HEADER LIPID BINDING PROTEIN 30-NOV-18 6N8R
TITLE CRYSTAL STRUCTURE OF THE HUMAN CELL POLARITY PROTEIN LETHAL GIANT
TITLE 2 LARVAE 2 (LGL2). APKC PHOSPHORYLATED, CRYSTAL FORM 2.
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;
COMPND 6 OTHER_DETAILS: HUMAN LGL2(13-978) APKC PHOSPHORYLATED AT S641, S645,
COMPND 7 S649, S653, S660, S663 AND S680. THE PHOSPHORYLATED RESIDUES ARE ALL
COMPND 8 POSITIONED IN AN UNSTRUCTERED LOOP.
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 6N8R 1 REMARK
REVDAT 4 27-NOV-19 6N8R 1 REMARK
REVDAT 3 12-JUN-19 6N8R 1 JRNL
REVDAT 2 29-MAY-19 6N8R 1 JRNL
REVDAT 1 08-MAY-19 6N8R 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. 1.91 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.14_3260
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) : 1.91
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.27
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 48.8
REMARK 3 NUMBER OF REFLECTIONS : 37726
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.197
REMARK 3 R VALUE (WORKING SET) : 0.196
REMARK 3 FREE R VALUE : 0.219
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1888
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 34.2778 - 4.4884 0.98 5767 275 0.1580 0.1822
REMARK 3 2 4.4884 - 3.5637 0.98 5602 298 0.1547 0.1647
REMARK 3 3 3.5637 - 3.1136 0.95 5397 282 0.1982 0.2252
REMARK 3 4 3.1136 - 2.8291 0.80 4526 256 0.2446 0.2735
REMARK 3 5 2.8291 - 2.6264 0.65 3651 179 0.2554 0.2996
REMARK 3 6 2.6264 - 2.4716 0.53 3008 156 0.2740 0.2869
REMARK 3 7 2.4716 - 2.3478 0.45 2542 144 0.2795 0.3060
REMARK 3 8 2.3478 - 2.2456 0.39 2156 110 0.3069 0.3228
REMARK 3 9 2.2456 - 2.1592 0.28 1567 97 0.2822 0.3028
REMARK 3 10 2.1592 - 2.0847 0.14 791 48 0.2892 0.3018
REMARK 3 11 2.0847 - 2.0195 0.08 457 24 0.3028 0.3465
REMARK 3 12 2.0195 - 1.9618 0.04 230 9 0.3510 0.3652
REMARK 3 13 1.9618 - 1.9102 0.03 144 10 0.3123 0.3937
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) : 0.230
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.470
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 39.68
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 : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
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 1 THROUGH 126 )
REMARK 3 ORIGIN FOR THE GROUP (A): 126.9632 -50.9747 145.9140
REMARK 3 T TENSOR
REMARK 3 T11: 0.2303 T22: 0.1030
REMARK 3 T33: 0.1393 T12: -0.1154
REMARK 3 T13: -0.0178 T23: 0.0896
REMARK 3 L TENSOR
REMARK 3 L11: 0.1069 L22: 0.0268
REMARK 3 L33: 0.1662 L12: -0.0268
REMARK 3 L13: -0.0500 L23: 0.0669
REMARK 3 S TENSOR
REMARK 3 S11: -0.0114 S12: -0.0523 S13: 0.0599
REMARK 3 S21: -0.1164 S22: -0.1043 S23: -0.0069
REMARK 3 S31: -0.2073 S32: 0.2225 S33: -0.0668
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 127 THROUGH 285 )
REMARK 3 ORIGIN FOR THE GROUP (A): 139.7048 -57.5882 171.6218
REMARK 3 T TENSOR
REMARK 3 T11: 0.2165 T22: 0.2762
REMARK 3 T33: 0.2095 T12: -0.0292
REMARK 3 T13: 0.0101 T23: 0.0299
REMARK 3 L TENSOR
REMARK 3 L11: 0.0209 L22: 0.0790
REMARK 3 L33: 0.0806 L12: -0.0313
REMARK 3 L13: 0.0278 L23: 0.0128
REMARK 3 S TENSOR
REMARK 3 S11: -0.0702 S12: 0.0092 S13: 0.0583
REMARK 3 S21: 0.0891 S22: 0.0609 S23: -0.1731
REMARK 3 S31: -0.0464 S32: 0.2773 S33: 0.0007
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 286 THROUGH 375 )
REMARK 3 ORIGIN FOR THE GROUP (A): 116.3410 -54.8752 167.4410
REMARK 3 T TENSOR
REMARK 3 T11: 0.2327 T22: 0.0915
REMARK 3 T33: 0.1372 T12: 0.0060
REMARK 3 T13: -0.0117 T23: -0.0096
REMARK 3 L TENSOR
REMARK 3 L11: 0.1377 L22: 0.0215
REMARK 3 L33: 0.0435 L12: 0.0168
REMARK 3 L13: -0.0548 L23: -0.0181
REMARK 3 S TENSOR
REMARK 3 S11: -0.0624 S12: -0.1676 S13: -0.0030
REMARK 3 S21: 0.0766 S22: -0.0214 S23: 0.0410
REMARK 3 S31: -0.0694 S32: 0.0018 S33: -0.0225
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 376 THROUGH 551 )
REMARK 3 ORIGIN FOR THE GROUP (A): 94.6512 -54.3104 151.6395
REMARK 3 T TENSOR
REMARK 3 T11: 0.2202 T22: 0.2602
REMARK 3 T33: 0.2144 T12: 0.0526
REMARK 3 T13: 0.0281 T23: -0.0483
REMARK 3 L TENSOR
REMARK 3 L11: 0.1610 L22: 0.1650
REMARK 3 L33: 0.2091 L12: 0.0033
REMARK 3 L13: 0.1341 L23: -0.1021
REMARK 3 S TENSOR
REMARK 3 S11: -0.0173 S12: -0.2262 S13: -0.0012
REMARK 3 S21: 0.1593 S22: -0.0150 S23: 0.0774
REMARK 3 S31: -0.2436 S32: -0.3389 S33: -0.0002
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 552 THROUGH 926 )
REMARK 3 ORIGIN FOR THE GROUP (A): 89.5625 -54.0663 131.0781
REMARK 3 T TENSOR
REMARK 3 T11: -0.0517 T22: 0.2706
REMARK 3 T33: 0.1689 T12: 0.1204
REMARK 3 T13: 0.0431 T23: -0.0415
REMARK 3 L TENSOR
REMARK 3 L11: 0.1524 L22: 0.1514
REMARK 3 L33: 0.4826 L12: -0.0999
REMARK 3 L13: -0.0339 L23: -0.0392
REMARK 3 S TENSOR
REMARK 3 S11: -0.0507 S12: 0.0124 S13: -0.0297
REMARK 3 S21: 0.1297 S22: -0.0414 S23: 0.0303
REMARK 3 S31: -0.2344 S32: -0.6346 S33: -0.2327
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 6N8R 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_1000238340.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-APR-18
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
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) : 0.97946
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 : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 66987
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.910
REMARK 200 RESOLUTION RANGE LOW (A) : 39.050
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 86.9
REMARK 200 DATA REDUNDANCY : 6.400
REMARK 200 R MERGE (I) : 0.11100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.91
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.95
REMARK 200 COMPLETENESS FOR SHELL (%) : 47.1
REMARK 200 DATA REDUNDANCY IN SHELL : 4.60
REMARK 200 R MERGE FOR SHELL (I) : 10.54800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.14
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.28
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG 1500, 100 MM SPG PH 8.0, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 295.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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 86.78500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 23.28100
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 86.78500
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 23.28100
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 CL CL A1001 LIES ON A SPECIAL POSITION.
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 SER A 261
REMARK 465 GLU A 262
REMARK 465 ALA A 263
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 ASP A 485
REMARK 465 SER A 631
REMARK 465 ASP A 632
REMARK 465 GLN A 633
REMARK 465 LEU A 634
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 708
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 LYS A 105 CG CD CE NZ
REMARK 470 ARG A 120 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 162 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 264 CG CD OE1 NE2
REMARK 470 GLN A 265 CG CD OE1 NE2
REMARK 470 LYS A 399 CG CD CE NZ
REMARK 470 ARG A 410 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 536 CG CD OE1 OE2
REMARK 470 GLU A 554 CG CD OE1 OE2
REMARK 470 TYR A 556 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ARG A 557 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 562 CG CD OE1 OE2
REMARK 470 PHE A 709 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG A 748 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 753 CG CD OE1 OE2
REMARK 470 ARG A 755 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 761 CG CD NE CZ NH1 NH2
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 159 -156.84 -79.67
REMARK 500 ALA A 160 79.98 52.63
REMARK 500 MET A 190 89.38 60.36
REMARK 500 ASP A 349 72.33 62.12
REMARK 500 HIS A 391 119.64 -161.72
REMARK 500 ASN A 395 82.71 56.35
REMARK 500 ASP A 501 -74.44 -79.63
REMARK 500 ASP A 552 46.15 -103.15
REMARK 500 GLN A 553 82.17 -156.41
REMARK 500 HIS A 561 107.87 -50.11
REMARK 500 THR A 710 -41.77 -144.44
REMARK 500 PHE A 712 110.95 -36.78
REMARK 500 LYS A 724 -52.61 -124.21
REMARK 500 ASP A 798 95.20 -164.63
REMARK 500 GLN A 884 -62.04 -94.27
REMARK 500 CYS A 889 -66.90 -141.94
REMARK 500 LEU A 928 78.84 -160.98
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A1427 DISTANCE = 7.09 ANGSTROMS
REMARK 525 HOH A1428 DISTANCE = 7.84 ANGSTROMS
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
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 1002
DBREF 6N8R A 13 978 UNP Q6P1M3 L2GL2_HUMAN 13 978
SEQADV 6N8R MET A 12 UNP Q6P1M3 INITIATING METHIONINE
SEQADV 6N8R GLU A 979 UNP Q6P1M3 EXPRESSION TAG
SEQADV 6N8R PHE A 980 UNP Q6P1M3 EXPRESSION TAG
SEQADV 6N8R THR A 981 UNP Q6P1M3 EXPRESSION TAG
SEQADV 6N8R THR A 982 UNP Q6P1M3 EXPRESSION TAG
SEQADV 6N8R ALA A 983 UNP Q6P1M3 EXPRESSION TAG
SEQADV 6N8R SER A 984 UNP Q6P1M3 EXPRESSION TAG
SEQADV 6N8R GLU A 985 UNP Q6P1M3 EXPRESSION TAG
SEQADV 6N8R ASN A 986 UNP Q6P1M3 EXPRESSION TAG
SEQADV 6N8R LEU A 987 UNP Q6P1M3 EXPRESSION TAG
SEQADV 6N8R TYR A 988 UNP Q6P1M3 EXPRESSION TAG
SEQADV 6N8R PHE A 989 UNP Q6P1M3 EXPRESSION TAG
SEQADV 6N8R 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
HET GOL A1002 6
HETNAM CL CHLORIDE ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 CL CL 1-
FORMUL 3 GOL C3 H8 O3
FORMUL 4 HOH *328(H2 O)
HELIX 1 AA1 ARG A 13 LEU A 20 1 8
HELIX 2 AA2 ALA A 126 GLN A 131 1 6
HELIX 3 AA3 GLU A 165 THR A 168 5 4
HELIX 4 AA4 SER A 170 ARG A 177 1 8
HELIX 5 AA5 LEU A 178 ARG A 183 5 6
HELIX 6 AA6 PRO A 305 GLY A 310 1 6
HELIX 7 AA7 PRO A 397 ASN A 412 1 16
HELIX 8 AA8 VAL A 466 PHE A 469 5 4
HELIX 9 AA9 ASP A 502 LEU A 505 5 4
HELIX 10 AB1 ALA A 752 MET A 756 5 5
HELIX 11 AB2 LEU A 793 ASP A 798 1 6
HELIX 12 AB3 LEU A 799 SER A 802 5 4
HELIX 13 AB4 LEU A 835 GLY A 840 1 6
HELIX 14 AB5 ASP A 894 CYS A 901 1 8
SHEET 1 AA1 4 PHE A 21 GLY A 30 0
SHEET 2 AA1 4 GLU A 917 SER A 924 -1 O ARG A 920 N VAL A 27
SHEET 3 AA1 4 GLN A 908 SER A 914 -1 N TYR A 911 O GLU A 919
SHEET 4 AA1 4 VAL A 902 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 GLY A 50 N SER A 36
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 GLY A 68 N ILE A 56
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 LYS A 105 -1 O TRP A 100 N LEU A 88
SHEET 4 AA3 4 ALA A 108 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 ALA A 163 -1 O ARG A 162 N GLN A 157
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 LEU A 224 N ILE A 215
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 ARG A 270 N GLN A 256
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 GLN A 322 N HIS A 319
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 LEU A 356 N GLY A 334
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 437 N VAL A 393
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 460 N PHE A 449
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 VAL A 583 N VAL A 528
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 ALA A 541 0
SHEET 2 AB3 2 PRO A 570 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 LYS A 625 N PHE A 611
SHEET 1 AB5 4 VAL A 713 THR A 721 0
SHEET 2 AB5 4 CYS A 730 THR A 737 -1 O SER A 732 N ALA A 719
SHEET 3 AB5 4 THR A 741 ARG A 748 -1 O LEU A 747 N PRO A 731
SHEET 4 AB5 4 ARG A 761 GLN A 769 -1 O ARG A 761 N ARG A 748
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 GLN A 818 N SER A 815
SHEET 4 AB6 4 SER A 828 LYS A 834 -1 O LYS A 830 N VAL A 821
SHEET 1 AB7 4 VAL A 843 GLY A 852 0
SHEET 2 AB7 4 GLY A 860 THR A 868 -1 O ALA A 865 N SER A 847
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 TYR A 887 -1 O GLN A 884 N VAL A 875
CISPEP 1 LEU A 158 PRO A 159 0 -1.02
CISPEP 2 GLY A 276 PRO A 277 0 5.51
CISPEP 3 TRP A 487 PRO A 488 0 -1.13
CISPEP 4 GLN A 586 PRO A 587 0 2.22
CISPEP 5 LEU A 824 PRO A 825 0 4.62
CISPEP 6 LEU A 878 PRO A 879 0 0.32
SITE 1 AC1 3 GLN A 22 PHE A 23 HOH A1139
SITE 1 AC2 11 VAL A 27 GLU A 28 HIS A 29 GLY A 30
SITE 2 AC2 11 GLU A 65 TYR A 378 LEU A 379 VAL A 455
SITE 3 AC2 11 CYS A 456 LEU A 457 HOH A1101
CRYST1 173.570 46.562 137.228 90.00 115.84 90.00 C 1 2 1 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 0.005761 0.000000 0.002790 0.00000
SCALE2 0.000000 0.021477 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008096 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
