HEADER PHOTOSYNTHESIS 08-MAY-18 6GHR
TITLE CYANOBACTERIAL GAPDH WITH FULL-LENGTH CP12
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE;
COMPND 3 CHAIN: B, C, D, A;
COMPND 4 EC: 1.2.1.-;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: CP12 POLYPEPTIDE;
COMPND 8 CHAIN: E, F;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;
SOURCE 3 ORGANISM_TAXID: 197221;
SOURCE 4 STRAIN: BP-1;
SOURCE 5 GENE: TLL1466;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI KRX;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 1452720;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PRSETA;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS BP-1;
SOURCE 11 ORGANISM_TAXID: 197221;
SOURCE 12 GENE: CP12;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI KRX;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 1452720;
SOURCE 15 EXPRESSION_SYSTEM_PLASMID: PRSETA
KEYWDS CALVIN CYCLE, REGULATION, PHOTOSYNTHESIS
EXPDTA X-RAY DIFFRACTION
AUTHOR C.R.MCFARLANE,J.W.MURRAY
REVDAT 3 17-JAN-24 6GHR 1 REMARK
REVDAT 2 20-NOV-19 6GHR 1 JRNL
REVDAT 1 08-MAY-19 6GHR 0
JRNL AUTH C.R.MCFARLANE,N.R.SHAH,B.V.KABASAKAL,B.ECHEVERRIA,
JRNL AUTH 2 C.A.R.COTTON,D.BUBECK,J.W.MURRAY
JRNL TITL STRUCTURAL BASIS OF LIGHT-INDUCED REDOX REGULATION IN THE
JRNL TITL 2 CALVIN-BENSON CYCLE IN CYANOBACTERIA.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 116 20984 2019
JRNL REFN ESSN 1091-6490
JRNL PMID 31570616
JRNL DOI 10.1073/PNAS.1906722116
REMARK 2
REMARK 2 RESOLUTION. 2.25 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.13_2998: ???)
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) : 2.25
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 71.23
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.460
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 76281
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.192
REMARK 3 R VALUE (WORKING SET) : 0.190
REMARK 3 FREE R VALUE : 0.227
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.980
REMARK 3 FREE R VALUE TEST SET COUNT : 3800
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 71.2615 - 6.7441 0.96 2835 135 0.1558 0.1887
REMARK 3 2 6.7441 - 5.3535 0.99 2754 137 0.1594 0.1760
REMARK 3 3 5.3535 - 4.6770 0.99 2724 151 0.1369 0.1739
REMARK 3 4 4.6770 - 4.2494 0.99 2731 132 0.1257 0.1504
REMARK 3 5 4.2494 - 3.9448 0.99 2715 140 0.1397 0.1826
REMARK 3 6 3.9448 - 3.7123 0.99 2670 140 0.1708 0.1899
REMARK 3 7 3.7123 - 3.5264 1.00 2710 163 0.1787 0.2464
REMARK 3 8 3.5264 - 3.3729 1.00 2694 142 0.1903 0.2149
REMARK 3 9 3.3729 - 3.2430 0.99 2659 153 0.1993 0.2203
REMARK 3 10 3.2430 - 3.1311 1.00 2695 142 0.2117 0.2603
REMARK 3 11 3.1311 - 3.0332 1.00 2682 142 0.2202 0.2514
REMARK 3 12 3.0332 - 2.9465 1.00 2669 163 0.2233 0.2777
REMARK 3 13 2.9465 - 2.8689 1.00 2702 130 0.2340 0.2804
REMARK 3 14 2.8689 - 2.7989 0.99 2654 136 0.2371 0.2908
REMARK 3 15 2.7989 - 2.7353 0.99 2679 132 0.2206 0.2363
REMARK 3 16 2.7353 - 2.6771 1.00 2666 140 0.2224 0.2791
REMARK 3 17 2.6771 - 2.6235 1.00 2653 135 0.2328 0.2916
REMARK 3 18 2.6235 - 2.5740 1.00 2684 156 0.2364 0.2508
REMARK 3 19 2.5740 - 2.5281 1.00 2677 133 0.2347 0.2559
REMARK 3 20 2.5281 - 2.4852 1.00 2639 155 0.2304 0.2688
REMARK 3 21 2.4852 - 2.4451 1.00 2663 150 0.2388 0.2793
REMARK 3 22 2.4451 - 2.4075 1.00 2668 144 0.2456 0.2761
REMARK 3 23 2.4075 - 2.3721 1.00 2692 124 0.2509 0.3086
REMARK 3 24 2.3721 - 2.3387 1.00 2640 119 0.2633 0.2890
REMARK 3 25 2.3387 - 2.3071 1.00 2694 146 0.2702 0.3038
REMARK 3 26 2.3071 - 2.2771 1.00 2697 112 0.2746 0.3023
REMARK 3 27 2.2771 - 2.2486 0.95 2535 148 0.2825 0.3399
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) : 0.270
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.130
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 33.67
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 : 0.002 11473
REMARK 3 ANGLE : 0.565 15629
REMARK 3 CHIRALITY : 0.046 1784
REMARK 3 PLANARITY : 0.004 2008
REMARK 3 DIHEDRAL : 9.562 7995
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 21
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'B' AND (RESID -4 THROUGH 72 )
REMARK 3 ORIGIN FOR THE GROUP (A): 45.3966 56.3052 77.3889
REMARK 3 T TENSOR
REMARK 3 T11: 0.2533 T22: 0.2391
REMARK 3 T33: 0.3290 T12: -0.0506
REMARK 3 T13: 0.0057 T23: 0.0355
REMARK 3 L TENSOR
REMARK 3 L11: 1.7287 L22: 7.0251
REMARK 3 L33: 2.7683 L12: -0.1341
REMARK 3 L13: -0.5322 L23: -0.3347
REMARK 3 S TENSOR
REMARK 3 S11: 0.0080 S12: 0.2243 S13: 0.2811
REMARK 3 S21: -0.5009 S22: -0.0330 S23: -0.3480
REMARK 3 S31: -0.1557 S32: 0.1496 S33: 0.0285
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 73 THROUGH 132 )
REMARK 3 ORIGIN FOR THE GROUP (A): 47.4764 66.0195 90.2919
REMARK 3 T TENSOR
REMARK 3 T11: 0.3069 T22: 0.2182
REMARK 3 T33: 0.4576 T12: -0.0661
REMARK 3 T13: -0.1405 T23: -0.0154
REMARK 3 L TENSOR
REMARK 3 L11: 8.9909 L22: 4.4116
REMARK 3 L33: 3.3288 L12: 0.3944
REMARK 3 L13: -3.0300 L23: -0.2665
REMARK 3 S TENSOR
REMARK 3 S11: 0.0128 S12: -0.2584 S13: 0.5744
REMARK 3 S21: 0.1484 S22: -0.0677 S23: -0.5914
REMARK 3 S31: -0.4725 S32: 0.3684 S33: 0.0630
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 133 THROUGH 202 )
REMARK 3 ORIGIN FOR THE GROUP (A): 28.4905 58.7690 95.0823
REMARK 3 T TENSOR
REMARK 3 T11: 0.2751 T22: 0.2360
REMARK 3 T33: 0.3550 T12: -0.0063
REMARK 3 T13: -0.0654 T23: -0.0369
REMARK 3 L TENSOR
REMARK 3 L11: 1.1185 L22: 1.5634
REMARK 3 L33: 0.4357 L12: -0.6684
REMARK 3 L13: -0.0041 L23: -0.2761
REMARK 3 S TENSOR
REMARK 3 S11: -0.0927 S12: -0.1523 S13: 0.3520
REMARK 3 S21: 0.0872 S22: -0.0343 S23: 0.0025
REMARK 3 S31: -0.1329 S32: 0.0057 S33: 0.1332
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 203 THROUGH 337 )
REMARK 3 ORIGIN FOR THE GROUP (A): 20.7866 56.7948 89.2849
REMARK 3 T TENSOR
REMARK 3 T11: 0.2249 T22: 0.2213
REMARK 3 T33: 0.3711 T12: 0.0068
REMARK 3 T13: -0.0522 T23: -0.0472
REMARK 3 L TENSOR
REMARK 3 L11: 1.5076 L22: 1.6664
REMARK 3 L33: 0.8937 L12: -0.1806
REMARK 3 L13: -0.0452 L23: 0.0848
REMARK 3 S TENSOR
REMARK 3 S11: -0.0886 S12: -0.0566 S13: 0.3192
REMARK 3 S21: 0.0178 S22: -0.0397 S23: 0.2565
REMARK 3 S31: -0.1761 S32: -0.0893 S33: 0.1015
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 0 THROUGH 153 )
REMARK 3 ORIGIN FOR THE GROUP (A): 54.0530 32.2451 113.1243
REMARK 3 T TENSOR
REMARK 3 T11: 0.3391 T22: 0.3428
REMARK 3 T33: 0.2100 T12: -0.0040
REMARK 3 T13: -0.1044 T23: -0.0015
REMARK 3 L TENSOR
REMARK 3 L11: 2.6692 L22: 1.9820
REMARK 3 L33: 1.5475 L12: -0.5551
REMARK 3 L13: -0.0778 L23: 0.7356
REMARK 3 S TENSOR
REMARK 3 S11: 0.0063 S12: -0.4060 S13: 0.1335
REMARK 3 S21: 0.3656 S22: 0.1085 S23: -0.2707
REMARK 3 S31: 0.0177 S32: 0.1809 S33: -0.0973
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 154 THROUGH 337 )
REMARK 3 ORIGIN FOR THE GROUP (A): 49.3810 18.2052 94.3043
REMARK 3 T TENSOR
REMARK 3 T11: 0.2415 T22: 0.2279
REMARK 3 T33: 0.2713 T12: 0.0233
REMARK 3 T13: -0.0578 T23: 0.0158
REMARK 3 L TENSOR
REMARK 3 L11: 1.0291 L22: 0.9538
REMARK 3 L33: 0.6840 L12: 0.2272
REMARK 3 L13: 0.2915 L23: 0.3214
REMARK 3 S TENSOR
REMARK 3 S11: 0.0197 S12: -0.0578 S13: -0.0842
REMARK 3 S21: 0.2147 S22: 0.0261 S23: -0.2958
REMARK 3 S31: 0.0886 S32: 0.0766 S33: -0.0425
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 55 THROUGH 63 )
REMARK 3 ORIGIN FOR THE GROUP (A): 3.7146 25.7245 78.8871
REMARK 3 T TENSOR
REMARK 3 T11: 0.4498 T22: 0.9528
REMARK 3 T33: 1.2142 T12: 0.0010
REMARK 3 T13: 0.0485 T23: -0.1249
REMARK 3 L TENSOR
REMARK 3 L11: 5.4458 L22: 5.9760
REMARK 3 L33: 9.1955 L12: -3.6064
REMARK 3 L13: 5.2671 L23: -0.3922
REMARK 3 S TENSOR
REMARK 3 S11: 0.6084 S12: -0.7102 S13: -1.4623
REMARK 3 S21: -0.1188 S22: -0.0785 S23: -0.2027
REMARK 3 S31: 0.0500 S32: -0.6527 S33: -0.5846
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 64 THROUGH 75 )
REMARK 3 ORIGIN FOR THE GROUP (A): 10.2867 27.2148 88.9008
REMARK 3 T TENSOR
REMARK 3 T11: 0.6127 T22: 0.6741
REMARK 3 T33: 0.8475 T12: 0.1131
REMARK 3 T13: 0.0261 T23: -0.1441
REMARK 3 L TENSOR
REMARK 3 L11: 4.0605 L22: 8.8303
REMARK 3 L33: 4.7595 L12: 5.9660
REMARK 3 L13: 4.3838 L23: 6.4906
REMARK 3 S TENSOR
REMARK 3 S11: -0.2288 S12: -0.6701 S13: 0.1667
REMARK 3 S21: -0.7758 S22: -0.5616 S23: 0.0611
REMARK 3 S31: -0.9087 S32: -1.7547 S33: 0.8146
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 1 THROUGH 52 )
REMARK 3 ORIGIN FOR THE GROUP (A): 34.1326 76.3000 117.9056
REMARK 3 T TENSOR
REMARK 3 T11: 1.6695 T22: 1.7241
REMARK 3 T33: 1.3410 T12: 0.4374
REMARK 3 T13: 0.2378 T23: 0.1599
REMARK 3 L TENSOR
REMARK 3 L11: 0.9854 L22: 5.0226
REMARK 3 L33: 0.1989 L12: -2.2431
REMARK 3 L13: -0.4601 L23: 1.0243
REMARK 3 S TENSOR
REMARK 3 S11: -0.3572 S12: 0.0834 S13: 0.3031
REMARK 3 S21: 0.8742 S22: 0.6667 S23: -0.1052
REMARK 3 S31: -0.2010 S32: -0.1189 S33: -0.4121
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 53 THROUGH 75 )
REMARK 3 ORIGIN FOR THE GROUP (A): 45.7322 53.1684 105.6325
REMARK 3 T TENSOR
REMARK 3 T11: 0.4330 T22: 0.3120
REMARK 3 T33: 0.4125 T12: -0.0545
REMARK 3 T13: -0.1089 T23: -0.0187
REMARK 3 L TENSOR
REMARK 3 L11: 4.6903 L22: 6.2768
REMARK 3 L33: 7.2343 L12: -1.8612
REMARK 3 L13: -0.3602 L23: 0.3681
REMARK 3 S TENSOR
REMARK 3 S11: -0.0839 S12: -0.1141 S13: 0.3362
REMARK 3 S21: 0.8497 S22: 0.0595 S23: -0.4216
REMARK 3 S31: -0.1013 S32: 0.4015 S33: 0.0091
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 0 THROUGH 170 )
REMARK 3 ORIGIN FOR THE GROUP (A): 22.0708 24.7397 64.0950
REMARK 3 T TENSOR
REMARK 3 T11: 0.2914 T22: 0.2539
REMARK 3 T33: 0.2575 T12: 0.0078
REMARK 3 T13: -0.0393 T23: -0.0028
REMARK 3 L TENSOR
REMARK 3 L11: 3.2682 L22: 2.0452
REMARK 3 L33: 0.9995 L12: -1.2825
REMARK 3 L13: 0.4329 L23: 0.2555
REMARK 3 S TENSOR
REMARK 3 S11: 0.0656 S12: 0.2403 S13: -0.2462
REMARK 3 S21: -0.3397 S22: -0.0927 S23: 0.4079
REMARK 3 S31: -0.0709 S32: -0.1439 S33: 0.0446
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 171 THROUGH 337 )
REMARK 3 ORIGIN FOR THE GROUP (A): 40.7693 22.1451 73.8445
REMARK 3 T TENSOR
REMARK 3 T11: 0.2220 T22: 0.2262
REMARK 3 T33: 0.2495 T12: -0.0128
REMARK 3 T13: 0.0013 T23: -0.0061
REMARK 3 L TENSOR
REMARK 3 L11: 1.1864 L22: 1.3173
REMARK 3 L33: 0.6952 L12: -0.3302
REMARK 3 L13: -0.1048 L23: 0.1142
REMARK 3 S TENSOR
REMARK 3 S11: -0.0136 S12: 0.1117 S13: -0.0303
REMARK 3 S21: -0.1271 S22: 0.0152 S23: -0.1234
REMARK 3 S31: 0.0289 S32: 0.0143 S33: 0.0010
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 0 THROUGH 23 )
REMARK 3 ORIGIN FOR THE GROUP (A): 13.6078 17.0560 107.6740
REMARK 3 T TENSOR
REMARK 3 T11: 0.5081 T22: 0.3584
REMARK 3 T33: 0.3845 T12: -0.0553
REMARK 3 T13: 0.1731 T23: 0.0371
REMARK 3 L TENSOR
REMARK 3 L11: 4.2061 L22: 1.1520
REMARK 3 L33: 2.6328 L12: -0.2226
REMARK 3 L13: -1.3104 L23: -0.5436
REMARK 3 S TENSOR
REMARK 3 S11: 0.0505 S12: -0.1801 S13: -0.0242
REMARK 3 S21: 0.6553 S22: -0.0380 S23: 0.4573
REMARK 3 S31: 0.4475 S32: -0.2405 S33: -0.0550
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 24 THROUGH 39 )
REMARK 3 ORIGIN FOR THE GROUP (A): 11.7607 12.7793 107.4045
REMARK 3 T TENSOR
REMARK 3 T11: 0.5851 T22: 0.5078
REMARK 3 T33: 0.4328 T12: -0.0347
REMARK 3 T13: 0.2478 T23: 0.0042
REMARK 3 L TENSOR
REMARK 3 L11: 4.0009 L22: 2.8426
REMARK 3 L33: 5.0921 L12: -1.1662
REMARK 3 L13: -2.9394 L23: 1.4491
REMARK 3 S TENSOR
REMARK 3 S11: -0.3258 S12: -0.1951 S13: -0.4416
REMARK 3 S21: 0.8490 S22: 0.0496 S23: 0.4835
REMARK 3 S31: 0.5365 S32: -0.0048 S33: 0.2783
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 40 THROUGH 72 )
REMARK 3 ORIGIN FOR THE GROUP (A): 23.0735 11.0707 103.0612
REMARK 3 T TENSOR
REMARK 3 T11: 0.4657 T22: 0.3469
REMARK 3 T33: 0.3065 T12: -0.0235
REMARK 3 T13: 0.0677 T23: 0.0443
REMARK 3 L TENSOR
REMARK 3 L11: 4.7654 L22: 6.9695
REMARK 3 L33: 1.8843 L12: 1.8309
REMARK 3 L13: -1.7226 L23: 0.6528
REMARK 3 S TENSOR
REMARK 3 S11: 0.0807 S12: -0.3774 S13: -0.4844
REMARK 3 S21: 0.7828 S22: -0.3930 S23: -0.0485
REMARK 3 S31: 0.3357 S32: 0.0551 S33: 0.3006
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 73 THROUGH 98 )
REMARK 3 ORIGIN FOR THE GROUP (A): 4.7586 10.2876 100.7329
REMARK 3 T TENSOR
REMARK 3 T11: 0.4883 T22: 0.4523
REMARK 3 T33: 0.5227 T12: -0.0711
REMARK 3 T13: 0.2266 T23: -0.0628
REMARK 3 L TENSOR
REMARK 3 L11: 5.7474 L22: 4.6069
REMARK 3 L33: 2.9292 L12: -0.7616
REMARK 3 L13: -1.5796 L23: 1.8168
REMARK 3 S TENSOR
REMARK 3 S11: -0.1559 S12: 0.3883 S13: -0.6202
REMARK 3 S21: 0.2334 S22: -0.2457 S23: 0.7315
REMARK 3 S31: 0.4959 S32: -0.5153 S33: 0.4225
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 99 THROUGH 132 )
REMARK 3 ORIGIN FOR THE GROUP (A): -0.7935 22.4587 100.0755
REMARK 3 T TENSOR
REMARK 3 T11: 0.3455 T22: 0.6367
REMARK 3 T33: 0.6862 T12: 0.0324
REMARK 3 T13: 0.1672 T23: -0.1047
REMARK 3 L TENSOR
REMARK 3 L11: 4.0823 L22: 3.6197
REMARK 3 L33: 3.8047 L12: 1.4388
REMARK 3 L13: -1.7753 L23: 2.1340
REMARK 3 S TENSOR
REMARK 3 S11: -0.0279 S12: 0.3813 S13: -0.4000
REMARK 3 S21: -0.1756 S22: -0.4042 S23: 1.3616
REMARK 3 S31: -0.0535 S32: -0.7206 S33: 0.3112
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 133 THROUGH 182 )
REMARK 3 ORIGIN FOR THE GROUP (A): 5.6251 37.9777 109.3028
REMARK 3 T TENSOR
REMARK 3 T11: 0.4178 T22: 0.4959
REMARK 3 T33: 0.5444 T12: 0.0262
REMARK 3 T13: 0.2491 T23: -0.0417
REMARK 3 L TENSOR
REMARK 3 L11: 0.4192 L22: 0.4394
REMARK 3 L33: 0.6727 L12: 0.3876
REMARK 3 L13: 0.0938 L23: -0.0689
REMARK 3 S TENSOR
REMARK 3 S11: -0.0835 S12: -0.0916 S13: -0.0637
REMARK 3 S21: 0.4039 S22: -0.0661 S23: 0.5230
REMARK 3 S31: 0.0362 S32: -0.3126 S33: 0.0547
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 183 THROUGH 216 )
REMARK 3 ORIGIN FOR THE GROUP (A): 16.6723 35.1600 87.6087
REMARK 3 T TENSOR
REMARK 3 T11: 0.2131 T22: 0.2620
REMARK 3 T33: 0.3896 T12: 0.0026
REMARK 3 T13: 0.0189 T23: -0.0044
REMARK 3 L TENSOR
REMARK 3 L11: 0.2671 L22: 2.8396
REMARK 3 L33: 3.5380 L12: -0.6884
REMARK 3 L13: -0.2738 L23: 0.8432
REMARK 3 S TENSOR
REMARK 3 S11: -0.0908 S12: 0.0238 S13: 0.0464
REMARK 3 S21: 0.1887 S22: -0.0832 S23: 0.5122
REMARK 3 S31: 0.1108 S32: -0.4172 S33: 0.1839
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 217 THROUGH 241 )
REMARK 3 ORIGIN FOR THE GROUP (A): 9.1385 41.1015 101.7424
REMARK 3 T TENSOR
REMARK 3 T11: 0.2777 T22: 0.3347
REMARK 3 T33: 0.5075 T12: -0.0433
REMARK 3 T13: 0.1270 T23: -0.0379
REMARK 3 L TENSOR
REMARK 3 L11: 1.0198 L22: 0.9081
REMARK 3 L33: 1.4816 L12: -0.0938
REMARK 3 L13: 0.6097 L23: -0.3094
REMARK 3 S TENSOR
REMARK 3 S11: 0.0349 S12: -0.2530 S13: 0.0685
REMARK 3 S21: 0.4097 S22: -0.0874 S23: 0.6368
REMARK 3 S31: 0.0105 S32: -0.5310 S33: 0.0772
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 242 THROUGH 337 )
REMARK 3 ORIGIN FOR THE GROUP (A): 15.8915 40.5251 112.7392
REMARK 3 T TENSOR
REMARK 3 T11: 0.4157 T22: 0.3988
REMARK 3 T33: 0.3273 T12: 0.0286
REMARK 3 T13: 0.1383 T23: -0.0595
REMARK 3 L TENSOR
REMARK 3 L11: 1.0785 L22: 1.4054
REMARK 3 L33: 1.3043 L12: 0.2104
REMARK 3 L13: -0.0761 L23: 0.2904
REMARK 3 S TENSOR
REMARK 3 S11: -0.0869 S12: -0.3308 S13: 0.1123
REMARK 3 S21: 0.5804 S22: 0.0202 S23: 0.4012
REMARK 3 S31: 0.0700 S32: -0.1616 S33: 0.0337
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 6GHR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 09-MAY-18.
REMARK 100 THE DEPOSITION ID IS D_1200009971.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-FEB-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I04
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97951
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XIA2
REMARK 200 DATA SCALING SOFTWARE : XIA2
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 76310
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.249
REMARK 200 RESOLUTION RANGE LOW (A) : 71.230
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : 0.09854
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.6800
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.33
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.8
REMARK 200 DATA REDUNDANCY IN SHELL : 2.90
REMARK 200 R MERGE FOR SHELL (I) : 0.46330
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.820
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 4BOY
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 4% TACSIMATE, PH 7 12% (W/V) PEG3350,
REMARK 280 VAPOR DIFFUSION, TEMPERATURE 290K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 66.71900
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 73.48200
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 66.71900
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 73.48200
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 24030 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 47250 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -174.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C, E, F, D, 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 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 B -16
REMARK 465 ARG B -15
REMARK 465 GLY B -14
REMARK 465 SER B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 HIS B -10
REMARK 465 HIS B -9
REMARK 465 HIS B -8
REMARK 465 HIS B -7
REMARK 465 GLY B -6
REMARK 465 LEU B -5
REMARK 465 MET C -16
REMARK 465 ARG C -15
REMARK 465 GLY C -14
REMARK 465 SER C -13
REMARK 465 HIS C -12
REMARK 465 HIS C -11
REMARK 465 HIS C -10
REMARK 465 HIS C -9
REMARK 465 HIS C -8
REMARK 465 HIS C -7
REMARK 465 GLY C -6
REMARK 465 LEU C -5
REMARK 465 VAL C -4
REMARK 465 PRO C -3
REMARK 465 ARG C -2
REMARK 465 GLY C -1
REMARK 465 GLY E -1
REMARK 465 SER E 0
REMARK 465 MET E 1
REMARK 465 SER E 2
REMARK 465 ASN E 3
REMARK 465 LEU E 4
REMARK 465 GLU E 5
REMARK 465 LYS E 6
REMARK 465 GLN E 7
REMARK 465 ILE E 8
REMARK 465 GLU E 9
REMARK 465 GLN E 10
REMARK 465 ALA E 11
REMARK 465 ARG E 12
REMARK 465 GLU E 13
REMARK 465 GLU E 14
REMARK 465 ALA E 15
REMARK 465 HIS E 16
REMARK 465 LYS E 17
REMARK 465 ILE E 18
REMARK 465 CYS E 19
REMARK 465 ASP E 20
REMARK 465 THR E 21
REMARK 465 GLU E 22
REMARK 465 GLY E 23
REMARK 465 ALA E 24
REMARK 465 THR E 25
REMARK 465 SER E 26
REMARK 465 GLY E 27
REMARK 465 GLN E 28
REMARK 465 CYS E 29
REMARK 465 ALA E 30
REMARK 465 ALA E 31
REMARK 465 ALA E 32
REMARK 465 TRP E 33
REMARK 465 ASP E 34
REMARK 465 ALA E 35
REMARK 465 LEU E 36
REMARK 465 GLU E 37
REMARK 465 GLU E 38
REMARK 465 LEU E 39
REMARK 465 GLN E 40
REMARK 465 ALA E 41
REMARK 465 GLU E 42
REMARK 465 ALA E 43
REMARK 465 ALA E 44
REMARK 465 HIS E 45
REMARK 465 GLN E 46
REMARK 465 ARG E 47
REMARK 465 ALA E 48
REMARK 465 GLU E 49
REMARK 465 GLN E 50
REMARK 465 GLN E 51
REMARK 465 ASP E 52
REMARK 465 HIS E 53
REMARK 465 LYS E 54
REMARK 465 GLY F -1
REMARK 465 SER F 0
REMARK 465 THR F 21
REMARK 465 GLU F 22
REMARK 465 GLY F 23
REMARK 465 ALA F 24
REMARK 465 THR F 25
REMARK 465 SER F 26
REMARK 465 MET D -16
REMARK 465 ARG D -15
REMARK 465 GLY D -14
REMARK 465 SER D -13
REMARK 465 HIS D -12
REMARK 465 HIS D -11
REMARK 465 HIS D -10
REMARK 465 HIS D -9
REMARK 465 HIS D -8
REMARK 465 HIS D -7
REMARK 465 GLY D -6
REMARK 465 LEU D -5
REMARK 465 VAL D -4
REMARK 465 PRO D -3
REMARK 465 ARG D -2
REMARK 465 GLY D -1
REMARK 465 MET A -16
REMARK 465 ARG A -15
REMARK 465 GLY A -14
REMARK 465 SER A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 HIS A -9
REMARK 465 HIS A -8
REMARK 465 HIS A -7
REMARK 465 GLY A -6
REMARK 465 LEU A -5
REMARK 465 VAL A -4
REMARK 465 PRO A -3
REMARK 465 ARG A -2
REMARK 465 GLY A -1
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ARG F 47 CG CD NE CZ NH1 NH2
REMARK 470 GLN F 51 CG CD OE1 NE2
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 OXT ASP E 75 OG1 THR A 155 2.14
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 PHE B 9 51.02 -95.96
REMARK 500 ASP B 64 -156.53 -118.92
REMARK 500 PRO B 87 46.43 -83.83
REMARK 500 PHE B 103 64.05 -108.53
REMARK 500 THR B 123 45.46 -88.52
REMARK 500 ASN B 138 18.71 -153.25
REMARK 500 ALA B 152 -160.33 56.99
REMARK 500 VAL B 241 131.09 73.66
REMARK 500 THR B 269 -101.78 -127.00
REMARK 500 ASP C 64 -159.44 -130.03
REMARK 500 THR C 123 48.17 -85.29
REMARK 500 ASN C 138 11.66 -145.20
REMARK 500 ALA C 152 -158.06 58.07
REMARK 500 ALA C 202 116.67 -37.21
REMARK 500 VAL C 241 133.87 76.65
REMARK 500 THR C 269 -90.50 -134.21
REMARK 500 HIS C 335 52.63 -116.60
REMARK 500 PHE D 9 49.81 -95.09
REMARK 500 ASP D 64 -153.30 -125.24
REMARK 500 PRO D 87 45.67 -80.99
REMARK 500 THR D 123 46.46 -85.55
REMARK 500 ASN D 138 12.41 -144.45
REMARK 500 ALA D 152 -163.02 58.61
REMARK 500 ASP D 191 108.53 -51.32
REMARK 500 HIS D 194 148.10 -170.46
REMARK 500 VAL D 241 125.78 72.88
REMARK 500 THR D 269 -91.13 -126.64
REMARK 500 HIS D 335 60.33 -115.13
REMARK 500 PHE A 9 58.87 -96.24
REMARK 500 ASN A 26 78.06 -115.06
REMARK 500 ASP A 64 -156.51 -129.37
REMARK 500 PRO A 87 48.65 -85.63
REMARK 500 PHE A 103 64.81 -111.98
REMARK 500 THR A 123 41.26 -82.78
REMARK 500 ASN A 138 12.62 -145.08
REMARK 500 ALA A 152 -159.55 56.88
REMARK 500 HIS A 194 141.32 -170.33
REMARK 500 VAL A 241 128.53 73.51
REMARK 500 THR A 269 -93.13 -128.67
REMARK 500 HIS A 335 50.04 -117.02
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 NAD B 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NAD C 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NAD D 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NAD A 1001
DBREF 6GHR B 1 337 UNP Q8DIW5 Q8DIW5_THEEB 1 337
DBREF 6GHR C 1 337 UNP Q8DIW5 Q8DIW5_THEEB 1 337
DBREF 6GHR E 1 75 UNP Q8DHX3 Q8DHX3_THEEB 1 75
DBREF 6GHR F 1 75 UNP Q8DHX3 Q8DHX3_THEEB 1 75
DBREF 6GHR D 1 337 UNP Q8DIW5 Q8DIW5_THEEB 1 337
DBREF 6GHR A 1 337 UNP Q8DIW5 Q8DIW5_THEEB 1 337
SEQADV 6GHR MET B -16 UNP Q8DIW5 INITIATING METHIONINE
SEQADV 6GHR ARG B -15 UNP Q8DIW5 EXPRESSION TAG
SEQADV 6GHR GLY B -14 UNP Q8DIW5 EXPRESSION TAG
SEQADV 6GHR SER B -13 UNP Q8DIW5 EXPRESSION TAG
SEQADV 6GHR HIS B -12 UNP Q8DIW5 EXPRESSION TAG
SEQADV 6GHR HIS B -11 UNP Q8DIW5 EXPRESSION TAG
SEQADV 6GHR HIS B -10 UNP Q8DIW5 EXPRESSION TAG
SEQADV 6GHR HIS B -9 UNP Q8DIW5 EXPRESSION TAG
SEQADV 6GHR HIS B -8 UNP Q8DIW5 EXPRESSION TAG
SEQADV 6GHR HIS B -7 UNP Q8DIW5 EXPRESSION TAG
SEQADV 6GHR GLY B -6 UNP Q8DIW5 EXPRESSION TAG
SEQADV 6GHR LEU B -5 UNP Q8DIW5 EXPRESSION TAG
SEQADV 6GHR VAL B -4 UNP Q8DIW5 EXPRESSION TAG
SEQADV 6GHR PRO B -3 UNP Q8DIW5 EXPRESSION TAG
SEQADV 6GHR ARG B -2 UNP Q8DIW5 EXPRESSION TAG
SEQADV 6GHR GLY B -1 UNP Q8DIW5 EXPRESSION TAG
SEQADV 6GHR SER B 0 UNP Q8DIW5 EXPRESSION TAG
SEQADV 6GHR MET C -16 UNP Q8DIW5 INITIATING METHIONINE
SEQADV 6GHR ARG C -15 UNP Q8DIW5 EXPRESSION TAG
SEQADV 6GHR GLY C -14 UNP Q8DIW5 EXPRESSION TAG
SEQADV 6GHR SER C -13 UNP Q8DIW5 EXPRESSION TAG
SEQADV 6GHR HIS C -12 UNP Q8DIW5 EXPRESSION TAG
SEQADV 6GHR HIS C -11 UNP Q8DIW5 EXPRESSION TAG
SEQADV 6GHR HIS C -10 UNP Q8DIW5 EXPRESSION TAG
SEQADV 6GHR HIS C -9 UNP Q8DIW5 EXPRESSION TAG
SEQADV 6GHR HIS C -8 UNP Q8DIW5 EXPRESSION TAG
SEQADV 6GHR HIS C -7 UNP Q8DIW5 EXPRESSION TAG
SEQADV 6GHR GLY C -6 UNP Q8DIW5 EXPRESSION TAG
SEQADV 6GHR LEU C -5 UNP Q8DIW5 EXPRESSION TAG
SEQADV 6GHR VAL C -4 UNP Q8DIW5 EXPRESSION TAG
SEQADV 6GHR PRO C -3 UNP Q8DIW5 EXPRESSION TAG
SEQADV 6GHR ARG C -2 UNP Q8DIW5 EXPRESSION TAG
SEQADV 6GHR GLY C -1 UNP Q8DIW5 EXPRESSION TAG
SEQADV 6GHR SER C 0 UNP Q8DIW5 EXPRESSION TAG
SEQADV 6GHR GLY E -1 UNP Q8DHX3 EXPRESSION TAG
SEQADV 6GHR SER E 0 UNP Q8DHX3 EXPRESSION TAG
SEQADV 6GHR GLY F -1 UNP Q8DHX3 EXPRESSION TAG
SEQADV 6GHR SER F 0 UNP Q8DHX3 EXPRESSION TAG
SEQADV 6GHR MET D -16 UNP Q8DIW5 INITIATING METHIONINE
SEQADV 6GHR ARG D -15 UNP Q8DIW5 EXPRESSION TAG
SEQADV 6GHR GLY D -14 UNP Q8DIW5 EXPRESSION TAG
SEQADV 6GHR SER D -13 UNP Q8DIW5 EXPRESSION TAG
SEQADV 6GHR HIS D -12 UNP Q8DIW5 EXPRESSION TAG
SEQADV 6GHR HIS D -11 UNP Q8DIW5 EXPRESSION TAG
SEQADV 6GHR HIS D -10 UNP Q8DIW5 EXPRESSION TAG
SEQADV 6GHR HIS D -9 UNP Q8DIW5 EXPRESSION TAG
SEQADV 6GHR HIS D -8 UNP Q8DIW5 EXPRESSION TAG
SEQADV 6GHR HIS D -7 UNP Q8DIW5 EXPRESSION TAG
SEQADV 6GHR GLY D -6 UNP Q8DIW5 EXPRESSION TAG
SEQADV 6GHR LEU D -5 UNP Q8DIW5 EXPRESSION TAG
SEQADV 6GHR VAL D -4 UNP Q8DIW5 EXPRESSION TAG
SEQADV 6GHR PRO D -3 UNP Q8DIW5 EXPRESSION TAG
SEQADV 6GHR ARG D -2 UNP Q8DIW5 EXPRESSION TAG
SEQADV 6GHR GLY D -1 UNP Q8DIW5 EXPRESSION TAG
SEQADV 6GHR SER D 0 UNP Q8DIW5 EXPRESSION TAG
SEQADV 6GHR MET A -16 UNP Q8DIW5 INITIATING METHIONINE
SEQADV 6GHR ARG A -15 UNP Q8DIW5 EXPRESSION TAG
SEQADV 6GHR GLY A -14 UNP Q8DIW5 EXPRESSION TAG
SEQADV 6GHR SER A -13 UNP Q8DIW5 EXPRESSION TAG
SEQADV 6GHR HIS A -12 UNP Q8DIW5 EXPRESSION TAG
SEQADV 6GHR HIS A -11 UNP Q8DIW5 EXPRESSION TAG
SEQADV 6GHR HIS A -10 UNP Q8DIW5 EXPRESSION TAG
SEQADV 6GHR HIS A -9 UNP Q8DIW5 EXPRESSION TAG
SEQADV 6GHR HIS A -8 UNP Q8DIW5 EXPRESSION TAG
SEQADV 6GHR HIS A -7 UNP Q8DIW5 EXPRESSION TAG
SEQADV 6GHR GLY A -6 UNP Q8DIW5 EXPRESSION TAG
SEQADV 6GHR LEU A -5 UNP Q8DIW5 EXPRESSION TAG
SEQADV 6GHR VAL A -4 UNP Q8DIW5 EXPRESSION TAG
SEQADV 6GHR PRO A -3 UNP Q8DIW5 EXPRESSION TAG
SEQADV 6GHR ARG A -2 UNP Q8DIW5 EXPRESSION TAG
SEQADV 6GHR GLY A -1 UNP Q8DIW5 EXPRESSION TAG
SEQADV 6GHR SER A 0 UNP Q8DIW5 EXPRESSION TAG
SEQRES 1 B 354 MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY LEU VAL
SEQRES 2 B 354 PRO ARG GLY SER MET VAL ARG VAL ALA ILE ASN GLY PHE
SEQRES 3 B 354 GLY ARG ILE GLY ARG ASN PHE MET ARG CYS TRP LEU GLN
SEQRES 4 B 354 ARG LYS ALA ASN SER LYS LEU GLU ILE VAL GLY ILE ASN
SEQRES 5 B 354 ASP THR SER ASP PRO ARG THR ASN ALA HIS LEU LEU LYS
SEQRES 6 B 354 TYR ASP SER MET LEU GLY ILE PHE GLN ASP ALA GLU ILE
SEQRES 7 B 354 THR ALA ASP ASP ASP CYS ILE TYR ALA GLY GLY HIS ALA
SEQRES 8 B 354 VAL LYS CYS VAL SER ASP ARG ASN PRO GLU ASN LEU PRO
SEQRES 9 B 354 TRP SER ALA TRP GLY ILE ASP LEU VAL ILE GLU ALA THR
SEQRES 10 B 354 GLY VAL PHE THR SER ARG GLU GLY ALA SER LYS HIS LEU
SEQRES 11 B 354 SER ALA GLY ALA LYS LYS VAL LEU ILE THR ALA PRO GLY
SEQRES 12 B 354 LYS GLY ASN ILE PRO THR TYR VAL VAL GLY VAL ASN HIS
SEQRES 13 B 354 HIS THR TYR ASP PRO SER GLU ASP ILE VAL SER ASN ALA
SEQRES 14 B 354 SER CYS THR THR ASN CYS LEU ALA PRO ILE VAL LYS VAL
SEQRES 15 B 354 LEU HIS GLU ALA PHE GLY ILE GLN GLN GLY MET MET THR
SEQRES 16 B 354 THR THR HIS SER TYR THR GLY ASP GLN ARG LEU LEU ASP
SEQRES 17 B 354 ALA SER HIS ARG ASP LEU ARG ARG ALA ARG ALA ALA ALA
SEQRES 18 B 354 MET ASN ILE VAL PRO THR SER THR GLY ALA ALA LYS ALA
SEQRES 19 B 354 VAL GLY LEU VAL ILE PRO GLU LEU GLN GLY LYS LEU ASN
SEQRES 20 B 354 GLY ILE ALA LEU ARG VAL PRO THR PRO ASN VAL SER VAL
SEQRES 21 B 354 VAL ASP PHE VAL ALA GLN VAL GLU LYS PRO THR ILE ALA
SEQRES 22 B 354 GLU GLN VAL ASN GLN VAL ILE LYS GLU ALA SER GLU THR
SEQRES 23 B 354 THR MET LYS GLY ILE ILE HIS TYR SER GLU LEU GLU LEU
SEQRES 24 B 354 VAL SER SER ASP TYR ARG GLY HIS ASN ALA SER SER ILE
SEQRES 25 B 354 LEU ASP ALA SER LEU THR MET VAL LEU GLY GLY ASN LEU
SEQRES 26 B 354 VAL LYS VAL VAL ALA TRP TYR ASP ASN GLU TRP GLY TYR
SEQRES 27 B 354 SER GLN ARG VAL LEU ASP LEU ALA GLU HIS MET ALA ALA
SEQRES 28 B 354 HIS TRP ALA
SEQRES 1 C 354 MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY LEU VAL
SEQRES 2 C 354 PRO ARG GLY SER MET VAL ARG VAL ALA ILE ASN GLY PHE
SEQRES 3 C 354 GLY ARG ILE GLY ARG ASN PHE MET ARG CYS TRP LEU GLN
SEQRES 4 C 354 ARG LYS ALA ASN SER LYS LEU GLU ILE VAL GLY ILE ASN
SEQRES 5 C 354 ASP THR SER ASP PRO ARG THR ASN ALA HIS LEU LEU LYS
SEQRES 6 C 354 TYR ASP SER MET LEU GLY ILE PHE GLN ASP ALA GLU ILE
SEQRES 7 C 354 THR ALA ASP ASP ASP CYS ILE TYR ALA GLY GLY HIS ALA
SEQRES 8 C 354 VAL LYS CYS VAL SER ASP ARG ASN PRO GLU ASN LEU PRO
SEQRES 9 C 354 TRP SER ALA TRP GLY ILE ASP LEU VAL ILE GLU ALA THR
SEQRES 10 C 354 GLY VAL PHE THR SER ARG GLU GLY ALA SER LYS HIS LEU
SEQRES 11 C 354 SER ALA GLY ALA LYS LYS VAL LEU ILE THR ALA PRO GLY
SEQRES 12 C 354 LYS GLY ASN ILE PRO THR TYR VAL VAL GLY VAL ASN HIS
SEQRES 13 C 354 HIS THR TYR ASP PRO SER GLU ASP ILE VAL SER ASN ALA
SEQRES 14 C 354 SER CYS THR THR ASN CYS LEU ALA PRO ILE VAL LYS VAL
SEQRES 15 C 354 LEU HIS GLU ALA PHE GLY ILE GLN GLN GLY MET MET THR
SEQRES 16 C 354 THR THR HIS SER TYR THR GLY ASP GLN ARG LEU LEU ASP
SEQRES 17 C 354 ALA SER HIS ARG ASP LEU ARG ARG ALA ARG ALA ALA ALA
SEQRES 18 C 354 MET ASN ILE VAL PRO THR SER THR GLY ALA ALA LYS ALA
SEQRES 19 C 354 VAL GLY LEU VAL ILE PRO GLU LEU GLN GLY LYS LEU ASN
SEQRES 20 C 354 GLY ILE ALA LEU ARG VAL PRO THR PRO ASN VAL SER VAL
SEQRES 21 C 354 VAL ASP PHE VAL ALA GLN VAL GLU LYS PRO THR ILE ALA
SEQRES 22 C 354 GLU GLN VAL ASN GLN VAL ILE LYS GLU ALA SER GLU THR
SEQRES 23 C 354 THR MET LYS GLY ILE ILE HIS TYR SER GLU LEU GLU LEU
SEQRES 24 C 354 VAL SER SER ASP TYR ARG GLY HIS ASN ALA SER SER ILE
SEQRES 25 C 354 LEU ASP ALA SER LEU THR MET VAL LEU GLY GLY ASN LEU
SEQRES 26 C 354 VAL LYS VAL VAL ALA TRP TYR ASP ASN GLU TRP GLY TYR
SEQRES 27 C 354 SER GLN ARG VAL LEU ASP LEU ALA GLU HIS MET ALA ALA
SEQRES 28 C 354 HIS TRP ALA
SEQRES 1 E 77 GLY SER MET SER ASN LEU GLU LYS GLN ILE GLU GLN ALA
SEQRES 2 E 77 ARG GLU GLU ALA HIS LYS ILE CYS ASP THR GLU GLY ALA
SEQRES 3 E 77 THR SER GLY GLN CYS ALA ALA ALA TRP ASP ALA LEU GLU
SEQRES 4 E 77 GLU LEU GLN ALA GLU ALA ALA HIS GLN ARG ALA GLU GLN
SEQRES 5 E 77 GLN ASP HIS LYS THR SER PHE GLN GLN TYR CYS ASP ASP
SEQRES 6 E 77 ASN PRO ASP ALA ALA GLU CYS ARG ILE TYR ASP ASP
SEQRES 1 F 77 GLY SER MET SER ASN LEU GLU LYS GLN ILE GLU GLN ALA
SEQRES 2 F 77 ARG GLU GLU ALA HIS LYS ILE CYS ASP THR GLU GLY ALA
SEQRES 3 F 77 THR SER GLY GLN CYS ALA ALA ALA TRP ASP ALA LEU GLU
SEQRES 4 F 77 GLU LEU GLN ALA GLU ALA ALA HIS GLN ARG ALA GLU GLN
SEQRES 5 F 77 GLN ASP HIS LYS THR SER PHE GLN GLN TYR CYS ASP ASP
SEQRES 6 F 77 ASN PRO ASP ALA ALA GLU CYS ARG ILE TYR ASP ASP
SEQRES 1 D 354 MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY LEU VAL
SEQRES 2 D 354 PRO ARG GLY SER MET VAL ARG VAL ALA ILE ASN GLY PHE
SEQRES 3 D 354 GLY ARG ILE GLY ARG ASN PHE MET ARG CYS TRP LEU GLN
SEQRES 4 D 354 ARG LYS ALA ASN SER LYS LEU GLU ILE VAL GLY ILE ASN
SEQRES 5 D 354 ASP THR SER ASP PRO ARG THR ASN ALA HIS LEU LEU LYS
SEQRES 6 D 354 TYR ASP SER MET LEU GLY ILE PHE GLN ASP ALA GLU ILE
SEQRES 7 D 354 THR ALA ASP ASP ASP CYS ILE TYR ALA GLY GLY HIS ALA
SEQRES 8 D 354 VAL LYS CYS VAL SER ASP ARG ASN PRO GLU ASN LEU PRO
SEQRES 9 D 354 TRP SER ALA TRP GLY ILE ASP LEU VAL ILE GLU ALA THR
SEQRES 10 D 354 GLY VAL PHE THR SER ARG GLU GLY ALA SER LYS HIS LEU
SEQRES 11 D 354 SER ALA GLY ALA LYS LYS VAL LEU ILE THR ALA PRO GLY
SEQRES 12 D 354 LYS GLY ASN ILE PRO THR TYR VAL VAL GLY VAL ASN HIS
SEQRES 13 D 354 HIS THR TYR ASP PRO SER GLU ASP ILE VAL SER ASN ALA
SEQRES 14 D 354 SER CYS THR THR ASN CYS LEU ALA PRO ILE VAL LYS VAL
SEQRES 15 D 354 LEU HIS GLU ALA PHE GLY ILE GLN GLN GLY MET MET THR
SEQRES 16 D 354 THR THR HIS SER TYR THR GLY ASP GLN ARG LEU LEU ASP
SEQRES 17 D 354 ALA SER HIS ARG ASP LEU ARG ARG ALA ARG ALA ALA ALA
SEQRES 18 D 354 MET ASN ILE VAL PRO THR SER THR GLY ALA ALA LYS ALA
SEQRES 19 D 354 VAL GLY LEU VAL ILE PRO GLU LEU GLN GLY LYS LEU ASN
SEQRES 20 D 354 GLY ILE ALA LEU ARG VAL PRO THR PRO ASN VAL SER VAL
SEQRES 21 D 354 VAL ASP PHE VAL ALA GLN VAL GLU LYS PRO THR ILE ALA
SEQRES 22 D 354 GLU GLN VAL ASN GLN VAL ILE LYS GLU ALA SER GLU THR
SEQRES 23 D 354 THR MET LYS GLY ILE ILE HIS TYR SER GLU LEU GLU LEU
SEQRES 24 D 354 VAL SER SER ASP TYR ARG GLY HIS ASN ALA SER SER ILE
SEQRES 25 D 354 LEU ASP ALA SER LEU THR MET VAL LEU GLY GLY ASN LEU
SEQRES 26 D 354 VAL LYS VAL VAL ALA TRP TYR ASP ASN GLU TRP GLY TYR
SEQRES 27 D 354 SER GLN ARG VAL LEU ASP LEU ALA GLU HIS MET ALA ALA
SEQRES 28 D 354 HIS TRP ALA
SEQRES 1 A 354 MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY LEU VAL
SEQRES 2 A 354 PRO ARG GLY SER MET VAL ARG VAL ALA ILE ASN GLY PHE
SEQRES 3 A 354 GLY ARG ILE GLY ARG ASN PHE MET ARG CYS TRP LEU GLN
SEQRES 4 A 354 ARG LYS ALA ASN SER LYS LEU GLU ILE VAL GLY ILE ASN
SEQRES 5 A 354 ASP THR SER ASP PRO ARG THR ASN ALA HIS LEU LEU LYS
SEQRES 6 A 354 TYR ASP SER MET LEU GLY ILE PHE GLN ASP ALA GLU ILE
SEQRES 7 A 354 THR ALA ASP ASP ASP CYS ILE TYR ALA GLY GLY HIS ALA
SEQRES 8 A 354 VAL LYS CYS VAL SER ASP ARG ASN PRO GLU ASN LEU PRO
SEQRES 9 A 354 TRP SER ALA TRP GLY ILE ASP LEU VAL ILE GLU ALA THR
SEQRES 10 A 354 GLY VAL PHE THR SER ARG GLU GLY ALA SER LYS HIS LEU
SEQRES 11 A 354 SER ALA GLY ALA LYS LYS VAL LEU ILE THR ALA PRO GLY
SEQRES 12 A 354 LYS GLY ASN ILE PRO THR TYR VAL VAL GLY VAL ASN HIS
SEQRES 13 A 354 HIS THR TYR ASP PRO SER GLU ASP ILE VAL SER ASN ALA
SEQRES 14 A 354 SER CYS THR THR ASN CYS LEU ALA PRO ILE VAL LYS VAL
SEQRES 15 A 354 LEU HIS GLU ALA PHE GLY ILE GLN GLN GLY MET MET THR
SEQRES 16 A 354 THR THR HIS SER TYR THR GLY ASP GLN ARG LEU LEU ASP
SEQRES 17 A 354 ALA SER HIS ARG ASP LEU ARG ARG ALA ARG ALA ALA ALA
SEQRES 18 A 354 MET ASN ILE VAL PRO THR SER THR GLY ALA ALA LYS ALA
SEQRES 19 A 354 VAL GLY LEU VAL ILE PRO GLU LEU GLN GLY LYS LEU ASN
SEQRES 20 A 354 GLY ILE ALA LEU ARG VAL PRO THR PRO ASN VAL SER VAL
SEQRES 21 A 354 VAL ASP PHE VAL ALA GLN VAL GLU LYS PRO THR ILE ALA
SEQRES 22 A 354 GLU GLN VAL ASN GLN VAL ILE LYS GLU ALA SER GLU THR
SEQRES 23 A 354 THR MET LYS GLY ILE ILE HIS TYR SER GLU LEU GLU LEU
SEQRES 24 A 354 VAL SER SER ASP TYR ARG GLY HIS ASN ALA SER SER ILE
SEQRES 25 A 354 LEU ASP ALA SER LEU THR MET VAL LEU GLY GLY ASN LEU
SEQRES 26 A 354 VAL LYS VAL VAL ALA TRP TYR ASP ASN GLU TRP GLY TYR
SEQRES 27 A 354 SER GLN ARG VAL LEU ASP LEU ALA GLU HIS MET ALA ALA
SEQRES 28 A 354 HIS TRP ALA
HET NAD B1001 44
HET NAD C1001 44
HET SO4 C1002 5
HET NAD D1001 44
HET NAD A1001 44
HETNAM NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE
HETNAM SO4 SULFATE ION
FORMUL 7 NAD 4(C21 H27 N7 O14 P2)
FORMUL 9 SO4 O4 S 2-
FORMUL 12 HOH *275(H2 O)
HELIX 1 AA1 GLY B 10 LYS B 24 1 15
HELIX 2 AA2 ALA B 25 SER B 27 5 3
HELIX 3 AA3 ASP B 39 LYS B 48 1 10
HELIX 4 AA4 ASN B 82 LEU B 86 5 5
HELIX 5 AA5 SER B 105 GLY B 116 1 12
HELIX 6 AA6 ASN B 138 TYR B 142 5 5
HELIX 7 AA7 SER B 153 GLY B 171 1 19
HELIX 8 AA8 ALA B 202 ASN B 206 5 5
HELIX 9 AA9 GLY B 213 ILE B 222 1 10
HELIX 10 AB1 PRO B 223 GLN B 226 5 4
HELIX 11 AB2 ILE B 255 THR B 269 1 15
HELIX 12 AB3 VAL B 283 ARG B 288 5 6
HELIX 13 AB4 SER B 299 THR B 301 5 3
HELIX 14 AB5 GLU B 318 HIS B 335 1 18
HELIX 15 AB6 GLY C 10 ARG C 23 1 14
HELIX 16 AB7 LYS C 24 SER C 27 5 4
HELIX 17 AB8 ASP C 39 TYR C 49 1 11
HELIX 18 AB9 ASN C 82 LEU C 86 5 5
HELIX 19 AC1 SER C 105 GLY C 116 1 12
HELIX 20 AC2 ASN C 138 TYR C 142 5 5
HELIX 21 AC3 SER C 153 GLY C 171 1 19
HELIX 22 AC4 ALA C 202 ASN C 206 5 5
HELIX 23 AC5 GLY C 213 ILE C 222 1 10
HELIX 24 AC6 PRO C 223 GLN C 226 5 4
HELIX 25 AC7 ILE C 255 THR C 269 1 15
HELIX 26 AC8 VAL C 283 ARG C 288 5 6
HELIX 27 AC9 SER C 299 THR C 301 5 3
HELIX 28 AD1 GLU C 318 HIS C 335 1 18
HELIX 29 AD2 SER E 56 ASN E 64 1 9
HELIX 30 AD3 ASN F 3 ASP F 20 1 18
HELIX 31 AD4 GLN F 28 HIS F 53 1 26
HELIX 32 AD5 THR F 55 ASN F 64 1 10
HELIX 33 AD6 GLY D 10 ARG D 23 1 14
HELIX 34 AD7 LYS D 24 SER D 27 5 4
HELIX 35 AD8 ASP D 39 TYR D 49 1 11
HELIX 36 AD9 ASN D 82 LEU D 86 5 5
HELIX 37 AE1 SER D 105 GLY D 116 1 12
HELIX 38 AE2 ASN D 138 TYR D 142 5 5
HELIX 39 AE3 SER D 153 GLY D 171 1 19
HELIX 40 AE4 ALA D 202 ASN D 206 5 5
HELIX 41 AE5 GLY D 213 ILE D 222 1 10
HELIX 42 AE6 PRO D 223 GLN D 226 5 4
HELIX 43 AE7 ILE D 255 THR D 269 1 15
HELIX 44 AE8 VAL D 283 ARG D 288 5 6
HELIX 45 AE9 SER D 299 THR D 301 5 3
HELIX 46 AF1 GLU D 318 HIS D 335 1 18
HELIX 47 AF2 GLY A 10 ARG A 23 1 14
HELIX 48 AF3 ASP A 39 LYS A 48 1 10
HELIX 49 AF4 ASN A 82 LEU A 86 5 5
HELIX 50 AF5 SER A 105 GLY A 116 1 12
HELIX 51 AF6 ASN A 138 TYR A 142 5 5
HELIX 52 AF7 SER A 153 GLY A 171 1 19
HELIX 53 AF8 ALA A 202 ASN A 206 5 5
HELIX 54 AF9 ALA A 217 ILE A 222 1 6
HELIX 55 AG1 PRO A 223 GLN A 226 5 4
HELIX 56 AG2 ILE A 255 THR A 269 1 15
HELIX 57 AG3 VAL A 283 ARG A 288 5 6
HELIX 58 AG4 SER A 299 THR A 301 5 3
HELIX 59 AG5 GLU A 318 HIS A 335 1 18
SHEET 1 AA1 8 ILE B 61 ALA B 63 0
SHEET 2 AA1 8 CYS B 67 ALA B 70 -1 O TYR B 69 N THR B 62
SHEET 3 AA1 8 HIS B 73 VAL B 78 -1 O VAL B 75 N ILE B 68
SHEET 4 AA1 8 LEU B 29 ASN B 35 1 N VAL B 32 O LYS B 76
SHEET 5 AA1 8 VAL B 2 ASN B 7 1 N VAL B 4 O VAL B 32
SHEET 6 AA1 8 LEU B 95 GLU B 98 1 O ILE B 97 N ALA B 5
SHEET 7 AA1 8 LYS B 119 ILE B 122 1 O LEU B 121 N VAL B 96
SHEET 8 AA1 8 ILE B 148 SER B 150 1 O VAL B 149 N ILE B 122
SHEET 1 AA2 2 TYR B 49 ASP B 50 0
SHEET 2 AA2 2 GLY B 54 ILE B 55 -1 O GLY B 54 N ASP B 50
SHEET 1 AA3 7 VAL B 208 SER B 211 0
SHEET 2 AA3 7 LEU B 229 VAL B 236 -1 O ARG B 235 N VAL B 208
SHEET 3 AA3 7 ILE B 172 SER B 182 1 N THR B 179 O LEU B 234
SHEET 4 AA3 7 SER B 242 VAL B 250 -1 O ASP B 245 N THR B 178
SHEET 5 AA3 7 LEU B 308 TYR B 315 -1 O ALA B 313 N VAL B 244
SHEET 6 AA3 7 SER B 294 ASP B 297 -1 N ASP B 297 O VAL B 312
SHEET 7 AA3 7 ILE B 275 SER B 278 1 N HIS B 276 O SER B 294
SHEET 1 AA4 6 VAL B 208 SER B 211 0
SHEET 2 AA4 6 LEU B 229 VAL B 236 -1 O ARG B 235 N VAL B 208
SHEET 3 AA4 6 ILE B 172 SER B 182 1 N THR B 179 O LEU B 234
SHEET 4 AA4 6 SER B 242 VAL B 250 -1 O ASP B 245 N THR B 178
SHEET 5 AA4 6 LEU B 308 TYR B 315 -1 O ALA B 313 N VAL B 244
SHEET 6 AA4 6 MET B 302 LEU B 304 -1 N MET B 302 O LYS B 310
SHEET 1 AA5 8 ILE C 61 ALA C 63 0
SHEET 2 AA5 8 CYS C 67 ALA C 70 -1 O TYR C 69 N THR C 62
SHEET 3 AA5 8 HIS C 73 VAL C 78 -1 O HIS C 73 N ALA C 70
SHEET 4 AA5 8 LEU C 29 ASN C 35 1 N ILE C 34 O LYS C 76
SHEET 5 AA5 8 VAL C 2 ASN C 7 1 N VAL C 4 O GLU C 30
SHEET 6 AA5 8 LEU C 95 GLU C 98 1 O ILE C 97 N ALA C 5
SHEET 7 AA5 8 LYS C 119 ILE C 122 1 O LEU C 121 N VAL C 96
SHEET 8 AA5 8 ILE C 148 SER C 150 1 O VAL C 149 N ILE C 122
SHEET 1 AA6 7 VAL C 208 THR C 210 0
SHEET 2 AA6 7 LEU C 229 VAL C 236 -1 O ARG C 235 N VAL C 208
SHEET 3 AA6 7 ILE C 172 SER C 182 1 N HIS C 181 O VAL C 236
SHEET 4 AA6 7 SER C 242 VAL C 250 -1 O GLN C 249 N GLN C 174
SHEET 5 AA6 7 LEU C 308 TYR C 315 -1 O TYR C 315 N SER C 242
SHEET 6 AA6 7 SER C 294 ASP C 297 -1 N ILE C 295 O TRP C 314
SHEET 7 AA6 7 ILE C 275 SER C 278 1 N HIS C 276 O SER C 294
SHEET 1 AA7 6 VAL C 208 THR C 210 0
SHEET 2 AA7 6 LEU C 229 VAL C 236 -1 O ARG C 235 N VAL C 208
SHEET 3 AA7 6 ILE C 172 SER C 182 1 N HIS C 181 O VAL C 236
SHEET 4 AA7 6 SER C 242 VAL C 250 -1 O GLN C 249 N GLN C 174
SHEET 5 AA7 6 LEU C 308 TYR C 315 -1 O TYR C 315 N SER C 242
SHEET 6 AA7 6 MET C 302 LEU C 304 -1 N MET C 302 O LYS C 310
SHEET 1 AA8 8 ILE D 61 ALA D 63 0
SHEET 2 AA8 8 CYS D 67 ALA D 70 -1 O TYR D 69 N THR D 62
SHEET 3 AA8 8 HIS D 73 VAL D 78 -1 O VAL D 75 N ILE D 68
SHEET 4 AA8 8 LEU D 29 ASN D 35 1 N ILE D 34 O VAL D 78
SHEET 5 AA8 8 VAL D 2 ASN D 7 1 N VAL D 4 O VAL D 32
SHEET 6 AA8 8 LEU D 95 GLU D 98 1 O ILE D 97 N ALA D 5
SHEET 7 AA8 8 LYS D 119 ILE D 122 1 O LEU D 121 N VAL D 96
SHEET 8 AA8 8 ILE D 148 SER D 150 1 O VAL D 149 N ILE D 122
SHEET 1 AA9 7 VAL D 208 SER D 211 0
SHEET 2 AA9 7 LEU D 229 VAL D 236 -1 O ARG D 235 N VAL D 208
SHEET 3 AA9 7 ILE D 172 SER D 182 1 N HIS D 181 O VAL D 236
SHEET 4 AA9 7 SER D 242 VAL D 250 -1 O GLN D 249 N GLN D 173
SHEET 5 AA9 7 LEU D 308 TYR D 315 -1 O ALA D 313 N VAL D 244
SHEET 6 AA9 7 SER D 294 ASP D 297 -1 N ASP D 297 O VAL D 312
SHEET 7 AA9 7 ILE D 275 SER D 278 1 N HIS D 276 O SER D 294
SHEET 1 AB1 6 VAL D 208 SER D 211 0
SHEET 2 AB1 6 LEU D 229 VAL D 236 -1 O ARG D 235 N VAL D 208
SHEET 3 AB1 6 ILE D 172 SER D 182 1 N HIS D 181 O VAL D 236
SHEET 4 AB1 6 SER D 242 VAL D 250 -1 O GLN D 249 N GLN D 173
SHEET 5 AB1 6 LEU D 308 TYR D 315 -1 O ALA D 313 N VAL D 244
SHEET 6 AB1 6 MET D 302 LEU D 304 -1 N MET D 302 O LYS D 310
SHEET 1 AB2 8 ILE A 61 ALA A 63 0
SHEET 2 AB2 8 CYS A 67 ALA A 70 -1 O TYR A 69 N THR A 62
SHEET 3 AB2 8 HIS A 73 VAL A 78 -1 O VAL A 75 N ILE A 68
SHEET 4 AB2 8 LEU A 29 ASN A 35 1 N ILE A 34 O LYS A 76
SHEET 5 AB2 8 VAL A 2 ASN A 7 1 N VAL A 4 O GLU A 30
SHEET 6 AB2 8 LEU A 95 GLU A 98 1 O ILE A 97 N ALA A 5
SHEET 7 AB2 8 LYS A 119 ILE A 122 1 O LEU A 121 N VAL A 96
SHEET 8 AB2 8 ILE A 148 SER A 150 1 O VAL A 149 N ILE A 122
SHEET 1 AB3 2 TYR A 49 ASP A 50 0
SHEET 2 AB3 2 GLY A 54 ILE A 55 -1 O GLY A 54 N ASP A 50
SHEET 1 AB4 7 VAL A 208 SER A 211 0
SHEET 2 AB4 7 LEU A 229 VAL A 236 -1 O ARG A 235 N VAL A 208
SHEET 3 AB4 7 ILE A 172 SER A 182 1 N HIS A 181 O VAL A 236
SHEET 4 AB4 7 SER A 242 VAL A 250 -1 O VAL A 247 N MET A 176
SHEET 5 AB4 7 LEU A 308 TYR A 315 -1 O TYR A 315 N SER A 242
SHEET 6 AB4 7 SER A 294 ASP A 297 -1 N ILE A 295 O TRP A 314
SHEET 7 AB4 7 ILE A 275 SER A 278 1 N HIS A 276 O SER A 294
SHEET 1 AB5 6 VAL A 208 SER A 211 0
SHEET 2 AB5 6 LEU A 229 VAL A 236 -1 O ARG A 235 N VAL A 208
SHEET 3 AB5 6 ILE A 172 SER A 182 1 N HIS A 181 O VAL A 236
SHEET 4 AB5 6 SER A 242 VAL A 250 -1 O VAL A 247 N MET A 176
SHEET 5 AB5 6 LEU A 308 TYR A 315 -1 O TYR A 315 N SER A 242
SHEET 6 AB5 6 MET A 302 LEU A 304 -1 N MET A 302 O LYS A 310
SSBOND 1 CYS E 61 CYS E 70 1555 1555 2.03
SSBOND 2 CYS F 19 CYS F 29 1555 1555 2.03
SSBOND 3 CYS F 61 CYS F 70 1555 1555 2.03
SITE 1 AC1 29 GLY B 8 PHE B 9 GLY B 10 ARG B 11
SITE 2 AC1 29 ILE B 12 ASN B 35 ASP B 36 THR B 37
SITE 3 AC1 29 ARG B 81 ALA B 99 THR B 100 GLY B 101
SITE 4 AC1 29 PHE B 103 THR B 123 CYS B 154 ASN B 317
SITE 5 AC1 29 TYR B 321 HOH B1101 HOH B1107 HOH B1108
SITE 6 AC1 29 HOH B1119 HOH B1126 HOH B1129 HOH B1135
SITE 7 AC1 29 HOH B1138 HOH B1140 HOH C1154 ASP F 66
SITE 8 AC1 29 TYR F 73
SITE 1 AC2 26 HOH B1114 GLY C 8 GLY C 10 ARG C 11
SITE 2 AC2 26 ILE C 12 ASN C 35 ASP C 36 THR C 37
SITE 3 AC2 26 ARG C 81 ALA C 99 THR C 100 GLY C 101
SITE 4 AC2 26 PHE C 103 THR C 123 ALA C 124 CYS C 154
SITE 5 AC2 26 ASN C 317 TYR C 321 HOH C1101 HOH C1113
SITE 6 AC2 26 HOH C1119 HOH C1128 HOH C1133 HOH C1138
SITE 7 AC2 26 HOH C1141 HOH F 101
SITE 1 AC3 7 SER C 153 CYS C 154 THR C 155 HIS C 181
SITE 2 AC3 7 THR C 212 GLY C 213 HOH C1145
SITE 1 AC4 23 GLY D 8 GLY D 10 ARG D 11 ILE D 12
SITE 2 AC4 23 ASN D 35 ASP D 36 THR D 37 ARG D 81
SITE 3 AC4 23 ALA D 99 THR D 100 GLY D 101 THR D 123
SITE 4 AC4 23 ALA D 124 CYS D 154 THR D 184 ASN D 317
SITE 5 AC4 23 TYR D 321 HOH D1104 HOH D1125 HOH D1133
SITE 6 AC4 23 HOH D1143 HOH D1157 HOH D1158
SITE 1 AC5 25 GLY A 8 PHE A 9 GLY A 10 ARG A 11
SITE 2 AC5 25 ILE A 12 ASN A 35 ASP A 36 THR A 37
SITE 3 AC5 25 ARG A 81 ALA A 99 THR A 100 GLY A 101
SITE 4 AC5 25 THR A 123 ALA A 124 CYS A 154 ASN A 317
SITE 5 AC5 25 TYR A 321 HOH A1105 HOH A1112 HOH A1124
SITE 6 AC5 25 HOH A1126 HOH A1127 HOH D1144 ASP E 66
SITE 7 AC5 25 TYR E 73
CRYST1 133.438 146.964 81.428 90.00 90.00 90.00 P 21 21 2 16
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 0.007494 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006804 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012281 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
