HEADER TRANSFERASE 18-DEC-14 4XCW
TITLE CRYSTAL STRUCTURE OF MOLYBDENUM COFACTOR BIOSYNTHESIS PROTEIN MOGA
TITLE 2 FROM HELICOBACTER PYLORI STR. J99
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MOLYBDOPTERIN ADENYLYLTRANSFERASE;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 SYNONYM: MPT ADENYLYLTRANSFERASE;
COMPND 5 EC: 2.7.7.75;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HELICOBACTER PYLORI (STRAIN J99 / ATCC 700824);
SOURCE 3 ORGANISM_TAXID: 85963;
SOURCE 4 STRAIN: J99 / ATCC 700824;
SOURCE 5 GENE: MOG, MOGA, JHP_0735;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PMCSG53
KEYWDS MOLYBDENUM COFACTOR, MOLYBDOPTERIN, MPT, PROBABLE MOLYBDOPTERIN
KEYWDS 2 BINDING DOMAIN, ALPHA AND BETA PROTEIN, MOLYBDENUM COFACTOR
KEYWDS 3 BIOSYNTHESIS PROTEIN FOLD, STRUCTURAL GENOMICS, CENTER FOR
KEYWDS 4 STRUCTURAL GENOMICS OF INFECTIOUS DISEASES, CSGID, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.J.STOGIOS,O.ONOPRIYENKO,A.SAVCHENKO,W.F.ANDERSON,CENTER FOR
AUTHOR 2 STRUCTURAL GENOMICS OF INFECTIOUS DISEASES (CSGID)
REVDAT 2 27-SEP-23 4XCW 1 SOURCE REMARK
REVDAT 1 04-FEB-15 4XCW 0
JRNL AUTH P.J.STOGIOS,O.ONOPRIYENKO,A.SAVCHENKO,W.F.ANDERSON,
JRNL AUTH 2 CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS DISEASES
JRNL AUTH 3 (CSGID)
JRNL TITL TO BE PUBLISHED
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.77
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.080
REMARK 3 COMPLETENESS FOR RANGE (%) : 90.6
REMARK 3 NUMBER OF REFLECTIONS : 87879
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.164
REMARK 3 R VALUE (WORKING SET) : 0.164
REMARK 3 FREE R VALUE : 0.199
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.180
REMARK 3 FREE R VALUE TEST SET COUNT : 1916
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 24.7766 - 4.3318 0.98 6676 146 0.1361 0.1605
REMARK 3 2 4.3318 - 3.4412 0.98 6603 156 0.1412 0.1638
REMARK 3 3 3.4412 - 3.0071 0.97 6513 141 0.1668 0.2250
REMARK 3 4 3.0071 - 2.7325 0.96 6489 146 0.1805 0.2102
REMARK 3 5 2.7325 - 2.5369 0.95 6413 138 0.1783 0.2273
REMARK 3 6 2.5369 - 2.3874 0.93 6365 141 0.1802 0.2227
REMARK 3 7 2.3874 - 2.2679 0.93 6239 139 0.1699 0.1845
REMARK 3 8 2.2679 - 2.1693 0.91 6213 140 0.1678 0.2133
REMARK 3 9 2.1693 - 2.0858 0.90 6121 142 0.1775 0.2100
REMARK 3 10 2.0858 - 2.0139 0.89 6037 131 0.1822 0.2160
REMARK 3 11 2.0139 - 1.9509 0.87 5801 125 0.1992 0.2576
REMARK 3 12 1.9509 - 1.8952 0.85 5797 124 0.2089 0.2549
REMARK 3 13 1.8952 - 1.8453 0.81 5510 120 0.2256 0.3108
REMARK 3 14 1.8453 - 1.8003 0.77 5186 127 0.2461 0.2817
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) : 0.180
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.040
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 : 0.005 8438
REMARK 3 ANGLE : 0.972 11422
REMARK 3 CHIRALITY : 0.037 1323
REMARK 3 PLANARITY : 0.006 1470
REMARK 3 DIHEDRAL : 12.458 3322
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 30
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN A AND RESID -1:19)
REMARK 3 ORIGIN FOR THE GROUP (A): -55.7167 58.0774 25.6353
REMARK 3 T TENSOR
REMARK 3 T11: 0.1297 T22: 0.2774
REMARK 3 T33: 0.1739 T12: 0.0591
REMARK 3 T13: 0.0315 T23: 0.0371
REMARK 3 L TENSOR
REMARK 3 L11: 4.9304 L22: 3.0500
REMARK 3 L33: 4.1992 L12: -1.7313
REMARK 3 L13: 0.0102 L23: -2.2020
REMARK 3 S TENSOR
REMARK 3 S11: 0.0756 S12: -0.0553 S13: -0.0989
REMARK 3 S21: 0.2542 S22: -0.0570 S23: -0.0239
REMARK 3 S31: -0.1607 S32: -0.4985 S33: -0.0304
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN A AND RESID 20:40)
REMARK 3 ORIGIN FOR THE GROUP (A): -54.7533 63.1180 18.6569
REMARK 3 T TENSOR
REMARK 3 T11: 0.2409 T22: 0.2733
REMARK 3 T33: 0.2824 T12: 0.0750
REMARK 3 T13: 0.0185 T23: 0.0294
REMARK 3 L TENSOR
REMARK 3 L11: 6.7963 L22: 7.6078
REMARK 3 L33: 6.0798 L12: 4.9398
REMARK 3 L13: 2.3006 L23: 3.6148
REMARK 3 S TENSOR
REMARK 3 S11: 0.0126 S12: 0.2470 S13: 0.7205
REMARK 3 S21: -0.5279 S22: -0.0661 S23: 0.6604
REMARK 3 S31: -0.7858 S32: -0.3135 S33: 0.0728
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN A AND RESID 41:66)
REMARK 3 ORIGIN FOR THE GROUP (A): -50.8388 62.9457 35.2364
REMARK 3 T TENSOR
REMARK 3 T11: 0.3027 T22: 0.3629
REMARK 3 T33: 0.2833 T12: 0.0660
REMARK 3 T13: 0.0670 T23: 0.0105
REMARK 3 L TENSOR
REMARK 3 L11: 3.2377 L22: 5.8419
REMARK 3 L33: 7.1004 L12: 3.5647
REMARK 3 L13: 3.5986 L23: 3.0804
REMARK 3 S TENSOR
REMARK 3 S11: 0.0266 S12: -0.4558 S13: 0.3089
REMARK 3 S21: 0.4256 S22: -0.1492 S23: 0.4133
REMARK 3 S31: -0.4764 S32: -0.3860 S33: 0.2367
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN A AND RESID 67:162)
REMARK 3 ORIGIN FOR THE GROUP (A): -41.1694 59.1674 24.2578
REMARK 3 T TENSOR
REMARK 3 T11: 0.2039 T22: 0.2225
REMARK 3 T33: 0.2256 T12: 0.0105
REMARK 3 T13: -0.0119 T23: 0.0269
REMARK 3 L TENSOR
REMARK 3 L11: 3.0524 L22: 1.8295
REMARK 3 L33: 1.3022 L12: 1.3980
REMARK 3 L13: -0.3304 L23: 0.1262
REMARK 3 S TENSOR
REMARK 3 S11: -0.0528 S12: 0.0662 S13: -0.0370
REMARK 3 S21: -0.0385 S22: 0.0991 S23: 0.0004
REMARK 3 S31: -0.0415 S32: -0.0469 S33: -0.0453
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: (CHAIN A AND RESID 163:176)
REMARK 3 ORIGIN FOR THE GROUP (A): -49.1418 46.0220 13.1215
REMARK 3 T TENSOR
REMARK 3 T11: 0.3086 T22: 0.3247
REMARK 3 T33: 0.4071 T12: -0.0103
REMARK 3 T13: -0.0066 T23: -0.0676
REMARK 3 L TENSOR
REMARK 3 L11: 2.8341 L22: 7.5722
REMARK 3 L33: 4.9391 L12: -4.1109
REMARK 3 L13: -0.5491 L23: -1.3623
REMARK 3 S TENSOR
REMARK 3 S11: 0.0065 S12: 0.2861 S13: -0.7220
REMARK 3 S21: -0.8141 S22: -0.0258 S23: 0.2223
REMARK 3 S31: 0.5828 S32: 0.0699 S33: -0.0668
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: (CHAIN B AND RESID -1:15)
REMARK 3 ORIGIN FOR THE GROUP (A): -12.0615 77.8150 27.3100
REMARK 3 T TENSOR
REMARK 3 T11: 0.2254 T22: 0.2791
REMARK 3 T33: 0.2700 T12: -0.1237
REMARK 3 T13: 0.0137 T23: -0.0417
REMARK 3 L TENSOR
REMARK 3 L11: 5.6293 L22: 7.5002
REMARK 3 L33: 7.2601 L12: -1.5425
REMARK 3 L13: 0.2604 L23: -2.4183
REMARK 3 S TENSOR
REMARK 3 S11: -0.1017 S12: 0.0667 S13: 0.5791
REMARK 3 S21: 0.1801 S22: -0.1496 S23: -0.6235
REMARK 3 S31: -0.2810 S32: 0.7028 S33: 0.3068
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: (CHAIN B AND RESID 16:23)
REMARK 3 ORIGIN FOR THE GROUP (A): 2.1718 67.1567 23.6246
REMARK 3 T TENSOR
REMARK 3 T11: 0.7857 T22: 0.9498
REMARK 3 T33: 0.7657 T12: 0.0449
REMARK 3 T13: -0.0653 T23: 0.1005
REMARK 3 L TENSOR
REMARK 3 L11: 5.5299 L22: 7.3235
REMARK 3 L33: 8.5274 L12: -6.3459
REMARK 3 L13: 6.8494 L23: -7.8135
REMARK 3 S TENSOR
REMARK 3 S11: -0.9846 S12: -0.6513 S13: -0.3056
REMARK 3 S21: 2.5076 S22: 0.0116 S23: -1.5878
REMARK 3 S31: -0.1004 S32: 1.7932 S33: 0.9045
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: (CHAIN B AND RESID 24:73)
REMARK 3 ORIGIN FOR THE GROUP (A): -12.1565 75.2842 29.0505
REMARK 3 T TENSOR
REMARK 3 T11: 0.1929 T22: 0.2414
REMARK 3 T33: 0.3356 T12: -0.0705
REMARK 3 T13: -0.0200 T23: -0.0372
REMARK 3 L TENSOR
REMARK 3 L11: 2.8290 L22: 4.3953
REMARK 3 L33: 6.5318 L12: -1.0568
REMARK 3 L13: -0.1739 L23: -1.7864
REMARK 3 S TENSOR
REMARK 3 S11: -0.0725 S12: -0.1367 S13: 0.4037
REMARK 3 S21: 0.1342 S22: 0.0136 S23: -0.6734
REMARK 3 S31: -0.3285 S32: 0.5572 S33: 0.0590
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: (CHAIN B AND RESID 74:131)
REMARK 3 ORIGIN FOR THE GROUP (A): -19.3027 62.4950 26.1943
REMARK 3 T TENSOR
REMARK 3 T11: 0.1576 T22: 0.1541
REMARK 3 T33: 0.1550 T12: -0.0082
REMARK 3 T13: 0.0088 T23: 0.0163
REMARK 3 L TENSOR
REMARK 3 L11: 3.5071 L22: 6.2729
REMARK 3 L33: 1.1806 L12: -2.3542
REMARK 3 L13: 0.1442 L23: 1.2474
REMARK 3 S TENSOR
REMARK 3 S11: 0.0565 S12: 0.0137 S13: -0.0900
REMARK 3 S21: -0.1120 S22: -0.0507 S23: -0.0916
REMARK 3 S31: -0.0505 S32: 0.0268 S33: -0.0083
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: (CHAIN B AND RESID 132:176)
REMARK 3 ORIGIN FOR THE GROUP (A): -22.2055 75.8600 17.3086
REMARK 3 T TENSOR
REMARK 3 T11: 0.2612 T22: 0.2109
REMARK 3 T33: 0.1941 T12: -0.0307
REMARK 3 T13: -0.0094 T23: 0.0527
REMARK 3 L TENSOR
REMARK 3 L11: 2.4470 L22: 4.7750
REMARK 3 L33: 5.3049 L12: -0.6468
REMARK 3 L13: -0.3335 L23: 0.2266
REMARK 3 S TENSOR
REMARK 3 S11: 0.1305 S12: 0.4970 S13: 0.3298
REMARK 3 S21: -0.6468 S22: -0.1013 S23: -0.0470
REMARK 3 S31: -0.2268 S32: -0.1576 S33: -0.0192
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: (CHAIN C AND RESID -1:12)
REMARK 3 ORIGIN FOR THE GROUP (A): -12.8809 33.2301 26.6797
REMARK 3 T TENSOR
REMARK 3 T11: 0.3195 T22: 0.2283
REMARK 3 T33: 0.6859 T12: 0.0691
REMARK 3 T13: 0.0370 T23: -0.0191
REMARK 3 L TENSOR
REMARK 3 L11: 9.5690 L22: 3.3593
REMARK 3 L33: 8.4038 L12: -3.0225
REMARK 3 L13: -6.4656 L23: 1.5805
REMARK 3 S TENSOR
REMARK 3 S11: -0.5700 S12: -0.2993 S13: -0.9425
REMARK 3 S21: 0.2920 S22: 0.2290 S23: -0.3418
REMARK 3 S31: 0.4890 S32: 0.4391 S33: 0.4372
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: (CHAIN C AND RESID 13:22)
REMARK 3 ORIGIN FOR THE GROUP (A): -35.5937 25.8528 27.9321
REMARK 3 T TENSOR
REMARK 3 T11: 0.8751 T22: 1.4457
REMARK 3 T33: 1.5092 T12: 0.3329
REMARK 3 T13: 0.0139 T23: 0.1716
REMARK 3 L TENSOR
REMARK 3 L11: 5.9536 L22: 6.0792
REMARK 3 L33: 1.3933 L12: 4.4721
REMARK 3 L13: -0.9285 L23: -2.3352
REMARK 3 S TENSOR
REMARK 3 S11: 0.5565 S12: -1.1808 S13: 1.5463
REMARK 3 S21: -0.2895 S22: 0.3968 S23: -0.5937
REMARK 3 S31: 0.2586 S32: -0.7284 S33: -1.1247
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: (CHAIN C AND RESID 23:49)
REMARK 3 ORIGIN FOR THE GROUP (A): -19.4114 30.7109 23.5776
REMARK 3 T TENSOR
REMARK 3 T11: 0.3762 T22: 0.2273
REMARK 3 T33: 0.7024 T12: 0.0127
REMARK 3 T13: 0.1074 T23: -0.0977
REMARK 3 L TENSOR
REMARK 3 L11: 5.6562 L22: 3.5720
REMARK 3 L33: 5.3235 L12: 2.6248
REMARK 3 L13: -1.5881 L23: -1.1717
REMARK 3 S TENSOR
REMARK 3 S11: -0.3165 S12: 0.1288 S13: -1.0696
REMARK 3 S21: 0.0677 S22: 0.1345 S23: 0.2575
REMARK 3 S31: 0.6337 S32: -0.0948 S33: 0.1832
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: (CHAIN C AND RESID 50:130)
REMARK 3 ORIGIN FOR THE GROUP (A): -25.4404 43.3780 29.7526
REMARK 3 T TENSOR
REMARK 3 T11: 0.1970 T22: 0.1893
REMARK 3 T33: 0.2794 T12: 0.0311
REMARK 3 T13: 0.0282 T23: 0.0054
REMARK 3 L TENSOR
REMARK 3 L11: 5.6719 L22: 2.4824
REMARK 3 L33: 1.9501 L12: -0.5254
REMARK 3 L13: 0.6731 L23: -0.6936
REMARK 3 S TENSOR
REMARK 3 S11: -0.0795 S12: -0.2136 S13: -0.5426
REMARK 3 S21: 0.1530 S22: 0.1039 S23: 0.1409
REMARK 3 S31: 0.1322 S32: 0.0194 S33: -0.0353
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: (CHAIN C AND RESID 131:175)
REMARK 3 ORIGIN FOR THE GROUP (A): -15.1757 41.4824 17.9057
REMARK 3 T TENSOR
REMARK 3 T11: 0.2468 T22: 0.3117
REMARK 3 T33: 0.3061 T12: 0.0314
REMARK 3 T13: 0.0333 T23: -0.1008
REMARK 3 L TENSOR
REMARK 3 L11: 3.6216 L22: 3.3983
REMARK 3 L33: 4.4455 L12: -0.4948
REMARK 3 L13: 0.2448 L23: 0.9271
REMARK 3 S TENSOR
REMARK 3 S11: -0.0333 S12: 0.9176 S13: -0.5847
REMARK 3 S21: -0.4343 S22: 0.0156 S23: -0.0725
REMARK 3 S31: 0.1723 S32: 0.1623 S33: 0.0251
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: (CHAIN D AND RESID -1:28)
REMARK 3 ORIGIN FOR THE GROUP (A): -71.3641 30.0803 60.8523
REMARK 3 T TENSOR
REMARK 3 T11: 0.2376 T22: 0.4298
REMARK 3 T33: 0.4199 T12: -0.0887
REMARK 3 T13: -0.0428 T23: 0.0307
REMARK 3 L TENSOR
REMARK 3 L11: 3.3196 L22: 7.6811
REMARK 3 L33: 7.6496 L12: 1.5200
REMARK 3 L13: 1.7828 L23: -0.3160
REMARK 3 S TENSOR
REMARK 3 S11: -0.3697 S12: -0.3486 S13: 0.3295
REMARK 3 S21: 0.2776 S22: 0.2728 S23: 0.9910
REMARK 3 S31: -0.1341 S32: -1.2281 S33: 0.0580
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: (CHAIN D AND RESID 29:66)
REMARK 3 ORIGIN FOR THE GROUP (A): -67.4067 29.3892 65.4479
REMARK 3 T TENSOR
REMARK 3 T11: 0.2571 T22: 0.3513
REMARK 3 T33: 0.3337 T12: -0.0533
REMARK 3 T13: -0.0451 T23: 0.0631
REMARK 3 L TENSOR
REMARK 3 L11: 2.2643 L22: 5.6859
REMARK 3 L33: 3.3675 L12: -1.0099
REMARK 3 L13: -1.4035 L23: 2.6818
REMARK 3 S TENSOR
REMARK 3 S11: -0.0213 S12: -0.1395 S13: -0.3214
REMARK 3 S21: 0.2394 S22: -0.1169 S23: 0.6073
REMARK 3 S31: 0.1948 S32: -0.7711 S33: 0.2020
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: (CHAIN D AND RESID 67:116)
REMARK 3 ORIGIN FOR THE GROUP (A): -61.3071 42.9204 61.4160
REMARK 3 T TENSOR
REMARK 3 T11: 0.2006 T22: 0.2143
REMARK 3 T33: 0.1824 T12: -0.0226
REMARK 3 T13: -0.0370 T23: -0.0164
REMARK 3 L TENSOR
REMARK 3 L11: 2.2694 L22: 6.1950
REMARK 3 L33: 0.9638 L12: -1.1526
REMARK 3 L13: -0.2000 L23: -1.1724
REMARK 3 S TENSOR
REMARK 3 S11: 0.0601 S12: 0.0248 S13: 0.0071
REMARK 3 S21: -0.0974 S22: -0.0638 S23: 0.0380
REMARK 3 S31: 0.0781 S32: -0.0677 S33: 0.0115
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: (CHAIN D AND RESID 117:166)
REMARK 3 ORIGIN FOR THE GROUP (A): -59.1071 32.2412 57.4169
REMARK 3 T TENSOR
REMARK 3 T11: 0.2243 T22: 0.1912
REMARK 3 T33: 0.2064 T12: -0.0458
REMARK 3 T13: -0.0201 T23: 0.0055
REMARK 3 L TENSOR
REMARK 3 L11: 2.7935 L22: 4.7591
REMARK 3 L33: 3.0689 L12: -0.4900
REMARK 3 L13: -0.0601 L23: -0.0582
REMARK 3 S TENSOR
REMARK 3 S11: 0.0558 S12: 0.1958 S13: -0.2271
REMARK 3 S21: -0.4693 S22: 0.0198 S23: 0.1263
REMARK 3 S31: 0.1537 S32: -0.1500 S33: -0.0867
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: (CHAIN D AND RESID 167:176)
REMARK 3 ORIGIN FOR THE GROUP (A): -51.1216 25.9677 48.5937
REMARK 3 T TENSOR
REMARK 3 T11: 0.6777 T22: 0.5819
REMARK 3 T33: 0.4936 T12: -0.0010
REMARK 3 T13: 0.1083 T23: -0.1115
REMARK 3 L TENSOR
REMARK 3 L11: 3.2699 L22: 2.4364
REMARK 3 L33: 8.3680 L12: 1.5197
REMARK 3 L13: 3.9862 L23: -0.2546
REMARK 3 S TENSOR
REMARK 3 S11: -0.4353 S12: 1.9079 S13: -0.8460
REMARK 3 S21: -0.7673 S22: 0.3887 S23: -0.6847
REMARK 3 S31: 0.5455 S32: 1.2029 S33: -0.0216
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: (CHAIN E AND RESID -1:15)
REMARK 3 ORIGIN FOR THE GROUP (A): -61.7146 72.7477 63.3876
REMARK 3 T TENSOR
REMARK 3 T11: 0.2638 T22: 0.1368
REMARK 3 T33: 0.2349 T12: 0.0382
REMARK 3 T13: 0.0095 T23: 0.0190
REMARK 3 L TENSOR
REMARK 3 L11: 7.8154 L22: 5.8413
REMARK 3 L33: 6.2971 L12: -0.1437
REMARK 3 L13: 0.8929 L23: 0.0933
REMARK 3 S TENSOR
REMARK 3 S11: -0.1592 S12: -0.1358 S13: 0.9642
REMARK 3 S21: 0.1235 S22: -0.0250 S23: -0.1479
REMARK 3 S31: -0.4869 S32: 0.0480 S33: 0.2585
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: (CHAIN E AND RESID 18:22)
REMARK 3 ORIGIN FOR THE GROUP (A): -45.9319 81.8464 59.6837
REMARK 3 T TENSOR
REMARK 3 T11: 1.0355 T22: 0.9616
REMARK 3 T33: 1.2903 T12: -0.0732
REMARK 3 T13: 0.1416 T23: 0.4595
REMARK 3 L TENSOR
REMARK 3 L11: 7.8787 L22: 6.7059
REMARK 3 L33: 3.1651 L12: 7.2746
REMARK 3 L13: 4.9880 L23: 4.5925
REMARK 3 S TENSOR
REMARK 3 S11: 0.5383 S12: 1.1374 S13: 2.6052
REMARK 3 S21: -0.9311 S22: 0.3286 S23: -0.4318
REMARK 3 S31: -1.3741 S32: -0.4736 S33: -0.8617
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: (CHAIN E AND RESID 23:66)
REMARK 3 ORIGIN FOR THE GROUP (A): -59.1533 72.0230 64.8322
REMARK 3 T TENSOR
REMARK 3 T11: 0.2562 T22: 0.1680
REMARK 3 T33: 0.3163 T12: 0.0348
REMARK 3 T13: -0.0123 T23: -0.0579
REMARK 3 L TENSOR
REMARK 3 L11: 4.9104 L22: 2.6661
REMARK 3 L33: 7.1445 L12: -0.1828
REMARK 3 L13: 2.6615 L23: -0.7021
REMARK 3 S TENSOR
REMARK 3 S11: -0.1322 S12: -0.1970 S13: 0.5893
REMARK 3 S21: 0.1435 S22: -0.0313 S23: -0.0582
REMARK 3 S31: -0.4399 S32: -0.0168 S33: 0.1621
REMARK 3 TLS GROUP : 24
REMARK 3 SELECTION: (CHAIN E AND RESID 67:163)
REMARK 3 ORIGIN FOR THE GROUP (A): -56.1722 61.0312 60.1960
REMARK 3 T TENSOR
REMARK 3 T11: 0.2258 T22: 0.2107
REMARK 3 T33: 0.1825 T12: 0.0239
REMARK 3 T13: -0.0190 T23: 0.0029
REMARK 3 L TENSOR
REMARK 3 L11: 4.5702 L22: 1.5220
REMARK 3 L33: 0.9677 L12: -0.8515
REMARK 3 L13: -0.5116 L23: 0.6206
REMARK 3 S TENSOR
REMARK 3 S11: 0.1249 S12: 0.1286 S13: 0.1894
REMARK 3 S21: -0.1260 S22: -0.0693 S23: -0.0029
REMARK 3 S31: -0.0134 S32: -0.0387 S33: -0.0517
REMARK 3 TLS GROUP : 25
REMARK 3 SELECTION: (CHAIN E AND RESID 164:176)
REMARK 3 ORIGIN FOR THE GROUP (A): -70.8947 61.4752 48.3613
REMARK 3 T TENSOR
REMARK 3 T11: 0.4557 T22: 0.3819
REMARK 3 T33: 0.3241 T12: -0.0267
REMARK 3 T13: -0.0797 T23: -0.0072
REMARK 3 L TENSOR
REMARK 3 L11: 2.5399 L22: 3.5573
REMARK 3 L33: 3.0023 L12: 2.2947
REMARK 3 L13: -1.0348 L23: -2.8747
REMARK 3 S TENSOR
REMARK 3 S11: -0.2561 S12: 0.5101 S13: 0.1303
REMARK 3 S21: -0.9693 S22: 0.3393 S23: 0.4155
REMARK 3 S31: 0.6873 S32: -0.5761 S33: -0.0923
REMARK 3 TLS GROUP : 26
REMARK 3 SELECTION: (CHAIN F AND RESID -1:23)
REMARK 3 ORIGIN FOR THE GROUP (A): -25.5528 42.6233 63.1589
REMARK 3 T TENSOR
REMARK 3 T11: 0.2687 T22: 0.3787
REMARK 3 T33: 0.8770 T12: 0.0802
REMARK 3 T13: 0.0495 T23: 0.0456
REMARK 3 L TENSOR
REMARK 3 L11: 2.7791 L22: 9.0035
REMARK 3 L33: 6.4444 L12: -0.9017
REMARK 3 L13: -0.0954 L23: 0.1109
REMARK 3 S TENSOR
REMARK 3 S11: -0.0647 S12: -0.6423 S13: -1.2929
REMARK 3 S21: 0.0565 S22: -0.4245 S23: -1.1409
REMARK 3 S31: 0.7649 S32: 0.7086 S33: 0.0344
REMARK 3 TLS GROUP : 27
REMARK 3 SELECTION: (CHAIN F AND RESID 24:74)
REMARK 3 ORIGIN FOR THE GROUP (A): -27.7570 43.7189 65.6045
REMARK 3 T TENSOR
REMARK 3 T11: 0.2514 T22: 0.3115
REMARK 3 T33: 0.6905 T12: 0.0322
REMARK 3 T13: -0.0572 T23: 0.0503
REMARK 3 L TENSOR
REMARK 3 L11: 3.7682 L22: 4.2114
REMARK 3 L33: 4.7720 L12: 1.5976
REMARK 3 L13: -1.7250 L23: 0.3772
REMARK 3 S TENSOR
REMARK 3 S11: 0.0745 S12: -0.4304 S13: -1.1617
REMARK 3 S21: 0.3045 S22: -0.2230 S23: -1.2789
REMARK 3 S31: 0.3258 S32: 0.4845 S33: 0.1072
REMARK 3 TLS GROUP : 28
REMARK 3 SELECTION: (CHAIN F AND RESID 75:119)
REMARK 3 ORIGIN FOR THE GROUP (A): -43.7479 41.8413 61.2921
REMARK 3 T TENSOR
REMARK 3 T11: 0.1580 T22: 0.2125
REMARK 3 T33: 0.2357 T12: 0.0068
REMARK 3 T13: 0.0149 T23: 0.0210
REMARK 3 L TENSOR
REMARK 3 L11: 3.5266 L22: 7.0173
REMARK 3 L33: 1.9036 L12: 2.8136
REMARK 3 L13: 1.3215 L23: 0.9287
REMARK 3 S TENSOR
REMARK 3 S11: -0.0072 S12: 0.0076 S13: -0.3654
REMARK 3 S21: -0.1305 S22: 0.1318 S23: -0.3038
REMARK 3 S31: 0.2001 S32: 0.0685 S33: -0.0783
REMARK 3 TLS GROUP : 29
REMARK 3 SELECTION: (CHAIN F AND RESID 120:169)
REMARK 3 ORIGIN FOR THE GROUP (A): -32.3578 50.5964 57.0849
REMARK 3 T TENSOR
REMARK 3 T11: 0.2274 T22: 0.2279
REMARK 3 T33: 0.3089 T12: -0.0250
REMARK 3 T13: 0.0682 T23: -0.0483
REMARK 3 L TENSOR
REMARK 3 L11: 3.4744 L22: 4.5813
REMARK 3 L33: 2.6977 L12: 1.5351
REMARK 3 L13: -0.8857 L23: 0.2213
REMARK 3 S TENSOR
REMARK 3 S11: -0.2385 S12: 0.2593 S13: -0.3795
REMARK 3 S21: -0.5622 S22: 0.2154 S23: -0.6986
REMARK 3 S31: 0.1195 S32: 0.1670 S33: -0.0140
REMARK 3 TLS GROUP : 30
REMARK 3 SELECTION: (CHAIN F AND RESID 170:176)
REMARK 3 ORIGIN FOR THE GROUP (A): -33.9594 63.2537 51.2377
REMARK 3 T TENSOR
REMARK 3 T11: 0.7576 T22: 0.4366
REMARK 3 T33: 0.5019 T12: -0.0845
REMARK 3 T13: 0.0384 T23: 0.0383
REMARK 3 L TENSOR
REMARK 3 L11: 4.7197 L22: 4.8631
REMARK 3 L33: 3.5172 L12: -4.5728
REMARK 3 L13: 0.4457 L23: -1.0786
REMARK 3 S TENSOR
REMARK 3 S11: -0.0689 S12: 1.0522 S13: 1.1292
REMARK 3 S21: -1.9808 S22: 0.2731 S23: -0.8937
REMARK 3 S31: -2.1404 S32: -0.1816 S33: -0.2008
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 4XCW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-DEC-14.
REMARK 100 THE DEPOSITION ID IS D_1000205455.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 31-OCT-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 91170
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.1
REMARK 200 DATA REDUNDANCY : 3.100
REMARK 200 R MERGE (I) : 0.04000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 36.9800
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.83
REMARK 200 COMPLETENESS FOR SHELL (%) : 90.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.10
REMARK 200 R MERGE FOR SHELL (I) : 0.59600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.670
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX (PHENIX.PHASER)
REMARK 200 STARTING MODEL: 2QQ1
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.29
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25%PEG 3350. 0.2M CALCIUM CHLORIDE
REMARK 280 DIHYDRATE, 0.1 M TRIS, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 310K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4480 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23770 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -40.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4500 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23770 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -40.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E, F
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 ASP A 13
REMARK 465 ARG A 14
REMARK 465 ALA A 15
REMARK 465 SER A 16
REMARK 465 LYS A 17
REMARK 465 GLN C 176
REMARK 465 LYS D 17
REMARK 465 GLY D 18
REMARK 465 VAL D 19
REMARK 465 SER E 16
REMARK 465 LYS E 17
REMARK 465 LYS F 17
REMARK 465 GLY F 18
REMARK 465 VAL F 19
REMARK 465 TYR F 20
REMARK 465 GLU F 21
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 NE2 GLN D 176 O HOH D 201 1.02
REMARK 500 CD GLN D 176 O HOH D 201 2.14
REMARK 500 OD2 ASP A 22 OH TYR A 44 2.16
REMARK 500 O HOH E 245 O HOH E 248 2.19
REMARK 500 O HOH E 279 O HOH E 342 2.19
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 ASN A 125 -112.07 52.97
REMARK 500 LEU A 158 30.05 72.68
REMARK 500 SER B 16 -50.23 -124.81
REMARK 500 ASN B 125 -112.77 53.92
REMARK 500 LYS B 175 -147.86 -81.71
REMARK 500 ARG C 14 -100.91 64.39
REMARK 500 GLU C 21 -17.47 -47.56
REMARK 500 ASP C 49 48.81 -69.23
REMARK 500 TYR C 110 -61.69 -97.08
REMARK 500 ASN C 125 -115.97 53.92
REMARK 500 PRO C 133 -174.88 -66.30
REMARK 500 LEU C 158 31.24 72.21
REMARK 500 ARG D 14 -16.76 68.75
REMARK 500 ALA D 15 41.68 -85.24
REMARK 500 ASP D 22 79.00 -65.62
REMARK 500 ASN D 125 -113.12 53.68
REMARK 500 PRO D 133 -169.03 -76.45
REMARK 500 ASP E 22 82.10 -153.90
REMARK 500 ASN E 125 -113.53 53.03
REMARK 500 PRO E 133 -170.91 -68.44
REMARK 500 ASN F 125 -113.73 53.22
REMARK 500 LEU F 158 31.92 72.52
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 362 DISTANCE = 6.07 ANGSTROMS
REMARK 525 HOH A 382 DISTANCE = 7.36 ANGSTROMS
REMARK 525 HOH A 384 DISTANCE = 5.81 ANGSTROMS
REMARK 525 HOH B 316 DISTANCE = 6.11 ANGSTROMS
REMARK 525 HOH B 359 DISTANCE = 6.74 ANGSTROMS
REMARK 525 HOH B 373 DISTANCE = 7.06 ANGSTROMS
REMARK 525 HOH C 307 DISTANCE = 7.20 ANGSTROMS
REMARK 525 HOH C 360 DISTANCE = 7.18 ANGSTROMS
REMARK 525 HOH D 322 DISTANCE = 6.30 ANGSTROMS
REMARK 525 HOH D 351 DISTANCE = 6.20 ANGSTROMS
REMARK 525 HOH D 384 DISTANCE = 6.39 ANGSTROMS
REMARK 525 HOH D 389 DISTANCE = 6.74 ANGSTROMS
REMARK 525 HOH E 378 DISTANCE = 6.32 ANGSTROMS
REMARK 525 HOH F 349 DISTANCE = 6.61 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: CSGID-IDP06143 RELATED DB: TARGETTRACK
DBREF 4XCW A 1 176 UNP Q9ZL45 MOG_HELPJ 1 176
DBREF 4XCW B 1 176 UNP Q9ZL45 MOG_HELPJ 1 176
DBREF 4XCW C 1 176 UNP Q9ZL45 MOG_HELPJ 1 176
DBREF 4XCW D 1 176 UNP Q9ZL45 MOG_HELPJ 1 176
DBREF 4XCW E 1 176 UNP Q9ZL45 MOG_HELPJ 1 176
DBREF 4XCW F 1 176 UNP Q9ZL45 MOG_HELPJ 1 176
SEQADV 4XCW GLN A -1 UNP Q9ZL45 EXPRESSION TAG
SEQADV 4XCW GLY A 0 UNP Q9ZL45 EXPRESSION TAG
SEQADV 4XCW GLN B -1 UNP Q9ZL45 EXPRESSION TAG
SEQADV 4XCW GLY B 0 UNP Q9ZL45 EXPRESSION TAG
SEQADV 4XCW GLN C -1 UNP Q9ZL45 EXPRESSION TAG
SEQADV 4XCW GLY C 0 UNP Q9ZL45 EXPRESSION TAG
SEQADV 4XCW GLN D -1 UNP Q9ZL45 EXPRESSION TAG
SEQADV 4XCW GLY D 0 UNP Q9ZL45 EXPRESSION TAG
SEQADV 4XCW GLN E -1 UNP Q9ZL45 EXPRESSION TAG
SEQADV 4XCW GLY E 0 UNP Q9ZL45 EXPRESSION TAG
SEQADV 4XCW GLN F -1 UNP Q9ZL45 EXPRESSION TAG
SEQADV 4XCW GLY F 0 UNP Q9ZL45 EXPRESSION TAG
SEQRES 1 A 178 GLN GLY MET GLN THR ILE HIS ILE GLY VAL LEU SER ALA
SEQRES 2 A 178 SER ASP ARG ALA SER LYS GLY VAL TYR GLU ASP LEU SER
SEQRES 3 A 178 GLY LYS ALA ILE GLN GLU VAL LEU SER GLU TYR LEU LEU
SEQRES 4 A 178 ASN PRO LEU GLU PHE HIS TYR GLU ILE VAL ALA ASP GLU
SEQRES 5 A 178 ARG ASP LEU ILE GLU LYS SER LEU ILE LYS MET CYS ASP
SEQRES 6 A 178 GLU TYR GLN CYS ASP LEU VAL VAL THR THR GLY GLY THR
SEQRES 7 A 178 GLY PRO ALA LEU ARG ASP ILE THR PRO GLU ALA THR LYS
SEQRES 8 A 178 LYS VAL CYS GLN LYS MET LEU PRO GLY PHE GLY GLU LEU
SEQRES 9 A 178 MET ARG MET THR SER LEU LYS TYR VAL PRO THR ALA ILE
SEQRES 10 A 178 LEU SER ARG GLN SER ALA GLY ILE ARG ASN LYS SER LEU
SEQRES 11 A 178 ILE ILE ASN LEU PRO GLY LYS PRO LYS SER ILE ARG GLU
SEQRES 12 A 178 CYS LEU GLU ALA VAL PHE PRO ALA ILE PRO TYR CYS VAL
SEQRES 13 A 178 ASP LEU ILE LEU GLY ASN TYR MET GLN VAL ASN GLU LYS
SEQRES 14 A 178 ASN ILE GLN ALA PHE ARG PRO LYS GLN
SEQRES 1 B 178 GLN GLY MET GLN THR ILE HIS ILE GLY VAL LEU SER ALA
SEQRES 2 B 178 SER ASP ARG ALA SER LYS GLY VAL TYR GLU ASP LEU SER
SEQRES 3 B 178 GLY LYS ALA ILE GLN GLU VAL LEU SER GLU TYR LEU LEU
SEQRES 4 B 178 ASN PRO LEU GLU PHE HIS TYR GLU ILE VAL ALA ASP GLU
SEQRES 5 B 178 ARG ASP LEU ILE GLU LYS SER LEU ILE LYS MET CYS ASP
SEQRES 6 B 178 GLU TYR GLN CYS ASP LEU VAL VAL THR THR GLY GLY THR
SEQRES 7 B 178 GLY PRO ALA LEU ARG ASP ILE THR PRO GLU ALA THR LYS
SEQRES 8 B 178 LYS VAL CYS GLN LYS MET LEU PRO GLY PHE GLY GLU LEU
SEQRES 9 B 178 MET ARG MET THR SER LEU LYS TYR VAL PRO THR ALA ILE
SEQRES 10 B 178 LEU SER ARG GLN SER ALA GLY ILE ARG ASN LYS SER LEU
SEQRES 11 B 178 ILE ILE ASN LEU PRO GLY LYS PRO LYS SER ILE ARG GLU
SEQRES 12 B 178 CYS LEU GLU ALA VAL PHE PRO ALA ILE PRO TYR CYS VAL
SEQRES 13 B 178 ASP LEU ILE LEU GLY ASN TYR MET GLN VAL ASN GLU LYS
SEQRES 14 B 178 ASN ILE GLN ALA PHE ARG PRO LYS GLN
SEQRES 1 C 178 GLN GLY MET GLN THR ILE HIS ILE GLY VAL LEU SER ALA
SEQRES 2 C 178 SER ASP ARG ALA SER LYS GLY VAL TYR GLU ASP LEU SER
SEQRES 3 C 178 GLY LYS ALA ILE GLN GLU VAL LEU SER GLU TYR LEU LEU
SEQRES 4 C 178 ASN PRO LEU GLU PHE HIS TYR GLU ILE VAL ALA ASP GLU
SEQRES 5 C 178 ARG ASP LEU ILE GLU LYS SER LEU ILE LYS MET CYS ASP
SEQRES 6 C 178 GLU TYR GLN CYS ASP LEU VAL VAL THR THR GLY GLY THR
SEQRES 7 C 178 GLY PRO ALA LEU ARG ASP ILE THR PRO GLU ALA THR LYS
SEQRES 8 C 178 LYS VAL CYS GLN LYS MET LEU PRO GLY PHE GLY GLU LEU
SEQRES 9 C 178 MET ARG MET THR SER LEU LYS TYR VAL PRO THR ALA ILE
SEQRES 10 C 178 LEU SER ARG GLN SER ALA GLY ILE ARG ASN LYS SER LEU
SEQRES 11 C 178 ILE ILE ASN LEU PRO GLY LYS PRO LYS SER ILE ARG GLU
SEQRES 12 C 178 CYS LEU GLU ALA VAL PHE PRO ALA ILE PRO TYR CYS VAL
SEQRES 13 C 178 ASP LEU ILE LEU GLY ASN TYR MET GLN VAL ASN GLU LYS
SEQRES 14 C 178 ASN ILE GLN ALA PHE ARG PRO LYS GLN
SEQRES 1 D 178 GLN GLY MET GLN THR ILE HIS ILE GLY VAL LEU SER ALA
SEQRES 2 D 178 SER ASP ARG ALA SER LYS GLY VAL TYR GLU ASP LEU SER
SEQRES 3 D 178 GLY LYS ALA ILE GLN GLU VAL LEU SER GLU TYR LEU LEU
SEQRES 4 D 178 ASN PRO LEU GLU PHE HIS TYR GLU ILE VAL ALA ASP GLU
SEQRES 5 D 178 ARG ASP LEU ILE GLU LYS SER LEU ILE LYS MET CYS ASP
SEQRES 6 D 178 GLU TYR GLN CYS ASP LEU VAL VAL THR THR GLY GLY THR
SEQRES 7 D 178 GLY PRO ALA LEU ARG ASP ILE THR PRO GLU ALA THR LYS
SEQRES 8 D 178 LYS VAL CYS GLN LYS MET LEU PRO GLY PHE GLY GLU LEU
SEQRES 9 D 178 MET ARG MET THR SER LEU LYS TYR VAL PRO THR ALA ILE
SEQRES 10 D 178 LEU SER ARG GLN SER ALA GLY ILE ARG ASN LYS SER LEU
SEQRES 11 D 178 ILE ILE ASN LEU PRO GLY LYS PRO LYS SER ILE ARG GLU
SEQRES 12 D 178 CYS LEU GLU ALA VAL PHE PRO ALA ILE PRO TYR CYS VAL
SEQRES 13 D 178 ASP LEU ILE LEU GLY ASN TYR MET GLN VAL ASN GLU LYS
SEQRES 14 D 178 ASN ILE GLN ALA PHE ARG PRO LYS GLN
SEQRES 1 E 178 GLN GLY MET GLN THR ILE HIS ILE GLY VAL LEU SER ALA
SEQRES 2 E 178 SER ASP ARG ALA SER LYS GLY VAL TYR GLU ASP LEU SER
SEQRES 3 E 178 GLY LYS ALA ILE GLN GLU VAL LEU SER GLU TYR LEU LEU
SEQRES 4 E 178 ASN PRO LEU GLU PHE HIS TYR GLU ILE VAL ALA ASP GLU
SEQRES 5 E 178 ARG ASP LEU ILE GLU LYS SER LEU ILE LYS MET CYS ASP
SEQRES 6 E 178 GLU TYR GLN CYS ASP LEU VAL VAL THR THR GLY GLY THR
SEQRES 7 E 178 GLY PRO ALA LEU ARG ASP ILE THR PRO GLU ALA THR LYS
SEQRES 8 E 178 LYS VAL CYS GLN LYS MET LEU PRO GLY PHE GLY GLU LEU
SEQRES 9 E 178 MET ARG MET THR SER LEU LYS TYR VAL PRO THR ALA ILE
SEQRES 10 E 178 LEU SER ARG GLN SER ALA GLY ILE ARG ASN LYS SER LEU
SEQRES 11 E 178 ILE ILE ASN LEU PRO GLY LYS PRO LYS SER ILE ARG GLU
SEQRES 12 E 178 CYS LEU GLU ALA VAL PHE PRO ALA ILE PRO TYR CYS VAL
SEQRES 13 E 178 ASP LEU ILE LEU GLY ASN TYR MET GLN VAL ASN GLU LYS
SEQRES 14 E 178 ASN ILE GLN ALA PHE ARG PRO LYS GLN
SEQRES 1 F 178 GLN GLY MET GLN THR ILE HIS ILE GLY VAL LEU SER ALA
SEQRES 2 F 178 SER ASP ARG ALA SER LYS GLY VAL TYR GLU ASP LEU SER
SEQRES 3 F 178 GLY LYS ALA ILE GLN GLU VAL LEU SER GLU TYR LEU LEU
SEQRES 4 F 178 ASN PRO LEU GLU PHE HIS TYR GLU ILE VAL ALA ASP GLU
SEQRES 5 F 178 ARG ASP LEU ILE GLU LYS SER LEU ILE LYS MET CYS ASP
SEQRES 6 F 178 GLU TYR GLN CYS ASP LEU VAL VAL THR THR GLY GLY THR
SEQRES 7 F 178 GLY PRO ALA LEU ARG ASP ILE THR PRO GLU ALA THR LYS
SEQRES 8 F 178 LYS VAL CYS GLN LYS MET LEU PRO GLY PHE GLY GLU LEU
SEQRES 9 F 178 MET ARG MET THR SER LEU LYS TYR VAL PRO THR ALA ILE
SEQRES 10 F 178 LEU SER ARG GLN SER ALA GLY ILE ARG ASN LYS SER LEU
SEQRES 11 F 178 ILE ILE ASN LEU PRO GLY LYS PRO LYS SER ILE ARG GLU
SEQRES 12 F 178 CYS LEU GLU ALA VAL PHE PRO ALA ILE PRO TYR CYS VAL
SEQRES 13 F 178 ASP LEU ILE LEU GLY ASN TYR MET GLN VAL ASN GLU LYS
SEQRES 14 F 178 ASN ILE GLN ALA PHE ARG PRO LYS GLN
FORMUL 7 HOH *1157(H2 O)
HELIX 1 AA1 ASP A 22 LEU A 36 1 15
HELIX 2 AA2 GLU A 50 GLU A 64 1 15
HELIX 3 AA3 ILE A 83 CYS A 92 1 10
HELIX 4 AA4 LEU A 96 LYS A 109 1 14
HELIX 5 AA5 TYR A 110 SER A 117 5 8
HELIX 6 AA6 LYS A 135 PHE A 147 1 13
HELIX 7 AA7 ALA A 149 ILE A 157 1 9
HELIX 8 AA8 ASP B 22 LEU B 36 1 15
HELIX 9 AA9 GLU B 50 GLU B 64 1 15
HELIX 10 AB1 ILE B 83 CYS B 92 1 10
HELIX 11 AB2 LEU B 96 LYS B 109 1 14
HELIX 12 AB3 TYR B 110 SER B 117 5 8
HELIX 13 AB4 LYS B 135 PHE B 147 1 13
HELIX 14 AB5 ALA B 149 ILE B 157 1 9
HELIX 15 AB6 ASP C 22 LEU C 36 1 15
HELIX 16 AB7 GLU C 50 GLU C 64 1 15
HELIX 17 AB8 ILE C 83 CYS C 92 1 10
HELIX 18 AB9 LEU C 96 LYS C 109 1 14
HELIX 19 AC1 TYR C 110 SER C 117 5 8
HELIX 20 AC2 LYS C 135 PHE C 147 1 13
HELIX 21 AC3 ALA C 149 ILE C 157 1 9
HELIX 22 AC4 ASP D 22 LEU D 36 1 15
HELIX 23 AC5 GLU D 50 GLU D 64 1 15
HELIX 24 AC6 ILE D 83 CYS D 92 1 10
HELIX 25 AC7 LEU D 96 LYS D 109 1 14
HELIX 26 AC8 TYR D 110 SER D 117 5 8
HELIX 27 AC9 LYS D 135 PHE D 147 1 13
HELIX 28 AD1 ALA D 149 ILE D 157 1 9
HELIX 29 AD2 ASP E 22 LEU E 36 1 15
HELIX 30 AD3 GLU E 50 GLU E 64 1 15
HELIX 31 AD4 ILE E 83 CYS E 92 1 10
HELIX 32 AD5 LEU E 96 LYS E 109 1 14
HELIX 33 AD6 TYR E 110 SER E 117 5 8
HELIX 34 AD7 LYS E 135 PHE E 147 1 13
HELIX 35 AD8 ALA E 149 ILE E 157 1 9
HELIX 36 AD9 LEU F 23 LEU F 36 1 14
HELIX 37 AE1 GLU F 50 GLU F 64 1 15
HELIX 38 AE2 ILE F 83 CYS F 92 1 10
HELIX 39 AE3 LEU F 96 LEU F 108 1 13
HELIX 40 AE4 LYS F 109 TYR F 110 5 2
HELIX 41 AE5 VAL F 111 SER F 117 5 7
HELIX 42 AE6 LYS F 135 PHE F 147 1 13
HELIX 43 AE7 ALA F 149 ILE F 157 1 9
SHEET 1 AA1 6 LEU A 40 VAL A 47 0
SHEET 2 AA1 6 ILE A 4 ALA A 11 1 N ILE A 6 O HIS A 43
SHEET 3 AA1 6 LEU A 69 THR A 73 1 O VAL A 71 N GLY A 7
SHEET 4 AA1 6 SER A 127 LEU A 132 1 O LEU A 128 N VAL A 70
SHEET 5 AA1 6 ALA A 121 ARG A 124 -1 N GLY A 122 O ILE A 129
SHEET 6 AA1 6 LYS A 94 MET A 95 -1 N LYS A 94 O ILE A 123
SHEET 1 AA2 6 LEU B 40 VAL B 47 0
SHEET 2 AA2 6 ILE B 4 ALA B 11 1 N SER B 10 O VAL B 47
SHEET 3 AA2 6 LEU B 69 THR B 73 1 O VAL B 71 N LEU B 9
SHEET 4 AA2 6 SER B 127 LEU B 132 1 O LEU B 132 N THR B 72
SHEET 5 AA2 6 ALA B 121 ARG B 124 -1 N GLY B 122 O ILE B 129
SHEET 6 AA2 6 LYS B 94 MET B 95 -1 N LYS B 94 O ILE B 123
SHEET 1 AA3 6 LEU C 40 VAL C 47 0
SHEET 2 AA3 6 ILE C 4 ALA C 11 1 N ILE C 6 O HIS C 43
SHEET 3 AA3 6 LEU C 69 THR C 73 1 O VAL C 71 N GLY C 7
SHEET 4 AA3 6 SER C 127 LEU C 132 1 O LEU C 128 N VAL C 70
SHEET 5 AA3 6 ALA C 121 ARG C 124 -1 N GLY C 122 O ILE C 129
SHEET 6 AA3 6 LYS C 94 MET C 95 -1 N LYS C 94 O ILE C 123
SHEET 1 AA4 6 LEU D 40 VAL D 47 0
SHEET 2 AA4 6 ILE D 4 ALA D 11 1 N ILE D 6 O HIS D 43
SHEET 3 AA4 6 LEU D 69 THR D 73 1 O VAL D 71 N GLY D 7
SHEET 4 AA4 6 SER D 127 LEU D 132 1 O LEU D 128 N VAL D 70
SHEET 5 AA4 6 ALA D 121 ARG D 124 -1 N GLY D 122 O ILE D 129
SHEET 6 AA4 6 LYS D 94 MET D 95 -1 N LYS D 94 O ILE D 123
SHEET 1 AA5 6 LEU E 40 VAL E 47 0
SHEET 2 AA5 6 ILE E 4 ALA E 11 1 N ILE E 6 O HIS E 43
SHEET 3 AA5 6 LEU E 69 THR E 73 1 O VAL E 71 N GLY E 7
SHEET 4 AA5 6 SER E 127 LEU E 132 1 O LEU E 128 N VAL E 70
SHEET 5 AA5 6 ALA E 121 ARG E 124 -1 N GLY E 122 O ILE E 129
SHEET 6 AA5 6 LYS E 94 MET E 95 -1 N LYS E 94 O ILE E 123
SHEET 1 AA6 6 LEU F 40 VAL F 47 0
SHEET 2 AA6 6 ILE F 4 ALA F 11 1 N ILE F 6 O HIS F 43
SHEET 3 AA6 6 LEU F 69 THR F 73 1 O LEU F 69 N GLY F 7
SHEET 4 AA6 6 SER F 127 LEU F 132 1 O LEU F 128 N VAL F 70
SHEET 5 AA6 6 ALA F 121 ARG F 124 -1 N GLY F 122 O ILE F 129
SHEET 6 AA6 6 LYS F 94 MET F 95 -1 N LYS F 94 O ILE F 123
CRYST1 65.619 66.018 76.049 71.97 86.42 60.22 P 1 6
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 0.015239 -0.008722 0.001956 0.00000
SCALE2 0.000000 0.017453 -0.005928 0.00000
SCALE3 0.000000 0.000000 0.013914 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
