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HEADER VIRAL PROTEIN 20-SEP-24 9JMM
TITLE CRYO-EM STRUCTURE OF THE SE-PANGOLINCOV (MJHKU4R-COV-1) RBD IN COMPLEX
TITLE 2 WITH HUMAN DPP4
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIPEPTIDYL PEPTIDASE 4 SOLUBLE FORM;
COMPND 3 CHAIN: A, C;
COMPND 4 SYNONYM: DIPEPTIDYL PEPTIDASE IV SOLUBLE FORM;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: SPIKE GLYCOPROTEIN,ISOFORM 1 OF IMMUNOGLOBULIN HEAVY
COMPND 8 CONSTANT GAMMA 1;
COMPND 9 CHAIN: B;
COMPND 10 FRAGMENT: RBD;
COMPND 11 SYNONYM: S GLYCOPROTEIN,E2,PEPLOMER PROTEIN,IG GAMMA-1 CHAIN C
COMPND 12 REGION,IG GAMMA-1 CHAIN C REGION EU,IG GAMMA-1 CHAIN C REGION KOL,IG
COMPND 13 GAMMA-1 CHAIN C REGION NIE;
COMPND 14 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: DPP4, ADCP2, CD26;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: PANGOLIN CORONAVIRUS HKU4/P251T/PANGOLIN/2018,
SOURCE 10 HOMO SAPIENS;
SOURCE 11 ORGANISM_COMMON: HUMAN;
SOURCE 12 ORGANISM_TAXID: 2929177, 9606;
SOURCE 13 GENE: S, IGHG1;
SOURCE 14 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 15 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 9606
KEYWDS COMPLEX, VIRAL PROTEIN
EXPDTA ELECTRON MICROSCOPY
AUTHOR H.YUAN,X.XIONG
REVDAT 1 18-JUN-25 9JMM 0
JRNL AUTH H.YUAN,X.XIONG
JRNL TITL THE COMPLEX OF SE-PANGOLINCOV-RBD AND HUMAN DPP4
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.80 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) : 2.800
REMARK 3 NUMBER OF PARTICLES : 721281
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 9JMM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 29-SEP-24.
REMARK 100 THE DEPOSITION ID IS D_1300048935.
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 : SE-PANGOLINCOV-RBD (MJHKU4R-COV
REMARK 245 -1):HUMAN DPP4 COMPLEX
REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : NULL
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 TALOS ARCTICA
REMARK 245 DETECTOR TYPE : GATAN K3 (6K X 4K)
REMARK 245 MINIMUM DEFOCUS (NM) : 800.00
REMARK 245 MAXIMUM DEFOCUS (NM) : 1600.00
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) : 6000.00
REMARK 245 ILLUMINATION MODE : OTHER
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: TRIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, B, D, E, F, G, H, I, J,
REMARK 350 AND CHAINS: K
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 15
REMARK 465 PRO A 16
REMARK 465 MET A 17
REMARK 465 GLY A 18
REMARK 465 SER A 19
REMARK 465 LEU A 20
REMARK 465 GLN A 21
REMARK 465 PRO A 22
REMARK 465 LEU A 23
REMARK 465 ALA A 24
REMARK 465 THR A 25
REMARK 465 LEU A 26
REMARK 465 TYR A 27
REMARK 465 LEU A 28
REMARK 465 LEU A 29
REMARK 465 GLY A 30
REMARK 465 MET A 31
REMARK 465 LEU A 32
REMARK 465 VAL A 33
REMARK 465 ALA A 34
REMARK 465 SER A 35
REMARK 465 VAL A 36
REMARK 465 LEU A 37
REMARK 465 ALA A 38
REMARK 465 HIS A 767
REMARK 465 HIS A 768
REMARK 465 HIS A 769
REMARK 465 HIS A 770
REMARK 465 HIS A 771
REMARK 465 HIS A 772
REMARK 465 MET C 15
REMARK 465 PRO C 16
REMARK 465 MET C 17
REMARK 465 GLY C 18
REMARK 465 SER C 19
REMARK 465 LEU C 20
REMARK 465 GLN C 21
REMARK 465 PRO C 22
REMARK 465 LEU C 23
REMARK 465 ALA C 24
REMARK 465 THR C 25
REMARK 465 LEU C 26
REMARK 465 TYR C 27
REMARK 465 LEU C 28
REMARK 465 LEU C 29
REMARK 465 GLY C 30
REMARK 465 MET C 31
REMARK 465 LEU C 32
REMARK 465 VAL C 33
REMARK 465 ALA C 34
REMARK 465 SER C 35
REMARK 465 VAL C 36
REMARK 465 LEU C 37
REMARK 465 ALA C 38
REMARK 465 HIS C 767
REMARK 465 HIS C 768
REMARK 465 HIS C 769
REMARK 465 HIS C 770
REMARK 465 HIS C 771
REMARK 465 HIS C 772
REMARK 465 MET B 356
REMARK 465 THR B 357
REMARK 465 CYS B 358
REMARK 465 LEU B 359
REMARK 465 THR B 360
REMARK 465 CYS B 361
REMARK 465 LEU B 362
REMARK 465 LEU B 363
REMARK 465 MET B 364
REMARK 465 PHE B 365
REMARK 465 LEU B 366
REMARK 465 LEU B 367
REMARK 465 MET B 368
REMARK 465 PHE B 369
REMARK 465 VAL B 370
REMARK 465 LYS B 371
REMARK 465 ASP B 372
REMARK 465 CYS B 373
REMARK 465 ASP B 374
REMARK 465 GLU B 375
REMARK 465 ALA B 376
REMARK 465 ALA B 377
REMARK 465 ALA B 378
REMARK 465 THR B 379
REMARK 465 GLY B 380
REMARK 465 THR B 381
REMARK 465 PHE B 382
REMARK 465 ILE B 383
REMARK 465 GLU B 384
REMARK 465 GLN B 385
REMARK 465 PRO B 386
REMARK 465 LYS B 387
REMARK 465 SER B 388
REMARK 465 LYS B 389
REMARK 465 GLU B 390
REMARK 465 THR B 413
REMARK 465 ASN B 414
REMARK 465 CYS B 415
REMARK 465 ASN B 416
REMARK 465 TYR B 417
REMARK 465 TYR B 585
REMARK 465 GLY B 586
REMARK 465 THR B 587
REMARK 465 ASP B 588
REMARK 465 THR B 589
REMARK 465 ASN B 590
REMARK 465 SER B 591
REMARK 465 VAL B 592
REMARK 465 CYS B 593
REMARK 465 PRO B 594
REMARK 465 MET B 595
REMARK 465 LEU B 596
REMARK 465 ASP B 597
REMARK 465 LEU B 598
REMARK 465 GLY B 599
REMARK 465 ASN B 600
REMARK 465 SER B 601
REMARK 465 SER B 602
REMARK 465 THR B 603
REMARK 465 ILE B 604
REMARK 465 THR B 605
REMARK 465 HIS B 606
REMARK 465 TYR B 607
REMARK 465 LEU B 608
REMARK 465 GLY B 609
REMARK 465 LYS B 610
REMARK 465 CYS B 611
REMARK 465 VAL B 612
REMARK 465 ASP B 613
REMARK 465 TYR B 614
REMARK 465 ASP B 615
REMARK 465 PRO B 616
REMARK 465 LEU B 617
REMARK 465 VAL B 618
REMARK 465 PRO B 619
REMARK 465 ARG B 620
REMARK 465 GLY B 621
REMARK 465 SER B 622
REMARK 465 GLY B 623
REMARK 465 GLY B 624
REMARK 465 GLY B 625
REMARK 465 GLY B 626
REMARK 465 ASP B 627
REMARK 465 PRO B 628
REMARK 465 GLU B 629
REMARK 465 PRO B 630
REMARK 465 LYS B 631
REMARK 465 SER B 632
REMARK 465 CYS B 633
REMARK 465 ASP B 634
REMARK 465 LYS B 635
REMARK 465 THR B 636
REMARK 465 HIS B 637
REMARK 465 THR B 638
REMARK 465 CYS B 639
REMARK 465 PRO B 640
REMARK 465 PRO B 641
REMARK 465 CYS B 642
REMARK 465 PRO B 643
REMARK 465 ALA B 644
REMARK 465 PRO B 645
REMARK 465 GLU B 646
REMARK 465 LEU B 647
REMARK 465 LEU B 648
REMARK 465 GLY B 649
REMARK 465 GLY B 650
REMARK 465 PRO B 651
REMARK 465 SER B 652
REMARK 465 VAL B 653
REMARK 465 PHE B 654
REMARK 465 LEU B 655
REMARK 465 PHE B 656
REMARK 465 PRO B 657
REMARK 465 PRO B 658
REMARK 465 LYS B 659
REMARK 465 PRO B 660
REMARK 465 LYS B 661
REMARK 465 ASP B 662
REMARK 465 THR B 663
REMARK 465 LEU B 664
REMARK 465 MET B 665
REMARK 465 ILE B 666
REMARK 465 SER B 667
REMARK 465 ARG B 668
REMARK 465 THR B 669
REMARK 465 PRO B 670
REMARK 465 GLU B 671
REMARK 465 VAL B 672
REMARK 465 THR B 673
REMARK 465 CYS B 674
REMARK 465 VAL B 675
REMARK 465 VAL B 676
REMARK 465 VAL B 677
REMARK 465 ASP B 678
REMARK 465 VAL B 679
REMARK 465 SER B 680
REMARK 465 HIS B 681
REMARK 465 GLU B 682
REMARK 465 ASP B 683
REMARK 465 PRO B 684
REMARK 465 GLU B 685
REMARK 465 VAL B 686
REMARK 465 LYS B 687
REMARK 465 PHE B 688
REMARK 465 ASN B 689
REMARK 465 TRP B 690
REMARK 465 TYR B 691
REMARK 465 VAL B 692
REMARK 465 ASP B 693
REMARK 465 GLY B 694
REMARK 465 VAL B 695
REMARK 465 GLU B 696
REMARK 465 VAL B 697
REMARK 465 HIS B 698
REMARK 465 ASN B 699
REMARK 465 ALA B 700
REMARK 465 LYS B 701
REMARK 465 THR B 702
REMARK 465 LYS B 703
REMARK 465 PRO B 704
REMARK 465 ARG B 705
REMARK 465 GLU B 706
REMARK 465 GLU B 707
REMARK 465 GLN B 708
REMARK 465 TYR B 709
REMARK 465 ASN B 710
REMARK 465 SER B 711
REMARK 465 THR B 712
REMARK 465 TYR B 713
REMARK 465 ARG B 714
REMARK 465 VAL B 715
REMARK 465 VAL B 716
REMARK 465 SER B 717
REMARK 465 VAL B 718
REMARK 465 LEU B 719
REMARK 465 THR B 720
REMARK 465 VAL B 721
REMARK 465 LEU B 722
REMARK 465 HIS B 723
REMARK 465 GLN B 724
REMARK 465 ASP B 725
REMARK 465 TRP B 726
REMARK 465 LEU B 727
REMARK 465 ASN B 728
REMARK 465 GLY B 729
REMARK 465 LYS B 730
REMARK 465 GLU B 731
REMARK 465 TYR B 732
REMARK 465 LYS B 733
REMARK 465 CYS B 734
REMARK 465 LYS B 735
REMARK 465 VAL B 736
REMARK 465 SER B 737
REMARK 465 ASN B 738
REMARK 465 LYS B 739
REMARK 465 ALA B 740
REMARK 465 LEU B 741
REMARK 465 PRO B 742
REMARK 465 ALA B 743
REMARK 465 PRO B 744
REMARK 465 ILE B 745
REMARK 465 GLU B 746
REMARK 465 LYS B 747
REMARK 465 THR B 748
REMARK 465 ILE B 749
REMARK 465 SER B 750
REMARK 465 LYS B 751
REMARK 465 ALA B 752
REMARK 465 LYS B 753
REMARK 465 GLY B 754
REMARK 465 GLN B 755
REMARK 465 PRO B 756
REMARK 465 ARG B 757
REMARK 465 GLU B 758
REMARK 465 PRO B 759
REMARK 465 GLN B 760
REMARK 465 VAL B 761
REMARK 465 TYR B 762
REMARK 465 THR B 763
REMARK 465 LEU B 764
REMARK 465 PRO B 765
REMARK 465 PRO B 766
REMARK 465 SER B 767
REMARK 465 ARG B 768
REMARK 465 ASP B 769
REMARK 465 GLU B 770
REMARK 465 LEU B 771
REMARK 465 THR B 772
REMARK 465 LYS B 773
REMARK 465 ASN B 774
REMARK 465 GLN B 775
REMARK 465 VAL B 776
REMARK 465 SER B 777
REMARK 465 LEU B 778
REMARK 465 THR B 779
REMARK 465 CYS B 780
REMARK 465 LEU B 781
REMARK 465 VAL B 782
REMARK 465 LYS B 783
REMARK 465 GLY B 784
REMARK 465 PHE B 785
REMARK 465 TYR B 786
REMARK 465 PRO B 787
REMARK 465 SER B 788
REMARK 465 ASP B 789
REMARK 465 ILE B 790
REMARK 465 ALA B 791
REMARK 465 VAL B 792
REMARK 465 GLU B 793
REMARK 465 TRP B 794
REMARK 465 GLU B 795
REMARK 465 SER B 796
REMARK 465 ASN B 797
REMARK 465 GLY B 798
REMARK 465 GLN B 799
REMARK 465 PRO B 800
REMARK 465 GLU B 801
REMARK 465 ASN B 802
REMARK 465 ASN B 803
REMARK 465 TYR B 804
REMARK 465 LYS B 805
REMARK 465 THR B 806
REMARK 465 THR B 807
REMARK 465 PRO B 808
REMARK 465 PRO B 809
REMARK 465 VAL B 810
REMARK 465 LEU B 811
REMARK 465 ASP B 812
REMARK 465 SER B 813
REMARK 465 ASP B 814
REMARK 465 GLY B 815
REMARK 465 SER B 816
REMARK 465 PHE B 817
REMARK 465 PHE B 818
REMARK 465 LEU B 819
REMARK 465 TYR B 820
REMARK 465 SER B 821
REMARK 465 LYS B 822
REMARK 465 LEU B 823
REMARK 465 THR B 824
REMARK 465 VAL B 825
REMARK 465 ASP B 826
REMARK 465 LYS B 827
REMARK 465 SER B 828
REMARK 465 ARG B 829
REMARK 465 TRP B 830
REMARK 465 GLN B 831
REMARK 465 GLN B 832
REMARK 465 GLY B 833
REMARK 465 ASN B 834
REMARK 465 VAL B 835
REMARK 465 PHE B 836
REMARK 465 SER B 837
REMARK 465 CYS B 838
REMARK 465 SER B 839
REMARK 465 VAL B 840
REMARK 465 MET B 841
REMARK 465 HIS B 842
REMARK 465 GLU B 843
REMARK 465 ALA B 844
REMARK 465 LEU B 845
REMARK 465 HIS B 846
REMARK 465 ASN B 847
REMARK 465 HIS B 848
REMARK 465 TYR B 849
REMARK 465 THR B 850
REMARK 465 GLN B 851
REMARK 465 LYS B 852
REMARK 465 SER B 853
REMARK 465 LEU B 854
REMARK 465 SER B 855
REMARK 465 LEU B 856
REMARK 465 SER B 857
REMARK 465 PRO B 858
REMARK 465 GLY B 859
REMARK 465 LYS B 860
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 OG SER B 538 O GLY B 541 2.13
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 TRP A 124 -164.77 -125.49
REMARK 500 ILE A 193 -60.15 -123.38
REMARK 500 SER A 242 -156.99 72.86
REMARK 500 THR A 401 46.35 -101.92
REMARK 500 ASP A 413 -2.61 69.55
REMARK 500 ASN A 450 87.86 -154.99
REMARK 500 SER A 630 -108.15 60.16
REMARK 500 ASP A 678 -76.27 -96.11
REMARK 500 ASN A 679 32.45 -146.05
REMARK 500 TRP C 124 -165.31 -124.37
REMARK 500 ILE C 193 -61.60 -122.69
REMARK 500 VAL C 207 -61.92 -96.85
REMARK 500 SER C 242 -160.43 -76.02
REMARK 500 ASP C 243 150.90 -45.41
REMARK 500 ARG C 343 38.84 -97.79
REMARK 500 SER C 446 14.10 -140.23
REMARK 500 ASN C 450 88.77 -153.38
REMARK 500 LEU C 519 -60.09 -99.01
REMARK 500 GLN C 586 29.11 -140.06
REMARK 500 SER C 630 -109.97 60.76
REMARK 500 ASP C 678 -61.40 -95.84
REMARK 500 ASN C 679 30.66 -144.27
REMARK 500 ARG C 691 33.93 -98.23
REMARK 500 ALA C 707 32.03 -97.67
REMARK 500 ASN B 406 51.00 -105.59
REMARK 500 LEU B 419 -99.59 60.10
REMARK 500 ASN B 429 -31.25 -142.61
REMARK 500 ASP B 439 7.68 82.94
REMARK 500 ARG B 443 -120.97 60.22
REMARK 500 PHE B 454 148.10 -175.53
REMARK 500 MET B 460 50.48 -91.11
REMARK 500 CYS B 510 104.22 -160.84
REMARK 500 SER B 514 118.11 -161.90
REMARK 500 ASN B 518 50.44 37.18
REMARK 500 SER B 538 73.57 53.15
REMARK 500 GLU B 544 179.56 60.05
REMARK 500 TYR B 556 -6.25 71.86
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: EMD-61606 RELATED DB: EMDB
REMARK 900 CRYO-EM STRUCTURE OF THE SE-PANGOLINCOV (MJHKU4R-COV-1) RBD IN
REMARK 900 COMPLEX WITH HUMAN DPP4
DBREF 9JMM A 39 766 UNP P27487 DPP4_HUMAN 39 766
DBREF 9JMM C 39 766 UNP P27487 DPP4_HUMAN 39 766
DBREF1 9JMM B 375 614 UNP A0AAE8ZFM2_9BETC
DBREF2 9JMM B A0AAE8ZFM2 375 614
DBREF 9JMM B 629 860 UNP P01857 IGHG1_HUMAN 99 330
SEQADV 9JMM MET A 15 UNP P27487 INITIATING METHIONINE
SEQADV 9JMM PRO A 16 UNP P27487 EXPRESSION TAG
SEQADV 9JMM MET A 17 UNP P27487 EXPRESSION TAG
SEQADV 9JMM GLY A 18 UNP P27487 EXPRESSION TAG
SEQADV 9JMM SER A 19 UNP P27487 EXPRESSION TAG
SEQADV 9JMM LEU A 20 UNP P27487 EXPRESSION TAG
SEQADV 9JMM GLN A 21 UNP P27487 EXPRESSION TAG
SEQADV 9JMM PRO A 22 UNP P27487 EXPRESSION TAG
SEQADV 9JMM LEU A 23 UNP P27487 EXPRESSION TAG
SEQADV 9JMM ALA A 24 UNP P27487 EXPRESSION TAG
SEQADV 9JMM THR A 25 UNP P27487 EXPRESSION TAG
SEQADV 9JMM LEU A 26 UNP P27487 EXPRESSION TAG
SEQADV 9JMM TYR A 27 UNP P27487 EXPRESSION TAG
SEQADV 9JMM LEU A 28 UNP P27487 EXPRESSION TAG
SEQADV 9JMM LEU A 29 UNP P27487 EXPRESSION TAG
SEQADV 9JMM GLY A 30 UNP P27487 EXPRESSION TAG
SEQADV 9JMM MET A 31 UNP P27487 EXPRESSION TAG
SEQADV 9JMM LEU A 32 UNP P27487 EXPRESSION TAG
SEQADV 9JMM VAL A 33 UNP P27487 EXPRESSION TAG
SEQADV 9JMM ALA A 34 UNP P27487 EXPRESSION TAG
SEQADV 9JMM SER A 35 UNP P27487 EXPRESSION TAG
SEQADV 9JMM VAL A 36 UNP P27487 EXPRESSION TAG
SEQADV 9JMM LEU A 37 UNP P27487 EXPRESSION TAG
SEQADV 9JMM ALA A 38 UNP P27487 EXPRESSION TAG
SEQADV 9JMM HIS A 767 UNP P27487 EXPRESSION TAG
SEQADV 9JMM HIS A 768 UNP P27487 EXPRESSION TAG
SEQADV 9JMM HIS A 769 UNP P27487 EXPRESSION TAG
SEQADV 9JMM HIS A 770 UNP P27487 EXPRESSION TAG
SEQADV 9JMM HIS A 771 UNP P27487 EXPRESSION TAG
SEQADV 9JMM HIS A 772 UNP P27487 EXPRESSION TAG
SEQADV 9JMM MET C 15 UNP P27487 INITIATING METHIONINE
SEQADV 9JMM PRO C 16 UNP P27487 EXPRESSION TAG
SEQADV 9JMM MET C 17 UNP P27487 EXPRESSION TAG
SEQADV 9JMM GLY C 18 UNP P27487 EXPRESSION TAG
SEQADV 9JMM SER C 19 UNP P27487 EXPRESSION TAG
SEQADV 9JMM LEU C 20 UNP P27487 EXPRESSION TAG
SEQADV 9JMM GLN C 21 UNP P27487 EXPRESSION TAG
SEQADV 9JMM PRO C 22 UNP P27487 EXPRESSION TAG
SEQADV 9JMM LEU C 23 UNP P27487 EXPRESSION TAG
SEQADV 9JMM ALA C 24 UNP P27487 EXPRESSION TAG
SEQADV 9JMM THR C 25 UNP P27487 EXPRESSION TAG
SEQADV 9JMM LEU C 26 UNP P27487 EXPRESSION TAG
SEQADV 9JMM TYR C 27 UNP P27487 EXPRESSION TAG
SEQADV 9JMM LEU C 28 UNP P27487 EXPRESSION TAG
SEQADV 9JMM LEU C 29 UNP P27487 EXPRESSION TAG
SEQADV 9JMM GLY C 30 UNP P27487 EXPRESSION TAG
SEQADV 9JMM MET C 31 UNP P27487 EXPRESSION TAG
SEQADV 9JMM LEU C 32 UNP P27487 EXPRESSION TAG
SEQADV 9JMM VAL C 33 UNP P27487 EXPRESSION TAG
SEQADV 9JMM ALA C 34 UNP P27487 EXPRESSION TAG
SEQADV 9JMM SER C 35 UNP P27487 EXPRESSION TAG
SEQADV 9JMM VAL C 36 UNP P27487 EXPRESSION TAG
SEQADV 9JMM LEU C 37 UNP P27487 EXPRESSION TAG
SEQADV 9JMM ALA C 38 UNP P27487 EXPRESSION TAG
SEQADV 9JMM HIS C 767 UNP P27487 EXPRESSION TAG
SEQADV 9JMM HIS C 768 UNP P27487 EXPRESSION TAG
SEQADV 9JMM HIS C 769 UNP P27487 EXPRESSION TAG
SEQADV 9JMM HIS C 770 UNP P27487 EXPRESSION TAG
SEQADV 9JMM HIS C 771 UNP P27487 EXPRESSION TAG
SEQADV 9JMM HIS C 772 UNP P27487 EXPRESSION TAG
SEQADV 9JMM MET B 356 UNP A0AAE8ZFM INITIATING METHIONINE
SEQADV 9JMM THR B 357 UNP A0AAE8ZFM EXPRESSION TAG
SEQADV 9JMM CYS B 358 UNP A0AAE8ZFM EXPRESSION TAG
SEQADV 9JMM LEU B 359 UNP A0AAE8ZFM EXPRESSION TAG
SEQADV 9JMM THR B 360 UNP A0AAE8ZFM EXPRESSION TAG
SEQADV 9JMM CYS B 361 UNP A0AAE8ZFM EXPRESSION TAG
SEQADV 9JMM LEU B 362 UNP A0AAE8ZFM EXPRESSION TAG
SEQADV 9JMM LEU B 363 UNP A0AAE8ZFM EXPRESSION TAG
SEQADV 9JMM MET B 364 UNP A0AAE8ZFM EXPRESSION TAG
SEQADV 9JMM PHE B 365 UNP A0AAE8ZFM EXPRESSION TAG
SEQADV 9JMM LEU B 366 UNP A0AAE8ZFM EXPRESSION TAG
SEQADV 9JMM LEU B 367 UNP A0AAE8ZFM EXPRESSION TAG
SEQADV 9JMM MET B 368 UNP A0AAE8ZFM EXPRESSION TAG
SEQADV 9JMM PHE B 369 UNP A0AAE8ZFM EXPRESSION TAG
SEQADV 9JMM VAL B 370 UNP A0AAE8ZFM EXPRESSION TAG
SEQADV 9JMM LYS B 371 UNP A0AAE8ZFM EXPRESSION TAG
SEQADV 9JMM ASP B 372 UNP A0AAE8ZFM EXPRESSION TAG
SEQADV 9JMM CYS B 373 UNP A0AAE8ZFM EXPRESSION TAG
SEQADV 9JMM ASP B 374 UNP A0AAE8ZFM EXPRESSION TAG
SEQADV 9JMM ALA B 482 UNP A0AAE8ZFM SER 482 CONFLICT
SEQADV 9JMM GLU B 544 UNP A0AAE8ZFM VAL 544 CONFLICT
SEQADV 9JMM ASP B 615 UNP A0AAE8ZFM LINKER
SEQADV 9JMM PRO B 616 UNP A0AAE8ZFM LINKER
SEQADV 9JMM LEU B 617 UNP A0AAE8ZFM LINKER
SEQADV 9JMM VAL B 618 UNP A0AAE8ZFM LINKER
SEQADV 9JMM PRO B 619 UNP A0AAE8ZFM LINKER
SEQADV 9JMM ARG B 620 UNP A0AAE8ZFM LINKER
SEQADV 9JMM GLY B 621 UNP A0AAE8ZFM LINKER
SEQADV 9JMM SER B 622 UNP A0AAE8ZFM LINKER
SEQADV 9JMM GLY B 623 UNP A0AAE8ZFM LINKER
SEQADV 9JMM GLY B 624 UNP A0AAE8ZFM LINKER
SEQADV 9JMM GLY B 625 UNP A0AAE8ZFM LINKER
SEQADV 9JMM GLY B 626 UNP A0AAE8ZFM LINKER
SEQADV 9JMM ASP B 627 UNP A0AAE8ZFM LINKER
SEQADV 9JMM PRO B 628 UNP A0AAE8ZFM LINKER
SEQRES 1 A 758 MET PRO MET GLY SER LEU GLN PRO LEU ALA THR LEU TYR
SEQRES 2 A 758 LEU LEU GLY MET LEU VAL ALA SER VAL LEU ALA SER ARG
SEQRES 3 A 758 LYS THR TYR THR LEU THR ASP TYR LEU LYS ASN THR TYR
SEQRES 4 A 758 ARG LEU LYS LEU TYR SER LEU ARG TRP ILE SER ASP HIS
SEQRES 5 A 758 GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU VAL PHE
SEQRES 6 A 758 ASN ALA GLU TYR GLY ASN SER SER VAL PHE LEU GLU ASN
SEQRES 7 A 758 SER THR PHE ASP GLU PHE GLY HIS SER ILE ASN ASP TYR
SEQRES 8 A 758 SER ILE SER PRO ASP GLY GLN PHE ILE LEU LEU GLU TYR
SEQRES 9 A 758 ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR ALA SER
SEQRES 10 A 758 TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU ILE THR
SEQRES 11 A 758 GLU GLU ARG ILE PRO ASN ASN THR GLN TRP VAL THR TRP
SEQRES 12 A 758 SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP ASN ASN
SEQRES 13 A 758 ASP ILE TYR VAL LYS ILE GLU PRO ASN LEU PRO SER TYR
SEQRES 14 A 758 ARG ILE THR TRP THR GLY LYS GLU ASP ILE ILE TYR ASN
SEQRES 15 A 758 GLY ILE THR ASP TRP VAL TYR GLU GLU GLU VAL PHE SER
SEQRES 16 A 758 ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY THR PHE
SEQRES 17 A 758 LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL PRO LEU
SEQRES 18 A 758 ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU GLN TYR
SEQRES 19 A 758 PRO LYS THR VAL ARG VAL PRO TYR PRO LYS ALA GLY ALA
SEQRES 20 A 758 VAL ASN PRO THR VAL LYS PHE PHE VAL VAL ASN THR ASP
SEQRES 21 A 758 SER LEU SER SER VAL THR ASN ALA THR SER ILE GLN ILE
SEQRES 22 A 758 THR ALA PRO ALA SER MET LEU ILE GLY ASP HIS TYR LEU
SEQRES 23 A 758 CYS ASP VAL THR TRP ALA THR GLN GLU ARG ILE SER LEU
SEQRES 24 A 758 GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL MET ASP
SEQRES 25 A 758 ILE CYS ASP TYR ASP GLU SER SER GLY ARG TRP ASN CYS
SEQRES 26 A 758 LEU VAL ALA ARG GLN HIS ILE GLU MET SER THR THR GLY
SEQRES 27 A 758 TRP VAL GLY ARG PHE ARG PRO SER GLU PRO HIS PHE THR
SEQRES 28 A 758 LEU ASP GLY ASN SER PHE TYR LYS ILE ILE SER ASN GLU
SEQRES 29 A 758 GLU GLY TYR ARG HIS ILE CYS TYR PHE GLN ILE ASP LYS
SEQRES 30 A 758 LYS ASP CYS THR PHE ILE THR LYS GLY THR TRP GLU VAL
SEQRES 31 A 758 ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU TYR TYR
SEQRES 32 A 758 ILE SER ASN GLU TYR LYS GLY MET PRO GLY GLY ARG ASN
SEQRES 33 A 758 LEU TYR LYS ILE GLN LEU SER ASP TYR THR LYS VAL THR
SEQRES 34 A 758 CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS GLN TYR
SEQRES 35 A 758 TYR SER VAL SER PHE SER LYS GLU ALA LYS TYR TYR GLN
SEQRES 36 A 758 LEU ARG CYS SER GLY PRO GLY LEU PRO LEU TYR THR LEU
SEQRES 37 A 758 HIS SER SER VAL ASN ASP LYS GLY LEU ARG VAL LEU GLU
SEQRES 38 A 758 ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASN VAL GLN
SEQRES 39 A 758 MET PRO SER LYS LYS LEU ASP PHE ILE ILE LEU ASN GLU
SEQRES 40 A 758 THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO HIS PHE
SEQRES 41 A 758 ASP LYS SER LYS LYS TYR PRO LEU LEU LEU ASP VAL TYR
SEQRES 42 A 758 ALA GLY PRO CYS SER GLN LYS ALA ASP THR VAL PHE ARG
SEQRES 43 A 758 LEU ASN TRP ALA THR TYR LEU ALA SER THR GLU ASN ILE
SEQRES 44 A 758 ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY TYR GLN
SEQRES 45 A 758 GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG LEU GLY
SEQRES 46 A 758 THR PHE GLU VAL GLU ASP GLN ILE GLU ALA ALA ARG GLN
SEQRES 47 A 758 PHE SER LYS MET GLY PHE VAL ASP ASN LYS ARG ILE ALA
SEQRES 48 A 758 ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR SER MET
SEQRES 49 A 758 VAL LEU GLY SER GLY SER GLY VAL PHE LYS CYS GLY ILE
SEQRES 50 A 758 ALA VAL ALA PRO VAL SER ARG TRP GLU TYR TYR ASP SER
SEQRES 51 A 758 VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR PRO GLU
SEQRES 52 A 758 ASP ASN LEU ASP HIS TYR ARG ASN SER THR VAL MET SER
SEQRES 53 A 758 ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU LEU ILE
SEQRES 54 A 758 HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN GLN SER
SEQRES 55 A 758 ALA GLN ILE SER LYS ALA LEU VAL ASP VAL GLY VAL ASP
SEQRES 56 A 758 PHE GLN ALA MET TRP TYR THR ASP GLU ASP HIS GLY ILE
SEQRES 57 A 758 ALA SER SER THR ALA HIS GLN HIS ILE TYR THR HIS MET
SEQRES 58 A 758 SER HIS PHE ILE LYS GLN CYS PHE SER LEU PRO HIS HIS
SEQRES 59 A 758 HIS HIS HIS HIS
SEQRES 1 C 758 MET PRO MET GLY SER LEU GLN PRO LEU ALA THR LEU TYR
SEQRES 2 C 758 LEU LEU GLY MET LEU VAL ALA SER VAL LEU ALA SER ARG
SEQRES 3 C 758 LYS THR TYR THR LEU THR ASP TYR LEU LYS ASN THR TYR
SEQRES 4 C 758 ARG LEU LYS LEU TYR SER LEU ARG TRP ILE SER ASP HIS
SEQRES 5 C 758 GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU VAL PHE
SEQRES 6 C 758 ASN ALA GLU TYR GLY ASN SER SER VAL PHE LEU GLU ASN
SEQRES 7 C 758 SER THR PHE ASP GLU PHE GLY HIS SER ILE ASN ASP TYR
SEQRES 8 C 758 SER ILE SER PRO ASP GLY GLN PHE ILE LEU LEU GLU TYR
SEQRES 9 C 758 ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR ALA SER
SEQRES 10 C 758 TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU ILE THR
SEQRES 11 C 758 GLU GLU ARG ILE PRO ASN ASN THR GLN TRP VAL THR TRP
SEQRES 12 C 758 SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP ASN ASN
SEQRES 13 C 758 ASP ILE TYR VAL LYS ILE GLU PRO ASN LEU PRO SER TYR
SEQRES 14 C 758 ARG ILE THR TRP THR GLY LYS GLU ASP ILE ILE TYR ASN
SEQRES 15 C 758 GLY ILE THR ASP TRP VAL TYR GLU GLU GLU VAL PHE SER
SEQRES 16 C 758 ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY THR PHE
SEQRES 17 C 758 LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL PRO LEU
SEQRES 18 C 758 ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU GLN TYR
SEQRES 19 C 758 PRO LYS THR VAL ARG VAL PRO TYR PRO LYS ALA GLY ALA
SEQRES 20 C 758 VAL ASN PRO THR VAL LYS PHE PHE VAL VAL ASN THR ASP
SEQRES 21 C 758 SER LEU SER SER VAL THR ASN ALA THR SER ILE GLN ILE
SEQRES 22 C 758 THR ALA PRO ALA SER MET LEU ILE GLY ASP HIS TYR LEU
SEQRES 23 C 758 CYS ASP VAL THR TRP ALA THR GLN GLU ARG ILE SER LEU
SEQRES 24 C 758 GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL MET ASP
SEQRES 25 C 758 ILE CYS ASP TYR ASP GLU SER SER GLY ARG TRP ASN CYS
SEQRES 26 C 758 LEU VAL ALA ARG GLN HIS ILE GLU MET SER THR THR GLY
SEQRES 27 C 758 TRP VAL GLY ARG PHE ARG PRO SER GLU PRO HIS PHE THR
SEQRES 28 C 758 LEU ASP GLY ASN SER PHE TYR LYS ILE ILE SER ASN GLU
SEQRES 29 C 758 GLU GLY TYR ARG HIS ILE CYS TYR PHE GLN ILE ASP LYS
SEQRES 30 C 758 LYS ASP CYS THR PHE ILE THR LYS GLY THR TRP GLU VAL
SEQRES 31 C 758 ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU TYR TYR
SEQRES 32 C 758 ILE SER ASN GLU TYR LYS GLY MET PRO GLY GLY ARG ASN
SEQRES 33 C 758 LEU TYR LYS ILE GLN LEU SER ASP TYR THR LYS VAL THR
SEQRES 34 C 758 CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS GLN TYR
SEQRES 35 C 758 TYR SER VAL SER PHE SER LYS GLU ALA LYS TYR TYR GLN
SEQRES 36 C 758 LEU ARG CYS SER GLY PRO GLY LEU PRO LEU TYR THR LEU
SEQRES 37 C 758 HIS SER SER VAL ASN ASP LYS GLY LEU ARG VAL LEU GLU
SEQRES 38 C 758 ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASN VAL GLN
SEQRES 39 C 758 MET PRO SER LYS LYS LEU ASP PHE ILE ILE LEU ASN GLU
SEQRES 40 C 758 THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO HIS PHE
SEQRES 41 C 758 ASP LYS SER LYS LYS TYR PRO LEU LEU LEU ASP VAL TYR
SEQRES 42 C 758 ALA GLY PRO CYS SER GLN LYS ALA ASP THR VAL PHE ARG
SEQRES 43 C 758 LEU ASN TRP ALA THR TYR LEU ALA SER THR GLU ASN ILE
SEQRES 44 C 758 ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY TYR GLN
SEQRES 45 C 758 GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG LEU GLY
SEQRES 46 C 758 THR PHE GLU VAL GLU ASP GLN ILE GLU ALA ALA ARG GLN
SEQRES 47 C 758 PHE SER LYS MET GLY PHE VAL ASP ASN LYS ARG ILE ALA
SEQRES 48 C 758 ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR SER MET
SEQRES 49 C 758 VAL LEU GLY SER GLY SER GLY VAL PHE LYS CYS GLY ILE
SEQRES 50 C 758 ALA VAL ALA PRO VAL SER ARG TRP GLU TYR TYR ASP SER
SEQRES 51 C 758 VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR PRO GLU
SEQRES 52 C 758 ASP ASN LEU ASP HIS TYR ARG ASN SER THR VAL MET SER
SEQRES 53 C 758 ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU LEU ILE
SEQRES 54 C 758 HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN GLN SER
SEQRES 55 C 758 ALA GLN ILE SER LYS ALA LEU VAL ASP VAL GLY VAL ASP
SEQRES 56 C 758 PHE GLN ALA MET TRP TYR THR ASP GLU ASP HIS GLY ILE
SEQRES 57 C 758 ALA SER SER THR ALA HIS GLN HIS ILE TYR THR HIS MET
SEQRES 58 C 758 SER HIS PHE ILE LYS GLN CYS PHE SER LEU PRO HIS HIS
SEQRES 59 C 758 HIS HIS HIS HIS
SEQRES 1 B 505 MET THR CYS LEU THR CYS LEU LEU MET PHE LEU LEU MET
SEQRES 2 B 505 PHE VAL LYS ASP CYS ASP GLU ALA ALA ALA THR GLY THR
SEQRES 3 B 505 PHE ILE GLU GLN PRO LYS SER LYS GLU CYS ASP PHE THR
SEQRES 4 B 505 PRO MET LEU VAL GLY VAL PRO PRO GLN VAL TYR ASN PHE
SEQRES 5 B 505 LYS ARG LEU VAL PHE THR ASN CYS ASN TYR ASN LEU THR
SEQRES 6 B 505 LYS LEU LEU SER LEU PHE MET VAL ASN GLU PHE SER CYS
SEQRES 7 B 505 ASN GLY ILE SER PRO ASP ALA ILE ALA ARG GLY CYS TYR
SEQRES 8 B 505 SER SER LEU THR VAL ASP TYR PHE ALA TYR PRO LEU SER
SEQRES 9 B 505 MET ARG SER TYR ILE GLN PRO GLY SER ALA GLY ASP ILE
SEQRES 10 B 505 SER LEU TYR ASN TYR LYS GLN SER PHE ALA ASN PRO THR
SEQRES 11 B 505 CYS ARG VAL LEU ALA THR ALA PRO ALA ASN LEU THR LEU
SEQRES 12 B 505 THR LYS PRO SER ALA TYR GLY TYR PHE GLN LYS CYS SER
SEQRES 13 B 505 ARG VAL SER GLY GLU HIS ASN SER VAL GLU THR PRO LEU
SEQRES 14 B 505 TYR ILE ASN PRO GLY GLU TYR SER ILE CYS ARG SER PHE
SEQRES 15 B 505 SER PRO TYR GLY PHE SER GLU ASP GLY GLU VAL PHE ARG
SEQRES 16 B 505 ARG GLN LEU THR GLN TYR GLU GLY GLY GLY ILE LEU VAL
SEQRES 17 B 505 GLY VAL GLY ALA LYS LEU ALA MET THR ASP LYS LEU GLU
SEQRES 18 B 505 MET GLY PHE ILE ILE SER VAL GLN TYR GLY THR ASP THR
SEQRES 19 B 505 ASN SER VAL CYS PRO MET LEU ASP LEU GLY ASN SER SER
SEQRES 20 B 505 THR ILE THR HIS TYR LEU GLY LYS CYS VAL ASP TYR ASP
SEQRES 21 B 505 PRO LEU VAL PRO ARG GLY SER GLY GLY GLY GLY ASP PRO
SEQRES 22 B 505 GLU PRO LYS SER CYS ASP LYS THR HIS THR CYS PRO PRO
SEQRES 23 B 505 CYS PRO ALA PRO GLU LEU LEU GLY GLY PRO SER VAL PHE
SEQRES 24 B 505 LEU PHE PRO PRO LYS PRO LYS ASP THR LEU MET ILE SER
SEQRES 25 B 505 ARG THR PRO GLU VAL THR CYS VAL VAL VAL ASP VAL SER
SEQRES 26 B 505 HIS GLU ASP PRO GLU VAL LYS PHE ASN TRP TYR VAL ASP
SEQRES 27 B 505 GLY VAL GLU VAL HIS ASN ALA LYS THR LYS PRO ARG GLU
SEQRES 28 B 505 GLU GLN TYR ASN SER THR TYR ARG VAL VAL SER VAL LEU
SEQRES 29 B 505 THR VAL LEU HIS GLN ASP TRP LEU ASN GLY LYS GLU TYR
SEQRES 30 B 505 LYS CYS LYS VAL SER ASN LYS ALA LEU PRO ALA PRO ILE
SEQRES 31 B 505 GLU LYS THR ILE SER LYS ALA LYS GLY GLN PRO ARG GLU
SEQRES 32 B 505 PRO GLN VAL TYR THR LEU PRO PRO SER ARG ASP GLU LEU
SEQRES 33 B 505 THR LYS ASN GLN VAL SER LEU THR CYS LEU VAL LYS GLY
SEQRES 34 B 505 PHE TYR PRO SER ASP ILE ALA VAL GLU TRP GLU SER ASN
SEQRES 35 B 505 GLY GLN PRO GLU ASN ASN TYR LYS THR THR PRO PRO VAL
SEQRES 36 B 505 LEU ASP SER ASP GLY SER PHE PHE LEU TYR SER LYS LEU
SEQRES 37 B 505 THR VAL ASP LYS SER ARG TRP GLN GLN GLY ASN VAL PHE
SEQRES 38 B 505 SER CYS SER VAL MET HIS GLU ALA LEU HIS ASN HIS TYR
SEQRES 39 B 505 THR GLN LYS SER LEU SER LEU SER PRO GLY LYS
HET NAG D 1 14
HET NAG D 2 14
HET BMA D 3 11
HET MAN D 4 11
HET MAN D 5 11
HET NAG E 1 14
HET NAG E 2 14
HET NAG F 1 14
HET NAG F 2 14
HET NAG G 1 14
HET NAG G 2 14
HET NAG H 1 14
HET NAG H 2 14
HET NAG I 1 14
HET NAG I 2 14
HET NAG J 1 14
HET NAG J 2 14
HET NAG K 1 14
HET NAG K 2 14
HET NAG A 801 14
HET NAG A 802 14
HET NAG A 803 14
HET NAG A 804 14
HET NAG C 801 14
HET NAG C 802 14
HET NAG C 803 14
HET NAG C 804 14
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM BMA BETA-D-MANNOPYRANOSE
HETNAM MAN ALPHA-D-MANNOPYRANOSE
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
HETSYN BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE
HETSYN MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE
FORMUL 4 NAG 24(C8 H15 N O6)
FORMUL 4 BMA C6 H12 O6
FORMUL 4 MAN 2(C6 H12 O6)
HELIX 1 AA1 THR A 44 LYS A 50 1 7
HELIX 2 AA2 GLU A 91 GLU A 97 1 7
HELIX 3 AA3 ASP A 200 VAL A 207 1 8
HELIX 4 AA4 ASP A 274 LEU A 276 5 3
HELIX 5 AA5 PRO A 290 ILE A 295 1 6
HELIX 6 AA6 VAL A 341 GLN A 344 5 4
HELIX 7 AA7 GLU A 421 MET A 425 5 5
HELIX 8 AA8 ASN A 497 LEU A 504 1 8
HELIX 9 AA9 ASN A 562 THR A 570 1 9
HELIX 10 AB1 GLY A 587 HIS A 592 1 6
HELIX 11 AB2 ALA A 593 ASN A 595 5 3
HELIX 12 AB3 THR A 600 GLY A 617 1 18
HELIX 13 AB4 SER A 630 GLY A 641 1 12
HELIX 14 AB5 ASP A 663 MET A 671 1 9
HELIX 15 AB6 ASN A 679 SER A 686 1 8
HELIX 16 AB7 VAL A 688 VAL A 698 5 11
HELIX 17 AB8 HIS A 712 GLY A 727 1 16
HELIX 18 AB9 SER A 744 SER A 764 1 21
HELIX 19 AC1 THR C 44 LYS C 50 1 7
HELIX 20 AC2 GLU C 91 PHE C 98 1 8
HELIX 21 AC3 ASP C 200 VAL C 207 1 8
HELIX 22 AC4 ASP C 274 LEU C 276 5 3
HELIX 23 AC5 PRO C 290 ILE C 295 1 6
HELIX 24 AC6 GLU C 421 MET C 425 5 5
HELIX 25 AC7 ASN C 497 GLN C 505 1 9
HELIX 26 AC8 ASN C 562 THR C 570 1 9
HELIX 27 AC9 GLY C 587 HIS C 592 1 6
HELIX 28 AD1 ALA C 593 ASN C 595 5 3
HELIX 29 AD2 THR C 600 GLY C 617 1 18
HELIX 30 AD3 SER C 630 GLY C 641 1 12
HELIX 31 AD4 ASP C 663 MET C 671 1 9
HELIX 32 AD5 ASN C 679 SER C 686 1 8
HELIX 33 AD6 VAL C 688 VAL C 698 5 11
HELIX 34 AD7 PHE C 713 GLY C 727 1 15
HELIX 35 AD8 SER C 745 PHE C 763 1 19
HELIX 36 AD9 PHE B 393 VAL B 398 1 6
HELIX 37 AE1 LYS B 421 LEU B 425 5 5
HELIX 38 AE2 ALA B 442 TYR B 446 5 5
HELIX 39 AE3 GLY B 470 ASN B 476 1 7
HELIX 40 AE4 SER B 532 PHE B 537 5 6
SHEET 1 AA1 2 LYS A 41 THR A 42 0
SHEET 2 AA1 2 VAL A 507 GLN A 508 1 O GLN A 508 N LYS A 41
SHEET 1 AA2 4 LEU A 60 TRP A 62 0
SHEET 2 AA2 4 GLU A 67 GLN A 72 -1 O LEU A 69 N ARG A 61
SHEET 3 AA2 4 ASN A 75 ASN A 80 -1 O PHE A 79 N TYR A 68
SHEET 4 AA2 4 SER A 86 LEU A 90 -1 O SER A 87 N VAL A 78
SHEET 1 AA3 4 ASP A 104 ILE A 107 0
SHEET 2 AA3 4 PHE A 113 LYS A 122 -1 O GLU A 117 N ASP A 104
SHEET 3 AA3 4 TYR A 128 ASP A 136 -1 O SER A 131 N TYR A 118
SHEET 4 AA3 4 GLN A 141 LEU A 142 -1 O GLN A 141 N ASP A 136
SHEET 1 AA4 4 TRP A 154 TRP A 157 0
SHEET 2 AA4 4 LEU A 164 TRP A 168 -1 O VAL A 167 N TRP A 154
SHEET 3 AA4 4 ASP A 171 LYS A 175 -1 O LYS A 175 N LEU A 164
SHEET 4 AA4 4 TYR A 183 ARG A 184 -1 O TYR A 183 N VAL A 174
SHEET 1 AA5 3 ILE A 194 ASN A 196 0
SHEET 2 AA5 3 PHE A 222 ASN A 229 -1 O PHE A 228 N TYR A 195
SHEET 3 AA5 3 LEU A 214 TRP A 216 -1 N TRP A 215 O ALA A 224
SHEET 1 AA6 4 ILE A 194 ASN A 196 0
SHEET 2 AA6 4 PHE A 222 ASN A 229 -1 O PHE A 228 N TYR A 195
SHEET 3 AA6 4 THR A 265 ASN A 272 -1 O PHE A 269 N TYR A 225
SHEET 4 AA6 4 SER A 284 ILE A 287 -1 O ILE A 285 N VAL A 270
SHEET 1 AA7 2 LEU A 235 PHE A 240 0
SHEET 2 AA7 2 LYS A 250 PRO A 255 -1 O LYS A 250 N PHE A 240
SHEET 1 AA8 4 HIS A 298 THR A 307 0
SHEET 2 AA8 4 ARG A 310 ARG A 317 -1 O LEU A 316 N TYR A 299
SHEET 3 AA8 4 TYR A 322 ASP A 331 -1 O ASP A 326 N LEU A 313
SHEET 4 AA8 4 ARG A 336 CYS A 339 -1 O ARG A 336 N ASP A 331
SHEET 1 AA9 4 HIS A 298 THR A 307 0
SHEET 2 AA9 4 ARG A 310 ARG A 317 -1 O LEU A 316 N TYR A 299
SHEET 3 AA9 4 TYR A 322 ASP A 331 -1 O ASP A 326 N LEU A 313
SHEET 4 AA9 4 HIS A 345 MET A 348 -1 O GLU A 347 N SER A 323
SHEET 1 AB1 4 HIS A 363 PHE A 364 0
SHEET 2 AB1 4 SER A 370 SER A 376 -1 O TYR A 372 N HIS A 363
SHEET 3 AB1 4 ARG A 382 GLN A 388 -1 O CYS A 385 N LYS A 373
SHEET 4 AB1 4 LYS A 391 PHE A 396 -1 O THR A 395 N TYR A 386
SHEET 1 AB2 4 VAL A 404 THR A 411 0
SHEET 2 AB2 4 TYR A 414 SER A 419 -1 O TYR A 416 N ALA A 409
SHEET 3 AB2 4 ASN A 430 GLN A 435 -1 O TYR A 432 N TYR A 417
SHEET 4 AB2 4 VAL A 442 CYS A 444 -1 O THR A 443 N LYS A 433
SHEET 1 AB3 4 TYR A 457 PHE A 461 0
SHEET 2 AB3 4 TYR A 467 CYS A 472 -1 O ARG A 471 N SER A 458
SHEET 3 AB3 4 LEU A 479 SER A 484 -1 O LEU A 479 N CYS A 472
SHEET 4 AB3 4 LYS A 489 GLU A 495 -1 O LEU A 491 N LEU A 482
SHEET 1 AB4 8 SER A 511 ILE A 518 0
SHEET 2 AB4 8 LYS A 523 LEU A 530 -1 O LEU A 530 N SER A 511
SHEET 3 AB4 8 ILE A 574 PHE A 578 -1 O VAL A 575 N ILE A 529
SHEET 4 AB4 8 TYR A 540 VAL A 546 1 N LEU A 543 O ILE A 574
SHEET 5 AB4 8 VAL A 619 TRP A 629 1 O ALA A 625 N LEU A 544
SHEET 6 AB4 8 CYS A 649 VAL A 653 1 O VAL A 653 N GLY A 628
SHEET 7 AB4 8 GLU A 699 GLY A 705 1 O LEU A 701 N ALA A 652
SHEET 8 AB4 8 GLN A 731 TYR A 735 1 O GLN A 731 N LEU A 702
SHEET 1 AB5 3 GLU C 67 GLN C 72 0
SHEET 2 AB5 3 ASN C 75 ASN C 80 -1 O LEU C 77 N TYR C 70
SHEET 3 AB5 3 GLY C 84 VAL C 88 -1 O SER C 87 N VAL C 78
SHEET 1 AB6 4 ASP C 104 ILE C 107 0
SHEET 2 AB6 4 PHE C 113 LYS C 122 -1 O LEU C 115 N SER C 106
SHEET 3 AB6 4 TYR C 128 ASP C 136 -1 O ASP C 133 N LEU C 116
SHEET 4 AB6 4 GLN C 141 LEU C 142 -1 O GLN C 141 N ASP C 136
SHEET 1 AB7 4 TRP C 154 TRP C 157 0
SHEET 2 AB7 4 LEU C 164 TRP C 168 -1 O VAL C 167 N TRP C 154
SHEET 3 AB7 4 ASP C 171 LYS C 175 -1 O LYS C 175 N LEU C 164
SHEET 4 AB7 4 TYR C 183 ARG C 184 -1 O TYR C 183 N VAL C 174
SHEET 1 AB8 3 ILE C 194 ASN C 196 0
SHEET 2 AB8 3 PHE C 222 ASN C 229 -1 O PHE C 228 N TYR C 195
SHEET 3 AB8 3 LEU C 214 TRP C 216 -1 N TRP C 215 O ALA C 224
SHEET 1 AB9 4 ILE C 194 ASN C 196 0
SHEET 2 AB9 4 PHE C 222 ASN C 229 -1 O PHE C 228 N TYR C 195
SHEET 3 AB9 4 THR C 265 ASN C 272 -1 O LYS C 267 N GLN C 227
SHEET 4 AB9 4 SER C 284 ILE C 287 -1 O ILE C 287 N PHE C 268
SHEET 1 AC1 2 LEU C 235 PHE C 240 0
SHEET 2 AC1 2 LYS C 250 PRO C 255 -1 O LYS C 250 N PHE C 240
SHEET 1 AC2 4 HIS C 298 THR C 307 0
SHEET 2 AC2 4 ARG C 310 ARG C 317 -1 O SER C 312 N THR C 304
SHEET 3 AC2 4 TYR C 322 ASP C 331 -1 O ASP C 326 N LEU C 313
SHEET 4 AC2 4 ARG C 336 MET C 348 -1 O HIS C 345 N MET C 325
SHEET 1 AC3 4 HIS C 363 PHE C 364 0
SHEET 2 AC3 4 SER C 370 SER C 376 -1 O TYR C 372 N HIS C 363
SHEET 3 AC3 4 ARG C 382 GLN C 388 -1 O CYS C 385 N LYS C 373
SHEET 4 AC3 4 THR C 395 PHE C 396 -1 O THR C 395 N TYR C 386
SHEET 1 AC4 4 VAL C 404 LEU C 410 0
SHEET 2 AC4 4 TYR C 414 SER C 419 -1 O ILE C 418 N ILE C 405
SHEET 3 AC4 4 ASN C 430 GLN C 435 -1 O TYR C 432 N TYR C 417
SHEET 4 AC4 4 VAL C 442 CYS C 444 -1 O THR C 443 N LYS C 433
SHEET 1 AC5 4 TYR C 457 PHE C 461 0
SHEET 2 AC5 4 TYR C 467 CYS C 472 -1 O GLN C 469 N SER C 460
SHEET 3 AC5 4 LEU C 479 SER C 484 -1 O LEU C 479 N CYS C 472
SHEET 4 AC5 4 LYS C 489 GLU C 495 -1 O GLU C 495 N TYR C 480
SHEET 1 AC6 8 SER C 511 ILE C 518 0
SHEET 2 AC6 8 LYS C 523 LEU C 530 -1 O LEU C 530 N SER C 511
SHEET 3 AC6 8 ILE C 574 PHE C 578 -1 O VAL C 575 N ILE C 529
SHEET 4 AC6 8 TYR C 540 VAL C 546 1 N LEU C 543 O ILE C 574
SHEET 5 AC6 8 VAL C 619 TRP C 629 1 O ASP C 620 N TYR C 540
SHEET 6 AC6 8 CYS C 649 VAL C 653 1 O VAL C 653 N GLY C 628
SHEET 7 AC6 8 GLU C 699 GLY C 705 1 O LEU C 701 N ALA C 652
SHEET 8 AC6 8 GLN C 731 TYR C 735 1 O GLN C 731 N TYR C 700
SHEET 1 AC7 3 LYS B 408 PHE B 412 0
SHEET 2 AC7 3 SER B 448 ALA B 455 -1 O LEU B 449 N PHE B 412
SHEET 3 AC7 3 MET B 577 GLN B 584 -1 O GLY B 578 N PHE B 454
SHEET 1 AC8 4 GLU B 521 PRO B 523 0
SHEET 2 AC8 4 ALA B 503 VAL B 513 -1 N ARG B 512 O THR B 522
SHEET 3 AC8 4 ILE B 561 ALA B 570 -1 O ALA B 567 N TYR B 506
SHEET 4 AC8 4 GLU B 547 GLN B 552 -1 N PHE B 549 O GLY B 564
SSBOND 1 CYS A 328 CYS A 339 1555 1555 2.03
SSBOND 2 CYS A 385 CYS A 394 1555 1555 2.03
SSBOND 3 CYS A 444 CYS A 447 1555 1555 2.03
SSBOND 4 CYS A 454 CYS A 472 1555 1555 2.03
SSBOND 5 CYS A 649 CYS A 762 1555 1555 2.03
SSBOND 6 CYS C 328 CYS C 339 1555 1555 2.03
SSBOND 7 CYS C 385 CYS C 394 1555 1555 2.02
SSBOND 8 CYS C 444 CYS C 447 1555 1555 2.03
SSBOND 9 CYS C 454 CYS C 472 1555 1555 2.03
SSBOND 10 CYS C 649 CYS C 762 1555 1555 2.03
SSBOND 11 CYS B 433 CYS B 486 1555 1555 2.04
SSBOND 12 CYS B 510 CYS B 534 1555 1555 2.03
LINK ND2 ASN A 85 C1 NAG A 802 1555 1555 1.44
LINK ND2 ASN A 92 C1 NAG A 801 1555 1555 1.44
LINK ND2 ASN A 150 C1 NAG A 803 1555 1555 1.44
LINK ND2 ASN A 219 C1 NAG F 1 1555 1555 1.44
LINK ND2 ASN A 229 C1 NAG D 1 1555 1555 1.44
LINK ND2 ASN A 281 C1 NAG G 1 1555 1555 1.44
LINK ND2 ASN A 321 C1 NAG E 1 1555 1555 1.44
LINK ND2 ASN A 685 C1 NAG A 804 1555 1555 1.45
LINK ND2 ASN C 85 C1 NAG C 802 1555 1555 1.44
LINK ND2 ASN C 92 C1 NAG C 801 1555 1555 1.44
LINK ND2 ASN C 150 C1 NAG C 804 1555 1555 1.44
LINK ND2 ASN C 219 C1 NAG H 1 1555 1555 1.44
LINK ND2 ASN C 229 C1 NAG I 1 1555 1555 1.44
LINK ND2 ASN C 281 C1 NAG J 1 1555 1555 1.44
LINK ND2 ASN C 321 C1 NAG K 1 1555 1555 1.44
LINK ND2 ASN C 685 C1 NAG C 803 1555 1555 1.44
LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.44
LINK O4 NAG D 2 C1 BMA D 3 1555 1555 1.44
LINK O3 BMA D 3 C1 MAN D 4 1555 1555 1.44
LINK O2 MAN D 4 C1 MAN D 5 1555 1555 1.45
LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.44
LINK O4 NAG F 1 C1 NAG F 2 1555 1555 1.44
LINK O4 NAG G 1 C1 NAG G 2 1555 1555 1.44
LINK O4 NAG H 1 C1 NAG H 2 1555 1555 1.44
LINK O4 NAG I 1 C1 NAG I 2 1555 1555 1.44
LINK O4 NAG J 1 C1 NAG J 2 1555 1555 1.44
LINK O4 NAG K 1 C1 NAG K 2 1555 1555 1.44
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
TER 5964 PRO A 766
TER 11928 PRO C 766
TER 13395 GLN B 584
MASTER 547 0 27 40 102 0 0 613761 3 409 157
END |