HEADER STRUCTURAL PROTEIN 29-AUG-17 5YA1
TITLE CRYSTAL STRUCTURE OF LSRK-HPR COMPLEX WITH ATP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: AUTOINDUCER-2 KINASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: AI-2 KINASE;
COMPND 5 EC: 2.7.1.189;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: PHOSPHOCARRIER PROTEIN HPR;
COMPND 9 CHAIN: C, D;
COMPND 10 SYNONYM: HISTIDINE-CONTAINING PROTEIN;
COMPND 11 EC: 2.7.11.-;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI (STRAIN K12);
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 STRAIN: K12;
SOURCE 5 GENE: LSRK, YDEV, B1511, JW1504;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI (STRAIN K12);
SOURCE 10 ORGANISM_TAXID: 83333;
SOURCE 11 STRAIN: K12;
SOURCE 12 GENE: PTSH, HPR, B2415, JW2408;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ATP BINDING, STRUCTURAL PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR K.S.RYU,J.H.HA
REVDAT 2 27-MAR-24 5YA1 1 REMARK
REVDAT 1 11-JUL-18 5YA1 0
JRNL AUTH J.H.HA,P.HAUK,K.CHO,Y.EO,X.MA,K.STEPHENS,S.CHA,M.JEONG,
JRNL AUTH 2 J.Y.SUH,H.O.SINTIM,W.E.BENTLEY,K.S.RYU
JRNL TITL EVIDENCE OF LINK BETWEEN QUORUM SENSING AND SUGAR METABOLISM
JRNL TITL 2 INESCHERICHIA COLIREVEALED VIA COCRYSTAL STRUCTURES OF LSRK
JRNL TITL 3 AND HPR
JRNL REF SCI ADV V. 4 R7063 2018
JRNL REFN ESSN 2375-2548
JRNL PMID 29868643
JRNL DOI 10.1126/SCIADV.AAR7063
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.97
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.500
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.8
REMARK 3 NUMBER OF REFLECTIONS : 55251
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.215
REMARK 3 R VALUE (WORKING SET) : 0.214
REMARK 3 FREE R VALUE : 0.254
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.610
REMARK 3 FREE R VALUE TEST SET COUNT : 1995
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 49.9821 - 6.5065 0.98 4125 160 0.1684 0.2226
REMARK 3 2 6.5065 - 5.1661 0.99 3969 152 0.1837 0.2123
REMARK 3 3 5.1661 - 4.5136 0.98 3924 144 0.1506 0.1976
REMARK 3 4 4.5136 - 4.1011 0.98 3841 140 0.1543 0.1929
REMARK 3 5 4.1011 - 3.8073 0.98 3834 147 0.1877 0.2055
REMARK 3 6 3.8073 - 3.5829 0.98 3810 141 0.2150 0.2486
REMARK 3 7 3.5829 - 3.4035 0.98 3820 146 0.2249 0.2663
REMARK 3 8 3.4035 - 3.2553 0.97 3756 147 0.2536 0.2940
REMARK 3 9 3.2553 - 3.1300 0.97 3789 143 0.2898 0.3740
REMARK 3 10 3.1300 - 3.0221 0.96 3719 139 0.2937 0.3226
REMARK 3 11 3.0221 - 2.9276 0.96 3711 132 0.3110 0.3664
REMARK 3 12 2.9276 - 2.8439 0.95 3688 139 0.3356 0.3359
REMARK 3 13 2.8439 - 2.7690 0.94 3649 132 0.3514 0.3721
REMARK 3 14 2.7690 - 2.7015 0.94 3621 133 0.3693 0.4200
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) : 0.490
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.750
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.004 8824
REMARK 3 ANGLE : 0.915 11994
REMARK 3 CHIRALITY : 0.031 1370
REMARK 3 PLANARITY : 0.004 1532
REMARK 3 DIHEDRAL : 14.098 3170
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 16
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 10 THROUGH 91 )
REMARK 3 ORIGIN FOR THE GROUP (A): 21.0562 23.9920 36.4260
REMARK 3 T TENSOR
REMARK 3 T11: 0.6029 T22: 1.0913
REMARK 3 T33: 0.7027 T12: 0.5486
REMARK 3 T13: 0.0815 T23: 0.1215
REMARK 3 L TENSOR
REMARK 3 L11: 7.4006 L22: 1.6512
REMARK 3 L33: 2.3644 L12: -1.8103
REMARK 3 L13: 2.1267 L23: 0.1445
REMARK 3 S TENSOR
REMARK 3 S11: 0.2572 S12: 0.4829 S13: 1.2506
REMARK 3 S21: -0.1289 S22: -0.1381 S23: 0.5034
REMARK 3 S31: -1.3540 S32: -1.2047 S33: 0.1561
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 92 THROUGH 239 )
REMARK 3 ORIGIN FOR THE GROUP (A): 43.8327 16.7427 38.7229
REMARK 3 T TENSOR
REMARK 3 T11: 0.5178 T22: 0.3816
REMARK 3 T33: 0.3290 T12: 0.2493
REMARK 3 T13: 0.0015 T23: 0.0762
REMARK 3 L TENSOR
REMARK 3 L11: 4.4652 L22: 1.5975
REMARK 3 L33: 2.4798 L12: 0.1752
REMARK 3 L13: -0.2380 L23: 0.3223
REMARK 3 S TENSOR
REMARK 3 S11: 0.0784 S12: 0.0603 S13: 0.2773
REMARK 3 S21: 0.0047 S22: -0.0077 S23: -0.0033
REMARK 3 S31: -0.4748 S32: -0.2936 S33: -0.0783
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 240 THROUGH 455 )
REMARK 3 ORIGIN FOR THE GROUP (A): 33.2856 18.2493 12.0574
REMARK 3 T TENSOR
REMARK 3 T11: 0.5133 T22: 0.9034
REMARK 3 T33: 0.4473 T12: 0.4309
REMARK 3 T13: -0.0746 T23: 0.0940
REMARK 3 L TENSOR
REMARK 3 L11: 1.3049 L22: 1.2800
REMARK 3 L33: 2.1049 L12: -0.5109
REMARK 3 L13: -0.0264 L23: -0.5309
REMARK 3 S TENSOR
REMARK 3 S11: 0.0586 S12: 0.4031 S13: -0.0799
REMARK 3 S21: -0.2851 S22: -0.0349 S23: -0.0990
REMARK 3 S31: -0.2813 S32: -0.4677 S33: 0.0372
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 456 THROUGH 504 )
REMARK 3 ORIGIN FOR THE GROUP (A): 25.6420 8.6677 15.0777
REMARK 3 T TENSOR
REMARK 3 T11: 0.3537 T22: 0.8792
REMARK 3 T33: 0.5383 T12: 0.1279
REMARK 3 T13: -0.0893 T23: -0.0419
REMARK 3 L TENSOR
REMARK 3 L11: 3.0691 L22: 4.0998
REMARK 3 L33: 7.2425 L12: 0.3427
REMARK 3 L13: -2.2387 L23: -2.2317
REMARK 3 S TENSOR
REMARK 3 S11: -0.3438 S12: 0.5334 S13: -0.4425
REMARK 3 S21: -0.8181 S22: 0.4854 S23: -0.0814
REMARK 3 S31: 0.9722 S32: -1.2831 S33: -0.1998
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 10 THROUGH 91 )
REMARK 3 ORIGIN FOR THE GROUP (A): 80.0086 -23.9636 36.4119
REMARK 3 T TENSOR
REMARK 3 T11: 0.6971 T22: 1.0291
REMARK 3 T33: 0.7076 T12: 0.4912
REMARK 3 T13: -0.0515 T23: -0.0888
REMARK 3 L TENSOR
REMARK 3 L11: 3.3846 L22: 1.3002
REMARK 3 L33: 2.4423 L12: -1.7340
REMARK 3 L13: -0.9669 L23: -0.2750
REMARK 3 S TENSOR
REMARK 3 S11: 0.1419 S12: 0.3497 S13: -1.1216
REMARK 3 S21: -0.1992 S22: -0.0576 S23: -0.3354
REMARK 3 S31: 1.2977 S32: 1.0682 S33: 0.0154
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 92 THROUGH 239 )
REMARK 3 ORIGIN FOR THE GROUP (A): 57.1841 -16.7383 38.7194
REMARK 3 T TENSOR
REMARK 3 T11: 0.5140 T22: 0.3840
REMARK 3 T33: 0.3149 T12: 0.2556
REMARK 3 T13: -0.0053 T23: -0.0785
REMARK 3 L TENSOR
REMARK 3 L11: 3.7894 L22: 1.8608
REMARK 3 L33: 2.3888 L12: 0.2566
REMARK 3 L13: -0.0482 L23: -0.4452
REMARK 3 S TENSOR
REMARK 3 S11: 0.0960 S12: 0.0304 S13: -0.2150
REMARK 3 S21: -0.0141 S22: -0.0516 S23: 0.0200
REMARK 3 S31: 0.4693 S32: 0.2689 S33: -0.0566
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 240 THROUGH 455 )
REMARK 3 ORIGIN FOR THE GROUP (A): 67.7317 -18.2080 12.0544
REMARK 3 T TENSOR
REMARK 3 T11: 0.4924 T22: 0.9367
REMARK 3 T33: 0.3772 T12: 0.5501
REMARK 3 T13: 0.1108 T23: -0.1479
REMARK 3 L TENSOR
REMARK 3 L11: 1.4602 L22: 1.2056
REMARK 3 L33: 1.7887 L12: -0.3888
REMARK 3 L13: 0.1220 L23: 0.4139
REMARK 3 S TENSOR
REMARK 3 S11: 0.0648 S12: 0.5350 S13: 0.1827
REMARK 3 S21: -0.2394 S22: -0.1844 S23: 0.0389
REMARK 3 S31: 0.1787 S32: 0.5838 S33: 0.0031
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 456 THROUGH 504 )
REMARK 3 ORIGIN FOR THE GROUP (A): 75.3479 -8.6832 15.0591
REMARK 3 T TENSOR
REMARK 3 T11: 0.3934 T22: 0.9139
REMARK 3 T33: 0.5304 T12: 0.1141
REMARK 3 T13: 0.0997 T23: 0.0330
REMARK 3 L TENSOR
REMARK 3 L11: 1.7059 L22: 3.0369
REMARK 3 L33: 7.8637 L12: -0.0522
REMARK 3 L13: 1.0081 L23: 1.3937
REMARK 3 S TENSOR
REMARK 3 S11: -0.2154 S12: 0.3725 S13: 0.4321
REMARK 3 S21: -0.7160 S22: 0.4396 S23: 0.1545
REMARK 3 S31: -0.9081 S32: 0.9886 S33: -0.4205
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 1 THROUGH 15 )
REMARK 3 ORIGIN FOR THE GROUP (A): 70.9437 21.8932 49.8393
REMARK 3 T TENSOR
REMARK 3 T11: 0.5386 T22: 1.0171
REMARK 3 T33: 0.6902 T12: -0.2588
REMARK 3 T13: 0.1188 T23: -0.0543
REMARK 3 L TENSOR
REMARK 3 L11: 8.1827 L22: 9.0119
REMARK 3 L33: 3.7050 L12: -0.2638
REMARK 3 L13: 5.2003 L23: -2.0926
REMARK 3 S TENSOR
REMARK 3 S11: 0.3471 S12: 0.3591 S13: 1.2507
REMARK 3 S21: 0.3771 S22: -1.5153 S23: -0.5178
REMARK 3 S31: -1.6131 S32: 2.7189 S33: 1.1093
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 16 THROUGH 37 )
REMARK 3 ORIGIN FOR THE GROUP (A): 64.9201 13.3151 46.7293
REMARK 3 T TENSOR
REMARK 3 T11: 0.5044 T22: 0.6111
REMARK 3 T33: 0.4101 T12: -0.1794
REMARK 3 T13: 0.1220 T23: 0.0307
REMARK 3 L TENSOR
REMARK 3 L11: 3.7209 L22: 5.5048
REMARK 3 L33: 8.0234 L12: -2.1858
REMARK 3 L13: 5.2203 L23: -3.3466
REMARK 3 S TENSOR
REMARK 3 S11: 0.0667 S12: 0.6365 S13: 0.4543
REMARK 3 S21: -1.1078 S22: 0.1733 S23: -0.3152
REMARK 3 S31: 0.0671 S32: 1.1033 S33: -0.1092
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 38 THROUGH 69 )
REMARK 3 ORIGIN FOR THE GROUP (A): 63.0680 20.1455 50.0193
REMARK 3 T TENSOR
REMARK 3 T11: 0.5917 T22: 0.5207
REMARK 3 T33: 0.3467 T12: -0.2418
REMARK 3 T13: 0.1086 T23: -0.0086
REMARK 3 L TENSOR
REMARK 3 L11: 7.7314 L22: 2.6423
REMARK 3 L33: 2.7290 L12: -1.1819
REMARK 3 L13: 0.3928 L23: 0.4341
REMARK 3 S TENSOR
REMARK 3 S11: 0.2583 S12: -0.3869 S13: 0.7004
REMARK 3 S21: 0.7639 S22: 0.0006 S23: 0.1331
REMARK 3 S31: -1.2880 S32: 0.7884 S33: -0.0980
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 70 THROUGH 85 )
REMARK 3 ORIGIN FOR THE GROUP (A): 73.3394 13.7013 50.1622
REMARK 3 T TENSOR
REMARK 3 T11: 0.5753 T22: 1.3905
REMARK 3 T33: 0.5722 T12: -0.1970
REMARK 3 T13: 0.0549 T23: 0.1197
REMARK 3 L TENSOR
REMARK 3 L11: 3.2505 L22: 7.5104
REMARK 3 L33: 5.3101 L12: 0.7318
REMARK 3 L13: -4.1159 L23: -1.6426
REMARK 3 S TENSOR
REMARK 3 S11: -0.0330 S12: 0.7628 S13: -0.4826
REMARK 3 S21: -1.2017 S22: -0.6382 S23: -1.5436
REMARK 3 S31: -0.6002 S32: 2.0139 S33: 0.8554
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 1 THROUGH 15 )
REMARK 3 ORIGIN FOR THE GROUP (A): 30.0667 -21.9033 49.8347
REMARK 3 T TENSOR
REMARK 3 T11: 0.6479 T22: 1.0340
REMARK 3 T33: 0.7077 T12: -0.2573
REMARK 3 T13: -0.1808 T23: 0.0031
REMARK 3 L TENSOR
REMARK 3 L11: 6.0378 L22: 6.2971
REMARK 3 L33: 3.0371 L12: 0.3687
REMARK 3 L13: -4.1127 L23: 0.9944
REMARK 3 S TENSOR
REMARK 3 S11: 0.2017 S12: 0.3161 S13: -1.1864
REMARK 3 S21: 0.0506 S22: -1.0626 S23: 0.6173
REMARK 3 S31: 1.3820 S32: -2.4250 S33: 0.7691
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 16 THROUGH 37 )
REMARK 3 ORIGIN FOR THE GROUP (A): 36.0423 -13.3446 46.7793
REMARK 3 T TENSOR
REMARK 3 T11: 0.4558 T22: 0.6750
REMARK 3 T33: 0.4561 T12: -0.1568
REMARK 3 T13: -0.1117 T23: -0.0074
REMARK 3 L TENSOR
REMARK 3 L11: 5.1632 L22: 6.5866
REMARK 3 L33: 7.4482 L12: -1.6100
REMARK 3 L13: -5.5328 L23: 1.4747
REMARK 3 S TENSOR
REMARK 3 S11: 0.2654 S12: 0.4471 S13: -0.4932
REMARK 3 S21: -0.5368 S22: -0.0157 S23: 0.3579
REMARK 3 S31: 0.0076 S32: -1.2105 S33: -0.1935
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 38 THROUGH 69 )
REMARK 3 ORIGIN FOR THE GROUP (A): 37.9506 -20.1544 50.0413
REMARK 3 T TENSOR
REMARK 3 T11: 0.5544 T22: 0.4723
REMARK 3 T33: 0.3258 T12: -0.2156
REMARK 3 T13: -0.1150 T23: 0.0233
REMARK 3 L TENSOR
REMARK 3 L11: 9.1873 L22: 4.0457
REMARK 3 L33: 3.7479 L12: -0.9503
REMARK 3 L13: -0.6500 L23: 0.1555
REMARK 3 S TENSOR
REMARK 3 S11: 0.2287 S12: -0.3569 S13: -0.7252
REMARK 3 S21: 0.8930 S22: 0.0402 S23: -0.1481
REMARK 3 S31: 1.4921 S32: -0.5402 S33: -0.2098
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 70 THROUGH 85 )
REMARK 3 ORIGIN FOR THE GROUP (A): 27.4976 -13.6158 50.1184
REMARK 3 T TENSOR
REMARK 3 T11: 0.5351 T22: 1.3897
REMARK 3 T33: 0.6446 T12: -0.1844
REMARK 3 T13: -0.0157 T23: -0.1019
REMARK 3 L TENSOR
REMARK 3 L11: 3.6757 L22: 4.6105
REMARK 3 L33: 5.6800 L12: 0.0618
REMARK 3 L13: 3.6089 L23: 2.4206
REMARK 3 S TENSOR
REMARK 3 S11: 0.2633 S12: 0.8608 S13: 0.4278
REMARK 3 S21: -0.7295 S22: -0.8761 S23: 1.7860
REMARK 3 S31: 0.7203 S32: -2.4781 S33: 0.8439
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 5YA1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 30-AUG-17.
REMARK 100 THE DEPOSITION ID IS D_1300004915.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-DEC-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : BL-17A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 S 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : PHENIX 1.9_1692
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 55273
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.7
REMARK 200 DATA REDUNDANCY : 8.200
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 25.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: PHENIX 1.9_1692
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 67.03
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.73
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 5~20% (V/V) PEG-400, 0.1M SODIUM
REMARK 280 PHOSPHATE-CITRATE (PH 4.2), 0.2M LITHIUM SULFATE, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 229.63533
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 114.81767
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 114.81767
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 229.63533
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3890 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23670 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3790 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23620 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D
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 HIS A -9
REMARK 465 HIS A -8
REMARK 465 HIS A -7
REMARK 465 HIS A -6
REMARK 465 HIS A -5
REMARK 465 HIS A -4
REMARK 465 SER A -3
REMARK 465 GLU A -2
REMARK 465 ASP A -1
REMARK 465 PRO A 0
REMARK 465 MET A 1
REMARK 465 ALA A 2
REMARK 465 ARG A 3
REMARK 465 LEU A 4
REMARK 465 PHE A 5
REMARK 465 THR A 6
REMARK 465 LEU A 7
REMARK 465 SER A 8
REMARK 465 GLU A 9
REMARK 465 LEU A 46
REMARK 465 ALA A 47
REMARK 465 VAL A 48
REMARK 465 PRO A 49
REMARK 465 ASP A 50
REMARK 465 VAL A 51
REMARK 465 PRO A 52
REMARK 465 GLY A 53
REMARK 465 SER A 54
REMARK 465 ASP A 364
REMARK 465 ARG A 365
REMARK 465 MET A 366
REMARK 465 ARG A 367
REMARK 465 PHE A 368
REMARK 465 LYS A 369
REMARK 465 THR A 370
REMARK 465 TRP A 371
REMARK 465 TRP A 505
REMARK 465 GLN A 506
REMARK 465 ALA A 507
REMARK 465 VAL A 508
REMARK 465 TYR A 509
REMARK 465 GLN A 510
REMARK 465 ASP A 511
REMARK 465 GLN A 512
REMARK 465 LEU A 513
REMARK 465 GLY A 514
REMARK 465 LEU A 515
REMARK 465 VAL A 516
REMARK 465 ASP A 517
REMARK 465 HIS A 518
REMARK 465 GLY A 519
REMARK 465 LEU A 520
REMARK 465 THR A 521
REMARK 465 THR A 522
REMARK 465 SER A 523
REMARK 465 LEU A 524
REMARK 465 TRP A 525
REMARK 465 LYS A 526
REMARK 465 ALA A 527
REMARK 465 PRO A 528
REMARK 465 GLY A 529
REMARK 465 LEU A 530
REMARK 465 HIS B -9
REMARK 465 HIS B -8
REMARK 465 HIS B -7
REMARK 465 HIS B -6
REMARK 465 HIS B -5
REMARK 465 HIS B -4
REMARK 465 SER B -3
REMARK 465 GLU B -2
REMARK 465 ASP B -1
REMARK 465 PRO B 0
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 ARG B 3
REMARK 465 LEU B 4
REMARK 465 PHE B 5
REMARK 465 THR B 6
REMARK 465 LEU B 7
REMARK 465 SER B 8
REMARK 465 GLU B 9
REMARK 465 LEU B 46
REMARK 465 ALA B 47
REMARK 465 VAL B 48
REMARK 465 PRO B 49
REMARK 465 ASP B 50
REMARK 465 VAL B 51
REMARK 465 PRO B 52
REMARK 465 GLY B 53
REMARK 465 SER B 54
REMARK 465 ASP B 364
REMARK 465 ARG B 365
REMARK 465 MET B 366
REMARK 465 ARG B 367
REMARK 465 PHE B 368
REMARK 465 LYS B 369
REMARK 465 THR B 370
REMARK 465 TRP B 371
REMARK 465 TRP B 505
REMARK 465 GLN B 506
REMARK 465 ALA B 507
REMARK 465 VAL B 508
REMARK 465 TYR B 509
REMARK 465 GLN B 510
REMARK 465 ASP B 511
REMARK 465 GLN B 512
REMARK 465 LEU B 513
REMARK 465 GLY B 514
REMARK 465 LEU B 515
REMARK 465 VAL B 516
REMARK 465 ASP B 517
REMARK 465 HIS B 518
REMARK 465 GLY B 519
REMARK 465 LEU B 520
REMARK 465 THR B 521
REMARK 465 THR B 522
REMARK 465 SER B 523
REMARK 465 LEU B 524
REMARK 465 TRP B 525
REMARK 465 LYS B 526
REMARK 465 ALA B 527
REMARK 465 PRO B 528
REMARK 465 GLY B 529
REMARK 465 LEU B 530
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 43 -127.63 -100.05
REMARK 500 GLU A 56 -108.89 -111.38
REMARK 500 ARG A 158 58.12 -95.62
REMARK 500 ALA A 267 -7.50 67.87
REMARK 500 ASN A 293 -71.25 -101.74
REMARK 500 PHE A 313 -120.86 61.91
REMARK 500 THR A 314 -109.80 54.35
REMARK 500 LYS A 453 -56.99 119.84
REMARK 500 GLU A 485 -119.99 -106.46
REMARK 500 ASP A 503 73.98 -156.37
REMARK 500 TRP B 43 -132.00 -95.97
REMARK 500 GLU B 56 -108.35 -109.69
REMARK 500 ARG B 158 57.99 -96.15
REMARK 500 ALA B 267 -7.50 67.88
REMARK 500 ASN B 293 -72.02 -100.82
REMARK 500 PHE B 313 -121.50 59.85
REMARK 500 THR B 314 -109.90 54.40
REMARK 500 LYS B 453 -61.45 124.62
REMARK 500 GLU B 485 -120.23 -106.67
REMARK 500 ASP D 69 36.31 -99.58
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 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HEZ A 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HEZ A 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 704
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 705
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 706
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 707
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ATP B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HEZ B 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HEZ B 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 B 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 B 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 C 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 D 101
DBREF 5YA1 A 1 530 UNP P77432 LSRK_ECOLI 1 530
DBREF 5YA1 B 1 530 UNP P77432 LSRK_ECOLI 1 530
DBREF 5YA1 C 1 85 UNP P0AA04 PTHP_ECOLI 1 85
DBREF 5YA1 D 1 85 UNP P0AA04 PTHP_ECOLI 1 85
SEQADV 5YA1 HIS A -9 UNP P77432 EXPRESSION TAG
SEQADV 5YA1 HIS A -8 UNP P77432 EXPRESSION TAG
SEQADV 5YA1 HIS A -7 UNP P77432 EXPRESSION TAG
SEQADV 5YA1 HIS A -6 UNP P77432 EXPRESSION TAG
SEQADV 5YA1 HIS A -5 UNP P77432 EXPRESSION TAG
SEQADV 5YA1 HIS A -4 UNP P77432 EXPRESSION TAG
SEQADV 5YA1 SER A -3 UNP P77432 EXPRESSION TAG
SEQADV 5YA1 GLU A -2 UNP P77432 EXPRESSION TAG
SEQADV 5YA1 ASP A -1 UNP P77432 EXPRESSION TAG
SEQADV 5YA1 PRO A 0 UNP P77432 EXPRESSION TAG
SEQADV 5YA1 HIS B -9 UNP P77432 EXPRESSION TAG
SEQADV 5YA1 HIS B -8 UNP P77432 EXPRESSION TAG
SEQADV 5YA1 HIS B -7 UNP P77432 EXPRESSION TAG
SEQADV 5YA1 HIS B -6 UNP P77432 EXPRESSION TAG
SEQADV 5YA1 HIS B -5 UNP P77432 EXPRESSION TAG
SEQADV 5YA1 HIS B -4 UNP P77432 EXPRESSION TAG
SEQADV 5YA1 SER B -3 UNP P77432 EXPRESSION TAG
SEQADV 5YA1 GLU B -2 UNP P77432 EXPRESSION TAG
SEQADV 5YA1 ASP B -1 UNP P77432 EXPRESSION TAG
SEQADV 5YA1 PRO B 0 UNP P77432 EXPRESSION TAG
SEQRES 1 A 540 HIS HIS HIS HIS HIS HIS SER GLU ASP PRO MET ALA ARG
SEQRES 2 A 540 LEU PHE THR LEU SER GLU SER LYS TYR TYR LEU MET ALA
SEQRES 3 A 540 LEU ASP ALA GLY THR GLY SER ILE ARG ALA VAL ILE PHE
SEQRES 4 A 540 ASP LEU GLU GLY ASN GLN ILE ALA VAL GLY GLN ALA GLU
SEQRES 5 A 540 TRP ARG HIS LEU ALA VAL PRO ASP VAL PRO GLY SER MET
SEQRES 6 A 540 GLU PHE ASP LEU ASN LYS ASN TRP GLN LEU ALA CYS GLU
SEQRES 7 A 540 CYS MET ARG GLN ALA LEU HIS ASN ALA GLY ILE ALA PRO
SEQRES 8 A 540 GLU TYR ILE ALA ALA VAL SER ALA CYS SER MET ARG GLU
SEQRES 9 A 540 GLY ILE VAL LEU TYR ASN ASN GLU GLY ALA PRO ILE TRP
SEQRES 10 A 540 ALA CYS ALA ASN VAL ASP ALA ARG ALA ALA ARG GLU VAL
SEQRES 11 A 540 SER GLU LEU LYS GLU LEU HIS ASN ASN THR PHE GLU ASN
SEQRES 12 A 540 GLU VAL TYR ARG ALA THR GLY GLN THR LEU ALA LEU SER
SEQRES 13 A 540 ALA ILE PRO ARG LEU LEU TRP LEU ALA HIS HIS ARG SER
SEQRES 14 A 540 ASP ILE TYR ARG GLN ALA SER THR ILE THR MET ILE SER
SEQRES 15 A 540 ASP TRP LEU ALA TYR MET LEU SER GLY GLU LEU ALA VAL
SEQRES 16 A 540 ASP PRO SER ASN ALA GLY THR THR GLY LEU LEU ASP LEU
SEQRES 17 A 540 THR THR ARG ASP TRP LYS PRO ALA LEU LEU ASP MET ALA
SEQRES 18 A 540 GLY LEU ARG ALA ASP ILE LEU SER PRO VAL LYS GLU THR
SEQRES 19 A 540 GLY THR LEU LEU GLY VAL VAL SER SER GLN ALA ALA GLU
SEQRES 20 A 540 LEU CYS GLY LEU LYS ALA GLY THR PRO VAL VAL VAL GLY
SEQRES 21 A 540 GLY GLY ASP VAL GLN LEU GLY CYS LEU GLY LEU GLY VAL
SEQRES 22 A 540 VAL ARG PRO ALA GLN THR ALA VAL LEU GLY GLY THR PHE
SEQRES 23 A 540 TRP GLN GLN VAL VAL ASN LEU ALA ALA PRO VAL THR ASP
SEQRES 24 A 540 PRO GLU MET ASN VAL ARG VAL ASN PRO HIS VAL ILE PRO
SEQRES 25 A 540 GLY MET VAL GLN ALA GLU SER ILE SER PHE PHE THR GLY
SEQRES 26 A 540 LEU THR MET ARG TRP PHE ARG ASP ALA PHE CYS ALA GLU
SEQRES 27 A 540 GLU LYS LEU ILE ALA GLU ARG LEU GLY ILE ASP THR TYR
SEQRES 28 A 540 THR LEU LEU GLU GLU MET ALA SER ARG VAL PRO PRO GLY
SEQRES 29 A 540 SER TRP GLY VAL MET PRO ILE PHE SER ASP ARG MET ARG
SEQRES 30 A 540 PHE LYS THR TRP TYR HIS ALA ALA PRO SER PHE ILE ASN
SEQRES 31 A 540 LEU SER ILE ASP PRO ASP LYS CYS ASN LYS ALA THR LEU
SEQRES 32 A 540 PHE ARG ALA LEU GLU GLU ASN ALA ALA ILE VAL SER ALA
SEQRES 33 A 540 CYS ASN LEU GLN GLN ILE ALA ASP PHE SER ASN ILE HIS
SEQRES 34 A 540 PRO SER SER LEU VAL PHE ALA GLY GLY GLY SER LYS GLY
SEQRES 35 A 540 LYS LEU TRP SER GLN ILE LEU ALA ASP VAL SER GLY LEU
SEQRES 36 A 540 PRO VAL ASN ILE PRO VAL VAL LYS GLU ALA THR ALA LEU
SEQRES 37 A 540 GLY CYS ALA ILE ALA ALA GLY VAL GLY ALA GLY ILE PHE
SEQRES 38 A 540 SER SER MET ALA GLU THR GLY GLU ARG LEU VAL ARG TRP
SEQRES 39 A 540 GLU ARG THR HIS THR PRO ASP PRO GLU LYS HIS GLU LEU
SEQRES 40 A 540 TYR GLN ASP SER ARG ASP LYS TRP GLN ALA VAL TYR GLN
SEQRES 41 A 540 ASP GLN LEU GLY LEU VAL ASP HIS GLY LEU THR THR SER
SEQRES 42 A 540 LEU TRP LYS ALA PRO GLY LEU
SEQRES 1 B 540 HIS HIS HIS HIS HIS HIS SER GLU ASP PRO MET ALA ARG
SEQRES 2 B 540 LEU PHE THR LEU SER GLU SER LYS TYR TYR LEU MET ALA
SEQRES 3 B 540 LEU ASP ALA GLY THR GLY SER ILE ARG ALA VAL ILE PHE
SEQRES 4 B 540 ASP LEU GLU GLY ASN GLN ILE ALA VAL GLY GLN ALA GLU
SEQRES 5 B 540 TRP ARG HIS LEU ALA VAL PRO ASP VAL PRO GLY SER MET
SEQRES 6 B 540 GLU PHE ASP LEU ASN LYS ASN TRP GLN LEU ALA CYS GLU
SEQRES 7 B 540 CYS MET ARG GLN ALA LEU HIS ASN ALA GLY ILE ALA PRO
SEQRES 8 B 540 GLU TYR ILE ALA ALA VAL SER ALA CYS SER MET ARG GLU
SEQRES 9 B 540 GLY ILE VAL LEU TYR ASN ASN GLU GLY ALA PRO ILE TRP
SEQRES 10 B 540 ALA CYS ALA ASN VAL ASP ALA ARG ALA ALA ARG GLU VAL
SEQRES 11 B 540 SER GLU LEU LYS GLU LEU HIS ASN ASN THR PHE GLU ASN
SEQRES 12 B 540 GLU VAL TYR ARG ALA THR GLY GLN THR LEU ALA LEU SER
SEQRES 13 B 540 ALA ILE PRO ARG LEU LEU TRP LEU ALA HIS HIS ARG SER
SEQRES 14 B 540 ASP ILE TYR ARG GLN ALA SER THR ILE THR MET ILE SER
SEQRES 15 B 540 ASP TRP LEU ALA TYR MET LEU SER GLY GLU LEU ALA VAL
SEQRES 16 B 540 ASP PRO SER ASN ALA GLY THR THR GLY LEU LEU ASP LEU
SEQRES 17 B 540 THR THR ARG ASP TRP LYS PRO ALA LEU LEU ASP MET ALA
SEQRES 18 B 540 GLY LEU ARG ALA ASP ILE LEU SER PRO VAL LYS GLU THR
SEQRES 19 B 540 GLY THR LEU LEU GLY VAL VAL SER SER GLN ALA ALA GLU
SEQRES 20 B 540 LEU CYS GLY LEU LYS ALA GLY THR PRO VAL VAL VAL GLY
SEQRES 21 B 540 GLY GLY ASP VAL GLN LEU GLY CYS LEU GLY LEU GLY VAL
SEQRES 22 B 540 VAL ARG PRO ALA GLN THR ALA VAL LEU GLY GLY THR PHE
SEQRES 23 B 540 TRP GLN GLN VAL VAL ASN LEU ALA ALA PRO VAL THR ASP
SEQRES 24 B 540 PRO GLU MET ASN VAL ARG VAL ASN PRO HIS VAL ILE PRO
SEQRES 25 B 540 GLY MET VAL GLN ALA GLU SER ILE SER PHE PHE THR GLY
SEQRES 26 B 540 LEU THR MET ARG TRP PHE ARG ASP ALA PHE CYS ALA GLU
SEQRES 27 B 540 GLU LYS LEU ILE ALA GLU ARG LEU GLY ILE ASP THR TYR
SEQRES 28 B 540 THR LEU LEU GLU GLU MET ALA SER ARG VAL PRO PRO GLY
SEQRES 29 B 540 SER TRP GLY VAL MET PRO ILE PHE SER ASP ARG MET ARG
SEQRES 30 B 540 PHE LYS THR TRP TYR HIS ALA ALA PRO SER PHE ILE ASN
SEQRES 31 B 540 LEU SER ILE ASP PRO ASP LYS CYS ASN LYS ALA THR LEU
SEQRES 32 B 540 PHE ARG ALA LEU GLU GLU ASN ALA ALA ILE VAL SER ALA
SEQRES 33 B 540 CYS ASN LEU GLN GLN ILE ALA ASP PHE SER ASN ILE HIS
SEQRES 34 B 540 PRO SER SER LEU VAL PHE ALA GLY GLY GLY SER LYS GLY
SEQRES 35 B 540 LYS LEU TRP SER GLN ILE LEU ALA ASP VAL SER GLY LEU
SEQRES 36 B 540 PRO VAL ASN ILE PRO VAL VAL LYS GLU ALA THR ALA LEU
SEQRES 37 B 540 GLY CYS ALA ILE ALA ALA GLY VAL GLY ALA GLY ILE PHE
SEQRES 38 B 540 SER SER MET ALA GLU THR GLY GLU ARG LEU VAL ARG TRP
SEQRES 39 B 540 GLU ARG THR HIS THR PRO ASP PRO GLU LYS HIS GLU LEU
SEQRES 40 B 540 TYR GLN ASP SER ARG ASP LYS TRP GLN ALA VAL TYR GLN
SEQRES 41 B 540 ASP GLN LEU GLY LEU VAL ASP HIS GLY LEU THR THR SER
SEQRES 42 B 540 LEU TRP LYS ALA PRO GLY LEU
SEQRES 1 C 85 MET PHE GLN GLN GLU VAL THR ILE THR ALA PRO ASN GLY
SEQRES 2 C 85 LEU HIS THR ARG PRO ALA ALA GLN PHE VAL LYS GLU ALA
SEQRES 3 C 85 LYS GLY PHE THR SER GLU ILE THR VAL THR SER ASN GLY
SEQRES 4 C 85 LYS SER ALA SER ALA LYS SER LEU PHE LYS LEU GLN THR
SEQRES 5 C 85 LEU GLY LEU THR GLN GLY THR VAL VAL THR ILE SER ALA
SEQRES 6 C 85 GLU GLY GLU ASP GLU GLN LYS ALA VAL GLU HIS LEU VAL
SEQRES 7 C 85 LYS LEU MET ALA GLU LEU GLU
SEQRES 1 D 85 MET PHE GLN GLN GLU VAL THR ILE THR ALA PRO ASN GLY
SEQRES 2 D 85 LEU HIS THR ARG PRO ALA ALA GLN PHE VAL LYS GLU ALA
SEQRES 3 D 85 LYS GLY PHE THR SER GLU ILE THR VAL THR SER ASN GLY
SEQRES 4 D 85 LYS SER ALA SER ALA LYS SER LEU PHE LYS LEU GLN THR
SEQRES 5 D 85 LEU GLY LEU THR GLN GLY THR VAL VAL THR ILE SER ALA
SEQRES 6 D 85 GLU GLY GLU ASP GLU GLN LYS ALA VAL GLU HIS LEU VAL
SEQRES 7 D 85 LYS LEU MET ALA GLU LEU GLU
HET ATP A 701 31
HET HEZ A 702 8
HET HEZ A 703 8
HET PO4 A 704 5
HET PO4 A 705 5
HET PO4 A 706 5
HET PO4 A 707 5
HET ATP B 601 31
HET HEZ B 602 8
HET HEZ B 603 8
HET PO4 B 604 5
HET PO4 B 605 5
HET PO4 C 101 5
HET PO4 D 101 5
HETNAM ATP ADENOSINE-5'-TRIPHOSPHATE
HETNAM HEZ HEXANE-1,6-DIOL
HETNAM PO4 PHOSPHATE ION
FORMUL 5 ATP 2(C10 H16 N5 O13 P3)
FORMUL 6 HEZ 4(C6 H14 O2)
FORMUL 8 PO4 8(O4 P 3-)
FORMUL 19 HOH *71(H2 O)
HELIX 1 AA1 ASP A 58 GLY A 78 1 21
HELIX 2 AA2 ALA A 80 GLU A 82 5 3
HELIX 3 AA3 ASN A 101 GLY A 103 5 3
HELIX 4 AA4 ASP A 113 ARG A 115 5 3
HELIX 5 AA5 ALA A 116 THR A 130 1 15
HELIX 6 AA6 THR A 130 GLY A 140 1 11
HELIX 7 AA7 ALA A 147 ARG A 158 1 12
HELIX 8 AA8 ARG A 158 ARG A 163 1 6
HELIX 9 AA9 ILE A 171 GLY A 181 1 11
HELIX 10 AB1 ASP A 186 GLY A 191 1 6
HELIX 11 AB2 THR A 192 GLY A 194 5 3
HELIX 12 AB3 LYS A 204 GLY A 212 1 9
HELIX 13 AB4 ARG A 214 SER A 219 1 6
HELIX 14 AB5 SER A 232 GLY A 240 1 9
HELIX 15 AB6 ASP A 253 LEU A 261 1 9
HELIX 16 AB7 THR A 314 CYS A 326 1 13
HELIX 17 AB8 CYS A 326 GLY A 337 1 12
HELIX 18 AB9 ASP A 339 VAL A 351 1 13
HELIX 19 AC1 GLY A 354 VAL A 358 5 5
HELIX 20 AC2 ASN A 389 ASN A 417 1 29
HELIX 21 AC3 GLY A 428 LYS A 431 5 4
HELIX 22 AC4 GLY A 432 GLY A 444 1 13
HELIX 23 AC5 ALA A 455 ALA A 468 1 14
HELIX 24 AC6 SER A 473 VAL A 482 1 10
HELIX 25 AC7 ASP A 491 ARG A 502 1 12
HELIX 26 AC8 ASP B 58 GLY B 78 1 21
HELIX 27 AC9 ALA B 80 GLU B 82 5 3
HELIX 28 AD1 ASN B 101 GLY B 103 5 3
HELIX 29 AD2 ASP B 113 ARG B 115 5 3
HELIX 30 AD3 ALA B 116 THR B 130 1 15
HELIX 31 AD4 THR B 130 GLY B 140 1 11
HELIX 32 AD5 ALA B 147 ARG B 158 1 12
HELIX 33 AD6 ARG B 158 ARG B 163 1 6
HELIX 34 AD7 ILE B 171 GLY B 181 1 11
HELIX 35 AD8 ASP B 186 GLY B 191 1 6
HELIX 36 AD9 THR B 192 GLY B 194 5 3
HELIX 37 AE1 LYS B 204 GLY B 212 1 9
HELIX 38 AE2 ARG B 214 SER B 219 1 6
HELIX 39 AE3 SER B 232 GLY B 240 1 9
HELIX 40 AE4 ASP B 253 LEU B 261 1 9
HELIX 41 AE5 THR B 314 CYS B 326 1 13
HELIX 42 AE6 CYS B 326 GLY B 337 1 12
HELIX 43 AE7 ASP B 339 VAL B 351 1 13
HELIX 44 AE8 GLY B 354 VAL B 358 5 5
HELIX 45 AE9 ASN B 389 ASN B 417 1 29
HELIX 46 AF1 GLY B 428 LYS B 431 5 4
HELIX 47 AF2 GLY B 432 GLY B 444 1 13
HELIX 48 AF3 ALA B 455 ALA B 468 1 14
HELIX 49 AF4 SER B 473 VAL B 482 1 10
HELIX 50 AF5 ASP B 491 ASP B 500 1 10
HELIX 51 AF6 HIS C 15 LYS C 27 1 13
HELIX 52 AF7 SER C 46 THR C 52 1 7
HELIX 53 AF8 ASP C 69 LEU C 84 1 16
HELIX 54 AF9 HIS D 15 LYS D 27 1 13
HELIX 55 AG1 SER D 46 THR D 52 1 7
HELIX 56 AG2 ASP D 69 LEU D 84 1 16
SHEET 1 AA1 6 GLN A 35 ALA A 41 0
SHEET 2 AA1 6 ILE A 24 PHE A 29 -1 N ALA A 26 O GLY A 39
SHEET 3 AA1 6 TYR A 13 ALA A 19 -1 N LEU A 14 O PHE A 29
SHEET 4 AA1 6 ILE A 84 SER A 91 1 O CYS A 90 N ALA A 19
SHEET 5 AA1 6 PRO A 246 GLY A 252 1 O VAL A 248 N VAL A 87
SHEET 6 AA1 6 LEU A 227 VAL A 230 -1 N GLY A 229 O VAL A 247
SHEET 1 AA2 3 PRO A 105 CYS A 109 0
SHEET 2 AA2 3 ILE A 96 TYR A 99 -1 N ILE A 96 O CYS A 109
SHEET 3 AA2 3 THR A 167 MET A 170 -1 O THR A 167 N TYR A 99
SHEET 1 AA3 2 LEU A 196 ASP A 197 0
SHEET 2 AA3 2 ASP A 202 TRP A 203 -1 O ASP A 202 N ASP A 197
SHEET 1 AA4 7 ARG A 295 PRO A 298 0
SHEET 2 AA4 7 VAL A 305 SER A 311 -1 O GLU A 308 N ARG A 295
SHEET 3 AA4 7 TRP A 277 LEU A 283 -1 N VAL A 281 O ALA A 307
SHEET 4 AA4 7 THR A 269 GLY A 273 -1 N LEU A 272 O GLN A 278
SHEET 5 AA4 7 LEU A 423 ALA A 426 1 O ALA A 426 N VAL A 271
SHEET 6 AA4 7 VAL A 447 PRO A 450 1 O ASN A 448 N LEU A 423
SHEET 7 AA4 7 TRP A 484 HIS A 488 -1 O HIS A 488 N VAL A 447
SHEET 1 AA5 2 MET A 359 ILE A 361 0
SHEET 2 AA5 2 SER A 377 ILE A 379 -1 O ILE A 379 N MET A 359
SHEET 1 AA6 6 GLN B 35 GLU B 42 0
SHEET 2 AA6 6 SER B 23 PHE B 29 -1 N ALA B 26 O GLY B 39
SHEET 3 AA6 6 TYR B 13 ALA B 19 -1 N LEU B 14 O PHE B 29
SHEET 4 AA6 6 ILE B 84 SER B 91 1 O ALA B 85 N TYR B 13
SHEET 5 AA6 6 PRO B 246 GLY B 252 1 O VAL B 248 N VAL B 87
SHEET 6 AA6 6 LEU B 227 VAL B 230 -1 N GLY B 229 O VAL B 247
SHEET 1 AA7 3 PRO B 105 CYS B 109 0
SHEET 2 AA7 3 ILE B 96 TYR B 99 -1 N ILE B 96 O CYS B 109
SHEET 3 AA7 3 THR B 167 MET B 170 -1 O THR B 169 N VAL B 97
SHEET 1 AA8 2 LEU B 196 ASP B 197 0
SHEET 2 AA8 2 ASP B 202 TRP B 203 -1 O ASP B 202 N ASP B 197
SHEET 1 AA9 7 ARG B 295 PRO B 298 0
SHEET 2 AA9 7 VAL B 305 SER B 311 -1 O GLU B 308 N ARG B 295
SHEET 3 AA9 7 TRP B 277 LEU B 283 -1 N VAL B 281 O ALA B 307
SHEET 4 AA9 7 THR B 269 GLY B 273 -1 N LEU B 272 O GLN B 278
SHEET 5 AA9 7 LEU B 423 ALA B 426 1 O ALA B 426 N GLY B 273
SHEET 6 AA9 7 VAL B 447 PRO B 450 1 O ASN B 448 N LEU B 423
SHEET 7 AA9 7 TRP B 484 HIS B 488 -1 O HIS B 488 N VAL B 447
SHEET 1 AB1 2 MET B 359 ILE B 361 0
SHEET 2 AB1 2 SER B 377 ILE B 379 -1 O ILE B 379 N MET B 359
SHEET 1 AB2 4 PHE C 2 THR C 7 0
SHEET 2 AB2 4 VAL C 60 GLU C 66 -1 O VAL C 61 N VAL C 6
SHEET 3 AB2 4 GLU C 32 SER C 37 -1 N THR C 34 O SER C 64
SHEET 4 AB2 4 LYS C 40 SER C 43 -1 O LYS C 40 N SER C 37
SHEET 1 AB3 4 PHE D 2 THR D 7 0
SHEET 2 AB3 4 VAL D 60 GLU D 66 -1 O VAL D 61 N VAL D 6
SHEET 3 AB3 4 GLU D 32 SER D 37 -1 N THR D 34 O SER D 64
SHEET 4 AB3 4 LYS D 40 SER D 43 -1 O LYS D 40 N SER D 37
CISPEP 1 VAL A 452 LYS A 453 0 1.01
CISPEP 2 VAL B 452 LYS B 453 0 1.25
SITE 1 AC1 10 GLY A 273 GLY A 315 MET A 318 ARG A 319
SITE 2 AC1 10 ARG A 322 TYR A 341 GLY A 428 GLY A 432
SITE 3 AC1 10 HOH A 805 HOH A 810
SITE 1 AC2 5 HIS A 127 GLU A 134 MET A 210 PO4 A 705
SITE 2 AC2 5 ALA C 20
SITE 1 AC3 7 MET A 92 LEU A 261 GLN A 278 LYS A 453
SITE 2 AC3 7 GLU A 454 ALA A 455 THR A 456
SITE 1 AC4 6 LYS A 204 PRO A 205 HOH A 808 LYS B 204
SITE 2 AC4 6 PRO B 205 HOH B 710
SITE 1 AC5 4 HIS A 127 HEZ A 702 LYS C 24 LYS C 27
SITE 1 AC6 4 ASP A 197 LYS A 204 ASP B 197 LYS B 204
SITE 1 AC7 4 ARG A 265 SER A 473 ALA A 475 GLU A 476
SITE 1 AC8 11 GLY B 273 GLY B 315 MET B 318 ARG B 319
SITE 2 AC8 11 ARG B 322 TYR B 341 GLY B 428 LYS B 431
SITE 3 AC8 11 GLY B 432 HOH B 702 HOH B 706
SITE 1 AC9 6 HIS B 127 GLU B 134 ALA B 206 MET B 210
SITE 2 AC9 6 PO4 B 604 ALA D 20
SITE 1 AD1 3 GLU B 454 ALA B 455 THR B 456
SITE 1 AD2 3 HIS B 127 HEZ B 602 LYS D 24
SITE 1 AD3 3 ARG B 265 ALA B 475 GLU B 476
SITE 1 AD4 2 ASN C 38 LYS C 40
SITE 1 AD5 3 ASN D 38 LYS D 40 HOH D 201
CRYST1 101.016 101.016 344.453 90.00 90.00 120.00 P 32 2 1 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 0.009899 0.005715 0.000000 0.00000
SCALE2 0.000000 0.011431 0.000000 0.00000
SCALE3 0.000000 0.000000 0.002903 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
