HEADER PROTEIN BINDING 12-NOV-17 6BLY
TITLE CRYO-EM STRUCTURE OF HUMAN CPSF-160-WDR33 COMPLEX AT 3.36A RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CLEAVAGE AND POLYADENYLATION SPECIFICITY FACTOR SUBUNIT 1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CLEAVAGE AND POLYADENYLATION SPECIFICITY FACTOR 160 KDA
COMPND 5 SUBUNIT, CPSF 160 KDA SUBUNIT;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: PRE-MRNA 3' END PROCESSING PROTEIN WDR33;
COMPND 9 CHAIN: B;
COMPND 10 SYNONYM: WD REPEAT-CONTAINING PROTEIN 33, WD REPEAT-CONTAINING
COMPND 11 PROTEIN WDC146;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: CPSF1, CPSF160;
SOURCE 6 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 11 ORGANISM_COMMON: HUMAN;
SOURCE 12 ORGANISM_TAXID: 9606;
SOURCE 13 GENE: WDR33, WDC146;
SOURCE 14 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 15 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 7111
KEYWDS POLYADENYLATION, SCAFFOLDING PROTEIN, WD40, PROTEIN BINDING
EXPDTA ELECTRON MICROSCOPY
AUTHOR Y.SUN,Y.ZHANG,K.HAMILTON,T.WALZ,L.TONG
REVDAT 6 13-MAR-24 6BLY 1 REMARK
REVDAT 5 01-JAN-20 6BLY 1 REMARK
REVDAT 4 28-FEB-18 6BLY 1 JRNL
REVDAT 3 20-DEC-17 6BLY 1 JRNL
REVDAT 2 06-DEC-17 6BLY 1 REMARK
REVDAT 1 22-NOV-17 6BLY 0
JRNL AUTH Y.SUN,Y.ZHANG,K.HAMILTON,J.L.MANLEY,Y.SHI,T.WALZ,L.TONG
JRNL TITL MOLECULAR BASIS FOR THE RECOGNITION OF THE HUMAN AAUAAA
JRNL TITL 2 POLYADENYLATION SIGNAL.
JRNL REF PROC. NATL. ACAD. SCI. V. 115 E1419 2018
JRNL REF 2 U.S.A.
JRNL REFN ESSN 1091-6490
JRNL PMID 29208711
JRNL DOI 10.1073/PNAS.1718723115
REMARK 2
REMARK 2 RESOLUTION. 3.36 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 SOFTWARE PACKAGES : GAUTOMATCH, CTFFIND, PHENIX, RELION
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) : 3.360
REMARK 3 NUMBER OF PARTICLES : 456310
REMARK 3 CTF CORRECTION METHOD : PHASE FLIPPING AND AMPLITUDE
REMARK 3 CORRECTION
REMARK 3
REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL
REMARK 3
REMARK 3 OTHER DETAILS: NULL
REMARK 4
REMARK 4 6BLY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-NOV-17.
REMARK 100 THE DEPOSITION ID IS D_1000231081.
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 : BINARY COMPLEX OF HUMAN CPSF
REMARK 245 -160-WDR33
REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 0.18
REMARK 245 SAMPLE SUPPORT DETAILS : NULL
REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL
REMARK 245 SAMPLE BUFFER : NULL
REMARK 245 PH : 7.90
REMARK 245 SAMPLE DETAILS : NULL
REMARK 245
REMARK 245 DATA ACQUISITION
REMARK 245 DATE OF EXPERIMENT : NULL
REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : 2468
REMARK 245 TEMPERATURE (KELVIN) : NULL
REMARK 245 MICROSCOPE MODEL : FEI TITAN KRIOS
REMARK 245 DETECTOR TYPE : GATAN K2 SUMMIT (4K X 4K)
REMARK 245 MINIMUM DEFOCUS (NM) : 1200.00
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) : 7000.00
REMARK 245 ILLUMINATION MODE : FLOOD BEAM
REMARK 245 NOMINAL MAGNIFICATION : 225000
REMARK 245 CALIBRATED MAGNIFICATION : 46729
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 ASP A 46
REMARK 465 ALA A 47
REMARK 465 GLU A 48
REMARK 465 ALA A 49
REMARK 465 LEU A 50
REMARK 465 THR A 51
REMARK 465 LYS A 52
REMARK 465 ASN A 53
REMARK 465 ASP A 54
REMARK 465 ARG A 55
REMARK 465 SER A 56
REMARK 465 THR A 57
REMARK 465 GLU A 58
REMARK 465 GLY A 59
REMARK 465 LYS A 60
REMARK 465 ALA A 61
REMARK 465 HIS A 62
REMARK 465 ARG A 166
REMARK 465 GLU A 167
REMARK 465 SER A 168
REMARK 465 LEU A 169
REMARK 465 ALA A 170
REMARK 465 GLU A 171
REMARK 465 GLU A 172
REMARK 465 HIS A 173
REMARK 465 GLU A 174
REMARK 465 GLY A 175
REMARK 465 LEU A 176
REMARK 465 VAL A 177
REMARK 465 GLY A 178
REMARK 465 GLU A 179
REMARK 465 GLY A 180
REMARK 465 GLN A 181
REMARK 465 ARG A 182
REMARK 465 GLN A 401
REMARK 465 GLU A 402
REMARK 465 PRO A 403
REMARK 465 PRO A 404
REMARK 465 ALA A 405
REMARK 465 SER A 406
REMARK 465 ALA A 407
REMARK 465 VAL A 408
REMARK 465 ARG A 409
REMARK 465 GLU A 410
REMARK 465 ALA A 411
REMARK 465 ALA A 412
REMARK 465 ASP A 413
REMARK 465 LYS A 414
REMARK 465 GLU A 415
REMARK 465 GLU A 416
REMARK 465 PRO A 417
REMARK 465 PRO A 418
REMARK 465 SER A 419
REMARK 465 LYS A 420
REMARK 465 LYS A 421
REMARK 465 LYS A 422
REMARK 465 ARG A 423
REMARK 465 VAL A 424
REMARK 465 ASP A 425
REMARK 465 ALA A 426
REMARK 465 THR A 427
REMARK 465 ALA A 428
REMARK 465 GLY A 429
REMARK 465 TRP A 430
REMARK 465 SER A 431
REMARK 465 ALA A 432
REMARK 465 ALA A 433
REMARK 465 GLY A 434
REMARK 465 LYS A 435
REMARK 465 SER A 436
REMARK 465 VAL A 437
REMARK 465 PRO A 438
REMARK 465 GLN A 439
REMARK 465 ASP A 440
REMARK 465 GLU A 441
REMARK 465 VAL A 442
REMARK 465 ASP A 443
REMARK 465 GLU A 444
REMARK 465 ILE A 445
REMARK 465 GLU A 446
REMARK 465 VAL A 447
REMARK 465 TYR A 448
REMARK 465 GLY A 449
REMARK 465 SER A 450
REMARK 465 GLU A 451
REMARK 465 ALA A 452
REMARK 465 GLN A 453
REMARK 465 SER A 454
REMARK 465 GLY A 455
REMARK 465 THR A 456
REMARK 465 GLN A 457
REMARK 465 LEU A 458
REMARK 465 VAL A 542
REMARK 465 ARG A 543
REMARK 465 LYS A 544
REMARK 465 GLU A 545
REMARK 465 GLU A 546
REMARK 465 GLU A 547
REMARK 465 ASP A 548
REMARK 465 ASN A 549
REMARK 465 PRO A 550
REMARK 465 LYS A 551
REMARK 465 GLY A 552
REMARK 465 GLU A 553
REMARK 465 GLY A 554
REMARK 465 THR A 555
REMARK 465 GLU A 556
REMARK 465 GLN A 557
REMARK 465 GLU A 558
REMARK 465 PRO A 559
REMARK 465 SER A 560
REMARK 465 THR A 561
REMARK 465 THR A 562
REMARK 465 PRO A 563
REMARK 465 GLU A 564
REMARK 465 ALA A 565
REMARK 465 ASP A 566
REMARK 465 ASP A 567
REMARK 465 ASP A 568
REMARK 465 GLY A 569
REMARK 465 ASP A 641
REMARK 465 LEU A 642
REMARK 465 GLY A 643
REMARK 465 SER A 674
REMARK 465 TYR A 675
REMARK 465 GLY A 676
REMARK 465 GLY A 677
REMARK 465 ARG A 678
REMARK 465 HIS A 679
REMARK 465 GLU A 711
REMARK 465 SER A 712
REMARK 465 ARG A 713
REMARK 465 LEU A 714
REMARK 465 GLY A 715
REMARK 465 GLY A 716
REMARK 465 ALA A 717
REMARK 465 ARG A 718
REMARK 465 ASP A 719
REMARK 465 GLU A 720
REMARK 465 LEU A 721
REMARK 465 GLY A 722
REMARK 465 GLY A 723
REMARK 465 ARG A 724
REMARK 465 SER A 725
REMARK 465 GLY A 726
REMARK 465 PRO A 727
REMARK 465 GLU A 728
REMARK 465 ALA A 729
REMARK 465 GLU A 730
REMARK 465 GLY A 731
REMARK 465 LEU A 732
REMARK 465 GLY A 733
REMARK 465 SER A 734
REMARK 465 GLU A 735
REMARK 465 THR A 736
REMARK 465 SER A 737
REMARK 465 PRO A 738
REMARK 465 THR A 739
REMARK 465 VAL A 740
REMARK 465 ASP A 741
REMARK 465 ASP A 742
REMARK 465 GLU A 743
REMARK 465 GLU A 744
REMARK 465 GLU A 745
REMARK 465 MET A 746
REMARK 465 LEU A 747
REMARK 465 TYR A 748
REMARK 465 GLY A 749
REMARK 465 ASP A 750
REMARK 465 SER A 751
REMARK 465 GLY A 752
REMARK 465 SER A 753
REMARK 465 LEU A 754
REMARK 465 PHE A 755
REMARK 465 SER A 756
REMARK 465 PRO A 757
REMARK 465 SER A 758
REMARK 465 LYS A 759
REMARK 465 GLU A 760
REMARK 465 GLU A 761
REMARK 465 ALA A 762
REMARK 465 ARG A 763
REMARK 465 ARG A 764
REMARK 465 SER A 765
REMARK 465 SER A 766
REMARK 465 GLN A 767
REMARK 465 PRO A 768
REMARK 465 PRO A 769
REMARK 465 ALA A 770
REMARK 465 ASP A 771
REMARK 465 ARG A 772
REMARK 465 ASP A 773
REMARK 465 PRO A 774
REMARK 465 ALA A 775
REMARK 465 PRO A 776
REMARK 465 PHE A 777
REMARK 465 ARG A 778
REMARK 465 ALA A 779
REMARK 465 GLU A 780
REMARK 465 SER A 822
REMARK 465 PHE A 823
REMARK 465 GLY A 824
REMARK 465 GLN A 825
REMARK 465 PRO A 826
REMARK 465 THR A 827
REMARK 465 THR A 828
REMARK 465 GLN A 829
REMARK 465 GLY A 830
REMARK 465 GLU A 831
REMARK 465 ALA A 832
REMARK 465 ARG A 833
REMARK 465 ARG A 834
REMARK 465 GLU A 835
REMARK 465 GLU A 836
REMARK 465 ALA A 837
REMARK 465 THR A 838
REMARK 465 ARG A 839
REMARK 465 GLN A 840
REMARK 465 GLY A 841
REMARK 465 GLU A 842
REMARK 465 LEU A 843
REMARK 465 SER A 881
REMARK 465 GLN A 882
REMARK 465 LEU A 883
REMARK 465 GLY A 884
REMARK 465 GLN A 885
REMARK 465 GLU A 903
REMARK 465 LYS A 904
REMARK 465 LYS A 905
REMARK 465 PRO A 906
REMARK 465 LYS A 907
REMARK 465 PRO A 908
REMARK 465 SER A 909
REMARK 465 LYS A 910
REMARK 465 LYS A 911
REMARK 465 LYS A 912
REMARK 465 ALA A 913
REMARK 465 GLU A 914
REMARK 465 GLY A 915
REMARK 465 GLY A 916
REMARK 465 GLY A 917
REMARK 465 ALA A 918
REMARK 465 GLU A 919
REMARK 465 GLU A 920
REMARK 465 GLY A 921
REMARK 465 ALA A 922
REMARK 465 GLY A 923
REMARK 465 ALA A 924
REMARK 465 ARG A 925
REMARK 465 GLY A 1318
REMARK 465 ALA A 1319
REMARK 465 THR A 1320
REMARK 465 GLU A 1321
REMARK 465 GLY A 1322
REMARK 465 LEU A 1323
REMARK 465 SER A 1324
REMARK 465 LYS A 1325
REMARK 465 LYS A 1326
REMARK 465 SER A 1327
REMARK 465 VAL A 1328
REMARK 465 VAL A 1329
REMARK 465 ARG A 1388
REMARK 465 ARG A 1389
REMARK 465 THR A 1390
REMARK 465 LEU A 1391
REMARK 465 GLN A 1392
REMARK 465 MET B -14
REMARK 465 GLY B -13
REMARK 465 SER B -12
REMARK 465 SER B -11
REMARK 465 HIS B -10
REMARK 465 HIS B -9
REMARK 465 HIS B -8
REMARK 465 HIS B -7
REMARK 465 HIS B -6
REMARK 465 HIS B -5
REMARK 465 SER B -4
REMARK 465 SER B -3
REMARK 465 GLY B -2
REMARK 465 LEU B -1
REMARK 465 VAL B 0
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 THR B 3
REMARK 465 GLU B 4
REMARK 465 ILE B 5
REMARK 465 GLY B 6
REMARK 465 SER B 7
REMARK 465 PRO B 8
REMARK 465 PRO B 9
REMARK 465 ARG B 10
REMARK 465 PHE B 11
REMARK 465 PHE B 12
REMARK 465 HIS B 13
REMARK 465 MET B 14
REMARK 465 PRO B 15
REMARK 465 ARG B 16
REMARK 465 PHE B 17
REMARK 465 GLN B 18
REMARK 465 HIS B 19
REMARK 465 GLN B 20
REMARK 465 ALA B 21
REMARK 465 PRO B 22
REMARK 465 ARG B 23
REMARK 465 GLN B 24
REMARK 465 LEU B 25
REMARK 465 PHE B 26
REMARK 465 TYR B 27
REMARK 465 LYS B 28
REMARK 465 ARG B 29
REMARK 465 PRO B 30
REMARK 465 ASP B 31
REMARK 465 PHE B 32
REMARK 465 ALA B 33
REMARK 465 GLN B 34
REMARK 465 GLN B 35
REMARK 465 GLN B 36
REMARK 465 ALA B 37
REMARK 465 MET B 38
REMARK 465 GLN B 39
REMARK 465 GLN B 40
REMARK 465 LEU B 41
REMARK 465 THR B 42
REMARK 465 PHE B 43
REMARK 465 ASP B 44
REMARK 465 GLY B 45
REMARK 465 LYS B 46
REMARK 465 ARG B 47
REMARK 465 MET B 48
REMARK 465 ARG B 49
REMARK 465 LYS B 50
REMARK 465 ALA B 51
REMARK 465 VAL B 52
REMARK 465 ASN B 53
REMARK 465 ARG B 54
REMARK 465 ASN B 418
REMARK 465 LEU B 419
REMARK 465 LEU B 420
REMARK 465 PRO B 421
REMARK 465 GLY B 422
REMARK 465 MET B 423
REMARK 465 SER B 424
REMARK 465 GLU B 425
REMARK 465 ASP B 426
REMARK 465 GLY B 427
REMARK 465 VAL B 428
REMARK 465 GLU B 429
REMARK 465 TYR B 430
REMARK 465 ASP B 431
REMARK 465 ASP B 432
REMARK 465 LEU B 433
REMARK 465 GLU B 434
REMARK 465 PRO B 435
REMARK 465 ASN B 436
REMARK 465 SER B 437
REMARK 465 LEU B 438
REMARK 465 ALA B 439
REMARK 465 VAL B 440
REMARK 465 ILE B 441
REMARK 465 PRO B 442
REMARK 465 GLY B 443
REMARK 465 MET B 444
REMARK 465 GLY B 445
REMARK 465 ILE B 446
REMARK 465 PRO B 447
REMARK 465 GLU B 448
REMARK 465 GLN B 449
REMARK 465 LEU B 450
REMARK 465 LYS B 451
REMARK 465 LEU B 452
REMARK 465 ALA B 453
REMARK 465 MET B 454
REMARK 465 GLU B 455
REMARK 465 GLN B 456
REMARK 465 GLU B 457
REMARK 465 GLN B 458
REMARK 465 MET B 459
REMARK 465 GLY B 460
REMARK 465 LYS B 461
REMARK 465 ASP B 462
REMARK 465 GLU B 463
REMARK 465 SER B 464
REMARK 465 ASN B 465
REMARK 465 GLU B 466
REMARK 465 ILE B 467
REMARK 465 GLU B 468
REMARK 465 MET B 469
REMARK 465 THR B 470
REMARK 465 ILE B 471
REMARK 465 PRO B 472
REMARK 465 GLY B 473
REMARK 465 LEU B 474
REMARK 465 ASP B 475
REMARK 465 TRP B 476
REMARK 465 GLY B 477
REMARK 465 MET B 478
REMARK 465 GLU B 479
REMARK 465 GLU B 480
REMARK 465 VAL B 481
REMARK 465 MET B 482
REMARK 465 GLN B 483
REMARK 465 LYS B 484
REMARK 465 ASP B 485
REMARK 465 GLN B 486
REMARK 465 LYS B 487
REMARK 465 LYS B 488
REMARK 465 VAL B 489
REMARK 465 PRO B 490
REMARK 465 GLN B 491
REMARK 465 LYS B 492
REMARK 465 LYS B 493
REMARK 465 VAL B 494
REMARK 465 PRO B 495
REMARK 465 TYR B 496
REMARK 465 ALA B 497
REMARK 465 LYS B 498
REMARK 465 PRO B 499
REMARK 465 ILE B 500
REMARK 465 PRO B 501
REMARK 465 ALA B 502
REMARK 465 GLN B 503
REMARK 465 PHE B 504
REMARK 465 GLN B 505
REMARK 465 GLN B 506
REMARK 465 ALA B 507
REMARK 465 TRP B 508
REMARK 465 MET B 509
REMARK 465 GLN B 510
REMARK 465 ASN B 511
REMARK 465 LYS B 512
REMARK 465 VAL B 513
REMARK 465 PRO B 514
REMARK 465 ILE B 515
REMARK 465 PRO B 516
REMARK 465 ALA B 517
REMARK 465 PRO B 518
REMARK 465 ASN B 519
REMARK 465 GLU B 520
REMARK 465 VAL B 521
REMARK 465 LEU B 522
REMARK 465 ASN B 523
REMARK 465 ASP B 524
REMARK 465 ARG B 525
REMARK 465 LYS B 526
REMARK 465 GLU B 527
REMARK 465 ASP B 528
REMARK 465 ILE B 529
REMARK 465 LYS B 530
REMARK 465 LEU B 531
REMARK 465 GLU B 532
REMARK 465 GLU B 533
REMARK 465 LYS B 534
REMARK 465 LYS B 535
REMARK 465 LYS B 536
REMARK 465 THR B 537
REMARK 465 GLN B 538
REMARK 465 ALA B 539
REMARK 465 GLU B 540
REMARK 465 ILE B 541
REMARK 465 GLU B 542
REMARK 465 GLN B 543
REMARK 465 GLU B 544
REMARK 465 MET B 545
REMARK 465 ALA B 546
REMARK 465 THR B 547
REMARK 465 LEU B 548
REMARK 465 GLN B 549
REMARK 465 TYR B 550
REMARK 465 THR B 551
REMARK 465 ASN B 552
REMARK 465 PRO B 553
REMARK 465 GLN B 554
REMARK 465 LEU B 555
REMARK 465 LEU B 556
REMARK 465 GLU B 557
REMARK 465 GLN B 558
REMARK 465 LEU B 559
REMARK 465 LYS B 560
REMARK 465 ILE B 561
REMARK 465 GLU B 562
REMARK 465 ARG B 563
REMARK 465 LEU B 564
REMARK 465 ALA B 565
REMARK 465 GLN B 566
REMARK 465 LYS B 567
REMARK 465 GLN B 568
REMARK 465 VAL B 569
REMARK 465 GLU B 570
REMARK 465 GLN B 571
REMARK 465 ILE B 572
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 PRO A 654 C - N - CA ANGL. DEV. = 12.5 DEGREES
REMARK 500 PRO A 654 C - N - CD ANGL. DEV. = -15.6 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 PHE A 75 55.73 -92.19
REMARK 500 ASP A 114 -168.59 -78.80
REMARK 500 GLU A 198 -3.81 68.51
REMARK 500 LYS A 199 71.00 58.75
REMARK 500 LEU A 201 -127.93 57.77
REMARK 500 ILE A 204 -60.55 -120.24
REMARK 500 TYR A 212 77.84 59.78
REMARK 500 PRO A 215 84.39 -69.46
REMARK 500 ARG A 230 74.90 -119.72
REMARK 500 ALA A 232 -20.82 -141.85
REMARK 500 TRP A 256 73.04 58.97
REMARK 500 SER A 260 33.78 -140.69
REMARK 500 THR A 304 30.81 -92.26
REMARK 500 SER A 331 -109.96 54.01
REMARK 500 SER A 368 -159.76 -153.17
REMARK 500 MET A 377 -153.99 -90.07
REMARK 500 GLU A 378 142.55 -37.71
REMARK 500 ALA A 476 -60.88 -90.83
REMARK 500 PHE A 485 41.46 -105.60
REMARK 500 LYS A 517 -152.34 -82.98
REMARK 500 SER A 518 137.91 -33.33
REMARK 500 THR A 597 -168.73 -78.80
REMARK 500 HIS A 636 -169.43 -160.08
REMARK 500 ASP A 653 87.92 58.22
REMARK 500 PRO A 654 46.74 10.93
REMARK 500 THR A 709 -60.70 -96.11
REMARK 500 LYS A 847 -61.92 -91.46
REMARK 500 LYS A 889 50.32 -92.48
REMARK 500 PRO A 984 -164.32 -72.27
REMARK 500 ARG A 985 109.06 -52.19
REMARK 500 LEU A 988 116.56 -162.14
REMARK 500 SER A1031 -4.39 68.74
REMARK 500 LYS A1032 61.57 61.34
REMARK 500 ARG A1062 -169.98 -123.98
REMARK 500 LYS A1169 72.94 -102.69
REMARK 500 LYS A1229 -73.32 -76.03
REMARK 500 SER A1230 -177.39 -177.77
REMARK 500 ASP A1263 -166.83 -115.19
REMARK 500 ARG A1276 65.63 75.72
REMARK 500 HIS A1385 -4.38 65.00
REMARK 500 TYR B 88 38.45 -95.79
REMARK 500 PRO B 95 1.37 -68.67
REMARK 500 ASN B 101 74.36 49.09
REMARK 500 PHE B 151 22.18 -72.10
REMARK 500 ASN B 152 -71.40 -56.39
REMARK 500 PHE B 153 145.43 -178.24
REMARK 500 MET B 167 115.29 -160.21
REMARK 500 PRO B 212 44.26 -78.05
REMARK 500 ASP B 214 36.86 -97.80
REMARK 500 THR B 255 -52.98 -123.30
REMARK 500
REMARK 500 THIS ENTRY HAS 55 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: EMD-7113 RELATED DB: EMDB
REMARK 900 CRYO-EM STRUCTURE OF HUMAN CPSF-160-WDR33 COMPLEX AT 3.36 A
REMARK 900 RESOLUTION
REMARK 900 RELATED ID: EMD-7112 RELATED DB: EMDB
REMARK 900 CRYO-EM STRUCTURE OF HUMAN CPSF-160-WDR33-CPSF-30-PAS RNA COMPLEX
REMARK 900 AT 3.4 A RESOLUTION
REMARK 900 RELATED ID: EMD-7114 RELATED DB: EMDB
REMARK 900 CRYO-EM STRUCTURE OF HUMAN CPSF-160-WDR33 COMPLEX AT 3.8 A
REMARK 900 RESOLUTION
DBREF 6BLY A 1 1443 UNP Q10570 CPSF1_HUMAN 1 1443
DBREF 6BLY B 1 572 UNP Q9C0J8 WDR33_HUMAN 1 572
SEQADV 6BLY MET B -14 UNP Q9C0J8 EXPRESSION TAG
SEQADV 6BLY GLY B -13 UNP Q9C0J8 EXPRESSION TAG
SEQADV 6BLY SER B -12 UNP Q9C0J8 EXPRESSION TAG
SEQADV 6BLY SER B -11 UNP Q9C0J8 EXPRESSION TAG
SEQADV 6BLY HIS B -10 UNP Q9C0J8 EXPRESSION TAG
SEQADV 6BLY HIS B -9 UNP Q9C0J8 EXPRESSION TAG
SEQADV 6BLY HIS B -8 UNP Q9C0J8 EXPRESSION TAG
SEQADV 6BLY HIS B -7 UNP Q9C0J8 EXPRESSION TAG
SEQADV 6BLY HIS B -6 UNP Q9C0J8 EXPRESSION TAG
SEQADV 6BLY HIS B -5 UNP Q9C0J8 EXPRESSION TAG
SEQADV 6BLY SER B -4 UNP Q9C0J8 EXPRESSION TAG
SEQADV 6BLY SER B -3 UNP Q9C0J8 EXPRESSION TAG
SEQADV 6BLY GLY B -2 UNP Q9C0J8 EXPRESSION TAG
SEQADV 6BLY LEU B -1 UNP Q9C0J8 EXPRESSION TAG
SEQADV 6BLY VAL B 0 UNP Q9C0J8 EXPRESSION TAG
SEQRES 1 A 1443 MET TYR ALA VAL TYR LYS GLN ALA HIS PRO PRO THR GLY
SEQRES 2 A 1443 LEU GLU PHE SER MET TYR CYS ASN PHE PHE ASN ASN SER
SEQRES 3 A 1443 GLU ARG ASN LEU VAL VAL ALA GLY THR SER GLN LEU TYR
SEQRES 4 A 1443 VAL TYR ARG LEU ASN ARG ASP ALA GLU ALA LEU THR LYS
SEQRES 5 A 1443 ASN ASP ARG SER THR GLU GLY LYS ALA HIS ARG GLU LYS
SEQRES 6 A 1443 LEU GLU LEU ALA ALA SER PHE SER PHE PHE GLY ASN VAL
SEQRES 7 A 1443 MET SER MET ALA SER VAL GLN LEU ALA GLY ALA LYS ARG
SEQRES 8 A 1443 ASP ALA LEU LEU LEU SER PHE LYS ASP ALA LYS LEU SER
SEQRES 9 A 1443 VAL VAL GLU TYR ASP PRO GLY THR HIS ASP LEU LYS THR
SEQRES 10 A 1443 LEU SER LEU HIS TYR PHE GLU GLU PRO GLU LEU ARG ASP
SEQRES 11 A 1443 GLY PHE VAL GLN ASN VAL HIS THR PRO ARG VAL ARG VAL
SEQRES 12 A 1443 ASP PRO ASP GLY ARG CYS ALA ALA MET LEU VAL TYR GLY
SEQRES 13 A 1443 THR ARG LEU VAL VAL LEU PRO PHE ARG ARG GLU SER LEU
SEQRES 14 A 1443 ALA GLU GLU HIS GLU GLY LEU VAL GLY GLU GLY GLN ARG
SEQRES 15 A 1443 SER SER PHE LEU PRO SER TYR ILE ILE ASP VAL ARG ALA
SEQRES 16 A 1443 LEU ASP GLU LYS LEU LEU ASN ILE ILE ASP LEU GLN PHE
SEQRES 17 A 1443 LEU HIS GLY TYR TYR GLU PRO THR LEU LEU ILE LEU PHE
SEQRES 18 A 1443 GLU PRO ASN GLN THR TRP PRO GLY ARG VAL ALA VAL ARG
SEQRES 19 A 1443 GLN ASP THR CYS SER ILE VAL ALA ILE SER LEU ASN ILE
SEQRES 20 A 1443 THR GLN LYS VAL HIS PRO VAL ILE TRP SER LEU THR SER
SEQRES 21 A 1443 LEU PRO PHE ASP CYS THR GLN ALA LEU ALA VAL PRO LYS
SEQRES 22 A 1443 PRO ILE GLY GLY VAL VAL VAL PHE ALA VAL ASN SER LEU
SEQRES 23 A 1443 LEU TYR LEU ASN GLN SER VAL PRO PRO TYR GLY VAL ALA
SEQRES 24 A 1443 LEU ASN SER LEU THR THR GLY THR THR ALA PHE PRO LEU
SEQRES 25 A 1443 ARG THR GLN GLU GLY VAL ARG ILE THR LEU ASP CYS ALA
SEQRES 26 A 1443 GLN ALA THR PHE ILE SER TYR ASP LYS MET VAL ILE SER
SEQRES 27 A 1443 LEU LYS GLY GLY GLU ILE TYR VAL LEU THR LEU ILE THR
SEQRES 28 A 1443 ASP GLY MET ARG SER VAL ARG ALA PHE HIS PHE ASP LYS
SEQRES 29 A 1443 ALA ALA ALA SER VAL LEU THR THR SER MET VAL THR MET
SEQRES 30 A 1443 GLU PRO GLY TYR LEU PHE LEU GLY SER ARG LEU GLY ASN
SEQRES 31 A 1443 SER LEU LEU LEU LYS TYR THR GLU LYS LEU GLN GLU PRO
SEQRES 32 A 1443 PRO ALA SER ALA VAL ARG GLU ALA ALA ASP LYS GLU GLU
SEQRES 33 A 1443 PRO PRO SER LYS LYS LYS ARG VAL ASP ALA THR ALA GLY
SEQRES 34 A 1443 TRP SER ALA ALA GLY LYS SER VAL PRO GLN ASP GLU VAL
SEQRES 35 A 1443 ASP GLU ILE GLU VAL TYR GLY SER GLU ALA GLN SER GLY
SEQRES 36 A 1443 THR GLN LEU ALA THR TYR SER PHE GLU VAL CYS ASP SER
SEQRES 37 A 1443 ILE LEU ASN ILE GLY PRO CYS ALA ASN ALA ALA VAL GLY
SEQRES 38 A 1443 GLU PRO ALA PHE LEU SER GLU GLU PHE GLN ASN SER PRO
SEQRES 39 A 1443 GLU PRO ASP LEU GLU ILE VAL VAL CYS SER GLY HIS GLY
SEQRES 40 A 1443 LYS ASN GLY ALA LEU SER VAL LEU GLN LYS SER ILE ARG
SEQRES 41 A 1443 PRO GLN VAL VAL THR THR PHE GLU LEU PRO GLY CYS TYR
SEQRES 42 A 1443 ASP MET TRP THR VAL ILE ALA PRO VAL ARG LYS GLU GLU
SEQRES 43 A 1443 GLU ASP ASN PRO LYS GLY GLU GLY THR GLU GLN GLU PRO
SEQRES 44 A 1443 SER THR THR PRO GLU ALA ASP ASP ASP GLY ARG ARG HIS
SEQRES 45 A 1443 GLY PHE LEU ILE LEU SER ARG GLU ASP SER THR MET ILE
SEQRES 46 A 1443 LEU GLN THR GLY GLN GLU ILE MET GLU LEU ASP THR SER
SEQRES 47 A 1443 GLY PHE ALA THR GLN GLY PRO THR VAL PHE ALA GLY ASN
SEQRES 48 A 1443 ILE GLY ASP ASN ARG TYR ILE VAL GLN VAL SER PRO LEU
SEQRES 49 A 1443 GLY ILE ARG LEU LEU GLU GLY VAL ASN GLN LEU HIS PHE
SEQRES 50 A 1443 ILE PRO VAL ASP LEU GLY ALA PRO ILE VAL GLN CYS ALA
SEQRES 51 A 1443 VAL ALA ASP PRO TYR VAL VAL ILE MET SER ALA GLU GLY
SEQRES 52 A 1443 HIS VAL THR MET PHE LEU LEU LYS SER ASP SER TYR GLY
SEQRES 53 A 1443 GLY ARG HIS HIS ARG LEU ALA LEU HIS LYS PRO PRO LEU
SEQRES 54 A 1443 HIS HIS GLN SER LYS VAL ILE THR LEU CYS LEU TYR ARG
SEQRES 55 A 1443 ASP LEU SER GLY MET PHE THR THR GLU SER ARG LEU GLY
SEQRES 56 A 1443 GLY ALA ARG ASP GLU LEU GLY GLY ARG SER GLY PRO GLU
SEQRES 57 A 1443 ALA GLU GLY LEU GLY SER GLU THR SER PRO THR VAL ASP
SEQRES 58 A 1443 ASP GLU GLU GLU MET LEU TYR GLY ASP SER GLY SER LEU
SEQRES 59 A 1443 PHE SER PRO SER LYS GLU GLU ALA ARG ARG SER SER GLN
SEQRES 60 A 1443 PRO PRO ALA ASP ARG ASP PRO ALA PRO PHE ARG ALA GLU
SEQRES 61 A 1443 PRO THR HIS TRP CYS LEU LEU VAL ARG GLU ASN GLY THR
SEQRES 62 A 1443 MET GLU ILE TYR GLN LEU PRO ASP TRP ARG LEU VAL PHE
SEQRES 63 A 1443 LEU VAL LYS ASN PHE PRO VAL GLY GLN ARG VAL LEU VAL
SEQRES 64 A 1443 ASP SER SER PHE GLY GLN PRO THR THR GLN GLY GLU ALA
SEQRES 65 A 1443 ARG ARG GLU GLU ALA THR ARG GLN GLY GLU LEU PRO LEU
SEQRES 66 A 1443 VAL LYS GLU VAL LEU LEU VAL ALA LEU GLY SER ARG GLN
SEQRES 67 A 1443 SER ARG PRO TYR LEU LEU VAL HIS VAL ASP GLN GLU LEU
SEQRES 68 A 1443 LEU ILE TYR GLU ALA PHE PRO HIS ASP SER GLN LEU GLY
SEQRES 69 A 1443 GLN GLY ASN LEU LYS VAL ARG PHE LYS LYS VAL PRO HIS
SEQRES 70 A 1443 ASN ILE ASN PHE ARG GLU LYS LYS PRO LYS PRO SER LYS
SEQRES 71 A 1443 LYS LYS ALA GLU GLY GLY GLY ALA GLU GLU GLY ALA GLY
SEQRES 72 A 1443 ALA ARG GLY ARG VAL ALA ARG PHE ARG TYR PHE GLU ASP
SEQRES 73 A 1443 ILE TYR GLY TYR SER GLY VAL PHE ILE CYS GLY PRO SER
SEQRES 74 A 1443 PRO HIS TRP LEU LEU VAL THR GLY ARG GLY ALA LEU ARG
SEQRES 75 A 1443 LEU HIS PRO MET ALA ILE ASP GLY PRO VAL ASP SER PHE
SEQRES 76 A 1443 ALA PRO PHE HIS ASN VAL ASN CYS PRO ARG GLY PHE LEU
SEQRES 77 A 1443 TYR PHE ASN ARG GLN GLY GLU LEU ARG ILE SER VAL LEU
SEQRES 78 A 1443 PRO ALA TYR LEU SER TYR ASP ALA PRO TRP PRO VAL ARG
SEQRES 79 A 1443 LYS ILE PRO LEU ARG CYS THR ALA HIS TYR VAL ALA TYR
SEQRES 80 A 1443 HIS VAL GLU SER LYS VAL TYR ALA VAL ALA THR SER THR
SEQRES 81 A 1443 ASN THR PRO CYS ALA ARG ILE PRO ARG MET THR GLY GLU
SEQRES 82 A 1443 GLU LYS GLU PHE GLU THR ILE GLU ARG ASP GLU ARG TYR
SEQRES 83 A 1443 ILE HIS PRO GLN GLN GLU ALA PHE SER ILE GLN LEU ILE
SEQRES 84 A 1443 SER PRO VAL SER TRP GLU ALA ILE PRO ASN ALA ARG ILE
SEQRES 85 A 1443 GLU LEU GLN GLU TRP GLU HIS VAL THR CYS MET LYS THR
SEQRES 86 A 1443 VAL SER LEU ARG SER GLU GLU THR VAL SER GLY LEU LYS
SEQRES 87 A 1443 GLY TYR VAL ALA ALA GLY THR CYS LEU MET GLN GLY GLU
SEQRES 88 A 1443 GLU VAL THR CYS ARG GLY ARG ILE LEU ILE MET ASP VAL
SEQRES 89 A 1443 ILE GLU VAL VAL PRO GLU PRO GLY GLN PRO LEU THR LYS
SEQRES 90 A 1443 ASN LYS PHE LYS VAL LEU TYR GLU LYS GLU GLN LYS GLY
SEQRES 91 A 1443 PRO VAL THR ALA LEU CYS HIS CYS ASN GLY HIS LEU VAL
SEQRES 92 A 1443 SER ALA ILE GLY GLN LYS ILE PHE LEU TRP SER LEU ARG
SEQRES 93 A 1443 ALA SER GLU LEU THR GLY MET ALA PHE ILE ASP THR GLN
SEQRES 94 A 1443 LEU TYR ILE HIS GLN MET ILE SER VAL LYS ASN PHE ILE
SEQRES 95 A 1443 LEU ALA ALA ASP VAL MET LYS SER ILE SER LEU LEU ARG
SEQRES 96 A 1443 TYR GLN GLU GLU SER LYS THR LEU SER LEU VAL SER ARG
SEQRES 97 A 1443 ASP ALA LYS PRO LEU GLU VAL TYR SER VAL ASP PHE MET
SEQRES 98 A 1443 VAL ASP ASN ALA GLN LEU GLY PHE LEU VAL SER ASP ARG
SEQRES 99 A 1443 ASP ARG ASN LEU MET VAL TYR MET TYR LEU PRO GLU ALA
SEQRES 100 A 1443 LYS GLU SER PHE GLY GLY MET ARG LEU LEU ARG ARG ALA
SEQRES 101 A 1443 ASP PHE HIS VAL GLY ALA HIS VAL ASN THR PHE TRP ARG
SEQRES 102 A 1443 THR PRO CYS ARG GLY ALA THR GLU GLY LEU SER LYS LYS
SEQRES 103 A 1443 SER VAL VAL TRP GLU ASN LYS HIS ILE THR TRP PHE ALA
SEQRES 104 A 1443 THR LEU ASP GLY GLY ILE GLY LEU LEU LEU PRO MET GLN
SEQRES 105 A 1443 GLU LYS THR TYR ARG ARG LEU LEU MET LEU GLN ASN ALA
SEQRES 106 A 1443 LEU THR THR MET LEU PRO HIS HIS ALA GLY LEU ASN PRO
SEQRES 107 A 1443 ARG ALA PHE ARG MET LEU HIS VAL ASP ARG ARG THR LEU
SEQRES 108 A 1443 GLN ASN ALA VAL ARG ASN VAL LEU ASP GLY GLU LEU LEU
SEQRES 109 A 1443 ASN ARG TYR LEU TYR LEU SER THR MET GLU ARG SER GLU
SEQRES 110 A 1443 LEU ALA LYS LYS ILE GLY THR THR PRO ASP ILE ILE LEU
SEQRES 111 A 1443 ASP ASP LEU LEU GLU THR ASP ARG VAL THR ALA HIS PHE
SEQRES 1 B 587 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 587 LEU VAL MET ALA THR GLU ILE GLY SER PRO PRO ARG PHE
SEQRES 3 B 587 PHE HIS MET PRO ARG PHE GLN HIS GLN ALA PRO ARG GLN
SEQRES 4 B 587 LEU PHE TYR LYS ARG PRO ASP PHE ALA GLN GLN GLN ALA
SEQRES 5 B 587 MET GLN GLN LEU THR PHE ASP GLY LYS ARG MET ARG LYS
SEQRES 6 B 587 ALA VAL ASN ARG LYS THR ILE ASP TYR ASN PRO SER VAL
SEQRES 7 B 587 ILE LYS TYR LEU GLU ASN ARG ILE TRP GLN ARG ASP GLN
SEQRES 8 B 587 ARG ASP MET ARG ALA ILE GLN PRO ASP ALA GLY TYR TYR
SEQRES 9 B 587 ASN ASP LEU VAL PRO PRO ILE GLY MET LEU ASN ASN PRO
SEQRES 10 B 587 MET ASN ALA VAL THR THR LYS PHE VAL ARG THR SER THR
SEQRES 11 B 587 ASN LYS VAL LYS CYS PRO VAL PHE VAL VAL ARG TRP THR
SEQRES 12 B 587 PRO GLU GLY ARG ARG LEU VAL THR GLY ALA SER SER GLY
SEQRES 13 B 587 GLU PHE THR LEU TRP ASN GLY LEU THR PHE ASN PHE GLU
SEQRES 14 B 587 THR ILE LEU GLN ALA HIS ASP SER PRO VAL ARG ALA MET
SEQRES 15 B 587 THR TRP SER HIS ASN ASP MET TRP MET LEU THR ALA ASP
SEQRES 16 B 587 HIS GLY GLY TYR VAL LYS TYR TRP GLN SER ASN MET ASN
SEQRES 17 B 587 ASN VAL LYS MET PHE GLN ALA HIS LYS GLU ALA ILE ARG
SEQRES 18 B 587 GLU ALA SER PHE SER PRO THR ASP ASN LYS PHE ALA THR
SEQRES 19 B 587 CYS SER ASP ASP GLY THR VAL ARG ILE TRP ASP PHE LEU
SEQRES 20 B 587 ARG CYS HIS GLU GLU ARG ILE LEU ARG GLY HIS GLY ALA
SEQRES 21 B 587 ASP VAL LYS CYS VAL ASP TRP HIS PRO THR LYS GLY LEU
SEQRES 22 B 587 VAL VAL SER GLY SER LYS ASP SER GLN GLN PRO ILE LYS
SEQRES 23 B 587 PHE TRP ASP PRO LYS THR GLY GLN SER LEU ALA THR LEU
SEQRES 24 B 587 HIS ALA HIS LYS ASN THR VAL MET GLU VAL LYS LEU ASN
SEQRES 25 B 587 LEU ASN GLY ASN TRP LEU LEU THR ALA SER ARG ASP HIS
SEQRES 26 B 587 LEU CYS LYS LEU PHE ASP ILE ARG ASN LEU LYS GLU GLU
SEQRES 27 B 587 LEU GLN VAL PHE ARG GLY HIS LYS LYS GLU ALA THR ALA
SEQRES 28 B 587 VAL ALA TRP HIS PRO VAL HIS GLU GLY LEU PHE ALA SER
SEQRES 29 B 587 GLY GLY SER ASP GLY SER LEU LEU PHE TRP HIS VAL GLY
SEQRES 30 B 587 VAL GLU LYS GLU VAL GLY GLY MET GLU MET ALA HIS GLU
SEQRES 31 B 587 GLY MET ILE TRP SER LEU ALA TRP HIS PRO LEU GLY HIS
SEQRES 32 B 587 ILE LEU CYS SER GLY SER ASN ASP HIS THR SER LYS PHE
SEQRES 33 B 587 TRP THR ARG ASN ARG PRO GLY ASP LYS MET ARG ASP ARG
SEQRES 34 B 587 TYR ASN LEU ASN LEU LEU PRO GLY MET SER GLU ASP GLY
SEQRES 35 B 587 VAL GLU TYR ASP ASP LEU GLU PRO ASN SER LEU ALA VAL
SEQRES 36 B 587 ILE PRO GLY MET GLY ILE PRO GLU GLN LEU LYS LEU ALA
SEQRES 37 B 587 MET GLU GLN GLU GLN MET GLY LYS ASP GLU SER ASN GLU
SEQRES 38 B 587 ILE GLU MET THR ILE PRO GLY LEU ASP TRP GLY MET GLU
SEQRES 39 B 587 GLU VAL MET GLN LYS ASP GLN LYS LYS VAL PRO GLN LYS
SEQRES 40 B 587 LYS VAL PRO TYR ALA LYS PRO ILE PRO ALA GLN PHE GLN
SEQRES 41 B 587 GLN ALA TRP MET GLN ASN LYS VAL PRO ILE PRO ALA PRO
SEQRES 42 B 587 ASN GLU VAL LEU ASN ASP ARG LYS GLU ASP ILE LYS LEU
SEQRES 43 B 587 GLU GLU LYS LYS LYS THR GLN ALA GLU ILE GLU GLN GLU
SEQRES 44 B 587 MET ALA THR LEU GLN TYR THR ASN PRO GLN LEU LEU GLU
SEQRES 45 B 587 GLN LEU LYS ILE GLU ARG LEU ALA GLN LYS GLN VAL GLU
SEQRES 46 B 587 GLN ILE
HELIX 1 AA1 SER A 487 GLN A 491 5 5
HELIX 2 AA2 HIS A 506 ASN A 509 5 4
HELIX 3 AA3 PRO A 1154 THR A 1156 5 3
HELIX 4 AA4 GLN A 1352 MET A 1369 1 18
HELIX 5 AA5 HIS A 1372 LEU A 1376 5 5
HELIX 6 AA6 ASN A 1377 ARG A 1382 1 6
HELIX 7 AA7 LEU A 1403 LEU A 1408 5 6
HELIX 8 AA8 SER A 1411 GLY A 1423 1 13
HELIX 9 AA9 THR A 1425 VAL A 1439 1 15
HELIX 10 AB1 TYR B 59 ARG B 70 1 12
HELIX 11 AB2 TYR B 88 LEU B 92 5 5
HELIX 12 AB3 ASN B 101 VAL B 106 5 6
SHEET 1 AA1 5 TRP A1312 THR A1314 0
SHEET 2 AA1 5 ILE A1335 ALA A1339 -1 O TRP A1337 N TRP A1312
SHEET 3 AA1 5 ILE A1345 PRO A1350 -1 O GLY A1346 N PHE A1338
SHEET 4 AA1 5 ALA A 3 HIS A 9 -1 N VAL A 4 O LEU A1349
SHEET 5 AA1 5 VAL A1398 ASP A1400 1 O LEU A1399 N TYR A 5
SHEET 1 AA2 4 LEU A 14 CYS A 20 0
SHEET 2 AA2 4 ASN A 29 GLY A 34 -1 O ALA A 33 N PHE A 16
SHEET 3 AA2 4 GLN A 37 ASN A 44 -1 O TYR A 41 N LEU A 30
SHEET 4 AA2 4 LYS A 65 SER A 73 -1 O GLU A 67 N ARG A 42
SHEET 1 AA3 4 SER A 80 VAL A 84 0
SHEET 2 AA3 4 ALA A 93 PHE A 98 -1 O LEU A 95 N ALA A 82
SHEET 3 AA3 4 LYS A 102 TYR A 108 -1 O LYS A 102 N PHE A 98
SHEET 4 AA3 4 LEU A 115 TYR A 122 -1 O LYS A 116 N GLU A 107
SHEET 1 AA4 4 ARG A 140 VAL A 143 0
SHEET 2 AA4 4 CYS A 149 VAL A 154 -1 O ALA A 151 N ARG A 142
SHEET 3 AA4 4 ARG A 158 PRO A 163 -1 O ARG A 158 N VAL A 154
SHEET 4 AA4 4 TYR A 189 ASP A 192 -1 O ILE A 191 N LEU A 159
SHEET 1 AA5 4 ASN A 202 PHE A 208 0
SHEET 2 AA5 4 THR A 216 GLU A 222 -1 O LEU A 220 N ASP A 205
SHEET 3 AA5 4 CYS A 238 SER A 244 -1 O ILE A 243 N LEU A 217
SHEET 4 AA5 4 VAL A 254 LEU A 261 -1 O LEU A 258 N ILE A 240
SHEET 1 AA6 5 CYS A 265 ALA A 270 0
SHEET 2 AA6 5 VAL A 278 ALA A 282 -1 O VAL A 279 N LEU A 269
SHEET 3 AA6 5 SER A 285 LEU A 289 -1 O LEU A 289 N VAL A 278
SHEET 4 AA6 5 TYR A 296 ALA A 299 -1 O TYR A 296 N TYR A 288
SHEET 5 AA6 5 ARG A 313 THR A 314 1 O ARG A 313 N GLY A 297
SHEET 1 AA7 4 GLN A 326 PHE A 329 0
SHEET 2 AA7 4 LYS A 334 SER A 338 -1 O SER A 338 N GLN A 326
SHEET 3 AA7 4 GLU A 343 THR A 351 -1 O LEU A 347 N MET A 335
SHEET 4 AA7 4 VAL A 357 HIS A 361 -1 O ARG A 358 N ILE A 350
SHEET 1 AA8 4 GLN A 326 PHE A 329 0
SHEET 2 AA8 4 LYS A 334 SER A 338 -1 O SER A 338 N GLN A 326
SHEET 3 AA8 4 GLU A 343 THR A 351 -1 O LEU A 347 N MET A 335
SHEET 4 AA8 4 LYS A 364 ALA A 367 -1 O ALA A 365 N ILE A 344
SHEET 1 AA9 4 VAL A 375 THR A 376 0
SHEET 2 AA9 4 TYR A 381 LEU A 384 -1 O PHE A 383 N VAL A 375
SHEET 3 AA9 4 LEU A 392 GLU A 398 -1 O LEU A 394 N LEU A 382
SHEET 4 AA9 4 TYR A 461 VAL A 465 -1 O GLU A 464 N LYS A 395
SHEET 1 AB1 4 ALA A 478 GLY A 481 0
SHEET 2 AB1 4 GLU A 499 SER A 504 -1 O GLU A 499 N GLY A 481
SHEET 3 AB1 4 ALA A 511 LEU A 515 -1 O SER A 513 N VAL A 502
SHEET 4 AB1 4 VAL A1013 PRO A1017 -1 O ILE A1016 N LEU A 512
SHEET 1 AB2 4 GLN A 522 THR A 526 0
SHEET 2 AB2 4 LEU A 996 VAL A1000 -1 O ILE A 998 N THR A 525
SHEET 3 AB2 4 GLY A 986 PHE A 990 -1 N PHE A 987 O SER A 999
SHEET 4 AB2 4 PHE A 975 PHE A 978 -1 N PHE A 978 O GLY A 986
SHEET 1 AB3 4 ASP A 534 ILE A 539 0
SHEET 2 AB3 4 HIS A 572 SER A 578 -1 O ILE A 576 N TRP A 536
SHEET 3 AB3 4 THR A 583 GLN A 587 -1 O MET A 584 N LEU A 577
SHEET 4 AB3 4 MET A 593 GLU A 594 -1 O MET A 593 N GLN A 587
SHEET 1 AB4 4 PHE A 608 ILE A 612 0
SHEET 2 AB4 4 TYR A 617 VAL A 621 -1 O VAL A 619 N GLY A 610
SHEET 3 AB4 4 GLY A 625 LEU A 629 -1 O ARG A 627 N GLN A 620
SHEET 4 AB4 4 PHE A 637 PRO A 639 -1 O ILE A 638 N ILE A 626
SHEET 1 AB5 3 ILE A 646 VAL A 651 0
SHEET 2 AB5 3 VAL A 656 SER A 660 -1 O MET A 659 N VAL A 647
SHEET 3 AB5 3 VAL A 665 PHE A 668 -1 O PHE A 668 N VAL A 656
SHEET 1 AB6 2 LEU A 670 LYS A 671 0
SHEET 2 AB6 2 ARG A 681 LEU A 682 -1 O ARG A 681 N LYS A 671
SHEET 1 AB7 4 VAL A 695 ARG A 702 0
SHEET 2 AB7 4 HIS A 783 ARG A 789 -1 O TRP A 784 N TYR A 701
SHEET 3 AB7 4 MET A 794 GLN A 798 -1 O TYR A 797 N CYS A 785
SHEET 4 AB7 4 LEU A 804 VAL A 808 -1 O VAL A 805 N ILE A 796
SHEET 1 AB8 4 VAL A 846 LEU A 854 0
SHEET 2 AB8 4 ARG A 860 VAL A 867 -1 O HIS A 866 N LYS A 847
SHEET 3 AB8 4 LEU A 871 TYR A 874 -1 O TYR A 874 N LEU A 863
SHEET 4 AB8 4 LYS A 894 VAL A 895 -1 O VAL A 895 N ILE A 873
SHEET 1 AB9 2 PHE A 877 PRO A 878 0
SHEET 2 AB9 2 VAL A 890 ARG A 891 -1 O ARG A 891 N PHE A 877
SHEET 1 AC1 4 PHE A 931 ILE A 937 0
SHEET 2 AC1 4 TYR A 940 ILE A 945 -1 O GLY A 942 N PHE A 934
SHEET 3 AC1 4 HIS A 951 VAL A 955 -1 O LEU A 953 N VAL A 943
SHEET 4 AC1 4 LEU A 961 PRO A 965 -1 O HIS A 964 N TRP A 952
SHEET 1 AC2 4 THR A1021 TYR A1024 0
SHEET 2 AC2 4 ALA A1037 PRO A1043 -1 O ALA A1037 N HIS A1023
SHEET 3 AC2 4 GLN A1070 ILE A1076 -1 O GLN A1071 N THR A1042
SHEET 4 AC2 4 ILE A1092 GLU A1093 -1 O ILE A1092 N ILE A1076
SHEET 1 AC3 2 TYR A1027 HIS A1028 0
SHEET 2 AC3 2 VAL A1033 TYR A1034 -1 O VAL A1033 N HIS A1028
SHEET 1 AC4 2 ARG A1046 MET A1050 0
SHEET 2 AC4 2 LYS A1055 THR A1059 -1 O GLU A1058 N ILE A1047
SHEET 1 AC5 4 GLU A1098 VAL A1106 0
SHEET 2 AC5 4 TYR A1120 LEU A1127 -1 O GLY A1124 N THR A1101
SHEET 3 AC5 4 GLY A1137 GLU A1146 -1 O MET A1142 N VAL A1121
SHEET 4 AC5 4 ASN A1158 GLU A1167 -1 O LYS A1161 N ASP A1143
SHEET 1 AC6 4 VAL A1172 HIS A1177 0
SHEET 2 AC6 4 LEU A1182 ILE A1186 -1 O VAL A1183 N CYS A1176
SHEET 3 AC6 4 LYS A1189 LEU A1195 -1 O TRP A1193 N LEU A1182
SHEET 4 AC6 4 LEU A1200 ALA A1204 -1 O THR A1201 N SER A1194
SHEET 1 AC7 2 ILE A1212 SER A1217 0
SHEET 2 AC7 2 ILE A1222 ASP A1226 -1 O LEU A1223 N ILE A1216
SHEET 1 AC8 2 SER A1232 GLN A1237 0
SHEET 2 AC8 2 THR A1242 ARG A1248 -1 O SER A1244 N ARG A1235
SHEET 1 AC9 3 VAL A1255 VAL A1258 0
SHEET 2 AC9 3 LEU A1267 ASP A1273 -1 O SER A1272 N TYR A1256
SHEET 3 AC9 3 MET A1261 VAL A1262 -1 N MET A1261 O GLY A1268
SHEET 1 AD1 4 VAL A1255 VAL A1258 0
SHEET 2 AD1 4 LEU A1267 ASP A1273 -1 O SER A1272 N TYR A1256
SHEET 3 AD1 4 LEU A1278 MET A1282 -1 O MET A1279 N VAL A1271
SHEET 4 AD1 4 LEU A1297 PHE A1302 -1 O ARG A1299 N VAL A1280
SHEET 1 AD2 4 LYS B 109 THR B 113 0
SHEET 2 AD2 4 SER B 399 THR B 403 -1 O THR B 403 N LYS B 109
SHEET 3 AD2 4 ILE B 389 SER B 394 -1 N LEU B 390 O TRP B 402
SHEET 4 AD2 4 ILE B 378 TRP B 383 -1 N TRP B 379 O GLY B 393
SHEET 1 AD3 4 VAL B 122 TRP B 127 0
SHEET 2 AD3 4 ARG B 133 ALA B 138 -1 O GLY B 137 N VAL B 124
SHEET 3 AD3 4 THR B 144 ASN B 147 -1 O TRP B 146 N LEU B 134
SHEET 4 AD3 4 THR B 155 ILE B 156 -1 O THR B 155 N LEU B 145
SHEET 1 AD4 4 VAL B 164 TRP B 169 0
SHEET 2 AD4 4 TRP B 175 ASP B 180 -1 O LEU B 177 N THR B 168
SHEET 3 AD4 4 TYR B 184 GLN B 189 -1 O LYS B 186 N THR B 178
SHEET 4 AD4 4 ASN B 194 GLN B 199 -1 O PHE B 198 N VAL B 185
SHEET 1 AD5 4 ILE B 205 PHE B 210 0
SHEET 2 AD5 4 LYS B 216 SER B 221 -1 O CYS B 220 N ARG B 206
SHEET 3 AD5 4 VAL B 226 ASP B 230 -1 O TRP B 229 N PHE B 217
SHEET 4 AD5 4 GLU B 236 LEU B 240 -1 O GLU B 237 N ILE B 228
SHEET 1 AD6 4 VAL B 250 TRP B 252 0
SHEET 2 AD6 4 VAL B 259 SER B 261 -1 O VAL B 260 N ASP B 251
SHEET 3 AD6 4 ILE B 270 PHE B 272 -1 O LYS B 271 N SER B 261
SHEET 4 AD6 4 THR B 283 LEU B 284 -1 O LEU B 284 N ILE B 270
SHEET 1 AD7 4 VAL B 291 LEU B 296 0
SHEET 2 AD7 4 TRP B 302 SER B 307 -1 O LEU B 304 N LYS B 295
SHEET 3 AD7 4 CYS B 312 ASP B 316 -1 O PHE B 315 N LEU B 303
SHEET 4 AD7 4 VAL B 326 PHE B 327 -1 O PHE B 327 N CYS B 312
SHEET 1 AD8 3 ALA B 334 TRP B 339 0
SHEET 2 AD8 3 LEU B 346 GLY B 351 -1 O GLY B 350 N ALA B 336
SHEET 3 AD8 3 LEU B 357 HIS B 360 -1 O LEU B 357 N SER B 349
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
(ATOM LINES ARE NOT SHOWN.)
END
