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HEADER MEMBRANE PROTEIN 04-SEP-22 8GS4
TITLE CRYO-EM STRUCTURE OF HUMAN NEUROLIGIN 2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NEUROLIGIN-2;
COMPND 3 CHAIN: A, B;
COMPND 4 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: NLGN2;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: HEK293
KEYWDS SYNAPSE PROTEIN, PLASMA MEMBRANE, MEMBRANE PROTEIN
EXPDTA ELECTRON MICROSCOPY
AUTHOR H.W.ZHANG,Z.Z.ZHANG,M.Z.HOU
REVDAT 1 01-MAR-23 8GS4 0
JRNL AUTH Z.ZHANG,M.HOU,H.OU,D.WANG,Z.LI,H.ZHANG,J.LU
JRNL TITL EXPRESSION AND STRUCTURAL ANALYSIS OF HUMAN NEUROLIGIN 2 AND
JRNL TITL 2 NEUROLIGIN 3 IMPLICATED IN AUTISM SPECTRUM DISORDERS.
JRNL REF FRONT ENDOCRINOL V. 13 67529 2022
JRNL REFN ESSN 1664-2392
JRNL PMID 36479216
JRNL DOI 10.3389/FENDO.2022.1067529
REMARK 2
REMARK 2 RESOLUTION. 3.50 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) : 3.500
REMARK 3 NUMBER OF PARTICLES : 192341
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 8GS4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 05-SEP-22.
REMARK 100 THE DEPOSITION ID IS D_1300032001.
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 : HOMODIMER OF NEUROLIGIN 2
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 TITAN KRIOS
REMARK 245 DETECTOR TYPE : GATAN K3 BIOQUANTUM (6K X
REMARK 245 4K)
REMARK 245 MINIMUM DEFOCUS (NM) : 1500.00
REMARK 245 MAXIMUM DEFOCUS (NM) : 2500.00
REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 NOMINAL CS : NULL
REMARK 245 IMAGING MODE : BRIGHT FIELD
REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 5000.00
REMARK 245 ILLUMINATION MODE : FLOOD BEAM
REMARK 245 NOMINAL MAGNIFICATION : NULL
REMARK 245 CALIBRATED MAGNIFICATION : NULL
REMARK 245 SOURCE : FIELD EMISSION GUN
REMARK 245 ACCELERATION VOLTAGE (KV) : 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 1
REMARK 465 TRP A 2
REMARK 465 LEU A 3
REMARK 465 LEU A 4
REMARK 465 ALA A 5
REMARK 465 LEU A 6
REMARK 465 CYS A 7
REMARK 465 LEU A 8
REMARK 465 VAL A 9
REMARK 465 GLY A 10
REMARK 465 LEU A 11
REMARK 465 ALA A 12
REMARK 465 GLY 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 ARG A 40
REMARK 465 PHE A 41
REMARK 465 THR A 150
REMARK 465 GLU A 151
REMARK 465 ASP A 152
REMARK 465 GLY A 153
REMARK 465 PRO A 154
REMARK 465 LEU A 155
REMARK 465 THR A 156
REMARK 465 LYS A 157
REMARK 465 LYS A 158
REMARK 465 ARG A 159
REMARK 465 ASP A 160
REMARK 465 GLU A 161
REMARK 465 ALA A 162
REMARK 465 THR A 163
REMARK 465 LEU A 164
REMARK 465 ASN A 165
REMARK 465 PRO A 166
REMARK 465 PRO A 167
REMARK 465 ASP A 168
REMARK 465 THR A 169
REMARK 465 ASP A 170
REMARK 465 ILE A 171
REMARK 465 ARG A 172
REMARK 465 ASP A 173
REMARK 465 PRO A 174
REMARK 465 ASP A 393
REMARK 465 SER A 394
REMARK 465 ALA A 395
REMARK 465 GLU A 396
REMARK 465 SER A 397
REMARK 465 GLU A 398
REMARK 465 ASP A 399
REMARK 465 GLY A 400
REMARK 465 GLN A 553
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 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 PRO A 633
REMARK 465 PRO A 634
REMARK 465 ALA A 635
REMARK 465 GLY A 636
REMARK 465 ALA A 637
REMARK 465 PRO A 638
REMARK 465 GLY A 639
REMARK 465 THR A 640
REMARK 465 ARG A 641
REMARK 465 ARG A 642
REMARK 465 PRO A 643
REMARK 465 PRO A 644
REMARK 465 PRO A 645
REMARK 465 PRO A 646
REMARK 465 ALA A 647
REMARK 465 THR A 648
REMARK 465 LEU A 649
REMARK 465 PRO A 650
REMARK 465 PRO A 651
REMARK 465 GLU A 652
REMARK 465 PRO A 653
REMARK 465 GLU A 654
REMARK 465 PRO A 655
REMARK 465 GLU A 656
REMARK 465 PRO A 657
REMARK 465 GLY A 658
REMARK 465 PRO A 659
REMARK 465 ARG A 660
REMARK 465 ALA A 661
REMARK 465 TYR A 662
REMARK 465 ASP A 663
REMARK 465 ARG A 664
REMARK 465 PHE A 665
REMARK 465 PRO A 666
REMARK 465 GLY A 667
REMARK 465 ASP A 668
REMARK 465 SER A 669
REMARK 465 ARG A 670
REMARK 465 ASP A 671
REMARK 465 TYR A 672
REMARK 465 SER A 673
REMARK 465 THR A 674
REMARK 465 GLU A 675
REMARK 465 LEU A 676
REMARK 465 SER A 677
REMARK 465 VAL A 678
REMARK 465 THR A 679
REMARK 465 VAL A 680
REMARK 465 ALA A 681
REMARK 465 VAL A 682
REMARK 465 GLY A 683
REMARK 465 ALA A 684
REMARK 465 SER A 685
REMARK 465 LEU A 686
REMARK 465 LEU A 687
REMARK 465 PHE A 688
REMARK 465 LEU A 689
REMARK 465 ASN A 690
REMARK 465 ILE A 691
REMARK 465 LEU A 692
REMARK 465 ALA A 693
REMARK 465 PHE A 694
REMARK 465 ALA A 695
REMARK 465 ALA A 696
REMARK 465 LEU A 697
REMARK 465 TYR A 698
REMARK 465 TYR A 699
REMARK 465 LYS A 700
REMARK 465 ARG A 701
REMARK 465 ASP A 702
REMARK 465 ARG A 703
REMARK 465 ARG A 704
REMARK 465 GLN A 705
REMARK 465 GLU A 706
REMARK 465 LEU A 707
REMARK 465 ARG A 708
REMARK 465 CYS A 709
REMARK 465 ARG A 710
REMARK 465 ARG A 711
REMARK 465 LEU A 712
REMARK 465 SER A 713
REMARK 465 PRO A 714
REMARK 465 PRO A 715
REMARK 465 GLY A 716
REMARK 465 GLY A 717
REMARK 465 SER A 718
REMARK 465 GLY A 719
REMARK 465 SER A 720
REMARK 465 GLY A 721
REMARK 465 VAL A 722
REMARK 465 PRO A 723
REMARK 465 GLY A 724
REMARK 465 GLY A 725
REMARK 465 GLY A 726
REMARK 465 PRO A 727
REMARK 465 LEU A 728
REMARK 465 LEU A 729
REMARK 465 PRO A 730
REMARK 465 ALA A 731
REMARK 465 ALA A 732
REMARK 465 GLY A 733
REMARK 465 ARG A 734
REMARK 465 GLU A 735
REMARK 465 LEU A 736
REMARK 465 PRO A 737
REMARK 465 PRO A 738
REMARK 465 GLU A 739
REMARK 465 GLU A 740
REMARK 465 GLU A 741
REMARK 465 LEU A 742
REMARK 465 VAL A 743
REMARK 465 SER A 744
REMARK 465 LEU A 745
REMARK 465 GLN A 746
REMARK 465 LEU A 747
REMARK 465 LYS A 748
REMARK 465 ARG A 749
REMARK 465 GLY A 750
REMARK 465 GLY A 751
REMARK 465 GLY A 752
REMARK 465 VAL A 753
REMARK 465 GLY A 754
REMARK 465 ALA A 755
REMARK 465 ASP A 756
REMARK 465 PRO A 757
REMARK 465 ALA A 758
REMARK 465 GLU A 759
REMARK 465 ALA A 760
REMARK 465 LEU A 761
REMARK 465 ARG A 762
REMARK 465 PRO A 763
REMARK 465 ALA A 764
REMARK 465 CYS A 765
REMARK 465 PRO A 766
REMARK 465 PRO A 767
REMARK 465 ASP A 768
REMARK 465 TYR A 769
REMARK 465 THR A 770
REMARK 465 LEU A 771
REMARK 465 ALA A 772
REMARK 465 LEU A 773
REMARK 465 ARG A 774
REMARK 465 ARG A 775
REMARK 465 ALA A 776
REMARK 465 PRO A 777
REMARK 465 ASP A 778
REMARK 465 ASP A 779
REMARK 465 VAL A 780
REMARK 465 PRO A 781
REMARK 465 LEU A 782
REMARK 465 LEU A 783
REMARK 465 ALA A 784
REMARK 465 PRO A 785
REMARK 465 GLY A 786
REMARK 465 ALA A 787
REMARK 465 LEU A 788
REMARK 465 THR A 789
REMARK 465 LEU A 790
REMARK 465 LEU A 791
REMARK 465 PRO A 792
REMARK 465 SER A 793
REMARK 465 GLY A 794
REMARK 465 LEU A 795
REMARK 465 GLY A 796
REMARK 465 PRO 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 SER A 805
REMARK 465 LEU A 806
REMARK 465 HIS A 807
REMARK 465 PRO A 808
REMARK 465 PHE A 809
REMARK 465 GLY A 810
REMARK 465 PRO A 811
REMARK 465 PHE A 812
REMARK 465 PRO A 813
REMARK 465 PRO A 814
REMARK 465 PRO A 815
REMARK 465 PRO A 816
REMARK 465 PRO A 817
REMARK 465 THR A 818
REMARK 465 ALA A 819
REMARK 465 THR A 820
REMARK 465 SER A 821
REMARK 465 HIS A 822
REMARK 465 ASN A 823
REMARK 465 ASN A 824
REMARK 465 THR A 825
REMARK 465 LEU A 826
REMARK 465 PRO A 827
REMARK 465 HIS A 828
REMARK 465 PRO A 829
REMARK 465 HIS A 830
REMARK 465 SER A 831
REMARK 465 THR A 832
REMARK 465 THR A 833
REMARK 465 ARG A 834
REMARK 465 VAL A 835
REMARK 465 MET B 1
REMARK 465 TRP B 2
REMARK 465 LEU B 3
REMARK 465 LEU B 4
REMARK 465 ALA B 5
REMARK 465 LEU B 6
REMARK 465 CYS B 7
REMARK 465 LEU B 8
REMARK 465 VAL B 9
REMARK 465 GLY B 10
REMARK 465 LEU B 11
REMARK 465 ALA B 12
REMARK 465 GLY 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 PHE B 41
REMARK 465 THR B 150
REMARK 465 GLU B 151
REMARK 465 ASP B 152
REMARK 465 GLY B 153
REMARK 465 PRO B 154
REMARK 465 LEU B 155
REMARK 465 THR B 156
REMARK 465 LYS B 157
REMARK 465 LYS B 158
REMARK 465 ARG B 159
REMARK 465 ASP B 160
REMARK 465 GLU B 161
REMARK 465 ALA B 162
REMARK 465 THR B 163
REMARK 465 LEU B 164
REMARK 465 ASN B 165
REMARK 465 PRO B 166
REMARK 465 PRO B 167
REMARK 465 ASP B 168
REMARK 465 THR B 169
REMARK 465 ASP B 170
REMARK 465 ILE B 171
REMARK 465 ARG B 172
REMARK 465 ASP B 173
REMARK 465 PRO B 174
REMARK 465 ASP B 393
REMARK 465 SER B 394
REMARK 465 ALA B 395
REMARK 465 GLU B 396
REMARK 465 SER B 397
REMARK 465 GLU B 398
REMARK 465 ASP B 399
REMARK 465 GLY B 400
REMARK 465 GLN B 553
REMARK 465 ASP B 554
REMARK 465 THR B 555
REMARK 465 LYS B 556
REMARK 465 PHE B 557
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 ASN B 610
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 PRO B 633
REMARK 465 PRO B 634
REMARK 465 ALA B 635
REMARK 465 GLY B 636
REMARK 465 ALA B 637
REMARK 465 PRO B 638
REMARK 465 GLY B 639
REMARK 465 THR B 640
REMARK 465 ARG B 641
REMARK 465 ARG B 642
REMARK 465 PRO B 643
REMARK 465 PRO B 644
REMARK 465 PRO B 645
REMARK 465 PRO B 646
REMARK 465 ALA B 647
REMARK 465 THR B 648
REMARK 465 LEU B 649
REMARK 465 PRO B 650
REMARK 465 PRO B 651
REMARK 465 GLU B 652
REMARK 465 PRO B 653
REMARK 465 GLU B 654
REMARK 465 PRO B 655
REMARK 465 GLU B 656
REMARK 465 PRO B 657
REMARK 465 GLY B 658
REMARK 465 PRO B 659
REMARK 465 ARG B 660
REMARK 465 ALA B 661
REMARK 465 TYR B 662
REMARK 465 ASP B 663
REMARK 465 ARG B 664
REMARK 465 PHE B 665
REMARK 465 PRO B 666
REMARK 465 GLY B 667
REMARK 465 ASP B 668
REMARK 465 SER B 669
REMARK 465 ARG B 670
REMARK 465 ASP B 671
REMARK 465 TYR B 672
REMARK 465 SER B 673
REMARK 465 THR B 674
REMARK 465 GLU B 675
REMARK 465 LEU B 676
REMARK 465 SER B 677
REMARK 465 VAL B 678
REMARK 465 THR B 679
REMARK 465 VAL B 680
REMARK 465 ALA B 681
REMARK 465 VAL B 682
REMARK 465 GLY B 683
REMARK 465 ALA B 684
REMARK 465 SER B 685
REMARK 465 LEU B 686
REMARK 465 LEU B 687
REMARK 465 PHE B 688
REMARK 465 LEU B 689
REMARK 465 ASN B 690
REMARK 465 ILE B 691
REMARK 465 LEU B 692
REMARK 465 ALA B 693
REMARK 465 PHE B 694
REMARK 465 ALA B 695
REMARK 465 ALA B 696
REMARK 465 LEU B 697
REMARK 465 TYR B 698
REMARK 465 TYR B 699
REMARK 465 LYS B 700
REMARK 465 ARG B 701
REMARK 465 ASP B 702
REMARK 465 ARG B 703
REMARK 465 ARG B 704
REMARK 465 GLN B 705
REMARK 465 GLU B 706
REMARK 465 LEU B 707
REMARK 465 ARG B 708
REMARK 465 CYS B 709
REMARK 465 ARG B 710
REMARK 465 ARG B 711
REMARK 465 LEU B 712
REMARK 465 SER B 713
REMARK 465 PRO B 714
REMARK 465 PRO B 715
REMARK 465 GLY B 716
REMARK 465 GLY B 717
REMARK 465 SER B 718
REMARK 465 GLY B 719
REMARK 465 SER B 720
REMARK 465 GLY B 721
REMARK 465 VAL B 722
REMARK 465 PRO B 723
REMARK 465 GLY B 724
REMARK 465 GLY B 725
REMARK 465 GLY B 726
REMARK 465 PRO B 727
REMARK 465 LEU B 728
REMARK 465 LEU B 729
REMARK 465 PRO B 730
REMARK 465 ALA B 731
REMARK 465 ALA B 732
REMARK 465 GLY B 733
REMARK 465 ARG B 734
REMARK 465 GLU B 735
REMARK 465 LEU B 736
REMARK 465 PRO B 737
REMARK 465 PRO B 738
REMARK 465 GLU B 739
REMARK 465 GLU B 740
REMARK 465 GLU B 741
REMARK 465 LEU B 742
REMARK 465 VAL B 743
REMARK 465 SER B 744
REMARK 465 LEU B 745
REMARK 465 GLN B 746
REMARK 465 LEU B 747
REMARK 465 LYS B 748
REMARK 465 ARG B 749
REMARK 465 GLY B 750
REMARK 465 GLY B 751
REMARK 465 GLY B 752
REMARK 465 VAL B 753
REMARK 465 GLY B 754
REMARK 465 ALA B 755
REMARK 465 ASP B 756
REMARK 465 PRO B 757
REMARK 465 ALA B 758
REMARK 465 GLU B 759
REMARK 465 ALA B 760
REMARK 465 LEU B 761
REMARK 465 ARG B 762
REMARK 465 PRO B 763
REMARK 465 ALA B 764
REMARK 465 CYS B 765
REMARK 465 PRO B 766
REMARK 465 PRO B 767
REMARK 465 ASP B 768
REMARK 465 TYR B 769
REMARK 465 THR B 770
REMARK 465 LEU B 771
REMARK 465 ALA B 772
REMARK 465 LEU B 773
REMARK 465 ARG B 774
REMARK 465 ARG B 775
REMARK 465 ALA B 776
REMARK 465 PRO B 777
REMARK 465 ASP B 778
REMARK 465 ASP B 779
REMARK 465 VAL B 780
REMARK 465 PRO B 781
REMARK 465 LEU B 782
REMARK 465 LEU B 783
REMARK 465 ALA B 784
REMARK 465 PRO B 785
REMARK 465 GLY B 786
REMARK 465 ALA B 787
REMARK 465 LEU B 788
REMARK 465 THR B 789
REMARK 465 LEU B 790
REMARK 465 LEU B 791
REMARK 465 PRO B 792
REMARK 465 SER B 793
REMARK 465 GLY B 794
REMARK 465 LEU B 795
REMARK 465 GLY B 796
REMARK 465 PRO 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 SER B 805
REMARK 465 LEU B 806
REMARK 465 HIS B 807
REMARK 465 PRO B 808
REMARK 465 PHE B 809
REMARK 465 GLY B 810
REMARK 465 PRO B 811
REMARK 465 PHE B 812
REMARK 465 PRO B 813
REMARK 465 PRO B 814
REMARK 465 PRO B 815
REMARK 465 PRO B 816
REMARK 465 PRO B 817
REMARK 465 THR B 818
REMARK 465 ALA B 819
REMARK 465 THR B 820
REMARK 465 SER B 821
REMARK 465 HIS B 822
REMARK 465 ASN B 823
REMARK 465 ASN B 824
REMARK 465 THR B 825
REMARK 465 LEU B 826
REMARK 465 PRO B 827
REMARK 465 HIS B 828
REMARK 465 PRO B 829
REMARK 465 HIS B 830
REMARK 465 SER B 831
REMARK 465 THR B 832
REMARK 465 THR B 833
REMARK 465 ARG B 834
REMARK 465 VAL B 835
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 ARG A 82 47.67 -94.49
REMARK 500 PRO A 120 -177.31 -69.30
REMARK 500 ASP A 197 93.48 -68.74
REMARK 500 LEU A 219 47.31 -83.34
REMARK 500 CYS A 270 49.16 -92.58
REMARK 500 LEU A 283 -61.19 -94.10
REMARK 500 GLN A 303 54.72 -145.18
REMARK 500 ALA A 323 54.03 -94.09
REMARK 500 CYS A 328 -32.59 -131.20
REMARK 500 ALA A 499 62.65 62.32
REMARK 500 TRP A 538 0.87 -64.19
REMARK 500 ARG A 564 -6.91 71.67
REMARK 500 HIS A 582 67.07 61.03
REMARK 500 PRO A 587 77.58 -68.40
REMARK 500 ARG B 82 47.67 -94.49
REMARK 500 PRO B 120 -177.33 -69.30
REMARK 500 ASP B 197 93.48 -68.74
REMARK 500 LEU B 219 47.31 -83.39
REMARK 500 CYS B 270 49.15 -92.51
REMARK 500 LEU B 283 -61.13 -94.17
REMARK 500 GLN B 303 54.71 -145.23
REMARK 500 ALA B 323 54.03 -94.09
REMARK 500 CYS B 328 -32.59 -131.20
REMARK 500 ALA B 499 62.69 62.32
REMARK 500 TRP B 538 0.87 -64.19
REMARK 500 ARG B 564 -6.91 71.67
REMARK 500 HIS B 582 67.07 61.03
REMARK 500 PRO B 587 77.58 -68.40
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 CYS A 106 PRO A 107 -146.14
REMARK 500 ALA A 462 PRO A 463 141.19
REMARK 500 CYS B 106 PRO B 107 -146.12
REMARK 500 ALA B 462 PRO B 463 141.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: EMD-34220 RELATED DB: EMDB
REMARK 900 CRYO-EM STRUCTURE OF HUMAN NEUROLIGIN 2
DBREF 8GS4 A 1 835 UNP Q8NFZ4 NLGN2_HUMAN 1 835
DBREF 8GS4 B 1 835 UNP Q8NFZ4 NLGN2_HUMAN 1 835
SEQRES 1 A 835 MET TRP LEU LEU ALA LEU CYS LEU VAL GLY LEU ALA GLY
SEQRES 2 A 835 ALA GLN ARG GLY GLY GLY GLY PRO GLY GLY GLY ALA PRO
SEQRES 3 A 835 GLY GLY PRO GLY LEU GLY LEU GLY SER LEU GLY GLU GLU
SEQRES 4 A 835 ARG PHE PRO VAL VAL ASN THR ALA TYR GLY ARG VAL ARG
SEQRES 5 A 835 GLY VAL ARG ARG GLU LEU ASN ASN GLU ILE LEU GLY PRO
SEQRES 6 A 835 VAL VAL GLN PHE LEU GLY VAL PRO TYR ALA THR PRO PRO
SEQRES 7 A 835 LEU GLY ALA ARG ARG PHE GLN PRO PRO GLU ALA PRO ALA
SEQRES 8 A 835 SER TRP PRO GLY VAL ARG ASN ALA THR THR LEU PRO PRO
SEQRES 9 A 835 ALA CYS PRO GLN ASN LEU HIS GLY ALA LEU PRO ALA ILE
SEQRES 10 A 835 MET LEU PRO VAL TRP PHE THR ASP ASN LEU GLU ALA ALA
SEQRES 11 A 835 ALA THR TYR VAL GLN ASN GLN SER GLU ASP CYS LEU TYR
SEQRES 12 A 835 LEU ASN LEU TYR VAL PRO THR GLU ASP GLY PRO LEU THR
SEQRES 13 A 835 LYS LYS ARG ASP GLU ALA THR LEU ASN PRO PRO ASP THR
SEQRES 14 A 835 ASP ILE ARG ASP PRO GLY LYS LYS PRO VAL MET LEU PHE
SEQRES 15 A 835 LEU HIS GLY GLY SER TYR MET GLU GLY THR GLY ASN MET
SEQRES 16 A 835 PHE ASP GLY SER VAL LEU ALA ALA TYR GLY ASN VAL ILE
SEQRES 17 A 835 VAL ALA THR LEU ASN TYR ARG LEU GLY VAL LEU GLY PHE
SEQRES 18 A 835 LEU SER THR GLY ASP GLN ALA ALA LYS GLY ASN TYR GLY
SEQRES 19 A 835 LEU LEU ASP GLN ILE GLN ALA LEU ARG TRP LEU SER GLU
SEQRES 20 A 835 ASN ILE ALA HIS PHE GLY GLY ASP PRO GLU ARG ILE THR
SEQRES 21 A 835 ILE PHE GLY SER GLY ALA GLY ALA SER CYS VAL ASN LEU
SEQRES 22 A 835 LEU ILE LEU SER HIS HIS SER GLU GLY LEU PHE GLN LYS
SEQRES 23 A 835 ALA ILE ALA GLN SER GLY THR ALA ILE SER SER TRP SER
SEQRES 24 A 835 VAL ASN TYR GLN PRO LEU LYS TYR THR ARG LEU LEU ALA
SEQRES 25 A 835 ALA LYS VAL GLY CYS ASP ARG GLU ASP SER ALA GLU ALA
SEQRES 26 A 835 VAL GLU CYS LEU ARG ARG LYS PRO SER ARG GLU LEU VAL
SEQRES 27 A 835 ASP GLN ASP VAL GLN PRO ALA ARG TYR HIS ILE ALA PHE
SEQRES 28 A 835 GLY PRO VAL VAL ASP GLY ASP VAL VAL PRO ASP ASP PRO
SEQRES 29 A 835 GLU ILE LEU MET GLN GLN GLY GLU PHE LEU ASN TYR ASP
SEQRES 30 A 835 MET LEU ILE GLY VAL ASN GLN GLY GLU GLY LEU LYS PHE
SEQRES 31 A 835 VAL GLU ASP SER ALA GLU SER GLU ASP GLY VAL SER ALA
SEQRES 32 A 835 SER ALA PHE ASP PHE THR VAL SER ASN PHE VAL ASP ASN
SEQRES 33 A 835 LEU TYR GLY TYR PRO GLU GLY LYS ASP VAL LEU ARG GLU
SEQRES 34 A 835 THR ILE LYS PHE MET TYR THR ASP TRP ALA ASP ARG ASP
SEQRES 35 A 835 ASN GLY GLU MET ARG ARG LYS THR LEU LEU ALA LEU PHE
SEQRES 36 A 835 THR ASP HIS GLN TRP VAL ALA PRO ALA VAL ALA THR ALA
SEQRES 37 A 835 LYS LEU HIS ALA ASP TYR GLN SER PRO VAL TYR PHE TYR
SEQRES 38 A 835 THR PHE TYR HIS HIS CYS GLN ALA GLU GLY ARG PRO GLU
SEQRES 39 A 835 TRP ALA ASP ALA ALA HIS GLY ASP GLU LEU PRO TYR VAL
SEQRES 40 A 835 PHE GLY VAL PRO MET VAL GLY ALA THR ASP LEU PHE PRO
SEQRES 41 A 835 CYS ASN PHE SER LYS ASN ASP VAL MET LEU SER ALA VAL
SEQRES 42 A 835 VAL MET THR TYR TRP THR ASN PHE ALA LYS THR GLY ASP
SEQRES 43 A 835 PRO ASN GLN PRO VAL PRO GLN ASP THR LYS PHE ILE HIS
SEQRES 44 A 835 THR LYS PRO ASN ARG PHE GLU GLU VAL VAL TRP SER LYS
SEQRES 45 A 835 PHE ASN SER LYS GLU LYS GLN TYR LEU HIS ILE GLY LEU
SEQRES 46 A 835 LYS PRO ARG VAL ARG ASP ASN TYR ARG ALA ASN LYS VAL
SEQRES 47 A 835 ALA PHE TRP LEU GLU LEU VAL PRO HIS LEU HIS ASN LEU
SEQRES 48 A 835 HIS THR GLU LEU PHE THR THR THR THR ARG LEU PRO PRO
SEQRES 49 A 835 TYR ALA THR ARG TRP PRO PRO ARG PRO PRO ALA GLY ALA
SEQRES 50 A 835 PRO GLY THR ARG ARG PRO PRO PRO PRO ALA THR LEU PRO
SEQRES 51 A 835 PRO GLU PRO GLU PRO GLU PRO GLY PRO ARG ALA TYR ASP
SEQRES 52 A 835 ARG PHE PRO GLY ASP SER ARG ASP TYR SER THR GLU LEU
SEQRES 53 A 835 SER VAL THR VAL ALA VAL GLY ALA SER LEU LEU PHE LEU
SEQRES 54 A 835 ASN ILE LEU ALA PHE ALA ALA LEU TYR TYR LYS ARG ASP
SEQRES 55 A 835 ARG ARG GLN GLU LEU ARG CYS ARG ARG LEU SER PRO PRO
SEQRES 56 A 835 GLY GLY SER GLY SER GLY VAL PRO GLY GLY GLY PRO LEU
SEQRES 57 A 835 LEU PRO ALA ALA GLY ARG GLU LEU PRO PRO GLU GLU GLU
SEQRES 58 A 835 LEU VAL SER LEU GLN LEU LYS ARG GLY GLY GLY VAL GLY
SEQRES 59 A 835 ALA ASP PRO ALA GLU ALA LEU ARG PRO ALA CYS PRO PRO
SEQRES 60 A 835 ASP TYR THR LEU ALA LEU ARG ARG ALA PRO ASP ASP VAL
SEQRES 61 A 835 PRO LEU LEU ALA PRO GLY ALA LEU THR LEU LEU PRO SER
SEQRES 62 A 835 GLY LEU GLY PRO PRO PRO PRO PRO PRO PRO PRO SER LEU
SEQRES 63 A 835 HIS PRO PHE GLY PRO PHE PRO PRO PRO PRO PRO THR ALA
SEQRES 64 A 835 THR SER HIS ASN ASN THR LEU PRO HIS PRO HIS SER THR
SEQRES 65 A 835 THR ARG VAL
SEQRES 1 B 835 MET TRP LEU LEU ALA LEU CYS LEU VAL GLY LEU ALA GLY
SEQRES 2 B 835 ALA GLN ARG GLY GLY GLY GLY PRO GLY GLY GLY ALA PRO
SEQRES 3 B 835 GLY GLY PRO GLY LEU GLY LEU GLY SER LEU GLY GLU GLU
SEQRES 4 B 835 ARG PHE PRO VAL VAL ASN THR ALA TYR GLY ARG VAL ARG
SEQRES 5 B 835 GLY VAL ARG ARG GLU LEU ASN ASN GLU ILE LEU GLY PRO
SEQRES 6 B 835 VAL VAL GLN PHE LEU GLY VAL PRO TYR ALA THR PRO PRO
SEQRES 7 B 835 LEU GLY ALA ARG ARG PHE GLN PRO PRO GLU ALA PRO ALA
SEQRES 8 B 835 SER TRP PRO GLY VAL ARG ASN ALA THR THR LEU PRO PRO
SEQRES 9 B 835 ALA CYS PRO GLN ASN LEU HIS GLY ALA LEU PRO ALA ILE
SEQRES 10 B 835 MET LEU PRO VAL TRP PHE THR ASP ASN LEU GLU ALA ALA
SEQRES 11 B 835 ALA THR TYR VAL GLN ASN GLN SER GLU ASP CYS LEU TYR
SEQRES 12 B 835 LEU ASN LEU TYR VAL PRO THR GLU ASP GLY PRO LEU THR
SEQRES 13 B 835 LYS LYS ARG ASP GLU ALA THR LEU ASN PRO PRO ASP THR
SEQRES 14 B 835 ASP ILE ARG ASP PRO GLY LYS LYS PRO VAL MET LEU PHE
SEQRES 15 B 835 LEU HIS GLY GLY SER TYR MET GLU GLY THR GLY ASN MET
SEQRES 16 B 835 PHE ASP GLY SER VAL LEU ALA ALA TYR GLY ASN VAL ILE
SEQRES 17 B 835 VAL ALA THR LEU ASN TYR ARG LEU GLY VAL LEU GLY PHE
SEQRES 18 B 835 LEU SER THR GLY ASP GLN ALA ALA LYS GLY ASN TYR GLY
SEQRES 19 B 835 LEU LEU ASP GLN ILE GLN ALA LEU ARG TRP LEU SER GLU
SEQRES 20 B 835 ASN ILE ALA HIS PHE GLY GLY ASP PRO GLU ARG ILE THR
SEQRES 21 B 835 ILE PHE GLY SER GLY ALA GLY ALA SER CYS VAL ASN LEU
SEQRES 22 B 835 LEU ILE LEU SER HIS HIS SER GLU GLY LEU PHE GLN LYS
SEQRES 23 B 835 ALA ILE ALA GLN SER GLY THR ALA ILE SER SER TRP SER
SEQRES 24 B 835 VAL ASN TYR GLN PRO LEU LYS TYR THR ARG LEU LEU ALA
SEQRES 25 B 835 ALA LYS VAL GLY CYS ASP ARG GLU ASP SER ALA GLU ALA
SEQRES 26 B 835 VAL GLU CYS LEU ARG ARG LYS PRO SER ARG GLU LEU VAL
SEQRES 27 B 835 ASP GLN ASP VAL GLN PRO ALA ARG TYR HIS ILE ALA PHE
SEQRES 28 B 835 GLY PRO VAL VAL ASP GLY ASP VAL VAL PRO ASP ASP PRO
SEQRES 29 B 835 GLU ILE LEU MET GLN GLN GLY GLU PHE LEU ASN TYR ASP
SEQRES 30 B 835 MET LEU ILE GLY VAL ASN GLN GLY GLU GLY LEU LYS PHE
SEQRES 31 B 835 VAL GLU ASP SER ALA GLU SER GLU ASP GLY VAL SER ALA
SEQRES 32 B 835 SER ALA PHE ASP PHE THR VAL SER ASN PHE VAL ASP ASN
SEQRES 33 B 835 LEU TYR GLY TYR PRO GLU GLY LYS ASP VAL LEU ARG GLU
SEQRES 34 B 835 THR ILE LYS PHE MET TYR THR ASP TRP ALA ASP ARG ASP
SEQRES 35 B 835 ASN GLY GLU MET ARG ARG LYS THR LEU LEU ALA LEU PHE
SEQRES 36 B 835 THR ASP HIS GLN TRP VAL ALA PRO ALA VAL ALA THR ALA
SEQRES 37 B 835 LYS LEU HIS ALA ASP TYR GLN SER PRO VAL TYR PHE TYR
SEQRES 38 B 835 THR PHE TYR HIS HIS CYS GLN ALA GLU GLY ARG PRO GLU
SEQRES 39 B 835 TRP ALA ASP ALA ALA HIS GLY ASP GLU LEU PRO TYR VAL
SEQRES 40 B 835 PHE GLY VAL PRO MET VAL GLY ALA THR ASP LEU PHE PRO
SEQRES 41 B 835 CYS ASN PHE SER LYS ASN ASP VAL MET LEU SER ALA VAL
SEQRES 42 B 835 VAL MET THR TYR TRP THR ASN PHE ALA LYS THR GLY ASP
SEQRES 43 B 835 PRO ASN GLN PRO VAL PRO GLN ASP THR LYS PHE ILE HIS
SEQRES 44 B 835 THR LYS PRO ASN ARG PHE GLU GLU VAL VAL TRP SER LYS
SEQRES 45 B 835 PHE ASN SER LYS GLU LYS GLN TYR LEU HIS ILE GLY LEU
SEQRES 46 B 835 LYS PRO ARG VAL ARG ASP ASN TYR ARG ALA ASN LYS VAL
SEQRES 47 B 835 ALA PHE TRP LEU GLU LEU VAL PRO HIS LEU HIS ASN LEU
SEQRES 48 B 835 HIS THR GLU LEU PHE THR THR THR THR ARG LEU PRO PRO
SEQRES 49 B 835 TYR ALA THR ARG TRP PRO PRO ARG PRO PRO ALA GLY ALA
SEQRES 50 B 835 PRO GLY THR ARG ARG PRO PRO PRO PRO ALA THR LEU PRO
SEQRES 51 B 835 PRO GLU PRO GLU PRO GLU PRO GLY PRO ARG ALA TYR ASP
SEQRES 52 B 835 ARG PHE PRO GLY ASP SER ARG ASP TYR SER THR GLU LEU
SEQRES 53 B 835 SER VAL THR VAL ALA VAL GLY ALA SER LEU LEU PHE LEU
SEQRES 54 B 835 ASN ILE LEU ALA PHE ALA ALA LEU TYR TYR LYS ARG ASP
SEQRES 55 B 835 ARG ARG GLN GLU LEU ARG CYS ARG ARG LEU SER PRO PRO
SEQRES 56 B 835 GLY GLY SER GLY SER GLY VAL PRO GLY GLY GLY PRO LEU
SEQRES 57 B 835 LEU PRO ALA ALA GLY ARG GLU LEU PRO PRO GLU GLU GLU
SEQRES 58 B 835 LEU VAL SER LEU GLN LEU LYS ARG GLY GLY GLY VAL GLY
SEQRES 59 B 835 ALA ASP PRO ALA GLU ALA LEU ARG PRO ALA CYS PRO PRO
SEQRES 60 B 835 ASP TYR THR LEU ALA LEU ARG ARG ALA PRO ASP ASP VAL
SEQRES 61 B 835 PRO LEU LEU ALA PRO GLY ALA LEU THR LEU LEU PRO SER
SEQRES 62 B 835 GLY LEU GLY PRO PRO PRO PRO PRO PRO PRO PRO SER LEU
SEQRES 63 B 835 HIS PRO PHE GLY PRO PHE PRO PRO PRO PRO PRO THR ALA
SEQRES 64 B 835 THR SER HIS ASN ASN THR LEU PRO HIS PRO HIS SER THR
SEQRES 65 B 835 THR ARG VAL
HELIX 1 AA1 PRO A 120 ASN A 126 1 7
HELIX 2 AA2 ASN A 126 THR A 132 1 7
HELIX 3 AA3 GLY A 193 ASP A 197 5 5
HELIX 4 AA4 SER A 199 GLY A 205 1 7
HELIX 5 AA5 GLY A 217 PHE A 221 5 5
HELIX 6 AA6 ASN A 232 ASN A 248 1 17
HELIX 7 AA7 GLY A 265 GLY A 267 5 3
HELIX 8 AA8 ALA A 268 LEU A 273 1 6
HELIX 9 AA9 GLN A 303 ARG A 309 1 7
HELIX 10 AB1 ALA A 325 ARG A 330 1 6
HELIX 11 AB2 ASP A 363 MET A 368 1 6
HELIX 12 AB3 ALA A 405 LEU A 417 1 13
HELIX 13 AB4 GLY A 423 TYR A 435 1 13
HELIX 14 AB5 ASP A 437 ARG A 441 5 5
HELIX 15 AB6 THR A 450 ALA A 453 5 4
HELIX 16 AB7 LEU A 454 TRP A 460 1 7
HELIX 17 AB8 PRO A 463 TYR A 474 1 12
HELIX 18 AB9 GLU A 503 GLY A 509 1 7
HELIX 19 AC1 VAL A 510 GLY A 514 5 5
HELIX 20 AC2 ASN A 526 GLY A 545 1 20
HELIX 21 AC3 ARG A 594 LEU A 604 1 11
HELIX 22 AC4 LEU A 604 HIS A 609 1 6
HELIX 23 AC5 PRO B 120 ASN B 126 1 7
HELIX 24 AC6 ASN B 126 THR B 132 1 7
HELIX 25 AC7 GLY B 193 ASP B 197 5 5
HELIX 26 AC8 SER B 199 GLY B 205 1 7
HELIX 27 AC9 GLY B 217 PHE B 221 5 5
HELIX 28 AD1 ASN B 232 ASN B 248 1 17
HELIX 29 AD2 GLY B 265 GLY B 267 5 3
HELIX 30 AD3 ALA B 268 LEU B 273 1 6
HELIX 31 AD4 GLN B 303 ARG B 309 1 7
HELIX 32 AD5 ALA B 325 ARG B 330 1 6
HELIX 33 AD6 ASP B 363 MET B 368 1 6
HELIX 34 AD7 ALA B 405 LEU B 417 1 13
HELIX 35 AD8 GLY B 423 TYR B 435 1 13
HELIX 36 AD9 ASP B 437 ARG B 441 5 5
HELIX 37 AE1 THR B 450 ALA B 453 5 4
HELIX 38 AE2 LEU B 454 TRP B 460 1 7
HELIX 39 AE3 PRO B 463 TYR B 474 1 12
HELIX 40 AE4 GLU B 503 GLY B 509 1 7
HELIX 41 AE5 VAL B 510 GLY B 514 5 5
HELIX 42 AE6 ASN B 526 GLY B 545 1 20
HELIX 43 AE7 ARG B 594 LEU B 604 1 11
HELIX 44 AE8 LEU B 604 HIS B 609 1 6
SHEET 1 AA1 2 VAL A 44 THR A 46 0
SHEET 2 AA1 2 GLY A 49 VAL A 51 -1 O VAL A 51 N VAL A 44
SHEET 1 AA2 2 VAL A 54 GLU A 57 0
SHEET 2 AA2 2 PRO A 65 GLN A 68 -1 O GLN A 68 N VAL A 54
SHEET 1 AA3 2 VAL A 72 PRO A 73 0
SHEET 2 AA3 2 TYR A 143 LEU A 144 -1 O LEU A 144 N VAL A 72
SHEET 1 AA4 3 ILE A 208 ALA A 210 0
SHEET 2 AA4 3 LYS A 177 LEU A 183 1 N PHE A 182 O ALA A 210
SHEET 3 AA4 3 GLY A 254 ILE A 259 1 O ASP A 255 N LYS A 177
SHEET 1 AA5 3 ILE A 208 ALA A 210 0
SHEET 2 AA5 3 LYS A 177 LEU A 183 1 N PHE A 182 O ALA A 210
SHEET 3 AA5 3 PHE A 262 GLY A 263 1 O PHE A 262 N LEU A 181
SHEET 1 AA6 3 ALA A 289 GLN A 290 0
SHEET 2 AA6 3 ILE A 380 ASN A 383 1 N GLY A 381 O ALA A 289
SHEET 3 AA6 3 THR A 482 PHE A 483 1 O PHE A 483 N VAL A 382
SHEET 1 AA7 2 VAL B 44 THR B 46 0
SHEET 2 AA7 2 GLY B 49 VAL B 51 -1 O VAL B 51 N VAL B 44
SHEET 1 AA8 2 VAL B 54 GLU B 57 0
SHEET 2 AA8 2 PRO B 65 GLN B 68 -1 O GLN B 68 N VAL B 54
SHEET 1 AA9 2 VAL B 72 PRO B 73 0
SHEET 2 AA9 2 TYR B 143 LEU B 144 -1 O LEU B 144 N VAL B 72
SHEET 1 AB1 3 ILE B 208 ALA B 210 0
SHEET 2 AB1 3 LYS B 177 LEU B 183 1 N PHE B 182 O ALA B 210
SHEET 3 AB1 3 GLY B 254 ILE B 259 1 O ASP B 255 N LYS B 177
SHEET 1 AB2 3 ILE B 208 ALA B 210 0
SHEET 2 AB2 3 LYS B 177 LEU B 183 1 N PHE B 182 O ALA B 210
SHEET 3 AB2 3 PHE B 262 GLY B 263 1 O PHE B 262 N LEU B 181
SHEET 1 AB3 3 ALA B 289 GLN B 290 0
SHEET 2 AB3 3 ILE B 380 ASN B 383 1 N GLY B 381 O ALA B 289
SHEET 3 AB3 3 THR B 482 PHE B 483 1 O PHE B 483 N VAL B 382
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
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 4126 HIS A 609
TER 8252 HIS B 609
MASTER 785 0 0 44 30 0 0 6 8250 2 12 130
END |