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HEADER MEMBRANE PROTEIN 16-FEB-23 8G7D
TITLE CRYO-EM STRUCTURE OF FULL LENGTH NEUROLIGIN-2 FROM MOUSE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NEUROLIGIN-1,NEUROLIGIN-2;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: NLGN1, KIAA1070, NLGN2, KIAA1366;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606
KEYWDS NEUROLIGIN-2, MEMBRANE PROTEIN
EXPDTA ELECTRON MICROSCOPY
AUTHOR R.BOYD,W.WANG
REVDAT 1 14-MAY-25 8G7D 0
JRNL AUTH R.BOYD,W.WANG
JRNL TITL CRYO-EM STRUCTURE OF FULL LENGTH MOUSE NEUROLIGIN-2 AT 3.28
JRNL TITL 2 ANGSTROMS RESOLUTION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 3.28 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 SOFTWARE PACKAGES : RELION, SERIALEM, CTFFIND, UCSF
REMARK 3 CHIMERA, RELION, CRYOSPARC, CRYOSPARC,
REMARK 3 CRYOSPARC, PHENIX
REMARK 3 RECONSTRUCTION SCHEMA : BACK PROJECTION
REMARK 3
REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT
REMARK 3 PDB ENTRY : 3BL8
REMARK 3 REFINEMENT SPACE : REAL
REMARK 3 REFINEMENT PROTOCOL : RIGID BODY FIT
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) : 3.280
REMARK 3 NUMBER OF PARTICLES : 77577
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 8G7D COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-FEB-23.
REMARK 100 THE DEPOSITION ID IS D_1000272083.
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 : NEUROLIGIN-2 DIMER
REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 5.20
REMARK 245 SAMPLE SUPPORT DETAILS : NULL
REMARK 245 SAMPLE VITRIFICATION DETAILS : BLOT FORCE 20, BLOT TIME 5S,
REMARK 245 SINGLE BLOT
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 : 4989
REMARK 245 TEMPERATURE (KELVIN) : NULL
REMARK 245 MICROSCOPE MODEL : FEI TITAN
REMARK 245 DETECTOR TYPE : GATAN K3 (6K X 4K)
REMARK 245 MINIMUM DEFOCUS (NM) : 1000.00
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 : 0.00
REMARK 245 IMAGING MODE : BRIGHT FIELD
REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 9000.00
REMARK 245 ILLUMINATION MODE : FLOOD BEAM
REMARK 245 NOMINAL MAGNIFICATION : 105000
REMARK 245 CALIBRATED MAGNIFICATION : 105000
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 MET A -41
REMARK 465 ALA A -40
REMARK 465 LEU A -39
REMARK 465 PRO A -38
REMARK 465 ARG A -37
REMARK 465 CYS A -36
REMARK 465 MET A -35
REMARK 465 TRP A -34
REMARK 465 PRO A -33
REMARK 465 ASN A -32
REMARK 465 TYR A -31
REMARK 465 VAL A -30
REMARK 465 TRP A -29
REMARK 465 ARG A -28
REMARK 465 ALA A -27
REMARK 465 MET A -26
REMARK 465 MET A -25
REMARK 465 ALA A -24
REMARK 465 CYS A -23
REMARK 465 VAL A -22
REMARK 465 VAL A -21
REMARK 465 HIS A -20
REMARK 465 ARG A -19
REMARK 465 GLY A -18
REMARK 465 SER A -17
REMARK 465 GLY A -16
REMARK 465 ALA A -15
REMARK 465 PRO A -14
REMARK 465 LEU A -13
REMARK 465 THR A -12
REMARK 465 LEU A -11
REMARK 465 CYS A -10
REMARK 465 LEU A -9
REMARK 465 LEU A -8
REMARK 465 GLY A -7
REMARK 465 CYS A -6
REMARK 465 LEU A -5
REMARK 465 LEU A -4
REMARK 465 GLN A -3
REMARK 465 THR A -2
REMARK 465 PHE A -1
REMARK 465 HIS A 0
REMARK 465 VAL A 1
REMARK 465 LEU A 2
REMARK 465 SER A 3
REMARK 465 GLN A 4
REMARK 465 LYS A 5
REMARK 465 TYR A 6
REMARK 465 PRO A 7
REMARK 465 TYR A 8
REMARK 465 ASP A 9
REMARK 465 VAL A 10
REMARK 465 PRO A 11
REMARK 465 ASP A 12
REMARK 465 TYR A 13
REMARK 465 ALA A 14
REMARK 465 GLN A 15
REMARK 465 ARG A 16
REMARK 465 GLY A 17
REMARK 465 GLY A 18
REMARK 465 GLY A 19
REMARK 465 GLY A 20
REMARK 465 PRO A 21
REMARK 465 GLY A 22
REMARK 465 GLY A 23
REMARK 465 GLY A 24
REMARK 465 ALA A 25
REMARK 465 PRO A 26
REMARK 465 GLY A 27
REMARK 465 GLY A 28
REMARK 465 PRO A 29
REMARK 465 GLY A 30
REMARK 465 LEU A 31
REMARK 465 GLY A 32
REMARK 465 LEU A 33
REMARK 465 GLY A 34
REMARK 465 SER A 35
REMARK 465 LEU A 36
REMARK 465 GLY A 37
REMARK 465 GLU A 38
REMARK 465 GLU A 39
REMARK 465 GLU A 151
REMARK 465 ASP A 152
REMARK 465 ASP A 170
REMARK 465 ILE A 171
REMARK 465 ARG A 172
REMARK 465 ASP A 173
REMARK 465 SER A 174
REMARK 465 ASP A 554
REMARK 465 THR A 555
REMARK 465 LYS A 556
REMARK 465 PHE A 557
REMARK 465 ILE A 558
REMARK 465 HIS A 559
REMARK 465 THR A 560
REMARK 465 LYS A 561
REMARK 465 PRO A 562
REMARK 465 ASN A 563
REMARK 465 HIS A 609
REMARK 465 ASN A 610
REMARK 465 LEU A 611
REMARK 465 HIS A 612
REMARK 465 THR A 613
REMARK 465 GLU A 614
REMARK 465 LEU A 615
REMARK 465 PHE A 616
REMARK 465 THR A 617
REMARK 465 THR A 618
REMARK 465 THR A 619
REMARK 465 THR A 620
REMARK 465 ARG A 621
REMARK 465 LEU A 622
REMARK 465 PRO A 623
REMARK 465 PRO A 624
REMARK 465 TYR A 625
REMARK 465 ALA A 626
REMARK 465 THR A 627
REMARK 465 ARG A 628
REMARK 465 TRP A 629
REMARK 465 PRO A 630
REMARK 465 PRO A 631
REMARK 465 ARG A 632
REMARK 465 THR A 633
REMARK 465 PRO A 634
REMARK 465 GLY A 635
REMARK 465 PRO A 636
REMARK 465 GLY A 637
REMARK 465 THR A 638
REMARK 465 SER A 639
REMARK 465 GLY A 640
REMARK 465 THR A 641
REMARK 465 ARG A 642
REMARK 465 ARG A 643
REMARK 465 PRO A 644
REMARK 465 PRO A 645
REMARK 465 PRO A 646
REMARK 465 PRO A 647
REMARK 465 ALA A 648
REMARK 465 THR A 649
REMARK 465 LEU A 650
REMARK 465 PRO A 651
REMARK 465 PRO A 652
REMARK 465 GLU A 653
REMARK 465 SER A 654
REMARK 465 ASP A 655
REMARK 465 ILE A 656
REMARK 465 ASP A 657
REMARK 465 LEU A 658
REMARK 465 GLY A 659
REMARK 465 PRO A 660
REMARK 465 ARG A 661
REMARK 465 ALA A 662
REMARK 465 TYR A 663
REMARK 465 ASP A 664
REMARK 465 ARG A 665
REMARK 465 PHE A 666
REMARK 465 PRO A 667
REMARK 465 GLY A 668
REMARK 465 ASP A 669
REMARK 465 SER A 670
REMARK 465 ARG A 671
REMARK 465 ASP A 672
REMARK 465 TYR A 673
REMARK 465 SER A 674
REMARK 465 THR A 675
REMARK 465 GLU A 676
REMARK 465 LEU A 677
REMARK 465 SER A 678
REMARK 465 VAL A 679
REMARK 465 THR A 680
REMARK 465 VAL A 681
REMARK 465 ALA A 682
REMARK 465 VAL A 683
REMARK 465 GLY A 684
REMARK 465 ALA A 685
REMARK 465 SER A 686
REMARK 465 LEU A 687
REMARK 465 LEU A 688
REMARK 465 PHE A 689
REMARK 465 LEU A 690
REMARK 465 ASN A 691
REMARK 465 ILE A 692
REMARK 465 LEU A 693
REMARK 465 ALA A 694
REMARK 465 PHE A 695
REMARK 465 ALA A 696
REMARK 465 ALA A 697
REMARK 465 LEU A 698
REMARK 465 TYR A 699
REMARK 465 TYR A 700
REMARK 465 LYS A 701
REMARK 465 ARG A 702
REMARK 465 ASP A 703
REMARK 465 ARG A 704
REMARK 465 ARG A 705
REMARK 465 GLN A 706
REMARK 465 GLU A 707
REMARK 465 LEU A 708
REMARK 465 ARG A 709
REMARK 465 CYS A 710
REMARK 465 ARG A 711
REMARK 465 ARG A 712
REMARK 465 LEU A 713
REMARK 465 SER A 714
REMARK 465 PRO A 715
REMARK 465 PRO A 716
REMARK 465 GLY A 717
REMARK 465 GLY A 718
REMARK 465 SER A 719
REMARK 465 GLY A 720
REMARK 465 SER A 721
REMARK 465 GLY A 722
REMARK 465 VAL A 723
REMARK 465 PRO A 724
REMARK 465 GLY A 725
REMARK 465 GLY A 726
REMARK 465 GLY A 727
REMARK 465 PRO A 728
REMARK 465 LEU A 729
REMARK 465 LEU A 730
REMARK 465 PRO A 731
REMARK 465 THR A 732
REMARK 465 ALA A 733
REMARK 465 GLY A 734
REMARK 465 ARG A 735
REMARK 465 GLU A 736
REMARK 465 LEU A 737
REMARK 465 PRO A 738
REMARK 465 PRO A 739
REMARK 465 GLU A 740
REMARK 465 GLU A 741
REMARK 465 GLU A 742
REMARK 465 LEU A 743
REMARK 465 VAL A 744
REMARK 465 SER A 745
REMARK 465 LEU A 746
REMARK 465 GLN A 747
REMARK 465 LEU A 748
REMARK 465 LYS A 749
REMARK 465 ARG A 750
REMARK 465 GLY A 751
REMARK 465 GLY A 752
REMARK 465 GLY A 753
REMARK 465 VAL A 754
REMARK 465 GLY A 755
REMARK 465 ALA A 756
REMARK 465 ASP A 757
REMARK 465 PRO A 758
REMARK 465 ALA A 759
REMARK 465 GLU A 760
REMARK 465 ALA A 761
REMARK 465 LEU A 762
REMARK 465 ARG A 763
REMARK 465 PRO A 764
REMARK 465 ALA A 765
REMARK 465 CYS A 766
REMARK 465 PRO A 767
REMARK 465 PRO A 768
REMARK 465 ASP A 769
REMARK 465 TYR A 770
REMARK 465 THR A 771
REMARK 465 LEU A 772
REMARK 465 ALA A 773
REMARK 465 LEU A 774
REMARK 465 ARG A 775
REMARK 465 ARG A 776
REMARK 465 ALA A 777
REMARK 465 PRO A 778
REMARK 465 ASP A 779
REMARK 465 ASP A 780
REMARK 465 VAL A 781
REMARK 465 PRO A 782
REMARK 465 LEU A 783
REMARK 465 LEU A 784
REMARK 465 ALA A 785
REMARK 465 PRO A 786
REMARK 465 GLY A 787
REMARK 465 ALA A 788
REMARK 465 LEU A 789
REMARK 465 THR A 790
REMARK 465 LEU A 791
REMARK 465 LEU A 792
REMARK 465 PRO A 793
REMARK 465 SER A 794
REMARK 465 GLY A 795
REMARK 465 LEU A 796
REMARK 465 GLY A 797
REMARK 465 PRO A 798
REMARK 465 PRO A 799
REMARK 465 PRO A 800
REMARK 465 PRO A 801
REMARK 465 PRO A 802
REMARK 465 PRO A 803
REMARK 465 PRO A 804
REMARK 465 PRO A 805
REMARK 465 SER A 806
REMARK 465 LEU A 807
REMARK 465 HIS A 808
REMARK 465 PRO A 809
REMARK 465 PHE A 810
REMARK 465 GLY A 811
REMARK 465 PRO A 812
REMARK 465 PHE A 813
REMARK 465 PRO A 814
REMARK 465 PRO A 815
REMARK 465 PRO A 816
REMARK 465 PRO A 817
REMARK 465 PRO A 818
REMARK 465 THR A 819
REMARK 465 ALA A 820
REMARK 465 THR A 821
REMARK 465 SER A 822
REMARK 465 HIS A 823
REMARK 465 ASN A 824
REMARK 465 ASN A 825
REMARK 465 THR A 826
REMARK 465 LEU A 827
REMARK 465 PRO A 828
REMARK 465 HIS A 829
REMARK 465 PRO A 830
REMARK 465 HIS A 831
REMARK 465 SER A 832
REMARK 465 THR A 833
REMARK 465 THR A 834
REMARK 465 ARG A 835
REMARK 465 VAL A 836
REMARK 465 SER A 837
REMARK 465 ASN A 838
REMARK 465 SER A 839
REMARK 465 LEU A 840
REMARK 465 GLU A 841
REMARK 465 VAL A 842
REMARK 465 LEU A 843
REMARK 465 PHE A 844
REMARK 465 GLN A 845
REMARK 465 MET B -41
REMARK 465 ALA B -40
REMARK 465 LEU B -39
REMARK 465 PRO B -38
REMARK 465 ARG B -37
REMARK 465 CYS B -36
REMARK 465 MET B -35
REMARK 465 TRP B -34
REMARK 465 PRO B -33
REMARK 465 ASN B -32
REMARK 465 TYR B -31
REMARK 465 VAL B -30
REMARK 465 TRP B -29
REMARK 465 ARG B -28
REMARK 465 ALA B -27
REMARK 465 MET B -26
REMARK 465 MET B -25
REMARK 465 ALA B -24
REMARK 465 CYS B -23
REMARK 465 VAL B -22
REMARK 465 VAL B -21
REMARK 465 HIS B -20
REMARK 465 ARG B -19
REMARK 465 GLY B -18
REMARK 465 SER B -17
REMARK 465 GLY B -16
REMARK 465 ALA B -15
REMARK 465 PRO B -14
REMARK 465 LEU B -13
REMARK 465 THR B -12
REMARK 465 LEU B -11
REMARK 465 CYS B -10
REMARK 465 LEU B -9
REMARK 465 LEU B -8
REMARK 465 GLY B -7
REMARK 465 CYS B -6
REMARK 465 LEU B -5
REMARK 465 LEU B -4
REMARK 465 GLN B -3
REMARK 465 THR B -2
REMARK 465 PHE B -1
REMARK 465 HIS B 0
REMARK 465 VAL B 1
REMARK 465 LEU B 2
REMARK 465 SER B 3
REMARK 465 GLN B 4
REMARK 465 LYS B 5
REMARK 465 TYR B 6
REMARK 465 PRO B 7
REMARK 465 TYR B 8
REMARK 465 ASP B 9
REMARK 465 VAL B 10
REMARK 465 PRO B 11
REMARK 465 ASP B 12
REMARK 465 TYR B 13
REMARK 465 ALA B 14
REMARK 465 GLN B 15
REMARK 465 ARG B 16
REMARK 465 GLY B 17
REMARK 465 GLY B 18
REMARK 465 GLY B 19
REMARK 465 GLY B 20
REMARK 465 PRO B 21
REMARK 465 GLY B 22
REMARK 465 GLY B 23
REMARK 465 GLY B 24
REMARK 465 ALA B 25
REMARK 465 PRO B 26
REMARK 465 GLY B 27
REMARK 465 GLY B 28
REMARK 465 PRO B 29
REMARK 465 GLY B 30
REMARK 465 LEU B 31
REMARK 465 GLY B 32
REMARK 465 LEU B 33
REMARK 465 GLY B 34
REMARK 465 SER B 35
REMARK 465 LEU B 36
REMARK 465 GLY B 37
REMARK 465 GLU B 38
REMARK 465 GLU B 39
REMARK 465 ARG B 40
REMARK 465 GLU B 151
REMARK 465 ASP B 152
REMARK 465 ASP B 170
REMARK 465 ILE B 171
REMARK 465 ARG B 172
REMARK 465 ASP B 173
REMARK 465 SER B 174
REMARK 465 ILE B 558
REMARK 465 HIS B 559
REMARK 465 THR B 560
REMARK 465 LYS B 561
REMARK 465 PRO B 562
REMARK 465 LEU B 611
REMARK 465 HIS B 612
REMARK 465 THR B 613
REMARK 465 GLU B 614
REMARK 465 LEU B 615
REMARK 465 PHE B 616
REMARK 465 THR B 617
REMARK 465 THR B 618
REMARK 465 THR B 619
REMARK 465 THR B 620
REMARK 465 ARG B 621
REMARK 465 LEU B 622
REMARK 465 PRO B 623
REMARK 465 PRO B 624
REMARK 465 TYR B 625
REMARK 465 ALA B 626
REMARK 465 THR B 627
REMARK 465 ARG B 628
REMARK 465 TRP B 629
REMARK 465 PRO B 630
REMARK 465 PRO B 631
REMARK 465 ARG B 632
REMARK 465 THR B 633
REMARK 465 PRO B 634
REMARK 465 GLY B 635
REMARK 465 PRO B 636
REMARK 465 GLY B 637
REMARK 465 THR B 638
REMARK 465 SER B 639
REMARK 465 GLY B 640
REMARK 465 THR B 641
REMARK 465 ARG B 642
REMARK 465 ARG B 643
REMARK 465 PRO B 644
REMARK 465 PRO B 645
REMARK 465 PRO B 646
REMARK 465 PRO B 647
REMARK 465 ALA B 648
REMARK 465 THR B 649
REMARK 465 LEU B 650
REMARK 465 PRO B 651
REMARK 465 PRO B 652
REMARK 465 GLU B 653
REMARK 465 SER B 654
REMARK 465 ASP B 655
REMARK 465 ILE B 656
REMARK 465 ASP B 657
REMARK 465 LEU B 658
REMARK 465 GLY B 659
REMARK 465 PRO B 660
REMARK 465 ARG B 661
REMARK 465 ALA B 662
REMARK 465 TYR B 663
REMARK 465 ASP B 664
REMARK 465 ARG B 665
REMARK 465 PHE B 666
REMARK 465 PRO B 667
REMARK 465 GLY B 668
REMARK 465 ASP B 669
REMARK 465 SER B 670
REMARK 465 ARG B 671
REMARK 465 ASP B 672
REMARK 465 TYR B 673
REMARK 465 SER B 674
REMARK 465 THR B 675
REMARK 465 GLU B 676
REMARK 465 LEU B 677
REMARK 465 SER B 678
REMARK 465 VAL B 679
REMARK 465 THR B 680
REMARK 465 VAL B 681
REMARK 465 ALA B 682
REMARK 465 VAL B 683
REMARK 465 GLY B 684
REMARK 465 ALA B 685
REMARK 465 SER B 686
REMARK 465 LEU B 687
REMARK 465 LEU B 688
REMARK 465 PHE B 689
REMARK 465 LEU B 690
REMARK 465 ASN B 691
REMARK 465 ILE B 692
REMARK 465 LEU B 693
REMARK 465 ALA B 694
REMARK 465 PHE B 695
REMARK 465 ALA B 696
REMARK 465 ALA B 697
REMARK 465 LEU B 698
REMARK 465 TYR B 699
REMARK 465 TYR B 700
REMARK 465 LYS B 701
REMARK 465 ARG B 702
REMARK 465 ASP B 703
REMARK 465 ARG B 704
REMARK 465 ARG B 705
REMARK 465 GLN B 706
REMARK 465 GLU B 707
REMARK 465 LEU B 708
REMARK 465 ARG B 709
REMARK 465 CYS B 710
REMARK 465 ARG B 711
REMARK 465 ARG B 712
REMARK 465 LEU B 713
REMARK 465 SER B 714
REMARK 465 PRO B 715
REMARK 465 PRO B 716
REMARK 465 GLY B 717
REMARK 465 GLY B 718
REMARK 465 SER B 719
REMARK 465 GLY B 720
REMARK 465 SER B 721
REMARK 465 GLY B 722
REMARK 465 VAL B 723
REMARK 465 PRO B 724
REMARK 465 GLY B 725
REMARK 465 GLY B 726
REMARK 465 GLY B 727
REMARK 465 PRO B 728
REMARK 465 LEU B 729
REMARK 465 LEU B 730
REMARK 465 PRO B 731
REMARK 465 THR B 732
REMARK 465 ALA B 733
REMARK 465 GLY B 734
REMARK 465 ARG B 735
REMARK 465 GLU B 736
REMARK 465 LEU B 737
REMARK 465 PRO B 738
REMARK 465 PRO B 739
REMARK 465 GLU B 740
REMARK 465 GLU B 741
REMARK 465 GLU B 742
REMARK 465 LEU B 743
REMARK 465 VAL B 744
REMARK 465 SER B 745
REMARK 465 LEU B 746
REMARK 465 GLN B 747
REMARK 465 LEU B 748
REMARK 465 LYS B 749
REMARK 465 ARG B 750
REMARK 465 GLY B 751
REMARK 465 GLY B 752
REMARK 465 GLY B 753
REMARK 465 VAL B 754
REMARK 465 GLY B 755
REMARK 465 ALA B 756
REMARK 465 ASP B 757
REMARK 465 PRO B 758
REMARK 465 ALA B 759
REMARK 465 GLU B 760
REMARK 465 ALA B 761
REMARK 465 LEU B 762
REMARK 465 ARG B 763
REMARK 465 PRO B 764
REMARK 465 ALA B 765
REMARK 465 CYS B 766
REMARK 465 PRO B 767
REMARK 465 PRO B 768
REMARK 465 ASP B 769
REMARK 465 TYR B 770
REMARK 465 THR B 771
REMARK 465 LEU B 772
REMARK 465 ALA B 773
REMARK 465 LEU B 774
REMARK 465 ARG B 775
REMARK 465 ARG B 776
REMARK 465 ALA B 777
REMARK 465 PRO B 778
REMARK 465 ASP B 779
REMARK 465 ASP B 780
REMARK 465 VAL B 781
REMARK 465 PRO B 782
REMARK 465 LEU B 783
REMARK 465 LEU B 784
REMARK 465 ALA B 785
REMARK 465 PRO B 786
REMARK 465 GLY B 787
REMARK 465 ALA B 788
REMARK 465 LEU B 789
REMARK 465 THR B 790
REMARK 465 LEU B 791
REMARK 465 LEU B 792
REMARK 465 PRO B 793
REMARK 465 SER B 794
REMARK 465 GLY B 795
REMARK 465 LEU B 796
REMARK 465 GLY B 797
REMARK 465 PRO B 798
REMARK 465 PRO B 799
REMARK 465 PRO B 800
REMARK 465 PRO B 801
REMARK 465 PRO B 802
REMARK 465 PRO B 803
REMARK 465 PRO B 804
REMARK 465 PRO B 805
REMARK 465 SER B 806
REMARK 465 LEU B 807
REMARK 465 HIS B 808
REMARK 465 PRO B 809
REMARK 465 PHE B 810
REMARK 465 GLY B 811
REMARK 465 PRO B 812
REMARK 465 PHE B 813
REMARK 465 PRO B 814
REMARK 465 PRO B 815
REMARK 465 PRO B 816
REMARK 465 PRO B 817
REMARK 465 PRO B 818
REMARK 465 THR B 819
REMARK 465 ALA B 820
REMARK 465 THR B 821
REMARK 465 SER B 822
REMARK 465 HIS B 823
REMARK 465 ASN B 824
REMARK 465 ASN B 825
REMARK 465 THR B 826
REMARK 465 LEU B 827
REMARK 465 PRO B 828
REMARK 465 HIS B 829
REMARK 465 PRO B 830
REMARK 465 HIS B 831
REMARK 465 SER B 832
REMARK 465 THR B 833
REMARK 465 THR B 834
REMARK 465 ARG B 835
REMARK 465 VAL B 836
REMARK 465 SER B 837
REMARK 465 ASN B 838
REMARK 465 SER B 839
REMARK 465 LEU B 840
REMARK 465 GLU B 841
REMARK 465 VAL B 842
REMARK 465 LEU B 843
REMARK 465 PHE B 844
REMARK 465 GLN B 845
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 ASN A 59 CG OD1 ND2
REMARK 470 GLU A 61 CG CD OE1 OE2
REMARK 470 GLU A 281 CG CD OE1 OE2
REMARK 470 GLU A 392 CG CD OE1 OE2
REMARK 470 ASP A 393 CG OD1 OD2
REMARK 470 GLU A 396 CG CD OE1 OE2
REMARK 470 GLU A 398 CG CD OE1 OE2
REMARK 470 GLU A 422 CG CD OE1 OE2
REMARK 470 LYS A 424 CG CD CE NZ
REMARK 470 ASP A 442 CG OD1 OD2
REMARK 470 GLU A 490 CG CD OE1 OE2
REMARK 470 GLU A 494 CG CD OE1 OE2
REMARK 470 LYS A 525 CG CD CE NZ
REMARK 470 GLN A 549 CG CD OE1 NE2
REMARK 470 ARG A 564 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 566 CG CD OE1 OE2
REMARK 470 GLU A 567 CG CD OE1 OE2
REMARK 470 ASN A 574 CG OD1 ND2
REMARK 470 LYS A 586 CG CD CE NZ
REMARK 470 ASN B 59 CG OD1 ND2
REMARK 470 ILE B 62 CG1 CG2 CD1
REMARK 470 GLN B 227 CG CD OE1 NE2
REMARK 470 GLU B 281 CG CD OE1 OE2
REMARK 470 ASP B 318 CG OD1 OD2
REMARK 470 ARG B 319 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 320 CG CD OE1 OE2
REMARK 470 ASP B 321 CG OD1 OD2
REMARK 470 GLU B 324 CG CD OE1 OE2
REMARK 470 ASP B 362 CG OD1 OD2
REMARK 470 GLU B 396 CG CD OE1 OE2
REMARK 470 GLU B 398 CG CD OE1 OE2
REMARK 470 ASP B 399 CG OD1 OD2
REMARK 470 GLU B 422 CG CD OE1 OE2
REMARK 470 HIS B 486 CG ND1 CD2 CE1 NE2
REMARK 470 GLN B 488 CG CD OE1 NE2
REMARK 470 GLU B 494 CG CD OE1 OE2
REMARK 470 ASP B 554 CG OD1 OD2
REMARK 470 LYS B 556 CG CD CE NZ
REMARK 470 ARG B 564 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 567 CG CD OE1 OE2
REMARK 470 LYS B 586 CG CD CE NZ
REMARK 470 ARG B 590 CG CD NE CZ NH1 NH2
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 ASN A 126 57.61 -96.49
REMARK 500 ASN A 136 57.50 -93.98
REMARK 500 ASP A 140 49.93 -81.63
REMARK 500 PRO A 256 0.82 -69.41
REMARK 500 ASP A 339 34.78 -96.20
REMARK 500 ASP A 363 137.20 -172.17
REMARK 500 ASN A 375 61.82 63.12
REMARK 500 SER A 394 58.16 -96.75
REMARK 500 ASP A 437 53.79 -119.93
REMARK 500 PRO A 547 4.87 -65.56
REMARK 500 LYS A 578 68.60 -68.86
REMARK 500 ARG A 590 -169.60 -79.29
REMARK 500 THR B 100 -32.34 -134.76
REMARK 500 ASN B 136 52.26 -91.79
REMARK 500 ASP B 140 49.04 -82.93
REMARK 500 CYS B 141 -159.37 -92.54
REMARK 500 LEU B 142 54.27 70.82
REMARK 500 MET B 189 32.88 -140.17
REMARK 500 ASP B 339 31.15 -93.97
REMARK 500 ASN B 375 62.56 61.43
REMARK 500 SER B 394 57.05 -95.75
REMARK 500 TYR B 418 -61.01 -100.59
REMARK 500 GLU B 422 33.11 -94.29
REMARK 500 PRO B 547 3.90 -67.08
REMARK 500 LYS B 578 68.82 -67.91
REMARK 500 LEU B 608 -60.58 -90.68
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: EMD-29811 RELATED DB: EMDB
REMARK 900 CRYO-EM STRUCTURE OF FULL LENGTH NEUROLIGIN-2 FROM MOUSE
DBREF 8G7D A -41 5 UNP Q99K10 NLGN1_MOUSE 1 47
DBREF 8G7D A 14 836 UNP Q69ZK9 NLGN2_MOUSE 14 836
DBREF 8G7D B -41 5 UNP Q99K10 NLGN1_MOUSE 1 47
DBREF 8G7D B 14 836 UNP Q69ZK9 NLGN2_MOUSE 14 836
SEQADV 8G7D TYR A 6 UNP Q99K10 LINKER
SEQADV 8G7D PRO A 7 UNP Q99K10 LINKER
SEQADV 8G7D TYR A 8 UNP Q99K10 LINKER
SEQADV 8G7D ASP A 9 UNP Q99K10 LINKER
SEQADV 8G7D VAL A 10 UNP Q99K10 LINKER
SEQADV 8G7D PRO A 11 UNP Q99K10 LINKER
SEQADV 8G7D ASP A 12 UNP Q99K10 LINKER
SEQADV 8G7D TYR A 13 UNP Q99K10 LINKER
SEQADV 8G7D A UNP Q69ZK9 GLY 153 DELETION
SEQADV 8G7D A UNP Q69ZK9 PRO 154 DELETION
SEQADV 8G7D A UNP Q69ZK9 LEU 155 DELETION
SEQADV 8G7D A UNP Q69ZK9 THR 156 DELETION
SEQADV 8G7D A UNP Q69ZK9 LYS 157 DELETION
SEQADV 8G7D A UNP Q69ZK9 LYS 158 DELETION
SEQADV 8G7D A UNP Q69ZK9 ARG 159 DELETION
SEQADV 8G7D A UNP Q69ZK9 ASP 160 DELETION
SEQADV 8G7D A UNP Q69ZK9 GLU 161 DELETION
SEQADV 8G7D A UNP Q69ZK9 ALA 162 DELETION
SEQADV 8G7D A UNP Q69ZK9 THR 163 DELETION
SEQADV 8G7D A UNP Q69ZK9 LEU 164 DELETION
SEQADV 8G7D A UNP Q69ZK9 ASN 165 DELETION
SEQADV 8G7D A UNP Q69ZK9 PRO 166 DELETION
SEQADV 8G7D A UNP Q69ZK9 PRO 167 DELETION
SEQADV 8G7D A UNP Q69ZK9 ASP 168 DELETION
SEQADV 8G7D A UNP Q69ZK9 THR 169 DELETION
SEQADV 8G7D SER A 837 UNP Q69ZK9 EXPRESSION TAG
SEQADV 8G7D ASN A 838 UNP Q69ZK9 EXPRESSION TAG
SEQADV 8G7D SER A 839 UNP Q69ZK9 EXPRESSION TAG
SEQADV 8G7D LEU A 840 UNP Q69ZK9 EXPRESSION TAG
SEQADV 8G7D GLU A 841 UNP Q69ZK9 EXPRESSION TAG
SEQADV 8G7D VAL A 842 UNP Q69ZK9 EXPRESSION TAG
SEQADV 8G7D LEU A 843 UNP Q69ZK9 EXPRESSION TAG
SEQADV 8G7D PHE A 844 UNP Q69ZK9 EXPRESSION TAG
SEQADV 8G7D GLN A 845 UNP Q69ZK9 EXPRESSION TAG
SEQADV 8G7D TYR B 6 UNP Q99K10 LINKER
SEQADV 8G7D PRO B 7 UNP Q99K10 LINKER
SEQADV 8G7D TYR B 8 UNP Q99K10 LINKER
SEQADV 8G7D ASP B 9 UNP Q99K10 LINKER
SEQADV 8G7D VAL B 10 UNP Q99K10 LINKER
SEQADV 8G7D PRO B 11 UNP Q99K10 LINKER
SEQADV 8G7D ASP B 12 UNP Q99K10 LINKER
SEQADV 8G7D TYR B 13 UNP Q99K10 LINKER
SEQADV 8G7D B UNP Q69ZK9 GLY 153 DELETION
SEQADV 8G7D B UNP Q69ZK9 PRO 154 DELETION
SEQADV 8G7D B UNP Q69ZK9 LEU 155 DELETION
SEQADV 8G7D B UNP Q69ZK9 THR 156 DELETION
SEQADV 8G7D B UNP Q69ZK9 LYS 157 DELETION
SEQADV 8G7D B UNP Q69ZK9 LYS 158 DELETION
SEQADV 8G7D B UNP Q69ZK9 ARG 159 DELETION
SEQADV 8G7D B UNP Q69ZK9 ASP 160 DELETION
SEQADV 8G7D B UNP Q69ZK9 GLU 161 DELETION
SEQADV 8G7D B UNP Q69ZK9 ALA 162 DELETION
SEQADV 8G7D B UNP Q69ZK9 THR 163 DELETION
SEQADV 8G7D B UNP Q69ZK9 LEU 164 DELETION
SEQADV 8G7D B UNP Q69ZK9 ASN 165 DELETION
SEQADV 8G7D B UNP Q69ZK9 PRO 166 DELETION
SEQADV 8G7D B UNP Q69ZK9 PRO 167 DELETION
SEQADV 8G7D B UNP Q69ZK9 ASP 168 DELETION
SEQADV 8G7D B UNP Q69ZK9 THR 169 DELETION
SEQADV 8G7D SER B 837 UNP Q69ZK9 EXPRESSION TAG
SEQADV 8G7D ASN B 838 UNP Q69ZK9 EXPRESSION TAG
SEQADV 8G7D SER B 839 UNP Q69ZK9 EXPRESSION TAG
SEQADV 8G7D LEU B 840 UNP Q69ZK9 EXPRESSION TAG
SEQADV 8G7D GLU B 841 UNP Q69ZK9 EXPRESSION TAG
SEQADV 8G7D VAL B 842 UNP Q69ZK9 EXPRESSION TAG
SEQADV 8G7D LEU B 843 UNP Q69ZK9 EXPRESSION TAG
SEQADV 8G7D PHE B 844 UNP Q69ZK9 EXPRESSION TAG
SEQADV 8G7D GLN B 845 UNP Q69ZK9 EXPRESSION TAG
SEQRES 1 A 870 MET ALA LEU PRO ARG CYS MET TRP PRO ASN TYR VAL TRP
SEQRES 2 A 870 ARG ALA MET MET ALA CYS VAL VAL HIS ARG GLY SER GLY
SEQRES 3 A 870 ALA PRO LEU THR LEU CYS LEU LEU GLY CYS LEU LEU GLN
SEQRES 4 A 870 THR PHE HIS VAL LEU SER GLN LYS TYR PRO TYR ASP VAL
SEQRES 5 A 870 PRO ASP TYR ALA GLN ARG GLY GLY GLY GLY PRO GLY GLY
SEQRES 6 A 870 GLY ALA PRO GLY GLY PRO GLY LEU GLY LEU GLY SER LEU
SEQRES 7 A 870 GLY GLU GLU ARG PHE PRO VAL VAL ASN THR ALA TYR GLY
SEQRES 8 A 870 ARG VAL ARG GLY VAL ARG ARG GLU LEU ASN ASN GLU ILE
SEQRES 9 A 870 LEU GLY PRO VAL VAL GLN PHE LEU GLY VAL PRO TYR ALA
SEQRES 10 A 870 THR PRO PRO LEU GLY ALA ARG ARG PHE GLN PRO PRO GLU
SEQRES 11 A 870 ALA PRO ALA SER TRP PRO GLY VAL ARG ASN ALA THR THR
SEQRES 12 A 870 LEU PRO PRO ALA CYS PRO GLN ASN LEU HIS GLY ALA LEU
SEQRES 13 A 870 PRO ALA ILE MET LEU PRO VAL TRP PHE THR ASP ASN LEU
SEQRES 14 A 870 GLU ALA ALA ALA THR TYR VAL GLN ASN GLN SER GLU ASP
SEQRES 15 A 870 CYS LEU TYR LEU ASN LEU TYR VAL PRO THR GLU ASP ASP
SEQRES 16 A 870 ILE ARG ASP SER GLY LYS LYS PRO VAL MET LEU PHE LEU
SEQRES 17 A 870 HIS GLY GLY SER TYR MET GLU GLY THR GLY ASN MET PHE
SEQRES 18 A 870 ASP GLY SER VAL LEU ALA ALA TYR GLY ASN VAL ILE VAL
SEQRES 19 A 870 VAL THR LEU ASN TYR ARG LEU GLY VAL LEU GLY PHE LEU
SEQRES 20 A 870 SER THR GLY ASP GLN ALA ALA LYS GLY ASN TYR GLY LEU
SEQRES 21 A 870 LEU ASP GLN ILE GLN ALA LEU ARG TRP LEU SER GLU ASN
SEQRES 22 A 870 ILE ALA HIS PHE GLY GLY ASP PRO GLU ARG ILE THR ILE
SEQRES 23 A 870 PHE GLY SER GLY ALA GLY ALA SER CYS VAL ASN LEU LEU
SEQRES 24 A 870 ILE LEU SER HIS HIS SER GLU GLY LEU PHE GLN LYS ALA
SEQRES 25 A 870 ILE ALA GLN SER GLY THR ALA ILE SER SER TRP SER VAL
SEQRES 26 A 870 ASN TYR GLN PRO LEU LYS TYR THR ARG LEU LEU ALA ALA
SEQRES 27 A 870 LYS VAL GLY CYS ASP ARG GLU ASP SER THR GLU ALA VAL
SEQRES 28 A 870 GLU CYS LEU ARG ARG LYS SER SER ARG GLU LEU VAL ASP
SEQRES 29 A 870 GLN ASP VAL GLN PRO ALA ARG TYR HIS ILE ALA PHE GLY
SEQRES 30 A 870 PRO VAL VAL ASP GLY ASP VAL VAL PRO ASP ASP PRO GLU
SEQRES 31 A 870 ILE LEU MET GLN GLN GLY GLU PHE LEU ASN TYR ASP MET
SEQRES 32 A 870 LEU ILE GLY VAL ASN GLN GLY GLU GLY LEU LYS PHE VAL
SEQRES 33 A 870 GLU ASP SER ALA GLU SER GLU ASP GLY VAL SER ALA SER
SEQRES 34 A 870 ALA PHE ASP PHE THR VAL SER ASN PHE VAL ASP ASN LEU
SEQRES 35 A 870 TYR GLY TYR PRO GLU GLY LYS ASP VAL LEU ARG GLU THR
SEQRES 36 A 870 ILE LYS PHE MET TYR THR ASP TRP ALA ASP ARG ASP ASN
SEQRES 37 A 870 GLY GLU MET ARG ARG LYS THR LEU LEU ALA LEU PHE THR
SEQRES 38 A 870 ASP HIS GLN TRP VAL ALA PRO ALA VAL ALA THR ALA LYS
SEQRES 39 A 870 LEU HIS ALA ASP TYR GLN SER PRO VAL TYR PHE TYR THR
SEQRES 40 A 870 PHE TYR HIS HIS CYS GLN ALA GLU GLY ARG PRO GLU TRP
SEQRES 41 A 870 ALA ASP ALA ALA HIS GLY ASP GLU LEU PRO TYR VAL PHE
SEQRES 42 A 870 GLY VAL PRO MET VAL GLY ALA THR ASP LEU PHE PRO CYS
SEQRES 43 A 870 ASN PHE SER LYS ASN ASP VAL MET LEU SER ALA VAL VAL
SEQRES 44 A 870 MET THR TYR TRP THR ASN PHE ALA LYS THR GLY ASP PRO
SEQRES 45 A 870 ASN GLN PRO VAL PRO GLN ASP THR LYS PHE ILE HIS THR
SEQRES 46 A 870 LYS PRO ASN ARG PHE GLU GLU VAL VAL TRP SER LYS PHE
SEQRES 47 A 870 ASN SER LYS GLU LYS GLN TYR LEU HIS ILE GLY LEU LYS
SEQRES 48 A 870 PRO ARG VAL ARG ASP ASN TYR ARG ALA ASN LYS VAL ALA
SEQRES 49 A 870 PHE TRP LEU GLU LEU VAL PRO HIS LEU HIS ASN LEU HIS
SEQRES 50 A 870 THR GLU LEU PHE THR THR THR THR ARG LEU PRO PRO TYR
SEQRES 51 A 870 ALA THR ARG TRP PRO PRO ARG THR PRO GLY PRO GLY THR
SEQRES 52 A 870 SER GLY THR ARG ARG PRO PRO PRO PRO ALA THR LEU PRO
SEQRES 53 A 870 PRO GLU SER ASP ILE ASP LEU GLY PRO ARG ALA TYR ASP
SEQRES 54 A 870 ARG PHE PRO GLY ASP SER ARG ASP TYR SER THR GLU LEU
SEQRES 55 A 870 SER VAL THR VAL ALA VAL GLY ALA SER LEU LEU PHE LEU
SEQRES 56 A 870 ASN ILE LEU ALA PHE ALA ALA LEU TYR TYR LYS ARG ASP
SEQRES 57 A 870 ARG ARG GLN GLU LEU ARG CYS ARG ARG LEU SER PRO PRO
SEQRES 58 A 870 GLY GLY SER GLY SER GLY VAL PRO GLY GLY GLY PRO LEU
SEQRES 59 A 870 LEU PRO THR ALA GLY ARG GLU LEU PRO PRO GLU GLU GLU
SEQRES 60 A 870 LEU VAL SER LEU GLN LEU LYS ARG GLY GLY GLY VAL GLY
SEQRES 61 A 870 ALA ASP PRO ALA GLU ALA LEU ARG PRO ALA CYS PRO PRO
SEQRES 62 A 870 ASP TYR THR LEU ALA LEU ARG ARG ALA PRO ASP ASP VAL
SEQRES 63 A 870 PRO LEU LEU ALA PRO GLY ALA LEU THR LEU LEU PRO SER
SEQRES 64 A 870 GLY LEU GLY PRO PRO PRO PRO PRO PRO PRO PRO SER LEU
SEQRES 65 A 870 HIS PRO PHE GLY PRO PHE PRO PRO PRO PRO PRO THR ALA
SEQRES 66 A 870 THR SER HIS ASN ASN THR LEU PRO HIS PRO HIS SER THR
SEQRES 67 A 870 THR ARG VAL SER ASN SER LEU GLU VAL LEU PHE GLN
SEQRES 1 B 870 MET ALA LEU PRO ARG CYS MET TRP PRO ASN TYR VAL TRP
SEQRES 2 B 870 ARG ALA MET MET ALA CYS VAL VAL HIS ARG GLY SER GLY
SEQRES 3 B 870 ALA PRO LEU THR LEU CYS LEU LEU GLY CYS LEU LEU GLN
SEQRES 4 B 870 THR PHE HIS VAL LEU SER GLN LYS TYR PRO TYR ASP VAL
SEQRES 5 B 870 PRO ASP TYR ALA GLN ARG GLY GLY GLY GLY PRO GLY GLY
SEQRES 6 B 870 GLY ALA PRO GLY GLY PRO GLY LEU GLY LEU GLY SER LEU
SEQRES 7 B 870 GLY GLU GLU ARG PHE PRO VAL VAL ASN THR ALA TYR GLY
SEQRES 8 B 870 ARG VAL ARG GLY VAL ARG ARG GLU LEU ASN ASN GLU ILE
SEQRES 9 B 870 LEU GLY PRO VAL VAL GLN PHE LEU GLY VAL PRO TYR ALA
SEQRES 10 B 870 THR PRO PRO LEU GLY ALA ARG ARG PHE GLN PRO PRO GLU
SEQRES 11 B 870 ALA PRO ALA SER TRP PRO GLY VAL ARG ASN ALA THR THR
SEQRES 12 B 870 LEU PRO PRO ALA CYS PRO GLN ASN LEU HIS GLY ALA LEU
SEQRES 13 B 870 PRO ALA ILE MET LEU PRO VAL TRP PHE THR ASP ASN LEU
SEQRES 14 B 870 GLU ALA ALA ALA THR TYR VAL GLN ASN GLN SER GLU ASP
SEQRES 15 B 870 CYS LEU TYR LEU ASN LEU TYR VAL PRO THR GLU ASP ASP
SEQRES 16 B 870 ILE ARG ASP SER GLY LYS LYS PRO VAL MET LEU PHE LEU
SEQRES 17 B 870 HIS GLY GLY SER TYR MET GLU GLY THR GLY ASN MET PHE
SEQRES 18 B 870 ASP GLY SER VAL LEU ALA ALA TYR GLY ASN VAL ILE VAL
SEQRES 19 B 870 VAL THR LEU ASN TYR ARG LEU GLY VAL LEU GLY PHE LEU
SEQRES 20 B 870 SER THR GLY ASP GLN ALA ALA LYS GLY ASN TYR GLY LEU
SEQRES 21 B 870 LEU ASP GLN ILE GLN ALA LEU ARG TRP LEU SER GLU ASN
SEQRES 22 B 870 ILE ALA HIS PHE GLY GLY ASP PRO GLU ARG ILE THR ILE
SEQRES 23 B 870 PHE GLY SER GLY ALA GLY ALA SER CYS VAL ASN LEU LEU
SEQRES 24 B 870 ILE LEU SER HIS HIS SER GLU GLY LEU PHE GLN LYS ALA
SEQRES 25 B 870 ILE ALA GLN SER GLY THR ALA ILE SER SER TRP SER VAL
SEQRES 26 B 870 ASN TYR GLN PRO LEU LYS TYR THR ARG LEU LEU ALA ALA
SEQRES 27 B 870 LYS VAL GLY CYS ASP ARG GLU ASP SER THR GLU ALA VAL
SEQRES 28 B 870 GLU CYS LEU ARG ARG LYS SER SER ARG GLU LEU VAL ASP
SEQRES 29 B 870 GLN ASP VAL GLN PRO ALA ARG TYR HIS ILE ALA PHE GLY
SEQRES 30 B 870 PRO VAL VAL ASP GLY ASP VAL VAL PRO ASP ASP PRO GLU
SEQRES 31 B 870 ILE LEU MET GLN GLN GLY GLU PHE LEU ASN TYR ASP MET
SEQRES 32 B 870 LEU ILE GLY VAL ASN GLN GLY GLU GLY LEU LYS PHE VAL
SEQRES 33 B 870 GLU ASP SER ALA GLU SER GLU ASP GLY VAL SER ALA SER
SEQRES 34 B 870 ALA PHE ASP PHE THR VAL SER ASN PHE VAL ASP ASN LEU
SEQRES 35 B 870 TYR GLY TYR PRO GLU GLY LYS ASP VAL LEU ARG GLU THR
SEQRES 36 B 870 ILE LYS PHE MET TYR THR ASP TRP ALA ASP ARG ASP ASN
SEQRES 37 B 870 GLY GLU MET ARG ARG LYS THR LEU LEU ALA LEU PHE THR
SEQRES 38 B 870 ASP HIS GLN TRP VAL ALA PRO ALA VAL ALA THR ALA LYS
SEQRES 39 B 870 LEU HIS ALA ASP TYR GLN SER PRO VAL TYR PHE TYR THR
SEQRES 40 B 870 PHE TYR HIS HIS CYS GLN ALA GLU GLY ARG PRO GLU TRP
SEQRES 41 B 870 ALA ASP ALA ALA HIS GLY ASP GLU LEU PRO TYR VAL PHE
SEQRES 42 B 870 GLY VAL PRO MET VAL GLY ALA THR ASP LEU PHE PRO CYS
SEQRES 43 B 870 ASN PHE SER LYS ASN ASP VAL MET LEU SER ALA VAL VAL
SEQRES 44 B 870 MET THR TYR TRP THR ASN PHE ALA LYS THR GLY ASP PRO
SEQRES 45 B 870 ASN GLN PRO VAL PRO GLN ASP THR LYS PHE ILE HIS THR
SEQRES 46 B 870 LYS PRO ASN ARG PHE GLU GLU VAL VAL TRP SER LYS PHE
SEQRES 47 B 870 ASN SER LYS GLU LYS GLN TYR LEU HIS ILE GLY LEU LYS
SEQRES 48 B 870 PRO ARG VAL ARG ASP ASN TYR ARG ALA ASN LYS VAL ALA
SEQRES 49 B 870 PHE TRP LEU GLU LEU VAL PRO HIS LEU HIS ASN LEU HIS
SEQRES 50 B 870 THR GLU LEU PHE THR THR THR THR ARG LEU PRO PRO TYR
SEQRES 51 B 870 ALA THR ARG TRP PRO PRO ARG THR PRO GLY PRO GLY THR
SEQRES 52 B 870 SER GLY THR ARG ARG PRO PRO PRO PRO ALA THR LEU PRO
SEQRES 53 B 870 PRO GLU SER ASP ILE ASP LEU GLY PRO ARG ALA TYR ASP
SEQRES 54 B 870 ARG PHE PRO GLY ASP SER ARG ASP TYR SER THR GLU LEU
SEQRES 55 B 870 SER VAL THR VAL ALA VAL GLY ALA SER LEU LEU PHE LEU
SEQRES 56 B 870 ASN ILE LEU ALA PHE ALA ALA LEU TYR TYR LYS ARG ASP
SEQRES 57 B 870 ARG ARG GLN GLU LEU ARG CYS ARG ARG LEU SER PRO PRO
SEQRES 58 B 870 GLY GLY SER GLY SER GLY VAL PRO GLY GLY GLY PRO LEU
SEQRES 59 B 870 LEU PRO THR ALA GLY ARG GLU LEU PRO PRO GLU GLU GLU
SEQRES 60 B 870 LEU VAL SER LEU GLN LEU LYS ARG GLY GLY GLY VAL GLY
SEQRES 61 B 870 ALA ASP PRO ALA GLU ALA LEU ARG PRO ALA CYS PRO PRO
SEQRES 62 B 870 ASP TYR THR LEU ALA LEU ARG ARG ALA PRO ASP ASP VAL
SEQRES 63 B 870 PRO LEU LEU ALA PRO GLY ALA LEU THR LEU LEU PRO SER
SEQRES 64 B 870 GLY LEU GLY PRO PRO PRO PRO PRO PRO PRO PRO SER LEU
SEQRES 65 B 870 HIS PRO PHE GLY PRO PHE PRO PRO PRO PRO PRO THR ALA
SEQRES 66 B 870 THR SER HIS ASN ASN THR LEU PRO HIS PRO HIS SER THR
SEQRES 67 B 870 THR ARG VAL SER ASN SER LEU GLU VAL LEU PHE GLN
HET NAG A1000 14
HET NAG A1001 14
HET NAG B1000 14
HET NAG B1001 14
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
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
FORMUL 3 NAG 4(C8 H15 N O6)
HELIX 1 AA1 PRO A 120 ASN A 126 1 7
HELIX 2 AA2 ASN A 126 ALA A 131 1 6
HELIX 3 AA3 GLY A 198 ASN A 206 1 9
HELIX 4 AA4 GLY A 217 LEU A 222 1 6
HELIX 5 AA5 ASN A 232 GLY A 253 1 22
HELIX 6 AA6 GLY A 265 LEU A 276 1 12
HELIX 7 AA7 GLN A 303 GLY A 316 1 14
HELIX 8 AA8 ASP A 321 LYS A 332 1 12
HELIX 9 AA9 SER A 333 ASP A 339 1 7
HELIX 10 AB1 ASP A 363 GLN A 370 1 8
HELIX 11 AB2 GLU A 386 PHE A 390 5 5
HELIX 12 AB3 ALA A 405 ASN A 416 1 12
HELIX 13 AB4 LYS A 424 TYR A 435 1 12
HELIX 14 AB5 ASP A 437 ARG A 441 5 5
HELIX 15 AB6 MET A 446 TRP A 460 1 15
HELIX 16 AB7 TRP A 460 TYR A 474 1 15
HELIX 17 AB8 GLU A 503 PHE A 508 1 6
HELIX 18 AB9 SER A 524 GLY A 545 1 22
HELIX 19 AC1 ARG A 594 GLU A 603 1 10
HELIX 20 AC2 GLU A 603 LEU A 608 1 6
HELIX 21 AC3 PRO B 120 ASN B 126 1 7
HELIX 22 AC4 ASN B 126 VAL B 134 1 9
HELIX 23 AC5 THR B 192 PHE B 196 5 5
HELIX 24 AC6 GLY B 198 ASN B 206 1 9
HELIX 25 AC7 GLY B 217 LEU B 222 1 6
HELIX 26 AC8 ASN B 232 GLY B 253 1 22
HELIX 27 AC9 GLY B 265 LEU B 276 1 12
HELIX 28 AD1 GLN B 303 GLY B 316 1 14
HELIX 29 AD2 ASP B 321 LYS B 332 1 12
HELIX 30 AD3 SER B 333 ASP B 339 1 7
HELIX 31 AD4 ASP B 363 GLN B 370 1 8
HELIX 32 AD5 GLU B 386 PHE B 390 5 5
HELIX 33 AD6 GLU B 392 GLU B 396 5 5
HELIX 34 AD7 SER B 402 ASN B 416 1 15
HELIX 35 AD8 LYS B 424 TYR B 435 1 12
HELIX 36 AD9 ASP B 437 ARG B 441 5 5
HELIX 37 AE1 MET B 446 TRP B 460 1 15
HELIX 38 AE2 TRP B 460 TYR B 474 1 15
HELIX 39 AE3 GLU B 503 PHE B 508 1 6
HELIX 40 AE4 SER B 524 THR B 544 1 21
HELIX 41 AE5 ARG B 594 GLU B 603 1 10
HELIX 42 AE6 LEU B 604 LEU B 608 5 5
SHEET 1 AA1 3 VAL A 43 ASN A 45 0
SHEET 2 AA1 3 ARG A 50 ARG A 52 -1 O VAL A 51 N VAL A 44
SHEET 3 AA1 3 VAL A 96 ASN A 98 1 O ARG A 97 N ARG A 50
SHEET 1 AA2 9 VAL A 66 PRO A 73 0
SHEET 2 AA2 9 TYR A 143 PRO A 149 -1 O VAL A 148 N VAL A 67
SHEET 3 AA2 9 ILE A 208 LEU A 212 -1 O THR A 211 N ASN A 145
SHEET 4 AA2 9 LYS A 177 LEU A 183 1 N PHE A 182 O VAL A 210
SHEET 5 AA2 9 GLY A 254 SER A 264 1 O THR A 260 N VAL A 179
SHEET 6 AA2 9 ILE A 288 GLN A 290 1 O ILE A 288 N ILE A 261
SHEET 7 AA2 9 MET A 378 ASN A 383 1 O LEU A 379 N ALA A 289
SHEET 8 AA2 9 VAL A 478 PHE A 483 1 O PHE A 483 N VAL A 382
SHEET 9 AA2 9 LEU A 581 ILE A 583 1 O LEU A 581 N THR A 482
SHEET 1 AA3 3 VAL B 43 ASN B 45 0
SHEET 2 AA3 3 ARG B 50 ARG B 52 -1 O VAL B 51 N VAL B 44
SHEET 3 AA3 3 VAL B 96 ASN B 98 1 O ARG B 97 N ARG B 50
SHEET 1 AA410 VAL B 66 LEU B 70 0
SHEET 2 AA410 LEU B 144 PRO B 149 -1 O VAL B 148 N VAL B 67
SHEET 3 AA410 ILE B 208 LEU B 212 -1 O THR B 211 N ASN B 145
SHEET 4 AA410 LYS B 177 LEU B 183 1 N MET B 180 O ILE B 208
SHEET 5 AA410 GLY B 254 SER B 264 1 O THR B 260 N VAL B 179
SHEET 6 AA410 LYS B 286 GLN B 290 1 O ILE B 288 N ILE B 261
SHEET 7 AA410 MET B 378 ASN B 383 1 O LEU B 379 N ALA B 289
SHEET 8 AA410 VAL B 478 PHE B 483 1 O PHE B 483 N VAL B 382
SHEET 9 AA410 TYR B 580 ILE B 583 1 O LEU B 581 N PHE B 480
SHEET 10 AA410 VAL B 589 ARG B 590 -1 O ARG B 590 N TYR B 580
SSBOND 1 CYS A 106 CYS A 141 1555 1555 2.03
SSBOND 2 CYS A 317 CYS A 328 1555 1555 2.03
SSBOND 3 CYS A 487 CYS A 521 1555 1555 2.03
SSBOND 4 CYS B 106 CYS B 141 1555 1555 2.03
SSBOND 5 CYS B 317 CYS B 328 1555 1555 2.03
SSBOND 6 CYS B 487 CYS B 521 1555 1555 2.03
LINK ND2 ASN A 98 C1 NAG A1000 1555 1555 1.44
LINK ND2 ASN A 522 C1 NAG A1001 1555 1555 1.44
LINK ND2 ASN B 98 C1 NAG B1000 1555 1555 1.45
LINK ND2 ASN B 522 C1 NAG B1001 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 4130 LEU A 608
TER 8292 ASN B 610
MASTER 862 0 4 42 25 0 0 6 8346 2 72 134
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