| content |
HEADER CELL ADHESION 20-JUL-17 5OJ6
TITLE CRYSTAL STRUCTURE OF THE CHICKEN MDGA1 ECTODOMAIN IN COMPLEX WITH THE
TITLE 2 HUMAN NEUROLIGIN 1 (NL1(-A-B)) CHOLINESTERASE DOMAIN.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NEUROLIGIN-1;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: MAM DOMAIN-CONTAINING GLYCOSYLPHOSPHATIDYLINOSITOL ANCHOR
COMPND 7 PROTEIN 1;
COMPND 8 CHAIN: B;
COMPND 9 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: NLGN1, KIAA1070;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: HEK293S GNTI-/-;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PHLSEC;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: GALLUS GALLUS;
SOURCE 12 ORGANISM_COMMON: CHICKEN;
SOURCE 13 ORGANISM_TAXID: 9031;
SOURCE 14 GENE: MDGA1;
SOURCE 15 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 17 EXPRESSION_SYSTEM_CELL_LINE: HEK293S GNTI-/-;
SOURCE 18 EXPRESSION_SYSTEM_PLASMID: PHLSEC
KEYWDS NEUROLIGIN-NEUREXIN, SYNAPSE FORMATION, AUSTISM SPECTRUM DISORDERS
KEYWDS 2 (ASDS), SYNAPTIC TRANSMISSION, CELL ADHESION
EXPDTA X-RAY DIFFRACTION
AUTHOR J.ELEGHEERT,A.J.CLAYTON,A.R.ARICESCU
REVDAT 1 23-AUG-17 5OJ6 0
JRNL AUTH J.ELEGHEERT,V.CVETKOVSKA,A.J.CLAYTON,C.HEROVEN,
JRNL AUTH 2 K.M.VENNEKENS,S.N.SMUKOWSKI,M.C.REGAN,W.JIA,A.C.SMITH,
JRNL AUTH 3 H.FURUKAWA,J.N.SAVAS,J.DE WIT,J.BEGBIE,A.M.CRAIG,
JRNL AUTH 4 A.R.ARICESCU
JRNL TITL STRUCTURAL MECHANISM FOR MODULATION OF SYNAPTIC
JRNL TITL 2 NEUROLIGIN-NEUREXIN SIGNALING BY MDGA PROTEINS
JRNL REF NEURON V. 95 896 2017
JRNL REFN ISSN 0896-6273
JRNL DOI 10.1016/J.NEURON.2017.07.040
REMARK 2
REMARK 2 RESOLUTION. 3.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (DEV_2044:)
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 72.36
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 3 NUMBER OF REFLECTIONS : 29572
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.229
REMARK 3 R VALUE (WORKING SET) : 0.227
REMARK 3 FREE R VALUE : 0.277
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.980
REMARK 3 FREE R VALUE TEST SET COUNT : 1474
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 72.3795 - 7.3371 0.97 2678 131 0.2352 0.2621
REMARK 3 2 7.3371 - 5.8244 0.99 2620 142 0.2448 0.2579
REMARK 3 3 5.8244 - 5.0884 1.00 2595 142 0.2035 0.2972
REMARK 3 4 5.0884 - 4.6233 0.98 2557 130 0.1837 0.2546
REMARK 3 5 4.6233 - 4.2919 0.97 2515 119 0.1890 0.2084
REMARK 3 6 4.2919 - 4.0389 0.99 2545 121 0.1994 0.2616
REMARK 3 7 4.0389 - 3.8366 0.99 2534 151 0.2241 0.3015
REMARK 3 8 3.8366 - 3.6696 0.99 2519 147 0.2546 0.2906
REMARK 3 9 3.6696 - 3.5284 0.99 2535 135 0.2663 0.3426
REMARK 3 10 3.5284 - 3.4066 1.00 2527 138 0.2906 0.3657
REMARK 3 11 3.4066 - 3.3001 0.96 2473 118 0.3181 0.3838
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.00
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.470
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.590
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 : 0.003 10061
REMARK 3 ANGLE : 0.939 13737
REMARK 3 CHIRALITY : 0.041 1569
REMARK 3 PLANARITY : 0.004 1774
REMARK 3 DIHEDRAL : 11.487 6051
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 5OJ6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 20-JUL-17.
REMARK 100 THE DEPOSITION ID IS D_1200005895.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-MAY-14
REMARK 200 TEMPERATURE (KELVIN) : 80
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I04-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.92000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XIA2
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29576
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.300
REMARK 200 RESOLUTION RANGE LOW (A) : 92.070
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 200 DATA REDUNDANCY : 4.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 15.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.39
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.4
REMARK 200 DATA REDUNDANCY IN SHELL : 4.60
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 5OJ2
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.84
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.92
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M NA.HEPES PH 7.0, 7.5% W/V
REMARK 280 PEG8000, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
REMARK 290 4555 X+1/2,-Y+1/2,-Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 54.71000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 92.07000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 54.71000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 92.07000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 14960 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 111120 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 37.0 KCAL/MOL
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 350 BIOMT1 2 -1.000000 0.000000 0.000000 109.42000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 368.28000
REMARK 350 BIOMT3 2 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 THR A 44
REMARK 465 GLY A 45
REMARK 465 GLN A 46
REMARK 465 LYS A 47
REMARK 465 LEU A 48
REMARK 465 ASP A 49
REMARK 465 ASP A 50
REMARK 465 ASP A 181
REMARK 465 ASP A 182
REMARK 465 ILE A 183
REMARK 465 THR A 577
REMARK 465 LYS A 578
REMARK 465 PHE A 579
REMARK 465 ILE A 580
REMARK 465 HIS A 581
REMARK 465 THR A 582
REMARK 465 LYS A 583
REMARK 465 ASN A 634
REMARK 465 ASP A 635
REMARK 465 ARG A 636
REMARK 465 THR A 637
REMARK 465 LYS A 638
REMARK 465 HIS A 639
REMARK 465 HIS A 640
REMARK 465 HIS A 641
REMARK 465 HIS A 642
REMARK 465 HIS A 643
REMARK 465 HIS A 644
REMARK 465 VAL B 38
REMARK 465 LYS B 39
REMARK 465 GLU B 40
REMARK 465 ASP B 41
REMARK 465 ASN B 42
REMARK 465 ILE B 43
REMARK 465 SER B 44
REMARK 465 ILE B 140
REMARK 465 SER B 141
REMARK 465 ASP B 142
REMARK 465 VAL B 143
REMARK 465 ARG B 144
REMARK 465 GLY B 145
REMARK 465 SER B 146
REMARK 465 SER B 179
REMARK 465 GLN B 180
REMARK 465 ASP B 181
REMARK 465 ASN B 182
REMARK 465 GLY B 183
REMARK 465 ALA B 378
REMARK 465 ARG B 379
REMARK 465 PHE B 380
REMARK 465 PRO B 584
REMARK 465 PRO B 585
REMARK 465 ALA B 586
REMARK 465 GLU B 587
REMARK 465 GLN B 588
REMARK 465 GLU B 735
REMARK 465 PRO B 736
REMARK 465 ILE B 737
REMARK 465 ASN B 738
REMARK 465 TYR B 739
REMARK 465 PRO B 740
REMARK 465 SER B 741
REMARK 465 PRO B 742
REMARK 465 THR B 743
REMARK 465 ASP B 744
REMARK 465 ASN B 745
REMARK 465 THR B 746
REMARK 465 CYS B 747
REMARK 465 ARG B 748
REMARK 465 PHE B 749
REMARK 465 GLU B 750
REMARK 465 ASP B 751
REMARK 465 GLU B 752
REMARK 465 LYS B 753
REMARK 465 ILE B 754
REMARK 465 CYS B 755
REMARK 465 GLY B 756
REMARK 465 PHE B 757
REMARK 465 VAL B 758
REMARK 465 GLN B 759
REMARK 465 ASP B 760
REMARK 465 LYS B 761
REMARK 465 MET B 762
REMARK 465 ASP B 763
REMARK 465 ASN B 764
REMARK 465 PHE B 765
REMARK 465 ASP B 766
REMARK 465 TRP B 767
REMARK 465 THR B 768
REMARK 465 ARG B 769
REMARK 465 GLN B 770
REMARK 465 ASN B 771
REMARK 465 ALA B 772
REMARK 465 LEU B 773
REMARK 465 THR B 774
REMARK 465 GLN B 775
REMARK 465 ASN B 776
REMARK 465 PRO B 777
REMARK 465 LYS B 778
REMARK 465 ARG B 779
REMARK 465 THR B 780
REMARK 465 VAL B 781
REMARK 465 ASN B 782
REMARK 465 THR B 783
REMARK 465 GLY B 784
REMARK 465 PRO B 785
REMARK 465 PRO B 786
REMARK 465 THR B 787
REMARK 465 ASP B 788
REMARK 465 ILE B 789
REMARK 465 SER B 790
REMARK 465 GLY B 791
REMARK 465 THR B 792
REMARK 465 PRO B 793
REMARK 465 GLU B 794
REMARK 465 GLY B 795
REMARK 465 TYR B 796
REMARK 465 TYR B 797
REMARK 465 MET B 798
REMARK 465 PHE B 799
REMARK 465 ILE B 800
REMARK 465 GLU B 801
REMARK 465 ALA B 802
REMARK 465 SER B 803
REMARK 465 ARG B 804
REMARK 465 PRO B 805
REMARK 465 ARG B 806
REMARK 465 VAL B 807
REMARK 465 THR B 808
REMARK 465 GLY B 809
REMARK 465 ASP B 810
REMARK 465 LYS B 811
REMARK 465 ALA B 812
REMARK 465 ARG B 813
REMARK 465 LEU B 814
REMARK 465 ILE B 815
REMARK 465 SER B 816
REMARK 465 PRO B 817
REMARK 465 LEU B 818
REMARK 465 TYR B 819
REMARK 465 ASN B 820
REMARK 465 ILE B 821
REMARK 465 THR B 822
REMARK 465 ALA B 823
REMARK 465 LYS B 824
REMARK 465 TYR B 825
REMARK 465 TYR B 826
REMARK 465 CYS B 827
REMARK 465 VAL B 828
REMARK 465 SER B 829
REMARK 465 PHE B 830
REMARK 465 TYR B 831
REMARK 465 TYR B 832
REMARK 465 HIS B 833
REMARK 465 MET B 834
REMARK 465 TYR B 835
REMARK 465 GLY B 836
REMARK 465 LYS B 837
REMARK 465 HIS B 838
REMARK 465 ILE B 839
REMARK 465 GLY B 840
REMARK 465 SER B 841
REMARK 465 LEU B 842
REMARK 465 ASN B 843
REMARK 465 LEU B 844
REMARK 465 LEU B 845
REMARK 465 VAL B 846
REMARK 465 ARG B 847
REMARK 465 VAL B 848
REMARK 465 ARG B 849
REMARK 465 ASN B 850
REMARK 465 LYS B 851
REMARK 465 ARG B 852
REMARK 465 ALA B 853
REMARK 465 ILE B 854
REMARK 465 ASP B 855
REMARK 465 THR B 856
REMARK 465 GLN B 857
REMARK 465 VAL B 858
REMARK 465 TRP B 859
REMARK 465 SER B 860
REMARK 465 LEU B 861
REMARK 465 SER B 862
REMARK 465 GLY B 863
REMARK 465 ASN B 864
REMARK 465 ARG B 865
REMARK 465 GLY B 866
REMARK 465 ASN B 867
REMARK 465 MET B 868
REMARK 465 TRP B 869
REMARK 465 GLN B 870
REMARK 465 GLN B 871
REMARK 465 ALA B 872
REMARK 465 HIS B 873
REMARK 465 VAL B 874
REMARK 465 PRO B 875
REMARK 465 ILE B 876
REMARK 465 ASN B 877
REMARK 465 PRO B 878
REMARK 465 PRO B 879
REMARK 465 GLY B 880
REMARK 465 PRO B 881
REMARK 465 PHE B 882
REMARK 465 GLN B 883
REMARK 465 ILE B 884
REMARK 465 ILE B 885
REMARK 465 PHE B 886
REMARK 465 GLU B 887
REMARK 465 GLY B 888
REMARK 465 VAL B 889
REMARK 465 ARG B 890
REMARK 465 GLY B 891
REMARK 465 THR B 892
REMARK 465 SER B 893
REMARK 465 TYR B 894
REMARK 465 GLU B 895
REMARK 465 GLY B 896
REMARK 465 ASP B 897
REMARK 465 ILE B 898
REMARK 465 ALA B 899
REMARK 465 ILE B 900
REMARK 465 ASP B 901
REMARK 465 ASP B 902
REMARK 465 VAL B 903
REMARK 465 THR B 904
REMARK 465 LEU B 905
REMARK 465 LYS B 906
REMARK 465 LYS B 907
REMARK 465 GLY B 908
REMARK 465 ASP B 909
REMARK 465 CYS B 910
REMARK 465 PRO B 911
REMARK 465 ARG B 912
REMARK 465 LYS B 913
REMARK 465 PRO B 914
REMARK 465 ILE B 915
REMARK 465 GLY B 916
REMARK 465 PRO B 917
REMARK 465 ASN B 918
REMARK 465 LYS B 919
REMARK 465 GLY B 920
REMARK 465 THR B 921
REMARK 465 LYS B 922
REMARK 465 HIS B 923
REMARK 465 HIS B 924
REMARK 465 HIS B 925
REMARK 465 HIS B 926
REMARK 465 HIS B 927
REMARK 465 HIS B 928
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 GLU A 163 CG CD OE1 OE2
REMARK 470 ARG A 184 CG CD NE CZ NH1 NH2
REMARK 470 ASP A 185 CG OD1 OD2
REMARK 470 GLN A 510 CG CD OE1 NE2
REMARK 470 HIS A 629 CG ND1 CD2 CE1 NE2
REMARK 470 HIS A 631 CG ND1 CD2 CE1 NE2
REMARK 470 PHE B 147 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASN B 203 CG OD1 ND2
REMARK 470 GLN B 289 CG CD OE1 NE2
REMARK 470 LYS B 376 CG CD CE NZ
REMARK 470 ARG B 388 CG CD NE CZ NH1 NH2
REMARK 470 ASN B 639 CG OD1 ND2
REMARK 470 LYS B 648 CG CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OG SER B 643 O4 NAG B 1001 4477 2.07
REMARK 500 O VAL B 273 NE2 GLN B 690 4577 2.09
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 PRO A 53 98.92 -67.80
REMARK 500 ASP A 106 -158.84 -99.81
REMARK 500 ASN A 138 44.84 -142.47
REMARK 500 THR A 162 55.10 -101.90
REMARK 500 ASP A 185 -110.99 59.03
REMARK 500 TYR A 201 -7.10 80.43
REMARK 500 ASP A 239 -158.43 -140.11
REMARK 500 ALA A 372 -63.22 -93.75
REMARK 500 ASP A 380 -75.00 -121.56
REMARK 500 TYR A 440 65.18 -112.22
REMARK 500 ASP A 462 40.95 79.70
REMARK 500 TRP A 482 -53.45 -124.87
REMARK 500 ARG A 610 158.63 178.85
REMARK 500 ARG A 616 43.60 39.61
REMARK 500 ASN A 632 9.63 81.14
REMARK 500 ASP B 81 -136.91 55.27
REMARK 500 LYS B 82 84.31 -66.40
REMARK 500 ARG B 171 55.97 -115.85
REMARK 500 GLN B 193 50.89 -101.78
REMARK 500 ASN B 285 19.93 51.24
REMARK 500 ASN B 312 18.73 -145.30
REMARK 500 PRO B 338 173.10 -57.14
REMARK 500 ASP B 382 -119.26 65.87
REMARK 500 LEU B 384 -56.42 72.43
REMARK 500 ASP B 404 70.70 56.12
REMARK 500 TYR B 410 107.81 -59.17
REMARK 500 GLN B 420 105.77 -58.77
REMARK 500 LYS B 446 -130.96 56.40
REMARK 500 SER B 457 -179.11 -62.05
REMARK 500 LEU B 562 -64.47 -98.46
REMARK 500 LEU B 581 -160.49 -110.72
REMARK 500 ASP B 590 -13.61 76.16
REMARK 500 VAL B 599 84.86 -65.40
REMARK 500 ASP B 636 64.97 -102.20
REMARK 500 GLN B 644 23.36 44.50
REMARK 500 LYS B 645 16.11 54.01
REMARK 500 VAL B 664 -159.27 -136.96
REMARK 500 LEU B 677 -53.37 68.46
REMARK 500 LYS B 691 162.70 175.09
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 1009
REMARK 800 bound to ASN B 90
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 1007
REMARK 800 bound to ASN B 235
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 1001
REMARK 800 bound to ASN B 257
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 1011
REMARK 800 bound to ASN B 292
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 1002
REMARK 800 bound to ASN B 307
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B
REMARK 800 1003 through BMA B 1005 bound to ASN B 331
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 1008
REMARK 800 bound to ASN B 432
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 1010
REMARK 800 bound to ASN B 577
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 1006
REMARK 800 bound to ASN B 649
DBREF 5OJ6 A 46 635 UNP Q8N2Q7 NLGN1_HUMAN 46 618
DBREF 5OJ6 B 19 919 UNP Q0WYX8 MDGA1_CHICK 19 919
SEQADV 5OJ6 THR A 44 UNP Q8N2Q7 EXPRESSION TAG
SEQADV 5OJ6 GLY A 45 UNP Q8N2Q7 EXPRESSION TAG
SEQADV 5OJ6 A UNP Q8N2Q7 GLY 278 DELETION
SEQADV 5OJ6 A UNP Q8N2Q7 ASN 279 DELETION
SEQADV 5OJ6 A UNP Q8N2Q7 ARG 280 DELETION
SEQADV 5OJ6 A UNP Q8N2Q7 TRP 281 DELETION
SEQADV 5OJ6 A UNP Q8N2Q7 SER 282 DELETION
SEQADV 5OJ6 A UNP Q8N2Q7 ASN 283 DELETION
SEQADV 5OJ6 A UNP Q8N2Q7 SER 284 DELETION
SEQADV 5OJ6 A UNP Q8N2Q7 THR 285 DELETION
SEQADV 5OJ6 A UNP Q8N2Q7 LYS 286 DELETION
SEQADV 5OJ6 ARG A 636 UNP Q8N2Q7 EXPRESSION TAG
SEQADV 5OJ6 THR A 637 UNP Q8N2Q7 EXPRESSION TAG
SEQADV 5OJ6 LYS A 638 UNP Q8N2Q7 EXPRESSION TAG
SEQADV 5OJ6 HIS A 639 UNP Q8N2Q7 EXPRESSION TAG
SEQADV 5OJ6 HIS A 640 UNP Q8N2Q7 EXPRESSION TAG
SEQADV 5OJ6 HIS A 641 UNP Q8N2Q7 EXPRESSION TAG
SEQADV 5OJ6 HIS A 642 UNP Q8N2Q7 EXPRESSION TAG
SEQADV 5OJ6 HIS A 643 UNP Q8N2Q7 EXPRESSION TAG
SEQADV 5OJ6 HIS A 644 UNP Q8N2Q7 EXPRESSION TAG
SEQADV 5OJ6 LYS B 120 UNP Q0WYX8 ARG 120 ENGINEERED MUTATION
SEQADV 5OJ6 GLY B 920 UNP Q0WYX8 EXPRESSION TAG
SEQADV 5OJ6 THR B 921 UNP Q0WYX8 EXPRESSION TAG
SEQADV 5OJ6 LYS B 922 UNP Q0WYX8 EXPRESSION TAG
SEQADV 5OJ6 HIS B 923 UNP Q0WYX8 EXPRESSION TAG
SEQADV 5OJ6 HIS B 924 UNP Q0WYX8 EXPRESSION TAG
SEQADV 5OJ6 HIS B 925 UNP Q0WYX8 EXPRESSION TAG
SEQADV 5OJ6 HIS B 926 UNP Q0WYX8 EXPRESSION TAG
SEQADV 5OJ6 HIS B 927 UNP Q0WYX8 EXPRESSION TAG
SEQADV 5OJ6 HIS B 928 UNP Q0WYX8 EXPRESSION TAG
SEQRES 1 A 575 THR GLY GLN LYS LEU ASP ASP VAL ASP PRO LEU VAL ALA
SEQRES 2 A 575 THR ASN PHE GLY LYS ILE ARG GLY ILE LYS LYS GLU LEU
SEQRES 3 A 575 ASN ASN GLU ILE LEU GLY PRO VAL ILE GLN PHE LEU GLY
SEQRES 4 A 575 VAL PRO TYR ALA ALA PRO PRO THR GLY GLU ARG ARG PHE
SEQRES 5 A 575 GLN PRO PRO GLU PRO PRO SER PRO TRP SER ASP ILE ARG
SEQRES 6 A 575 ASN ALA THR GLN PHE ALA PRO VAL CYS PRO GLN ASN ILE
SEQRES 7 A 575 ILE ASP GLY ARG LEU PRO GLU VAL MET LEU PRO VAL TRP
SEQRES 8 A 575 PHE THR ASN ASN LEU ASP VAL VAL SER SER TYR VAL GLN
SEQRES 9 A 575 ASP GLN SER GLU ASP CYS LEU TYR LEU ASN ILE TYR VAL
SEQRES 10 A 575 PRO THR GLU ASP ASP ILE ARG ASP SER GLY GLY PRO LYS
SEQRES 11 A 575 PRO VAL MET VAL TYR ILE HIS GLY GLY SER TYR MET GLU
SEQRES 12 A 575 GLY THR GLY ASN LEU TYR ASP GLY SER VAL LEU ALA SER
SEQRES 13 A 575 TYR GLY ASN VAL ILE VAL ILE THR VAL ASN TYR ARG LEU
SEQRES 14 A 575 GLY VAL LEU GLY PHE LEU SER THR GLY ASP GLN ALA ALA
SEQRES 15 A 575 LYS GLY ASN TYR GLY LEU LEU ASP LEU ILE GLN ALA LEU
SEQRES 16 A 575 ARG TRP THR SER GLU ASN ILE GLY PHE PHE GLY GLY ASP
SEQRES 17 A 575 PRO LEU ARG ILE THR VAL PHE GLY SER GLY ALA GLY GLY
SEQRES 18 A 575 SER CYS VAL ASN LEU LEU THR LEU SER HIS TYR SER GLU
SEQRES 19 A 575 GLY LEU PHE GLN ARG ALA ILE ALA GLN SER GLY THR ALA
SEQRES 20 A 575 LEU SER SER TRP ALA VAL SER PHE GLN PRO ALA LYS TYR
SEQRES 21 A 575 ALA ARG MET LEU ALA THR LYS VAL GLY CYS ASN VAL SER
SEQRES 22 A 575 ASP THR VAL GLU LEU VAL GLU CYS LEU GLN LYS LYS PRO
SEQRES 23 A 575 TYR LYS GLU LEU VAL ASP GLN ASP ILE GLN PRO ALA ARG
SEQRES 24 A 575 TYR HIS ILE ALA PHE GLY PRO VAL ILE ASP GLY ASP VAL
SEQRES 25 A 575 ILE PRO ASP ASP PRO GLN ILE LEU MET GLU GLN GLY GLU
SEQRES 26 A 575 PHE LEU ASN TYR ASP ILE MET LEU GLY VAL ASN GLN GLY
SEQRES 27 A 575 GLU GLY LEU LYS PHE VAL GLU ASN ILE VAL ASP SER ASP
SEQRES 28 A 575 ASP GLY ILE SER ALA SER ASP PHE ASP PHE ALA VAL SER
SEQRES 29 A 575 ASN PHE VAL ASP ASN LEU TYR GLY TYR PRO GLU GLY LYS
SEQRES 30 A 575 ASP VAL LEU ARG GLU THR ILE LYS PHE MET TYR THR ASP
SEQRES 31 A 575 TRP ALA ASP ARG HIS ASN PRO GLU THR ARG ARG LYS THR
SEQRES 32 A 575 LEU LEU ALA LEU PHE THR ASP HIS GLN TRP VAL ALA PRO
SEQRES 33 A 575 ALA VAL ALA THR ALA ASP LEU HIS SER ASN PHE GLY SER
SEQRES 34 A 575 PRO THR TYR PHE TYR ALA PHE TYR HIS HIS CYS GLN THR
SEQRES 35 A 575 ASP GLN VAL PRO ALA TRP ALA ASP ALA ALA HIS GLY ASP
SEQRES 36 A 575 GLU VAL PRO TYR VAL LEU GLY ILE PRO MET ILE GLY PRO
SEQRES 37 A 575 THR GLU LEU PHE PRO CYS ASN PHE SER LYS ASN ASP VAL
SEQRES 38 A 575 MET LEU SER ALA VAL VAL MET THR TYR TRP THR ASN PHE
SEQRES 39 A 575 ALA LYS THR GLY ASP PRO ASN GLN PRO VAL PRO GLN ASP
SEQRES 40 A 575 THR LYS PHE ILE HIS THR LYS PRO ASN ARG PHE GLU GLU
SEQRES 41 A 575 VAL ALA TRP THR ARG TYR SER GLN LYS ASP GLN LEU TYR
SEQRES 42 A 575 LEU HIS ILE GLY LEU LYS PRO ARG VAL LYS GLU HIS TYR
SEQRES 43 A 575 ARG ALA ASN LYS VAL ASN LEU TRP LEU GLU LEU VAL PRO
SEQRES 44 A 575 HIS LEU HIS ASN LEU ASN ASP ARG THR LYS HIS HIS HIS
SEQRES 45 A 575 HIS HIS HIS
SEQRES 1 B 910 GLN GLY VAL TYR ALA PRO ALA GLN ALA GLN ILE ILE HIS
SEQRES 2 B 910 ALA GLY GLN ALA CYS VAL VAL LYS GLU ASP ASN ILE SER
SEQRES 3 B 910 GLU ARG VAL TYR THR ILE ARG GLU GLY ASP THR LEU VAL
SEQRES 4 B 910 LEU GLN CYS LEU VAL THR GLY HIS PRO ARG PRO GLN VAL
SEQRES 5 B 910 ARG TRP THR LYS THR ALA GLY SER ALA SER ASP LYS PHE
SEQRES 6 B 910 GLN GLU THR SER VAL LEU ASN GLU THR LEU ARG ILE GLU
SEQRES 7 B 910 LYS ILE GLN ARG LEU GLN GLY GLY ARG TYR TYR CYS LYS
SEQRES 8 B 910 ALA GLU ASN GLY VAL GLY VAL PRO ALA ILE LYS SER ILE
SEQRES 9 B 910 ARG VAL ASP VAL GLN TYR LEU ASP GLU PRO VAL LEU THR
SEQRES 10 B 910 VAL HIS GLN THR ILE SER ASP VAL ARG GLY SER PHE TYR
SEQRES 11 B 910 GLN GLU LYS THR VAL PHE LEU ARG CYS THR VAL ASN SER
SEQRES 12 B 910 ASN PRO PRO ALA ARG PHE ILE TRP LYS ARG GLY ALA GLU
SEQRES 13 B 910 THR LEU SER HIS SER GLN ASP ASN GLY VAL ASP ILE TYR
SEQRES 14 B 910 GLU PRO LEU TYR THR GLN GLY GLU THR LYS VAL LEU LYS
SEQRES 15 B 910 LEU LYS ASN LEU ARG PRO GLN ASP TYR ALA SER TYR THR
SEQRES 16 B 910 CYS GLN VAL SER VAL ARG ASN VAL CYS SER ILE PRO ASP
SEQRES 17 B 910 LYS SER ILE THR PHE GLN LEU THR ASN THR THR ALA PRO
SEQRES 18 B 910 PRO ALA LEU LYS LEU SER VAL ASN GLU THR LEU VAL VAL
SEQRES 19 B 910 ASN PRO GLY ASP ASN VAL THR MET GLN CYS SER LEU THR
SEQRES 20 B 910 GLY GLY ASP PRO GLN PRO GLU VAL LEU TRP SER HIS SER
SEQRES 21 B 910 PRO GLY PRO LEU PRO PRO ASN SER LEU VAL GLN GLY GLY
SEQRES 22 B 910 ASN LEU THR ILE TRP ARG ILE ARG VAL GLU ASP SER GLY
SEQRES 23 B 910 TYR TYR ASN CYS THR ALA ILE ASN ASN VAL GLY ASN PRO
SEQRES 24 B 910 ALA LYS LYS THR VAL ASN LEU LEU VAL ARG SER MET LYS
SEQRES 25 B 910 ASN ALA THR PHE GLN ILE THR PRO ASP VAL ILE LYS GLU
SEQRES 26 B 910 SER GLU THR ILE GLN LEU GLY GLN ASP LEU LYS LEU SER
SEQRES 27 B 910 CYS HIS VAL ASP ALA VAL PRO GLN GLU LYS VAL VAL TYR
SEQRES 28 B 910 SER TRP TYR LYS ASN GLY LYS PRO ALA ARG PHE SER ASP
SEQRES 29 B 910 ARG LEU LEU ILE THR ARG ASN ASP PRO GLU LEU PRO PRO
SEQRES 30 B 910 VAL THR CYS SER LEU GLU ILE ILE ASP LEU ARG PHE SER
SEQRES 31 B 910 ASP TYR GLY THR TYR LEU CYS VAL ALA THR PHE GLN GLY
SEQRES 32 B 910 ALA PRO ILE PRO ASP LEU SER VAL GLU VAL ASN ILE SER
SEQRES 33 B 910 SER GLU THR VAL PRO PRO THR ILE SER VAL PRO LYS GLY
SEQRES 34 B 910 GLN SER THR ILE THR VAL ARG GLU GLY SER ARG ALA GLU
SEQRES 35 B 910 LEU GLN CYS GLU VAL ARG GLY LYS PRO LYS PRO PRO ILE
SEQRES 36 B 910 ILE TRP SER ARG VAL ASP LYS GLU THR PRO MET PRO SER
SEQRES 37 B 910 GLY THR MET THR VAL GLU THR TYR ASP GLY LYS LEU ARG
SEQRES 38 B 910 LEU GLU SER VAL SER ARG ASP MET SER GLY THR TYR LYS
SEQRES 39 B 910 CYS GLN THR ALA ARG TYR ASN GLY PHE ASN ILE ARG PRO
SEQRES 40 B 910 ARG GLU ALA LEU VAL GLN LEU ASN VAL GLN PHE PRO PRO
SEQRES 41 B 910 VAL VAL GLU PRO ALA PHE GLN ASP VAL ARG GLN GLY MET
SEQRES 42 B 910 GLY ARG SER VAL THR LEU ARG CYS THR MET LEU LYS GLY
SEQRES 43 B 910 SER PRO MET LYS VAL ALA THR SER VAL TRP ARG PHE ASN
SEQRES 44 B 910 GLY THR LEU LEU ALA GLN PRO PRO ALA GLU GLN GLN ASP
SEQRES 45 B 910 TYR SER GLU LEU LYS VAL ASP SER VAL SER ARG GLU THR
SEQRES 46 B 910 SER GLY SER TYR GLU CYS SER ILE SER ASN ASP VAL GLY
SEQRES 47 B 910 VAL SER ALA CYS LEU PHE GLN VAL SER ALA LYS ALA TYR
SEQRES 48 B 910 SER PRO GLU PHE TYR TYR ASP THR PRO ASN PRO THR LEU
SEQRES 49 B 910 SER GLN LYS GLN SER LYS ASN TYR SER TYR ILE LEU GLN
SEQRES 50 B 910 TRP THR GLN LYS GLU PRO ASP ALA VAL ASP PRO ILE LEU
SEQRES 51 B 910 LYS TYR ARG LEU GLU VAL ARG GLN LEU ALA GLN ARG ASN
SEQRES 52 B 910 THR ILE GLN THR PHE ILE PRO VAL GLN LYS MET GLU LYS
SEQRES 53 B 910 GLY LEU LEU LEU GLU HIS ILE LEU PRO ASN LEU LYS VAL
SEQRES 54 B 910 PRO GLN SER TYR GLU VAL ARG LEU THR PRO ILE THR SER
SEQRES 55 B 910 PHE GLY ALA GLY ASP MET ALA ALA ARG ILE ILE ARG TYR
SEQRES 56 B 910 MET GLU PRO ILE ASN TYR PRO SER PRO THR ASP ASN THR
SEQRES 57 B 910 CYS ARG PHE GLU ASP GLU LYS ILE CYS GLY PHE VAL GLN
SEQRES 58 B 910 ASP LYS MET ASP ASN PHE ASP TRP THR ARG GLN ASN ALA
SEQRES 59 B 910 LEU THR GLN ASN PRO LYS ARG THR VAL ASN THR GLY PRO
SEQRES 60 B 910 PRO THR ASP ILE SER GLY THR PRO GLU GLY TYR TYR MET
SEQRES 61 B 910 PHE ILE GLU ALA SER ARG PRO ARG VAL THR GLY ASP LYS
SEQRES 62 B 910 ALA ARG LEU ILE SER PRO LEU TYR ASN ILE THR ALA LYS
SEQRES 63 B 910 TYR TYR CYS VAL SER PHE TYR TYR HIS MET TYR GLY LYS
SEQRES 64 B 910 HIS ILE GLY SER LEU ASN LEU LEU VAL ARG VAL ARG ASN
SEQRES 65 B 910 LYS ARG ALA ILE ASP THR GLN VAL TRP SER LEU SER GLY
SEQRES 66 B 910 ASN ARG GLY ASN MET TRP GLN GLN ALA HIS VAL PRO ILE
SEQRES 67 B 910 ASN PRO PRO GLY PRO PHE GLN ILE ILE PHE GLU GLY VAL
SEQRES 68 B 910 ARG GLY THR SER TYR GLU GLY ASP ILE ALA ILE ASP ASP
SEQRES 69 B 910 VAL THR LEU LYS LYS GLY ASP CYS PRO ARG LYS PRO ILE
SEQRES 70 B 910 GLY PRO ASN LYS GLY THR LYS HIS HIS HIS HIS HIS HIS
HET NAG B1001 14
HET NAG B1002 14
HET NAG B1003 14
HET NAG B1004 14
HET BMA B1005 11
HET NAG B1006 14
HET NAG B1007 14
HET NAG B1008 14
HET NAG B1009 14
HET NAG B1010 14
HET NAG B1011 14
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM BMA BETA-D-MANNOSE
FORMUL 3 NAG 10(C8 H15 N O6)
FORMUL 5 BMA C6 H12 O6
HELIX 1 AA1 THR A 90 ARG A 94 5 5
HELIX 2 AA2 PRO A 132 ASN A 137 1 6
HELIX 3 AA3 ASN A 138 VAL A 146 1 9
HELIX 4 AA4 THR A 205 TYR A 209 5 5
HELIX 5 AA5 GLY A 211 ASN A 219 1 9
HELIX 6 AA6 LEU A 229 LEU A 235 1 7
HELIX 7 AA7 ASN A 245 ILE A 262 1 18
HELIX 8 AA8 GLY A 263 PHE A 265 5 3
HELIX 9 AA9 GLY A 278 LEU A 289 1 12
HELIX 10 AB1 SER A 290 GLU A 294 5 5
HELIX 11 AB2 GLN A 325 GLY A 338 1 14
HELIX 12 AB3 ASP A 343 GLN A 352 1 10
HELIX 13 AB4 PRO A 355 ASP A 361 1 7
HELIX 14 AB5 ASP A 385 GLN A 392 1 8
HELIX 15 AB6 GLY A 409 ASN A 415 1 7
HELIX 16 AB7 SER A 424 TYR A 440 1 17
HELIX 17 AB8 GLY A 445 TYR A 457 1 13
HELIX 18 AB9 ASN A 465 TRP A 482 1 18
HELIX 19 AC1 TRP A 482 PHE A 496 1 15
HELIX 20 AC2 GLU A 525 LEU A 530 1 6
HELIX 21 AC3 GLY A 531 GLY A 536 5 6
HELIX 22 AC4 SER A 546 GLY A 567 1 22
HELIX 23 AC5 ARG A 616 GLU A 625 1 10
HELIX 24 AC6 GLU A 625 LEU A 630 1 6
HELIX 25 AC7 ARG B 205 TYR B 209 5 5
HELIX 26 AC8 ASN B 220 ILE B 224 5 5
HELIX 27 AC9 ARG B 299 SER B 303 5 5
HELIX 28 AD1 PRO B 363 GLU B 365 5 3
HELIX 29 AD2 ARG B 406 TYR B 410 5 5
HELIX 30 AD3 SER B 504 SER B 508 5 5
HELIX 31 AD4 GLU B 660 VAL B 664 5 5
SHEET 1 AA1 3 LEU A 54 THR A 57 0
SHEET 2 AA1 3 GLY A 60 ARG A 63 -1 O GLY A 60 N THR A 57
SHEET 3 AA1 3 ILE A 107 ASN A 109 1 O ARG A 108 N ARG A 63
SHEET 1 AA211 ILE A 65 LYS A 67 0
SHEET 2 AA211 VAL A 77 PRO A 84 -1 O VAL A 77 N LYS A 67
SHEET 3 AA211 TYR A 155 PRO A 161 -1 O VAL A 160 N ILE A 78
SHEET 4 AA211 ILE A 221 VAL A 225 -1 O VAL A 222 N TYR A 159
SHEET 5 AA211 LYS A 190 TYR A 195 1 N MET A 193 O ILE A 221
SHEET 6 AA211 GLY A 267 SER A 277 1 O THR A 273 N VAL A 192
SHEET 7 AA211 ARG A 308 GLN A 312 1 O ILE A 310 N VAL A 274
SHEET 8 AA211 ASP A 399 ASN A 405 1 O MET A 401 N ALA A 311
SHEET 9 AA211 THR A 500 PHE A 505 1 O PHE A 505 N VAL A 404
SHEET 10 AA211 LEU A 601 ILE A 605 1 O LEU A 603 N PHE A 502
SHEET 11 AA211 ARG A 610 GLU A 613 -1 O LYS A 612 N TYR A 602
SHEET 1 AA3 3 ALA B 23 GLY B 33 0
SHEET 2 AA3 3 LEU B 56 HIS B 65 -1 O GLN B 59 N ILE B 30
SHEET 3 AA3 3 THR B 92 ILE B 95 -1 O LEU B 93 N LEU B 58
SHEET 1 AA4 4 VAL B 47 ARG B 51 0
SHEET 2 AA4 4 ALA B 118 LEU B 129 1 O ARG B 123 N TYR B 48
SHEET 3 AA4 4 GLY B 104 GLU B 111 -1 N ALA B 110 O ALA B 118
SHEET 4 AA4 4 GLN B 69 THR B 75 -1 N GLN B 69 O GLU B 111
SHEET 1 AA5 3 VAL B 47 ARG B 51 0
SHEET 2 AA5 3 ALA B 118 LEU B 129 1 O ARG B 123 N TYR B 48
SHEET 3 AA5 3 SER B 161 ASN B 162 -1 O ASN B 162 N TYR B 128
SHEET 1 AA6 4 VAL B 133 HIS B 137 0
SHEET 2 AA6 4 VAL B 153 THR B 158 -1 O THR B 158 N VAL B 133
SHEET 3 AA6 4 THR B 196 LEU B 201 -1 O LYS B 197 N CYS B 157
SHEET 4 AA6 4 ASP B 185 TYR B 187 -1 N ASP B 185 O LYS B 200
SHEET 1 AA7 3 ARG B 166 LYS B 170 0
SHEET 2 AA7 3 SER B 211 SER B 217 -1 O SER B 217 N ARG B 166
SHEET 3 AA7 3 LYS B 227 GLN B 232 -1 O PHE B 231 N TYR B 212
SHEET 1 AA8 4 ALA B 238 LEU B 244 0
SHEET 2 AA8 4 VAL B 258 ASP B 268 -1 O ASP B 268 N ALA B 238
SHEET 3 AA8 4 ASN B 292 ILE B 295 -1 O LEU B 293 N MET B 260
SHEET 4 AA8 4 SER B 286 VAL B 288 -1 N LEU B 287 O THR B 294
SHEET 1 AA9 4 THR B 249 VAL B 252 0
SHEET 2 AA9 4 ALA B 318 VAL B 326 1 O LEU B 325 N LEU B 250
SHEET 3 AA9 4 GLY B 304 ILE B 311 -1 N CYS B 308 O LYS B 320
SHEET 4 AA9 4 GLU B 272 SER B 278 -1 N LEU B 274 O THR B 309
SHEET 1 AB1 5 LEU B 385 ARG B 388 0
SHEET 2 AB1 5 CYS B 398 ILE B 402 -1 O SER B 399 N ARG B 388
SHEET 3 AB1 5 LEU B 353 ALA B 361 -1 N LEU B 355 O LEU B 400
SHEET 4 AB1 5 MET B 329 THR B 337 -1 N LYS B 330 O ASP B 360
SHEET 5 AB1 5 GLY B 520 PHE B 521 1 O GLY B 520 N ILE B 336
SHEET 1 AB2 3 VAL B 367 LYS B 373 0
SHEET 2 AB2 3 THR B 412 PHE B 419 -1 O LEU B 414 N TYR B 372
SHEET 3 AB2 3 LEU B 427 ASN B 432 -1 O VAL B 431 N TYR B 413
SHEET 1 AB3 2 VAL B 438 SER B 443 0
SHEET 2 AB3 2 GLU B 464 LYS B 468 -1 O ARG B 466 N THR B 441
SHEET 1 AB4 5 THR B 450 ARG B 454 0
SHEET 2 AB4 5 GLU B 527 GLU B 541 1 O GLN B 535 N VAL B 453
SHEET 3 AB4 5 GLY B 509 THR B 515 -1 N GLY B 509 O LEU B 532
SHEET 4 AB4 5 ILE B 473 ARG B 477 -1 N SER B 476 O LYS B 512
SHEET 5 AB4 5 VAL B 491 THR B 493 -1 O THR B 493 N ILE B 473
SHEET 1 AB5 4 THR B 450 ARG B 454 0
SHEET 2 AB5 4 GLU B 527 GLU B 541 1 O GLN B 535 N VAL B 453
SHEET 3 AB5 4 VAL B 555 SER B 565 -1 O THR B 560 N GLU B 541
SHEET 4 AB5 4 TYR B 591 VAL B 596 -1 O LEU B 594 N LEU B 557
SHEET 1 AB6 2 ALA B 459 GLN B 462 0
SHEET 2 AB6 2 LYS B 497 LEU B 500 -1 O LEU B 500 N ALA B 459
SHEET 1 AB7 5 PHE B 544 ARG B 548 0
SHEET 2 AB7 5 VAL B 617 SER B 625 1 O GLN B 623 N VAL B 547
SHEET 3 AB7 5 GLY B 605 SER B 612 -1 N GLY B 605 O VAL B 624
SHEET 4 AB7 5 THR B 571 PHE B 576 -1 N VAL B 573 O SER B 610
SHEET 5 AB7 5 THR B 579 LEU B 580 -1 O THR B 579 N PHE B 576
SHEET 1 AB8 3 PRO B 631 PHE B 633 0
SHEET 2 AB8 3 ASN B 649 GLN B 658 -1 O THR B 657 N GLU B 632
SHEET 3 AB8 3 PRO B 640 LEU B 642 -1 N THR B 641 O SER B 651
SHEET 1 AB9 3 PRO B 631 PHE B 633 0
SHEET 2 AB9 3 ASN B 649 GLN B 658 -1 O THR B 657 N GLU B 632
SHEET 3 AB9 3 LEU B 698 LYS B 706 -1 O LEU B 698 N TRP B 656
SHEET 1 AC1 4 ILE B 683 PRO B 688 0
SHEET 2 AC1 4 LYS B 669 ARG B 675 -1 N TYR B 670 O ILE B 687
SHEET 3 AC1 4 SER B 710 THR B 719 -1 O THR B 716 N ARG B 671
SHEET 4 AC1 4 GLY B 722 ALA B 723 -1 O GLY B 722 N THR B 719
SHEET 1 AC2 4 ILE B 683 PRO B 688 0
SHEET 2 AC2 4 LYS B 669 ARG B 675 -1 N TYR B 670 O ILE B 687
SHEET 3 AC2 4 SER B 710 THR B 719 -1 O THR B 716 N ARG B 671
SHEET 4 AC2 4 ALA B 727 ARG B 732 -1 O ARG B 729 N VAL B 713
SSBOND 1 CYS A 117 CYS A 153 1555 1555 2.03
SSBOND 2 CYS A 339 CYS A 350 1555 1555 2.03
SSBOND 3 CYS A 509 CYS A 543 1555 1555 2.03
SSBOND 4 CYS B 36 CYS B 222 1555 1555 2.03
SSBOND 5 CYS B 60 CYS B 108 1555 1555 2.03
SSBOND 6 CYS B 157 CYS B 214 1555 1555 2.04
SSBOND 7 CYS B 262 CYS B 308 1555 1555 2.03
SSBOND 8 CYS B 357 CYS B 415 1555 1555 2.03
SSBOND 9 CYS B 463 CYS B 513 1555 1555 2.04
SSBOND 10 CYS B 559 CYS B 620 1555 1555 2.03
LINK ND2 ASN B 90 C1 NAG B1009 1555 1555 1.44
LINK ND2 ASN B 235 C1 NAG B1007 1555 1555 1.44
LINK ND2 ASN B 257 C1 NAG B1001 1555 1555 1.44
LINK ND2 ASN B 292 C1 NAG B1011 1555 1555 1.43
LINK ND2 ASN B 307 C1 NAG B1002 1555 1555 1.44
LINK ND2 ASN B 331 C1 NAG B1003 1555 1555 1.44
LINK ND2 ASN B 432 C1 NAG B1008 1555 1555 1.44
LINK ND2 ASN B 577 C1 NAG B1010 1555 1555 1.44
LINK ND2 ASN B 649 C1 NAG B1006 1555 1555 1.44
LINK O4 NAG B1003 C1 NAG B1004 1555 1555 1.44
LINK O4 NAG B1004 C1 BMA B1005 1555 1555 1.44
CISPEP 1 GLN A 571 PRO A 572 0 -0.61
CISPEP 2 HIS B 65 PRO B 66 0 -0.71
CISPEP 3 ASN B 162 PRO B 163 0 -1.96
CISPEP 4 ASP B 268 PRO B 269 0 0.51
CISPEP 5 SER B 278 PRO B 279 0 -0.50
CISPEP 6 PRO B 283 PRO B 284 0 -0.36
CISPEP 7 LYS B 468 PRO B 469 0 -2.83
CISPEP 8 GLU B 541 PRO B 542 0 1.88
CISPEP 9 SER B 565 PRO B 566 0 1.93
SITE 1 AC1 5 GLN A 147 LYS A 357 LEU B 89 ASN B 90
SITE 2 AC1 5 THR B 92
SITE 1 AC2 3 ASN B 235 LYS B 627 NAG B1010
SITE 1 AC3 5 ASN B 257 TRP B 296 SER B 643 SER B 651
SITE 2 AC3 5 NAG B1006
SITE 1 AC4 8 GLN B 261 LEU B 287 GLN B 289 ASN B 292
SITE 2 AC4 8 THR B 294 TRP B 296 HIS B 700 ILE B 701
SITE 1 AC5 4 SER B 276 HIS B 277 SER B 278 ASN B 307
SITE 1 AC6 6 ASN B 331 THR B 333 GLN B 335 HIS B 358
SITE 2 AC6 6 PRO B 394 TYR B 518
SITE 1 AC7 3 THR B 412 GLU B 430 ASN B 432
SITE 1 AC8 5 PHE B 576 ASN B 577 GLU B 602 SER B 604
SITE 2 AC8 5 NAG B1007
SITE 1 AC9 4 SER B 647 ASN B 649 LYS B 706 NAG B1001
CRYST1 109.420 184.140 96.470 90.00 90.00 90.00 P 21 21 2 4
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 0.009139 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005431 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010366 0.00000
TER 4279 LEU A 633
TER 9661 MET B 734
MASTER 602 0 11 31 79 0 14 6 9810 2 180 115
END |