HEADER TRANSFERASE 23-JUL-12 4G9H
TITLE CRYSTAL STRUCTURE OF GLUTAHTIONE S-TRANSFERASE HOMOLOG FROM YERSINIA
TITLE 2 PESTIS, TARGET EFI-501894, WITH BOUND GLUTATHIONE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUTATHIONE S-TRANSFERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: GLUTATHIONINE S-TRANSFERASE;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: YERSINIA PESTIS;
SOURCE 3 ORGANISM_TAXID: 632;
SOURCE 4 GENE: GST, GST2, Y1968, YP_2153;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET
KEYWDS GST, GLUTATHIONE S-TRANSFERASE, ENZYME FUNCTION INITIATIVE, EFI,
KEYWDS 2 STRUCTURAL GENOMICS, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.W.VETTING,R.TORO,R.BHOSLE,N.F.AL OBAIDI,L.L.MORISCO,S.R.WASSERMAN,
AUTHOR 2 S.SOJITRA,E.WASHINGTON,A.SCOTT GLENN,S.CHOWDHURY,B.EVANS,J.HAMMONDS,
AUTHOR 3 B.HILLERICH,J.LOVE,R.D.SEIDEL,H.J.IMKER,R.N.ARMSTRONG,J.A.GERLT,
AUTHOR 4 S.C.ALMO,ENZYME FUNCTION INITIATIVE (EFI)
REVDAT 1 15-AUG-12 4G9H 0
JRNL AUTH M.W.VETTING,R.TORO,R.BHOSLE,N.F.AL OBAIDI,L.L.MORISCO,
JRNL AUTH 2 S.R.WASSERMAN,S.SOJITRA,E.WASHINGTON,A.SCOTT GLENN,
JRNL AUTH 3 S.CHOWDHURY,B.EVANS,J.HAMMONDS,B.HILLERICH,J.LOVE,
JRNL AUTH 4 R.D.SEIDEL,H.J.IMKER,R.N.ARMSTRONG,J.A.GERLT,S.C.ALMO,
JRNL AUTH 5 ENZYME FUNCTION INITIATIVE (EFI)
JRNL TITL CRYSTAL STRUCTURE OF GLUTAHTIONE S-TRANSFERASE HOMOLOG FROM
JRNL TITL 2 YERSINIA PESTIS, TARGET EFI-501894, WITH BOUND GLUTATHIONE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8_1069)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.77
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 34755
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.178
REMARK 3 R VALUE (WORKING SET) : 0.176
REMARK 3 FREE R VALUE : 0.216
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.040
REMARK 3 FREE R VALUE TEST SET COUNT : 1751
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 34.7749 - 4.9335 0.99 2759 120 0.1727 0.1967
REMARK 3 2 4.9335 - 3.9176 1.00 2625 128 0.1453 0.1848
REMARK 3 3 3.9176 - 3.4229 1.00 2564 147 0.1678 0.1917
REMARK 3 4 3.4229 - 3.1101 1.00 2537 142 0.1782 0.1891
REMARK 3 5 3.1101 - 2.8873 1.00 2533 139 0.1870 0.2465
REMARK 3 6 2.8873 - 2.7172 1.00 2520 151 0.1783 0.2364
REMARK 3 7 2.7172 - 2.5811 1.00 2498 133 0.1810 0.2490
REMARK 3 8 2.5811 - 2.4688 1.00 2476 163 0.1783 0.2360
REMARK 3 9 2.4688 - 2.3738 1.00 2499 127 0.1966 0.2286
REMARK 3 10 2.3738 - 2.2919 1.00 2539 116 0.1892 0.2707
REMARK 3 11 2.2919 - 2.2202 1.00 2476 120 0.2170 0.2691
REMARK 3 12 2.2202 - 2.1568 1.00 2491 129 0.2093 0.2839
REMARK 3 13 2.1568 - 2.1000 1.00 2487 136 0.2224 0.2648
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) : 0.190
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.990
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.50
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.007 3383
REMARK 3 ANGLE : 1.019 4599
REMARK 3 CHIRALITY : 0.064 515
REMARK 3 PLANARITY : 0.004 593
REMARK 3 DIHEDRAL : 14.756 1280
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 18
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: chain 'A' and (resid 0 through 30 )
REMARK 3 ORIGIN FOR THE GROUP (A): 47.7014 97.7130 30.2589
REMARK 3 T TENSOR
REMARK 3 T11: 0.2792 T22: 0.2397
REMARK 3 T33: 0.4297 T12: -0.3046
REMARK 3 T13: -0.3705 T23: 0.0110
REMARK 3 L TENSOR
REMARK 3 L11: 0.7030 L22: 0.6832
REMARK 3 L33: 0.3940 L12: 0.3747
REMARK 3 L13: 0.0681 L23: -0.1211
REMARK 3 S TENSOR
REMARK 3 S11: -0.0296 S12: -0.1633 S13: 0.2635
REMARK 3 S21: 0.2639 S22: -0.0463 S23: -0.3942
REMARK 3 S31: -0.3982 S32: 0.4961 S33: -0.1216
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: chain 'A' and (resid 31 through 54 )
REMARK 3 ORIGIN FOR THE GROUP (A): 43.2643 106.3733 42.1844
REMARK 3 T TENSOR
REMARK 3 T11: 1.1616 T22: 0.5357
REMARK 3 T33: 0.4603 T12: -0.2038
REMARK 3 T13: -0.2077 T23: -0.1641
REMARK 3 L TENSOR
REMARK 3 L11: 0.5482 L22: 0.0023
REMARK 3 L33: 0.2713 L12: 0.0328
REMARK 3 L13: 0.3862 L23: 0.0217
REMARK 3 S TENSOR
REMARK 3 S11: -0.0429 S12: -0.2602 S13: 0.2787
REMARK 3 S21: 0.2121 S22: 0.0676 S23: -0.2661
REMARK 3 S31: -0.2934 S32: 0.2280 S33: -0.0152
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: chain 'A' and (resid 55 through 66 )
REMARK 3 ORIGIN FOR THE GROUP (A): 44.0772 108.5088 27.7338
REMARK 3 T TENSOR
REMARK 3 T11: 0.5010 T22: 0.2689
REMARK 3 T33: 0.4631 T12: -0.3149
REMARK 3 T13: -0.0382 T23: -0.1090
REMARK 3 L TENSOR
REMARK 3 L11: 2.4975 L22: 3.7943
REMARK 3 L33: 0.0930 L12: 1.8416
REMARK 3 L13: 0.3295 L23: -0.1035
REMARK 3 S TENSOR
REMARK 3 S11: -0.1359 S12: 0.0492 S13: 0.1329
REMARK 3 S21: 0.0293 S22: -0.0119 S23: -0.1284
REMARK 3 S31: -0.0320 S32: 0.0406 S33: -0.1022
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: chain 'A' and (resid 67 through 105 )
REMARK 3 ORIGIN FOR THE GROUP (A): 34.7896 95.9255 19.1485
REMARK 3 T TENSOR
REMARK 3 T11: 0.1921 T22: 0.1730
REMARK 3 T33: 0.1772 T12: -0.0425
REMARK 3 T13: 0.0157 T23: -0.0008
REMARK 3 L TENSOR
REMARK 3 L11: 1.4732 L22: 1.3752
REMARK 3 L33: 1.7728 L12: 0.5717
REMARK 3 L13: -0.0112 L23: -0.4064
REMARK 3 S TENSOR
REMARK 3 S11: -0.0333 S12: 0.2821 S13: -0.0379
REMARK 3 S21: 0.0498 S22: 0.0467 S23: -0.1394
REMARK 3 S31: -0.1489 S32: 0.1455 S33: 0.0115
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: chain 'A' and (resid 106 through 119 )
REMARK 3 ORIGIN FOR THE GROUP (A): 28.9206 92.7569 43.4382
REMARK 3 T TENSOR
REMARK 3 T11: 0.5479 T22: 0.2120
REMARK 3 T33: 0.2647 T12: 0.0724
REMARK 3 T13: 0.0238 T23: 0.0369
REMARK 3 L TENSOR
REMARK 3 L11: 0.6165 L22: 0.0402
REMARK 3 L33: 3.3115 L12: 0.0745
REMARK 3 L13: -0.7541 L23: -0.3683
REMARK 3 S TENSOR
REMARK 3 S11: -0.2635 S12: -0.1778 S13: 0.2334
REMARK 3 S21: 0.3141 S22: 0.0153 S23: -0.0818
REMARK 3 S31: -0.3365 S32: 0.0288 S33: 0.0622
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: chain 'A' and (resid 120 through 141 )
REMARK 3 ORIGIN FOR THE GROUP (A): 23.0622 84.3797 37.4709
REMARK 3 T TENSOR
REMARK 3 T11: 0.4014 T22: 0.2312
REMARK 3 T33: 0.2486 T12: 0.0671
REMARK 3 T13: 0.0739 T23: 0.0648
REMARK 3 L TENSOR
REMARK 3 L11: 1.0207 L22: 1.4075
REMARK 3 L33: 5.9007 L12: -0.4219
REMARK 3 L13: -1.4094 L23: 2.2110
REMARK 3 S TENSOR
REMARK 3 S11: -0.1170 S12: -0.1079 S13: 0.0572
REMARK 3 S21: 0.3912 S22: 0.1684 S23: 0.3154
REMARK 3 S31: -0.1101 S32: -0.4938 S33: -0.0031
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: chain 'A' and (resid 142 through 168 )
REMARK 3 ORIGIN FOR THE GROUP (A): 35.9847 85.2646 25.5516
REMARK 3 T TENSOR
REMARK 3 T11: 0.2117 T22: 0.1278
REMARK 3 T33: 0.2231 T12: 0.0142
REMARK 3 T13: -0.0018 T23: 0.0088
REMARK 3 L TENSOR
REMARK 3 L11: 2.1158 L22: 2.1474
REMARK 3 L33: 1.3625 L12: 0.5449
REMARK 3 L13: -0.1710 L23: -0.1181
REMARK 3 S TENSOR
REMARK 3 S11: -0.1910 S12: 0.1085 S13: -0.2220
REMARK 3 S21: 0.0415 S22: -0.0110 S23: -0.2920
REMARK 3 S31: 0.2178 S32: 0.2175 S33: 0.1378
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: chain 'A' and (resid 169 through 188 )
REMARK 3 ORIGIN FOR THE GROUP (A): 33.2002 77.5939 32.5871
REMARK 3 T TENSOR
REMARK 3 T11: 0.3522 T22: 0.1416
REMARK 3 T33: 0.2242 T12: 0.0443
REMARK 3 T13: -0.0597 T23: 0.0110
REMARK 3 L TENSOR
REMARK 3 L11: 1.8816 L22: 1.7857
REMARK 3 L33: 2.3706 L12: 0.8876
REMARK 3 L13: 1.1577 L23: 0.1711
REMARK 3 S TENSOR
REMARK 3 S11: -0.0763 S12: 0.0262 S13: -0.2774
REMARK 3 S21: 0.2388 S22: 0.1811 S23: -0.1525
REMARK 3 S31: 0.3089 S32: -0.1884 S33: -0.0459
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: chain 'A' and (resid 189 through 201 )
REMARK 3 ORIGIN FOR THE GROUP (A): 49.4606 87.2075 31.5449
REMARK 3 T TENSOR
REMARK 3 T11: 0.1811 T22: 0.5223
REMARK 3 T33: 0.6657 T12: 0.0329
REMARK 3 T13: -0.1808 T23: 0.1764
REMARK 3 L TENSOR
REMARK 3 L11: 2.2218 L22: 0.7230
REMARK 3 L33: 0.3592 L12: -0.4267
REMARK 3 L13: 0.2888 L23: 0.1540
REMARK 3 S TENSOR
REMARK 3 S11: -0.0145 S12: -0.2372 S13: 0.0138
REMARK 3 S21: 0.1974 S22: 0.0181 S23: -0.3001
REMARK 3 S31: 0.0659 S32: 0.2647 S33: -0.0726
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: chain 'B' and (resid 0 through 54 )
REMARK 3 ORIGIN FOR THE GROUP (A): 10.3756 96.4208 20.8364
REMARK 3 T TENSOR
REMARK 3 T11: 0.2409 T22: 0.2323
REMARK 3 T33: 0.4330 T12: -0.0535
REMARK 3 T13: 0.0450 T23: 0.0056
REMARK 3 L TENSOR
REMARK 3 L11: 0.7406 L22: 1.8174
REMARK 3 L33: 1.0650 L12: 0.2697
REMARK 3 L13: 0.0788 L23: 0.1514
REMARK 3 S TENSOR
REMARK 3 S11: -0.0145 S12: 0.0333 S13: -0.3589
REMARK 3 S21: -0.0157 S22: -0.0961 S23: 0.7735
REMARK 3 S31: 0.2597 S32: -0.4418 S33: 0.0561
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: chain 'B' and (resid 55 through 66 )
REMARK 3 ORIGIN FOR THE GROUP (A): 17.6521 93.3969 13.8731
REMARK 3 T TENSOR
REMARK 3 T11: 0.3096 T22: 0.2735
REMARK 3 T33: 0.2043 T12: -0.0790
REMARK 3 T13: -0.0160 T23: -0.0449
REMARK 3 L TENSOR
REMARK 3 L11: 2.3128 L22: 1.9946
REMARK 3 L33: 1.4539 L12: 0.2053
REMARK 3 L13: 0.5820 L23: 1.6590
REMARK 3 S TENSOR
REMARK 3 S11: 0.1914 S12: 0.3836 S13: -0.2117
REMARK 3 S21: -0.0593 S22: -0.1354 S23: 0.1602
REMARK 3 S31: 0.0817 S32: -0.0494 S33: -0.0408
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: chain 'B' and (resid 67 through 105 )
REMARK 3 ORIGIN FOR THE GROUP (A): 27.5970 107.0017 19.2282
REMARK 3 T TENSOR
REMARK 3 T11: 0.2800 T22: 0.1296
REMARK 3 T33: 0.1976 T12: -0.0148
REMARK 3 T13: 0.0236 T23: 0.0271
REMARK 3 L TENSOR
REMARK 3 L11: 1.7289 L22: 1.2952
REMARK 3 L33: 1.3677 L12: 0.3410
REMARK 3 L13: -0.2296 L23: 0.0554
REMARK 3 S TENSOR
REMARK 3 S11: -0.0213 S12: 0.1947 S13: 0.1360
REMARK 3 S21: -0.0790 S22: 0.0045 S23: -0.2622
REMARK 3 S31: -0.4487 S32: 0.1611 S33: 0.0409
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: chain 'B' and (resid 106 through 119 )
REMARK 3 ORIGIN FOR THE GROUP (A): 16.5301 97.9498 40.4006
REMARK 3 T TENSOR
REMARK 3 T11: 0.4363 T22: 0.3036
REMARK 3 T33: 0.3399 T12: 0.0271
REMARK 3 T13: 0.1765 T23: 0.1269
REMARK 3 L TENSOR
REMARK 3 L11: 1.5334 L22: 0.0814
REMARK 3 L33: 1.1667 L12: -0.0815
REMARK 3 L13: 0.1167 L23: 0.2945
REMARK 3 S TENSOR
REMARK 3 S11: -0.0165 S12: -0.3621 S13: -0.4965
REMARK 3 S21: 0.1743 S22: 0.1099 S23: 0.3683
REMARK 3 S31: 0.2452 S32: -0.2574 S33: 0.0249
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: chain 'B' and (resid 120 through 141 )
REMARK 3 ORIGIN FOR THE GROUP (A): 22.8126 107.4726 43.9222
REMARK 3 T TENSOR
REMARK 3 T11: 0.6060 T22: 0.3847
REMARK 3 T33: 0.2289 T12: 0.1836
REMARK 3 T13: 0.0529 T23: 0.0128
REMARK 3 L TENSOR
REMARK 3 L11: 2.0178 L22: 2.8713
REMARK 3 L33: 1.3083 L12: 0.3285
REMARK 3 L13: 0.1770 L23: -1.4426
REMARK 3 S TENSOR
REMARK 3 S11: -0.3272 S12: -0.7923 S13: -0.2135
REMARK 3 S21: 0.5568 S22: 0.1946 S23: 0.1490
REMARK 3 S31: -0.1097 S32: 0.1882 S33: 0.1170
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: chain 'B' and (resid 142 through 153 )
REMARK 3 ORIGIN FOR THE GROUP (A): 25.9707 119.0988 25.3801
REMARK 3 T TENSOR
REMARK 3 T11: 0.4942 T22: 0.1496
REMARK 3 T33: 0.2915 T12: -0.0691
REMARK 3 T13: -0.0367 T23: -0.0160
REMARK 3 L TENSOR
REMARK 3 L11: 3.0001 L22: 4.8322
REMARK 3 L33: 1.8515 L12: 1.1076
REMARK 3 L13: -0.1765 L23: 1.6806
REMARK 3 S TENSOR
REMARK 3 S11: -0.1018 S12: 0.0198 S13: 0.4302
REMARK 3 S21: -0.0057 S22: 0.0341 S23: -0.2146
REMARK 3 S31: -0.3843 S32: 0.2633 S33: 0.0373
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: chain 'B' and (resid 154 through 168 )
REMARK 3 ORIGIN FOR THE GROUP (A): 16.8085 108.8116 30.7046
REMARK 3 T TENSOR
REMARK 3 T11: 0.3061 T22: 0.1785
REMARK 3 T33: 0.1665 T12: 0.0389
REMARK 3 T13: 0.0546 T23: 0.0357
REMARK 3 L TENSOR
REMARK 3 L11: 1.1396 L22: 1.1069
REMARK 3 L33: 2.1245 L12: 0.4101
REMARK 3 L13: -0.2780 L23: -0.7672
REMARK 3 S TENSOR
REMARK 3 S11: -0.1114 S12: -0.2822 S13: -0.0684
REMARK 3 S21: 0.3342 S22: 0.1022 S23: 0.0962
REMARK 3 S31: -0.2220 S32: -0.2653 S33: -0.0412
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: chain 'B' and (resid 169 through 188 )
REMARK 3 ORIGIN FOR THE GROUP (A): 17.6163 117.0835 36.8010
REMARK 3 T TENSOR
REMARK 3 T11: 0.5421 T22: 0.2870
REMARK 3 T33: 0.2123 T12: 0.1556
REMARK 3 T13: 0.0239 T23: -0.0197
REMARK 3 L TENSOR
REMARK 3 L11: 1.7482 L22: 1.8076
REMARK 3 L33: 3.0880 L12: 0.1815
REMARK 3 L13: 0.7758 L23: 0.0522
REMARK 3 S TENSOR
REMARK 3 S11: -0.1739 S12: -0.3328 S13: 0.1477
REMARK 3 S21: 0.5830 S22: 0.0827 S23: -0.0771
REMARK 3 S31: -0.3419 S32: 0.0906 S33: 0.0233
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: chain 'B' and (resid 189 through 201 )
REMARK 3 ORIGIN FOR THE GROUP (A): 7.3722 111.1759 22.0555
REMARK 3 T TENSOR
REMARK 3 T11: 0.1767 T22: 0.2002
REMARK 3 T33: 0.2964 T12: 0.0259
REMARK 3 T13: 0.0483 T23: 0.0787
REMARK 3 L TENSOR
REMARK 3 L11: 1.8752 L22: 4.0996
REMARK 3 L33: 2.1678 L12: 1.0453
REMARK 3 L13: 0.5001 L23: -0.2794
REMARK 3 S TENSOR
REMARK 3 S11: -0.0107 S12: -0.2148 S13: -0.2274
REMARK 3 S21: 0.0597 S22: 0.0585 S23: 0.5710
REMARK 3 S31: -0.0069 S32: -0.2743 S33: -0.0628
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 4G9H COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-JUL-12.
REMARK 100 THE RCSB ID CODE IS RCSB073906.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-JUL-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 31-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9793
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX 225 HE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 34816
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 75.709
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 9.600
REMARK 200 R MERGE (I) : 0.10700
REMARK 200 R SYM (I) : 0.10700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.13
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 9.70
REMARK 200 R MERGE FOR SHELL (I) : 0.79100
REMARK 200 R SYM FOR SHELL (I) : 0.79100
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: 2PMT
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.31
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.02
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN (10 MM HEPES PH 7.5, 100 MM
REMARK 280 NACL); RESERVOIR (0.6 M NACL, 0.1 M MES PH 6.5, 20% PEG4000);
REMARK 280 CRYOPROTECTION (RESERVOIR, + 20% GLYCEROL), SITTING DROP VAPOR
REMARK 280 DIFFUCTION, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 74.39300
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 43.97250
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 43.97250
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 37.19650
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 43.97250
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 43.97250
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 111.58950
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 43.97250
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 43.97250
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 37.19650
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 43.97250
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 43.97250
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 111.58950
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 74.39300
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 300 REMARK: BIOLOGICAL UNIT IS DIMER
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: 4840 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16850 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A -1
REMARK 465 LYS A 202
REMARK 465 ALA A 203
REMARK 465 GLU A 204
REMARK 465 ASN A 205
REMARK 465 LEU A 206
REMARK 465 TYR A 207
REMARK 465 PHE A 208
REMARK 465 GLN A 209
REMARK 465 MET B -1
REMARK 465 LYS B 202
REMARK 465 ALA B 203
REMARK 465 GLU B 204
REMARK 465 ASN B 205
REMARK 465 LEU B 206
REMARK 465 TYR B 207
REMARK 465 PHE B 208
REMARK 465 GLN B 209
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 MET B 2 N CA C O CB CG SD
REMARK 480 MET B 2 CE
REMARK 480 VAL B 162 N CA C O CB CG1 CG2
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 OD1 ASP B 80 O HOH B 431 2.14
REMARK 500 OE1 GLU B 188 O HOH B 474 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 VAL A 34 -62.73 -99.21
REMARK 500 GLU A 66 109.64 72.95
REMARK 500 LEU A 106 -66.02 -99.10
REMARK 500 ALA B 10 -177.72 -68.83
REMARK 500 ILE B 47 -61.15 -97.18
REMARK 500 GLU B 66 112.89 74.36
REMARK 500 LEU B 106 -68.13 -91.77
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 GSH A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GSH B 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: EFI-501894 RELATED DB: TARGETTRACK
DBREF 4G9H A 1 202 UNP Q8D0L3 Q8D0L3_YERPE 1 202
DBREF 4G9H B 1 202 UNP Q8D0L3 Q8D0L3_YERPE 1 202
SEQADV 4G9H MET A -1 UNP Q8D0L3 INITIATING METHIONINE
SEQADV 4G9H VAL A 0 UNP Q8D0L3 EXPRESSION TAG
SEQADV 4G9H ALA A 203 UNP Q8D0L3 EXPRESSION TAG
SEQADV 4G9H GLU A 204 UNP Q8D0L3 EXPRESSION TAG
SEQADV 4G9H ASN A 205 UNP Q8D0L3 EXPRESSION TAG
SEQADV 4G9H LEU A 206 UNP Q8D0L3 EXPRESSION TAG
SEQADV 4G9H TYR A 207 UNP Q8D0L3 EXPRESSION TAG
SEQADV 4G9H PHE A 208 UNP Q8D0L3 EXPRESSION TAG
SEQADV 4G9H GLN A 209 UNP Q8D0L3 EXPRESSION TAG
SEQADV 4G9H MET B -1 UNP Q8D0L3 INITIATING METHIONINE
SEQADV 4G9H VAL B 0 UNP Q8D0L3 EXPRESSION TAG
SEQADV 4G9H ALA B 203 UNP Q8D0L3 EXPRESSION TAG
SEQADV 4G9H GLU B 204 UNP Q8D0L3 EXPRESSION TAG
SEQADV 4G9H ASN B 205 UNP Q8D0L3 EXPRESSION TAG
SEQADV 4G9H LEU B 206 UNP Q8D0L3 EXPRESSION TAG
SEQADV 4G9H TYR B 207 UNP Q8D0L3 EXPRESSION TAG
SEQADV 4G9H PHE B 208 UNP Q8D0L3 EXPRESSION TAG
SEQADV 4G9H GLN B 209 UNP Q8D0L3 EXPRESSION TAG
SEQRES 1 A 211 MET VAL MET MET LYS LEU PHE TYR LYS PRO GLY ALA CYS
SEQRES 2 A 211 SER LEU SER PRO HIS ILE VAL LEU ARG GLU ALA GLY LEU
SEQRES 3 A 211 ASP PHE SER ILE GLU ARG VAL ASP LEU VAL THR LYS LYS
SEQRES 4 A 211 THR GLU THR GLY ALA ASP TYR LEU SER ILE ASN PRO LYS
SEQRES 5 A 211 GLY GLN VAL PRO ALA LEU VAL LEU ASP ASP GLY SER LEU
SEQRES 6 A 211 LEU THR GLU GLY VAL ALA ILE VAL GLN TYR LEU ALA ASP
SEQRES 7 A 211 LYS VAL PRO ASP ARG HIS LEU ILE ALA PRO SER GLY THR
SEQRES 8 A 211 LEU SER ARG TYR HIS ALA ILE GLU TRP LEU ASN PHE ILE
SEQRES 9 A 211 ALA THR GLU LEU HIS LYS GLY PHE SER PRO LEU PHE ASN
SEQRES 10 A 211 PRO ASN THR PRO ASP GLU TYR LYS THR ILE VAL ARG GLU
SEQRES 11 A 211 ARG LEU ASP LYS GLN PHE SER TYR VAL ASP SER VAL LEU
SEQRES 12 A 211 ALA GLU HIS ASP TYR LEU LEU GLY LYS LYS PHE SER VAL
SEQRES 13 A 211 ALA ASP ALA TYR LEU PHE THR VAL SER ARG TRP ALA ASN
SEQRES 14 A 211 ALA LEU ASN LEU GLN ILE LYS GLU ARG SER HIS LEU ASP
SEQRES 15 A 211 GLN TYR MET ALA ARG VAL ALA GLU ARG PRO ALA VAL LYS
SEQRES 16 A 211 ALA ALA LEU ALA ALA GLU ASP ILE LYS ALA GLU ASN LEU
SEQRES 17 A 211 TYR PHE GLN
SEQRES 1 B 211 MET VAL MET MET LYS LEU PHE TYR LYS PRO GLY ALA CYS
SEQRES 2 B 211 SER LEU SER PRO HIS ILE VAL LEU ARG GLU ALA GLY LEU
SEQRES 3 B 211 ASP PHE SER ILE GLU ARG VAL ASP LEU VAL THR LYS LYS
SEQRES 4 B 211 THR GLU THR GLY ALA ASP TYR LEU SER ILE ASN PRO LYS
SEQRES 5 B 211 GLY GLN VAL PRO ALA LEU VAL LEU ASP ASP GLY SER LEU
SEQRES 6 B 211 LEU THR GLU GLY VAL ALA ILE VAL GLN TYR LEU ALA ASP
SEQRES 7 B 211 LYS VAL PRO ASP ARG HIS LEU ILE ALA PRO SER GLY THR
SEQRES 8 B 211 LEU SER ARG TYR HIS ALA ILE GLU TRP LEU ASN PHE ILE
SEQRES 9 B 211 ALA THR GLU LEU HIS LYS GLY PHE SER PRO LEU PHE ASN
SEQRES 10 B 211 PRO ASN THR PRO ASP GLU TYR LYS THR ILE VAL ARG GLU
SEQRES 11 B 211 ARG LEU ASP LYS GLN PHE SER TYR VAL ASP SER VAL LEU
SEQRES 12 B 211 ALA GLU HIS ASP TYR LEU LEU GLY LYS LYS PHE SER VAL
SEQRES 13 B 211 ALA ASP ALA TYR LEU PHE THR VAL SER ARG TRP ALA ASN
SEQRES 14 B 211 ALA LEU ASN LEU GLN ILE LYS GLU ARG SER HIS LEU ASP
SEQRES 15 B 211 GLN TYR MET ALA ARG VAL ALA GLU ARG PRO ALA VAL LYS
SEQRES 16 B 211 ALA ALA LEU ALA ALA GLU ASP ILE LYS ALA GLU ASN LEU
SEQRES 17 B 211 TYR PHE GLN
HET GSH A 301 20
HET GOL A 302 6
HET GSH B 301 20
HETNAM GSH GLUTATHIONE
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 GSH 2(C10 H17 N3 O6 S)
FORMUL 4 GOL C3 H8 O3
FORMUL 6 HOH *248(H2 O)
HELIX 1 1 SER A 12 GLY A 23 1 12
HELIX 2 2 ASP A 43 ASN A 48 1 6
HELIX 3 3 GLU A 66 VAL A 78 1 13
HELIX 4 4 PRO A 79 HIS A 82 5 4
HELIX 5 5 THR A 89 LEU A 106 1 18
HELIX 6 6 LEU A 106 ASN A 115 1 10
HELIX 7 7 PRO A 119 ALA A 142 1 24
HELIX 8 8 SER A 153 LEU A 169 1 17
HELIX 9 9 ARG A 176 GLU A 188 1 13
HELIX 10 10 ARG A 189 GLU A 199 1 11
HELIX 11 11 SER B 12 GLY B 23 1 12
HELIX 12 12 ASP B 43 ILE B 47 5 5
HELIX 13 13 GLU B 66 VAL B 78 1 13
HELIX 14 14 PRO B 79 HIS B 82 5 4
HELIX 15 15 THR B 89 LEU B 106 1 18
HELIX 16 16 HIS B 107 ASN B 115 5 9
HELIX 17 17 PRO B 119 ALA B 142 1 24
HELIX 18 18 SER B 153 LEU B 169 1 17
HELIX 19 19 ARG B 176 GLU B 188 1 13
HELIX 20 20 ARG B 189 GLU B 199 1 11
SHEET 1 A 5 LYS A 37 THR A 38 0
SHEET 2 A 5 PHE A 26 ASP A 32 -1 N ASP A 32 O LYS A 37
SHEET 3 A 5 MET A 2 TYR A 6 1 N MET A 2 O SER A 27
SHEET 4 A 5 ALA A 55 VAL A 57 -1 O VAL A 57 N LYS A 3
SHEET 5 A 5 LEU A 63 THR A 65 -1 O LEU A 64 N LEU A 56
SHEET 1 B 5 LYS B 37 THR B 38 0
SHEET 2 B 5 PHE B 26 ASP B 32 -1 N ASP B 32 O LYS B 37
SHEET 3 B 5 MET B 2 TYR B 6 1 N LEU B 4 O GLU B 29
SHEET 4 B 5 ALA B 55 VAL B 57 -1 O ALA B 55 N PHE B 5
SHEET 5 B 5 LEU B 63 THR B 65 -1 O LEU B 64 N LEU B 56
CISPEP 1 VAL A 53 PRO A 54 0 -1.92
CISPEP 2 VAL B 53 PRO B 54 0 -2.90
SITE 1 AC1 15 CYS A 11 LEU A 33 LYS A 36 GLY A 51
SITE 2 AC1 15 GLN A 52 VAL A 53 GLU A 66 GLY A 67
SITE 3 AC1 15 HOH A 409 HOH A 410 HOH A 491 HOH A 516
SITE 4 AC1 15 ASN B 100 THR B 104 GLU B 105
SITE 1 AC2 8 HIS A 82 LEU A 83 ILE A 84 ALA A 85
SITE 2 AC2 8 LYS A 151 PHE A 152 SER A 153 HOH A 412
SITE 1 AC3 18 ASN A 100 THR A 104 GLU A 105 CYS B 11
SITE 2 AC3 18 LEU B 33 LYS B 36 GLN B 52 VAL B 53
SITE 3 AC3 18 GLU B 66 GLY B 67 HIS B 107 TRP B 165
SITE 4 AC3 18 HOH B 404 HOH B 416 HOH B 450 HOH B 463
SITE 5 AC3 18 HOH B 516 HOH B 517
CRYST1 87.945 87.945 148.786 90.00 90.00 90.00 P 41 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 0.011371 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011371 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006721 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
