
REMARK 500 PRO A3581 C - N - CA ANGL. DEV. = -9.4 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 CYS A 10 169.55 67.47
REMARK 500 ALA A 28 89.84 -61.16
REMARK 500 LEU A 29 -23.71 64.93
REMARK 500 LEU A 65 -52.27 -140.53
REMARK 500 VAL A 67 -72.93 -84.51
REMARK 500 SER A 72 -145.42 -83.19
REMARK 500 LEU A 73 -141.08 62.01
REMARK 500 GLN A 98 -151.69 -72.69
REMARK 500 SER A 140 22.55 -69.97
REMARK 500 MET A 144 -74.53 -86.08
REMARK 500 ASP A 145 -154.31 62.06
REMARK 500 LEU A 162 -152.06 -71.44
REMARK 500 LYS A 165 -121.33 59.56
REMARK 500 PRO A 167 94.40 -58.73
REMARK 500 MET A 189 44.26 -76.21
REMARK 500 THR A 209 -60.10 165.75
REMARK 500 LEU A 220 -73.68 -88.62
REMARK 500 LEU A 227 4.57 -65.15
REMARK 500 LYS A 236 179.56 58.14
REMARK 500 GLU A 239 1.07 81.66
REMARK 500 ILE A 248 -61.20 -104.83
REMARK 500 ALA A 276 -62.25 -25.68
REMARK 500 TYR A 290 32.18 -94.05
REMARK 500 ALA A 302 45.63 -79.24
REMARK 500 ASN A 305 79.20 -68.51
REMARK 500 GLU A 307 -19.10 57.06
REMARK 500 LEU A 316 -70.84 -71.81
REMARK 500 LYS A 329 22.80 -77.59
REMARK 500 ALA A 331 -168.05 -70.45
REMARK 500 MET A 333 -167.11 -59.20
REMARK 500 HIS A 334 -85.18 64.38
REMARK 500 LYS A 335 -38.52 49.87
REMARK 500 GLU A 358 -66.41 53.58
REMARK 500 SER A 360 -9.26 -58.28
REMARK 500 GLN A 399 -6.40 -50.62
REMARK 500 THR A 400 5.39 -67.43
REMARK 500 GLN A 409 -5.56 63.26
REMARK 500 VAL A 430 -34.26 63.23
REMARK 500 PRO A 433 -4.47 -59.89
REMARK 500 LYS A 471 -65.82 -108.00
REMARK 500 VAL A 474 -27.71 -31.32
REMARK 500 VAL A 496 45.94 -108.10
REMARK 500 ARG A 532 30.82 -78.37
REMARK 500 SER A 559 -80.04 -47.10
REMARK 500 ASN A 561 6.97 -64.78
REMARK 500 TYR A 565 9.54 -53.54
REMARK 500 ASP A 566 22.31 -74.12
REMARK 500 GLU A 567 6.50 51.48
REMARK 500 ILE A 585 -148.03 -121.41
REMARK 500 PRO A 608 4.95 -66.83
REMARK 500
REMARK 500 THIS ENTRY HAS 425 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: EMD-8752 RELATED DB: EMDB
REMARK 900 RELATED ID: EMD-8751 RELATED DB: EMDB
REMARK 900 CRYO-EM STRUCTURE OF DNAPKCS
DBREF 5W1R A 1 4128 UNP P78527 PRKDC_HUMAN 1 4128
SEQRES 1 A 4128 MET ALA GLY SER GLY ALA GLY VAL ARG CYS SER LEU LEU
SEQRES 2 A 4128 ARG LEU GLN GLU THR LEU SER ALA ALA ASP ARG CYS GLY
SEQRES 3 A 4128 ALA ALA LEU ALA GLY HIS GLN LEU ILE ARG GLY LEU GLY
SEQRES 4 A 4128 GLN GLU CYS VAL LEU SER SER SER PRO ALA VAL LEU ALA
SEQRES 5 A 4128 LEU GLN THR SER LEU VAL PHE SER ARG ASP PHE GLY LEU
SEQRES 6 A 4128 LEU VAL PHE VAL ARG LYS SER LEU ASN SER ILE GLU PHE
SEQRES 7 A 4128 ARG GLU CYS ARG GLU GLU ILE LEU LYS PHE LEU CYS ILE
SEQRES 8 A 4128 PHE LEU GLU LYS MET GLY GLN LYS ILE ALA PRO TYR SER
SEQRES 9 A 4128 VAL GLU ILE LYS ASN THR CYS THR SER VAL TYR THR LYS
SEQRES 10 A 4128 ASP ARG ALA ALA LYS CYS LYS ILE PRO ALA LEU ASP LEU
SEQRES 11 A 4128 LEU ILE LYS LEU LEU GLN THR PHE ARG SER SER ARG LEU
SEQRES 12 A 4128 MET ASP GLU PHE LYS ILE GLY GLU LEU PHE SER LYS PHE
SEQRES 13 A 4128 TYR GLY GLU LEU ALA LEU LYS LYS LYS ILE PRO ASP THR
SEQRES 14 A 4128 VAL LEU GLU LYS VAL TYR GLU LEU LEU GLY LEU LEU GLY
SEQRES 15 A 4128 GLU VAL HIS PRO SER GLU MET ILE ASN ASN ALA GLU ASN
SEQRES 16 A 4128 LEU PHE ARG ALA PHE LEU GLY GLU LEU LYS THR GLN MET
SEQRES 17 A 4128 THR SER ALA VAL ARG GLU PRO LYS LEU PRO VAL LEU ALA
SEQRES 18 A 4128 GLY CYS LEU LYS GLY LEU SER SER LEU LEU CYS ASN PHE
SEQRES 19 A 4128 THR LYS SER MET GLU GLU ASP PRO GLN THR SER ARG GLU
SEQRES 20 A 4128 ILE PHE ASN PHE VAL LEU LYS ALA ILE ARG PRO GLN ILE
SEQRES 21 A 4128 ASP LEU LYS ARG TYR ALA VAL PRO SER ALA GLY LEU ARG
SEQRES 22 A 4128 LEU PHE ALA LEU HIS ALA SER GLN PHE SER THR CYS LEU
SEQRES 23 A 4128 LEU ASP ASN TYR VAL SER LEU PHE GLU VAL LEU LEU LYS
SEQRES 24 A 4128 TRP CYS ALA HIS THR ASN VAL GLU LEU LYS LYS ALA ALA
SEQRES 25 A 4128 LEU SER ALA LEU GLU SER PHE LEU LYS GLN VAL SER ASN
SEQRES 26 A 4128 MET VAL ALA LYS ASN ALA GLU MET HIS LYS ASN LYS LEU
SEQRES 27 A 4128 GLN TYR PHE MET GLU GLN PHE TYR GLY ILE ILE ARG ASN
SEQRES 28 A 4128 VAL ASP SER ASN ASN LYS GLU LEU SER ILE ALA ILE ARG
SEQRES 29 A 4128 GLY TYR GLY LEU PHE ALA GLY PRO CYS LYS VAL ILE ASN
SEQRES 30 A 4128 ALA LYS ASP VAL ASP PHE MET TYR VAL GLU LEU ILE GLN
SEQRES 31 A 4128 ARG CYS LYS GLN MET PHE LEU THR GLN THR ASP THR GLY
SEQRES 32 A 4128 ASP ASP ARG VAL TYR GLN MET PRO SER PHE LEU GLN SER
SEQRES 33 A 4128 VAL ALA SER VAL LEU LEU TYR LEU ASP THR VAL PRO GLU
SEQRES 34 A 4128 VAL TYR THR PRO VAL LEU GLU HIS LEU VAL VAL MET GLN
SEQRES 35 A 4128 ILE ASP SER PHE PRO GLN TYR SER PRO LYS MET GLN LEU
SEQRES 36 A 4128 VAL CYS CYS ARG ALA ILE VAL LYS VAL PHE LEU ALA LEU
SEQRES 37 A 4128 ALA ALA LYS GLY PRO VAL LEU ARG ASN CYS ILE SER THR
SEQRES 38 A 4128 VAL VAL HIS GLN GLY LEU ILE ARG ILE CYS SER LYS PRO
SEQRES 39 A 4128 VAL VAL LEU PRO LYS GLY PRO GLU SER GLU SER GLU ASP
SEQRES 40 A 4128 HIS ARG ALA SER GLY GLU VAL ARG THR GLY LYS TRP LYS
SEQRES 41 A 4128 VAL PRO THR TYR LYS ASP TYR VAL ASP LEU PHE ARG HIS
SEQRES 42 A 4128 LEU LEU SER SER ASP GLN MET MET ASP SER ILE LEU ALA
SEQRES 43 A 4128 ASP GLU ALA PHE PHE SER VAL ASN SER SER SER GLU SER
SEQRES 44 A 4128 LEU ASN HIS LEU LEU TYR ASP GLU PHE VAL LYS SER VAL
SEQRES 45 A 4128 LEU LYS ILE VAL GLU LYS LEU ASP LEU THR LEU GLU ILE
SEQRES 46 A 4128 GLN THR VAL GLY GLU GLN GLU ASN GLY ASP GLU ALA PRO
SEQRES 47 A 4128 GLY VAL TRP MET ILE PRO THR SER ASP PRO ALA ALA ASN
SEQRES 48 A 4128 LEU HIS PRO ALA LYS PRO LYS ASP PHE SER ALA PHE ILE
SEQRES 49 A 4128 ASN LEU VAL GLU PHE CYS ARG GLU ILE LEU PRO GLU LYS
SEQRES 50 A 4128 GLN ALA GLU PHE PHE GLU PRO TRP VAL TYR SER PHE SER
SEQRES 51 A 4128 TYR GLU LEU ILE LEU GLN SER THR ARG LEU PRO LEU ILE
SEQRES 52 A 4128 SER GLY PHE TYR LYS LEU LEU SER ILE THR VAL ARG ASN
SEQRES 53 A 4128 ALA LYS LYS ILE LYS TYR PHE GLU GLY VAL SER PRO LYS
SEQRES 54 A 4128 SER LEU LYS HIS SER PRO GLU ASP PRO GLU LYS TYR SER
SEQRES 55 A 4128 CYS PHE ALA LEU PHE VAL LYS PHE GLY LYS GLU VAL ALA
SEQRES 56 A 4128 VAL LYS MET LYS GLN TYR LYS ASP GLU LEU LEU ALA SER
SEQRES 57 A 4128 CYS LEU THR PHE LEU LEU SER LEU PRO HIS ASN ILE ILE
SEQRES 58 A 4128 GLU LEU ASP VAL ARG ALA TYR VAL PRO ALA LEU GLN MET
SEQRES 59 A 4128 ALA PHE LYS LEU GLY LEU SER TYR THR PRO LEU ALA GLU
SEQRES 60 A 4128 VAL GLY LEU ASN ALA LEU GLU GLU TRP SER ILE TYR ILE
SEQRES 61 A 4128 ASP ARG HIS VAL MET GLN PRO TYR TYR LYS ASP ILE LEU
SEQRES 62 A 4128 PRO CYS LEU ASP GLY TYR LEU LYS THR SER ALA LEU SER
SEQRES 63 A 4128 ASP GLU THR LYS ASN ASN TRP GLU VAL SER ALA LEU SER
SEQRES 64 A 4128 ARG ALA ALA GLN LYS GLY PHE ASN LYS VAL VAL LEU LYS
SEQRES 65 A 4128 HIS LEU LYS LYS THR LYS ASN LEU SER SER ASN GLU ALA
SEQRES 66 A 4128 ILE SER LEU GLU GLU ILE ARG ILE ARG VAL VAL GLN MET
SEQRES 67 A 4128 LEU GLY SER LEU GLY GLY GLN ILE ASN LYS ASN LEU LEU
SEQRES 68 A 4128 THR VAL THR SER SER ASP GLU MET MET LYS SER TYR VAL
SEQRES 69 A 4128 ALA TRP ASP ARG GLU LYS ARG LEU SER PHE ALA VAL PRO
SEQRES 70 A 4128 PHE ARG GLU MET LYS PRO VAL ILE PHE LEU ASP VAL PHE
SEQRES 71 A 4128 LEU PRO ARG VAL THR GLU LEU ALA LEU THR ALA SER ASP
SEQRES 72 A 4128 ARG GLN THR LYS VAL ALA ALA CYS GLU LEU LEU HIS SER
SEQRES 73 A 4128 MET VAL MET PHE MET LEU GLY LYS ALA THR GLN MET PRO
SEQRES 74 A 4128 GLU GLY GLY GLN GLY ALA PRO PRO MET TYR GLN LEU TYR
SEQRES 75 A 4128 LYS ARG THR PHE PRO VAL LEU LEU ARG LEU ALA CYS ASP
SEQRES 76 A 4128 VAL ASP GLN VAL THR ARG GLN LEU TYR GLU PRO LEU VAL
SEQRES 77 A 4128 MET GLN LEU ILE HIS TRP PHE THR ASN ASN LYS LYS PHE
SEQRES 78 A 4128 GLU SER GLN ASP THR VAL ALA LEU LEU GLU ALA ILE LEU
SEQRES 79 A 4128 ASP GLY ILE VAL ASP PRO VAL ASP SER THR LEU ARG ASP
SEQRES 80 A 4128 PHE CYS GLY ARG CYS ILE ARG GLU PHE LEU LYS TRP SER
SEQRES 81 A 4128 ILE LYS GLN ILE THR PRO GLN GLN GLN GLU LYS SER PRO
SEQRES 82 A 4128 VAL ASN THR LYS SER LEU PHE LYS ARG LEU TYR SER LEU
SEQRES 83 A 4128 ALA LEU HIS PRO ASN ALA PHE LYS ARG LEU GLY ALA SER
SEQRES 84 A 4128 LEU ALA PHE ASN ASN ILE TYR ARG GLU PHE ARG GLU GLU
SEQRES 85 A 4128 GLU SER LEU VAL GLU GLN PHE VAL PHE GLU ALA LEU VAL
SEQRES 86 A 4128 ILE TYR MET GLU SER LEU ALA LEU ALA HIS ALA ASP GLU
SEQRES 87 A 4128 LYS SER LEU GLY THR ILE GLN GLN CYS CYS ASP ALA ILE
SEQRES 88 A 4128 ASP HIS LEU CYS ARG ILE ILE GLU LYS LYS HIS VAL SER
SEQRES 89 A 4128 LEU ASN LYS ALA LYS LYS ARG ARG LEU PRO ARG GLY PHE
SEQRES 90 A 4128 PRO PRO SER ALA SER LEU CYS LEU LEU ASP LEU VAL LYS
SEQRES 91 A 4128 TRP LEU LEU ALA HIS CYS GLY ARG PRO GLN THR GLU CYS
SEQRES 92 A 4128 ARG HIS LYS SER ILE GLU LEU PHE TYR LYS PHE VAL PRO
SEQRES 93 A 4128 LEU LEU PRO GLY ASN ARG SER PRO ASN LEU TRP LEU LYS
SEQRES 94 A 4128 ASP VAL LEU LYS GLU GLU GLY VAL SER PHE LEU ILE ASN
SEQRES 95 A 4128 THR PHE GLU GLY GLY GLY CYS GLY GLN PRO SER GLY ILE
SEQRES 96 A 4128 LEU ALA GLN PRO THR LEU LEU TYR LEU ARG GLY PRO PHE
SEQRES 97 A 4128 SER LEU GLN ALA THR LEU CYS TRP LEU ASP LEU LEU LEU
SEQRES 98 A 4128 ALA ALA LEU GLU CYS TYR ASN THR PHE ILE GLY GLU ARG
SEQRES 99 A 4128 THR VAL GLY ALA LEU GLN VAL LEU GLY THR GLU ALA GLN
SEQRES 100 A 4128 SER SER LEU LEU LYS ALA VAL ALA PHE PHE LEU GLU SER
SEQRES 101 A 4128 ILE ALA MET HIS ASP ILE ILE ALA ALA GLU LYS CYS PHE
SEQRES 102 A 4128 GLY THR GLY ALA ALA GLY ASN ARG THR SER PRO GLN GLU
SEQRES 103 A 4128 GLY GLU ARG TYR ASN TYR SER LYS CYS THR VAL VAL VAL
SEQRES 104 A 4128 ARG ILE MET GLU PHE THR THR THR LEU LEU ASN THR SER
SEQRES 105 A 4128 PRO GLU GLY TRP LYS LEU LEU LYS LYS ASP LEU CYS ASN
SEQRES 106 A 4128 THR HIS LEU MET ARG VAL LEU VAL GLN THR LEU CYS GLU
SEQRES 107 A 4128 PRO ALA SER ILE GLY PHE ASN ILE GLY ASP VAL GLN VAL
SEQRES 108 A 4128 MET ALA HIS LEU PRO ASP VAL CYS VAL ASN LEU MET LYS
SEQRES 109 A 4128 ALA LEU LYS MET SER PRO TYR LYS ASP ILE LEU GLU THR
SEQRES 110 A 4128 HIS LEU ARG GLU LYS ILE THR ALA GLN SER ILE GLU GLU
SEQRES 111 A 4128 LEU CYS ALA VAL ASN LEU TYR GLY PRO ASP ALA GLN VAL
SEQRES 112 A 4128 ASP ARG SER ARG LEU ALA ALA VAL VAL SER ALA CYS LYS
SEQRES 113 A 4128 GLN LEU HIS ARG ALA GLY LEU LEU HIS ASN ILE LEU PRO
SEQRES 114 A 4128 SER GLN SER THR ASP LEU HIS HIS SER VAL GLY THR GLU
SEQRES 115 A 4128 LEU LEU SER LEU VAL TYR LYS GLY ILE ALA PRO GLY ASP
SEQRES 116 A 4128 GLU ARG GLN CYS LEU PRO SER LEU ASP LEU SER CYS LYS
SEQRES 117 A 4128 GLN LEU ALA SER GLY LEU LEU GLU LEU ALA PHE ALA PHE
SEQRES 118 A 4128 GLY GLY LEU CYS GLU ARG LEU VAL SER LEU LEU LEU ASN
SEQRES 119 A 4128 PRO ALA VAL LEU SER THR ALA SER LEU GLY SER SER GLN
SEQRES 120 A 4128 GLY SER VAL ILE HIS PHE SER HIS GLY GLU TYR PHE TYR
SEQRES 121 A 4128 SER LEU PHE SER GLU THR ILE ASN THR GLU LEU LEU LYS
SEQRES 122 A 4128 ASN LEU ASP LEU ALA VAL LEU GLU LEU MET GLN SER SER
SEQRES 123 A 4128 VAL ASP ASN THR LYS MET VAL SER ALA VAL LEU ASN GLY
SEQRES 124 A 4128 MET LEU ASP GLN SER PHE ARG GLU ARG ALA ASN GLN LYS
SEQRES 125 A 4128 HIS GLN GLY LEU LYS LEU ALA THR THR ILE LEU GLN HIS
SEQRES 126 A 4128 TRP LYS LYS CYS ASP SER TRP TRP ALA LYS ASP SER PRO
SEQRES 127 A 4128 LEU GLU THR LYS MET ALA VAL LEU ALA LEU LEU ALA LYS
SEQRES 128 A 4128 ILE LEU GLN ILE ASP SER SER VAL SER PHE ASN THR SER
SEQRES 129 A 4128 HIS GLY SER PHE PRO GLU VAL PHE THR THR TYR ILE SER
SEQRES 130 A 4128 LEU LEU ALA ASP THR LYS LEU ASP LEU HIS LEU LYS GLY
SEQRES 131 A 4128 GLN ALA VAL THR LEU LEU PRO PHE PHE THR SER LEU THR
SEQRES 132 A 4128 GLY GLY SER LEU GLU GLU LEU ARG ARG VAL LEU GLU GLN
SEQRES 133 A 4128 LEU ILE VAL ALA HIS PHE PRO MET GLN SER ARG GLU PHE
SEQRES 134 A 4128 PRO PRO GLY THR PRO ARG PHE ASN ASN TYR VAL ASP CYS
SEQRES 135 A 4128 MET LYS LYS PHE LEU ASP ALA LEU GLU LEU SER GLN SER
SEQRES 136 A 4128 PRO MET LEU LEU GLU LEU MET THR GLU VAL LEU CYS ARG
SEQRES 137 A 4128 GLU GLN GLN HIS VAL MET GLU GLU LEU PHE GLN SER SER
SEQRES 138 A 4128 PHE ARG ARG ILE ALA ARG ARG GLY SER CYS VAL THR GLN
SEQRES 139 A 4128 VAL GLY LEU LEU GLU SER VAL TYR GLU MET PHE ARG LYS
SEQRES 140 A 4128 ASP ASP PRO ARG LEU SER PHE THR ARG GLN SER PHE VAL
SEQRES 141 A 4128 ASP ARG SER LEU LEU THR LEU LEU TRP HIS CYS SER LEU
SEQRES 142 A 4128 ASP ALA LEU ARG GLU PHE PHE SER THR ILE VAL VAL ASP
SEQRES 143 A 4128 ALA ILE ASP VAL LEU LYS SER ARG PHE THR LYS LEU ASN
SEQRES 144 A 4128 GLU SER THR PHE ASP THR GLN ILE THR LYS LYS MET GLY
SEQRES 145 A 4128 TYR TYR LYS ILE LEU ASP VAL MET TYR SER ARG LEU PRO
SEQRES 146 A 4128 LYS ASP ASP VAL HIS ALA LYS GLU SER LYS ILE ASN GLN
SEQRES 147 A 4128 VAL PHE HIS GLY SER CYS ILE THR GLU GLY ASN GLU LEU
SEQRES 148 A 4128 THR LYS THR LEU ILE LYS LEU CYS TYR ASP ALA PHE THR
SEQRES 149 A 4128 GLU ASN MET ALA GLY GLU ASN GLN LEU LEU GLU ARG ARG
SEQRES 150 A 4128 ARG LEU TYR HIS CYS ALA ALA TYR ASN CYS ALA ILE SER
SEQRES 151 A 4128 VAL ILE CYS CYS VAL PHE ASN GLU LEU LYS PHE TYR GLN
SEQRES 152 A 4128 GLY PHE LEU PHE SER GLU LYS PRO GLU LYS ASN LEU LEU
SEQRES 153 A 4128 ILE PHE GLU ASN LEU ILE ASP LEU LYS ARG ARG TYR ASN
SEQRES 154 A 4128 PHE PRO VAL GLU VAL GLU VAL PRO MET GLU ARG LYS LYS
SEQRES 155 A 4128 LYS TYR ILE GLU ILE ARG LYS GLU ALA ARG GLU ALA ALA
SEQRES 156 A 4128 ASN GLY ASP SER ASP GLY PRO SER TYR MET SER SER LEU
SEQRES 157 A 4128 SER TYR LEU ALA ASP SER THR LEU SER GLU GLU MET SER
SEQRES 158 A 4128 GLN PHE ASP PHE SER THR GLY VAL GLN SER TYR SER TYR
SEQRES 159 A 4128 SER SER GLN ASP PRO ARG PRO ALA THR GLY ARG PHE ARG
SEQRES 160 A 4128 ARG ARG GLU GLN ARG ASP PRO THR VAL HIS ASP ASP VAL
SEQRES 161 A 4128 LEU GLU LEU GLU MET ASP GLU LEU ASN ARG HIS GLU CYS
SEQRES 162 A 4128 MET ALA PRO LEU THR ALA LEU VAL LYS HIS MET HIS ARG
SEQRES 163 A 4128 SER LEU GLY PRO PRO GLN GLY GLU GLU ASP SER VAL PRO
SEQRES 164 A 4128 ARG ASP LEU PRO SER TRP MET LYS PHE LEU HIS GLY LYS
SEQRES 165 A 4128 LEU GLY ASN PRO ILE VAL PRO LEU ASN ILE ARG LEU PHE
SEQRES 166 A 4128 LEU ALA LYS LEU VAL ILE ASN THR GLU GLU VAL PHE ARG
SEQRES 167 A 4128 PRO TYR ALA LYS HIS TRP LEU SER PRO LEU LEU GLN LEU
SEQRES 168 A 4128 ALA ALA SER GLU ASN ASN GLY GLY GLU GLY ILE HIS TYR
SEQRES 169 A 4128 MET VAL VAL GLU ILE VAL ALA THR ILE LEU SER TRP THR
SEQRES 170 A 4128 GLY LEU ALA THR PRO THR GLY VAL PRO LYS ASP GLU VAL
SEQRES 171 A 4128 LEU ALA ASN ARG LEU LEU ASN PHE LEU MET LYS HIS VAL
SEQRES 172 A 4128 PHE HIS PRO LYS ARG ALA VAL PHE ARG HIS ASN LEU GLU
SEQRES 173 A 4128 ILE ILE LYS THR LEU VAL GLU CYS TRP LYS ASP CYS LEU
SEQRES 174 A 4128 SER ILE PRO TYR ARG LEU ILE PHE GLU LYS PHE SER GLY
SEQRES 175 A 4128 LYS ASP PRO ASN SER LYS ASP ASN SER VAL GLY ILE GLN
SEQRES 176 A 4128 LEU LEU GLY ILE VAL MET ALA ASN ASP LEU PRO PRO TYR
SEQRES 177 A 4128 ASP PRO GLN CYS GLY ILE GLN SER SER GLU TYR PHE GLN
SEQRES 178 A 4128 ALA LEU VAL ASN ASN MET SER PHE VAL ARG TYR LYS GLU
SEQRES 179 A 4128 VAL TYR ALA ALA ALA ALA GLU VAL LEU GLY LEU ILE LEU
SEQRES 180 A 4128 ARG TYR VAL MET GLU ARG LYS ASN ILE LEU GLU GLU SER
SEQRES 181 A 4128 LEU CYS GLU LEU VAL ALA LYS GLN LEU LYS GLN HIS GLN
SEQRES 182 A 4128 ASN THR MET GLU ASP LYS PHE ILE VAL CYS LEU ASN LYS
SEQRES 183 A 4128 VAL THR LYS SER PHE PRO PRO LEU ALA ASP ARG PHE MET
SEQRES 184 A 4128 ASN ALA VAL PHE PHE LEU LEU PRO LYS PHE HIS GLY VAL
SEQRES 185 A 4128 LEU LYS THR LEU CYS LEU GLU VAL VAL LEU CYS ARG VAL
SEQRES 186 A 4128 GLU GLY MET THR GLU LEU TYR PHE GLN LEU LYS SER LYS
SEQRES 187 A 4128 ASP PHE VAL GLN VAL MET ARG HIS ARG ASP ASP GLU ARG
SEQRES 188 A 4128 GLN LYS VAL CYS LEU ASP ILE ILE TYR LYS MET MET PRO
SEQRES 189 A 4128 LYS LEU LYS PRO VAL GLU LEU ARG GLU LEU LEU ASN PRO
SEQRES 190 A 4128 VAL VAL GLU PHE VAL SER HIS PRO SER THR THR CYS ARG
SEQRES 191 A 4128 GLU GLN MET TYR ASN ILE LEU MET TRP ILE HIS ASP ASN
SEQRES 192 A 4128 TYR ARG ASP PRO GLU SER GLU THR ASP ASN ASP SER GLN
SEQRES 193 A 4128 GLU ILE PHE LYS LEU ALA LYS ASP VAL LEU ILE GLN GLY
SEQRES 194 A 4128 LEU ILE ASP GLU ASN PRO GLY LEU GLN LEU ILE ILE ARG
SEQRES 195 A 4128 ASN PHE TRP SER HIS GLU THR ARG LEU PRO SER ASN THR
SEQRES 196 A 4128 LEU ASP ARG LEU LEU ALA LEU ASN SER LEU TYR SER PRO
SEQRES 197 A 4128 LYS ILE GLU VAL HIS PHE LEU SER LEU ALA THR ASN PHE
SEQRES 198 A 4128 LEU LEU GLU MET THR SER MET SER PRO ASP TYR PRO ASN
SEQRES 199 A 4128 PRO MET PHE GLU HIS PRO LEU SER GLU CYS GLU PHE GLN
SEQRES 200 A 4128 GLU TYR THR ILE ASP SER ASP TRP ARG PHE ARG SER THR
SEQRES 201 A 4128 VAL LEU THR PRO MET PHE VAL GLU THR GLN ALA SER GLN
SEQRES 202 A 4128 GLY THR LEU GLN THR ARG THR GLN GLU GLY SER LEU SER
SEQRES 203 A 4128 ALA ARG TRP PRO VAL ALA GLY GLN ILE ARG ALA THR GLN
SEQRES 204 A 4128 GLN GLN HIS ASP PHE THR LEU THR GLN THR ALA ASP GLY
SEQRES 205 A 4128 ARG SER SER PHE ASP TRP LEU THR GLY SER SER THR ASP
SEQRES 206 A 4128 PRO LEU VAL ASP HIS THR SER PRO SER SER ASP SER LEU
SEQRES 207 A 4128 LEU PHE ALA HIS LYS ARG SER GLU ARG LEU GLN ARG ALA
SEQRES 208 A 4128 PRO LEU LYS SER VAL GLY PRO ASP PHE GLY LYS LYS ARG
SEQRES 209 A 4128 LEU GLY LEU PRO GLY ASP GLU VAL ASP ASN LYS VAL LYS
SEQRES 210 A 4128 GLY ALA ALA GLY ARG THR ASP LEU LEU ARG LEU ARG ARG
SEQRES 211 A 4128 ARG PHE MET ARG ASP GLN GLU LYS LEU SER LEU MET TYR
SEQRES 212 A 4128 ALA ARG LYS GLY VAL ALA GLU GLN LYS ARG GLU LYS GLU
SEQRES 213 A 4128 ILE LYS SER GLU LEU LYS MET LYS GLN ASP ALA GLN VAL
SEQRES 214 A 4128 VAL LEU TYR ARG SER TYR ARG HIS GLY ASP LEU PRO ASP
SEQRES 215 A 4128 ILE GLN ILE LYS HIS SER SER LEU ILE THR PRO LEU GLN
SEQRES 216 A 4128 ALA VAL ALA GLN ARG ASP PRO ILE ILE ALA LYS GLN LEU
SEQRES 217 A 4128 PHE SER SER LEU PHE SER GLY ILE LEU LYS GLU MET ASP
SEQRES 218 A 4128 LYS PHE LYS THR LEU SER GLU LYS ASN ASN ILE THR GLN
SEQRES 219 A 4128 LYS LEU LEU GLN ASP PHE ASN ARG PHE LEU ASN THR THR
SEQRES 220 A 4128 PHE SER PHE PHE PRO PRO PHE VAL SER CYS ILE GLN ASP
SEQRES 221 A 4128 ILE SER CYS GLN HIS ALA ALA LEU LEU SER LEU ASP PRO
SEQRES 222 A 4128 ALA ALA VAL SER ALA GLY CYS LEU ALA SER LEU GLN GLN
SEQRES 223 A 4128 PRO VAL GLY ILE ARG LEU LEU GLU GLU ALA LEU LEU ARG
SEQRES 224 A 4128 LEU LEU PRO ALA GLU LEU PRO ALA LYS ARG VAL ARG GLY
SEQRES 225 A 4128 LYS ALA ARG LEU PRO PRO ASP VAL LEU ARG TRP VAL GLU
SEQRES 226 A 4128 LEU ALA LYS LEU TYR ARG SER ILE GLY GLU TYR ASP VAL
SEQRES 227 A 4128 LEU ARG GLY ILE PHE THR SER GLU ILE GLY THR LYS GLN
SEQRES 228 A 4128 ILE THR GLN SER ALA LEU LEU ALA GLU ALA ARG SER ASP
SEQRES 229 A 4128 TYR SER GLU ALA ALA LYS GLN TYR ASP GLU ALA LEU ASN
SEQRES 230 A 4128 LYS GLN ASP TRP VAL ASP GLY GLU PRO THR GLU ALA GLU
SEQRES 231 A 4128 LYS ASP PHE TRP GLU LEU ALA SER LEU ASP CYS TYR ASN
SEQRES 232 A 4128 HIS LEU ALA GLU TRP LYS SER LEU GLU TYR CYS SER THR
SEQRES 233 A 4128 ALA SER ILE ASP SER GLU ASN PRO PRO ASP LEU ASN LYS
SEQRES 234 A 4128 ILE TRP SER GLU PRO PHE TYR GLN GLU THR TYR LEU PRO
SEQRES 235 A 4128 TYR MET ILE ARG SER LYS LEU LYS LEU LEU LEU GLN GLY
SEQRES 236 A 4128 GLU ALA ASP GLN SER LEU LEU THR PHE ILE ASP LYS ALA
SEQRES 237 A 4128 MET HIS GLY GLU LEU GLN LYS ALA ILE LEU GLU LEU HIS
SEQRES 238 A 4128 TYR SER GLN GLU LEU SER LEU LEU TYR LEU LEU GLN ASP
SEQRES 239 A 4128 ASP VAL ASP ARG ALA LYS TYR TYR ILE GLN ASN GLY ILE
SEQRES 240 A 4128 GLN SER PHE MET GLN ASN TYR SER SER ILE ASP VAL LEU
SEQRES 241 A 4128 LEU HIS GLN SER ARG LEU THR LYS LEU GLN SER VAL GLN
SEQRES 242 A 4128 ALA LEU THR GLU ILE GLN GLU PHE ILE SER PHE ILE SER
SEQRES 243 A 4128 LYS GLN GLY ASN LEU SER SER GLN VAL PRO LEU LYS ARG
SEQRES 244 A 4128 LEU LEU ASN THR TRP THR ASN ARG TYR PRO ASP ALA LYS
SEQRES 245 A 4128 MET ASP PRO MET ASN ILE TRP ASP ASP ILE ILE THR ASN
SEQRES 246 A 4128 ARG CYS PHE PHE LEU SER LYS ILE GLU GLU LYS LEU THR
SEQRES 247 A 4128 PRO LEU PRO GLU ASP ASN SER MET ASN VAL ASP GLN ASP
SEQRES 248 A 4128 GLY ASP PRO SER ASP ARG MET GLU VAL GLN GLU GLN GLU
SEQRES 249 A 4128 GLU ASP ILE SER SER LEU ILE ARG SER CYS LYS PHE SER
SEQRES 250 A 4128 MET LYS MET LYS MET ILE ASP SER ALA ARG LYS GLN ASN
SEQRES 251 A 4128 ASN PHE SER LEU ALA MET LYS LEU LEU LYS GLU LEU HIS
SEQRES 252 A 4128 LYS GLU SER LYS THR ARG ASP ASP TRP LEU VAL SER TRP
SEQRES 253 A 4128 VAL GLN SER TYR CYS ARG LEU SER HIS CYS ARG SER ARG
SEQRES 254 A 4128 SER GLN GLY CYS SER GLU GLN VAL LEU THR VAL LEU LYS
SEQRES 255 A 4128 THR VAL SER LEU LEU ASP GLU ASN ASN VAL SER SER TYR
SEQRES 256 A 4128 LEU SER LYS ASN ILE LEU ALA PHE ARG ASP GLN ASN ILE
SEQRES 257 A 4128 LEU LEU GLY THR THR TYR ARG ILE ILE ALA ASN ALA LEU
SEQRES 258 A 4128 SER SER GLU PRO ALA CYS LEU ALA GLU ILE GLU GLU ASP
SEQRES 259 A 4128 LYS ALA ARG ARG ILE LEU GLU LEU SER GLY SER SER SER
SEQRES 260 A 4128 GLU ASP SER GLU LYS VAL ILE ALA GLY LEU TYR GLN ARG
SEQRES 261 A 4128 ALA PHE GLN HIS LEU SER GLU ALA VAL GLN ALA ALA GLU
SEQRES 262 A 4128 GLU GLU ALA GLN PRO PRO SER TRP SER CYS GLY PRO ALA
SEQRES 263 A 4128 ALA GLY VAL ILE ASP ALA TYR MET THR LEU ALA ASP PHE
SEQRES 264 A 4128 CYS ASP GLN GLN LEU ARG LYS GLU GLU GLU ASN ALA SER
SEQRES 265 A 4128 VAL ILE ASP SER ALA GLU LEU GLN ALA TYR PRO ALA LEU
SEQRES 266 A 4128 VAL VAL GLU LYS MET LEU LYS ALA LEU LYS LEU ASN SER
SEQRES 267 A 4128 ASN GLU ALA ARG LEU LYS PHE PRO ARG LEU LEU GLN ILE
SEQRES 268 A 4128 ILE GLU ARG TYR PRO GLU GLU THR LEU SER LEU MET THR
SEQRES 269 A 4128 LYS GLU ILE SER SER VAL PRO CYS TRP GLN PHE ILE SER
SEQRES 270 A 4128 TRP ILE SER HIS MET VAL ALA LEU LEU ASP LYS ASP GLN
SEQRES 271 A 4128 ALA VAL ALA VAL GLN HIS SER VAL GLU GLU ILE THR ASP
SEQRES 272 A 4128 ASN TYR PRO GLN ALA ILE VAL TYR PRO PHE ILE ILE SER
SEQRES 273 A 4128 SER GLU SER TYR SER PHE LYS ASP THR SER THR GLY HIS
SEQRES 274 A 4128 LYS ASN LYS GLU PHE VAL ALA ARG ILE LYS SER LYS LEU
SEQRES 275 A 4128 ASP GLN GLY GLY VAL ILE GLN ASP PHE ILE ASN ALA LEU
SEQRES 276 A 4128 ASP GLN LEU SER ASN PRO GLU LEU LEU PHE LYS ASP TRP
SEQRES 277 A 4128 SER ASN ASP VAL ARG ALA GLU LEU ALA LYS THR PRO VAL
SEQRES 278 A 4128 ASN LYS LYS ASN ILE GLU LYS MET TYR GLU ARG MET TYR
SEQRES 279 A 4128 ALA ALA LEU GLY ASP PRO LYS ALA PRO GLY LEU GLY ALA
SEQRES 280 A 4128 PHE ARG ARG LYS PHE ILE GLN THR PHE GLY LYS GLU PHE
SEQRES 281 A 4128 ASP LYS HIS PHE GLY LYS GLY GLY SER LYS LEU LEU ARG
SEQRES 282 A 4128 MET LYS LEU SER ASP PHE ASN ASP ILE THR ASN MET LEU
SEQRES 283 A 4128 LEU LEU LYS MET ASN LYS ASP SER LYS PRO PRO GLY ASN
SEQRES 284 A 4128 LEU LYS GLU CYS SER PRO TRP MET SER ASP PHE LYS VAL
SEQRES 285 A 4128 GLU PHE LEU ARG ASN GLU LEU GLU ILE PRO GLY GLN TYR
SEQRES 286 A 4128 ASP GLY ARG GLY LYS PRO LEU PRO GLU TYR HIS VAL ARG
SEQRES 287 A 4128 ILE ALA GLY PHE ASP GLU ARG VAL THR VAL MET ALA SER
SEQRES 288 A 4128 LEU ARG ARG PRO LYS ARG ILE ILE ILE ARG GLY HIS ASP
SEQRES 289 A 4128 GLU ARG GLU HIS PRO PHE LEU VAL LYS GLY GLY GLU ASP
SEQRES 290 A 4128 LEU ARG GLN ASP GLN ARG VAL GLU GLN LEU PHE GLN VAL
SEQRES 291 A 4128 MET ASN GLY ILE LEU ALA GLN ASP SER ALA CYS SER GLN
SEQRES 292 A 4128 ARG ALA LEU GLN LEU ARG THR TYR SER VAL VAL PRO MET
SEQRES 293 A 4128 THR SER ARG LEU GLY LEU ILE GLU TRP LEU GLU ASN THR
SEQRES 294 A 4128 VAL THR LEU LYS ASP LEU LEU LEU ASN THR MET SER GLN
SEQRES 295 A 4128 GLU GLU LYS ALA ALA TYR LEU SER ASP PRO ARG ALA PRO
SEQRES 296 A 4128 PRO CYS GLU TYR LYS ASP TRP LEU THR LYS MET SER GLY
SEQRES 297 A 4128 LYS HIS ASP VAL GLY ALA TYR MET LEU MET TYR LYS GLY
SEQRES 298 A 4128 ALA ASN ARG THR GLU THR VAL THR SER PHE ARG LYS ARG
SEQRES 299 A 4128 GLU SER LYS VAL PRO ALA ASP LEU LEU LYS ARG ALA PHE
SEQRES 300 A 4128 VAL ARG MET SER THR SER PRO GLU ALA PHE LEU ALA LEU
SEQRES 301 A 4128 ARG SER HIS PHE ALA SER SER HIS ALA LEU ILE CYS ILE
SEQRES 302 A 4128 SER HIS TRP ILE LEU GLY ILE GLY ASP ARG HIS LEU ASN
SEQRES 303 A 4128 ASN PHE MET VAL ALA MET GLU THR GLY GLY VAL ILE GLY
SEQRES 304 A 4128 ILE ASP PHE GLY HIS ALA PHE GLY SER ALA THR GLN PHE
SEQRES 305 A 4128 LEU PRO VAL PRO GLU LEU MET PRO PHE ARG LEU THR ARG
SEQRES 306 A 4128 GLN PHE ILE ASN LEU MET LEU PRO MET LYS GLU THR GLY
SEQRES 307 A 4128 LEU MET TYR SER ILE MET VAL HIS ALA LEU ARG ALA PHE
SEQRES 308 A 4128 ARG SER ASP PRO GLY LEU LEU THR ASN THR MET ASP VAL
SEQRES 309 A 4128 PHE VAL LYS GLU PRO SER PHE ASP TRP LYS ASN PHE GLU
SEQRES 310 A 4128 GLN LYS MET LEU LYS LYS GLY GLY SER TRP ILE GLN GLU
SEQRES 311 A 4128 ILE ASN VAL ALA GLU LYS ASN TRP TYR PRO ARG GLN LYS
SEQRES 312 A 4128 ILE CYS TYR ALA LYS ARG LYS LEU ALA GLY ALA ASN PRO
SEQRES 313 A 4128 ALA VAL ILE THR CYS ASP GLU LEU LEU LEU GLY HIS GLU
SEQRES 314 A 4128 LYS ALA PRO ALA PHE ARG ASP TYR VAL ALA VAL ALA ARG
SEQRES 315 A 4128 GLY SER LYS ASP HIS ASN ILE ARG ALA GLN GLU PRO GLU
SEQRES 316 A 4128 SER GLY LEU SER GLU GLU THR GLN VAL LYS CYS LEU MET
SEQRES 317 A 4128 ASP GLN ALA THR ASP PRO ASN ILE LEU GLY ARG THR TRP
SEQRES 318 A 4128 GLU GLY TRP GLU PRO TRP MET
HELIX 1 AA1 SER A 11 SER A 20 1 10
HELIX 2 AA2 GLY A 31 LEU A 44 1 14
HELIX 3 AA3 VAL A 50 LEU A 65 1 16
HELIX 4 AA4 ASN A 74 MET A 96 1 23
HELIX 5 AA5 ILE A 100 ASP A 118 1 19
HELIX 6 AA6 LEU A 128 SER A 140 1 13
HELIX 7 AA7 PHE A 147 LEU A 162 1 16
HELIX 8 AA8 VAL A 170 HIS A 185 1 16
HELIX 9 AA9 ASN A 191 THR A 206 1 16
HELIX 10 AB1 LYS A 216 LEU A 230 1 15
HELIX 11 AB2 GLU A 239 ILE A 248 1 10
HELIX 12 AB3 ILE A 248 LEU A 253 1 6
HELIX 13 AB4 GLN A 259 LYS A 263 5 5
HELIX 14 AB5 TYR A 265 PHE A 275 1 11
HELIX 15 AB6 PHE A 275 THR A 284 1 10
HELIX 16 AB7 TYR A 290 ALA A 302 1 13
HELIX 17 AB8 LEU A 308 LYS A 329 1 22
HELIX 18 AB9 LYS A 335 VAL A 352 1 18
HELIX 19 AC1 LEU A 359 TYR A 366 1 8
HELIX 20 AC2 CYS A 373 ALA A 378 5 6
HELIX 21 AC3 ASP A 382 THR A 398 1 17
HELIX 22 AC4 GLN A 399 ASP A 401 5 3
HELIX 23 AC5 GLN A 409 LEU A 422 1 14
HELIX 24 AC6 TYR A 431 SER A 445 1 15
HELIX 25 AC7 SER A 450 GLY A 472 1 23
HELIX 26 AC8 PRO A 473 ARG A 489 1 17
HELIX 27 AC9 HIS A 533 GLN A 539 1 7
HELIX 28 AD1 ASP A 547 LEU A 564 1 18
HELIX 29 AD2 LYS A 570 THR A 582 1 13
HELIX 30 AD3 VAL A 588 ASP A 595 1 8
HELIX 31 AD4 SER A 606 ASN A 611 1 6
HELIX 32 AD5 ASN A 611 ALA A 622 1 12
HELIX 33 AD6 GLU A 632 GLN A 638 1 7
HELIX 34 AD7 GLN A 638 PHE A 649 1 12
HELIX 35 AD8 LEU A 653 LEU A 660 1 8
HELIX 36 AD9 LEU A 660 GLY A 665 1 6
HELIX 37 AE1 LEU A 670 ASN A 676 1 7
HELIX 38 AE2 ALA A 677 TYR A 682 1 6
HELIX 39 AE3 PRO A 698 GLU A 713 1 16
HELIX 40 AE4 VAL A 714 LYS A 719 1 6
HELIX 41 AE5 GLU A 724 CYS A 729 1 6
HELIX 42 AE6 ILE A 741 VAL A 749 1 9
HELIX 43 AE7 PRO A 750 ALA A 755 1 6
HELIX 44 AE8 LEU A 770 ARG A 782 1 13
HELIX 45 AE9 TYR A 788 LYS A 801 1 14
HELIX 46 AF1 THR A 802 LEU A 805 5 4
HELIX 47 AF2 SER A 847 GLY A 860 1 14
HELIX 48 AF3 ILE A 866 ASP A 877 1 12
HELIX 49 AF4 VAL A 909 THR A 920 1 12
HELIX 50 AF5 ALA A 921 ASP A 923 5 3
HELIX 51 AF6 ARG A 924 ALA A 945 1 22
HELIX 52 AF7 PRO A 956 LEU A 961 1 6
HELIX 53 AF8 PHE A 966 VAL A 976 1 11
HELIX 54 AF9 GLN A 978 LEU A 991 1 14
HELIX 55 AG1 LEU A 991 LYS A 999 1 9
HELIX 56 AG2 SER A 1003 ALA A 1012 1 10
HELIX 57 AG3 ILE A 1013 LEU A 1014 5 2
HELIX 58 AG4 ASP A 1015 ASP A 1019 5 5
HELIX 59 AG5 VAL A 1021 GLY A 1030 1 10
HELIX 60 AG6 ARG A 1031 ILE A 1041 1 11
HELIX 61 AG7 ASN A 1055 LEU A 1068 1 14
HELIX 62 AG8 LEU A 1068 PHE A 1073 1 6
HELIX 63 AG9 GLY A 1077 GLU A 1092 1 16
HELIX 64 AH1 LEU A 1095 VAL A 1100 1 6
HELIX 65 AH2 VAL A 1100 ASP A 1117 1 18
HELIX 66 AH3 ILE A 1124 ILE A 1137 1 14
HELIX 67 AH4 ASN A 1146 ARG A 1151 1 6
HELIX 68 AH5 ARG A 1151 GLY A 1156 1 6
HELIX 69 AH6 LEU A 1168 GLY A 1177 1 10
HELIX 70 AH7 GLY A 1216 GLU A 1225 1 10
HELIX 71 AH8 ALA A 1252 GLU A 1265 1 14
HELIX 72 AH9 CYS A 1266 PHE A 1270 5 5
HELIX 73 AI1 GLN A 1287 ASP A 1305 1 19
HELIX 74 AI2 PRO A 1324 ASN A 1350 1 27
HELIX 75 AI3 LEU A 1368 VAL A 1373 1 6
HELIX 76 AI4 CYS A 1377 ILE A 1382 1 6
HELIX 77 AI5 GLN A 1390 MET A 1408 1 19
HELIX 78 AI6 TYR A 1411 ARG A 1420 1 10
HELIX 79 AI7 ILE A 1423 ILE A 1428 1 6
HELIX 80 AI8 ILE A 1428 ALA A 1433 1 6
HELIX 81 AI9 GLN A 1442 GLN A 1457 1 16
HELIX 82 AJ1 LEU A 1458 ALA A 1461 5 4
HELIX 83 AJ2 HIS A 1477 LEU A 1486 1 10
HELIX 84 AJ3 SER A 1506 ALA A 1511 1 6
HELIX 85 AJ4 GLY A 1513 PHE A 1521 1 9
HELIX 86 AJ5 GLY A 1522 GLU A 1526 5 5
HELIX 87 AJ6 SER A 1549 GLY A 1556 1 8
HELIX 88 AJ7 TYR A 1560 THR A 1566 1 7
HELIX 89 AJ8 ILE A 1567 ASP A 1576 1 10
HELIX 90 AJ9 LEU A 1580 ASP A 1588 1 9
HELIX 91 AK1 VAL A 1593 ARG A 1608 1 16
HELIX 92 AK2 PRO A 1638 MET A 1643 1 6
HELIX 93 AK3 LYS A 1651 ASP A 1656 1 6
HELIX 94 AK4 SER A 1677 LEU A 1695 1 19
HELIX 95 AK5 PHE A 1698 LEU A 1702 5 5
HELIX 96 AK6 LEU A 1710 HIS A 1721 1 12
HELIX 97 AK7 ASN A 1738 LEU A 1752 1 15
HELIX 98 AK8 TYR A 1802 LYS A 1807 1 6
HELIX 99 AK9 LEU A 1858 GLY A 1872 1 15
HELIX 100 AL1 TYR A 1873 LEU A 1877 5 5
HELIX 101 AL2 VAL A 1879 TYR A 1881 5 3
HELIX 102 AL3 SER A 1882 HIS A 1890 1 9
HELIX 103 AL4 LYS A 1895 ASN A 1909 1 15
HELIX 104 AL5 LEU A 1915 ALA A 1928 1 14
HELIX 105 AL6 GLU A 1935 SER A 1950 1 16
HELIX 106 AL7 ASN A 1957 GLU A 1969 1 13
HELIX 107 AL8 GLU A 1979 GLU A 1999 1 21
HELIX 108 AL9 LYS A 2002 ALA A 2011 1 10
HELIX 109 AM1 ALA A 2011 GLY A 2021 1 11
HELIX 110 AM2 LEU A 2036 ASP A 2044 1 9
HELIX 111 AM3 ASP A 2044 VAL A 2049 1 6
HELIX 112 AM4 VAL A 2049 TYR A 2054 1 6
HELIX 113 AM5 PRO A 2074 LEU A 2081 1 8
HELIX 114 AM6 LEU A 2081 ARG A 2090 1 10
HELIX 115 AM7 CYS A 2093 HIS A 2105 1 13
HELIX 116 AM8 VAL A 2118 LEU A 2122 1 5
HELIX 117 AM9 ILE A 2137 LYS A 2148 1 12
HELIX 118 AN1 ASN A 2152 VAL A 2156 5 5
HELIX 119 AN2 PHE A 2157 LEU A 2165 1 9
HELIX 120 AN3 LEU A 2169 SER A 2174 1 6
HELIX 121 AN4 GLY A 2181 ILE A 2193 1 13
HELIX 122 AN5 TRP A 2196 THR A 2201 1 6
HELIX 123 AN6 GLU A 2209 VAL A 2223 1 15
HELIX 124 AN7 ARG A 2232 TRP A 2245 1 14
HELIX 125 AN8 SER A 2250 PHE A 2260 1 11
HELIX 126 AN9 ASN A 2270 GLN A 2275 1 6
HELIX 127 AO1 GLN A 2275 VAL A 2280 1 6
HELIX 128 AO2 TYR A 2288 SER A 2297 1 10
HELIX 129 AO3 GLU A 2298 SER A 2308 1 11
HELIX 130 AO4 VAL A 2315 ARG A 2333 1 19
HELIX 131 AO5 GLU A 2338 GLN A 2351 1 14
HELIX 132 AO6 GLU A 2357 ASN A 2365 1 9
HELIX 133 AO7 LYS A 2366 SER A 2370 5 5
HELIX 134 AO8 PHE A 2378 LEU A 2385 1 8
HELIX 135 AO9 LEU A 2393 GLY A 2407 1 15
HELIX 136 AP1 LEU A 2415 ARG A 2425 1 11
HELIX 137 AP2 GLU A 2430 LYS A 2433 5 4
HELIX 138 AP3 VAL A 2434 TYR A 2440 1 7
HELIX 139 AP4 LYS A 2441 MET A 2443 5 3
HELIX 140 AP5 LYS A 2447 PHE A 2461 1 15
HELIX 141 AP6 CYS A 2469 ASN A 2483 1 15
HELIX 142 AP7 ASP A 2494 GLY A 2509 1 16
HELIX 143 AP8 PRO A 2515 SER A 2526 1 12
HELIX 144 AP9 THR A 2535 SER A 2547 1 13
HELIX 145 AQ1 PHE A 2554 THR A 2566 1 13
HELIX 146 AQ2 HIS A 2787 THR A 2792 1 6
HELIX 147 AQ3 THR A 2792 ASP A 2801 1 10
HELIX 148 AQ4 LYS A 2806 LYS A 2818 1 13
HELIX 149 AQ5 LYS A 2818 PHE A 2823 1 6
HELIX 150 AQ6 THR A 2825 ARG A 2842 1 18
HELIX 151 AQ7 ARG A 2842 THR A 2847 1 6
HELIX 152 AQ8 SER A 2856 SER A 2862 1 7
HELIX 153 AQ9 VAL A 2876 SER A 2883 1 8
HELIX 154 AR1 PRO A 2887 GLU A 2895 1 9
HELIX 155 AR2 LEU A 2916 ARG A 2922 1 7
HELIX 156 AR3 TYR A 2930 LEU A 2939 1 10
HELIX 157 AR4 GLU A 2946 LEU A 2957 1 12
HELIX 158 AR5 GLU A 2960 ALA A 2968 1 9
HELIX 159 AR6 LYS A 2970 ALA A 2975 1 6
HELIX 160 AR7 GLU A 2985 GLU A 2990 1 6
HELIX 161 AR8 GLU A 2990 TYR A 3002 1 13
HELIX 162 AR9 GLU A 3007 ALA A 3017 1 11
HELIX 163 AS1 PRO A 3025 SER A 3032 1 8
HELIX 164 AS2 GLN A 3037 THR A 3039 5 3
HELIX 165 AS3 TYR A 3040 SER A 3047 1 8
HELIX 166 AS4 SER A 3047 GLN A 3054 1 8
HELIX 167 AS5 SER A 3060 GLY A 3071 1 12
HELIX 168 AS6 LYS A 3075 LEU A 3080 1 6
HELIX 169 AS7 SER A 3083 TYR A 3090 1 8
HELIX 170 AS8 VAL A 3096 TYR A 3114 1 19
HELIX 171 AS9 VAL A 3119 GLN A 3130 1 12
HELIX 172 AT1 GLN A 3130 SER A 3146 1 17
HELIX 173 AT2 SER A 3146 VAL A 3155 1 10
HELIX 174 AT3 PRO A 3156 TYR A 3168 1 13
HELIX 175 AT4 ASN A 3177 GLU A 3195 1 19
HELIX 176 AT5 SER A 3228 SER A 3245 1 18
HELIX 177 AT6 ALA A 3246 GLN A 3249 5 4
HELIX 178 AT7 SER A 3253 GLU A 3265 1 13
HELIX 179 AT8 THR A 3268 ARG A 3287 1 20
HELIX 180 AT9 GLN A 3291 VAL A 3312 1 22
HELIX 181 AU1 TYR A 3315 TYR A 3334 1 20
HELIX 182 AU2 ALA A 3346 GLU A 3353 1 8
HELIX 183 AU3 GLU A 3353 ARG A 3358 1 6
HELIX 184 AU4 ARG A 3380 GLU A 3394 1 15
HELIX 185 AU5 GLU A 3395 TRP A 3401 5 7
HELIX 186 AU6 ALA A 3407 GLU A 3427 1 21
HELIX 187 AU7 VAL A 3433 GLN A 3440 1 8
HELIX 188 AU8 TYR A 3442 ALA A 3444 5 3
HELIX 189 AU9 LEU A 3445 MET A 3450 1 6
HELIX 190 AV1 ASN A 3459 ILE A 3472 1 14
HELIX 191 AV2 TYR A 3475 LYS A 3485 1 11
HELIX 192 AV3 TRP A 3498 LYS A 3508 1 11
HELIX 193 AV4 ALA A 3511 ASP A 3523 1 13
HELIX 194 AV5 ILE A 3529 SER A 3539 1 11
HELIX 195 AV6 GLY A 3548 LYS A 3561 1 14
HELIX 196 AV7 ILE A 3568 ASN A 3580 1 13
HELIX 197 AV8 PRO A 3581 ARG A 3593 1 13
HELIX 198 AV9 LYS A 3603 MET A 3613 1 11
HELIX 199 AW1 ALA A 3622 ALA A 3627 1 6
HELIX 200 AW2 LYS A 3631 GLY A 3648 1 18
HELIX 201 AW3 ASP A 3658 LYS A 3675 1 18
HELIX 202 AW4 TRP A 3686 PHE A 3690 5 5
HELIX 203 AW5 GLU A 3693 ASN A 3697 5 5
HELIX 204 AW6 ARG A 3759 ASN A 3772 1 14
HELIX 205 AW7 ASP A 3778 ARG A 3784 1 7
HELIX 206 AW8 LEU A 3812 ASN A 3818 1 7
HELIX 207 AW9 MET A 3820 SER A 3847 1 28
HELIX 208 AX1 LYS A 3860 LYS A 3877 1 18
HELIX 209 AX2 LYS A 3877 MET A 3890 1 14
HELIX 210 AX3 ALA A 3896 GLY A 3919 1 24
HELIX 211 AX4 GLY A 3947 PHE A 3952 1 6
HELIX 212 AX5 THR A 3964 LEU A 3972 1 9
HELIX 213 AX6 LEU A 3979 SER A 3993 1 15
HELIX 214 AX7 PRO A 3995 VAL A 4006 1 12
HELIX 215 AX8 ASN A 4015 MET A 4020 1 6
HELIX 216 AX9 ARG A 4041 ALA A 4052 1 12
HELIX 217 AY1 VAL A 4058 LEU A 4066 1 9
HELIX 218 AY2 PRO A 4072 ARG A 4082 1 11
HELIX 219 AY3 ARG A 4082 HIS A 4087 1 6
HELIX 220 AY4 GLU A 4101 ASP A 4113 1 13
HELIX 221 AY5 ASP A 4113 ARG A 4119 1 7
SHEET 1 AA1 3 ILE A3719 PHE A3722 0
SHEET 2 AA1 3 LYS A3736 GLY A3742 -1 O ARG A3741 N ALA A3720
SHEET 3 AA1 3 THR A3727 VAL A3728 -1 N THR A3727 O ARG A3737
SHEET 1 AA2 5 ILE A3719 PHE A3722 0
SHEET 2 AA2 5 LYS A3736 GLY A3742 -1 O ARG A3741 N ALA A3720
SHEET 3 AA2 5 GLU A3747 VAL A3752 -1 O PHE A3750 N ILE A3738
SHEET 4 AA2 5 LEU A3800 GLU A3804 -1 O ILE A3803 N LEU A3751
SHEET 5 AA2 5 VAL A3794 MET A3796 -1 N VAL A3794 O LEU A3802
SHEET 1 AA3 2 THR A3809 THR A3811 0
SHEET 2 AA3 2 MET A3929 ALA A3931 -1 O VAL A3930 N VAL A3810
LINK O GLN A 990 NE1 TRP A 994 1555 1555 1.24
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 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
(ATOM LINES ARE NOT SHOWN.)
END
