HEADER HYDROLASE/IMMUNE SYSTEM 27-FEB-15 4YH7
TITLE CRYSTAL STRUCTURE OF PTPDELTA ECTODOMAIN IN COMPLEX WITH IL1RAPL1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE DELTA;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 21-854;
COMPND 5 SYNONYM: R-PTP-DELTA;
COMPND 6 EC: 3.1.3.48;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: INTERLEUKIN-1 RECEPTOR ACCESSORY PROTEIN-LIKE 1;
COMPND 10 CHAIN: B;
COMPND 11 FRAGMENT: UNP RESIDUES 19-352;
COMPND 12 SYNONYM: IL1RAPL-1,X-LINKED INTERLEUKIN-1 RECEPTOR ACCESSORY PROTEIN-
COMPND 13 LIKE 1;
COMPND 14 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: PTPRD;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: FREESTYLE 293-F;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 12 ORGANISM_COMMON: MOUSE;
SOURCE 13 ORGANISM_TAXID: 10090;
SOURCE 14 GENE: IL1RAPL1;
SOURCE 15 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 16 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 18 EXPRESSION_SYSTEM_CELL_LINE: FREESTYLE 293-F
KEYWDS TRANS-SYNAPTIC COMPLEX, SYNAPSE ORGANIZER, HYDROLASE-IMMUNE SYSTEM
KEYWDS 2 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR A.YAMAGATA,S.FUKAI
REVDAT 4 08-NOV-23 4YH7 1 HETSYN LINK
REVDAT 3 29-JUL-20 4YH7 1 COMPND REMARK HETNAM LINK
REVDAT 3 2 1 SITE ATOM
REVDAT 2 05-FEB-20 4YH7 1 SOURCE REMARK
REVDAT 1 06-MAY-15 4YH7 0
JRNL AUTH A.YAMAGATA,T.YOSHIDA,Y.SATO,S.GOTO-ITO,T.UEMURA,A.MAEDA,
JRNL AUTH 2 T.SHIROSHIMA,S.IWASAWA-OKAMOTO,H.MORI,M.MISHINA,S.FUKAI
JRNL TITL MECHANISMS OF SPLICING-DEPENDENT TRANS-SYNAPTIC ADHESION BY
JRNL TITL 2 PTP DELTA-IL1RAPL1/IL-1RACP FOR SYNAPTIC DIFFERENTIATION.
JRNL REF NAT COMMUN V. 6 6926 2015
JRNL REFN ESSN 2041-1723
JRNL PMID 25908590
JRNL DOI 10.1038/NCOMMS7926
REMARK 2
REMARK 2 RESOLUTION. 4.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.2_1309)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 4.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.09
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.430
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.4
REMARK 3 NUMBER OF REFLECTIONS : 17614
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.292
REMARK 3 R VALUE (WORKING SET) : 0.290
REMARK 3 FREE R VALUE : 0.325
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.090
REMARK 3 FREE R VALUE TEST SET COUNT : 896
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 39.0917 - 7.9756 0.99 2992 148 0.2821 0.3185
REMARK 3 2 7.9756 - 6.3392 0.99 2907 149 0.3152 0.3302
REMARK 3 3 6.3392 - 5.5405 0.97 2853 137 0.2676 0.3234
REMARK 3 4 5.5405 - 5.0350 0.97 2780 164 0.2791 0.3165
REMARK 3 5 5.0350 - 4.6748 0.93 2660 169 0.2937 0.3307
REMARK 3 6 4.6748 - 4.3996 0.87 2526 129 0.3324 0.3566
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.660
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 37.840
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.006 7414
REMARK 3 ANGLE : 1.575 10078
REMARK 3 CHIRALITY : 0.064 1141
REMARK 3 PLANARITY : 0.008 1297
REMARK 3 DIHEDRAL : 19.831 2810
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4YH7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 11-MAR-15.
REMARK 100 THE DEPOSITION ID IS D_1000207456.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-JUN-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL41XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX225HE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17618
REMARK 200 RESOLUTION RANGE HIGH (A) : 4.400
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.6
REMARK 200 DATA REDUNDANCY : 4.200
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.07200
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 4.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 4.48
REMARK 200 COMPLETENESS FOR SHELL (%) : 86.0
REMARK 200 DATA REDUNDANCY IN SHELL : 2.20
REMARK 200 R MERGE FOR SHELL (I) : 0.42400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: HKL-2000
REMARK 200 STARTING MODEL: 4YFC, 2DJU, 2DLH
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 77.19
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 5.39
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15% PEG4000, 0.1 M MES, PH 6.0, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 41
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 3555 -Y,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X,Z+3/4
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X,-Y,Z
REMARK 290 7555 -Y+1/2,X,Z+3/4
REMARK 290 8555 Y,-X+1/2,Z+1/4
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 143.14750
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 143.14750
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 35.09150
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 143.14750
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 17.54575
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 143.14750
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 52.63725
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 143.14750
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 143.14750
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 35.09150
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 -1.000000 0.000000 143.14750
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 52.63725
REMARK 290 SMTRY1 8 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 143.14750
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 17.54575
REMARK 290
REMARK 290 REMARK: NULL
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5210 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 50150 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 14.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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 GLN A 613
REMARK 465 SER A 614
REMARK 465 MET A 615
REMARK 465 PHE A 616
REMARK 465 ALA A 617
REMARK 465 LYS A 618
REMARK 465 ASN A 619
REMARK 465 PHE A 620
REMARK 465 HIS A 621
REMARK 465 VAL A 622
REMARK 465 LYS A 623
REMARK 465 ALA A 624
REMARK 465 VAL A 625
REMARK 465 MET A 626
REMARK 465 LYS A 627
REMARK 465 THR A 628
REMARK 465 SER A 629
REMARK 465 VAL A 630
REMARK 465 LEU A 631
REMARK 465 LEU A 632
REMARK 465 SER A 633
REMARK 465 TRP A 634
REMARK 465 GLU A 635
REMARK 465 ILE A 636
REMARK 465 PRO A 637
REMARK 465 GLU A 638
REMARK 465 ASN A 639
REMARK 465 TYR A 640
REMARK 465 ASN A 641
REMARK 465 SER A 642
REMARK 465 ALA A 643
REMARK 465 MET A 644
REMARK 465 PRO A 645
REMARK 465 PHE A 646
REMARK 465 LYS A 647
REMARK 465 ILE A 648
REMARK 465 LEU A 649
REMARK 465 TYR A 650
REMARK 465 ASP A 651
REMARK 465 ASP A 652
REMARK 465 GLY A 653
REMARK 465 LYS A 654
REMARK 465 MET A 655
REMARK 465 VAL A 656
REMARK 465 GLU A 657
REMARK 465 GLU A 658
REMARK 465 VAL A 659
REMARK 465 ASP A 660
REMARK 465 GLY A 661
REMARK 465 ARG A 662
REMARK 465 ALA A 663
REMARK 465 THR A 664
REMARK 465 GLN A 665
REMARK 465 LYS A 666
REMARK 465 LEU A 667
REMARK 465 ILE A 668
REMARK 465 VAL A 669
REMARK 465 ASN A 670
REMARK 465 LEU A 671
REMARK 465 LYS A 672
REMARK 465 PRO A 673
REMARK 465 GLU A 674
REMARK 465 LYS A 675
REMARK 465 SER A 676
REMARK 465 TYR A 677
REMARK 465 SER A 678
REMARK 465 PHE A 679
REMARK 465 VAL A 680
REMARK 465 LEU A 681
REMARK 465 THR A 682
REMARK 465 ASN A 683
REMARK 465 ARG A 684
REMARK 465 GLY A 685
REMARK 465 ASN A 686
REMARK 465 SER A 687
REMARK 465 ALA A 688
REMARK 465 GLY A 689
REMARK 465 GLY A 690
REMARK 465 LEU A 691
REMARK 465 GLN A 692
REMARK 465 HIS A 693
REMARK 465 ARG A 694
REMARK 465 VAL A 695
REMARK 465 THR A 696
REMARK 465 ALA A 697
REMARK 465 LYS A 698
REMARK 465 THR A 699
REMARK 465 ALA A 700
REMARK 465 PRO A 701
REMARK 465 ASP A 702
REMARK 465 VAL A 703
REMARK 465 LEU A 704
REMARK 465 ARG A 705
REMARK 465 THR A 706
REMARK 465 LYS A 707
REMARK 465 PRO A 708
REMARK 465 ALA A 709
REMARK 465 PHE A 710
REMARK 465 ILE A 711
REMARK 465 GLY A 712
REMARK 465 LYS A 713
REMARK 465 THR A 714
REMARK 465 ASN A 715
REMARK 465 LEU A 716
REMARK 465 ASP A 717
REMARK 465 GLY A 718
REMARK 465 MET A 719
REMARK 465 ILE A 720
REMARK 465 THR A 721
REMARK 465 VAL A 722
REMARK 465 GLN A 723
REMARK 465 LEU A 724
REMARK 465 PRO A 725
REMARK 465 ASP A 726
REMARK 465 VAL A 727
REMARK 465 PRO A 728
REMARK 465 ALA A 729
REMARK 465 ASN A 730
REMARK 465 GLU A 731
REMARK 465 ASN A 732
REMARK 465 ILE A 733
REMARK 465 LYS A 734
REMARK 465 GLY A 735
REMARK 465 TYR A 736
REMARK 465 TYR A 737
REMARK 465 ILE A 738
REMARK 465 ILE A 739
REMARK 465 ILE A 740
REMARK 465 VAL A 741
REMARK 465 PRO A 742
REMARK 465 LEU A 743
REMARK 465 LYS A 744
REMARK 465 LYS A 745
REMARK 465 SER A 746
REMARK 465 ARG A 747
REMARK 465 GLY A 748
REMARK 465 LYS A 749
REMARK 465 PHE A 750
REMARK 465 ILE A 751
REMARK 465 LYS A 752
REMARK 465 PRO A 753
REMARK 465 TRP A 754
REMARK 465 GLU A 755
REMARK 465 SER A 756
REMARK 465 PRO A 757
REMARK 465 ASP A 758
REMARK 465 GLU A 759
REMARK 465 MET A 760
REMARK 465 GLU A 761
REMARK 465 LEU A 762
REMARK 465 ASP A 763
REMARK 465 GLU A 764
REMARK 465 LEU A 765
REMARK 465 LEU A 766
REMARK 465 LYS A 767
REMARK 465 GLU A 768
REMARK 465 ILE A 769
REMARK 465 SER A 770
REMARK 465 ARG A 771
REMARK 465 LYS A 772
REMARK 465 ARG A 773
REMARK 465 ARG A 774
REMARK 465 SER A 775
REMARK 465 ILE A 776
REMARK 465 ARG A 777
REMARK 465 TYR A 778
REMARK 465 GLY A 779
REMARK 465 ARG A 780
REMARK 465 GLU A 781
REMARK 465 VAL A 782
REMARK 465 GLU A 783
REMARK 465 LEU A 784
REMARK 465 LYS A 785
REMARK 465 PRO A 786
REMARK 465 TYR A 787
REMARK 465 ILE A 788
REMARK 465 ALA A 789
REMARK 465 ALA A 790
REMARK 465 HIS A 791
REMARK 465 PHE A 792
REMARK 465 ASP A 793
REMARK 465 VAL A 794
REMARK 465 LEU A 795
REMARK 465 PRO A 796
REMARK 465 THR A 797
REMARK 465 GLU A 798
REMARK 465 PHE A 799
REMARK 465 THR A 800
REMARK 465 LEU A 801
REMARK 465 GLY A 802
REMARK 465 ASP A 803
REMARK 465 ASP A 804
REMARK 465 LYS A 805
REMARK 465 HIS A 806
REMARK 465 TYR A 807
REMARK 465 GLY A 808
REMARK 465 GLY A 809
REMARK 465 PHE A 810
REMARK 465 THR A 811
REMARK 465 ASN A 812
REMARK 465 LYS A 813
REMARK 465 GLN A 814
REMARK 465 LEU A 815
REMARK 465 GLN A 816
REMARK 465 SER A 817
REMARK 465 GLY A 818
REMARK 465 GLN A 819
REMARK 465 GLU A 820
REMARK 465 TYR A 821
REMARK 465 VAL A 822
REMARK 465 PHE A 823
REMARK 465 PHE A 824
REMARK 465 VAL A 825
REMARK 465 LEU A 826
REMARK 465 ALA A 827
REMARK 465 VAL A 828
REMARK 465 MET A 829
REMARK 465 ASP A 830
REMARK 465 HIS A 831
REMARK 465 ALA A 832
REMARK 465 GLU A 833
REMARK 465 SER A 834
REMARK 465 LYS A 835
REMARK 465 MET A 836
REMARK 465 TYR A 837
REMARK 465 ALA A 838
REMARK 465 THR A 839
REMARK 465 SER A 840
REMARK 465 PRO A 841
REMARK 465 TYR A 842
REMARK 465 SER A 843
REMARK 465 ASP A 844
REMARK 465 PRO A 845
REMARK 465 VAL A 846
REMARK 465 VAL A 847
REMARK 465 SER A 848
REMARK 465 MET A 849
REMARK 465 ASP A 850
REMARK 465 LEU A 851
REMARK 465 ASP A 852
REMARK 465 PRO A 853
REMARK 465 GLN A 854
REMARK 465 PRO A 855
REMARK 465 ILE A 856
REMARK 465 THR A 857
REMARK 465 ASP A 858
REMARK 465 GLU A 859
REMARK 465 GLU A 860
REMARK 465 GLU A 861
REMARK 465 LYS A 862
REMARK 465 HIS A 863
REMARK 465 HIS A 864
REMARK 465 HIS A 865
REMARK 465 HIS A 866
REMARK 465 HIS A 867
REMARK 465 HIS A 868
REMARK 465 ALA B 12
REMARK 465 GLN B 13
REMARK 465 PRO B 14
REMARK 465 ALA B 15
REMARK 465 ALA B 16
REMARK 465 ARG B 17
REMARK 465 ASP B 18
REMARK 465 LEU B 19
REMARK 465 LYS B 20
REMARK 465 VAL B 21
REMARK 465 VAL B 22
REMARK 465 THR B 23
REMARK 465 LYS B 24
REMARK 465 ARG B 25
REMARK 465 GLY B 26
REMARK 465 SER B 27
REMARK 465 ALA B 28
REMARK 465 ASP B 29
REMARK 465 GLY B 30
REMARK 465 LEU B 172
REMARK 465 PRO B 173
REMARK 465 THR B 174
REMARK 465 ARG B 175
REMARK 465 HIS B 359
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 LYS B 353 CG CD CE NZ
REMARK 470 HIS B 354 CG ND1 CD2 CE1 NE2
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 NH2 ARG A 98 OE2 GLU B 291 2.09
REMARK 500 O ARG A 124 NE2 GLN A 127 2.13
REMARK 500 NH2 ARG A 196 OD1 ASP B 37 2.19
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 A 357 C - N - CA ANGL. DEV. = 9.0 DEGREES
REMARK 500 VAL A 358 CG1 - CB - CG2 ANGL. DEV. = -14.4 DEGREES
REMARK 500 PRO A 414 C - N - CA ANGL. DEV. = -10.1 DEGREES
REMARK 500 PRO A 448 C - N - CA ANGL. DEV. = 10.1 DEGREES
REMARK 500 THR A 518 N - CA - C ANGL. DEV. = 16.5 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 ASP A 39 151.60 -47.20
REMARK 500 LYS A 67 71.92 49.45
REMARK 500 LYS A 70 80.90 -41.50
REMARK 500 ASN A 73 135.19 -174.26
REMARK 500 SER A 85 -118.25 -66.71
REMARK 500 GLU A 100 98.87 -54.46
REMARK 500 ASN A 110 24.81 -72.68
REMARK 500 ASP A 126 -2.88 -54.32
REMARK 500 GLN A 127 38.35 -157.97
REMARK 500 PHE A 170 -19.59 84.48
REMARK 500 ASP A 174 110.77 55.79
REMARK 500 ASN A 178 1.33 38.52
REMARK 500 LEU A 278 55.35 -92.43
REMARK 500 ALA A 280 -65.35 -103.49
REMARK 500 ASN A 299 -74.88 -100.27
REMARK 500 ASP A 300 67.81 -116.35
REMARK 500 ARG A 302 -78.57 -108.76
REMARK 500 SER A 313 -163.07 -103.41
REMARK 500 ALA A 320 128.92 -175.05
REMARK 500 THR A 335 41.01 71.40
REMARK 500 PRO A 336 85.90 -66.29
REMARK 500 ASN A 404 -168.62 -124.12
REMARK 500 ASN A 405 2.98 -63.32
REMARK 500 LEU A 436 -89.62 -104.97
REMARK 500 TYR A 461 76.58 -104.07
REMARK 500 PRO A 466 41.82 -76.08
REMARK 500 MET A 474 154.94 150.58
REMARK 500 GLN A 482 1.90 47.03
REMARK 500 ASP A 513 11.35 169.76
REMARK 500 VAL A 516 142.05 -29.50
REMARK 500 GLN A 519 -123.26 -124.14
REMARK 500 GLN A 525 144.88 -37.84
REMARK 500 PRO A 546 -177.53 -69.42
REMARK 500 SER A 548 108.85 -46.66
REMARK 500 ASP A 560 103.14 -58.01
REMARK 500 GLN A 563 32.59 -91.71
REMARK 500 ASN A 585 51.92 37.44
REMARK 500 SER A 593 108.04 -162.19
REMARK 500 SER B 35 -166.58 57.70
REMARK 500 VAL B 45 101.79 -50.58
REMARK 500 TYR B 57 54.66 -101.82
REMARK 500 TYR B 59 -71.29 -61.83
REMARK 500 PRO B 88 62.02 -69.84
REMARK 500 ILE B 89 106.45 20.46
REMARK 500 ASP B 92 -152.15 -88.92
REMARK 500 SER B 94 -78.57 -90.04
REMARK 500 ARG B 95 -78.58 -72.46
REMARK 500 ASN B 122 -109.85 -79.07
REMARK 500 SER B 123 0.07 -155.66
REMARK 500 THR B 140 100.91 -37.69
REMARK 500
REMARK 500 THIS ENTRY HAS 72 RAMACHANDRAN OUTLIERS.
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 PRO B 88 ILE B 89 148.87
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4YH6 RELATED DB: PDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 SEQUENCE OF THE CHAIN A WAS BASED ON ISOFORM 12 OF DATABASE UNP
REMARK 999 Q64487
DBREF 4YH7 A 28 861 UNP Q64487 PTPRD_MOUSE 21 854
DBREF 4YH7 B 19 352 UNP P59823 IRPL1_MOUSE 19 352
SEQADV 4YH7 LYS A 862 UNP Q64487 EXPRESSION TAG
SEQADV 4YH7 HIS A 863 UNP Q64487 EXPRESSION TAG
SEQADV 4YH7 HIS A 864 UNP Q64487 EXPRESSION TAG
SEQADV 4YH7 HIS A 865 UNP Q64487 EXPRESSION TAG
SEQADV 4YH7 HIS A 866 UNP Q64487 EXPRESSION TAG
SEQADV 4YH7 HIS A 867 UNP Q64487 EXPRESSION TAG
SEQADV 4YH7 HIS A 868 UNP Q64487 EXPRESSION TAG
SEQADV 4YH7 ALA B 12 UNP P59823 EXPRESSION TAG
SEQADV 4YH7 GLN B 13 UNP P59823 EXPRESSION TAG
SEQADV 4YH7 PRO B 14 UNP P59823 EXPRESSION TAG
SEQADV 4YH7 ALA B 15 UNP P59823 EXPRESSION TAG
SEQADV 4YH7 ALA B 16 UNP P59823 EXPRESSION TAG
SEQADV 4YH7 ARG B 17 UNP P59823 EXPRESSION TAG
SEQADV 4YH7 ASP B 18 UNP P59823 EXPRESSION TAG
SEQADV 4YH7 LYS B 353 UNP P59823 EXPRESSION TAG
SEQADV 4YH7 HIS B 354 UNP P59823 EXPRESSION TAG
SEQADV 4YH7 HIS B 355 UNP P59823 EXPRESSION TAG
SEQADV 4YH7 HIS B 356 UNP P59823 EXPRESSION TAG
SEQADV 4YH7 HIS B 357 UNP P59823 EXPRESSION TAG
SEQADV 4YH7 HIS B 358 UNP P59823 EXPRESSION TAG
SEQADV 4YH7 HIS B 359 UNP P59823 EXPRESSION TAG
SEQRES 1 A 841 GLU THR PRO PRO ARG PHE THR ARG THR PRO VAL ASP GLN
SEQRES 2 A 841 THR GLY VAL SER GLY GLY VAL ALA SER PHE ILE CYS GLN
SEQRES 3 A 841 ALA THR GLY ASP PRO ARG PRO LYS ILE VAL TRP ASN LYS
SEQRES 4 A 841 LYS GLY LYS LYS VAL SER ASN GLN ARG PHE GLU VAL ILE
SEQRES 5 A 841 GLU PHE ASP ASP GLY SER GLY SER VAL LEU ARG ILE GLN
SEQRES 6 A 841 PRO LEU ARG THR PRO ARG ASP GLU ALA ILE TYR GLU CYS
SEQRES 7 A 841 VAL ALA SER ASN ASN VAL GLY GLU ILE SER VAL SER THR
SEQRES 8 A 841 ARG LEU THR VAL LEU ARG GLU ASP GLN ILE PRO ARG GLY
SEQRES 9 A 841 PHE PRO THR ILE ASP MET GLY PRO GLN LEU LYS VAL VAL
SEQRES 10 A 841 GLU ARG THR ARG THR ALA THR MET LEU CYS ALA ALA SER
SEQRES 11 A 841 GLY ASN PRO ASP PRO GLU ILE THR TRP PHE LYS ASP PHE
SEQRES 12 A 841 LEU PRO VAL ASP THR SER ASN ASN ASN GLY ARG ILE LYS
SEQRES 13 A 841 GLN LEU ARG SER GLU SER ILE GLY GLY THR PRO ILE ARG
SEQRES 14 A 841 GLY ALA LEU GLN ILE GLU GLN SER GLU GLU SER ASP GLN
SEQRES 15 A 841 GLY LYS TYR GLU CYS VAL ALA THR ASN SER ALA GLY THR
SEQRES 16 A 841 ARG TYR SER ALA PRO ALA ASN LEU TYR VAL ARG GLU LEU
SEQRES 17 A 841 ARG GLU VAL ARG ARG VAL PRO PRO ARG PHE SER ILE PRO
SEQRES 18 A 841 PRO THR ASN HIS GLU ILE MET PRO GLY GLY SER VAL ASN
SEQRES 19 A 841 ILE THR CYS VAL ALA VAL GLY SER PRO MET PRO TYR VAL
SEQRES 20 A 841 LYS TRP MET LEU GLY ALA GLU ASP LEU THR PRO GLU ASP
SEQRES 21 A 841 ASP MET PRO ILE GLY ARG ASN VAL LEU GLU LEU ASN ASP
SEQRES 22 A 841 VAL ARG GLN SER ALA ASN TYR THR CYS VAL ALA MET SER
SEQRES 23 A 841 THR LEU GLY VAL ILE GLU ALA ILE ALA GLN ILE THR VAL
SEQRES 24 A 841 LYS ALA LEU PRO LYS PRO PRO GLY THR PRO VAL VAL THR
SEQRES 25 A 841 GLU SER THR ALA THR SER ILE THR LEU THR TRP ASP SER
SEQRES 26 A 841 GLY ASN PRO GLU PRO VAL SER TYR TYR ILE ILE GLN HIS
SEQRES 27 A 841 LYS PRO LYS ASN SER GLU GLU PRO TYR LYS GLU ILE ASP
SEQRES 28 A 841 GLY ILE ALA THR THR ARG TYR SER VAL ALA GLY LEU SER
SEQRES 29 A 841 PRO TYR SER ASP TYR GLU PHE ARG VAL VAL ALA VAL ASN
SEQRES 30 A 841 ASN ILE GLY ARG GLY PRO ALA SER GLU PRO VAL LEU THR
SEQRES 31 A 841 GLN THR SER GLU GLN ALA PRO SER SER ALA PRO ARG ASP
SEQRES 32 A 841 VAL GLN ALA ARG MET LEU SER SER THR THR ILE LEU VAL
SEQRES 33 A 841 GLN TRP LYS GLU PRO GLU GLU PRO ASN GLY GLN ILE GLN
SEQRES 34 A 841 GLY TYR ARG VAL TYR TYR THR MET ASP PRO THR GLN HIS
SEQRES 35 A 841 VAL ASN ASN TRP MET LYS HIS ASN VAL ALA ASP SER GLN
SEQRES 36 A 841 ILE THR THR ILE GLY ASN LEU VAL PRO GLN LYS THR TYR
SEQRES 37 A 841 SER VAL LYS VAL LEU ALA PHE THR SER ILE GLY ASP GLY
SEQRES 38 A 841 PRO LEU SER SER ASP ILE GLN VAL ILE THR GLN THR GLY
SEQRES 39 A 841 VAL PRO GLY GLN PRO LEU ASN PHE LYS ALA GLU PRO GLU
SEQRES 40 A 841 SER GLU THR SER ILE LEU LEU SER TRP THR PRO PRO ARG
SEQRES 41 A 841 SER ASP THR ILE ALA SER TYR GLU LEU VAL TYR ARG ASP
SEQRES 42 A 841 GLY ASP GLN GLY GLU GLU GLN ARG ILE THR ILE GLU PRO
SEQRES 43 A 841 GLY THR SER TYR ARG LEU GLN GLY LEU LYS PRO ASN SER
SEQRES 44 A 841 LEU TYR TYR PHE ARG LEU SER ALA ARG SER PRO GLN GLY
SEQRES 45 A 841 LEU GLY ALA SER THR ALA GLU ILE SER ALA ARG THR MET
SEQRES 46 A 841 GLN SER MET PHE ALA LYS ASN PHE HIS VAL LYS ALA VAL
SEQRES 47 A 841 MET LYS THR SER VAL LEU LEU SER TRP GLU ILE PRO GLU
SEQRES 48 A 841 ASN TYR ASN SER ALA MET PRO PHE LYS ILE LEU TYR ASP
SEQRES 49 A 841 ASP GLY LYS MET VAL GLU GLU VAL ASP GLY ARG ALA THR
SEQRES 50 A 841 GLN LYS LEU ILE VAL ASN LEU LYS PRO GLU LYS SER TYR
SEQRES 51 A 841 SER PHE VAL LEU THR ASN ARG GLY ASN SER ALA GLY GLY
SEQRES 52 A 841 LEU GLN HIS ARG VAL THR ALA LYS THR ALA PRO ASP VAL
SEQRES 53 A 841 LEU ARG THR LYS PRO ALA PHE ILE GLY LYS THR ASN LEU
SEQRES 54 A 841 ASP GLY MET ILE THR VAL GLN LEU PRO ASP VAL PRO ALA
SEQRES 55 A 841 ASN GLU ASN ILE LYS GLY TYR TYR ILE ILE ILE VAL PRO
SEQRES 56 A 841 LEU LYS LYS SER ARG GLY LYS PHE ILE LYS PRO TRP GLU
SEQRES 57 A 841 SER PRO ASP GLU MET GLU LEU ASP GLU LEU LEU LYS GLU
SEQRES 58 A 841 ILE SER ARG LYS ARG ARG SER ILE ARG TYR GLY ARG GLU
SEQRES 59 A 841 VAL GLU LEU LYS PRO TYR ILE ALA ALA HIS PHE ASP VAL
SEQRES 60 A 841 LEU PRO THR GLU PHE THR LEU GLY ASP ASP LYS HIS TYR
SEQRES 61 A 841 GLY GLY PHE THR ASN LYS GLN LEU GLN SER GLY GLN GLU
SEQRES 62 A 841 TYR VAL PHE PHE VAL LEU ALA VAL MET ASP HIS ALA GLU
SEQRES 63 A 841 SER LYS MET TYR ALA THR SER PRO TYR SER ASP PRO VAL
SEQRES 64 A 841 VAL SER MET ASP LEU ASP PRO GLN PRO ILE THR ASP GLU
SEQRES 65 A 841 GLU GLU LYS HIS HIS HIS HIS HIS HIS
SEQRES 1 B 348 ALA GLN PRO ALA ALA ARG ASP LEU LYS VAL VAL THR LYS
SEQRES 2 B 348 ARG GLY SER ALA ASP GLY CYS THR ASP TRP SER VAL ASP
SEQRES 3 B 348 ILE LYS LYS TYR GLN VAL LEU VAL GLY GLU PRO VAL ARG
SEQRES 4 B 348 ILE LYS CYS ALA LEU PHE TYR GLY TYR ILE ARG THR ASN
SEQRES 5 B 348 TYR SER LEU ALA GLN SER ALA GLY LEU SER LEU MET TRP
SEQRES 6 B 348 TYR LYS SER SER GLY PRO GLY ASP PHE GLU GLU PRO ILE
SEQRES 7 B 348 ALA PHE ASP GLY SER ARG MET SER LYS GLU GLU ASP SER
SEQRES 8 B 348 ILE TRP PHE ARG PRO THR LEU LEU GLN ASP SER GLY LEU
SEQRES 9 B 348 TYR ALA CYS VAL ILE ARG ASN SER THR TYR CYS MET LYS
SEQRES 10 B 348 VAL SER ILE SER LEU THR VAL GLY GLU ASN ASP THR GLY
SEQRES 11 B 348 LEU CYS TYR ASN SER LYS MET LYS TYR PHE GLU LYS ALA
SEQRES 12 B 348 GLU LEU SER LYS SER LYS GLU ILE SER CYS ARG ASP ILE
SEQRES 13 B 348 GLU ASP PHE LEU LEU PRO THR ARG GLU PRO GLU ILE LEU
SEQRES 14 B 348 TRP TYR LYS GLU CYS ARG THR LYS ALA TRP ARG PRO SER
SEQRES 15 B 348 ILE VAL PHE LYS ARG ASP THR LEU LEU ILE LYS GLU VAL
SEQRES 16 B 348 LYS GLU ASP ASP ILE GLY ASN TYR THR CYS GLU LEU LYS
SEQRES 17 B 348 TYR GLY GLY PHE VAL VAL ARG ARG THR THR GLU LEU THR
SEQRES 18 B 348 VAL THR ALA PRO LEU THR ASP LYS PRO PRO LYS LEU LEU
SEQRES 19 B 348 TYR PRO MET GLU SER LYS LEU THR VAL GLN GLU THR GLN
SEQRES 20 B 348 LEU GLY GLY SER ALA ASN LEU THR CYS ARG ALA PHE PHE
SEQRES 21 B 348 GLY TYR SER GLY ASP VAL SER PRO LEU ILE TYR TRP MET
SEQRES 22 B 348 LYS GLY GLU LYS PHE ILE GLU ASP LEU ASP GLU ASN ARG
SEQRES 23 B 348 VAL TRP GLU SER ASP ILE ARG ILE LEU LYS GLU HIS LEU
SEQRES 24 B 348 GLY GLU GLN GLU VAL SER ILE SER LEU ILE VAL ASP SER
SEQRES 25 B 348 VAL GLU GLU GLY ASP LEU GLY ASN TYR SER CYS TYR VAL
SEQRES 26 B 348 GLU ASN GLY ASN GLY ARG ARG HIS ALA SER VAL LEU LEU
SEQRES 27 B 348 HIS LYS ARG LYS HIS HIS HIS HIS HIS HIS
HET NAG C 1 14
HET NAG C 2 14
HET NAG D 1 14
HET NAG D 2 14
HET BMA D 3 11
HET MAN D 4 11
HET MAN D 5 11
HET NAG B 401 14
HET NAG B 402 14
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM BMA BETA-D-MANNOPYRANOSE
HETNAM MAN ALPHA-D-MANNOPYRANOSE
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
HETSYN BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE
HETSYN MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE
FORMUL 3 NAG 6(C8 H15 N O6)
FORMUL 4 BMA C6 H12 O6
FORMUL 4 MAN 2(C6 H12 O6)
HELIX 1 AA1 ARG A 124 ILE A 128 5 5
HELIX 2 AA2 GLU A 205 GLN A 209 5 5
HELIX 3 AA3 HIS A 469 TRP A 473 5 5
HELIX 4 AA4 ALA B 54 TYR B 57 5 4
HELIX 5 AA5 ASN B 63 ALA B 70 1 8
HELIX 6 AA6 LEU B 109 SER B 113 5 5
HELIX 7 AA7 LYS B 207 ILE B 211 5 5
HELIX 8 AA8 ILE B 290 ASP B 294 1 5
SHEET 1 AA1 4 ARG A 32 ARG A 35 0
SHEET 2 AA1 4 ALA A 48 THR A 55 -1 O THR A 55 N ARG A 32
SHEET 3 AA1 4 SER A 87 ILE A 91 -1 O ILE A 91 N ALA A 48
SHEET 4 AA1 4 PHE A 76 GLU A 80 -1 N ILE A 79 O VAL A 88
SHEET 1 AA2 5 GLN A 40 VAL A 43 0
SHEET 2 AA2 5 GLY A 112 LEU A 123 1 O LEU A 123 N GLY A 42
SHEET 3 AA2 5 ALA A 101 ASN A 109 -1 N ALA A 107 O ILE A 114
SHEET 4 AA2 5 LYS A 61 LYS A 66 -1 N ASN A 65 O GLU A 104
SHEET 5 AA2 5 LYS A 69 LYS A 70 -1 O LYS A 69 N LYS A 66
SHEET 1 AA3 4 THR A 134 MET A 137 0
SHEET 2 AA3 4 ALA A 150 SER A 157 -1 O ALA A 155 N MET A 137
SHEET 3 AA3 4 ILE A 195 ILE A 201 -1 O ILE A 201 N ALA A 150
SHEET 4 AA3 4 ILE A 182 ARG A 186 -1 N LYS A 183 O GLN A 200
SHEET 1 AA4 5 LYS A 142 GLU A 145 0
SHEET 2 AA4 5 ALA A 228 ARG A 233 1 O ARG A 233 N VAL A 144
SHEET 3 AA4 5 GLY A 210 ASN A 218 -1 N TYR A 212 O ALA A 228
SHEET 4 AA4 5 GLU A 163 LYS A 168 -1 N GLU A 163 O THR A 217
SHEET 5 AA4 5 LEU A 171 PRO A 172 -1 O LEU A 171 N LYS A 168
SHEET 1 AA5 4 LYS A 142 GLU A 145 0
SHEET 2 AA5 4 ALA A 228 ARG A 233 1 O ARG A 233 N VAL A 144
SHEET 3 AA5 4 GLY A 210 ASN A 218 -1 N TYR A 212 O ALA A 228
SHEET 4 AA5 4 GLY A 221 TYR A 224 -1 O ARG A 223 N ALA A 216
SHEET 1 AA6 3 ARG A 244 ILE A 247 0
SHEET 2 AA6 3 VAL A 260 VAL A 267 -1 O VAL A 267 N ARG A 244
SHEET 3 AA6 3 ARG A 293 LEU A 298 -1 O LEU A 296 N ILE A 262
SHEET 1 AA7 4 HIS A 252 GLU A 253 0
SHEET 2 AA7 4 ILE A 321 THR A 325 1 O GLN A 323 N HIS A 252
SHEET 3 AA7 4 ALA A 305 MET A 312 -1 N TYR A 307 O ALA A 322
SHEET 4 AA7 4 TYR A 273 MET A 277 -1 N MET A 277 O THR A 308
SHEET 1 AA8 4 HIS A 252 GLU A 253 0
SHEET 2 AA8 4 ILE A 321 THR A 325 1 O GLN A 323 N HIS A 252
SHEET 3 AA8 4 ALA A 305 MET A 312 -1 N TYR A 307 O ALA A 322
SHEET 4 AA8 4 VAL A 317 ILE A 318 -1 O ILE A 318 N ALA A 311
SHEET 1 AA9 3 GLY A 334 SER A 341 0
SHEET 2 AA9 3 ILE A 346 ASP A 351 -1 O THR A 347 N GLU A 340
SHEET 3 AA9 3 ARG A 384 VAL A 387 -1 O TYR A 385 N LEU A 348
SHEET 1 AB1 4 LYS A 375 ILE A 380 0
SHEET 2 AB1 4 TYR A 360 LYS A 366 -1 N HIS A 365 O LYS A 375
SHEET 3 AB1 4 ASP A 395 VAL A 403 -1 O GLU A 397 N LYS A 366
SHEET 4 AB1 4 VAL A 415 GLN A 418 -1 O VAL A 415 N PHE A 398
SHEET 1 AB2 3 ARG A 429 MET A 435 0
SHEET 2 AB2 3 ILE A 441 LYS A 446 -1 O LEU A 442 N ARG A 434
SHEET 3 AB2 3 ILE A 483 ILE A 486 -1 O THR A 484 N VAL A 443
SHEET 1 AB3 3 GLY A 457 VAL A 460 0
SHEET 2 AB3 3 VAL A 497 PHE A 502 -1 O LEU A 500 N ARG A 459
SHEET 3 AB3 3 ASP A 507 ILE A 514 -1 O ILE A 514 N VAL A 497
SHEET 1 AB4 3 LEU A 527 GLU A 532 0
SHEET 2 AB4 3 SER A 538 THR A 544 -1 O LEU A 540 N GLU A 532
SHEET 3 AB4 3 SER A 576 GLN A 580 -1 O LEU A 579 N ILE A 539
SHEET 1 AB5 4 GLN A 567 ILE A 571 0
SHEET 2 AB5 4 SER A 553 ASP A 560 -1 N TYR A 558 O GLN A 567
SHEET 3 AB5 4 LEU A 587 ARG A 595 -1 O TYR A 589 N ARG A 559
SHEET 4 AB5 4 LEU A 600 SER A 603 -1 O GLY A 601 N ALA A 594
SHEET 1 AB6 4 GLN A 567 ILE A 571 0
SHEET 2 AB6 4 SER A 553 ASP A 560 -1 N TYR A 558 O GLN A 567
SHEET 3 AB6 4 LEU A 587 ARG A 595 -1 O TYR A 589 N ARG A 559
SHEET 4 AB6 4 ILE A 607 ARG A 610 -1 O ALA A 609 N TYR A 588
SHEET 1 AB7 3 THR B 32 VAL B 36 0
SHEET 2 AB7 3 CYS B 126 GLY B 136 1 O LYS B 128 N TRP B 34
SHEET 3 AB7 3 TYR B 41 LEU B 44 1 N TYR B 41 O SER B 132
SHEET 1 AB8 4 THR B 32 VAL B 36 0
SHEET 2 AB8 4 CYS B 126 GLY B 136 1 O LYS B 128 N TRP B 34
SHEET 3 AB8 4 GLY B 114 ARG B 121 -1 N GLY B 114 O LEU B 133
SHEET 4 AB8 4 SER B 73 SER B 79 -1 N MET B 75 O VAL B 119
SHEET 1 AB9 2 VAL B 49 LYS B 52 0
SHEET 2 AB9 2 SER B 102 PHE B 105 -1 O PHE B 105 N VAL B 49
SHEET 1 AC1 4 TYR B 150 GLU B 155 0
SHEET 2 AC1 4 PHE B 223 THR B 234 1 O THR B 234 N ALA B 154
SHEET 3 AC1 4 GLY B 212 TYR B 220 -1 N GLY B 212 O LEU B 231
SHEET 4 AC1 4 TYR B 182 LYS B 183 -1 N TYR B 182 O THR B 215
SHEET 1 AC2 3 LYS B 160 ILE B 162 0
SHEET 2 AC2 3 LEU B 201 ILE B 203 -1 O ILE B 203 N LYS B 160
SHEET 3 AC2 3 ILE B 194 PHE B 196 -1 N VAL B 195 O LEU B 202
SHEET 1 AC3 4 LYS B 243 TYR B 246 0
SHEET 2 AC3 4 ALA B 263 PHE B 271 -1 O ARG B 268 N TYR B 246
SHEET 3 AC3 4 GLU B 312 VAL B 321 -1 O VAL B 321 N ALA B 263
SHEET 4 AC3 4 VAL B 298 GLU B 300 -1 N TRP B 299 O ILE B 320
SHEET 1 AC4 4 LYS B 243 TYR B 246 0
SHEET 2 AC4 4 ALA B 263 PHE B 271 -1 O ARG B 268 N TYR B 246
SHEET 3 AC4 4 GLU B 312 VAL B 321 -1 O VAL B 321 N ALA B 263
SHEET 4 AC4 4 ARG B 304 HIS B 309 -1 N ARG B 304 O SER B 316
SHEET 1 AC5 5 THR B 253 GLU B 256 0
SHEET 2 AC5 5 GLY B 341 HIS B 350 1 O LEU B 348 N GLN B 255
SHEET 3 AC5 5 GLY B 330 ASN B 338 -1 N VAL B 336 O ARG B 343
SHEET 4 AC5 5 LEU B 280 LYS B 285 -1 N TYR B 282 O TYR B 335
SHEET 5 AC5 5 LYS B 288 PHE B 289 -1 O LYS B 288 N LYS B 285
SSBOND 1 CYS A 52 CYS A 105 1555 1555 2.03
SSBOND 2 CYS A 264 CYS A 309 1555 1555 2.03
SSBOND 3 CYS B 31 CYS B 126 1555 1555 2.03
SSBOND 4 CYS B 53 CYS B 118 1555 1555 2.04
SSBOND 5 CYS B 143 CYS B 185 1555 1555 2.04
SSBOND 6 CYS B 164 CYS B 216 1555 1555 2.03
SSBOND 7 CYS B 267 CYS B 334 1555 1555 2.03
LINK ND2 ASN B 122 C1 NAG B 401 1555 1555 1.46
LINK ND2 ASN B 138 C1 NAG B 402 1555 1555 1.45
LINK ND2 ASN B 213 C1 NAG C 1 1555 1555 1.44
LINK ND2 ASN B 264 C1 NAG D 1 1555 1555 1.45
LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.44
LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.45
LINK O4 NAG D 2 C1 BMA D 3 1555 1555 1.44
LINK O3 BMA D 3 C1 MAN D 4 1555 1555 1.46
LINK O6 BMA D 3 C1 MAN D 5 1555 1555 1.46
CISPEP 1 ASP A 57 PRO A 58 0 1.06
CISPEP 2 GLN A 92 PRO A 93 0 -1.91
CISPEP 3 THR A 96 PRO A 97 0 -2.58
CISPEP 4 ASN A 159 PRO A 160 0 2.65
CISPEP 5 SER A 269 PRO A 270 0 1.34
CISPEP 6 PRO B 82 GLY B 83 0 -1.69
CISPEP 7 ARG B 106 PRO B 107 0 -0.38
CISPEP 8 GLY B 221 GLY B 222 0 7.04
CISPEP 9 TYR B 246 PRO B 247 0 -4.83
CISPEP 10 LEU B 310 GLY B 311 0 -10.61
CISPEP 11 GLU B 326 GLY B 327 0 9.93
CRYST1 286.295 286.295 70.183 90.00 90.00 90.00 I 41 8
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 0.003493 0.000000 0.000000 0.00000
SCALE2 0.000000 0.003493 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014248 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
