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HEADER MEMBRANE PROTEIN 04-SEP-22 8GS3
TITLE CRYO-EM STRUCTURE OF HUMAN NEUROLIGIN 3
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NEUROLIGIN-3;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: GLIOTACTIN HOMOLOG;
COMPND 5 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: NLGN3, NL3;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: HEK293
KEYWDS NEUROLIGIN, SYNAPSE PROTEIN, PLASMA MEMBRANE, MEMBRANE PROTEIN
EXPDTA ELECTRON MICROSCOPY
AUTHOR H.W.ZHANG,Z.Z.ZHANG,M.Z.HOU
REVDAT 1 20-SEP-23 8GS3 0
JRNL AUTH H.W.ZHANG,Z.Z.ZHANG,M.Z.HOU
JRNL TITL CRYO-EM STRUCTURE OF HUMAN NEUROLIGIN 3
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 3.90 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) : 3.900
REMARK 3 NUMBER OF PARTICLES : 255939
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 8GS3 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_1300031994.
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 3
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 K2 SUMMIT (4K X 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 ARG A 4
REMARK 465 LEU A 5
REMARK 465 GLY A 6
REMARK 465 PRO A 7
REMARK 465 PRO A 8
REMARK 465 SER A 9
REMARK 465 LEU A 10
REMARK 465 SER A 11
REMARK 465 LEU A 12
REMARK 465 SER A 13
REMARK 465 PRO A 14
REMARK 465 LYS A 15
REMARK 465 PRO A 16
REMARK 465 THR A 17
REMARK 465 VAL A 18
REMARK 465 GLY A 19
REMARK 465 ARG A 20
REMARK 465 SER A 21
REMARK 465 LEU A 22
REMARK 465 CYS A 23
REMARK 465 LEU A 24
REMARK 465 THR A 25
REMARK 465 LEU A 26
REMARK 465 TRP A 27
REMARK 465 PHE A 28
REMARK 465 LEU A 29
REMARK 465 SER A 30
REMARK 465 LEU A 31
REMARK 465 ALA A 32
REMARK 465 LEU A 33
REMARK 465 ARG A 34
REMARK 465 ALA A 35
REMARK 465 SER A 36
REMARK 465 THR A 37
REMARK 465 GLN A 38
REMARK 465 ALA A 39
REMARK 465 PRO A 40
REMARK 465 GLU A 151
REMARK 465 ASP A 152
REMARK 465 VAL A 153
REMARK 465 LYS A 154
REMARK 465 ARG A 155
REMARK 465 ILE A 156
REMARK 465 SER A 157
REMARK 465 LYS A 158
REMARK 465 GLU A 159
REMARK 465 CYS A 160
REMARK 465 ALA A 161
REMARK 465 ARG A 162
REMARK 465 LYS A 163
REMARK 465 PRO A 164
REMARK 465 ASN A 165
REMARK 465 LYS A 166
REMARK 465 LYS A 167
REMARK 465 ILE A 168
REMARK 465 CYS A 169
REMARK 465 ARG A 170
REMARK 465 LYS A 171
REMARK 465 GLY A 172
REMARK 465 GLY A 173
REMARK 465 SER A 174
REMARK 465 GLY A 175
REMARK 465 ALA A 176
REMARK 465 LYS A 177
REMARK 465 LYS A 178
REMARK 465 GLN A 179
REMARK 465 GLY A 180
REMARK 465 GLU A 181
REMARK 465 ASP A 182
REMARK 465 LEU A 183
REMARK 465 ALA A 184
REMARK 465 ASP A 185
REMARK 465 ASN A 186
REMARK 465 ASP A 187
REMARK 465 GLY A 188
REMARK 465 ASP A 189
REMARK 465 GLU A 190
REMARK 465 ASP A 191
REMARK 465 GLU A 192
REMARK 465 ASP A 193
REMARK 465 ILE A 194
REMARK 465 ARG A 195
REMARK 465 ASP A 196
REMARK 465 THR A 578
REMARK 465 LYS A 579
REMARK 465 PHE A 580
REMARK 465 ILE A 581
REMARK 465 HIS A 582
REMARK 465 THR A 583
REMARK 465 LYS A 584
REMARK 465 ALA A 585
REMARK 465 ASN A 586
REMARK 465 ARG A 587
REMARK 465 PHE A 588
REMARK 465 GLU A 589
REMARK 465 GLU A 590
REMARK 465 LEU A 634
REMARK 465 HIS A 635
REMARK 465 ASP A 636
REMARK 465 MET A 637
REMARK 465 PHE A 638
REMARK 465 HIS A 639
REMARK 465 TYR A 640
REMARK 465 THR A 641
REMARK 465 SER A 642
REMARK 465 THR A 643
REMARK 465 THR A 644
REMARK 465 THR A 645
REMARK 465 LYS A 646
REMARK 465 VAL A 647
REMARK 465 PRO A 648
REMARK 465 PRO A 649
REMARK 465 PRO A 650
REMARK 465 ASP A 651
REMARK 465 THR A 652
REMARK 465 THR A 653
REMARK 465 HIS A 654
REMARK 465 SER A 655
REMARK 465 SER A 656
REMARK 465 HIS A 657
REMARK 465 ILE A 658
REMARK 465 THR A 659
REMARK 465 ARG A 660
REMARK 465 ARG A 661
REMARK 465 PRO A 662
REMARK 465 ASN A 663
REMARK 465 GLY A 664
REMARK 465 LYS A 665
REMARK 465 THR A 666
REMARK 465 TRP A 667
REMARK 465 SER A 668
REMARK 465 THR A 669
REMARK 465 LYS A 670
REMARK 465 ARG A 671
REMARK 465 PRO A 672
REMARK 465 ALA A 673
REMARK 465 ILE A 674
REMARK 465 SER A 675
REMARK 465 PRO A 676
REMARK 465 ALA A 677
REMARK 465 TYR A 678
REMARK 465 SER A 679
REMARK 465 ASN A 680
REMARK 465 GLU A 681
REMARK 465 ASN A 682
REMARK 465 ALA A 683
REMARK 465 GLN A 684
REMARK 465 GLY A 685
REMARK 465 SER A 686
REMARK 465 TRP A 687
REMARK 465 ASN A 688
REMARK 465 GLY A 689
REMARK 465 ASP A 690
REMARK 465 GLN A 691
REMARK 465 ASP A 692
REMARK 465 ALA A 693
REMARK 465 GLY A 694
REMARK 465 PRO A 695
REMARK 465 LEU A 696
REMARK 465 LEU A 697
REMARK 465 VAL A 698
REMARK 465 GLU A 699
REMARK 465 ASN A 700
REMARK 465 PRO A 701
REMARK 465 ARG A 702
REMARK 465 ASP A 703
REMARK 465 TYR A 704
REMARK 465 SER A 705
REMARK 465 THR A 706
REMARK 465 GLU A 707
REMARK 465 LEU A 708
REMARK 465 SER A 709
REMARK 465 VAL A 710
REMARK 465 THR A 711
REMARK 465 ILE A 712
REMARK 465 ALA A 713
REMARK 465 VAL A 714
REMARK 465 GLY A 715
REMARK 465 ALA A 716
REMARK 465 SER A 717
REMARK 465 LEU A 718
REMARK 465 LEU A 719
REMARK 465 PHE A 720
REMARK 465 LEU A 721
REMARK 465 ASN A 722
REMARK 465 VAL A 723
REMARK 465 LEU A 724
REMARK 465 ALA A 725
REMARK 465 PHE A 726
REMARK 465 ALA A 727
REMARK 465 ALA A 728
REMARK 465 LEU A 729
REMARK 465 TYR A 730
REMARK 465 TYR A 731
REMARK 465 ARG A 732
REMARK 465 LYS A 733
REMARK 465 ASP A 734
REMARK 465 LYS A 735
REMARK 465 ARG A 736
REMARK 465 ARG A 737
REMARK 465 GLN A 738
REMARK 465 GLU A 739
REMARK 465 PRO A 740
REMARK 465 LEU A 741
REMARK 465 ARG A 742
REMARK 465 GLN A 743
REMARK 465 PRO A 744
REMARK 465 SER A 745
REMARK 465 PRO A 746
REMARK 465 GLN A 747
REMARK 465 ARG A 748
REMARK 465 GLY A 749
REMARK 465 ALA A 750
REMARK 465 GLY A 751
REMARK 465 ALA A 752
REMARK 465 PRO A 753
REMARK 465 GLU A 754
REMARK 465 LEU A 755
REMARK 465 GLY A 756
REMARK 465 ALA A 757
REMARK 465 ALA A 758
REMARK 465 PRO A 759
REMARK 465 GLU A 760
REMARK 465 GLU A 761
REMARK 465 GLU A 762
REMARK 465 LEU A 763
REMARK 465 ALA A 764
REMARK 465 ALA A 765
REMARK 465 LEU A 766
REMARK 465 GLN A 767
REMARK 465 LEU A 768
REMARK 465 GLY A 769
REMARK 465 PRO A 770
REMARK 465 THR A 771
REMARK 465 HIS A 772
REMARK 465 HIS A 773
REMARK 465 GLU A 774
REMARK 465 CYS A 775
REMARK 465 GLU A 776
REMARK 465 ALA A 777
REMARK 465 GLY A 778
REMARK 465 PRO A 779
REMARK 465 PRO A 780
REMARK 465 HIS A 781
REMARK 465 ASP A 782
REMARK 465 THR A 783
REMARK 465 LEU A 784
REMARK 465 ARG A 785
REMARK 465 LEU A 786
REMARK 465 THR A 787
REMARK 465 ALA A 788
REMARK 465 LEU A 789
REMARK 465 PRO A 790
REMARK 465 ASP A 791
REMARK 465 TYR A 792
REMARK 465 THR A 793
REMARK 465 LEU A 794
REMARK 465 THR A 795
REMARK 465 LEU A 796
REMARK 465 ARG A 797
REMARK 465 ARG A 798
REMARK 465 SER A 799
REMARK 465 PRO A 800
REMARK 465 ASP A 801
REMARK 465 ASP A 802
REMARK 465 ILE A 803
REMARK 465 PRO A 804
REMARK 465 LEU A 805
REMARK 465 MET A 806
REMARK 465 THR A 807
REMARK 465 PRO A 808
REMARK 465 ASN A 809
REMARK 465 THR A 810
REMARK 465 ILE A 811
REMARK 465 THR A 812
REMARK 465 MET A 813
REMARK 465 ILE A 814
REMARK 465 PRO A 815
REMARK 465 ASN A 816
REMARK 465 SER A 817
REMARK 465 LEU A 818
REMARK 465 VAL A 819
REMARK 465 GLY A 820
REMARK 465 LEU A 821
REMARK 465 GLN A 822
REMARK 465 THR A 823
REMARK 465 LEU A 824
REMARK 465 HIS A 825
REMARK 465 PRO A 826
REMARK 465 TYR A 827
REMARK 465 ASN A 828
REMARK 465 THR A 829
REMARK 465 PHE A 830
REMARK 465 ALA A 831
REMARK 465 ALA A 832
REMARK 465 GLY A 833
REMARK 465 PHE A 834
REMARK 465 ASN A 835
REMARK 465 SER A 836
REMARK 465 THR A 837
REMARK 465 GLY A 838
REMARK 465 LEU A 839
REMARK 465 PRO A 840
REMARK 465 HIS A 841
REMARK 465 SER A 842
REMARK 465 HIS A 843
REMARK 465 SER A 844
REMARK 465 THR A 845
REMARK 465 THR A 846
REMARK 465 ARG A 847
REMARK 465 VAL A 848
REMARK 465 MET B 1
REMARK 465 TRP B 2
REMARK 465 LEU B 3
REMARK 465 ARG B 4
REMARK 465 LEU B 5
REMARK 465 GLY B 6
REMARK 465 PRO B 7
REMARK 465 PRO B 8
REMARK 465 SER B 9
REMARK 465 LEU B 10
REMARK 465 SER B 11
REMARK 465 LEU B 12
REMARK 465 SER B 13
REMARK 465 PRO B 14
REMARK 465 LYS B 15
REMARK 465 PRO B 16
REMARK 465 THR B 17
REMARK 465 VAL B 18
REMARK 465 GLY B 19
REMARK 465 ARG B 20
REMARK 465 SER B 21
REMARK 465 LEU B 22
REMARK 465 CYS B 23
REMARK 465 LEU B 24
REMARK 465 THR B 25
REMARK 465 LEU B 26
REMARK 465 TRP B 27
REMARK 465 PHE B 28
REMARK 465 LEU B 29
REMARK 465 SER B 30
REMARK 465 LEU B 31
REMARK 465 ALA B 32
REMARK 465 LEU B 33
REMARK 465 ARG B 34
REMARK 465 ALA B 35
REMARK 465 SER B 36
REMARK 465 THR B 37
REMARK 465 GLN B 38
REMARK 465 ALA B 39
REMARK 465 PRO B 40
REMARK 465 GLU B 151
REMARK 465 ASP B 152
REMARK 465 VAL B 153
REMARK 465 LYS B 154
REMARK 465 ARG B 155
REMARK 465 ILE B 156
REMARK 465 SER B 157
REMARK 465 LYS B 158
REMARK 465 GLU B 159
REMARK 465 CYS B 160
REMARK 465 ALA B 161
REMARK 465 ARG B 162
REMARK 465 LYS B 163
REMARK 465 PRO B 164
REMARK 465 ASN B 165
REMARK 465 LYS B 166
REMARK 465 LYS B 167
REMARK 465 ILE B 168
REMARK 465 CYS B 169
REMARK 465 ARG B 170
REMARK 465 LYS B 171
REMARK 465 GLY B 172
REMARK 465 GLY B 173
REMARK 465 SER B 174
REMARK 465 GLY B 175
REMARK 465 ALA B 176
REMARK 465 LYS B 177
REMARK 465 LYS B 178
REMARK 465 GLN B 179
REMARK 465 GLY B 180
REMARK 465 GLU B 181
REMARK 465 ASP B 182
REMARK 465 LEU B 183
REMARK 465 ALA B 184
REMARK 465 ASP B 185
REMARK 465 ASN B 186
REMARK 465 ASP B 187
REMARK 465 GLY B 188
REMARK 465 ASP B 189
REMARK 465 GLU B 190
REMARK 465 ASP B 191
REMARK 465 GLU B 192
REMARK 465 ASP B 193
REMARK 465 ILE B 194
REMARK 465 ARG B 195
REMARK 465 ASP B 196
REMARK 465 SER B 197
REMARK 465 THR B 578
REMARK 465 LYS B 579
REMARK 465 PHE B 580
REMARK 465 ILE B 581
REMARK 465 HIS B 582
REMARK 465 THR B 583
REMARK 465 LYS B 584
REMARK 465 ALA B 585
REMARK 465 ASN B 586
REMARK 465 ARG B 587
REMARK 465 PHE B 588
REMARK 465 GLU B 589
REMARK 465 GLU B 590
REMARK 465 LEU B 634
REMARK 465 HIS B 635
REMARK 465 ASP B 636
REMARK 465 MET B 637
REMARK 465 PHE B 638
REMARK 465 HIS B 639
REMARK 465 TYR B 640
REMARK 465 THR B 641
REMARK 465 SER B 642
REMARK 465 THR B 643
REMARK 465 THR B 644
REMARK 465 THR B 645
REMARK 465 LYS B 646
REMARK 465 VAL B 647
REMARK 465 PRO B 648
REMARK 465 PRO B 649
REMARK 465 PRO B 650
REMARK 465 ASP B 651
REMARK 465 THR B 652
REMARK 465 THR B 653
REMARK 465 HIS B 654
REMARK 465 SER B 655
REMARK 465 SER B 656
REMARK 465 HIS B 657
REMARK 465 ILE B 658
REMARK 465 THR B 659
REMARK 465 ARG B 660
REMARK 465 ARG B 661
REMARK 465 PRO B 662
REMARK 465 ASN B 663
REMARK 465 GLY B 664
REMARK 465 LYS B 665
REMARK 465 THR B 666
REMARK 465 TRP B 667
REMARK 465 SER B 668
REMARK 465 THR B 669
REMARK 465 LYS B 670
REMARK 465 ARG B 671
REMARK 465 PRO B 672
REMARK 465 ALA B 673
REMARK 465 ILE B 674
REMARK 465 SER B 675
REMARK 465 PRO B 676
REMARK 465 ALA B 677
REMARK 465 TYR B 678
REMARK 465 SER B 679
REMARK 465 ASN B 680
REMARK 465 GLU B 681
REMARK 465 ASN B 682
REMARK 465 ALA B 683
REMARK 465 GLN B 684
REMARK 465 GLY B 685
REMARK 465 SER B 686
REMARK 465 TRP B 687
REMARK 465 ASN B 688
REMARK 465 GLY B 689
REMARK 465 ASP B 690
REMARK 465 GLN B 691
REMARK 465 ASP B 692
REMARK 465 ALA B 693
REMARK 465 GLY B 694
REMARK 465 PRO B 695
REMARK 465 LEU B 696
REMARK 465 LEU B 697
REMARK 465 VAL B 698
REMARK 465 GLU B 699
REMARK 465 ASN B 700
REMARK 465 PRO B 701
REMARK 465 ARG B 702
REMARK 465 ASP B 703
REMARK 465 TYR B 704
REMARK 465 SER B 705
REMARK 465 THR B 706
REMARK 465 GLU B 707
REMARK 465 LEU B 708
REMARK 465 SER B 709
REMARK 465 VAL B 710
REMARK 465 THR B 711
REMARK 465 ILE B 712
REMARK 465 ALA B 713
REMARK 465 VAL B 714
REMARK 465 GLY B 715
REMARK 465 ALA B 716
REMARK 465 SER B 717
REMARK 465 LEU B 718
REMARK 465 LEU B 719
REMARK 465 PHE B 720
REMARK 465 LEU B 721
REMARK 465 ASN B 722
REMARK 465 VAL B 723
REMARK 465 LEU B 724
REMARK 465 ALA B 725
REMARK 465 PHE B 726
REMARK 465 ALA B 727
REMARK 465 ALA B 728
REMARK 465 LEU B 729
REMARK 465 TYR B 730
REMARK 465 TYR B 731
REMARK 465 ARG B 732
REMARK 465 LYS B 733
REMARK 465 ASP B 734
REMARK 465 LYS B 735
REMARK 465 ARG B 736
REMARK 465 ARG B 737
REMARK 465 GLN B 738
REMARK 465 GLU B 739
REMARK 465 PRO B 740
REMARK 465 LEU B 741
REMARK 465 ARG B 742
REMARK 465 GLN B 743
REMARK 465 PRO B 744
REMARK 465 SER B 745
REMARK 465 PRO B 746
REMARK 465 GLN B 747
REMARK 465 ARG B 748
REMARK 465 GLY B 749
REMARK 465 ALA B 750
REMARK 465 GLY B 751
REMARK 465 ALA B 752
REMARK 465 PRO B 753
REMARK 465 GLU B 754
REMARK 465 LEU B 755
REMARK 465 GLY B 756
REMARK 465 ALA B 757
REMARK 465 ALA B 758
REMARK 465 PRO B 759
REMARK 465 GLU B 760
REMARK 465 GLU B 761
REMARK 465 GLU B 762
REMARK 465 LEU B 763
REMARK 465 ALA B 764
REMARK 465 ALA B 765
REMARK 465 LEU B 766
REMARK 465 GLN B 767
REMARK 465 LEU B 768
REMARK 465 GLY B 769
REMARK 465 PRO B 770
REMARK 465 THR B 771
REMARK 465 HIS B 772
REMARK 465 HIS B 773
REMARK 465 GLU B 774
REMARK 465 CYS B 775
REMARK 465 GLU B 776
REMARK 465 ALA B 777
REMARK 465 GLY B 778
REMARK 465 PRO B 779
REMARK 465 PRO B 780
REMARK 465 HIS B 781
REMARK 465 ASP B 782
REMARK 465 THR B 783
REMARK 465 LEU B 784
REMARK 465 ARG B 785
REMARK 465 LEU B 786
REMARK 465 THR B 787
REMARK 465 ALA B 788
REMARK 465 LEU B 789
REMARK 465 PRO B 790
REMARK 465 ASP B 791
REMARK 465 TYR B 792
REMARK 465 THR B 793
REMARK 465 LEU B 794
REMARK 465 THR B 795
REMARK 465 LEU B 796
REMARK 465 ARG B 797
REMARK 465 ARG B 798
REMARK 465 SER B 799
REMARK 465 PRO B 800
REMARK 465 ASP B 801
REMARK 465 ASP B 802
REMARK 465 ILE B 803
REMARK 465 PRO B 804
REMARK 465 LEU B 805
REMARK 465 MET B 806
REMARK 465 THR B 807
REMARK 465 PRO B 808
REMARK 465 ASN B 809
REMARK 465 THR B 810
REMARK 465 ILE B 811
REMARK 465 THR B 812
REMARK 465 MET B 813
REMARK 465 ILE B 814
REMARK 465 PRO B 815
REMARK 465 ASN B 816
REMARK 465 SER B 817
REMARK 465 LEU B 818
REMARK 465 VAL B 819
REMARK 465 GLY B 820
REMARK 465 LEU B 821
REMARK 465 GLN B 822
REMARK 465 THR B 823
REMARK 465 LEU B 824
REMARK 465 HIS B 825
REMARK 465 PRO B 826
REMARK 465 TYR B 827
REMARK 465 ASN B 828
REMARK 465 THR B 829
REMARK 465 PHE B 830
REMARK 465 ALA B 831
REMARK 465 ALA B 832
REMARK 465 GLY B 833
REMARK 465 PHE B 834
REMARK 465 ASN B 835
REMARK 465 SER B 836
REMARK 465 THR B 837
REMARK 465 GLY B 838
REMARK 465 LEU B 839
REMARK 465 PRO B 840
REMARK 465 HIS B 841
REMARK 465 SER B 842
REMARK 465 HIS B 843
REMARK 465 SER B 844
REMARK 465 THR B 845
REMARK 465 THR B 846
REMARK 465 ARG B 847
REMARK 465 VAL B 848
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 CD1 LEU B 58 CD1 LEU B 63 1.92
REMARK 500 OD2 ASP B 492 OH TYR B 596 2.18
REMARK 500 O HIS A 207 OH TYR A 237 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 CYS B 141 CB CYS B 141 SG 0.236
REMARK 500 PRO B 201 CB PRO B 201 CG 0.769
REMARK 500 PRO B 201 CG PRO B 201 CD -0.663
REMARK 500 PRO B 201 CD PRO B 201 N 0.162
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 PRO B 201 C - N - CD ANGL. DEV. = 32.1 DEGREES
REMARK 500 PRO B 201 CA - N - CD ANGL. DEV. = -34.1 DEGREES
REMARK 500 PRO B 201 CA - CB - CG ANGL. DEV. = -20.1 DEGREES
REMARK 500 PRO B 201 CB - CG - CD ANGL. DEV. = 106.5 DEGREES
REMARK 500 PRO B 201 N - CD - CG ANGL. DEV. = -10.0 DEGREES
REMARK 500 ASP B 364 CB - CG - OD1 ANGL. DEV. = 5.7 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 SER A 210 16.81 -144.99
REMARK 500 PRO A 543 8.61 -66.92
REMARK 500 CYS A 544 150.11 -49.44
REMARK 500 GLU B 136 64.06 60.16
REMARK 500 PRO B 201 161.14 -47.21
REMARK 500 SER B 210 16.44 -142.49
REMARK 500 PHE B 244 16.33 -141.18
REMARK 500 TYR B 443 68.88 60.25
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: EMD-34219 RELATED DB: EMDB
REMARK 900 CRYO-EM STRUCTURE OF HUMAN NEUROLIGIN 3
DBREF 8GS3 A 1 848 UNP Q9NZ94 NLGN3_HUMAN 1 848
DBREF 8GS3 B 1 848 UNP Q9NZ94 NLGN3_HUMAN 1 848
SEQRES 1 A 848 MET TRP LEU ARG LEU GLY PRO PRO SER LEU SER LEU SER
SEQRES 2 A 848 PRO LYS PRO THR VAL GLY ARG SER LEU CYS LEU THR LEU
SEQRES 3 A 848 TRP PHE LEU SER LEU ALA LEU ARG ALA SER THR GLN ALA
SEQRES 4 A 848 PRO ALA PRO THR VAL ASN THR HIS PHE GLY LYS LEU ARG
SEQRES 5 A 848 GLY ALA ARG VAL PRO LEU PRO SER GLU ILE LEU GLY PRO
SEQRES 6 A 848 VAL ASP GLN TYR LEU GLY VAL PRO TYR ALA ALA PRO PRO
SEQRES 7 A 848 ILE GLY GLU LYS ARG PHE LEU PRO PRO GLU PRO PRO PRO
SEQRES 8 A 848 SER TRP SER GLY ILE ARG ASN ALA THR HIS PHE PRO PRO
SEQRES 9 A 848 VAL CYS PRO GLN ASN ILE HIS THR ALA VAL PRO GLU VAL
SEQRES 10 A 848 MET LEU PRO VAL TRP PHE THR ALA ASN LEU ASP ILE VAL
SEQRES 11 A 848 ALA THR TYR ILE GLN GLU PRO ASN GLU ASP CYS LEU TYR
SEQRES 12 A 848 LEU ASN VAL TYR VAL PRO THR GLU ASP VAL LYS ARG ILE
SEQRES 13 A 848 SER LYS GLU CYS ALA ARG LYS PRO ASN LYS LYS ILE CYS
SEQRES 14 A 848 ARG LYS GLY GLY SER GLY ALA LYS LYS GLN GLY GLU ASP
SEQRES 15 A 848 LEU ALA ASP ASN ASP GLY ASP GLU ASP GLU ASP ILE ARG
SEQRES 16 A 848 ASP SER GLY ALA LYS PRO VAL MET VAL TYR ILE HIS GLY
SEQRES 17 A 848 GLY SER TYR MET GLU GLY THR GLY ASN MET ILE ASP GLY
SEQRES 18 A 848 SER ILE LEU ALA SER TYR GLY ASN VAL ILE VAL ILE THR
SEQRES 19 A 848 LEU ASN TYR ARG VAL GLY VAL LEU GLY PHE LEU SER THR
SEQRES 20 A 848 GLY ASP GLN ALA ALA LYS GLY ASN TYR GLY LEU LEU ASP
SEQRES 21 A 848 GLN ILE GLN ALA LEU ARG TRP VAL SER GLU ASN ILE ALA
SEQRES 22 A 848 PHE PHE GLY GLY ASP PRO ARG ARG ILE THR VAL PHE GLY
SEQRES 23 A 848 SER GLY ILE GLY ALA SER CYS VAL SER LEU LEU THR LEU
SEQRES 24 A 848 SER HIS HIS SER GLU GLY LEU PHE GLN ARG ALA ILE ILE
SEQRES 25 A 848 GLN SER GLY SER ALA LEU SER SER TRP ALA VAL ASN TYR
SEQRES 26 A 848 GLN PRO VAL LYS TYR THR SER LEU LEU ALA ASP LYS VAL
SEQRES 27 A 848 GLY CYS ASN VAL LEU ASP THR VAL ASP MET VAL ASP CYS
SEQRES 28 A 848 LEU ARG GLN LYS SER ALA LYS GLU LEU VAL GLU GLN ASP
SEQRES 29 A 848 ILE GLN PRO ALA ARG TYR HIS VAL ALA PHE GLY PRO VAL
SEQRES 30 A 848 ILE ASP GLY ASP VAL ILE PRO ASP ASP PRO GLU ILE LEU
SEQRES 31 A 848 MET GLU GLN GLY GLU PHE LEU ASN TYR ASP ILE MET LEU
SEQRES 32 A 848 GLY VAL ASN GLN GLY GLU GLY LEU LYS PHE VAL GLU GLY
SEQRES 33 A 848 VAL VAL ASP PRO GLU ASP GLY VAL SER GLY THR ASP PHE
SEQRES 34 A 848 ASP TYR SER VAL SER ASN PHE VAL ASP ASN LEU TYR GLY
SEQRES 35 A 848 TYR PRO GLU GLY LYS ASP THR LEU ARG GLU THR ILE LYS
SEQRES 36 A 848 PHE MET TYR THR ASP TRP ALA ASP ARG ASP ASN PRO GLU
SEQRES 37 A 848 THR ARG ARG LYS THR LEU VAL ALA LEU PHE THR ASP HIS
SEQRES 38 A 848 GLN TRP VAL GLU PRO SER VAL VAL THR ALA ASP LEU HIS
SEQRES 39 A 848 ALA ARG TYR GLY SER PRO THR TYR PHE TYR ALA PHE TYR
SEQRES 40 A 848 HIS HIS CYS GLN SER LEU MET LYS PRO ALA TRP SER ASP
SEQRES 41 A 848 ALA ALA HIS GLY ASP GLU VAL PRO TYR VAL PHE GLY VAL
SEQRES 42 A 848 PRO MET VAL GLY PRO THR ASP LEU PHE PRO CYS ASN PHE
SEQRES 43 A 848 SER LYS ASN ASP VAL MET LEU SER ALA VAL VAL MET THR
SEQRES 44 A 848 TYR TRP THR ASN PHE ALA LYS THR GLY ASP PRO ASN LYS
SEQRES 45 A 848 PRO VAL PRO GLN ASP THR LYS PHE ILE HIS THR LYS ALA
SEQRES 46 A 848 ASN ARG PHE GLU GLU VAL ALA TRP SER LYS TYR ASN PRO
SEQRES 47 A 848 ARG ASP GLN LEU TYR LEU HIS ILE GLY LEU LYS PRO ARG
SEQRES 48 A 848 VAL ARG ASP HIS TYR ARG ALA THR LYS VAL ALA PHE TRP
SEQRES 49 A 848 LYS HIS LEU VAL PRO HIS LEU TYR ASN LEU HIS ASP MET
SEQRES 50 A 848 PHE HIS TYR THR SER THR THR THR LYS VAL PRO PRO PRO
SEQRES 51 A 848 ASP THR THR HIS SER SER HIS ILE THR ARG ARG PRO ASN
SEQRES 52 A 848 GLY LYS THR TRP SER THR LYS ARG PRO ALA ILE SER PRO
SEQRES 53 A 848 ALA TYR SER ASN GLU ASN ALA GLN GLY SER TRP ASN GLY
SEQRES 54 A 848 ASP GLN ASP ALA GLY PRO LEU LEU VAL GLU ASN PRO ARG
SEQRES 55 A 848 ASP TYR SER THR GLU LEU SER VAL THR ILE ALA VAL GLY
SEQRES 56 A 848 ALA SER LEU LEU PHE LEU ASN VAL LEU ALA PHE ALA ALA
SEQRES 57 A 848 LEU TYR TYR ARG LYS ASP LYS ARG ARG GLN GLU PRO LEU
SEQRES 58 A 848 ARG GLN PRO SER PRO GLN ARG GLY ALA GLY ALA PRO GLU
SEQRES 59 A 848 LEU GLY ALA ALA PRO GLU GLU GLU LEU ALA ALA LEU GLN
SEQRES 60 A 848 LEU GLY PRO THR HIS HIS GLU CYS GLU ALA GLY PRO PRO
SEQRES 61 A 848 HIS ASP THR LEU ARG LEU THR ALA LEU PRO ASP TYR THR
SEQRES 62 A 848 LEU THR LEU ARG ARG SER PRO ASP ASP ILE PRO LEU MET
SEQRES 63 A 848 THR PRO ASN THR ILE THR MET ILE PRO ASN SER LEU VAL
SEQRES 64 A 848 GLY LEU GLN THR LEU HIS PRO TYR ASN THR PHE ALA ALA
SEQRES 65 A 848 GLY PHE ASN SER THR GLY LEU PRO HIS SER HIS SER THR
SEQRES 66 A 848 THR ARG VAL
SEQRES 1 B 848 MET TRP LEU ARG LEU GLY PRO PRO SER LEU SER LEU SER
SEQRES 2 B 848 PRO LYS PRO THR VAL GLY ARG SER LEU CYS LEU THR LEU
SEQRES 3 B 848 TRP PHE LEU SER LEU ALA LEU ARG ALA SER THR GLN ALA
SEQRES 4 B 848 PRO ALA PRO THR VAL ASN THR HIS PHE GLY LYS LEU ARG
SEQRES 5 B 848 GLY ALA ARG VAL PRO LEU PRO SER GLU ILE LEU GLY PRO
SEQRES 6 B 848 VAL ASP GLN TYR LEU GLY VAL PRO TYR ALA ALA PRO PRO
SEQRES 7 B 848 ILE GLY GLU LYS ARG PHE LEU PRO PRO GLU PRO PRO PRO
SEQRES 8 B 848 SER TRP SER GLY ILE ARG ASN ALA THR HIS PHE PRO PRO
SEQRES 9 B 848 VAL CYS PRO GLN ASN ILE HIS THR ALA VAL PRO GLU VAL
SEQRES 10 B 848 MET LEU PRO VAL TRP PHE THR ALA ASN LEU ASP ILE VAL
SEQRES 11 B 848 ALA THR TYR ILE GLN GLU PRO ASN GLU ASP CYS LEU TYR
SEQRES 12 B 848 LEU ASN VAL TYR VAL PRO THR GLU ASP VAL LYS ARG ILE
SEQRES 13 B 848 SER LYS GLU CYS ALA ARG LYS PRO ASN LYS LYS ILE CYS
SEQRES 14 B 848 ARG LYS GLY GLY SER GLY ALA LYS LYS GLN GLY GLU ASP
SEQRES 15 B 848 LEU ALA ASP ASN ASP GLY ASP GLU ASP GLU ASP ILE ARG
SEQRES 16 B 848 ASP SER GLY ALA LYS PRO VAL MET VAL TYR ILE HIS GLY
SEQRES 17 B 848 GLY SER TYR MET GLU GLY THR GLY ASN MET ILE ASP GLY
SEQRES 18 B 848 SER ILE LEU ALA SER TYR GLY ASN VAL ILE VAL ILE THR
SEQRES 19 B 848 LEU ASN TYR ARG VAL GLY VAL LEU GLY PHE LEU SER THR
SEQRES 20 B 848 GLY ASP GLN ALA ALA LYS GLY ASN TYR GLY LEU LEU ASP
SEQRES 21 B 848 GLN ILE GLN ALA LEU ARG TRP VAL SER GLU ASN ILE ALA
SEQRES 22 B 848 PHE PHE GLY GLY ASP PRO ARG ARG ILE THR VAL PHE GLY
SEQRES 23 B 848 SER GLY ILE GLY ALA SER CYS VAL SER LEU LEU THR LEU
SEQRES 24 B 848 SER HIS HIS SER GLU GLY LEU PHE GLN ARG ALA ILE ILE
SEQRES 25 B 848 GLN SER GLY SER ALA LEU SER SER TRP ALA VAL ASN TYR
SEQRES 26 B 848 GLN PRO VAL LYS TYR THR SER LEU LEU ALA ASP LYS VAL
SEQRES 27 B 848 GLY CYS ASN VAL LEU ASP THR VAL ASP MET VAL ASP CYS
SEQRES 28 B 848 LEU ARG GLN LYS SER ALA LYS GLU LEU VAL GLU GLN ASP
SEQRES 29 B 848 ILE GLN PRO ALA ARG TYR HIS VAL ALA PHE GLY PRO VAL
SEQRES 30 B 848 ILE ASP GLY ASP VAL ILE PRO ASP ASP PRO GLU ILE LEU
SEQRES 31 B 848 MET GLU GLN GLY GLU PHE LEU ASN TYR ASP ILE MET LEU
SEQRES 32 B 848 GLY VAL ASN GLN GLY GLU GLY LEU LYS PHE VAL GLU GLY
SEQRES 33 B 848 VAL VAL ASP PRO GLU ASP GLY VAL SER GLY THR ASP PHE
SEQRES 34 B 848 ASP TYR SER VAL SER ASN PHE VAL ASP ASN LEU TYR GLY
SEQRES 35 B 848 TYR PRO GLU GLY LYS ASP THR LEU ARG GLU THR ILE LYS
SEQRES 36 B 848 PHE MET TYR THR ASP TRP ALA ASP ARG ASP ASN PRO GLU
SEQRES 37 B 848 THR ARG ARG LYS THR LEU VAL ALA LEU PHE THR ASP HIS
SEQRES 38 B 848 GLN TRP VAL GLU PRO SER VAL VAL THR ALA ASP LEU HIS
SEQRES 39 B 848 ALA ARG TYR GLY SER PRO THR TYR PHE TYR ALA PHE TYR
SEQRES 40 B 848 HIS HIS CYS GLN SER LEU MET LYS PRO ALA TRP SER ASP
SEQRES 41 B 848 ALA ALA HIS GLY ASP GLU VAL PRO TYR VAL PHE GLY VAL
SEQRES 42 B 848 PRO MET VAL GLY PRO THR ASP LEU PHE PRO CYS ASN PHE
SEQRES 43 B 848 SER LYS ASN ASP VAL MET LEU SER ALA VAL VAL MET THR
SEQRES 44 B 848 TYR TRP THR ASN PHE ALA LYS THR GLY ASP PRO ASN LYS
SEQRES 45 B 848 PRO VAL PRO GLN ASP THR LYS PHE ILE HIS THR LYS ALA
SEQRES 46 B 848 ASN ARG PHE GLU GLU VAL ALA TRP SER LYS TYR ASN PRO
SEQRES 47 B 848 ARG ASP GLN LEU TYR LEU HIS ILE GLY LEU LYS PRO ARG
SEQRES 48 B 848 VAL ARG ASP HIS TYR ARG ALA THR LYS VAL ALA PHE TRP
SEQRES 49 B 848 LYS HIS LEU VAL PRO HIS LEU TYR ASN LEU HIS ASP MET
SEQRES 50 B 848 PHE HIS TYR THR SER THR THR THR LYS VAL PRO PRO PRO
SEQRES 51 B 848 ASP THR THR HIS SER SER HIS ILE THR ARG ARG PRO ASN
SEQRES 52 B 848 GLY LYS THR TRP SER THR LYS ARG PRO ALA ILE SER PRO
SEQRES 53 B 848 ALA TYR SER ASN GLU ASN ALA GLN GLY SER TRP ASN GLY
SEQRES 54 B 848 ASP GLN ASP ALA GLY PRO LEU LEU VAL GLU ASN PRO ARG
SEQRES 55 B 848 ASP TYR SER THR GLU LEU SER VAL THR ILE ALA VAL GLY
SEQRES 56 B 848 ALA SER LEU LEU PHE LEU ASN VAL LEU ALA PHE ALA ALA
SEQRES 57 B 848 LEU TYR TYR ARG LYS ASP LYS ARG ARG GLN GLU PRO LEU
SEQRES 58 B 848 ARG GLN PRO SER PRO GLN ARG GLY ALA GLY ALA PRO GLU
SEQRES 59 B 848 LEU GLY ALA ALA PRO GLU GLU GLU LEU ALA ALA LEU GLN
SEQRES 60 B 848 LEU GLY PRO THR HIS HIS GLU CYS GLU ALA GLY PRO PRO
SEQRES 61 B 848 HIS ASP THR LEU ARG LEU THR ALA LEU PRO ASP TYR THR
SEQRES 62 B 848 LEU THR LEU ARG ARG SER PRO ASP ASP ILE PRO LEU MET
SEQRES 63 B 848 THR PRO ASN THR ILE THR MET ILE PRO ASN SER LEU VAL
SEQRES 64 B 848 GLY LEU GLN THR LEU HIS PRO TYR ASN THR PHE ALA ALA
SEQRES 65 B 848 GLY PHE ASN SER THR GLY LEU PRO HIS SER HIS SER THR
SEQRES 66 B 848 THR ARG VAL
HELIX 1 AA1 ILE A 79 ARG A 83 5 5
HELIX 2 AA2 PRO A 120 ASN A 126 1 7
HELIX 3 AA3 ASN A 126 GLN A 135 1 10
HELIX 4 AA4 GLY A 221 ASN A 229 1 9
HELIX 5 AA5 VAL A 239 LEU A 245 1 7
HELIX 6 AA6 ASN A 255 ILE A 272 1 18
HELIX 7 AA7 ALA A 273 PHE A 275 5 3
HELIX 8 AA8 GLY A 288 LEU A 299 1 12
HELIX 9 AA9 SER A 300 GLU A 304 5 5
HELIX 10 AB1 GLN A 326 GLY A 339 1 14
HELIX 11 AB2 ASP A 344 LYS A 355 1 12
HELIX 12 AB3 SER A 356 GLN A 363 1 8
HELIX 13 AB4 ASP A 386 GLY A 394 1 9
HELIX 14 AB5 GLU A 395 TYR A 399 5 5
HELIX 15 AB6 LEU A 411 GLY A 416 1 6
HELIX 16 AB7 SER A 425 GLY A 442 1 18
HELIX 17 AB8 GLY A 446 TYR A 458 1 13
HELIX 18 AB9 ASN A 466 TRP A 483 1 18
HELIX 19 AC1 TRP A 483 ALA A 495 1 13
HELIX 20 AC2 ARG A 496 GLY A 498 5 3
HELIX 21 AC3 GLU A 526 PHE A 531 1 6
HELIX 22 AC4 GLY A 532 GLY A 537 1 6
HELIX 23 AC5 SER A 547 GLY A 568 1 22
HELIX 24 AC6 ARG A 617 HIS A 626 1 10
HELIX 25 AC7 HIS A 626 TYR A 632 1 7
HELIX 26 AC8 ILE B 79 ARG B 83 5 5
HELIX 27 AC9 PRO B 120 ASN B 126 1 7
HELIX 28 AD1 ASN B 126 GLN B 135 1 10
HELIX 29 AD2 THR B 215 ILE B 219 5 5
HELIX 30 AD3 GLY B 221 ASN B 229 1 9
HELIX 31 AD4 GLY B 240 LEU B 245 1 6
HELIX 32 AD5 ASN B 255 ILE B 272 1 18
HELIX 33 AD6 ALA B 273 PHE B 275 5 3
HELIX 34 AD7 GLY B 288 LEU B 299 1 12
HELIX 35 AD8 SER B 300 GLU B 304 5 5
HELIX 36 AD9 GLN B 326 GLY B 339 1 14
HELIX 37 AE1 ASP B 344 LYS B 355 1 12
HELIX 38 AE2 SER B 356 GLN B 363 1 8
HELIX 39 AE3 ASP B 386 GLY B 394 1 9
HELIX 40 AE4 GLU B 395 TYR B 399 5 5
HELIX 41 AE5 LEU B 411 GLY B 416 1 6
HELIX 42 AE6 SER B 425 GLY B 442 1 18
HELIX 43 AE7 GLY B 446 TYR B 458 1 13
HELIX 44 AE8 ASN B 466 TRP B 483 1 18
HELIX 45 AE9 TRP B 483 ALA B 495 1 13
HELIX 46 AF1 ARG B 496 GLY B 498 5 3
HELIX 47 AF2 GLU B 526 PHE B 531 1 6
HELIX 48 AF3 GLY B 532 GLY B 537 1 6
HELIX 49 AF4 SER B 547 GLY B 568 1 22
HELIX 50 AF5 ARG B 617 HIS B 626 1 10
HELIX 51 AF6 HIS B 626 TYR B 632 1 7
SHEET 1 AA1 3 THR A 43 THR A 46 0
SHEET 2 AA1 3 GLY A 49 ARG A 52 -1 O GLY A 49 N THR A 46
SHEET 3 AA1 3 ILE A 96 ASN A 98 1 O ARG A 97 N LYS A 50
SHEET 1 AA211 ALA A 54 VAL A 56 0
SHEET 2 AA211 VAL A 66 PRO A 73 -1 O VAL A 66 N VAL A 56
SHEET 3 AA211 TYR A 143 PRO A 149 -1 O LEU A 144 N VAL A 72
SHEET 4 AA211 ILE A 231 LEU A 235 -1 O VAL A 232 N TYR A 147
SHEET 5 AA211 LYS A 200 ILE A 206 1 N TYR A 205 O ILE A 233
SHEET 6 AA211 GLY A 277 SER A 287 1 O ASP A 278 N LYS A 200
SHEET 7 AA211 ARG A 309 GLN A 313 1 O GLN A 313 N GLY A 286
SHEET 8 AA211 ASP A 400 ASN A 406 1 O ASP A 400 N ALA A 310
SHEET 9 AA211 THR A 501 PHE A 506 1 O PHE A 506 N VAL A 405
SHEET 10 AA211 LEU A 602 ILE A 606 1 O LEU A 604 N ALA A 505
SHEET 11 AA211 ARG A 611 ASP A 614 -1 O ARG A 611 N HIS A 605
SHEET 1 AA3 3 THR B 43 THR B 46 0
SHEET 2 AA3 3 GLY B 49 ARG B 52 -1 O LEU B 51 N VAL B 44
SHEET 3 AA3 3 ILE B 96 ASN B 98 1 O ARG B 97 N ARG B 52
SHEET 1 AA411 ALA B 54 VAL B 56 0
SHEET 2 AA411 VAL B 66 PRO B 73 -1 O GLN B 68 N ALA B 54
SHEET 3 AA411 TYR B 143 PRO B 149 -1 O LEU B 144 N VAL B 72
SHEET 4 AA411 ILE B 231 ASN B 236 -1 O VAL B 232 N TYR B 147
SHEET 5 AA411 LYS B 200 ILE B 206 1 N TYR B 205 O ILE B 233
SHEET 6 AA411 GLY B 277 SER B 287 1 O ASP B 278 N LYS B 200
SHEET 7 AA411 ARG B 309 GLN B 313 1 O ARG B 309 N ILE B 282
SHEET 8 AA411 ASP B 400 ASN B 406 1 O ASP B 400 N ALA B 310
SHEET 9 AA411 THR B 501 PHE B 506 1 O PHE B 506 N VAL B 405
SHEET 10 AA411 LEU B 602 ILE B 606 1 O ILE B 606 N ALA B 505
SHEET 11 AA411 ARG B 611 ASP B 614 -1 O ARG B 613 N TYR B 603
SSBOND 1 CYS A 106 CYS A 141 1555 1555 2.04
SSBOND 2 CYS A 340 CYS A 351 1555 1555 2.03
SSBOND 3 CYS A 510 CYS A 544 1555 1555 2.03
SSBOND 4 CYS B 106 CYS B 141 1555 1555 2.64
SSBOND 5 CYS B 340 CYS B 351 1555 1555 2.05
SSBOND 6 CYS B 510 CYS B 544 1555 1555 2.04
CISPEP 1 LYS A 572 PRO A 573 0 -0.35
CISPEP 2 LYS B 572 PRO B 573 0 -0.01
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 4192 ASN A 633
TER 8378 ASN B 633
MASTER 816 0 0 51 28 0 0 6 8376 2 12 132
END |