HEADER HYDROLASE/HYDROLASE INHIBITOR 01-MAY-14 4Q9J
TITLE P-GLYCOPROTEIN COCRYSTALLISED WITH QZ-VAL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MULTIDRUG RESISTANCE PROTEIN 1A;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ATP-BINDING CASSETTE SUB-FAMILY B MEMBER 1A, MDR1A,
COMPND 5 MULTIDRUG RESISTANCE PROTEIN 3, P-GLYCOPROTEIN 3;
COMPND 6 EC: 3.6.3.44;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: N-{[5-AMINO-1-(5-O-PHOSPHONO-BETA-D-ARABINOFURANOSYL)-1H-
COMPND 10 IMIDAZOL-4-YL]CARBONYL}-L-ASPARTIC ACID;
COMPND 11 CHAIN: C, D, B;
COMPND 12 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: ABCB1A, ABCB4, MDR1A, MDR3, PGY-3, PGY3;
SOURCE 6 EXPRESSION_SYSTEM: PICHIA PASTORIS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 4922;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: KM71H;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PPICZ;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES
KEYWDS MEMBRANE PROTEIN, TRANSPORTER, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR A.P.MCGRATH,P.SZEWCZYK,G.CHANG
REVDAT 3 15-NOV-23 4Q9J 1 SEQADV LINK ATOM
REVDAT 2 18-MAR-15 4Q9J 1 JRNL
REVDAT 1 04-MAR-15 4Q9J 0
JRNL AUTH P.SZEWCZYK,H.TAO,A.P.MCGRATH,M.VILLALUZ,S.D.REES,S.C.LEE,
JRNL AUTH 2 R.DOSHI,I.L.URBATSCH,Q.ZHANG,G.CHANG
JRNL TITL SNAPSHOTS OF LIGAND ENTRY, MALLEABLE BINDING AND INDUCED
JRNL TITL 2 HELICAL MOVEMENT IN P-GLYCOPROTEIN.
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 71 732 2015
JRNL REFN ISSN 0907-4449
JRNL PMID 25760620
JRNL DOI 10.1107/S1399004715000978
REMARK 2
REMARK 2 RESOLUTION. 3.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.8.2_1309
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 78.37
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.930
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.0
REMARK 3 NUMBER OF REFLECTIONS : NULL
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.262
REMARK 3 R VALUE (WORKING SET) : 0.261
REMARK 3 FREE R VALUE : 0.282
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.070
REMARK 3 FREE R VALUE TEST SET COUNT : 2526
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 78.3864 - 9.4295 0.86 2379 120 0.2277 0.2180
REMARK 3 2 9.4295 - 7.4864 0.95 2603 149 0.2010 0.1987
REMARK 3 3 7.4864 - 6.5406 0.95 2616 183 0.2597 0.3156
REMARK 3 4 6.5406 - 5.9428 0.95 2617 151 0.2894 0.3690
REMARK 3 5 5.9428 - 5.5170 0.95 2608 150 0.2830 0.3350
REMARK 3 6 5.5170 - 5.1918 0.96 2651 156 0.2695 0.2862
REMARK 3 7 5.1918 - 4.9318 0.96 2640 139 0.2662 0.3303
REMARK 3 8 4.9318 - 4.7172 0.95 2687 121 0.2590 0.2803
REMARK 3 9 4.7172 - 4.5356 0.95 2674 114 0.2580 0.2991
REMARK 3 10 4.5356 - 4.3791 0.96 2654 126 0.2753 0.3152
REMARK 3 11 4.3791 - 4.2422 0.96 2661 135 0.2632 0.3396
REMARK 3 12 4.2422 - 4.1209 0.96 2632 135 0.2812 0.2766
REMARK 3 13 4.1209 - 4.0124 0.96 2629 153 0.3013 0.2980
REMARK 3 14 4.0124 - 3.9145 0.95 2674 132 0.3106 0.3102
REMARK 3 15 3.9145 - 3.8256 0.96 2616 137 0.3544 0.3575
REMARK 3 16 3.8256 - 3.7441 0.95 2640 148 0.3667 0.4214
REMARK 3 17 3.7441 - 3.6693 0.96 2668 135 0.3872 0.4098
REMARK 3 18 3.6693 - 3.6000 0.96 2651 142 0.3970 0.4000
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) : 0.500
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 34.280
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 152.6
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 160.7
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 : 0.004 9493
REMARK 3 ANGLE : 0.801 12842
REMARK 3 CHIRALITY : 0.046 1468
REMARK 3 PLANARITY : 0.003 1627
REMARK 3 DIHEDRAL : 12.924 3423
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 30 THROUGH 217 )
REMARK 3 ORIGIN FOR THE GROUP (A): 53.0995 -5.3110 1.2418
REMARK 3 T TENSOR
REMARK 3 T11: 0.6084 T22: 0.6592
REMARK 3 T33: 0.7035 T12: -0.3767
REMARK 3 T13: 0.1901 T23: -0.3887
REMARK 3 L TENSOR
REMARK 3 L11: 4.6215 L22: 2.4023
REMARK 3 L33: 4.7890 L12: -0.1019
REMARK 3 L13: -2.4747 L23: -0.9909
REMARK 3 S TENSOR
REMARK 3 S11: 0.1972 S12: 1.3271 S13: 0.2376
REMARK 3 S21: -0.6577 S22: 0.3516 S23: -0.7618
REMARK 3 S31: -0.0097 S32: -0.5027 S33: -0.5340
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 218 THROUGH 318 )
REMARK 3 ORIGIN FOR THE GROUP (A): 79.7544 12.2862 21.2551
REMARK 3 T TENSOR
REMARK 3 T11: 1.8163 T22: 1.3268
REMARK 3 T33: 1.7257 T12: 0.2992
REMARK 3 T13: 0.1084 T23: -0.6215
REMARK 3 L TENSOR
REMARK 3 L11: -1.5916 L22: 6.7767
REMARK 3 L33: 8.1201 L12: -2.0442
REMARK 3 L13: -3.4623 L23: 9.4784
REMARK 3 S TENSOR
REMARK 3 S11: -0.2483 S12: 0.2532 S13: -0.5447
REMARK 3 S21: 2.2846 S22: -0.8251 S23: 1.4395
REMARK 3 S31: 2.5403 S32: -0.4111 S33: 0.6846
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 319 THROUGH 740 )
REMARK 3 ORIGIN FOR THE GROUP (A): 32.9412 14.0013 35.6669
REMARK 3 T TENSOR
REMARK 3 T11: 1.2585 T22: 0.6150
REMARK 3 T33: 0.9999 T12: 0.1907
REMARK 3 T13: 0.3525 T23: -0.0725
REMARK 3 L TENSOR
REMARK 3 L11: 2.5997 L22: 0.8825
REMARK 3 L33: 1.1108 L12: 0.7897
REMARK 3 L13: -1.2461 L23: -0.3072
REMARK 3 S TENSOR
REMARK 3 S11: 0.3525 S12: 0.2917 S13: 0.7092
REMARK 3 S21: 0.0335 S22: 0.0014 S23: 0.5251
REMARK 3 S31: -0.2354 S32: -0.3051 S33: -0.3572
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 741 THROUGH 1029 )
REMARK 3 ORIGIN FOR THE GROUP (A): 65.0676 17.0980 8.5576
REMARK 3 T TENSOR
REMARK 3 T11: 0.8558 T22: 0.9862
REMARK 3 T33: 0.9157 T12: -0.0892
REMARK 3 T13: 0.3893 T23: -0.2061
REMARK 3 L TENSOR
REMARK 3 L11: 0.7819 L22: 0.4524
REMARK 3 L33: -0.2324 L12: 0.0419
REMARK 3 L13: 0.1340 L23: -0.5905
REMARK 3 S TENSOR
REMARK 3 S11: 0.0010 S12: 0.2978 S13: 0.1126
REMARK 3 S21: 0.0116 S22: 0.1177 S23: 0.0060
REMARK 3 S31: 0.1266 S32: 0.1477 S33: -0.1335
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1030 THROUGH 1273 )
REMARK 3 ORIGIN FOR THE GROUP (A): 72.8514 43.1483 57.2078
REMARK 3 T TENSOR
REMARK 3 T11: 0.7160 T22: 0.6293
REMARK 3 T33: 0.6398 T12: 0.1002
REMARK 3 T13: 0.1979 T23: 0.0279
REMARK 3 L TENSOR
REMARK 3 L11: 4.7445 L22: 4.1031
REMARK 3 L33: 1.7586 L12: -1.1165
REMARK 3 L13: -0.4241 L23: 0.4511
REMARK 3 S TENSOR
REMARK 3 S11: -0.0597 S12: -0.3501 S13: -0.3104
REMARK 3 S21: 0.1780 S22: 0.3577 S23: -0.1815
REMARK 3 S31: 0.3864 S32: 0.1749 S33: -0.3249
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 4Q9J COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-MAY-14.
REMARK 100 THE DEPOSITION ID IS D_1000085774.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-OCT-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CLSI
REMARK 200 BEAMLINE : 08ID-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97942
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX-300
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.20
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26969
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.600
REMARK 200 RESOLUTION RANGE LOW (A) : 88.740
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.4
REMARK 200 DATA REDUNDANCY : 4.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.07900
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.79
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.5
REMARK 200 DATA REDUNDANCY IN SHELL : 4.30
REMARK 200 R MERGE FOR SHELL (I) : 0.64900
REMARK 200 R SYM FOR SHELL (I) : 0.64900
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.100
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 (%): 70.13
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.12
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 600, LI2O4S, HEPES, EDTA, PH 7,
REMARK 280 VAPOR DIFFUSION, TEMPERATURE 277.15K
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 44.37000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 94.99500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 69.33000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 94.99500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 44.37000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 69.33000
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 APPLY THE FOLLOWING TO CHAINS: A, C, D, 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 400
REMARK 400 COMPOUND
REMARK 400
REMARK 400 THE CYCLIC-TRIS-VALINYLSELENAZOLE IS PEPTIDE-LIKE, A MEMBER OF
REMARK 400 INHIBITOR CLASS.
REMARK 400
REMARK 400 GROUP: 1
REMARK 400 NAME: CYCLIC-TRIS-VALINYLSELENAZOLE
REMARK 400 CHAIN: C, D, B
REMARK 400 COMPONENT_1: PEPTIDE LIKE POLYMER
REMARK 400 DESCRIPTION: NULL
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 1
REMARK 465 GLU A 2
REMARK 465 LEU A 3
REMARK 465 GLU A 4
REMARK 465 GLU A 5
REMARK 465 ASP A 6
REMARK 465 LEU A 7
REMARK 465 LYS A 8
REMARK 465 GLY A 9
REMARK 465 ARG A 10
REMARK 465 ALA A 11
REMARK 465 ASP A 12
REMARK 465 LYS A 13
REMARK 465 ASN A 14
REMARK 465 PHE A 15
REMARK 465 SER A 16
REMARK 465 LYS A 17
REMARK 465 MET A 18
REMARK 465 GLY A 19
REMARK 465 LYS A 20
REMARK 465 LYS A 21
REMARK 465 SER A 22
REMARK 465 LYS A 23
REMARK 465 LYS A 24
REMARK 465 GLU A 25
REMARK 465 LYS A 26
REMARK 465 LYS A 27
REMARK 465 GLU A 28
REMARK 465 LYS A 29
REMARK 465 ALA A 627
REMARK 465 GLY A 628
REMARK 465 ASN A 629
REMARK 465 GLU A 630
REMARK 465 ILE A 631
REMARK 465 GLU A 632
REMARK 465 LEU A 633
REMARK 465 GLY A 634
REMARK 465 ASN A 635
REMARK 465 GLU A 636
REMARK 465 ALA A 637
REMARK 465 CYS A 638
REMARK 465 LYS A 639
REMARK 465 SER A 640
REMARK 465 LYS A 641
REMARK 465 ASP A 642
REMARK 465 GLU A 643
REMARK 465 ILE A 644
REMARK 465 ASP A 645
REMARK 465 ASN A 646
REMARK 465 LEU A 647
REMARK 465 ASP A 648
REMARK 465 MET A 649
REMARK 465 SER A 650
REMARK 465 SER A 651
REMARK 465 LYS A 652
REMARK 465 ASP A 653
REMARK 465 SER A 654
REMARK 465 GLY A 655
REMARK 465 SER A 656
REMARK 465 SER A 657
REMARK 465 LEU A 658
REMARK 465 ILE A 659
REMARK 465 ARG A 660
REMARK 465 ARG A 661
REMARK 465 ARG A 662
REMARK 465 SER A 663
REMARK 465 THR A 664
REMARK 465 ARG A 665
REMARK 465 LYS A 666
REMARK 465 SER A 667
REMARK 465 ILE A 668
REMARK 465 CYS A 669
REMARK 465 GLY A 670
REMARK 465 PRO A 671
REMARK 465 HIS A 672
REMARK 465 ASP A 673
REMARK 465 GLN A 674
REMARK 465 ASP A 675
REMARK 465 ARG A 676
REMARK 465 LYS A 677
REMARK 465 LEU A 678
REMARK 465 SER A 679
REMARK 465 THR A 680
REMARK 465 LYS A 681
REMARK 465 GLU A 682
REMARK 465 ALA A 683
REMARK 465 LEU A 684
REMARK 465 ASP A 685
REMARK 465 GLU A 686
REMARK 465 ASP A 687
REMARK 465 VAL A 688
REMARK 465 HIS A 1279
REMARK 465 HIS A 1280
REMARK 465 HIS A 1281
REMARK 465 HIS A 1282
REMARK 465 HIS A 1283
REMARK 465 HIS A 1284
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 OD2 ASP A 801 OH TYR A 1083 2.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 VAL C 2 N - CA - CB ANGL. DEV. = -19.1 DEGREES
REMARK 500 VAL C 2 CA - CB - CG1 ANGL. DEV. = 11.1 DEGREES
REMARK 500 VAL C 4 CA - CB - CG1 ANGL. DEV. = 11.9 DEGREES
REMARK 500 VAL C 4 N - CA - C ANGL. DEV. = -22.1 DEGREES
REMARK 500 VAL D 4 CA - CB - CG2 ANGL. DEV. = 10.7 DEGREES
REMARK 500 VAL D 4 CA - C - N ANGL. DEV. = 13.9 DEGREES
REMARK 500 VAL B 4 CA - CB - CG2 ANGL. DEV. = 12.0 DEGREES
REMARK 500 VAL B 4 CA - C - N ANGL. DEV. = 13.5 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 TRP A 44 -107.12 54.49
REMARK 500 SER A 88 -79.34 -69.94
REMARK 500 GLN A 90 -64.31 -136.70
REMARK 500 ARG A 97 -71.88 -104.32
REMARK 500 GLN A 128 -70.04 -46.49
REMARK 500 PRO A 219 40.20 -74.60
REMARK 500 VAL A 220 -58.95 -143.92
REMARK 500 ASP A 372 -104.78 60.14
REMARK 500 SER A 373 -10.13 90.74
REMARK 500 PRO A 398 39.34 -66.92
REMARK 500 ARG A 400 -138.51 64.21
REMARK 500 LEU A 409 143.24 -174.94
REMARK 500 ASP A 450 -130.31 57.54
REMARK 500 HIS A 514 -4.42 70.19
REMARK 500 GLN A 515 -135.76 57.26
REMARK 500 ARG A 573 -153.98 -88.93
REMARK 500 GLU A 574 -18.04 80.11
REMARK 500 VAL A 603 -75.76 -129.80
REMARK 500 TYR A 706 -16.04 70.66
REMARK 500 LEU A 768 -70.99 -59.75
REMARK 500 GLN A 852 -9.48 64.25
REMARK 500 THR A 907 -137.27 55.80
REMARK 500 TYR A 958 -108.03 59.04
REMARK 500 PRO A1044 42.86 -81.97
REMARK 500 SER A1045 -78.15 -108.86
REMARK 500 LEU A1092 -63.39 -120.07
REMARK 500 CYS A1121 179.66 177.77
REMARK 500 SER A1133 -0.74 69.48
REMARK 500 LYS A1160 -133.98 56.23
REMARK 500 ASP A1167 -13.07 78.52
REMARK 500 THR A1204 -133.63 42.02
REMARK 500 GLU A1219 -17.57 74.86
REMARK 500 LYS A1248 -63.38 -95.28
REMARK 500 VAL C 4 -73.44 -94.70
REMARK 500 VAL D 2 -15.08 -150.15
REMARK 500 VAL D 4 -62.67 -90.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 THE PLACEMENT OF THE BOUND CYCLIC-TRIS-VALINYLSELENAZOLE PEPTIDE-
REMARK 600 LIKE LIGAND WAS CONFIRMED USING THE ANOMALOUS SCATTERING FROM THE
REMARK 600 INCORPORATED SELENIUMS, SEE PRIMARY CITATION FOR DETAILS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4Q9H RELATED DB: PDB
REMARK 900 RELATED ID: 4Q9I RELATED DB: PDB
REMARK 900 RELATED ID: 4Q9K RELATED DB: PDB
REMARK 900 RELATED ID: 4Q9L RELATED DB: PDB
DBREF 4Q9J A 1 1276 UNP P21447 MDR1A_MOUSE 1 1276
DBREF 4Q9J C 1 6 PDB 4Q9J 4Q9J 1 6
DBREF 4Q9J D 1 6 PDB 4Q9J 4Q9J 1 6
DBREF 4Q9J B 1 6 PDB 4Q9J 4Q9J 1 6
SEQADV 4Q9J GLN A 83 UNP P21447 ASN 83 CONFLICT
SEQADV 4Q9J GLN A 87 UNP P21447 ASN 87 CONFLICT
SEQADV 4Q9J GLN A 90 UNP P21447 ASN 90 CONFLICT
SEQADV 4Q9J LEU A 1277 UNP P21447 EXPRESSION TAG
SEQADV 4Q9J GLU A 1278 UNP P21447 EXPRESSION TAG
SEQADV 4Q9J HIS A 1279 UNP P21447 EXPRESSION TAG
SEQADV 4Q9J HIS A 1280 UNP P21447 EXPRESSION TAG
SEQADV 4Q9J HIS A 1281 UNP P21447 EXPRESSION TAG
SEQADV 4Q9J HIS A 1282 UNP P21447 EXPRESSION TAG
SEQADV 4Q9J HIS A 1283 UNP P21447 EXPRESSION TAG
SEQADV 4Q9J HIS A 1284 UNP P21447 EXPRESSION TAG
SEQRES 1 A 1284 MET GLU LEU GLU GLU ASP LEU LYS GLY ARG ALA ASP LYS
SEQRES 2 A 1284 ASN PHE SER LYS MET GLY LYS LYS SER LYS LYS GLU LYS
SEQRES 3 A 1284 LYS GLU LYS LYS PRO ALA VAL SER VAL LEU THR MET PHE
SEQRES 4 A 1284 ARG TYR ALA GLY TRP LEU ASP ARG LEU TYR MET LEU VAL
SEQRES 5 A 1284 GLY THR LEU ALA ALA ILE ILE HIS GLY VAL ALA LEU PRO
SEQRES 6 A 1284 LEU MET MET LEU ILE PHE GLY ASP MET THR ASP SER PHE
SEQRES 7 A 1284 ALA SER VAL GLY GLN VAL SER LYS GLN SER THR GLN MET
SEQRES 8 A 1284 SER GLU ALA ASP LYS ARG ALA MET PHE ALA LYS LEU GLU
SEQRES 9 A 1284 GLU GLU MET THR THR TYR ALA TYR TYR TYR THR GLY ILE
SEQRES 10 A 1284 GLY ALA GLY VAL LEU ILE VAL ALA TYR ILE GLN VAL SER
SEQRES 11 A 1284 PHE TRP CYS LEU ALA ALA GLY ARG GLN ILE HIS LYS ILE
SEQRES 12 A 1284 ARG GLN LYS PHE PHE HIS ALA ILE MET ASN GLN GLU ILE
SEQRES 13 A 1284 GLY TRP PHE ASP VAL HIS ASP VAL GLY GLU LEU ASN THR
SEQRES 14 A 1284 ARG LEU THR ASP ASP VAL SER LYS ILE ASN GLU GLY ILE
SEQRES 15 A 1284 GLY ASP LYS ILE GLY MET PHE PHE GLN ALA MET ALA THR
SEQRES 16 A 1284 PHE PHE GLY GLY PHE ILE ILE GLY PHE THR ARG GLY TRP
SEQRES 17 A 1284 LYS LEU THR LEU VAL ILE LEU ALA ILE SER PRO VAL LEU
SEQRES 18 A 1284 GLY LEU SER ALA GLY ILE TRP ALA LYS ILE LEU SER SER
SEQRES 19 A 1284 PHE THR ASP LYS GLU LEU HIS ALA TYR ALA LYS ALA GLY
SEQRES 20 A 1284 ALA VAL ALA GLU GLU VAL LEU ALA ALA ILE ARG THR VAL
SEQRES 21 A 1284 ILE ALA PHE GLY GLY GLN LYS LYS GLU LEU GLU ARG TYR
SEQRES 22 A 1284 ASN ASN ASN LEU GLU GLU ALA LYS ARG LEU GLY ILE LYS
SEQRES 23 A 1284 LYS ALA ILE THR ALA ASN ILE SER MET GLY ALA ALA PHE
SEQRES 24 A 1284 LEU LEU ILE TYR ALA SER TYR ALA LEU ALA PHE TRP TYR
SEQRES 25 A 1284 GLY THR SER LEU VAL ILE SER LYS GLU TYR SER ILE GLY
SEQRES 26 A 1284 GLN VAL LEU THR VAL PHE PHE SER VAL LEU ILE GLY ALA
SEQRES 27 A 1284 PHE SER VAL GLY GLN ALA SER PRO ASN ILE GLU ALA PHE
SEQRES 28 A 1284 ALA ASN ALA ARG GLY ALA ALA TYR GLU VAL PHE LYS ILE
SEQRES 29 A 1284 ILE ASP ASN LYS PRO SER ILE ASP SER PHE SER LYS SER
SEQRES 30 A 1284 GLY HIS LYS PRO ASP ASN ILE GLN GLY ASN LEU GLU PHE
SEQRES 31 A 1284 LYS ASN ILE HIS PHE SER TYR PRO SER ARG LYS GLU VAL
SEQRES 32 A 1284 GLN ILE LEU LYS GLY LEU ASN LEU LYS VAL LYS SER GLY
SEQRES 33 A 1284 GLN THR VAL ALA LEU VAL GLY ASN SER GLY CYS GLY LYS
SEQRES 34 A 1284 SER THR THR VAL GLN LEU MET GLN ARG LEU TYR ASP PRO
SEQRES 35 A 1284 LEU ASP GLY MET VAL SER ILE ASP GLY GLN ASP ILE ARG
SEQRES 36 A 1284 THR ILE ASN VAL ARG TYR LEU ARG GLU ILE ILE GLY VAL
SEQRES 37 A 1284 VAL SER GLN GLU PRO VAL LEU PHE ALA THR THR ILE ALA
SEQRES 38 A 1284 GLU ASN ILE ARG TYR GLY ARG GLU ASP VAL THR MET ASP
SEQRES 39 A 1284 GLU ILE GLU LYS ALA VAL LYS GLU ALA ASN ALA TYR ASP
SEQRES 40 A 1284 PHE ILE MET LYS LEU PRO HIS GLN PHE ASP THR LEU VAL
SEQRES 41 A 1284 GLY GLU ARG GLY ALA GLN LEU SER GLY GLY GLN LYS GLN
SEQRES 42 A 1284 ARG ILE ALA ILE ALA ARG ALA LEU VAL ARG ASN PRO LYS
SEQRES 43 A 1284 ILE LEU LEU LEU ASP GLU ALA THR SER ALA LEU ASP THR
SEQRES 44 A 1284 GLU SER GLU ALA VAL VAL GLN ALA ALA LEU ASP LYS ALA
SEQRES 45 A 1284 ARG GLU GLY ARG THR THR ILE VAL ILE ALA HIS ARG LEU
SEQRES 46 A 1284 SER THR VAL ARG ASN ALA ASP VAL ILE ALA GLY PHE ASP
SEQRES 47 A 1284 GLY GLY VAL ILE VAL GLU GLN GLY ASN HIS ASP GLU LEU
SEQRES 48 A 1284 MET ARG GLU LYS GLY ILE TYR PHE LYS LEU VAL MET THR
SEQRES 49 A 1284 GLN THR ALA GLY ASN GLU ILE GLU LEU GLY ASN GLU ALA
SEQRES 50 A 1284 CYS LYS SER LYS ASP GLU ILE ASP ASN LEU ASP MET SER
SEQRES 51 A 1284 SER LYS ASP SER GLY SER SER LEU ILE ARG ARG ARG SER
SEQRES 52 A 1284 THR ARG LYS SER ILE CYS GLY PRO HIS ASP GLN ASP ARG
SEQRES 53 A 1284 LYS LEU SER THR LYS GLU ALA LEU ASP GLU ASP VAL PRO
SEQRES 54 A 1284 PRO ALA SER PHE TRP ARG ILE LEU LYS LEU ASN SER THR
SEQRES 55 A 1284 GLU TRP PRO TYR PHE VAL VAL GLY ILE PHE CYS ALA ILE
SEQRES 56 A 1284 ILE ASN GLY GLY LEU GLN PRO ALA PHE SER VAL ILE PHE
SEQRES 57 A 1284 SER LYS VAL VAL GLY VAL PHE THR ASN GLY GLY PRO PRO
SEQRES 58 A 1284 GLU THR GLN ARG GLN ASN SER ASN LEU PHE SER LEU LEU
SEQRES 59 A 1284 PHE LEU ILE LEU GLY ILE ILE SER PHE ILE THR PHE PHE
SEQRES 60 A 1284 LEU GLN GLY PHE THR PHE GLY LYS ALA GLY GLU ILE LEU
SEQRES 61 A 1284 THR LYS ARG LEU ARG TYR MET VAL PHE LYS SER MET LEU
SEQRES 62 A 1284 ARG GLN ASP VAL SER TRP PHE ASP ASP PRO LYS ASN THR
SEQRES 63 A 1284 THR GLY ALA LEU THR THR ARG LEU ALA ASN ASP ALA ALA
SEQRES 64 A 1284 GLN VAL LYS GLY ALA THR GLY SER ARG LEU ALA VAL ILE
SEQRES 65 A 1284 PHE GLN ASN ILE ALA ASN LEU GLY THR GLY ILE ILE ILE
SEQRES 66 A 1284 SER LEU ILE TYR GLY TRP GLN LEU THR LEU LEU LEU LEU
SEQRES 67 A 1284 ALA ILE VAL PRO ILE ILE ALA ILE ALA GLY VAL VAL GLU
SEQRES 68 A 1284 MET LYS MET LEU SER GLY GLN ALA LEU LYS ASP LYS LYS
SEQRES 69 A 1284 GLU LEU GLU GLY SER GLY LYS ILE ALA THR GLU ALA ILE
SEQRES 70 A 1284 GLU ASN PHE ARG THR VAL VAL SER LEU THR ARG GLU GLN
SEQRES 71 A 1284 LYS PHE GLU THR MET TYR ALA GLN SER LEU GLN ILE PRO
SEQRES 72 A 1284 TYR ARG ASN ALA MET LYS LYS ALA HIS VAL PHE GLY ILE
SEQRES 73 A 1284 THR PHE SER PHE THR GLN ALA MET MET TYR PHE SER TYR
SEQRES 74 A 1284 ALA ALA CYS PHE ARG PHE GLY ALA TYR LEU VAL THR GLN
SEQRES 75 A 1284 GLN LEU MET THR PHE GLU ASN VAL LEU LEU VAL PHE SER
SEQRES 76 A 1284 ALA ILE VAL PHE GLY ALA MET ALA VAL GLY GLN VAL SER
SEQRES 77 A 1284 SER PHE ALA PRO ASP TYR ALA LYS ALA THR VAL SER ALA
SEQRES 78 A 1284 SER HIS ILE ILE ARG ILE ILE GLU LYS THR PRO GLU ILE
SEQRES 79 A 1284 ASP SER TYR SER THR GLN GLY LEU LYS PRO ASN MET LEU
SEQRES 80 A 1284 GLU GLY ASN VAL GLN PHE SER GLY VAL VAL PHE ASN TYR
SEQRES 81 A 1284 PRO THR ARG PRO SER ILE PRO VAL LEU GLN GLY LEU SER
SEQRES 82 A 1284 LEU GLU VAL LYS LYS GLY GLN THR LEU ALA LEU VAL GLY
SEQRES 83 A 1284 SER SER GLY CYS GLY LYS SER THR VAL VAL GLN LEU LEU
SEQRES 84 A 1284 GLU ARG PHE TYR ASP PRO MET ALA GLY SER VAL PHE LEU
SEQRES 85 A 1284 ASP GLY LYS GLU ILE LYS GLN LEU ASN VAL GLN TRP LEU
SEQRES 86 A 1284 ARG ALA GLN LEU GLY ILE VAL SER GLN GLU PRO ILE LEU
SEQRES 87 A 1284 PHE ASP CYS SER ILE ALA GLU ASN ILE ALA TYR GLY ASP
SEQRES 88 A 1284 ASN SER ARG VAL VAL SER TYR GLU GLU ILE VAL ARG ALA
SEQRES 89 A 1284 ALA LYS GLU ALA ASN ILE HIS GLN PHE ILE ASP SER LEU
SEQRES 90 A 1284 PRO ASP LYS TYR ASN THR ARG VAL GLY ASP LYS GLY THR
SEQRES 91 A 1284 GLN LEU SER GLY GLY GLN LYS GLN ARG ILE ALA ILE ALA
SEQRES 92 A 1284 ARG ALA LEU VAL ARG GLN PRO HIS ILE LEU LEU LEU ASP
SEQRES 93 A 1284 GLU ALA THR SER ALA LEU ASP THR GLU SER GLU LYS VAL
SEQRES 94 A 1284 VAL GLN GLU ALA LEU ASP LYS ALA ARG GLU GLY ARG THR
SEQRES 95 A 1284 CYS ILE VAL ILE ALA HIS ARG LEU SER THR ILE GLN ASN
SEQRES 96 A 1284 ALA ASP LEU ILE VAL VAL ILE GLN ASN GLY LYS VAL LYS
SEQRES 97 A 1284 GLU HIS GLY THR HIS GLN GLN LEU LEU ALA GLN LYS GLY
SEQRES 98 A 1284 ILE TYR PHE SER MET VAL SER VAL GLN ALA GLY ALA LYS
SEQRES 99 A 1284 ARG SER LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 C 6 30F VAL 30F VAL 30F VAL
SEQRES 1 D 6 30F VAL 30F VAL 30F VAL
SEQRES 1 B 6 30F VAL 30F VAL 30F VAL
MODRES 4Q9J 30F C 1 SEC (2Z)-2-AMINO-3-SELANYLPROP-2-ENOIC ACID
MODRES 4Q9J 30F C 3 SEC (2Z)-2-AMINO-3-SELANYLPROP-2-ENOIC ACID
MODRES 4Q9J 30F C 5 SEC (2Z)-2-AMINO-3-SELANYLPROP-2-ENOIC ACID
MODRES 4Q9J 30F D 1 SEC (2Z)-2-AMINO-3-SELANYLPROP-2-ENOIC ACID
MODRES 4Q9J 30F D 3 SEC (2Z)-2-AMINO-3-SELANYLPROP-2-ENOIC ACID
MODRES 4Q9J 30F D 5 SEC (2Z)-2-AMINO-3-SELANYLPROP-2-ENOIC ACID
MODRES 4Q9J 30F B 1 SEC (2Z)-2-AMINO-3-SELANYLPROP-2-ENOIC ACID
MODRES 4Q9J 30F B 3 SEC (2Z)-2-AMINO-3-SELANYLPROP-2-ENOIC ACID
MODRES 4Q9J 30F B 5 SEC (2Z)-2-AMINO-3-SELANYLPROP-2-ENOIC ACID
HET 30F C 1 6
HET 30F C 3 6
HET 30F C 5 6
HET 30F D 1 6
HET 30F D 3 6
HET 30F D 5 6
HET 30F B 1 6
HET 30F B 3 6
HET 30F B 5 6
HETNAM 30F (2Z)-2-AMINO-3-SELANYLPROP-2-ENOIC ACID
FORMUL 2 30F 9(C3 H5 N O2 SE)
HELIX 1 1 LEU A 36 ARG A 40 5 5
HELIX 2 2 TRP A 44 SER A 88 1 45
HELIX 3 3 SER A 92 LYS A 96 5 5
HELIX 4 4 ARG A 97 GLN A 154 1 58
HELIX 5 5 GLU A 155 VAL A 161 1 7
HELIX 6 6 ASP A 163 GLY A 183 1 21
HELIX 7 7 ASP A 184 GLY A 207 1 24
HELIX 8 8 TRP A 208 ILE A 217 1 10
HELIX 9 9 ILE A 217 LEU A 232 1 16
HELIX 10 10 GLU A 239 ALA A 256 1 18
HELIX 11 11 ALA A 256 PHE A 263 1 8
HELIX 12 12 GLY A 265 SER A 319 1 55
HELIX 13 13 SER A 323 ASN A 367 1 45
HELIX 14 14 SER A 399 VAL A 403 5 5
HELIX 15 15 CYS A 427 GLN A 437 1 11
HELIX 16 16 ASN A 458 ILE A 465 1 8
HELIX 17 17 THR A 479 TYR A 486 1 8
HELIX 18 18 THR A 492 ALA A 503 1 12
HELIX 19 19 ALA A 505 LEU A 512 1 8
HELIX 20 20 HIS A 514 THR A 518 5 5
HELIX 21 21 SER A 528 ARG A 543 1 16
HELIX 22 22 ASP A 558 ARG A 573 1 16
HELIX 23 23 ASN A 607 LYS A 615 1 9
HELIX 24 24 GLY A 616 GLN A 625 1 10
HELIX 25 25 TRP A 694 SER A 701 1 8
HELIX 26 26 PHE A 707 ASN A 737 1 31
HELIX 27 27 PRO A 740 GLU A 742 5 3
HELIX 28 28 THR A 743 GLN A 795 1 53
HELIX 29 29 ASP A 796 ASP A 801 1 6
HELIX 30 30 THR A 806 GLY A 826 1 21
HELIX 31 31 GLY A 826 GLY A 850 1 25
HELIX 32 32 GLN A 852 ASN A 899 1 48
HELIX 33 33 ASN A 899 THR A 907 1 9
HELIX 34 34 ARG A 908 ALA A 957 1 50
HELIX 35 35 THR A 966 PHE A 990 1 25
HELIX 36 36 PHE A 990 LYS A 1010 1 21
HELIX 37 37 CYS A 1070 GLU A 1080 1 11
HELIX 38 38 ASN A 1101 GLN A 1108 1 8
HELIX 39 39 ILE A 1123 ALA A 1128 1 6
HELIX 40 40 TYR A 1129 ASP A 1131 5 3
HELIX 41 41 SER A 1137 ALA A 1148 1 12
HELIX 42 42 ILE A 1150 ASP A 1155 1 6
HELIX 43 43 ASP A 1159 ASN A 1162 5 4
HELIX 44 44 SER A 1173 ARG A 1188 1 16
HELIX 45 45 ASP A 1203 ARG A 1218 1 16
HELIX 46 46 ARG A 1229 ILE A 1233 5 5
HELIX 47 47 THR A 1252 GLN A 1259 1 8
HELIX 48 48 GLY A 1261 LEU A 1277 1 17
SHEET 1 A 4 ASN A 410 VAL A 413 0
SHEET 2 A 4 LEU A 388 HIS A 394 -1 N PHE A 390 O LEU A 411
SHEET 3 A 4 ASP A 444 ILE A 449 -1 O SER A 448 N GLU A 389
SHEET 4 A 4 GLN A 452 ASP A 453 -1 O GLN A 452 N ILE A 449
SHEET 1 B 6 ILE A 466 VAL A 469 0
SHEET 2 B 6 ILE A 547 ASP A 551 1 O ILE A 547 N GLY A 467
SHEET 3 B 6 THR A 577 ILE A 581 1 O ILE A 581 N LEU A 550
SHEET 4 B 6 THR A 418 VAL A 422 1 N VAL A 419 O VAL A 580
SHEET 5 B 6 VAL A 593 ASP A 598 1 O ALA A 595 N VAL A 422
SHEET 6 B 6 VAL A 601 GLY A 606 -1 O VAL A 603 N GLY A 596
SHEET 1 C 3 LEU A1049 VAL A1056 0
SHEET 2 C 3 VAL A1031 PHE A1038 -1 N PHE A1033 O LEU A1054
SHEET 3 C 3 ALA A1087 PHE A1091 -1 O ALA A1087 N VAL A1037
SHEET 1 D 6 LEU A1109 VAL A1112 0
SHEET 2 D 6 ILE A1192 LEU A1195 1 O ILE A1192 N GLY A1110
SHEET 3 D 6 THR A1222 VAL A1225 1 O THR A1222 N LEU A1193
SHEET 4 D 6 THR A1061 GLY A1066 1 N LEU A1062 O CYS A1223
SHEET 5 D 6 LEU A1238 GLN A1243 1 O ILE A1242 N VAL A1065
SHEET 6 D 6 LYS A1246 GLY A1251 -1 O GLU A1249 N VAL A1241
SHEET 1 E 2 CYS A1121 SER A1122 0
SHEET 2 E 2 ARG A1164 VAL A1165 -1 O VAL A1165 N CYS A1121
LINK C 30F C 1 N VAL C 2 1555 1555 1.42
LINK SE2 30F C 1 C VAL C 6 1555 1555 1.89
LINK N 30F C 1 C VAL C 6 1555 1555 1.37
LINK C VAL C 2 N 30F C 3 1555 1555 1.38
LINK C VAL C 2 SE2 30F C 3 1555 1555 1.89
LINK C 30F C 3 N VAL C 4 1555 1555 1.41
LINK C VAL C 4 SE2 30F C 5 1555 1555 1.89
LINK C VAL C 4 N 30F C 5 1555 1555 1.41
LINK C 30F C 5 N VAL C 6 1555 1555 1.42
LINK C 30F D 1 N VAL D 2 1555 1555 1.43
LINK SE2 30F D 1 C VAL D 6 1555 1555 1.89
LINK N 30F D 1 C VAL D 6 1555 1555 1.39
LINK C VAL D 2 N 30F D 3 1555 1555 1.38
LINK C VAL D 2 SE2 30F D 3 1555 1555 1.88
LINK C 30F D 3 N VAL D 4 1555 1555 1.40
LINK C VAL D 4 SE2 30F D 5 1555 1555 1.88
LINK C VAL D 4 N 30F D 5 1555 1555 1.42
LINK C 30F D 5 N VAL D 6 1555 1555 1.42
LINK C 30F B 1 N VAL B 2 1555 1555 1.43
LINK SE2 30F B 1 C VAL B 6 1555 1555 1.89
LINK N 30F B 1 C VAL B 6 1555 1555 1.40
LINK C VAL B 2 N 30F B 3 1555 1555 1.38
LINK C VAL B 2 SE2 30F B 3 1555 1555 1.87
LINK C 30F B 3 N VAL B 4 1555 1555 1.41
LINK C VAL B 4 SE2 30F B 5 1555 1555 1.88
LINK C VAL B 4 N 30F B 5 1555 1555 1.41
LINK C 30F B 5 N VAL B 6 1555 1555 1.41
CRYST1 88.740 138.660 189.990 90.00 90.00 90.00 P 21 21 21 12
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 0.011269 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007212 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005263 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
