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HEADER CELL ADHESION 23-JUN-20 7CEE
TITLE CRYSTAL STRUCTURE OF MOUSE 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: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: NLGN3;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: HEK293F
KEYWDS SYNAPSE ORGANIZATION, TRANS-SYNAPTIC COMPLEX, ESTERASE DOMAIN, CELL
KEYWDS 2 ADHESION
EXPDTA X-RAY DIFFRACTION
AUTHOR A.YAMAGATA,T.YOSHIDA,T.SHIROSHIMA,A.MAEDA,S.FUKAI
REVDAT 1 24-FEB-21 7CEE 0
JRNL AUTH T.YOSHIDA,A.YAMAGATA,A.IMAI,J.KIM,H.IZUMI,T.SHIROSHIMA,
JRNL AUTH 2 A.MAEDA,S.IWASAWA-OKAMOTO,K.AZECHI,F.OSAKA,T.SAITO,
JRNL AUTH 3 K.MAENAKA,T.SHIMADA,Y.FUKATA,M.FUKATA,Y.KOSHIDAKA,K.TAKAO,
JRNL AUTH 4 S.TANAKA,S.OKABE,K.TABUCHI,T.UEMURA,M.MISHINA,H.MORI,S.FUKAI
JRNL TITL NON-CANONICAL INTERACTION BETWEEN NEUROLIGIN 3 AND PROTEIN
JRNL TITL 2 TYROSINE PHOSPHATASE DELTA UNDERLIES AUTISM-RELATED
JRNL TITL 3 PHENOTYPES
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.76 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
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) : 2.76
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.66
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.430
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.3
REMARK 3 NUMBER OF REFLECTIONS : 50376
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.219
REMARK 3 R VALUE (WORKING SET) : 0.218
REMARK 3 FREE R VALUE : 0.251
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.960
REMARK 3 FREE R VALUE TEST SET COUNT : 2501
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 49.6640 - 7.2337 1.00 2899 162 0.1837 0.2036
REMARK 3 2 7.2337 - 5.7443 1.00 2762 172 0.1888 0.1839
REMARK 3 3 5.7443 - 5.0190 1.00 2756 133 0.1699 0.2175
REMARK 3 4 5.0190 - 4.5604 1.00 2735 134 0.1609 0.1931
REMARK 3 5 4.5604 - 4.2338 1.00 2708 150 0.1664 0.2134
REMARK 3 6 4.2338 - 3.9843 1.00 2685 153 0.1823 0.2219
REMARK 3 7 3.9843 - 3.7848 0.99 2652 170 0.2042 0.2681
REMARK 3 8 3.7848 - 3.6201 0.99 2673 134 0.2167 0.2885
REMARK 3 9 3.6201 - 3.4808 0.99 2691 111 0.2317 0.2596
REMARK 3 10 3.4808 - 3.3607 0.99 2699 118 0.2356 0.2565
REMARK 3 11 3.3607 - 3.2556 0.99 2685 110 0.2415 0.2999
REMARK 3 12 3.2556 - 3.1626 0.99 2650 122 0.2699 0.2902
REMARK 3 13 3.1626 - 3.0793 0.98 2620 145 0.2927 0.3242
REMARK 3 14 3.0793 - 3.0042 0.98 2612 142 0.3174 0.3608
REMARK 3 15 3.0042 - 2.9359 0.98 2621 145 0.3299 0.3900
REMARK 3 16 2.9359 - 2.8735 0.98 2581 132 0.3496 0.3882
REMARK 3 17 2.8735 - 2.8160 0.98 2645 151 0.3663 0.4044
REMARK 3 18 2.8160 - 2.7630 0.84 2201 117 0.3790 0.3877
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) : 0.420
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.760
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 55.71
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 70.86
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 8692
REMARK 3 ANGLE : 0.871 11878
REMARK 3 CHIRALITY : 0.045 1297
REMARK 3 PLANARITY : 0.004 1547
REMARK 3 DIHEDRAL : 13.792 3106
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): 41.5403 13.8112 -10.5651
REMARK 3 T TENSOR
REMARK 3 T11: 0.5600 T22: 0.5819
REMARK 3 T33: 0.5394 T12: 0.0115
REMARK 3 T13: -0.0480 T23: -0.0504
REMARK 3 L TENSOR
REMARK 3 L11: 1.5988 L22: 0.0812
REMARK 3 L33: 1.1163 L12: -0.0363
REMARK 3 L13: -1.2903 L23: 0.1352
REMARK 3 S TENSOR
REMARK 3 S11: 0.0287 S12: 0.1898 S13: 0.0452
REMARK 3 S21: -0.0630 S22: -0.0066 S23: 0.0001
REMARK 3 S31: -0.0314 S32: -0.0852 S33: -0.0001
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 1
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN A AND SEGID A
REMARK 3 SELECTION : CHAIN B AND SEGID B
REMARK 3 ATOM PAIRS NUMBER : 5038
REMARK 3 RMSD : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 7CEE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 24-JUN-20.
REMARK 100 THE DEPOSITION ID IS D_1300017476.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-JUN-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
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) : 1.0000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 S 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 50446
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.760
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 (%) : 99.1
REMARK 200 DATA REDUNDANCY : 7.700
REMARK 200 R MERGE (I) : 0.11100
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 4.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.76
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.81
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.7
REMARK 200 DATA REDUNDANCY IN SHELL : 4.80
REMARK 200 R MERGE FOR SHELL (I) : 0.39800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 3BIX
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.32
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.35
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15% PEG 3350, 0.2 M AMMONIUM CHLORIDE,
REMARK 280 0.1 M MES-NA, PH 6.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 32.92100
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 88.97500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 83.57100
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 88.97500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 32.92100
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 83.57100
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2570 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 40630 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -4.0 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 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 ALA A 36
REMARK 465 PRO A 37
REMARK 465 GLU A 148
REMARK 465 ASP A 149
REMARK 465 GLY A 150
REMARK 465 SER A 151
REMARK 465 GLY A 152
REMARK 465 ALA A 153
REMARK 465 LYS A 154
REMARK 465 LYS A 155
REMARK 465 GLN A 156
REMARK 465 GLY A 157
REMARK 465 GLU A 158
REMARK 465 ASP A 159
REMARK 465 LEU A 160
REMARK 465 ALA A 161
REMARK 465 ASP A 162
REMARK 465 ASN A 163
REMARK 465 ASP A 164
REMARK 465 GLY A 165
REMARK 465 ASP A 166
REMARK 465 GLU A 167
REMARK 465 ASP A 168
REMARK 465 GLU A 169
REMARK 465 ASP A 170
REMARK 465 ILE A 171
REMARK 465 ARG A 172
REMARK 465 ASP A 173
REMARK 465 THR A 555
REMARK 465 LYS A 556
REMARK 465 PHE A 557
REMARK 465 ILE A 558
REMARK 465 HIS A 559
REMARK 465 THR A 560
REMARK 465 LYS A 561
REMARK 465 ALA A 562
REMARK 465 ASN A 563
REMARK 465 ARG A 564
REMARK 465 PHE A 565
REMARK 465 GLU A 566
REMARK 465 GLU A 567
REMARK 465 LEU A 611
REMARK 465 HIS A 612
REMARK 465 ASP A 613
REMARK 465 MET A 614
REMARK 465 PHE A 615
REMARK 465 HIS A 616
REMARK 465 TYR A 617
REMARK 465 THR A 618
REMARK 465 SER A 619
REMARK 465 THR A 620
REMARK 465 THR A 621
REMARK 465 THR A 622
REMARK 465 LYS A 623
REMARK 465 VAL A 624
REMARK 465 PRO A 625
REMARK 465 PRO A 626
REMARK 465 PRO A 627
REMARK 465 ASP A 628
REMARK 465 THR A 629
REMARK 465 THR A 630
REMARK 465 HIS A 631
REMARK 465 SER A 632
REMARK 465 SER A 633
REMARK 465 HIS A 634
REMARK 465 ILE A 635
REMARK 465 THR A 636
REMARK 465 ARG A 637
REMARK 465 ARG A 638
REMARK 465 PRO A 639
REMARK 465 ASN A 640
REMARK 465 GLY A 641
REMARK 465 LYS A 642
REMARK 465 THR A 643
REMARK 465 TRP A 644
REMARK 465 SER A 645
REMARK 465 THR A 646
REMARK 465 LYS A 647
REMARK 465 ARG A 648
REMARK 465 PRO A 649
REMARK 465 ALA A 650
REMARK 465 ILE A 651
REMARK 465 SER A 652
REMARK 465 PRO A 653
REMARK 465 ALA A 654
REMARK 465 TYR A 655
REMARK 465 SER A 656
REMARK 465 ASN A 657
REMARK 465 GLU A 658
REMARK 465 ASN A 659
REMARK 465 ALA A 660
REMARK 465 PRO A 661
REMARK 465 GLY A 662
REMARK 465 SER A 663
REMARK 465 TRP A 664
REMARK 465 ASN A 665
REMARK 465 GLY A 666
REMARK 465 ASP A 667
REMARK 465 GLN A 668
REMARK 465 ASP A 669
REMARK 465 ALA A 670
REMARK 465 GLY A 671
REMARK 465 PRO A 672
REMARK 465 LEU A 673
REMARK 465 LEU A 674
REMARK 465 VAL A 675
REMARK 465 GLU A 676
REMARK 465 ASN A 677
REMARK 465 PRO A 678
REMARK 465 ARG A 679
REMARK 465 ASP A 680
REMARK 465 TYR A 681
REMARK 465 SER A 682
REMARK 465 THR A 683
REMARK 465 GLU A 684
REMARK 465 HIS A 685
REMARK 465 HIS A 686
REMARK 465 HIS A 687
REMARK 465 HIS A 688
REMARK 465 HIS A 689
REMARK 465 HIS A 690
REMARK 465 ALA B 36
REMARK 465 PRO B 37
REMARK 465 GLU B 148
REMARK 465 ASP B 149
REMARK 465 GLY B 150
REMARK 465 SER B 151
REMARK 465 GLY B 152
REMARK 465 ALA B 153
REMARK 465 LYS B 154
REMARK 465 LYS B 155
REMARK 465 GLN B 156
REMARK 465 GLY B 157
REMARK 465 GLU B 158
REMARK 465 ASP B 159
REMARK 465 LEU B 160
REMARK 465 ALA B 161
REMARK 465 ASP B 162
REMARK 465 ASN B 163
REMARK 465 ASP B 164
REMARK 465 GLY B 165
REMARK 465 ASP B 166
REMARK 465 GLU B 167
REMARK 465 ASP B 168
REMARK 465 GLU B 169
REMARK 465 ASP B 170
REMARK 465 ILE B 171
REMARK 465 ARG B 172
REMARK 465 ASP B 173
REMARK 465 SER B 174
REMARK 465 THR B 555
REMARK 465 LYS B 556
REMARK 465 PHE B 557
REMARK 465 ILE B 558
REMARK 465 HIS B 559
REMARK 465 THR B 560
REMARK 465 LYS B 561
REMARK 465 ALA B 562
REMARK 465 ASN B 563
REMARK 465 ARG B 564
REMARK 465 PHE B 565
REMARK 465 GLU B 566
REMARK 465 GLU B 567
REMARK 465 LEU B 611
REMARK 465 HIS B 612
REMARK 465 ASP B 613
REMARK 465 MET B 614
REMARK 465 PHE B 615
REMARK 465 HIS B 616
REMARK 465 TYR B 617
REMARK 465 THR B 618
REMARK 465 SER B 619
REMARK 465 THR B 620
REMARK 465 THR B 621
REMARK 465 THR B 622
REMARK 465 LYS B 623
REMARK 465 VAL B 624
REMARK 465 PRO B 625
REMARK 465 PRO B 626
REMARK 465 PRO B 627
REMARK 465 ASP B 628
REMARK 465 THR B 629
REMARK 465 THR B 630
REMARK 465 HIS B 631
REMARK 465 SER B 632
REMARK 465 SER B 633
REMARK 465 HIS B 634
REMARK 465 ILE B 635
REMARK 465 THR B 636
REMARK 465 ARG B 637
REMARK 465 ARG B 638
REMARK 465 PRO B 639
REMARK 465 ASN B 640
REMARK 465 GLY B 641
REMARK 465 LYS B 642
REMARK 465 THR B 643
REMARK 465 TRP B 644
REMARK 465 SER B 645
REMARK 465 THR B 646
REMARK 465 LYS B 647
REMARK 465 ARG B 648
REMARK 465 PRO B 649
REMARK 465 ALA B 650
REMARK 465 ILE B 651
REMARK 465 SER B 652
REMARK 465 PRO B 653
REMARK 465 ALA B 654
REMARK 465 TYR B 655
REMARK 465 SER B 656
REMARK 465 ASN B 657
REMARK 465 GLU B 658
REMARK 465 ASN B 659
REMARK 465 ALA B 660
REMARK 465 PRO B 661
REMARK 465 GLY B 662
REMARK 465 SER B 663
REMARK 465 TRP B 664
REMARK 465 ASN B 665
REMARK 465 GLY B 666
REMARK 465 ASP B 667
REMARK 465 GLN B 668
REMARK 465 ASP B 669
REMARK 465 ALA B 670
REMARK 465 GLY B 671
REMARK 465 PRO B 672
REMARK 465 LEU B 673
REMARK 465 LEU B 674
REMARK 465 VAL B 675
REMARK 465 GLU B 676
REMARK 465 ASN B 677
REMARK 465 PRO B 678
REMARK 465 ARG B 679
REMARK 465 ASP B 680
REMARK 465 TYR B 681
REMARK 465 SER B 682
REMARK 465 THR B 683
REMARK 465 GLU B 684
REMARK 465 HIS B 685
REMARK 465 HIS B 686
REMARK 465 HIS B 687
REMARK 465 HIS B 688
REMARK 465 HIS B 689
REMARK 465 HIS B 690
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 OD1 ASN B 95 OG1 THR B 97 2.13
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 187 16.94 -149.63
REMARK 500 TYR A 188 -8.34 78.01
REMARK 500 PHE A 221 11.38 -142.37
REMARK 500 ASP A 226 -153.37 -138.10
REMARK 500 ARG A 258 72.91 -112.77
REMARK 500 ASP A 358 -78.39 -114.83
REMARK 500 ASP A 440 65.29 -157.03
REMARK 500 TRP A 460 -59.03 -121.15
REMARK 500 PRO A 520 13.58 -68.66
REMARK 500 SER B 187 17.01 -150.17
REMARK 500 TYR B 188 -7.91 78.90
REMARK 500 PHE B 221 11.29 -142.98
REMARK 500 ASP B 226 -153.15 -138.75
REMARK 500 ARG B 258 72.84 -112.85
REMARK 500 ASP B 358 -78.11 -114.58
REMARK 500 ASP B 440 64.49 -156.96
REMARK 500 TRP B 460 -58.62 -121.33
REMARK 500 PRO B 520 14.36 -68.19
REMARK 500
REMARK 500 REMARK: NULL
DBREF 7CEE A 36 684 UNP Q8BYM5 NLGN3_MOUSE 36 684
DBREF 7CEE B 36 684 UNP Q8BYM5 NLGN3_MOUSE 36 684
SEQADV 7CEE HIS A 685 UNP Q8BYM5 EXPRESSION TAG
SEQADV 7CEE HIS A 686 UNP Q8BYM5 EXPRESSION TAG
SEQADV 7CEE HIS A 687 UNP Q8BYM5 EXPRESSION TAG
SEQADV 7CEE HIS A 688 UNP Q8BYM5 EXPRESSION TAG
SEQADV 7CEE HIS A 689 UNP Q8BYM5 EXPRESSION TAG
SEQADV 7CEE HIS A 690 UNP Q8BYM5 EXPRESSION TAG
SEQADV 7CEE HIS B 685 UNP Q8BYM5 EXPRESSION TAG
SEQADV 7CEE HIS B 686 UNP Q8BYM5 EXPRESSION TAG
SEQADV 7CEE HIS B 687 UNP Q8BYM5 EXPRESSION TAG
SEQADV 7CEE HIS B 688 UNP Q8BYM5 EXPRESSION TAG
SEQADV 7CEE HIS B 689 UNP Q8BYM5 EXPRESSION TAG
SEQADV 7CEE HIS B 690 UNP Q8BYM5 EXPRESSION TAG
SEQRES 1 A 655 ALA PRO ALA PRO THR VAL ASN THR HIS PHE GLY LYS LEU
SEQRES 2 A 655 ARG GLY ALA ARG VAL PRO LEU PRO SER GLU ILE LEU GLY
SEQRES 3 A 655 PRO VAL ASP GLN TYR LEU GLY VAL PRO TYR ALA ALA PRO
SEQRES 4 A 655 PRO ILE GLY GLU LYS ARG PHE LEU PRO PRO GLU PRO PRO
SEQRES 5 A 655 PRO SER TRP SER GLY ILE ARG ASN ALA THR HIS PHE PRO
SEQRES 6 A 655 PRO VAL CYS PRO GLN ASN ILE HIS THR ALA VAL PRO GLU
SEQRES 7 A 655 VAL MET LEU PRO VAL TRP PHE THR ALA ASN LEU ASP ILE
SEQRES 8 A 655 VAL ALA THR TYR ILE GLN GLU PRO ASN GLU ASP CYS LEU
SEQRES 9 A 655 TYR LEU ASN VAL TYR VAL PRO THR GLU ASP GLY SER GLY
SEQRES 10 A 655 ALA LYS LYS GLN GLY GLU ASP LEU ALA ASP ASN ASP GLY
SEQRES 11 A 655 ASP GLU ASP GLU ASP ILE ARG ASP SER GLY ALA LYS PRO
SEQRES 12 A 655 VAL MET VAL TYR ILE HIS GLY GLY SER TYR MET GLU GLY
SEQRES 13 A 655 THR GLY ASN MET ILE ASP GLY SER VAL LEU ALA SER TYR
SEQRES 14 A 655 GLY ASN VAL ILE VAL ILE THR LEU ASN TYR ARG VAL GLY
SEQRES 15 A 655 VAL LEU GLY PHE LEU SER THR GLY ASP GLN ALA ALA LYS
SEQRES 16 A 655 GLY ASN TYR GLY LEU LEU ASP GLN ILE GLN ALA LEU ARG
SEQRES 17 A 655 TRP VAL SER GLU ASN ILE ALA PHE PHE GLY GLY ASP PRO
SEQRES 18 A 655 ARG ARG ILE THR VAL PHE GLY SER GLY ILE GLY ALA SER
SEQRES 19 A 655 CYS VAL SER LEU LEU THR LEU SER HIS HIS SER GLU GLY
SEQRES 20 A 655 LEU PHE GLN ARG ALA ILE ILE GLN SER GLY SER ALA LEU
SEQRES 21 A 655 SER SER TRP ALA VAL ASN TYR GLN PRO VAL LYS TYR THR
SEQRES 22 A 655 SER LEU LEU ALA ASP LYS VAL GLY CYS ASN VAL LEU ASP
SEQRES 23 A 655 THR VAL ASP MET VAL ASP CYS LEU ARG GLN LYS SER ALA
SEQRES 24 A 655 LYS GLU LEU VAL GLU GLN ASP ILE GLN PRO ALA ARG TYR
SEQRES 25 A 655 HIS VAL ALA PHE GLY PRO VAL ILE ASP GLY ASP VAL ILE
SEQRES 26 A 655 PRO ASP ASP PRO GLU ILE LEU MET GLU GLN GLY GLU PHE
SEQRES 27 A 655 LEU ASN TYR ASP ILE MET LEU GLY VAL ASN GLN GLY GLU
SEQRES 28 A 655 GLY LEU LYS PHE VAL GLU GLY VAL VAL ASP PRO GLU ASP
SEQRES 29 A 655 GLY VAL SER GLY THR ASP PHE ASP TYR SER VAL SER ASN
SEQRES 30 A 655 PHE VAL ASP ASN LEU TYR GLY TYR PRO GLU GLY LYS ASP
SEQRES 31 A 655 THR LEU ARG GLU THR ILE LYS PHE MET TYR THR ASP TRP
SEQRES 32 A 655 ALA ASP ARG ASP ASN PRO GLU THR ARG ARG LYS THR LEU
SEQRES 33 A 655 VAL ALA LEU PHE THR ASP HIS GLN TRP VAL GLU PRO SER
SEQRES 34 A 655 VAL VAL THR ALA ASP LEU HIS ALA ARG TYR GLY SER PRO
SEQRES 35 A 655 THR TYR PHE TYR ALA PHE TYR HIS HIS CYS GLN SER LEU
SEQRES 36 A 655 MET LYS PRO ALA TRP SER ASP ALA ALA HIS GLY ASP GLU
SEQRES 37 A 655 VAL PRO TYR VAL PHE GLY VAL PRO MET VAL GLY PRO THR
SEQRES 38 A 655 ASP LEU PHE PRO CYS ASN PHE SER LYS ASN ASP VAL MET
SEQRES 39 A 655 LEU SER ALA VAL VAL MET THR TYR TRP THR ASN PHE ALA
SEQRES 40 A 655 LYS THR GLY ASP PRO ASN LYS PRO VAL PRO GLN ASP THR
SEQRES 41 A 655 LYS PHE ILE HIS THR LYS ALA ASN ARG PHE GLU GLU VAL
SEQRES 42 A 655 ALA TRP SER LYS TYR ASN PRO ARG ASP GLN LEU TYR LEU
SEQRES 43 A 655 HIS ILE GLY LEU LYS PRO ARG VAL ARG ASP HIS TYR ARG
SEQRES 44 A 655 ALA THR LYS VAL ALA PHE TRP LYS HIS LEU VAL PRO HIS
SEQRES 45 A 655 LEU TYR ASN LEU HIS ASP MET PHE HIS TYR THR SER THR
SEQRES 46 A 655 THR THR LYS VAL PRO PRO PRO ASP THR THR HIS SER SER
SEQRES 47 A 655 HIS ILE THR ARG ARG PRO ASN GLY LYS THR TRP SER THR
SEQRES 48 A 655 LYS ARG PRO ALA ILE SER PRO ALA TYR SER ASN GLU ASN
SEQRES 49 A 655 ALA PRO GLY SER TRP ASN GLY ASP GLN ASP ALA GLY PRO
SEQRES 50 A 655 LEU LEU VAL GLU ASN PRO ARG ASP TYR SER THR GLU HIS
SEQRES 51 A 655 HIS HIS HIS HIS HIS
SEQRES 1 B 655 ALA PRO ALA PRO THR VAL ASN THR HIS PHE GLY LYS LEU
SEQRES 2 B 655 ARG GLY ALA ARG VAL PRO LEU PRO SER GLU ILE LEU GLY
SEQRES 3 B 655 PRO VAL ASP GLN TYR LEU GLY VAL PRO TYR ALA ALA PRO
SEQRES 4 B 655 PRO ILE GLY GLU LYS ARG PHE LEU PRO PRO GLU PRO PRO
SEQRES 5 B 655 PRO SER TRP SER GLY ILE ARG ASN ALA THR HIS PHE PRO
SEQRES 6 B 655 PRO VAL CYS PRO GLN ASN ILE HIS THR ALA VAL PRO GLU
SEQRES 7 B 655 VAL MET LEU PRO VAL TRP PHE THR ALA ASN LEU ASP ILE
SEQRES 8 B 655 VAL ALA THR TYR ILE GLN GLU PRO ASN GLU ASP CYS LEU
SEQRES 9 B 655 TYR LEU ASN VAL TYR VAL PRO THR GLU ASP GLY SER GLY
SEQRES 10 B 655 ALA LYS LYS GLN GLY GLU ASP LEU ALA ASP ASN ASP GLY
SEQRES 11 B 655 ASP GLU ASP GLU ASP ILE ARG ASP SER GLY ALA LYS PRO
SEQRES 12 B 655 VAL MET VAL TYR ILE HIS GLY GLY SER TYR MET GLU GLY
SEQRES 13 B 655 THR GLY ASN MET ILE ASP GLY SER VAL LEU ALA SER TYR
SEQRES 14 B 655 GLY ASN VAL ILE VAL ILE THR LEU ASN TYR ARG VAL GLY
SEQRES 15 B 655 VAL LEU GLY PHE LEU SER THR GLY ASP GLN ALA ALA LYS
SEQRES 16 B 655 GLY ASN TYR GLY LEU LEU ASP GLN ILE GLN ALA LEU ARG
SEQRES 17 B 655 TRP VAL SER GLU ASN ILE ALA PHE PHE GLY GLY ASP PRO
SEQRES 18 B 655 ARG ARG ILE THR VAL PHE GLY SER GLY ILE GLY ALA SER
SEQRES 19 B 655 CYS VAL SER LEU LEU THR LEU SER HIS HIS SER GLU GLY
SEQRES 20 B 655 LEU PHE GLN ARG ALA ILE ILE GLN SER GLY SER ALA LEU
SEQRES 21 B 655 SER SER TRP ALA VAL ASN TYR GLN PRO VAL LYS TYR THR
SEQRES 22 B 655 SER LEU LEU ALA ASP LYS VAL GLY CYS ASN VAL LEU ASP
SEQRES 23 B 655 THR VAL ASP MET VAL ASP CYS LEU ARG GLN LYS SER ALA
SEQRES 24 B 655 LYS GLU LEU VAL GLU GLN ASP ILE GLN PRO ALA ARG TYR
SEQRES 25 B 655 HIS VAL ALA PHE GLY PRO VAL ILE ASP GLY ASP VAL ILE
SEQRES 26 B 655 PRO ASP ASP PRO GLU ILE LEU MET GLU GLN GLY GLU PHE
SEQRES 27 B 655 LEU ASN TYR ASP ILE MET LEU GLY VAL ASN GLN GLY GLU
SEQRES 28 B 655 GLY LEU LYS PHE VAL GLU GLY VAL VAL ASP PRO GLU ASP
SEQRES 29 B 655 GLY VAL SER GLY THR ASP PHE ASP TYR SER VAL SER ASN
SEQRES 30 B 655 PHE VAL ASP ASN LEU TYR GLY TYR PRO GLU GLY LYS ASP
SEQRES 31 B 655 THR LEU ARG GLU THR ILE LYS PHE MET TYR THR ASP TRP
SEQRES 32 B 655 ALA ASP ARG ASP ASN PRO GLU THR ARG ARG LYS THR LEU
SEQRES 33 B 655 VAL ALA LEU PHE THR ASP HIS GLN TRP VAL GLU PRO SER
SEQRES 34 B 655 VAL VAL THR ALA ASP LEU HIS ALA ARG TYR GLY SER PRO
SEQRES 35 B 655 THR TYR PHE TYR ALA PHE TYR HIS HIS CYS GLN SER LEU
SEQRES 36 B 655 MET LYS PRO ALA TRP SER ASP ALA ALA HIS GLY ASP GLU
SEQRES 37 B 655 VAL PRO TYR VAL PHE GLY VAL PRO MET VAL GLY PRO THR
SEQRES 38 B 655 ASP LEU PHE PRO CYS ASN PHE SER LYS ASN ASP VAL MET
SEQRES 39 B 655 LEU SER ALA VAL VAL MET THR TYR TRP THR ASN PHE ALA
SEQRES 40 B 655 LYS THR GLY ASP PRO ASN LYS PRO VAL PRO GLN ASP THR
SEQRES 41 B 655 LYS PHE ILE HIS THR LYS ALA ASN ARG PHE GLU GLU VAL
SEQRES 42 B 655 ALA TRP SER LYS TYR ASN PRO ARG ASP GLN LEU TYR LEU
SEQRES 43 B 655 HIS ILE GLY LEU LYS PRO ARG VAL ARG ASP HIS TYR ARG
SEQRES 44 B 655 ALA THR LYS VAL ALA PHE TRP LYS HIS LEU VAL PRO HIS
SEQRES 45 B 655 LEU TYR ASN LEU HIS ASP MET PHE HIS TYR THR SER THR
SEQRES 46 B 655 THR THR LYS VAL PRO PRO PRO ASP THR THR HIS SER SER
SEQRES 47 B 655 HIS ILE THR ARG ARG PRO ASN GLY LYS THR TRP SER THR
SEQRES 48 B 655 LYS ARG PRO ALA ILE SER PRO ALA TYR SER ASN GLU ASN
SEQRES 49 B 655 ALA PRO GLY SER TRP ASN GLY ASP GLN ASP ALA GLY PRO
SEQRES 50 B 655 LEU LEU VAL GLU ASN PRO ARG ASP TYR SER THR GLU HIS
SEQRES 51 B 655 HIS HIS HIS HIS HIS
HET NAG A1001 14
HET NAG A1002 14
HET NAG B1001 14
HET NAG B1002 14
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
FORMUL 3 NAG 4(C8 H15 N O6)
FORMUL 7 HOH *59(H2 O)
HELIX 1 AA1 ILE A 76 ARG A 80 5 5
HELIX 2 AA2 PRO A 117 ALA A 122 1 6
HELIX 3 AA3 ASN A 123 GLN A 132 1 10
HELIX 4 AA4 THR A 192 ILE A 196 5 5
HELIX 5 AA5 GLY A 198 ASN A 206 1 9
HELIX 6 AA6 VAL A 216 LEU A 222 1 7
HELIX 7 AA7 ASN A 232 ILE A 249 1 18
HELIX 8 AA8 ALA A 250 PHE A 252 5 3
HELIX 9 AA9 GLY A 265 LEU A 276 1 12
HELIX 10 AB1 GLN A 303 VAL A 315 1 13
HELIX 11 AB2 ASP A 321 LYS A 332 1 12
HELIX 12 AB3 SER A 333 GLN A 340 1 8
HELIX 13 AB4 ASP A 363 GLY A 371 1 9
HELIX 14 AB5 GLU A 372 TYR A 376 5 5
HELIX 15 AB6 GLY A 387 VAL A 395 5 9
HELIX 16 AB7 SER A 402 GLY A 419 1 18
HELIX 17 AB8 GLY A 423 TYR A 435 1 13
HELIX 18 AB9 ASN A 443 TRP A 460 1 18
HELIX 19 AC1 TRP A 460 ALA A 472 1 13
HELIX 20 AC2 GLU A 503 PHE A 508 1 6
HELIX 21 AC3 GLY A 509 VAL A 513 5 5
HELIX 22 AC4 SER A 524 GLY A 545 1 22
HELIX 23 AC5 ARG A 594 HIS A 603 1 10
HELIX 24 AC6 HIS A 603 TYR A 609 1 7
HELIX 25 AC7 ILE B 76 ARG B 80 5 5
HELIX 26 AC8 PRO B 117 ALA B 122 1 6
HELIX 27 AC9 ASN B 123 GLN B 132 1 10
HELIX 28 AD1 THR B 192 ILE B 196 5 5
HELIX 29 AD2 GLY B 198 ASN B 206 1 9
HELIX 30 AD3 VAL B 216 LEU B 222 1 7
HELIX 31 AD4 ASN B 232 ILE B 249 1 18
HELIX 32 AD5 ALA B 250 PHE B 252 5 3
HELIX 33 AD6 GLY B 265 LEU B 276 1 12
HELIX 34 AD7 GLN B 303 VAL B 315 1 13
HELIX 35 AD8 ASP B 321 LYS B 332 1 12
HELIX 36 AD9 SER B 333 GLN B 340 1 8
HELIX 37 AE1 ASP B 363 GLY B 371 1 9
HELIX 38 AE2 GLU B 372 TYR B 376 5 5
HELIX 39 AE3 GLY B 387 GLU B 392 1 6
HELIX 40 AE4 GLY B 393 VAL B 395 5 3
HELIX 41 AE5 SER B 402 GLY B 419 1 18
HELIX 42 AE6 GLY B 423 TYR B 435 1 13
HELIX 43 AE7 ASN B 443 TRP B 460 1 18
HELIX 44 AE8 TRP B 460 ALA B 472 1 13
HELIX 45 AE9 GLU B 503 PHE B 508 1 6
HELIX 46 AF1 GLY B 509 VAL B 513 5 5
HELIX 47 AF2 SER B 524 GLY B 545 1 22
HELIX 48 AF3 ARG B 594 HIS B 603 1 10
HELIX 49 AF4 HIS B 603 TYR B 609 1 7
SHEET 1 AA1 3 THR A 40 THR A 43 0
SHEET 2 AA1 3 GLY A 46 ARG A 49 -1 O LEU A 48 N VAL A 41
SHEET 3 AA1 3 ILE A 93 ASN A 95 1 O ARG A 94 N ARG A 49
SHEET 1 AA211 ALA A 51 VAL A 53 0
SHEET 2 AA211 VAL A 63 PRO A 70 -1 O GLN A 65 N ALA A 51
SHEET 3 AA211 TYR A 140 PRO A 146 -1 O VAL A 145 N ASP A 64
SHEET 4 AA211 ILE A 208 LEU A 212 -1 O THR A 211 N ASN A 142
SHEET 5 AA211 LYS A 177 ILE A 183 1 N MET A 180 O ILE A 208
SHEET 6 AA211 GLY A 254 SER A 264 1 O THR A 260 N VAL A 181
SHEET 7 AA211 ARG A 286 GLN A 290 1 O ARG A 286 N VAL A 261
SHEET 8 AA211 ASP A 377 ASN A 383 1 O MET A 379 N ILE A 289
SHEET 9 AA211 THR A 478 PHE A 483 1 O PHE A 483 N VAL A 382
SHEET 10 AA211 LEU A 579 ILE A 583 1 O LEU A 581 N PHE A 480
SHEET 11 AA211 ARG A 588 ASP A 591 -1 O ARG A 590 N TYR A 580
SHEET 1 AA3 3 THR B 40 THR B 43 0
SHEET 2 AA3 3 GLY B 46 ARG B 49 -1 O LEU B 48 N VAL B 41
SHEET 3 AA3 3 ARG B 94 ASN B 95 1 O ARG B 94 N ARG B 49
SHEET 1 AA411 ALA B 51 VAL B 53 0
SHEET 2 AA411 VAL B 63 PRO B 70 -1 O GLN B 65 N ALA B 51
SHEET 3 AA411 TYR B 140 PRO B 146 -1 O VAL B 145 N ASP B 64
SHEET 4 AA411 ILE B 208 LEU B 212 -1 O THR B 211 N ASN B 142
SHEET 5 AA411 LYS B 177 ILE B 183 1 N MET B 180 O ILE B 208
SHEET 6 AA411 GLY B 254 SER B 264 1 O THR B 260 N VAL B 181
SHEET 7 AA411 ARG B 286 GLN B 290 1 O ARG B 286 N VAL B 261
SHEET 8 AA411 ASP B 377 ASN B 383 1 O MET B 379 N ILE B 289
SHEET 9 AA411 THR B 478 PHE B 483 1 O PHE B 483 N VAL B 382
SHEET 10 AA411 LEU B 579 ILE B 583 1 O LEU B 581 N PHE B 480
SHEET 11 AA411 ARG B 588 ASP B 591 -1 O ARG B 588 N HIS B 582
SSBOND 1 CYS A 103 CYS A 138 1555 1555 2.03
SSBOND 2 CYS A 317 CYS A 328 1555 1555 2.03
SSBOND 3 CYS A 487 CYS A 521 1555 1555 2.03
SSBOND 4 CYS B 103 CYS B 138 1555 1555 2.03
SSBOND 5 CYS B 317 CYS B 328 1555 1555 2.03
SSBOND 6 CYS B 487 CYS B 521 1555 1555 2.03
LINK ND2 ASN A 95 C1 NAG A1001 1555 1555 1.44
LINK ND2 ASN A 522 C1 NAG A1002 1555 1555 1.45
LINK ND2 ASN B 95 C1 NAG B1001 1555 1555 1.44
LINK ND2 ASN B 522 C1 NAG B1002 1555 1555 1.45
CISPEP 1 LYS A 549 PRO A 550 0 2.96
CISPEP 2 LYS B 549 PRO B 550 0 2.98
CRYST1 65.842 167.142 177.950 90.00 90.00 90.00 P 21 21 21 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 0.015188 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005983 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005620 0.00000
TER 4191 ASN A 610
TER 8376 ASN B 610
MASTER 526 0 4 49 28 0 0 6 8489 2 72 102
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