HEADER LIPID BINDING PROTEIN 30-NOV-18 6N8P
TITLE CRYSTAL STRUCTURE OF THE HUMAN CELL POLARITY PROTEIN LETHAL GIANT
TITLE 2 LARVAE 2 (LGL2). UNPHOSPHORYLATED, CRYSTAL FORM 1.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LETHAL(2) GIANT LARVAE PROTEIN HOMOLOG 2;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: HGL;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: LLGL2;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: SF9
KEYWDS LGL, POLARITY, BETA PROPELLER, LIPID BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR L.ALMAGOR,W.I.WEIS
REVDAT 5 13-MAR-24 6N8P 1 REMARK
REVDAT 4 27-NOV-19 6N8P 1 REMARK
REVDAT 3 12-JUN-19 6N8P 1 JRNL
REVDAT 2 29-MAY-19 6N8P 1 JRNL
REVDAT 1 08-MAY-19 6N8P 0
JRNL AUTH L.ALMAGOR,I.S.UFIMTSEV,A.AYER,J.LI,W.I.WEIS
JRNL TITL STRUCTURAL INSIGHTS INTO THE APKC REGULATORY SWITCH
JRNL TITL 2 MECHANISM OF THE HUMAN CELL POLARITY PROTEIN LETHAL GIANT
JRNL TITL 3 LARVAE 2.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 116 10804 2019
JRNL REFN ESSN 1091-6490
JRNL PMID 31088962
JRNL DOI 10.1073/PNAS.1821514116
REMARK 2
REMARK 2 RESOLUTION. 3.19 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.13_2998: ???)
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) : 3.19
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.35
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 20221
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.208
REMARK 3 R VALUE (WORKING SET) : 0.204
REMARK 3 FREE R VALUE : 0.250
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.840
REMARK 3 FREE R VALUE TEST SET COUNT : 1989
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 39.3525 - 7.6788 0.99 1406 160 0.1882 0.2019
REMARK 3 2 7.6788 - 6.1022 1.00 1332 141 0.2091 0.2565
REMARK 3 3 6.1022 - 5.3330 1.00 1324 138 0.1935 0.2425
REMARK 3 4 5.3330 - 4.8464 1.00 1315 146 0.1628 0.2331
REMARK 3 5 4.8464 - 4.4995 1.00 1309 131 0.1627 0.1923
REMARK 3 6 4.4995 - 4.2346 1.00 1278 149 0.1672 0.2094
REMARK 3 7 4.2346 - 4.0227 1.00 1305 139 0.1902 0.2255
REMARK 3 8 4.0227 - 3.8478 1.00 1276 150 0.2144 0.2740
REMARK 3 9 3.8478 - 3.6997 1.00 1299 132 0.2217 0.3168
REMARK 3 10 3.6997 - 3.5722 1.00 1266 155 0.2354 0.2616
REMARK 3 11 3.5722 - 3.4605 1.00 1295 123 0.2473 0.3198
REMARK 3 12 3.4605 - 3.3617 1.00 1291 147 0.2581 0.3166
REMARK 3 13 3.3617 - 3.2732 1.00 1267 137 0.2673 0.3304
REMARK 3 14 3.2732 - 3.1934 0.98 1269 141 0.3266 0.3834
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.460
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.210
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 : 0.002 6624
REMARK 3 ANGLE : 0.479 9030
REMARK 3 CHIRALITY : 0.042 1009
REMARK 3 PLANARITY : 0.004 1173
REMARK 3 DIHEDRAL : 11.126 3921
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 5
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 18 THROUGH 159 )
REMARK 3 ORIGIN FOR THE GROUP (A): -0.2452 64.5389 62.2552
REMARK 3 T TENSOR
REMARK 3 T11: 0.4169 T22: 0.5276
REMARK 3 T33: 0.6054 T12: -0.0089
REMARK 3 T13: 0.0768 T23: 0.0222
REMARK 3 L TENSOR
REMARK 3 L11: 0.9696 L22: 2.4822
REMARK 3 L33: 2.4205 L12: -0.0928
REMARK 3 L13: 0.4310 L23: 1.2714
REMARK 3 S TENSOR
REMARK 3 S11: 0.0043 S12: -0.2291 S13: -0.1764
REMARK 3 S21: 0.0223 S22: -0.0577 S23: 0.4793
REMARK 3 S31: -0.0170 S32: -0.3339 S33: 0.0714
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 160 THROUGH 291 )
REMARK 3 ORIGIN FOR THE GROUP (A): 14.8672 82.8849 73.7856
REMARK 3 T TENSOR
REMARK 3 T11: 0.4444 T22: 0.4662
REMARK 3 T33: 0.4023 T12: 0.0179
REMARK 3 T13: -0.0255 T23: -0.0634
REMARK 3 L TENSOR
REMARK 3 L11: 3.1592 L22: 2.6656
REMARK 3 L33: 3.0189 L12: 0.4176
REMARK 3 L13: -0.9886 L23: -1.4462
REMARK 3 S TENSOR
REMARK 3 S11: -0.1151 S12: -0.5507 S13: 0.1230
REMARK 3 S21: 0.5285 S22: 0.0406 S23: 0.1681
REMARK 3 S31: -0.3684 S32: 0.3265 S33: 0.0596
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 292 THROUGH 523 )
REMARK 3 ORIGIN FOR THE GROUP (A): 13.1067 71.9277 37.7569
REMARK 3 T TENSOR
REMARK 3 T11: 0.4718 T22: 0.5622
REMARK 3 T33: 0.4757 T12: 0.0100
REMARK 3 T13: 0.0106 T23: -0.0158
REMARK 3 L TENSOR
REMARK 3 L11: 0.7500 L22: 0.5852
REMARK 3 L33: 2.4609 L12: 0.4608
REMARK 3 L13: 1.0298 L23: 0.9697
REMARK 3 S TENSOR
REMARK 3 S11: -0.0776 S12: 0.0604 S13: -0.0399
REMARK 3 S21: -0.2076 S22: -0.0345 S23: -0.0013
REMARK 3 S31: -0.1170 S32: 0.1533 S33: 0.0989
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 524 THROUGH 822 )
REMARK 3 ORIGIN FOR THE GROUP (A): -2.7010 66.0942 7.3713
REMARK 3 T TENSOR
REMARK 3 T11: 0.5632 T22: 0.6073
REMARK 3 T33: 0.5071 T12: 0.0171
REMARK 3 T13: -0.0962 T23: -0.0053
REMARK 3 L TENSOR
REMARK 3 L11: 1.1055 L22: 1.8985
REMARK 3 L33: 1.3263 L12: 0.9582
REMARK 3 L13: -0.3189 L23: 0.0166
REMARK 3 S TENSOR
REMARK 3 S11: -0.1174 S12: 0.2122 S13: 0.1376
REMARK 3 S21: -0.2730 S22: 0.0757 S23: 0.1438
REMARK 3 S31: -0.2596 S32: -0.1870 S33: 0.0269
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 823 THROUGH 926 )
REMARK 3 ORIGIN FOR THE GROUP (A): -9.3876 55.5441 30.3379
REMARK 3 T TENSOR
REMARK 3 T11: 0.5594 T22: 0.7688
REMARK 3 T33: 0.6934 T12: -0.0739
REMARK 3 T13: -0.0351 T23: 0.0091
REMARK 3 L TENSOR
REMARK 3 L11: 1.7368 L22: 0.2820
REMARK 3 L33: 3.5558 L12: 0.7073
REMARK 3 L13: 2.4905 L23: 1.0054
REMARK 3 S TENSOR
REMARK 3 S11: -0.0207 S12: -0.4759 S13: 0.0498
REMARK 3 S21: 0.3369 S22: -0.0164 S23: 0.2376
REMARK 3 S31: 0.1605 S32: -0.6676 S33: -0.0003
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 6N8P COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-DEC-18.
REMARK 100 THE DEPOSITION ID IS D_1000238170.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-JUL-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL12-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0055
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20282
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.190
REMARK 200 RESOLUTION RANGE LOW (A) : 39.350
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 6.500
REMARK 200 R MERGE (I) : 0.41900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.19
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.41
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.5
REMARK 200 DATA REDUNDANCY IN SHELL : 6.80
REMARK 200 R MERGE FOR SHELL (I) : 2.09700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.47
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 19.8 % PEG 3350, 0.29 M NA2SO4, 0.1 M
REMARK 280 BIS-TRIS PROPANE PH 7.5, 3% METHANOL, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 295.15K
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 39.34950
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 63.31950
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 59.24450
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 63.31950
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 39.34950
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 59.24450
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 12
REMARK 465 ARG A 13
REMARK 465 GLU A 14
REMARK 465 ARG A 15
REMARK 465 LEU A 16
REMARK 465 LYS A 17
REMARK 465 THR A 471
REMARK 465 ASP A 472
REMARK 465 THR A 473
REMARK 465 ASP A 474
REMARK 465 PRO A 475
REMARK 465 ASN A 476
REMARK 465 GLU A 477
REMARK 465 ASN A 478
REMARK 465 PHE A 479
REMARK 465 SER A 480
REMARK 465 ALA A 481
REMARK 465 GLN A 482
REMARK 465 GLY A 483
REMARK 465 GLU A 484
REMARK 465 ALA A 635
REMARK 465 LEU A 636
REMARK 465 GLU A 637
REMARK 465 GLY A 638
REMARK 465 PRO A 639
REMARK 465 LEU A 640
REMARK 465 SER A 641
REMARK 465 ARG A 642
REMARK 465 VAL A 643
REMARK 465 LYS A 644
REMARK 465 SER A 645
REMARK 465 LEU A 646
REMARK 465 LYS A 647
REMARK 465 LYS A 648
REMARK 465 SER A 649
REMARK 465 LEU A 650
REMARK 465 ARG A 651
REMARK 465 GLN A 652
REMARK 465 SER A 653
REMARK 465 PHE A 654
REMARK 465 ARG A 655
REMARK 465 ARG A 656
REMARK 465 MET A 657
REMARK 465 ARG A 658
REMARK 465 ARG A 659
REMARK 465 SER A 660
REMARK 465 ARG A 661
REMARK 465 VAL A 662
REMARK 465 SER A 663
REMARK 465 SER A 664
REMARK 465 ARG A 665
REMARK 465 LYS A 666
REMARK 465 ARG A 667
REMARK 465 HIS A 668
REMARK 465 PRO A 669
REMARK 465 ALA A 670
REMARK 465 GLY A 671
REMARK 465 PRO A 672
REMARK 465 PRO A 673
REMARK 465 GLY A 674
REMARK 465 GLU A 675
REMARK 465 ALA A 676
REMARK 465 GLN A 677
REMARK 465 GLU A 678
REMARK 465 GLY A 679
REMARK 465 SER A 680
REMARK 465 ALA A 681
REMARK 465 LYS A 682
REMARK 465 ALA A 683
REMARK 465 GLU A 684
REMARK 465 ARG A 685
REMARK 465 PRO A 686
REMARK 465 GLY A 687
REMARK 465 LEU A 688
REMARK 465 GLN A 689
REMARK 465 ASN A 690
REMARK 465 MET A 691
REMARK 465 GLU A 692
REMARK 465 LEU A 693
REMARK 465 ALA A 694
REMARK 465 PRO A 695
REMARK 465 VAL A 696
REMARK 465 GLN A 697
REMARK 465 ARG A 698
REMARK 465 LYS A 699
REMARK 465 ILE A 700
REMARK 465 GLU A 701
REMARK 465 ALA A 702
REMARK 465 ARG A 703
REMARK 465 SER A 704
REMARK 465 ALA A 705
REMARK 465 GLU A 706
REMARK 465 ASP A 707
REMARK 465 SER A 853
REMARK 465 ARG A 854
REMARK 465 ARG A 855
REMARK 465 ALA A 856
REMARK 465 GLU A 857
REMARK 465 ASP A 858
REMARK 465 ALA A 938
REMARK 465 GLU A 939
REMARK 465 THR A 940
REMARK 465 LYS A 941
REMARK 465 ASN A 942
REMARK 465 HIS A 943
REMARK 465 ARG A 944
REMARK 465 PRO A 945
REMARK 465 GLY A 946
REMARK 465 ASN A 947
REMARK 465 GLY A 948
REMARK 465 ALA A 949
REMARK 465 GLY A 950
REMARK 465 PRO A 951
REMARK 465 LYS A 952
REMARK 465 LYS A 953
REMARK 465 ALA A 954
REMARK 465 PRO A 955
REMARK 465 SER A 956
REMARK 465 ARG A 957
REMARK 465 ALA A 958
REMARK 465 ARG A 959
REMARK 465 ASN A 960
REMARK 465 SER A 961
REMARK 465 GLY A 962
REMARK 465 THR A 963
REMARK 465 GLN A 964
REMARK 465 SER A 965
REMARK 465 ASP A 966
REMARK 465 GLY A 967
REMARK 465 GLU A 968
REMARK 465 GLU A 969
REMARK 465 LYS A 970
REMARK 465 GLN A 971
REMARK 465 PRO A 972
REMARK 465 GLY A 973
REMARK 465 LEU A 974
REMARK 465 VAL A 975
REMARK 465 MET A 976
REMARK 465 GLU A 977
REMARK 465 ARG A 978
REMARK 465 GLU A 979
REMARK 465 PHE A 980
REMARK 465 THR A 981
REMARK 465 THR A 982
REMARK 465 ALA A 983
REMARK 465 SER A 984
REMARK 465 GLU A 985
REMARK 465 ASN A 986
REMARK 465 LEU A 987
REMARK 465 TYR A 988
REMARK 465 PHE A 989
REMARK 465 GLN A 990
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 ARG A 18 CG CD NE CZ NH1 NH2
REMARK 470 ASP A 19 CG OD1 OD2
REMARK 470 LYS A 105 CG CD CE NZ
REMARK 470 ARG A 162 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 554 CG CD OE1 OE2
REMARK 470 ARG A 557 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 559 CG CD CE NZ
REMARK 470 GLU A 562 CG CD OE1 OE2
REMARK 470 ARG A 620 CG CD NE CZ NH1 NH2
REMARK 470 SER A 631 OG
REMARK 470 ASP A 632 CG OD1 OD2
REMARK 470 GLN A 633 CG CD OE1 NE2
REMARK 470 LYS A 724 CG CD CE NZ
REMARK 470 LYS A 926 CG CD CE NZ
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 THR A 26 -130.25 -119.50
REMARK 500 GLN A 34 70.14 53.48
REMARK 500 SER A 36 -6.66 -152.46
REMARK 500 ARG A 120 -71.44 -105.86
REMARK 500 PRO A 159 -157.19 -77.27
REMARK 500 ALA A 160 -24.06 72.18
REMARK 500 HIS A 184 98.89 -67.47
REMARK 500 LEU A 194 94.33 -160.69
REMARK 500 ARG A 270 119.06 -167.37
REMARK 500 SER A 308 -44.07 -149.45
REMARK 500 ASP A 349 74.24 54.98
REMARK 500 TYR A 351 -7.51 -156.94
REMARK 500 SER A 381 98.34 -68.24
REMARK 500 ASN A 395 83.85 57.08
REMARK 500 ASN A 412 42.43 -103.57
REMARK 500 ALA A 452 40.66 -87.93
REMARK 500 VAL A 455 -65.06 -130.30
REMARK 500 LEU A 550 51.72 -109.22
REMARK 500 LEU A 564 -164.36 -76.97
REMARK 500 THR A 607 -161.46 -115.40
REMARK 500 LYS A 724 -70.16 -98.46
REMARK 500 LYS A 830 -15.22 -153.17
REMARK 500 LEU A 838 -79.32 -104.91
REMARK 500 SER A 888 82.63 -150.36
REMARK 500 SER A 900 69.86 -105.00
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 residue CL A 1001
DBREF 6N8P A 13 978 UNP Q6P1M3 L2GL2_HUMAN 13 978
SEQADV 6N8P MET A 12 UNP Q6P1M3 INITIATING METHIONINE
SEQADV 6N8P GLU A 979 UNP Q6P1M3 EXPRESSION TAG
SEQADV 6N8P PHE A 980 UNP Q6P1M3 EXPRESSION TAG
SEQADV 6N8P THR A 981 UNP Q6P1M3 EXPRESSION TAG
SEQADV 6N8P THR A 982 UNP Q6P1M3 EXPRESSION TAG
SEQADV 6N8P ALA A 983 UNP Q6P1M3 EXPRESSION TAG
SEQADV 6N8P SER A 984 UNP Q6P1M3 EXPRESSION TAG
SEQADV 6N8P GLU A 985 UNP Q6P1M3 EXPRESSION TAG
SEQADV 6N8P ASN A 986 UNP Q6P1M3 EXPRESSION TAG
SEQADV 6N8P LEU A 987 UNP Q6P1M3 EXPRESSION TAG
SEQADV 6N8P TYR A 988 UNP Q6P1M3 EXPRESSION TAG
SEQADV 6N8P PHE A 989 UNP Q6P1M3 EXPRESSION TAG
SEQADV 6N8P GLN A 990 UNP Q6P1M3 EXPRESSION TAG
SEQRES 1 A 979 MET ARG GLU ARG LEU LYS ARG ASP LEU PHE GLN PHE ASN
SEQRES 2 A 979 LYS THR VAL GLU HIS GLY PHE PRO HIS GLN PRO SER ALA
SEQRES 3 A 979 LEU GLY TYR SER PRO SER LEU ARG ILE LEU ALA ILE GLY
SEQRES 4 A 979 THR ARG SER GLY ALA ILE LYS LEU TYR GLY ALA PRO GLY
SEQRES 5 A 979 VAL GLU PHE MET GLY LEU HIS GLN GLU ASN ASN ALA VAL
SEQRES 6 A 979 THR GLN ILE HIS LEU LEU PRO GLY GLN CYS GLN LEU VAL
SEQRES 7 A 979 THR LEU LEU ASP ASP ASN SER LEU HIS LEU TRP SER LEU
SEQRES 8 A 979 LYS VAL LYS GLY GLY ALA SER GLU LEU GLN GLU ASP GLU
SEQRES 9 A 979 SER PHE THR LEU ARG GLY PRO PRO GLY ALA ALA PRO SER
SEQRES 10 A 979 ALA THR GLN ILE THR VAL VAL LEU PRO HIS SER SER CYS
SEQRES 11 A 979 GLU LEU LEU TYR LEU GLY THR GLU SER GLY ASN VAL PHE
SEQRES 12 A 979 VAL VAL GLN LEU PRO ALA PHE ARG ALA LEU GLU ASP ARG
SEQRES 13 A 979 THR ILE SER SER ASP ALA VAL LEU GLN ARG LEU PRO GLU
SEQRES 14 A 979 GLU ALA ARG HIS ARG ARG VAL PHE GLU MET VAL GLU ALA
SEQRES 15 A 979 LEU GLN GLU HIS PRO ARG ASP PRO ASN GLN ILE LEU ILE
SEQRES 16 A 979 GLY TYR SER ARG GLY LEU VAL VAL ILE TRP ASP LEU GLN
SEQRES 17 A 979 GLY SER ARG VAL LEU TYR HIS PHE LEU SER SER GLN GLN
SEQRES 18 A 979 LEU GLU ASN ILE TRP TRP GLN ARG ASP GLY ARG LEU LEU
SEQRES 19 A 979 VAL SER CYS HIS SER ASP GLY SER TYR CYS GLN TRP PRO
SEQRES 20 A 979 VAL SER SER GLU ALA GLN GLN PRO GLU PRO LEU ARG SER
SEQRES 21 A 979 LEU VAL PRO TYR GLY PRO PHE PRO CYS LYS ALA ILE THR
SEQRES 22 A 979 ARG ILE LEU TRP LEU THR THR ARG GLN GLY LEU PRO PHE
SEQRES 23 A 979 THR ILE PHE GLN GLY GLY MET PRO ARG ALA SER TYR GLY
SEQRES 24 A 979 ASP ARG HIS CYS ILE SER VAL ILE HIS ASP GLY GLN GLN
SEQRES 25 A 979 THR ALA PHE ASP PHE THR SER ARG VAL ILE GLY PHE THR
SEQRES 26 A 979 VAL LEU THR GLU ALA ASP PRO ALA ALA THR PHE ASP ASP
SEQRES 27 A 979 PRO TYR ALA LEU VAL VAL LEU ALA GLU GLU GLU LEU VAL
SEQRES 28 A 979 VAL ILE ASP LEU GLN THR ALA GLY TRP PRO PRO VAL GLN
SEQRES 29 A 979 LEU PRO TYR LEU ALA SER LEU HIS CYS SER ALA ILE THR
SEQRES 30 A 979 CYS SER HIS HIS VAL SER ASN ILE PRO LEU LYS LEU TRP
SEQRES 31 A 979 GLU ARG ILE ILE ALA ALA GLY SER ARG GLN ASN ALA HIS
SEQRES 32 A 979 PHE SER THR MET GLU TRP PRO ILE ASP GLY GLY THR SER
SEQRES 33 A 979 LEU THR PRO ALA PRO PRO GLN ARG ASP LEU LEU LEU THR
SEQRES 34 A 979 GLY HIS GLU ASP GLY THR VAL ARG PHE TRP ASP ALA SER
SEQRES 35 A 979 GLY VAL CYS LEU ARG LEU LEU TYR LYS LEU SER THR VAL
SEQRES 36 A 979 ARG VAL PHE LEU THR ASP THR ASP PRO ASN GLU ASN PHE
SEQRES 37 A 979 SER ALA GLN GLY GLU ASP GLU TRP PRO PRO LEU ARG LYS
SEQRES 38 A 979 VAL GLY SER PHE ASP PRO TYR SER ASP ASP PRO ARG LEU
SEQRES 39 A 979 GLY ILE GLN LYS ILE PHE LEU CYS LYS TYR SER GLY TYR
SEQRES 40 A 979 LEU ALA VAL ALA GLY THR ALA GLY GLN VAL LEU VAL LEU
SEQRES 41 A 979 GLU LEU ASN ASP GLU ALA ALA GLU GLN ALA VAL GLU GLN
SEQRES 42 A 979 VAL GLU ALA ASP LEU LEU GLN ASP GLN GLU GLY TYR ARG
SEQRES 43 A 979 TRP LYS GLY HIS GLU ARG LEU ALA ALA ARG SER GLY PRO
SEQRES 44 A 979 VAL ARG PHE GLU PRO GLY PHE GLN PRO PHE VAL LEU VAL
SEQRES 45 A 979 GLN CYS GLN PRO PRO ALA VAL VAL THR SER LEU ALA LEU
SEQRES 46 A 979 HIS SER GLU TRP ARG LEU VAL ALA PHE GLY THR SER HIS
SEQRES 47 A 979 GLY PHE GLY LEU PHE ASP HIS GLN GLN ARG ARG GLN VAL
SEQRES 48 A 979 PHE VAL LYS CYS THR LEU HIS PRO SER ASP GLN LEU ALA
SEQRES 49 A 979 LEU GLU GLY PRO LEU SER ARG VAL LYS SER LEU LYS LYS
SEQRES 50 A 979 SER LEU ARG GLN SER PHE ARG ARG MET ARG ARG SER ARG
SEQRES 51 A 979 VAL SER SER ARG LYS ARG HIS PRO ALA GLY PRO PRO GLY
SEQRES 52 A 979 GLU ALA GLN GLU GLY SER ALA LYS ALA GLU ARG PRO GLY
SEQRES 53 A 979 LEU GLN ASN MET GLU LEU ALA PRO VAL GLN ARG LYS ILE
SEQRES 54 A 979 GLU ALA ARG SER ALA GLU ASP SER PHE THR GLY PHE VAL
SEQRES 55 A 979 ARG THR LEU TYR PHE ALA ASP THR TYR LEU LYS ASP SER
SEQRES 56 A 979 SER ARG HIS CYS PRO SER LEU TRP ALA GLY THR ASN GLY
SEQRES 57 A 979 GLY THR ILE TYR ALA PHE SER LEU ARG VAL PRO PRO ALA
SEQRES 58 A 979 GLU ARG ARG MET ASP GLU PRO VAL ARG ALA GLU GLN ALA
SEQRES 59 A 979 LYS GLU ILE GLN LEU MET HIS ARG ALA PRO VAL VAL GLY
SEQRES 60 A 979 ILE LEU VAL LEU ASP GLY HIS SER VAL PRO LEU PRO GLU
SEQRES 61 A 979 PRO LEU GLU VAL ALA HIS ASP LEU SER LYS SER PRO ASP
SEQRES 62 A 979 MET GLN GLY SER HIS GLN LEU LEU VAL VAL SER GLU GLU
SEQRES 63 A 979 GLN PHE LYS VAL PHE THR LEU PRO LYS VAL SER ALA LYS
SEQRES 64 A 979 LEU LYS LEU LYS LEU THR ALA LEU GLU GLY SER ARG VAL
SEQRES 65 A 979 ARG ARG VAL SER VAL ALA HIS PHE GLY SER ARG ARG ALA
SEQRES 66 A 979 GLU ASP TYR GLY GLU HIS HIS LEU ALA VAL LEU THR ASN
SEQRES 67 A 979 LEU GLY ASP ILE GLN VAL VAL SER LEU PRO LEU LEU LYS
SEQRES 68 A 979 PRO GLN VAL ARG TYR SER CYS ILE ARG ARG GLU ASP VAL
SEQRES 69 A 979 SER GLY ILE ALA SER CYS VAL PHE THR LYS TYR GLY GLN
SEQRES 70 A 979 GLY PHE TYR LEU ILE SER PRO SER GLU PHE GLU ARG PHE
SEQRES 71 A 979 SER LEU SER THR LYS TRP LEU VAL GLU PRO ARG CYS LEU
SEQRES 72 A 979 VAL ASP SER ALA GLU THR LYS ASN HIS ARG PRO GLY ASN
SEQRES 73 A 979 GLY ALA GLY PRO LYS LYS ALA PRO SER ARG ALA ARG ASN
SEQRES 74 A 979 SER GLY THR GLN SER ASP GLY GLU GLU LYS GLN PRO GLY
SEQRES 75 A 979 LEU VAL MET GLU ARG GLU PHE THR THR ALA SER GLU ASN
SEQRES 76 A 979 LEU TYR PHE GLN
HET CL A1001 1
HETNAM CL CHLORIDE ION
FORMUL 2 CL CL 1-
HELIX 1 AA1 ALA A 126 THR A 130 5 5
HELIX 2 AA2 SER A 170 GLN A 176 1 7
HELIX 3 AA3 ARG A 177 LEU A 178 5 2
HELIX 4 AA4 PRO A 179 ARG A 183 5 5
HELIX 5 AA5 SER A 308 ARG A 312 5 5
HELIX 6 AA6 PRO A 397 GLN A 411 1 15
HELIX 7 AA7 VAL A 466 PHE A 469 5 4
HELIX 8 AA8 ASP A 502 LEU A 505 5 4
HELIX 9 AA9 PRO A 751 ARG A 755 5 5
HELIX 10 AB1 ASP A 798 SER A 802 5 5
HELIX 11 AB2 LEU A 835 GLY A 840 1 6
HELIX 12 AB3 ASP A 894 SER A 900 1 7
SHEET 1 AA1 4 ASN A 24 GLY A 30 0
SHEET 2 AA1 4 GLU A 917 SER A 922 -1 O PHE A 918 N HIS A 29
SHEET 3 AA1 4 GLN A 908 SER A 914 -1 N TYR A 911 O GLU A 919
SHEET 4 AA1 4 CYS A 901 PHE A 903 -1 N VAL A 902 O PHE A 910
SHEET 1 AA2 4 PRO A 35 SER A 41 0
SHEET 2 AA2 4 ILE A 46 THR A 51 -1 O ALA A 48 N GLY A 39
SHEET 3 AA2 4 ALA A 55 TYR A 59 -1 O TYR A 59 N LEU A 47
SHEET 4 AA2 4 GLU A 65 LEU A 69 -1 O PHE A 66 N LEU A 58
SHEET 1 AA3 4 VAL A 76 LEU A 81 0
SHEET 2 AA3 4 GLN A 87 LEU A 92 -1 O LEU A 91 N THR A 77
SHEET 3 AA3 4 SER A 96 VAL A 104 -1 O TRP A 100 N LEU A 88
SHEET 4 AA3 4 SER A 109 THR A 118 -1 O PHE A 117 N LEU A 97
SHEET 1 AA4 4 ILE A 132 PRO A 137 0
SHEET 2 AA4 4 LEU A 143 THR A 148 -1 O GLY A 147 N THR A 133
SHEET 3 AA4 4 VAL A 153 GLN A 157 -1 O PHE A 154 N LEU A 146
SHEET 4 AA4 4 ARG A 162 ILE A 169 -1 O ILE A 169 N VAL A 153
SHEET 1 AA5 4 VAL A 191 HIS A 197 0
SHEET 2 AA5 4 ASP A 200 TYR A 208 -1 O LEU A 205 N GLN A 195
SHEET 3 AA5 4 LEU A 212 ASP A 217 -1 O TRP A 216 N ILE A 204
SHEET 4 AA5 4 ARG A 222 LEU A 228 -1 O ARG A 222 N ASP A 217
SHEET 1 AA6 4 LEU A 233 TRP A 238 0
SHEET 2 AA6 4 LEU A 244 HIS A 249 -1 O CYS A 248 N GLU A 234
SHEET 3 AA6 4 TYR A 254 PRO A 258 -1 O TRP A 257 N LEU A 245
SHEET 4 AA6 4 ARG A 270 LEU A 272 -1 O LEU A 272 N TYR A 254
SHEET 1 AA7 5 ILE A 283 LEU A 289 0
SHEET 2 AA7 5 PHE A 297 GLY A 302 -1 O PHE A 297 N LEU A 289
SHEET 3 AA7 5 HIS A 313 HIS A 319 -1 O SER A 316 N PHE A 300
SHEET 4 AA7 5 GLN A 322 PHE A 328 -1 O PHE A 328 N HIS A 313
SHEET 5 AA7 5 LEU A 490 LYS A 492 1 O ARG A 491 N ASP A 327
SHEET 1 AA8 3 VAL A 332 THR A 339 0
SHEET 2 AA8 3 PRO A 350 ALA A 357 -1 O VAL A 354 N THR A 336
SHEET 3 AA8 3 LEU A 361 ASP A 365 -1 O VAL A 362 N VAL A 355
SHEET 1 AA9 4 ILE A 387 VAL A 393 0
SHEET 2 AA9 4 LEU A 437 HIS A 442 -1 O LEU A 439 N HIS A 391
SHEET 3 AA9 4 THR A 446 ASP A 451 -1 O TRP A 450 N LEU A 438
SHEET 4 AA9 4 ARG A 458 SER A 464 -1 O LEU A 463 N VAL A 447
SHEET 1 AB1 2 THR A 426 SER A 427 0
SHEET 2 AB1 2 CYS A 933 LEU A 934 -1 O LEU A 934 N THR A 426
SHEET 1 AB2 5 ILE A 507 LEU A 512 0
SHEET 2 AB2 5 TYR A 518 GLY A 523 -1 O ALA A 522 N GLN A 508
SHEET 3 AB2 5 GLN A 527 ASN A 534 -1 O LEU A 531 N LEU A 519
SHEET 4 AB2 5 GLY A 576 GLN A 586 -1 O GLN A 578 N GLU A 532
SHEET 5 AB2 5 GLU A 543 ASP A 548 1 N GLU A 543 O LEU A 582
SHEET 1 AB3 2 ALA A 538 GLN A 540 0
SHEET 2 AB3 2 VAL A 571 PHE A 573 -1 O PHE A 573 N ALA A 538
SHEET 1 AB4 4 SER A 593 HIS A 597 0
SHEET 2 AB4 4 LEU A 602 GLY A 606 -1 O ALA A 604 N ALA A 595
SHEET 3 AB4 4 GLY A 610 ASP A 615 -1 O PHE A 614 N VAL A 603
SHEET 4 AB4 4 ARG A 620 CYS A 626 -1 O ARG A 620 N ASP A 615
SHEET 1 AB5 4 VAL A 713 THR A 721 0
SHEET 2 AB5 4 CYS A 730 THR A 737 -1 O GLY A 736 N ARG A 714
SHEET 3 AB5 4 THR A 741 ARG A 748 -1 O TYR A 743 N ALA A 735
SHEET 4 AB5 4 ARG A 761 GLN A 769 -1 O ALA A 765 N ALA A 744
SHEET 1 AB6 4 VAL A 776 LEU A 782 0
SHEET 2 AB6 4 GLN A 810 SER A 815 -1 O LEU A 812 N LEU A 780
SHEET 3 AB6 4 GLN A 818 THR A 823 -1 O PHE A 822 N LEU A 811
SHEET 4 AB6 4 SER A 828 LYS A 834 -1 O LEU A 833 N PHE A 819
SHEET 1 AB7 4 VAL A 843 HIS A 850 0
SHEET 2 AB7 4 HIS A 862 THR A 868 -1 O LEU A 867 N ARG A 844
SHEET 3 AB7 4 ILE A 873 SER A 877 -1 O GLN A 874 N VAL A 866
SHEET 4 AB7 4 PRO A 883 ARG A 886 -1 O GLN A 884 N VAL A 875
CISPEP 1 LEU A 158 PRO A 159 0 -2.36
CISPEP 2 TRP A 487 PRO A 488 0 -1.23
CISPEP 3 GLN A 586 PRO A 587 0 2.15
CISPEP 4 LEU A 824 PRO A 825 0 2.82
CISPEP 5 LEU A 878 PRO A 879 0 -3.07
SITE 1 AC1 3 LYS A 514 LYS A 801 TYR A 906
CRYST1 78.699 118.489 126.639 90.00 90.00 90.00 P 21 21 21 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 0.012707 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008440 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007896 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
