HEADER HYDROLASE 01-JUL-16 5KOY
TITLE MOUSE PGP 34 LINKER DELETED BOUND WITH ATP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MULTIDRUG RESISTANCE PROTEIN 1A;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: ATP-BINDING CASSETTE SUB-FAMILY B MEMBER 1A,MDR1A,MULTIDRUG
COMPND 5 RESISTANCE PROTEIN 3,P-GLYCOPROTEIN 3;
COMPND 6 EC: 3.6.3.44;
COMPND 7 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: KOMAGATAELLA PHAFFII GS115;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 644223
KEYWDS MOUSE PGP, MULTIDRUG RESISTANCE, DRUG TRANSPORT, ATP BOUND, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.XIA,L.ESSER,F.ZHOU
REVDAT 3 04-OCT-23 5KOY 1 REMARK
REVDAT 2 25-JAN-17 5KOY 1 JRNL
REVDAT 1 14-DEC-16 5KOY 0
JRNL AUTH L.ESSER,F.ZHOU,K.M.PLUCHINO,J.SHILOACH,J.MA,W.K.TANG,
JRNL AUTH 2 C.GUTIERREZ,A.ZHANG,S.SHUKLA,J.P.MADIGAN,T.ZHOU,P.D.KWONG,
JRNL AUTH 3 S.V.AMBUDKAR,M.M.GOTTESMAN,D.XIA
JRNL TITL STRUCTURES OF THE MULTIDRUG TRANSPORTER P-GLYCOPROTEIN
JRNL TITL 2 REVEAL ASYMMETRIC ATP BINDING AND THE MECHANISM OF
JRNL TITL 3 POLYSPECIFICITY.
JRNL REF J. BIOL. CHEM. V. 292 446 2017
JRNL REFN ESSN 1083-351X
JRNL PMID 27864369
JRNL DOI 10.1074/JBC.M116.755884
REMARK 2
REMARK 2 RESOLUTION. 3.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.11.1_2575
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) : 3.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 21.30
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 41144
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.248
REMARK 3 R VALUE (WORKING SET) : 0.246
REMARK 3 FREE R VALUE : 0.289
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.740
REMARK 3 FREE R VALUE TEST SET COUNT : 1951
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 21.3019 - 9.0533 1.00 2959 148 0.2064 0.2606
REMARK 3 2 9.0533 - 7.2799 1.00 2868 143 0.2190 0.2322
REMARK 3 3 7.2799 - 6.3881 1.00 2849 142 0.2562 0.3091
REMARK 3 4 6.3881 - 5.8171 1.00 2788 138 0.2781 0.3209
REMARK 3 5 5.8171 - 5.4074 1.00 2797 140 0.2787 0.3307
REMARK 3 6 5.4074 - 5.0932 1.00 2808 140 0.2580 0.3138
REMARK 3 7 5.0932 - 4.8413 1.00 2776 137 0.2417 0.2836
REMARK 3 8 4.8413 - 4.6328 1.00 2771 139 0.2417 0.2903
REMARK 3 9 4.6328 - 4.4561 1.00 2773 137 0.2507 0.2682
REMARK 3 10 4.4561 - 4.3036 1.00 2764 139 0.2617 0.3232
REMARK 3 11 4.3036 - 4.1701 1.00 2771 137 0.2801 0.3118
REMARK 3 12 4.1701 - 4.0517 1.00 2769 138 0.3063 0.3279
REMARK 3 13 4.0517 - 3.9458 1.00 2757 137 0.3275 0.3600
REMARK 3 14 3.9458 - 3.8501 1.00 2743 136 0.3476 0.3957
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) : 0.600
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.970
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 150.4
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 : 0.007 18724
REMARK 3 ANGLE : 1.031 25329
REMARK 3 CHIRALITY : 0.054 2916
REMARK 3 PLANARITY : 0.006 3207
REMARK 3 DIHEDRAL : 13.467 11149
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 32
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN A AND RESID 31:81)
REMARK 3 ORIGIN FOR THE GROUP (A): 40.2499 58.4524 5.6137
REMARK 3 T TENSOR
REMARK 3 T11: 0.7864 T22: 1.2917
REMARK 3 T33: 1.3801 T12: -0.0041
REMARK 3 T13: 0.4092 T23: -0.8343
REMARK 3 L TENSOR
REMARK 3 L11: 0.9300 L22: 2.4047
REMARK 3 L33: 5.2061 L12: -0.3913
REMARK 3 L13: -1.2542 L23: -2.6344
REMARK 3 S TENSOR
REMARK 3 S11: -0.3189 S12: 1.1332 S13: -0.6194
REMARK 3 S21: 0.5882 S22: -0.1550 S23: 0.8097
REMARK 3 S31: 0.1970 S32: 0.7497 S33: -1.5144
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN A AND RESID 82:99)
REMARK 3 ORIGIN FOR THE GROUP (A): 19.9782 25.9085 -17.5505
REMARK 3 T TENSOR
REMARK 3 T11: 2.9981 T22: 1.4902
REMARK 3 T33: 2.0830 T12: -0.2849
REMARK 3 T13: 0.8787 T23: -0.5272
REMARK 3 L TENSOR
REMARK 3 L11: 7.6285 L22: 1.5076
REMARK 3 L33: 5.6036 L12: -1.0687
REMARK 3 L13: 6.5259 L23: -0.8059
REMARK 3 S TENSOR
REMARK 3 S11: 1.8824 S12: -0.3131 S13: -0.3699
REMARK 3 S21: 1.3231 S22: 0.0659 S23: 0.2169
REMARK 3 S31: 1.7086 S32: 0.5816 S33: 2.8812
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN A AND RESID 100:203)
REMARK 3 ORIGIN FOR THE GROUP (A): 38.4609 64.5451 15.5907
REMARK 3 T TENSOR
REMARK 3 T11: 1.6365 T22: 1.3804
REMARK 3 T33: 1.4498 T12: -0.2008
REMARK 3 T13: 0.2255 T23: -0.3001
REMARK 3 L TENSOR
REMARK 3 L11: 0.4605 L22: 1.4338
REMARK 3 L33: 0.9161 L12: -0.4899
REMARK 3 L13: -0.6686 L23: 1.7281
REMARK 3 S TENSOR
REMARK 3 S11: 0.1154 S12: 0.1041 S13: -0.3935
REMARK 3 S21: -0.3137 S22: -0.3544 S23: -0.4797
REMARK 3 S31: 0.1567 S32: 0.5625 S33: -0.2844
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN A AND RESID 204:237)
REMARK 3 ORIGIN FOR THE GROUP (A): 23.3037 70.3015 -6.2528
REMARK 3 T TENSOR
REMARK 3 T11: 2.6536 T22: 1.0910
REMARK 3 T33: 0.7584 T12: -1.0888
REMARK 3 T13: 0.1349 T23: 0.3724
REMARK 3 L TENSOR
REMARK 3 L11: 7.6170 L22: 5.9401
REMARK 3 L33: 3.9782 L12: -1.9482
REMARK 3 L13: -4.2354 L23: 0.6068
REMARK 3 S TENSOR
REMARK 3 S11: -0.6201 S12: -0.7872 S13: 0.8171
REMARK 3 S21: 1.4565 S22: 0.7315 S23: 0.6638
REMARK 3 S31: 0.8357 S32: -0.3529 S33: -2.5891
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: (CHAIN A AND RESID 238:327)
REMARK 3 ORIGIN FOR THE GROUP (A): 9.4522 76.4014 9.6034
REMARK 3 T TENSOR
REMARK 3 T11: 2.0203 T22: 1.3174
REMARK 3 T33: 1.5764 T12: -0.0855
REMARK 3 T13: 0.3048 T23: -0.1066
REMARK 3 L TENSOR
REMARK 3 L11: 1.6373 L22: 4.5412
REMARK 3 L33: 5.8886 L12: -2.7332
REMARK 3 L13: -3.0248 L23: 5.7248
REMARK 3 S TENSOR
REMARK 3 S11: 0.9064 S12: 1.1034 S13: -0.6229
REMARK 3 S21: -2.3228 S22: -1.2262 S23: 0.8336
REMARK 3 S31: -2.0454 S32: -1.3311 S33: -0.0080
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: (CHAIN A AND RESID 328:431)
REMARK 3 ORIGIN FOR THE GROUP (A): 44.8909 91.6284 31.0941
REMARK 3 T TENSOR
REMARK 3 T11: 2.4023 T22: 1.8133
REMARK 3 T33: 1.5749 T12: -0.1257
REMARK 3 T13: 0.2691 T23: -0.2443
REMARK 3 L TENSOR
REMARK 3 L11: 2.1055 L22: 0.0491
REMARK 3 L33: 1.7220 L12: -0.0588
REMARK 3 L13: -0.0189 L23: 0.9111
REMARK 3 S TENSOR
REMARK 3 S11: 0.7151 S12: 0.0559 S13: 0.0859
REMARK 3 S21: 0.2964 S22: -0.5682 S23: -0.4994
REMARK 3 S31: -0.0324 S32: -0.0796 S33: -0.0811
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: (CHAIN A AND RESID 432:581)
REMARK 3 ORIGIN FOR THE GROUP (A): 45.1972 90.0411 56.2771
REMARK 3 T TENSOR
REMARK 3 T11: 1.7147 T22: 1.2495
REMARK 3 T33: 1.4355 T12: -0.3927
REMARK 3 T13: -0.0325 T23: -0.2891
REMARK 3 L TENSOR
REMARK 3 L11: 4.1312 L22: 5.6943
REMARK 3 L33: 3.2892 L12: 1.3746
REMARK 3 L13: 0.2555 L23: -0.6104
REMARK 3 S TENSOR
REMARK 3 S11: 0.1036 S12: -0.2865 S13: -0.4509
REMARK 3 S21: -0.1949 S22: 0.2321 S23: -0.1447
REMARK 3 S31: -0.9775 S32: 0.0996 S33: 0.0002
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: (CHAIN A AND RESID 582:731)
REMARK 3 ORIGIN FOR THE GROUP (A): 21.4607 88.3681 35.6637
REMARK 3 T TENSOR
REMARK 3 T11: 1.0962 T22: 0.8712
REMARK 3 T33: 0.5078 T12: -0.2675
REMARK 3 T13: 0.1331 T23: -0.0137
REMARK 3 L TENSOR
REMARK 3 L11: 1.1531 L22: 0.8352
REMARK 3 L33: 1.5055 L12: -0.2897
REMARK 3 L13: 0.1384 L23: 0.7902
REMARK 3 S TENSOR
REMARK 3 S11: -0.3213 S12: 0.1039 S13: 0.1319
REMARK 3 S21: -0.4811 S22: -0.1837 S23: 0.7161
REMARK 3 S31: -0.2084 S32: -0.4560 S33: -0.0006
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: (CHAIN A AND RESID 732:771)
REMARK 3 ORIGIN FOR THE GROUP (A): 9.0096 55.5098 -11.6320
REMARK 3 T TENSOR
REMARK 3 T11: 2.2680 T22: 1.6109
REMARK 3 T33: 1.5533 T12: -0.2206
REMARK 3 T13: -0.1354 T23: -0.5728
REMARK 3 L TENSOR
REMARK 3 L11: 4.8245 L22: 0.4015
REMARK 3 L33: 0.0125 L12: 0.6587
REMARK 3 L13: -0.0594 L23: 0.2684
REMARK 3 S TENSOR
REMARK 3 S11: 0.4877 S12: 1.7370 S13: -0.8836
REMARK 3 S21: -0.7722 S22: -2.4189 S23: 2.0548
REMARK 3 S31: -0.9376 S32: -1.7289 S33: -0.1555
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: (CHAIN A AND RESID 772:883)
REMARK 3 ORIGIN FOR THE GROUP (A): 9.3397 64.3371 21.2236
REMARK 3 T TENSOR
REMARK 3 T11: 1.3147 T22: 1.1984
REMARK 3 T33: 1.7388 T12: -0.4209
REMARK 3 T13: 0.2218 T23: -0.1652
REMARK 3 L TENSOR
REMARK 3 L11: 1.8477 L22: 3.2362
REMARK 3 L33: 4.2092 L12: -2.9220
REMARK 3 L13: -0.2033 L23: 1.5063
REMARK 3 S TENSOR
REMARK 3 S11: 0.0532 S12: 0.0336 S13: -0.2598
REMARK 3 S21: -0.7011 S22: -0.0905 S23: 0.4822
REMARK 3 S31: -0.4825 S32: 0.2445 S33: 0.0000
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: (CHAIN A AND RESID 884:962)
REMARK 3 ORIGIN FOR THE GROUP (A): 36.3347 61.9722 26.5780
REMARK 3 T TENSOR
REMARK 3 T11: 1.0745 T22: 1.1821
REMARK 3 T33: 1.5268 T12: -0.3027
REMARK 3 T13: 0.4503 T23: -0.0899
REMARK 3 L TENSOR
REMARK 3 L11: 0.9984 L22: 1.5263
REMARK 3 L33: 3.1888 L12: -1.1412
REMARK 3 L13: 0.8100 L23: 0.1883
REMARK 3 S TENSOR
REMARK 3 S11: 0.0201 S12: 0.4016 S13: -0.3494
REMARK 3 S21: 1.5457 S22: 0.6971 S23: -0.4835
REMARK 3 S31: 1.3509 S32: 1.0303 S33: 0.0111
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: (CHAIN A AND RESID 963:1017)
REMARK 3 ORIGIN FOR THE GROUP (A): 8.9318 60.0354 16.6752
REMARK 3 T TENSOR
REMARK 3 T11: 2.0380 T22: 1.6248
REMARK 3 T33: 1.7178 T12: -0.0055
REMARK 3 T13: -0.0432 T23: -0.4108
REMARK 3 L TENSOR
REMARK 3 L11: 0.1241 L22: 0.9433
REMARK 3 L33: 2.9541 L12: 0.3629
REMARK 3 L13: 0.7772 L23: 1.2685
REMARK 3 S TENSOR
REMARK 3 S11: 0.0415 S12: 0.2888 S13: -0.9182
REMARK 3 S21: -0.3192 S22: 0.2906 S23: 0.4470
REMARK 3 S31: -0.0882 S32: 0.9220 S33: -0.0002
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: (CHAIN A AND RESID 1018:1136)
REMARK 3 ORIGIN FOR THE GROUP (A): -4.1870 93.0052 52.4332
REMARK 3 T TENSOR
REMARK 3 T11: 1.8815 T22: 1.4927
REMARK 3 T33: 1.7794 T12: -0.2024
REMARK 3 T13: 0.2358 T23: -0.2421
REMARK 3 L TENSOR
REMARK 3 L11: 2.5822 L22: 0.8181
REMARK 3 L33: 2.4187 L12: -1.5349
REMARK 3 L13: -1.3631 L23: 0.0755
REMARK 3 S TENSOR
REMARK 3 S11: 0.3287 S12: -0.8450 S13: -1.6222
REMARK 3 S21: 0.1826 S22: -0.2353 S23: 0.3455
REMARK 3 S31: -0.5576 S32: 0.3814 S33: 0.0757
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: (CHAIN A AND RESID 1137:1226)
REMARK 3 ORIGIN FOR THE GROUP (A): 2.4004 110.4612 44.0290
REMARK 3 T TENSOR
REMARK 3 T11: 1.8732 T22: 0.5271
REMARK 3 T33: 1.0025 T12: -0.3878
REMARK 3 T13: 0.6277 T23: -0.5390
REMARK 3 L TENSOR
REMARK 3 L11: 2.2448 L22: 2.1891
REMARK 3 L33: 5.8164 L12: -0.4425
REMARK 3 L13: 2.1620 L23: -2.9054
REMARK 3 S TENSOR
REMARK 3 S11: 1.4244 S12: 0.0452 S13: -1.1392
REMARK 3 S21: 0.6252 S22: -1.0259 S23: 1.3729
REMARK 3 S31: -0.0610 S32: 1.7880 S33: -0.1676
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: (CHAIN A AND RESID 1227:1234)
REMARK 3 ORIGIN FOR THE GROUP (A): 8.8986 106.9346 62.7163
REMARK 3 T TENSOR
REMARK 3 T11: 2.8312 T22: 1.2979
REMARK 3 T33: 2.5054 T12: -1.8216
REMARK 3 T13: 0.7117 T23: -1.0075
REMARK 3 L TENSOR
REMARK 3 L11: 1.9324 L22: 3.6028
REMARK 3 L33: 1.9120 L12: 0.4676
REMARK 3 L13: 0.4892 L23: 1.0615
REMARK 3 S TENSOR
REMARK 3 S11: -0.3688 S12: 1.1352 S13: -1.6316
REMARK 3 S21: -0.8368 S22: 0.6604 S23: -1.5720
REMARK 3 S31: 0.3413 S32: 0.5054 S33: -1.0900
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: (CHAIN A AND RESID 1235:1272)
REMARK 3 ORIGIN FOR THE GROUP (A): 6.6251 102.0436 72.0769
REMARK 3 T TENSOR
REMARK 3 T11: 1.7411 T22: 1.9944
REMARK 3 T33: 1.3132 T12: 0.0181
REMARK 3 T13: 0.4136 T23: -0.5498
REMARK 3 L TENSOR
REMARK 3 L11: 1.3011 L22: 0.4964
REMARK 3 L33: 0.4139 L12: 0.6454
REMARK 3 L13: 0.4272 L23: -0.1426
REMARK 3 S TENSOR
REMARK 3 S11: 0.7099 S12: -0.3609 S13: 1.1110
REMARK 3 S21: -0.4862 S22: -1.6031 S23: 0.1971
REMARK 3 S31: 0.6161 S32: -0.1069 S33: -0.0118
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: (CHAIN B AND RESID 31:84)
REMARK 3 ORIGIN FOR THE GROUP (A): 25.1002 58.5884 87.2850
REMARK 3 T TENSOR
REMARK 3 T11: 1.3506 T22: 1.5460
REMARK 3 T33: 1.5388 T12: -0.0919
REMARK 3 T13: 0.5415 T23: -0.2925
REMARK 3 L TENSOR
REMARK 3 L11: 0.1088 L22: -0.0892
REMARK 3 L33: 2.1519 L12: 0.2584
REMARK 3 L13: 0.1874 L23: -0.8893
REMARK 3 S TENSOR
REMARK 3 S11: 1.6674 S12: 0.6417 S13: 0.5862
REMARK 3 S21: 0.9443 S22: -0.5523 S23: 0.1689
REMARK 3 S31: -1.3810 S32: -0.4080 S33: 0.0585
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: (CHAIN B AND RESID 85:178)
REMARK 3 ORIGIN FOR THE GROUP (A): 27.4824 56.1536 78.3584
REMARK 3 T TENSOR
REMARK 3 T11: 1.2888 T22: 1.3755
REMARK 3 T33: 1.3307 T12: -0.0157
REMARK 3 T13: -0.0195 T23: 0.3755
REMARK 3 L TENSOR
REMARK 3 L11: 3.5771 L22: 1.6510
REMARK 3 L33: 1.5912 L12: 0.6574
REMARK 3 L13: -1.9511 L23: -0.0727
REMARK 3 S TENSOR
REMARK 3 S11: 0.2632 S12: -0.2775 S13: -0.2130
REMARK 3 S21: 0.2318 S22: 0.1588 S23: -0.0142
REMARK 3 S31: 0.1297 S32: 0.0944 S33: -0.0001
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: (CHAIN B AND RESID 179:230)
REMARK 3 ORIGIN FOR THE GROUP (A): 29.7315 48.0839 94.9359
REMARK 3 T TENSOR
REMARK 3 T11: 1.3531 T22: 1.9049
REMARK 3 T33: 1.5146 T12: -0.2042
REMARK 3 T13: 0.2275 T23: -0.1057
REMARK 3 L TENSOR
REMARK 3 L11: 1.6369 L22: 2.3954
REMARK 3 L33: 3.4564 L12: 1.9294
REMARK 3 L13: -1.1849 L23: -2.4666
REMARK 3 S TENSOR
REMARK 3 S11: -0.0215 S12: 0.3984 S13: 0.2836
REMARK 3 S21: -0.6825 S22: 0.0728 S23: -1.3115
REMARK 3 S31: 1.8601 S32: -0.8296 S33: 0.0076
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: (CHAIN B AND RESID 231:306)
REMARK 3 ORIGIN FOR THE GROUP (A): 49.2286 22.1171 76.7404
REMARK 3 T TENSOR
REMARK 3 T11: 1.7247 T22: 2.3971
REMARK 3 T33: 2.1261 T12: -0.4568
REMARK 3 T13: 0.3604 T23: -0.3159
REMARK 3 L TENSOR
REMARK 3 L11: 3.6484 L22: 3.5369
REMARK 3 L33: 2.2990 L12: -3.9740
REMARK 3 L13: -1.6427 L23: -1.0594
REMARK 3 S TENSOR
REMARK 3 S11: -0.5567 S12: -1.8927 S13: -0.5130
REMARK 3 S21: 0.1460 S22: 0.6429 S23: 1.2217
REMARK 3 S31: -0.9330 S32: 1.7161 S33: 0.1069
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: (CHAIN B AND RESID 307:366)
REMARK 3 ORIGIN FOR THE GROUP (A): 28.9032 47.3815 92.8816
REMARK 3 T TENSOR
REMARK 3 T11: 1.2026 T22: 1.9779
REMARK 3 T33: 1.9345 T12: 0.1050
REMARK 3 T13: 0.2956 T23: 0.4177
REMARK 3 L TENSOR
REMARK 3 L11: 3.3977 L22: 0.3139
REMARK 3 L33: 1.9147 L12: 2.2334
REMARK 3 L13: -3.2257 L23: -1.0136
REMARK 3 S TENSOR
REMARK 3 S11: -0.8639 S12: -1.1017 S13: -1.6153
REMARK 3 S21: -0.0584 S22: -0.2948 S23: -0.3880
REMARK 3 S31: 0.7567 S32: 1.4822 S33: -0.0905
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: (CHAIN B AND RESID 367:510)
REMARK 3 ORIGIN FOR THE GROUP (A): 72.8157 67.6563 51.9829
REMARK 3 T TENSOR
REMARK 3 T11: 1.1733 T22: 1.5595
REMARK 3 T33: 1.4347 T12: -0.1026
REMARK 3 T13: 0.2995 T23: -0.1230
REMARK 3 L TENSOR
REMARK 3 L11: 3.7231 L22: 4.4501
REMARK 3 L33: 6.0312 L12: 1.9007
REMARK 3 L13: 0.9660 L23: 0.2664
REMARK 3 S TENSOR
REMARK 3 S11: -0.0470 S12: -0.3817 S13: 0.2549
REMARK 3 S21: -0.0603 S22: 0.0635 S23: -0.5326
REMARK 3 S31: -0.6346 S32: -0.2564 S33: 0.0002
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: (CHAIN B AND RESID 511:585)
REMARK 3 ORIGIN FOR THE GROUP (A): 68.7355 60.4341 38.4767
REMARK 3 T TENSOR
REMARK 3 T11: 1.2689 T22: 1.3763
REMARK 3 T33: 1.5057 T12: -0.0330
REMARK 3 T13: 0.2272 T23: -0.0345
REMARK 3 L TENSOR
REMARK 3 L11: 3.9719 L22: 0.2502
REMARK 3 L33: 2.0619 L12: -0.2387
REMARK 3 L13: 0.9550 L23: -1.0347
REMARK 3 S TENSOR
REMARK 3 S11: -0.1991 S12: 0.6405 S13: 0.1917
REMARK 3 S21: -0.6492 S22: -0.3568 S23: 0.6539
REMARK 3 S31: -0.4713 S32: -0.0472 S33: 0.0003
REMARK 3 TLS GROUP : 24
REMARK 3 SELECTION: (CHAIN B AND RESID 586:693)
REMARK 3 ORIGIN FOR THE GROUP (A): 85.2987 53.2470 45.1995
REMARK 3 T TENSOR
REMARK 3 T11: 1.6656 T22: 1.9815
REMARK 3 T33: 1.9178 T12: 0.4587
REMARK 3 T13: 0.5605 T23: -0.2335
REMARK 3 L TENSOR
REMARK 3 L11: 1.7097 L22: 0.0690
REMARK 3 L33: 0.1800 L12: 0.5473
REMARK 3 L13: -0.3995 L23: -0.3342
REMARK 3 S TENSOR
REMARK 3 S11: -0.9045 S12: -0.1854 S13: -0.5672
REMARK 3 S21: -0.7699 S22: -0.4010 S23: -0.0845
REMARK 3 S31: 0.5396 S32: -0.5775 S33: -0.0129
REMARK 3 TLS GROUP : 25
REMARK 3 SELECTION: (CHAIN B AND RESID 694:743)
REMARK 3 ORIGIN FOR THE GROUP (A): 19.1200 23.8349 84.4596
REMARK 3 T TENSOR
REMARK 3 T11: 1.1851 T22: 1.1424
REMARK 3 T33: 2.0430 T12: -0.6891
REMARK 3 T13: 0.3625 T23: 0.3255
REMARK 3 L TENSOR
REMARK 3 L11: 4.9844 L22: 1.1275
REMARK 3 L33: 1.8519 L12: -1.3354
REMARK 3 L13: -0.5834 L23: -0.9544
REMARK 3 S TENSOR
REMARK 3 S11: -0.2947 S12: -1.7739 S13: -0.0647
REMARK 3 S21: 0.0301 S22: 1.0772 S23: -0.9728
REMARK 3 S31: -0.2085 S32: -0.0534 S33: -0.1576
REMARK 3 TLS GROUP : 26
REMARK 3 SELECTION: (CHAIN B AND RESID 744:763)
REMARK 3 ORIGIN FOR THE GROUP (A): 15.3833 26.6653 100.3473
REMARK 3 T TENSOR
REMARK 3 T11: 1.2261 T22: 0.4299
REMARK 3 T33: 1.6470 T12: -0.3069
REMARK 3 T13: 0.6561 T23: 1.6783
REMARK 3 L TENSOR
REMARK 3 L11: 1.9742 L22: 6.4328
REMARK 3 L33: 1.5744 L12: 7.9694
REMARK 3 L13: 0.4174 L23: -0.3863
REMARK 3 S TENSOR
REMARK 3 S11: -0.0935 S12: -2.1414 S13: 1.6520
REMARK 3 S21: 2.3851 S22: -0.7943 S23: 3.4236
REMARK 3 S31: -0.5130 S32: -1.5295 S33: -13.8898
REMARK 3 TLS GROUP : 27
REMARK 3 SELECTION: (CHAIN B AND RESID 764:883)
REMARK 3 ORIGIN FOR THE GROUP (A): 31.9416 29.1393 70.0570
REMARK 3 T TENSOR
REMARK 3 T11: 1.3688 T22: 1.4146
REMARK 3 T33: 1.7210 T12: -0.4009
REMARK 3 T13: 0.1081 T23: -0.0945
REMARK 3 L TENSOR
REMARK 3 L11: 2.7709 L22: 1.5927
REMARK 3 L33: 3.7583 L12: -2.4916
REMARK 3 L13: -2.9557 L23: 1.5775
REMARK 3 S TENSOR
REMARK 3 S11: -0.0460 S12: -0.1713 S13: -0.2529
REMARK 3 S21: 0.0520 S22: 0.4109 S23: 0.1835
REMARK 3 S31: -0.0007 S32: -0.4218 S33: -0.0001
REMARK 3 TLS GROUP : 28
REMARK 3 SELECTION: (CHAIN B AND RESID 884:989)
REMARK 3 ORIGIN FOR THE GROUP (A): 27.9437 52.6691 70.6161
REMARK 3 T TENSOR
REMARK 3 T11: 1.4329 T22: 1.6980
REMARK 3 T33: 1.7118 T12: -0.2748
REMARK 3 T13: 0.2182 T23: -0.0937
REMARK 3 L TENSOR
REMARK 3 L11: 4.2723 L22: 0.0203
REMARK 3 L33: 2.6318 L12: -0.1101
REMARK 3 L13: -3.3522 L23: -1.6586
REMARK 3 S TENSOR
REMARK 3 S11: -0.7268 S12: 0.9281 S13: -1.6029
REMARK 3 S21: 0.0089 S22: 0.4680 S23: -0.5190
REMARK 3 S31: 0.2717 S32: -0.7997 S33: 0.0085
REMARK 3 TLS GROUP : 29
REMARK 3 SELECTION: (CHAIN B AND RESID 990:1135)
REMARK 3 ORIGIN FOR THE GROUP (A): 62.4290 17.4065 47.4449
REMARK 3 T TENSOR
REMARK 3 T11: 2.0032 T22: 2.0840
REMARK 3 T33: 1.9934 T12: -0.5212
REMARK 3 T13: 0.3937 T23: -0.2121
REMARK 3 L TENSOR
REMARK 3 L11: 1.7459 L22: 1.3782
REMARK 3 L33: 4.1249 L12: -0.6882
REMARK 3 L13: 1.8993 L23: 0.6555
REMARK 3 S TENSOR
REMARK 3 S11: -0.7550 S12: -0.1452 S13: -0.9130
REMARK 3 S21: -0.4328 S22: -0.1946 S23: 0.6349
REMARK 3 S31: 0.1542 S32: 0.9791 S33: -0.0007
REMARK 3 TLS GROUP : 30
REMARK 3 SELECTION: (CHAIN B AND RESID 1136:1161)
REMARK 3 ORIGIN FOR THE GROUP (A): 82.5855 8.9795 66.5126
REMARK 3 T TENSOR
REMARK 3 T11: 1.2551 T22: 3.5087
REMARK 3 T33: 2.4616 T12: 0.3575
REMARK 3 T13: -0.2332 T23: -0.9457
REMARK 3 L TENSOR
REMARK 3 L11: 1.9860 L22: 2.8776
REMARK 3 L33: 1.9871 L12: 0.8474
REMARK 3 L13: 5.3220 L23: -5.0447
REMARK 3 S TENSOR
REMARK 3 S11: -2.4696 S12: -1.7634 S13: 1.8790
REMARK 3 S21: 1.1827 S22: -2.4815 S23: 0.4417
REMARK 3 S31: -0.3308 S32: 2.2863 S33: -9.5316
REMARK 3 TLS GROUP : 31
REMARK 3 SELECTION: (CHAIN B AND RESID 1162:1198)
REMARK 3 ORIGIN FOR THE GROUP (A): 76.7889 17.4622 60.0217
REMARK 3 T TENSOR
REMARK 3 T11: 1.4082 T22: 3.0175
REMARK 3 T33: 1.6770 T12: -0.7424
REMARK 3 T13: 0.0204 T23: 0.1910
REMARK 3 L TENSOR
REMARK 3 L11: 1.5735 L22: 0.0808
REMARK 3 L33: 1.9749 L12: -0.0149
REMARK 3 L13: 3.2639 L23: 0.7019
REMARK 3 S TENSOR
REMARK 3 S11: -0.5513 S12: 0.0085 S13: -0.5746
REMARK 3 S21: -0.1234 S22: 0.2074 S23: 0.4733
REMARK 3 S31: -3.2669 S32: 1.4507 S33: -0.1223
REMARK 3 TLS GROUP : 32
REMARK 3 SELECTION: (CHAIN B AND RESID 1199:1271)
REMARK 3 ORIGIN FOR THE GROUP (A): 85.3059 23.4419 40.7279
REMARK 3 T TENSOR
REMARK 3 T11: 1.0520 T22: 3.0176
REMARK 3 T33: 1.0334 T12: -0.7918
REMARK 3 T13: 0.7037 T23: -0.5812
REMARK 3 L TENSOR
REMARK 3 L11: 7.7196 L22: 0.9142
REMARK 3 L33: 8.2308 L12: -1.3702
REMARK 3 L13: -1.4372 L23: 1.1868
REMARK 3 S TENSOR
REMARK 3 S11: -0.4067 S12: 1.6630 S13: 1.8864
REMARK 3 S21: -0.9541 S22: 0.2570 S23: 0.1061
REMARK 3 S31: -1.6551 S32: -0.4738 S33: -2.1482
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 5KOY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-JUL-16.
REMARK 100 THE DEPOSITION ID IS D_1000222569.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-MAR-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 9.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 42251
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.800
REMARK 200 RESOLUTION RANGE LOW (A) : 34.724
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 14.50
REMARK 200 R MERGE (I) : 0.13200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.87
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.5
REMARK 200 DATA REDUNDANCY IN SHELL : 9.50
REMARK 200 R MERGE FOR SHELL (I) : 0.99700
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 5KPD
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 68.16
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.86
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM GLYCINE PH 9.0, 150 MM NACL,
REMARK 280 31% PEG400. AFTER CRYSTALS GREW, CRYSTALS WERE SOAKED IN
REMARK 280 CRYOPROTECTANT SOLUTION WITH 18 MM ATP, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 277K
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 48.76000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 187.52600
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 58.21950
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 187.52600
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 48.76000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 58.21950
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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 LYS A 30
REMARK 465 ALA A 661
REMARK 465 GLY A 662
REMARK 465 ASN A 663
REMARK 465 GLU A 664
REMARK 465 ILE A 665
REMARK 465 GLU A 666
REMARK 465 LEU A 667
REMARK 465 GLY A 668
REMARK 465 ASN A 669
REMARK 465 GLU A 670
REMARK 465 ALA A 671
REMARK 465 CYS A 672
REMARK 465 LYS A 673
REMARK 465 SER A 674
REMARK 465 LYS A 675
REMARK 465 ASP A 676
REMARK 465 GLU A 677
REMARK 465 ILE A 678
REMARK 465 ASP A 679
REMARK 465 ASN A 680
REMARK 465 LEU A 681
REMARK 465 ASP A 682
REMARK 465 ALA A 683
REMARK 465 LEU A 684
REMARK 465 ASP A 685
REMARK 465 GLU A 686
REMARK 465 ALA A 1273
REMARK 465 LYS A 1274
REMARK 465 ARG A 1275
REMARK 465 SER A 1276
REMARK 465 HIS A 1277
REMARK 465 HIS A 1278
REMARK 465 HIS A 1279
REMARK 465 HIS A 1280
REMARK 465 HIS A 1281
REMARK 465 HIS A 1282
REMARK 465 MET B 1
REMARK 465 GLU B 2
REMARK 465 LEU B 3
REMARK 465 GLU B 4
REMARK 465 GLU B 5
REMARK 465 ASP B 6
REMARK 465 LEU B 7
REMARK 465 LYS B 8
REMARK 465 GLY B 9
REMARK 465 ARG B 10
REMARK 465 ALA B 11
REMARK 465 ASP B 12
REMARK 465 LYS B 13
REMARK 465 ASN B 14
REMARK 465 PHE B 15
REMARK 465 SER B 16
REMARK 465 LYS B 17
REMARK 465 MET B 18
REMARK 465 GLY B 19
REMARK 465 LYS B 20
REMARK 465 LYS B 21
REMARK 465 SER B 22
REMARK 465 LYS B 23
REMARK 465 LYS B 24
REMARK 465 GLU B 25
REMARK 465 LYS B 26
REMARK 465 LYS B 27
REMARK 465 GLU B 28
REMARK 465 LYS B 29
REMARK 465 LYS B 30
REMARK 465 ALA B 661
REMARK 465 GLY B 662
REMARK 465 ASN B 663
REMARK 465 GLU B 664
REMARK 465 ILE B 665
REMARK 465 GLU B 666
REMARK 465 LEU B 667
REMARK 465 GLY B 668
REMARK 465 ASN B 669
REMARK 465 GLU B 670
REMARK 465 ALA B 671
REMARK 465 CYS B 672
REMARK 465 LYS B 673
REMARK 465 SER B 674
REMARK 465 LYS B 675
REMARK 465 ASP B 676
REMARK 465 GLU B 677
REMARK 465 ILE B 678
REMARK 465 ASP B 679
REMARK 465 ASN B 680
REMARK 465 LEU B 681
REMARK 465 ASP B 682
REMARK 465 ALA B 683
REMARK 465 LEU B 684
REMARK 465 ASP B 685
REMARK 465 GLU B 686
REMARK 465 GLY B 1272
REMARK 465 ALA B 1273
REMARK 465 LYS B 1274
REMARK 465 ARG B 1275
REMARK 465 SER B 1276
REMARK 465 HIS B 1277
REMARK 465 HIS B 1278
REMARK 465 HIS B 1279
REMARK 465 HIS B 1280
REMARK 465 HIS B 1281
REMARK 465 HIS B 1282
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 O ALA A 1198 HG1 THR A 1199 1.51
REMARK 500 O ALA B 1198 HG1 THR B 1199 1.53
REMARK 500 O PRO B 1158 OG1 THR B 1163 2.11
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 ARG A 206 46.74 -96.09
REMARK 500 SER A 377 -62.55 -91.67
REMARK 500 LEU A 411 134.82 171.12
REMARK 500 ALA A 477 76.83 -67.98
REMARK 500 ARG A 488 99.67 -166.97
REMARK 500 ASN A 504 21.39 80.27
REMARK 500 GLN A 515 -113.97 5.00
REMARK 500 ASN A 544 68.89 32.24
REMARK 500 SER A 555 -67.33 -140.34
REMARK 500 GLU A 574 96.99 -67.13
REMARK 500 ASN A 805 59.43 -96.42
REMARK 500 ALA A 815 -60.38 -108.91
REMARK 500 ASN A 838 -63.90 -94.07
REMARK 500 ARG A 908 31.51 -96.89
REMARK 500 LEU A1054 137.15 179.17
REMARK 500 GLN A1108 30.61 -88.53
REMARK 500 ASP A1120 93.43 -57.93
REMARK 500 CYS A1121 170.33 175.66
REMARK 500 VAL A1136 117.52 -14.61
REMARK 500 SER A1137 -169.46 -110.95
REMARK 500 ASN A1149 20.71 80.71
REMARK 500 LYS A1160 -95.07 -13.52
REMARK 500 ARG B 206 48.07 -96.66
REMARK 500 SER B 377 -62.90 -91.44
REMARK 500 LEU B 411 135.45 171.48
REMARK 500 ALA B 477 76.74 -68.10
REMARK 500 ARG B 488 97.98 -167.31
REMARK 500 ASN B 504 20.45 80.58
REMARK 500 GLN B 515 -101.49 -5.39
REMARK 500 ASN B 544 68.33 32.06
REMARK 500 SER B 555 -67.15 -138.91
REMARK 500 ASN B 805 59.51 -97.10
REMARK 500 ALA B 815 -60.17 -108.88
REMARK 500 ASN B 838 -63.42 -93.44
REMARK 500 ARG B 908 31.15 -96.98
REMARK 500 LEU B1054 135.03 -179.09
REMARK 500 GLN B1108 30.91 -88.37
REMARK 500 ASP B1120 93.18 -57.09
REMARK 500 CYS B1121 169.31 175.37
REMARK 500 VAL B1136 114.69 -13.87
REMARK 500 ASN B1149 21.08 80.70
REMARK 500 LYS B1160 -115.47 32.94
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 ATP A 2000
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ATP B 2000
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5KO2 RELATED DB: PDB
REMARK 900 RELATED ID: 5KPD RELATED DB: PDB
REMARK 900 RELATED ID: 5KPJ RELATED DB: PDB
REMARK 900 RELATED ID: 5KPI RELATED DB: PDB
DBREF 5KOY A 1 1276 UNP P21447 MDR1A_MOUSE 1 1276
DBREF 5KOY B 1 1276 UNP P21447 MDR1A_MOUSE 1 1276
SEQADV 5KOY GLN A 552 UNP P21447 GLU 552 ENGINEERED MUTATION
SEQADV 5KOY A UNP P21447 MET 649 DELETION
SEQADV 5KOY A UNP P21447 SER 650 DELETION
SEQADV 5KOY A UNP P21447 SER 651 DELETION
SEQADV 5KOY A UNP P21447 LYS 652 DELETION
SEQADV 5KOY A UNP P21447 ASP 653 DELETION
SEQADV 5KOY A UNP P21447 SER 654 DELETION
SEQADV 5KOY A UNP P21447 GLY 655 DELETION
SEQADV 5KOY A UNP P21447 SER 656 DELETION
SEQADV 5KOY A UNP P21447 SER 657 DELETION
SEQADV 5KOY A UNP P21447 LEU 658 DELETION
SEQADV 5KOY A UNP P21447 ILE 659 DELETION
SEQADV 5KOY A UNP P21447 ARG 660 DELETION
SEQADV 5KOY A UNP P21447 ARG 661 DELETION
SEQADV 5KOY A UNP P21447 ARG 662 DELETION
SEQADV 5KOY A UNP P21447 SER 663 DELETION
SEQADV 5KOY A UNP P21447 THR 664 DELETION
SEQADV 5KOY A UNP P21447 ARG 665 DELETION
SEQADV 5KOY A UNP P21447 LYS 666 DELETION
SEQADV 5KOY A UNP P21447 SER 667 DELETION
SEQADV 5KOY A UNP P21447 ILE 668 DELETION
SEQADV 5KOY A UNP P21447 CYS 669 DELETION
SEQADV 5KOY A UNP P21447 GLY 670 DELETION
SEQADV 5KOY A UNP P21447 PRO 671 DELETION
SEQADV 5KOY A UNP P21447 HIS 672 DELETION
SEQADV 5KOY A UNP P21447 ASP 673 DELETION
SEQADV 5KOY A UNP P21447 GLN 674 DELETION
SEQADV 5KOY A UNP P21447 ASP 675 DELETION
SEQADV 5KOY A UNP P21447 ARG 676 DELETION
SEQADV 5KOY A UNP P21447 LYS 677 DELETION
SEQADV 5KOY A UNP P21447 LEU 678 DELETION
SEQADV 5KOY A UNP P21447 SER 679 DELETION
SEQADV 5KOY A UNP P21447 THR 680 DELETION
SEQADV 5KOY A UNP P21447 LYS 681 DELETION
SEQADV 5KOY A UNP P21447 GLU 682 DELETION
SEQADV 5KOY GLN A 1197 UNP P21447 GLU 1197 CONFLICT
SEQADV 5KOY HIS A 1277 UNP P21447 EXPRESSION TAG
SEQADV 5KOY HIS A 1278 UNP P21447 EXPRESSION TAG
SEQADV 5KOY HIS A 1279 UNP P21447 EXPRESSION TAG
SEQADV 5KOY HIS A 1280 UNP P21447 EXPRESSION TAG
SEQADV 5KOY HIS A 1281 UNP P21447 EXPRESSION TAG
SEQADV 5KOY HIS A 1282 UNP P21447 EXPRESSION TAG
SEQADV 5KOY GLN B 552 UNP P21447 GLU 552 ENGINEERED MUTATION
SEQADV 5KOY B UNP P21447 MET 649 DELETION
SEQADV 5KOY B UNP P21447 SER 650 DELETION
SEQADV 5KOY B UNP P21447 SER 651 DELETION
SEQADV 5KOY B UNP P21447 LYS 652 DELETION
SEQADV 5KOY B UNP P21447 ASP 653 DELETION
SEQADV 5KOY B UNP P21447 SER 654 DELETION
SEQADV 5KOY B UNP P21447 GLY 655 DELETION
SEQADV 5KOY B UNP P21447 SER 656 DELETION
SEQADV 5KOY B UNP P21447 SER 657 DELETION
SEQADV 5KOY B UNP P21447 LEU 658 DELETION
SEQADV 5KOY B UNP P21447 ILE 659 DELETION
SEQADV 5KOY B UNP P21447 ARG 660 DELETION
SEQADV 5KOY B UNP P21447 ARG 661 DELETION
SEQADV 5KOY B UNP P21447 ARG 662 DELETION
SEQADV 5KOY B UNP P21447 SER 663 DELETION
SEQADV 5KOY B UNP P21447 THR 664 DELETION
SEQADV 5KOY B UNP P21447 ARG 665 DELETION
SEQADV 5KOY B UNP P21447 LYS 666 DELETION
SEQADV 5KOY B UNP P21447 SER 667 DELETION
SEQADV 5KOY B UNP P21447 ILE 668 DELETION
SEQADV 5KOY B UNP P21447 CYS 669 DELETION
SEQADV 5KOY B UNP P21447 GLY 670 DELETION
SEQADV 5KOY B UNP P21447 PRO 671 DELETION
SEQADV 5KOY B UNP P21447 HIS 672 DELETION
SEQADV 5KOY B UNP P21447 ASP 673 DELETION
SEQADV 5KOY B UNP P21447 GLN 674 DELETION
SEQADV 5KOY B UNP P21447 ASP 675 DELETION
SEQADV 5KOY B UNP P21447 ARG 676 DELETION
SEQADV 5KOY B UNP P21447 LYS 677 DELETION
SEQADV 5KOY B UNP P21447 LEU 678 DELETION
SEQADV 5KOY B UNP P21447 SER 679 DELETION
SEQADV 5KOY B UNP P21447 THR 680 DELETION
SEQADV 5KOY B UNP P21447 LYS 681 DELETION
SEQADV 5KOY B UNP P21447 GLU 682 DELETION
SEQADV 5KOY GLN B 1197 UNP P21447 GLU 1197 CONFLICT
SEQADV 5KOY HIS B 1277 UNP P21447 EXPRESSION TAG
SEQADV 5KOY HIS B 1278 UNP P21447 EXPRESSION TAG
SEQADV 5KOY HIS B 1279 UNP P21447 EXPRESSION TAG
SEQADV 5KOY HIS B 1280 UNP P21447 EXPRESSION TAG
SEQADV 5KOY HIS B 1281 UNP P21447 EXPRESSION TAG
SEQADV 5KOY HIS B 1282 UNP P21447 EXPRESSION TAG
SEQRES 1 A 1248 MET GLU LEU GLU GLU ASP LEU LYS GLY ARG ALA ASP LYS
SEQRES 2 A 1248 ASN PHE SER LYS MET GLY LYS LYS SER LYS LYS GLU LYS
SEQRES 3 A 1248 LYS GLU LYS LYS PRO ALA VAL SER VAL LEU THR MET PHE
SEQRES 4 A 1248 ARG TYR ALA GLY TRP LEU ASP ARG LEU TYR MET LEU VAL
SEQRES 5 A 1248 GLY THR LEU ALA ALA ILE ILE HIS GLY VAL ALA LEU PRO
SEQRES 6 A 1248 LEU MET MET LEU ILE PHE GLY ASP MET THR ASP SER PHE
SEQRES 7 A 1248 ALA SER VAL GLY ASN VAL SER LYS ASN SER THR ASN MET
SEQRES 8 A 1248 SER GLU ALA ASP LYS ARG ALA MET PHE ALA LYS LEU GLU
SEQRES 9 A 1248 GLU GLU MET THR THR TYR ALA TYR TYR TYR THR GLY ILE
SEQRES 10 A 1248 GLY ALA GLY VAL LEU ILE VAL ALA TYR ILE GLN VAL SER
SEQRES 11 A 1248 PHE TRP CYS LEU ALA ALA GLY ARG GLN ILE HIS LYS ILE
SEQRES 12 A 1248 ARG GLN LYS PHE PHE HIS ALA ILE MET ASN GLN GLU ILE
SEQRES 13 A 1248 GLY TRP PHE ASP VAL HIS ASP VAL GLY GLU LEU ASN THR
SEQRES 14 A 1248 ARG LEU THR ASP ASP VAL SER LYS ILE ASN GLU GLY ILE
SEQRES 15 A 1248 GLY ASP LYS ILE GLY MET PHE PHE GLN ALA MET ALA THR
SEQRES 16 A 1248 PHE PHE GLY GLY PHE ILE ILE GLY PHE THR ARG GLY TRP
SEQRES 17 A 1248 LYS LEU THR LEU VAL ILE LEU ALA ILE SER PRO VAL LEU
SEQRES 18 A 1248 GLY LEU SER ALA GLY ILE TRP ALA LYS ILE LEU SER SER
SEQRES 19 A 1248 PHE THR ASP LYS GLU LEU HIS ALA TYR ALA LYS ALA GLY
SEQRES 20 A 1248 ALA VAL ALA GLU GLU VAL LEU ALA ALA ILE ARG THR VAL
SEQRES 21 A 1248 ILE ALA PHE GLY GLY GLN LYS LYS GLU LEU GLU ARG TYR
SEQRES 22 A 1248 ASN ASN ASN LEU GLU GLU ALA LYS ARG LEU GLY ILE LYS
SEQRES 23 A 1248 LYS ALA ILE THR ALA ASN ILE SER MET GLY ALA ALA PHE
SEQRES 24 A 1248 LEU LEU ILE TYR ALA SER TYR ALA LEU ALA PHE TRP TYR
SEQRES 25 A 1248 GLY THR SER LEU VAL ILE SER LYS GLU TYR SER ILE GLY
SEQRES 26 A 1248 GLN VAL LEU THR VAL PHE PHE SER VAL LEU ILE GLY ALA
SEQRES 27 A 1248 PHE SER VAL GLY GLN ALA SER PRO ASN ILE GLU ALA PHE
SEQRES 28 A 1248 ALA ASN ALA ARG GLY ALA ALA TYR GLU VAL PHE LYS ILE
SEQRES 29 A 1248 ILE ASP ASN LYS PRO SER ILE ASP SER PHE SER LYS SER
SEQRES 30 A 1248 GLY HIS LYS PRO ASP ASN ILE GLN GLY ASN LEU GLU PHE
SEQRES 31 A 1248 LYS ASN ILE HIS PHE SER TYR PRO SER ARG LYS GLU VAL
SEQRES 32 A 1248 GLN ILE LEU LYS GLY LEU ASN LEU LYS VAL LYS SER GLY
SEQRES 33 A 1248 GLN THR VAL ALA LEU VAL GLY ASN SER GLY CYS GLY LYS
SEQRES 34 A 1248 SER THR THR VAL GLN LEU MET GLN ARG LEU TYR ASP PRO
SEQRES 35 A 1248 LEU ASP GLY MET VAL SER ILE ASP GLY GLN ASP ILE ARG
SEQRES 36 A 1248 THR ILE ASN VAL ARG TYR LEU ARG GLU ILE ILE GLY VAL
SEQRES 37 A 1248 VAL SER GLN GLU PRO VAL LEU PHE ALA THR THR ILE ALA
SEQRES 38 A 1248 GLU ASN ILE ARG TYR GLY ARG GLU ASP VAL THR MET ASP
SEQRES 39 A 1248 GLU ILE GLU LYS ALA VAL LYS GLU ALA ASN ALA TYR ASP
SEQRES 40 A 1248 PHE ILE MET LYS LEU PRO HIS GLN PHE ASP THR LEU VAL
SEQRES 41 A 1248 GLY GLU ARG GLY ALA GLN LEU SER GLY GLY GLN LYS GLN
SEQRES 42 A 1248 ARG ILE ALA ILE ALA ARG ALA LEU VAL ARG ASN PRO LYS
SEQRES 43 A 1248 ILE LEU LEU LEU ASP GLN ALA THR SER ALA LEU ASP THR
SEQRES 44 A 1248 GLU SER GLU ALA VAL VAL GLN ALA ALA LEU ASP LYS ALA
SEQRES 45 A 1248 ARG GLU GLY ARG THR THR ILE VAL ILE ALA HIS ARG LEU
SEQRES 46 A 1248 SER THR VAL ARG ASN ALA ASP VAL ILE ALA GLY PHE ASP
SEQRES 47 A 1248 GLY GLY VAL ILE VAL GLU GLN GLY ASN HIS ASP GLU LEU
SEQRES 48 A 1248 MET ARG GLU LYS GLY ILE TYR PHE LYS LEU VAL MET THR
SEQRES 49 A 1248 GLN THR ALA GLY ASN GLU ILE GLU LEU GLY ASN GLU ALA
SEQRES 50 A 1248 CYS LYS SER LYS ASP GLU ILE ASP ASN LEU ASP ALA LEU
SEQRES 51 A 1248 ASP GLU ASP VAL PRO PRO ALA SER PHE TRP ARG ILE LEU
SEQRES 52 A 1248 LYS LEU ASN SER THR GLU TRP PRO TYR PHE VAL VAL GLY
SEQRES 53 A 1248 ILE PHE CYS ALA ILE ILE ASN GLY GLY LEU GLN PRO ALA
SEQRES 54 A 1248 PHE SER VAL ILE PHE SER LYS VAL VAL GLY VAL PHE THR
SEQRES 55 A 1248 ASN GLY GLY PRO PRO GLU THR GLN ARG GLN ASN SER ASN
SEQRES 56 A 1248 LEU PHE SER LEU LEU PHE LEU ILE LEU GLY ILE ILE SER
SEQRES 57 A 1248 PHE ILE THR PHE PHE LEU GLN GLY PHE THR PHE GLY LYS
SEQRES 58 A 1248 ALA GLY GLU ILE LEU THR LYS ARG LEU ARG TYR MET VAL
SEQRES 59 A 1248 PHE LYS SER MET LEU ARG GLN ASP VAL SER TRP PHE ASP
SEQRES 60 A 1248 ASP PRO LYS ASN THR THR GLY ALA LEU THR THR ARG LEU
SEQRES 61 A 1248 ALA ASN ASP ALA ALA GLN VAL LYS GLY ALA THR GLY SER
SEQRES 62 A 1248 ARG LEU ALA VAL ILE PHE GLN ASN ILE ALA ASN LEU GLY
SEQRES 63 A 1248 THR GLY ILE ILE ILE SER LEU ILE TYR GLY TRP GLN LEU
SEQRES 64 A 1248 THR LEU LEU LEU LEU ALA ILE VAL PRO ILE ILE ALA ILE
SEQRES 65 A 1248 ALA GLY VAL VAL GLU MET LYS MET LEU SER GLY GLN ALA
SEQRES 66 A 1248 LEU LYS ASP LYS LYS GLU LEU GLU GLY SER GLY LYS ILE
SEQRES 67 A 1248 ALA THR GLU ALA ILE GLU ASN PHE ARG THR VAL VAL SER
SEQRES 68 A 1248 LEU THR ARG GLU GLN LYS PHE GLU THR MET TYR ALA GLN
SEQRES 69 A 1248 SER LEU GLN ILE PRO TYR ARG ASN ALA MET LYS LYS ALA
SEQRES 70 A 1248 HIS VAL PHE GLY ILE THR PHE SER PHE THR GLN ALA MET
SEQRES 71 A 1248 MET TYR PHE SER TYR ALA ALA CYS PHE ARG PHE GLY ALA
SEQRES 72 A 1248 TYR LEU VAL THR GLN GLN LEU MET THR PHE GLU ASN VAL
SEQRES 73 A 1248 LEU LEU VAL PHE SER ALA ILE VAL PHE GLY ALA MET ALA
SEQRES 74 A 1248 VAL GLY GLN VAL SER SER PHE ALA PRO ASP TYR ALA LYS
SEQRES 75 A 1248 ALA THR VAL SER ALA SER HIS ILE ILE ARG ILE ILE GLU
SEQRES 76 A 1248 LYS THR PRO GLU ILE ASP SER TYR SER THR GLN GLY LEU
SEQRES 77 A 1248 LYS PRO ASN MET LEU GLU GLY ASN VAL GLN PHE SER GLY
SEQRES 78 A 1248 VAL VAL PHE ASN TYR PRO THR ARG PRO SER ILE PRO VAL
SEQRES 79 A 1248 LEU GLN GLY LEU SER LEU GLU VAL LYS LYS GLY GLN THR
SEQRES 80 A 1248 LEU ALA LEU VAL GLY SER SER GLY CYS GLY LYS SER THR
SEQRES 81 A 1248 VAL VAL GLN LEU LEU GLU ARG PHE TYR ASP PRO MET ALA
SEQRES 82 A 1248 GLY SER VAL PHE LEU ASP GLY LYS GLU ILE LYS GLN LEU
SEQRES 83 A 1248 ASN VAL GLN TRP LEU ARG ALA GLN LEU GLY ILE VAL SER
SEQRES 84 A 1248 GLN GLU PRO ILE LEU PHE ASP CYS SER ILE ALA GLU ASN
SEQRES 85 A 1248 ILE ALA TYR GLY ASP ASN SER ARG VAL VAL SER TYR GLU
SEQRES 86 A 1248 GLU ILE VAL ARG ALA ALA LYS GLU ALA ASN ILE HIS GLN
SEQRES 87 A 1248 PHE ILE ASP SER LEU PRO ASP LYS TYR ASN THR ARG VAL
SEQRES 88 A 1248 GLY ASP LYS GLY THR GLN LEU SER GLY GLY GLN LYS GLN
SEQRES 89 A 1248 ARG ILE ALA ILE ALA ARG ALA LEU VAL ARG GLN PRO HIS
SEQRES 90 A 1248 ILE LEU LEU LEU ASP GLN ALA THR SER ALA LEU ASP THR
SEQRES 91 A 1248 GLU SER GLU LYS VAL VAL GLN GLU ALA LEU ASP LYS ALA
SEQRES 92 A 1248 ARG GLU GLY ARG THR CYS ILE VAL ILE ALA HIS ARG LEU
SEQRES 93 A 1248 SER THR ILE GLN ASN ALA ASP LEU ILE VAL VAL ILE GLN
SEQRES 94 A 1248 ASN GLY LYS VAL LYS GLU HIS GLY THR HIS GLN GLN LEU
SEQRES 95 A 1248 LEU ALA GLN LYS GLY ILE TYR PHE SER MET VAL SER VAL
SEQRES 96 A 1248 GLN ALA GLY ALA LYS ARG SER HIS HIS HIS HIS HIS HIS
SEQRES 1 B 1248 MET GLU LEU GLU GLU ASP LEU LYS GLY ARG ALA ASP LYS
SEQRES 2 B 1248 ASN PHE SER LYS MET GLY LYS LYS SER LYS LYS GLU LYS
SEQRES 3 B 1248 LYS GLU LYS LYS PRO ALA VAL SER VAL LEU THR MET PHE
SEQRES 4 B 1248 ARG TYR ALA GLY TRP LEU ASP ARG LEU TYR MET LEU VAL
SEQRES 5 B 1248 GLY THR LEU ALA ALA ILE ILE HIS GLY VAL ALA LEU PRO
SEQRES 6 B 1248 LEU MET MET LEU ILE PHE GLY ASP MET THR ASP SER PHE
SEQRES 7 B 1248 ALA SER VAL GLY ASN VAL SER LYS ASN SER THR ASN MET
SEQRES 8 B 1248 SER GLU ALA ASP LYS ARG ALA MET PHE ALA LYS LEU GLU
SEQRES 9 B 1248 GLU GLU MET THR THR TYR ALA TYR TYR TYR THR GLY ILE
SEQRES 10 B 1248 GLY ALA GLY VAL LEU ILE VAL ALA TYR ILE GLN VAL SER
SEQRES 11 B 1248 PHE TRP CYS LEU ALA ALA GLY ARG GLN ILE HIS LYS ILE
SEQRES 12 B 1248 ARG GLN LYS PHE PHE HIS ALA ILE MET ASN GLN GLU ILE
SEQRES 13 B 1248 GLY TRP PHE ASP VAL HIS ASP VAL GLY GLU LEU ASN THR
SEQRES 14 B 1248 ARG LEU THR ASP ASP VAL SER LYS ILE ASN GLU GLY ILE
SEQRES 15 B 1248 GLY ASP LYS ILE GLY MET PHE PHE GLN ALA MET ALA THR
SEQRES 16 B 1248 PHE PHE GLY GLY PHE ILE ILE GLY PHE THR ARG GLY TRP
SEQRES 17 B 1248 LYS LEU THR LEU VAL ILE LEU ALA ILE SER PRO VAL LEU
SEQRES 18 B 1248 GLY LEU SER ALA GLY ILE TRP ALA LYS ILE LEU SER SER
SEQRES 19 B 1248 PHE THR ASP LYS GLU LEU HIS ALA TYR ALA LYS ALA GLY
SEQRES 20 B 1248 ALA VAL ALA GLU GLU VAL LEU ALA ALA ILE ARG THR VAL
SEQRES 21 B 1248 ILE ALA PHE GLY GLY GLN LYS LYS GLU LEU GLU ARG TYR
SEQRES 22 B 1248 ASN ASN ASN LEU GLU GLU ALA LYS ARG LEU GLY ILE LYS
SEQRES 23 B 1248 LYS ALA ILE THR ALA ASN ILE SER MET GLY ALA ALA PHE
SEQRES 24 B 1248 LEU LEU ILE TYR ALA SER TYR ALA LEU ALA PHE TRP TYR
SEQRES 25 B 1248 GLY THR SER LEU VAL ILE SER LYS GLU TYR SER ILE GLY
SEQRES 26 B 1248 GLN VAL LEU THR VAL PHE PHE SER VAL LEU ILE GLY ALA
SEQRES 27 B 1248 PHE SER VAL GLY GLN ALA SER PRO ASN ILE GLU ALA PHE
SEQRES 28 B 1248 ALA ASN ALA ARG GLY ALA ALA TYR GLU VAL PHE LYS ILE
SEQRES 29 B 1248 ILE ASP ASN LYS PRO SER ILE ASP SER PHE SER LYS SER
SEQRES 30 B 1248 GLY HIS LYS PRO ASP ASN ILE GLN GLY ASN LEU GLU PHE
SEQRES 31 B 1248 LYS ASN ILE HIS PHE SER TYR PRO SER ARG LYS GLU VAL
SEQRES 32 B 1248 GLN ILE LEU LYS GLY LEU ASN LEU LYS VAL LYS SER GLY
SEQRES 33 B 1248 GLN THR VAL ALA LEU VAL GLY ASN SER GLY CYS GLY LYS
SEQRES 34 B 1248 SER THR THR VAL GLN LEU MET GLN ARG LEU TYR ASP PRO
SEQRES 35 B 1248 LEU ASP GLY MET VAL SER ILE ASP GLY GLN ASP ILE ARG
SEQRES 36 B 1248 THR ILE ASN VAL ARG TYR LEU ARG GLU ILE ILE GLY VAL
SEQRES 37 B 1248 VAL SER GLN GLU PRO VAL LEU PHE ALA THR THR ILE ALA
SEQRES 38 B 1248 GLU ASN ILE ARG TYR GLY ARG GLU ASP VAL THR MET ASP
SEQRES 39 B 1248 GLU ILE GLU LYS ALA VAL LYS GLU ALA ASN ALA TYR ASP
SEQRES 40 B 1248 PHE ILE MET LYS LEU PRO HIS GLN PHE ASP THR LEU VAL
SEQRES 41 B 1248 GLY GLU ARG GLY ALA GLN LEU SER GLY GLY GLN LYS GLN
SEQRES 42 B 1248 ARG ILE ALA ILE ALA ARG ALA LEU VAL ARG ASN PRO LYS
SEQRES 43 B 1248 ILE LEU LEU LEU ASP GLN ALA THR SER ALA LEU ASP THR
SEQRES 44 B 1248 GLU SER GLU ALA VAL VAL GLN ALA ALA LEU ASP LYS ALA
SEQRES 45 B 1248 ARG GLU GLY ARG THR THR ILE VAL ILE ALA HIS ARG LEU
SEQRES 46 B 1248 SER THR VAL ARG ASN ALA ASP VAL ILE ALA GLY PHE ASP
SEQRES 47 B 1248 GLY GLY VAL ILE VAL GLU GLN GLY ASN HIS ASP GLU LEU
SEQRES 48 B 1248 MET ARG GLU LYS GLY ILE TYR PHE LYS LEU VAL MET THR
SEQRES 49 B 1248 GLN THR ALA GLY ASN GLU ILE GLU LEU GLY ASN GLU ALA
SEQRES 50 B 1248 CYS LYS SER LYS ASP GLU ILE ASP ASN LEU ASP ALA LEU
SEQRES 51 B 1248 ASP GLU ASP VAL PRO PRO ALA SER PHE TRP ARG ILE LEU
SEQRES 52 B 1248 LYS LEU ASN SER THR GLU TRP PRO TYR PHE VAL VAL GLY
SEQRES 53 B 1248 ILE PHE CYS ALA ILE ILE ASN GLY GLY LEU GLN PRO ALA
SEQRES 54 B 1248 PHE SER VAL ILE PHE SER LYS VAL VAL GLY VAL PHE THR
SEQRES 55 B 1248 ASN GLY GLY PRO PRO GLU THR GLN ARG GLN ASN SER ASN
SEQRES 56 B 1248 LEU PHE SER LEU LEU PHE LEU ILE LEU GLY ILE ILE SER
SEQRES 57 B 1248 PHE ILE THR PHE PHE LEU GLN GLY PHE THR PHE GLY LYS
SEQRES 58 B 1248 ALA GLY GLU ILE LEU THR LYS ARG LEU ARG TYR MET VAL
SEQRES 59 B 1248 PHE LYS SER MET LEU ARG GLN ASP VAL SER TRP PHE ASP
SEQRES 60 B 1248 ASP PRO LYS ASN THR THR GLY ALA LEU THR THR ARG LEU
SEQRES 61 B 1248 ALA ASN ASP ALA ALA GLN VAL LYS GLY ALA THR GLY SER
SEQRES 62 B 1248 ARG LEU ALA VAL ILE PHE GLN ASN ILE ALA ASN LEU GLY
SEQRES 63 B 1248 THR GLY ILE ILE ILE SER LEU ILE TYR GLY TRP GLN LEU
SEQRES 64 B 1248 THR LEU LEU LEU LEU ALA ILE VAL PRO ILE ILE ALA ILE
SEQRES 65 B 1248 ALA GLY VAL VAL GLU MET LYS MET LEU SER GLY GLN ALA
SEQRES 66 B 1248 LEU LYS ASP LYS LYS GLU LEU GLU GLY SER GLY LYS ILE
SEQRES 67 B 1248 ALA THR GLU ALA ILE GLU ASN PHE ARG THR VAL VAL SER
SEQRES 68 B 1248 LEU THR ARG GLU GLN LYS PHE GLU THR MET TYR ALA GLN
SEQRES 69 B 1248 SER LEU GLN ILE PRO TYR ARG ASN ALA MET LYS LYS ALA
SEQRES 70 B 1248 HIS VAL PHE GLY ILE THR PHE SER PHE THR GLN ALA MET
SEQRES 71 B 1248 MET TYR PHE SER TYR ALA ALA CYS PHE ARG PHE GLY ALA
SEQRES 72 B 1248 TYR LEU VAL THR GLN GLN LEU MET THR PHE GLU ASN VAL
SEQRES 73 B 1248 LEU LEU VAL PHE SER ALA ILE VAL PHE GLY ALA MET ALA
SEQRES 74 B 1248 VAL GLY GLN VAL SER SER PHE ALA PRO ASP TYR ALA LYS
SEQRES 75 B 1248 ALA THR VAL SER ALA SER HIS ILE ILE ARG ILE ILE GLU
SEQRES 76 B 1248 LYS THR PRO GLU ILE ASP SER TYR SER THR GLN GLY LEU
SEQRES 77 B 1248 LYS PRO ASN MET LEU GLU GLY ASN VAL GLN PHE SER GLY
SEQRES 78 B 1248 VAL VAL PHE ASN TYR PRO THR ARG PRO SER ILE PRO VAL
SEQRES 79 B 1248 LEU GLN GLY LEU SER LEU GLU VAL LYS LYS GLY GLN THR
SEQRES 80 B 1248 LEU ALA LEU VAL GLY SER SER GLY CYS GLY LYS SER THR
SEQRES 81 B 1248 VAL VAL GLN LEU LEU GLU ARG PHE TYR ASP PRO MET ALA
SEQRES 82 B 1248 GLY SER VAL PHE LEU ASP GLY LYS GLU ILE LYS GLN LEU
SEQRES 83 B 1248 ASN VAL GLN TRP LEU ARG ALA GLN LEU GLY ILE VAL SER
SEQRES 84 B 1248 GLN GLU PRO ILE LEU PHE ASP CYS SER ILE ALA GLU ASN
SEQRES 85 B 1248 ILE ALA TYR GLY ASP ASN SER ARG VAL VAL SER TYR GLU
SEQRES 86 B 1248 GLU ILE VAL ARG ALA ALA LYS GLU ALA ASN ILE HIS GLN
SEQRES 87 B 1248 PHE ILE ASP SER LEU PRO ASP LYS TYR ASN THR ARG VAL
SEQRES 88 B 1248 GLY ASP LYS GLY THR GLN LEU SER GLY GLY GLN LYS GLN
SEQRES 89 B 1248 ARG ILE ALA ILE ALA ARG ALA LEU VAL ARG GLN PRO HIS
SEQRES 90 B 1248 ILE LEU LEU LEU ASP GLN ALA THR SER ALA LEU ASP THR
SEQRES 91 B 1248 GLU SER GLU LYS VAL VAL GLN GLU ALA LEU ASP LYS ALA
SEQRES 92 B 1248 ARG GLU GLY ARG THR CYS ILE VAL ILE ALA HIS ARG LEU
SEQRES 93 B 1248 SER THR ILE GLN ASN ALA ASP LEU ILE VAL VAL ILE GLN
SEQRES 94 B 1248 ASN GLY LYS VAL LYS GLU HIS GLY THR HIS GLN GLN LEU
SEQRES 95 B 1248 LEU ALA GLN LYS GLY ILE TYR PHE SER MET VAL SER VAL
SEQRES 96 B 1248 GLN ALA GLY ALA LYS ARG SER HIS HIS HIS HIS HIS HIS
HET ATP A2000 43
HET ATP B2000 43
HETNAM ATP ADENOSINE-5'-TRIPHOSPHATE
FORMUL 3 ATP 2(C10 H16 N5 O13 P3)
HELIX 1 AA1 SER A 34 PHE A 39 1 6
HELIX 2 AA2 GLY A 43 ASN A 83 1 41
HELIX 3 AA3 ASN A 83 SER A 88 1 6
HELIX 4 AA4 ASP A 95 ASN A 153 1 59
HELIX 5 AA5 GLU A 155 HIS A 162 1 8
HELIX 6 AA6 ASP A 163 ASP A 173 1 11
HELIX 7 AA7 ASP A 173 GLY A 181 1 9
HELIX 8 AA8 GLY A 183 ARG A 206 1 24
HELIX 9 AA9 TRP A 208 ALA A 256 1 49
HELIX 10 AB1 ALA A 256 PHE A 263 1 8
HELIX 11 AB2 LYS A 267 ASN A 276 1 10
HELIX 12 AB3 GLU A 278 SER A 319 1 42
HELIX 13 AB4 SER A 323 ALA A 344 1 22
HELIX 14 AB5 ALA A 344 ASN A 367 1 24
HELIX 15 AB6 GLY A 428 GLN A 437 1 10
HELIX 16 AB7 ARG A 455 ILE A 457 5 3
HELIX 17 AB8 ASN A 458 ILE A 465 1 8
HELIX 18 AB9 THR A 479 TYR A 486 1 8
HELIX 19 AC1 THR A 492 ALA A 503 1 12
HELIX 20 AC2 ALA A 505 LYS A 511 1 7
HELIX 21 AC3 HIS A 514 THR A 518 5 5
HELIX 22 AC4 SER A 528 ASN A 544 1 17
HELIX 23 AC5 ASP A 558 GLU A 574 1 17
HELIX 24 AC6 ARG A 584 ASN A 590 1 7
HELIX 25 AC7 ASN A 607 LYS A 615 1 9
HELIX 26 AC8 GLY A 616 GLN A 625 1 10
HELIX 27 AC9 SER A 692 ASN A 700 1 9
HELIX 28 AD1 GLU A 703 GLY A 738 1 36
HELIX 29 AD2 THR A 743 GLN A 795 1 53
HELIX 30 AD3 ASP A 796 ASP A 802 1 7
HELIX 31 AD4 THR A 806 ASN A 816 1 11
HELIX 32 AD5 ALA A 819 THR A 825 5 7
HELIX 33 AD6 GLY A 826 GLY A 850 1 25
HELIX 34 AD7 GLY A 850 GLU A 898 1 49
HELIX 35 AD8 ASN A 899 THR A 907 1 9
HELIX 36 AD9 ARG A 908 GLN A 962 1 55
HELIX 37 AE1 THR A 966 SER A 989 1 24
HELIX 38 AE2 ASP A 993 LYS A 1010 1 18
HELIX 39 AE3 GLY A 1069 GLU A 1080 1 12
HELIX 40 AE4 LYS A 1098 LEU A 1100 5 3
HELIX 41 AE5 ASN A 1101 GLN A 1108 1 8
HELIX 42 AE6 SER A 1122 TYR A 1129 1 8
HELIX 43 AE7 SER A 1137 ALA A 1148 1 12
HELIX 44 AE8 ILE A 1150 SER A 1156 1 7
HELIX 45 AE9 ASP A 1159 THR A 1163 5 5
HELIX 46 AF1 SER A 1173 GLN A 1189 1 17
HELIX 47 AF2 ASP A 1203 GLU A 1219 1 17
HELIX 48 AF3 ARG A 1229 ASN A 1235 1 7
HELIX 49 AF4 THR A 1252 LYS A 1260 1 9
HELIX 50 AF5 GLY A 1261 GLY A 1272 1 12
HELIX 51 AF6 SER B 34 PHE B 39 1 6
HELIX 52 AF7 GLY B 43 ASN B 83 1 41
HELIX 53 AF8 ASN B 83 SER B 88 1 6
HELIX 54 AF9 SER B 92 ASN B 153 1 62
HELIX 55 AG1 GLU B 155 HIS B 162 1 8
HELIX 56 AG2 ASP B 163 ASP B 173 1 11
HELIX 57 AG3 ASP B 173 GLY B 181 1 9
HELIX 58 AG4 GLY B 183 ARG B 206 1 24
HELIX 59 AG5 TRP B 208 ALA B 256 1 49
HELIX 60 AG6 ALA B 256 PHE B 263 1 8
HELIX 61 AG7 LYS B 267 ASN B 276 1 10
HELIX 62 AG8 GLU B 278 SER B 319 1 42
HELIX 63 AG9 SER B 323 ALA B 344 1 22
HELIX 64 AH1 ALA B 344 ASN B 367 1 24
HELIX 65 AH2 GLY B 428 GLN B 437 1 10
HELIX 66 AH3 ARG B 455 ILE B 457 5 3
HELIX 67 AH4 ASN B 458 ILE B 465 1 8
HELIX 68 AH5 THR B 479 TYR B 486 1 8
HELIX 69 AH6 THR B 492 ALA B 503 1 12
HELIX 70 AH7 ALA B 505 LYS B 511 1 7
HELIX 71 AH8 HIS B 514 THR B 518 5 5
HELIX 72 AH9 SER B 528 ASN B 544 1 17
HELIX 73 AI1 ASP B 558 GLU B 574 1 17
HELIX 74 AI2 ARG B 584 ASN B 590 1 7
HELIX 75 AI3 ASN B 607 LYS B 615 1 9
HELIX 76 AI4 GLY B 616 GLN B 625 1 10
HELIX 77 AI5 SER B 692 ASN B 700 1 9
HELIX 78 AI6 GLU B 703 GLY B 738 1 36
HELIX 79 AI7 THR B 743 GLN B 795 1 53
HELIX 80 AI8 ASP B 796 ASP B 802 1 7
HELIX 81 AI9 THR B 806 ASN B 816 1 11
HELIX 82 AJ1 ALA B 819 THR B 825 5 7
HELIX 83 AJ2 GLY B 826 GLY B 850 1 25
HELIX 84 AJ3 GLY B 850 GLU B 898 1 49
HELIX 85 AJ4 ASN B 899 THR B 907 1 9
HELIX 86 AJ5 ARG B 908 ARG B 954 1 47
HELIX 87 AJ6 ARG B 954 GLN B 962 1 9
HELIX 88 AJ7 THR B 966 SER B 989 1 24
HELIX 89 AJ8 ASP B 993 LYS B 1010 1 18
HELIX 90 AJ9 CYS B 1070 GLU B 1080 1 11
HELIX 91 AK1 LYS B 1098 LEU B 1100 5 3
HELIX 92 AK2 ASN B 1101 GLN B 1108 1 8
HELIX 93 AK3 SER B 1122 TYR B 1129 1 8
HELIX 94 AK4 SER B 1137 ALA B 1148 1 12
HELIX 95 AK5 ILE B 1150 SER B 1156 1 7
HELIX 96 AK6 ASP B 1159 THR B 1163 5 5
HELIX 97 AK7 SER B 1173 GLN B 1189 1 17
HELIX 98 AK8 ASP B 1203 GLU B 1219 1 17
HELIX 99 AK9 ARG B 1229 ALA B 1236 1 8
HELIX 100 AL1 THR B 1252 GLN B 1259 1 8
HELIX 101 AL2 GLY B 1261 ALA B 1271 1 11
SHEET 1 AA1 4 LEU A 406 VAL A 413 0
SHEET 2 AA1 4 LEU A 388 PHE A 395 -1 N ILE A 393 O LEU A 409
SHEET 3 AA1 4 MET A 446 ILE A 449 -1 O MET A 446 N LYS A 391
SHEET 4 AA1 4 GLN A 452 ASP A 453 -1 O GLN A 452 N ILE A 449
SHEET 1 AA2 6 ILE A 466 VAL A 469 0
SHEET 2 AA2 6 ILE A 547 ASP A 551 1 O LEU A 549 N GLY A 467
SHEET 3 AA2 6 THR A 577 ILE A 581 1 O THR A 577 N LEU A 548
SHEET 4 AA2 6 THR A 418 VAL A 422 1 N VAL A 419 O VAL A 580
SHEET 5 AA2 6 VAL A 593 ASP A 598 1 O PHE A 597 N VAL A 422
SHEET 6 AA2 6 VAL A 601 GLY A 606 -1 O GLU A 604 N GLY A 596
SHEET 1 AA3 4 PRO A1047 VAL A1056 0
SHEET 2 AA3 4 VAL A1031 ASN A1039 -1 N PHE A1033 O LEU A1054
SHEET 3 AA3 4 ALA A1087 LEU A1092 -1 O ALA A1087 N VAL A1037
SHEET 4 AA3 4 LYS A1095 GLU A1096 -1 O LYS A1095 N LEU A1092
SHEET 1 AA4 6 LEU A1109 VAL A1112 0
SHEET 2 AA4 6 ILE A1192 ASP A1196 1 O LEU A1194 N GLY A1110
SHEET 3 AA4 6 THR A1222 ILE A1226 1 O ILE A1224 N LEU A1193
SHEET 4 AA4 6 THR A1061 GLY A1066 1 N LEU A1062 O VAL A1225
SHEET 5 AA4 6 LEU A1238 GLN A1243 1 O LEU A1238 N ALA A1063
SHEET 6 AA4 6 LYS A1246 GLY A1251 -1 O LYS A1246 N GLN A1243
SHEET 1 AA5 4 LEU B 406 VAL B 413 0
SHEET 2 AA5 4 LEU B 388 PHE B 395 -1 N PHE B 390 O LEU B 411
SHEET 3 AA5 4 MET B 446 ILE B 449 -1 O MET B 446 N LYS B 391
SHEET 4 AA5 4 GLN B 452 ASP B 453 -1 O GLN B 452 N ILE B 449
SHEET 1 AA6 6 ILE B 466 VAL B 469 0
SHEET 2 AA6 6 ILE B 547 ASP B 551 1 O LEU B 549 N GLY B 467
SHEET 3 AA6 6 THR B 577 ILE B 581 1 O ILE B 579 N LEU B 550
SHEET 4 AA6 6 THR B 418 VAL B 422 1 N LEU B 421 O VAL B 580
SHEET 5 AA6 6 VAL B 593 ASP B 598 1 O VAL B 593 N ALA B 420
SHEET 6 AA6 6 VAL B 601 GLY B 606 -1 O GLY B 606 N ILE B 594
SHEET 1 AA7 4 PRO B1047 VAL B1056 0
SHEET 2 AA7 4 VAL B1031 ASN B1039 -1 N PHE B1033 O LEU B1054
SHEET 3 AA7 4 ALA B1087 LEU B1092 -1 O SER B1089 N SER B1034
SHEET 4 AA7 4 LYS B1095 GLU B1096 -1 O LYS B1095 N LEU B1092
SHEET 1 AA8 6 LEU B1109 VAL B1112 0
SHEET 2 AA8 6 ILE B1192 ASP B1196 1 O LEU B1194 N GLY B1110
SHEET 3 AA8 6 THR B1222 ILE B1226 1 O ILE B1224 N LEU B1193
SHEET 4 AA8 6 THR B1061 VAL B1065 1 N LEU B1064 O VAL B1225
SHEET 5 AA8 6 LEU B1238 GLN B1243 1 O VAL B1240 N VAL B1065
SHEET 6 AA8 6 LYS B1246 GLY B1251 -1 O LYS B1246 N GLN B1243
SITE 1 AC1 8 ASP A 160 TYR A 397 ILE A 405 SER A 425
SITE 2 AC1 8 GLY A 428 LYS A 429 SER A 430 GLN A 552
SITE 1 AC2 12 ASP B 160 TYR B 397 SER B 399 SER B 425
SITE 2 AC2 12 GLY B 426 CYS B 427 GLY B 428 LYS B 429
SITE 3 AC2 12 SER B 430 THR B 431 GLN B 552 ARG B 901
CRYST1 97.520 116.439 375.052 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 0.010254 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008588 0.000000 0.00000
SCALE3 0.000000 0.000000 0.002666 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
