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HEADER HYDROLASE 28-MAR-23 8S9J
TITLE FPHA, STAPHYLOCOCCUS AUREUS FLUOROPHOSPHONATE-BINDING SERINE
TITLE 2 HYDROLASES A, APO FORM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FLUOROPHOSPHONATE-BINDING SERINE HYDROLASE A;
COMPND 3 CHAIN: A, B, C, D, E, F, G;
COMPND 4 FRAGMENT: N-TERMINAL GPG FROM EXPRESSION TAG;
COMPND 5 EC: 3.1.1.-;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS USA300-CA-263;
SOURCE 3 ORGANISM_TAXID: 1385529;
SOURCE 4 GENE: PNBA, DD547_02485, EP54_14100, EQ90_00535, GO814_08475,
SOURCE 5 GO942_08205, GQX37_11595, NCTC13131_01802, SAGV69_02939,
SOURCE 6 SAHC1335_00445, SAMEA2077334_00038, SAMEA2078260_00273,
SOURCE 7 SAMEA2078588_00580, SAMEA2080344_00347, SAMEA2081063_01648,
SOURCE 8 SAMEA2081470_00272, SAMEA70146418_00277;
SOURCE 9 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 10 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 11 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 12 EXPRESSION_SYSTEM_PLASMID: F1006
KEYWDS FPHA, STAPHYLOCOCCUS AUREUS, S. AUREUS, FLUOROPHOSPHONATE-BINDING,
KEYWDS 2 SERINE HYDROLASES, LIPASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.FELLNER
REVDAT 1 10-APR-24 8S9J 0
JRNL AUTH M.FELLNER
JRNL TITL FPHA, STAPHYLOCOCCUS AUREUS FLUOROPHOSPHONATE-BINDING SERINE
JRNL TITL 2 HYDROLASES A, APO FORM
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.25 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.20.1-4487
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) : 2.25
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.50
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 3 NUMBER OF REFLECTIONS : 212711
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.243
REMARK 3 R VALUE (WORKING SET) : 0.241
REMARK 3 FREE R VALUE : 0.277
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.060
REMARK 3 FREE R VALUE TEST SET COUNT : 10754
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 49.5000 - 6.9700 0.96 6924 353 0.1853 0.2008
REMARK 3 2 6.9700 - 5.5400 0.97 6715 417 0.2138 0.2308
REMARK 3 3 5.5400 - 4.8400 0.97 6750 373 0.1954 0.2536
REMARK 3 4 4.8400 - 4.4000 0.98 6699 398 0.1713 0.2097
REMARK 3 5 4.4000 - 4.0800 0.98 6682 397 0.1780 0.2205
REMARK 3 6 4.0800 - 3.8400 0.98 6772 338 0.1963 0.2306
REMARK 3 7 3.8400 - 3.6500 0.98 6694 370 0.2091 0.2529
REMARK 3 8 3.6500 - 3.4900 0.98 6754 347 0.2213 0.2432
REMARK 3 9 3.4900 - 3.3500 0.98 6717 370 0.2442 0.2877
REMARK 3 10 3.3500 - 3.2400 0.98 6714 350 0.2693 0.3209
REMARK 3 11 3.2400 - 3.1400 0.99 6716 368 0.2653 0.3153
REMARK 3 12 3.1400 - 3.0500 0.99 6764 334 0.2835 0.3043
REMARK 3 13 3.0500 - 2.9700 0.99 6732 341 0.2817 0.3134
REMARK 3 14 2.9700 - 2.9000 0.99 6728 360 0.2932 0.3493
REMARK 3 15 2.9000 - 2.8300 0.99 6750 322 0.3076 0.3720
REMARK 3 16 2.8300 - 2.7700 0.99 6693 398 0.3117 0.3400
REMARK 3 17 2.7700 - 2.7100 0.99 6716 345 0.3124 0.3219
REMARK 3 18 2.7100 - 2.6600 0.99 6722 377 0.3098 0.3430
REMARK 3 19 2.6600 - 2.6200 0.99 6779 326 0.3096 0.3624
REMARK 3 20 2.6200 - 2.5700 0.99 6746 330 0.3085 0.3390
REMARK 3 21 2.5700 - 2.5300 0.99 6758 331 0.3146 0.3630
REMARK 3 22 2.5300 - 2.4900 0.99 6732 357 0.3117 0.3616
REMARK 3 23 2.4900 - 2.4500 0.99 6751 370 0.3192 0.3537
REMARK 3 24 2.4500 - 2.4200 0.99 6701 373 0.3199 0.3764
REMARK 3 25 2.4200 - 2.3900 0.99 6766 341 0.3396 0.4109
REMARK 3 26 2.3900 - 2.3600 0.99 6743 349 0.3321 0.3658
REMARK 3 27 2.3600 - 2.3300 0.99 6773 349 0.3305 0.3589
REMARK 3 28 2.3300 - 2.3000 0.99 6736 371 0.3360 0.3702
REMARK 3 29 2.3000 - 2.2700 0.99 6710 371 0.3392 0.3817
REMARK 3 30 2.2700 - 2.2500 0.96 6520 328 0.3597 0.3909
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
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) : 0.360
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 32.100
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 : 0.008 NULL
REMARK 3 ANGLE : 1.013 35806
REMARK 3 CHIRALITY : 0.055 3826
REMARK 3 PLANARITY : 0.009 4618
REMARK 3 DIHEDRAL : 17.135 9489
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 42
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID -1 THROUGH 49 )
REMARK 3 ORIGIN FOR THE GROUP (A): 59.7471 -83.6408 -25.8103
REMARK 3 T TENSOR
REMARK 3 T11: 0.4273 T22: 0.4186
REMARK 3 T33: 0.8574 T12: -0.1013
REMARK 3 T13: 0.2670 T23: -0.2442
REMARK 3 L TENSOR
REMARK 3 L11: 0.8266 L22: 2.2567
REMARK 3 L33: 1.5989 L12: -0.5571
REMARK 3 L13: 0.6699 L23: -0.9096
REMARK 3 S TENSOR
REMARK 3 S11: 0.0082 S12: -0.1963 S13: -0.0355
REMARK 3 S21: 0.2427 S22: -0.0129 S23: -0.1790
REMARK 3 S31: -0.1583 S32: 0.0748 S33: 0.0069
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 50 THROUGH 78 )
REMARK 3 ORIGIN FOR THE GROUP (A): 44.1728 -72.4550 -29.1315
REMARK 3 T TENSOR
REMARK 3 T11: 0.5593 T22: 0.4646
REMARK 3 T33: 0.9227 T12: -0.0453
REMARK 3 T13: 0.3014 T23: -0.2274
REMARK 3 L TENSOR
REMARK 3 L11: 2.5220 L22: 0.3494
REMARK 3 L33: 0.5852 L12: 0.9408
REMARK 3 L13: 1.2152 L23: 0.4548
REMARK 3 S TENSOR
REMARK 3 S11: -0.1726 S12: -0.5016 S13: 0.3794
REMARK 3 S21: 0.1125 S22: 0.2279 S23: 0.3819
REMARK 3 S31: -0.5453 S32: -0.1073 S33: -0.0476
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 79 THROUGH 285 )
REMARK 3 ORIGIN FOR THE GROUP (A): 55.4598 -74.6750 -40.3404
REMARK 3 T TENSOR
REMARK 3 T11: 0.4608 T22: 0.4000
REMARK 3 T33: 0.9549 T12: -0.1448
REMARK 3 T13: 0.3249 T23: -0.2479
REMARK 3 L TENSOR
REMARK 3 L11: 0.3525 L22: 0.6333
REMARK 3 L33: 0.8242 L12: -0.1156
REMARK 3 L13: 0.2487 L23: 0.0986
REMARK 3 S TENSOR
REMARK 3 S11: 0.0728 S12: -0.0077 S13: 0.1928
REMARK 3 S21: 0.0030 S22: 0.0216 S23: 0.0032
REMARK 3 S31: -0.2963 S32: 0.0979 S33: -0.0892
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 286 THROUGH 314 )
REMARK 3 ORIGIN FOR THE GROUP (A): 40.5254 -74.6989 -51.8077
REMARK 3 T TENSOR
REMARK 3 T11: 0.5313 T22: 0.3676
REMARK 3 T33: 0.8919 T12: -0.1072
REMARK 3 T13: 0.3640 T23: -0.1863
REMARK 3 L TENSOR
REMARK 3 L11: 1.3967 L22: 2.1118
REMARK 3 L33: 1.1693 L12: -1.0024
REMARK 3 L13: 0.2797 L23: 0.0034
REMARK 3 S TENSOR
REMARK 3 S11: 0.1227 S12: 0.0223 S13: 0.1763
REMARK 3 S21: 0.0004 S22: 0.0375 S23: 0.1038
REMARK 3 S31: -0.2818 S32: -0.1129 S33: -0.1572
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 315 THROUGH 363 )
REMARK 3 ORIGIN FOR THE GROUP (A): 41.9992 -68.6128 -59.3538
REMARK 3 T TENSOR
REMARK 3 T11: 0.5538 T22: 0.4171
REMARK 3 T33: 0.8686 T12: -0.1103
REMARK 3 T13: 0.2887 T23: -0.1752
REMARK 3 L TENSOR
REMARK 3 L11: 1.4216 L22: 6.7263
REMARK 3 L33: 0.8430 L12: -2.1907
REMARK 3 L13: 0.1782 L23: -0.1006
REMARK 3 S TENSOR
REMARK 3 S11: 0.2186 S12: 0.0866 S13: 0.5304
REMARK 3 S21: -0.1741 S22: -0.0276 S23: -0.3016
REMARK 3 S31: -0.4106 S32: 0.1248 S33: -0.1827
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 364 THROUGH 450 )
REMARK 3 ORIGIN FOR THE GROUP (A): 35.5128 -86.5371 -47.6337
REMARK 3 T TENSOR
REMARK 3 T11: 0.3981 T22: 0.3224
REMARK 3 T33: 0.8969 T12: -0.0845
REMARK 3 T13: 0.2427 T23: -0.1885
REMARK 3 L TENSOR
REMARK 3 L11: 1.5367 L22: 1.7766
REMARK 3 L33: 1.5729 L12: -0.4762
REMARK 3 L13: -0.1062 L23: -0.1871
REMARK 3 S TENSOR
REMARK 3 S11: -0.0016 S12: 0.1028 S13: -0.3094
REMARK 3 S21: 0.0047 S22: 0.0776 S23: 0.1996
REMARK 3 S31: -0.0811 S32: -0.0503 S33: -0.0790
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESID -1 THROUGH 69 )
REMARK 3 ORIGIN FOR THE GROUP (A): 0.7040 -55.9814 15.2120
REMARK 3 T TENSOR
REMARK 3 T11: 0.7779 T22: 1.0800
REMARK 3 T33: 0.4726 T12: 0.6009
REMARK 3 T13: 0.1480 T23: 0.2118
REMARK 3 L TENSOR
REMARK 3 L11: 2.2234 L22: 1.4798
REMARK 3 L33: 0.2870 L12: -0.5939
REMARK 3 L13: 0.4705 L23: 0.0282
REMARK 3 S TENSOR
REMARK 3 S11: -0.0953 S12: -0.3711 S13: -0.1659
REMARK 3 S21: 0.2682 S22: 0.1554 S23: -0.0561
REMARK 3 S31: 0.0171 S32: -0.0895 S33: -0.0575
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 70 THROUGH 200 )
REMARK 3 ORIGIN FOR THE GROUP (A): 4.5306 -50.9411 7.5320
REMARK 3 T TENSOR
REMARK 3 T11: 0.7591 T22: 0.8892
REMARK 3 T33: 0.4673 T12: 0.6922
REMARK 3 T13: 0.2440 T23: 0.1206
REMARK 3 L TENSOR
REMARK 3 L11: 0.8913 L22: 0.9271
REMARK 3 L33: 0.4395 L12: -0.4642
REMARK 3 L13: -0.2802 L23: 0.4099
REMARK 3 S TENSOR
REMARK 3 S11: -0.1036 S12: -0.3027 S13: 0.0265
REMARK 3 S21: 0.0824 S22: 0.0811 S23: -0.1461
REMARK 3 S31: -0.1455 S32: 0.0437 S33: -0.0062
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 201 THROUGH 241 )
REMARK 3 ORIGIN FOR THE GROUP (A): 15.8466 -38.8831 9.7003
REMARK 3 T TENSOR
REMARK 3 T11: 1.0827 T22: 0.9064
REMARK 3 T33: 0.6224 T12: 0.5605
REMARK 3 T13: 0.0905 T23: 0.0025
REMARK 3 L TENSOR
REMARK 3 L11: 1.1006 L22: 0.9226
REMARK 3 L33: 1.1929 L12: 0.7258
REMARK 3 L13: 0.7431 L23: -0.0743
REMARK 3 S TENSOR
REMARK 3 S11: -0.2555 S12: -0.5178 S13: 0.1575
REMARK 3 S21: 0.1329 S22: 0.0154 S23: -0.0828
REMARK 3 S31: -0.5220 S32: -0.2131 S33: 0.2393
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 242 THROUGH 314 )
REMARK 3 ORIGIN FOR THE GROUP (A): 8.9026 -34.1130 8.2866
REMARK 3 T TENSOR
REMARK 3 T11: 1.0375 T22: 0.8910
REMARK 3 T33: 0.5592 T12: 0.5058
REMARK 3 T13: 0.1413 T23: -0.0318
REMARK 3 L TENSOR
REMARK 3 L11: 1.1243 L22: 0.5884
REMARK 3 L33: 0.5646 L12: -0.1843
REMARK 3 L13: 0.5524 L23: -0.4918
REMARK 3 S TENSOR
REMARK 3 S11: -0.1846 S12: -0.4306 S13: 0.1290
REMARK 3 S21: -0.0191 S22: 0.1397 S23: -0.1927
REMARK 3 S31: -0.5309 S32: -0.1265 S33: 0.0488
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 315 THROUGH 363 )
REMARK 3 ORIGIN FOR THE GROUP (A): 9.6833 -26.4629 -5.0718
REMARK 3 T TENSOR
REMARK 3 T11: 1.3460 T22: 0.8301
REMARK 3 T33: 0.5352 T12: 0.4759
REMARK 3 T13: 0.1456 T23: 0.0084
REMARK 3 L TENSOR
REMARK 3 L11: 0.7775 L22: 3.8347
REMARK 3 L33: 1.3546 L12: -1.3998
REMARK 3 L13: -0.8728 L23: 2.2769
REMARK 3 S TENSOR
REMARK 3 S11: -0.1166 S12: -0.1661 S13: 0.2124
REMARK 3 S21: -0.5167 S22: 0.2063 S23: -0.3818
REMARK 3 S31: -0.3010 S32: 0.0881 S33: -0.0920
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 364 THROUGH 450 )
REMARK 3 ORIGIN FOR THE GROUP (A): -4.7654 -42.7162 -10.3274
REMARK 3 T TENSOR
REMARK 3 T11: 1.0460 T22: 0.7232
REMARK 3 T33: 0.3939 T12: 0.6806
REMARK 3 T13: 0.2078 T23: 0.0395
REMARK 3 L TENSOR
REMARK 3 L11: 1.1216 L22: 1.8606
REMARK 3 L33: 0.7795 L12: -0.7372
REMARK 3 L13: -0.2623 L23: 0.7075
REMARK 3 S TENSOR
REMARK 3 S11: -0.0092 S12: -0.0410 S13: 0.1552
REMARK 3 S21: -0.2587 S22: -0.0032 S23: -0.0849
REMARK 3 S31: -0.2558 S32: -0.1454 S33: -0.0067
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'C' AND (RESID -1 THROUGH 21 )
REMARK 3 ORIGIN FOR THE GROUP (A): 30.2787 -58.2337 -24.5157
REMARK 3 T TENSOR
REMARK 3 T11: 1.1143 T22: 0.3823
REMARK 3 T33: 0.8088 T12: 0.0500
REMARK 3 T13: 0.4269 T23: -0.0512
REMARK 3 L TENSOR
REMARK 3 L11: 2.2193 L22: 0.1423
REMARK 3 L33: 1.5777 L12: 0.0574
REMARK 3 L13: 0.9284 L23: -0.3857
REMARK 3 S TENSOR
REMARK 3 S11: -0.1010 S12: 0.2405 S13: -0.0701
REMARK 3 S21: -0.7159 S22: 0.2297 S23: -0.6478
REMARK 3 S31: -0.7757 S32: 0.1318 S33: -0.1380
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 22 THROUGH 49 )
REMARK 3 ORIGIN FOR THE GROUP (A): 39.2205 -58.7688 -6.8720
REMARK 3 T TENSOR
REMARK 3 T11: 0.7464 T22: 0.4527
REMARK 3 T33: 0.9734 T12: 0.1203
REMARK 3 T13: 0.3111 T23: -0.1116
REMARK 3 L TENSOR
REMARK 3 L11: 2.0499 L22: 0.3464
REMARK 3 L33: 4.3181 L12: -0.3592
REMARK 3 L13: 0.5182 L23: 0.9988
REMARK 3 S TENSOR
REMARK 3 S11: -0.2738 S12: -0.2594 S13: 0.2098
REMARK 3 S21: -0.2286 S22: 0.3318 S23: -0.5857
REMARK 3 S31: -0.6169 S32: 0.1111 S33: -0.0768
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 50 THROUGH 78 )
REMARK 3 ORIGIN FOR THE GROUP (A): 40.6514 -77.1446 -16.7610
REMARK 3 T TENSOR
REMARK 3 T11: 0.5776 T22: 0.4747
REMARK 3 T33: 1.1264 T12: 0.0395
REMARK 3 T13: 0.3118 T23: -0.1454
REMARK 3 L TENSOR
REMARK 3 L11: 1.4977 L22: 0.9628
REMARK 3 L33: 1.3343 L12: -0.1831
REMARK 3 L13: -0.0992 L23: 1.1311
REMARK 3 S TENSOR
REMARK 3 S11: 0.0279 S12: -0.0125 S13: -0.4561
REMARK 3 S21: -0.3226 S22: 0.3384 S23: -0.6084
REMARK 3 S31: -0.0038 S32: 0.3702 S33: -0.3679
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 79 THROUGH 200 )
REMARK 3 ORIGIN FOR THE GROUP (A): 29.6594 -68.9656 -8.8530
REMARK 3 T TENSOR
REMARK 3 T11: 0.5664 T22: 0.4096
REMARK 3 T33: 0.8319 T12: 0.1736
REMARK 3 T13: 0.3289 T23: 0.0670
REMARK 3 L TENSOR
REMARK 3 L11: 1.2553 L22: 1.2526
REMARK 3 L33: 1.6626 L12: -0.3813
REMARK 3 L13: 0.3106 L23: 0.8486
REMARK 3 S TENSOR
REMARK 3 S11: -0.1756 S12: -0.2297 S13: -0.1962
REMARK 3 S21: -0.1059 S22: 0.2828 S23: -0.4077
REMARK 3 S31: -0.3302 S32: -0.0398 S33: -0.1147
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 201 THROUGH 285 )
REMARK 3 ORIGIN FOR THE GROUP (A): 38.8537 -77.2266 4.5060
REMARK 3 T TENSOR
REMARK 3 T11: 0.6126 T22: 0.5857
REMARK 3 T33: 1.0422 T12: 0.2591
REMARK 3 T13: 0.1665 T23: 0.1445
REMARK 3 L TENSOR
REMARK 3 L11: 0.9773 L22: 0.8361
REMARK 3 L33: 1.3454 L12: 0.8098
REMARK 3 L13: 0.8670 L23: 0.4009
REMARK 3 S TENSOR
REMARK 3 S11: 0.0186 S12: -0.2678 S13: -0.5482
REMARK 3 S21: 0.2133 S22: 0.1787 S23: -0.6684
REMARK 3 S31: 0.0654 S32: 0.0397 S33: -0.1973
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 286 THROUGH 314 )
REMARK 3 ORIGIN FOR THE GROUP (A): 24.1573 -88.5112 -4.8107
REMARK 3 T TENSOR
REMARK 3 T11: 0.4834 T22: 0.5980
REMARK 3 T33: 0.9588 T12: 0.1735
REMARK 3 T13: 0.2690 T23: 0.2587
REMARK 3 L TENSOR
REMARK 3 L11: 1.1830 L22: 3.0636
REMARK 3 L33: 2.7149 L12: -0.4929
REMARK 3 L13: 1.2511 L23: 0.8750
REMARK 3 S TENSOR
REMARK 3 S11: -0.0866 S12: -0.5011 S13: -0.5457
REMARK 3 S21: 0.3396 S22: 0.3554 S23: -0.2775
REMARK 3 S31: 0.1955 S32: 0.0655 S33: -0.2702
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 315 THROUGH 363 )
REMARK 3 ORIGIN FOR THE GROUP (A): 24.6858 -93.5751 3.5313
REMARK 3 T TENSOR
REMARK 3 T11: 0.5972 T22: 0.8886
REMARK 3 T33: 1.1062 T12: 0.2260
REMARK 3 T13: 0.0886 T23: 0.3942
REMARK 3 L TENSOR
REMARK 3 L11: 1.7070 L22: 4.3529
REMARK 3 L33: 2.6770 L12: -1.6330
REMARK 3 L13: 0.4466 L23: 1.2090
REMARK 3 S TENSOR
REMARK 3 S11: -0.3251 S12: -0.9674 S13: -0.7402
REMARK 3 S21: 0.9147 S22: 0.6612 S23: -0.4310
REMARK 3 S31: 0.4734 S32: 0.0655 S33: -0.3383
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 364 THROUGH 450 )
REMARK 3 ORIGIN FOR THE GROUP (A): 17.2857 -85.9174 -15.8646
REMARK 3 T TENSOR
REMARK 3 T11: 0.4353 T22: 0.4395
REMARK 3 T33: 0.9024 T12: 0.1405
REMARK 3 T13: 0.2630 T23: 0.2078
REMARK 3 L TENSOR
REMARK 3 L11: 2.3137 L22: 1.8096
REMARK 3 L33: 2.1581 L12: -1.2615
REMARK 3 L13: -0.2012 L23: 1.2992
REMARK 3 S TENSOR
REMARK 3 S11: 0.0299 S12: -0.2418 S13: -0.4992
REMARK 3 S21: -0.0862 S22: 0.1953 S23: -0.1506
REMARK 3 S31: -0.0900 S32: -0.2623 S33: -0.2101
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 0 THROUGH 241 )
REMARK 3 ORIGIN FOR THE GROUP (A): -11.4103 -90.1580 -41.6202
REMARK 3 T TENSOR
REMARK 3 T11: 0.5423 T22: 0.5567
REMARK 3 T33: 0.5863 T12: 0.2293
REMARK 3 T13: 0.2574 T23: 0.1516
REMARK 3 L TENSOR
REMARK 3 L11: 3.1241 L22: 1.7413
REMARK 3 L33: 1.9691 L12: 0.3079
REMARK 3 L13: 0.5742 L23: 1.3165
REMARK 3 S TENSOR
REMARK 3 S11: -0.0179 S12: -0.1694 S13: -0.5225
REMARK 3 S21: -0.3961 S22: 0.0640 S23: -0.0888
REMARK 3 S31: -0.5527 S32: -0.6110 S33: -0.0402
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 242 THROUGH 324 )
REMARK 3 ORIGIN FOR THE GROUP (A): -21.1559 -96.9139 -27.3011
REMARK 3 T TENSOR
REMARK 3 T11: 0.4233 T22: 1.0021
REMARK 3 T33: 0.7480 T12: 0.1794
REMARK 3 T13: 0.1624 T23: 0.2517
REMARK 3 L TENSOR
REMARK 3 L11: 1.0668 L22: 1.0906
REMARK 3 L33: 1.9704 L12: 1.0761
REMARK 3 L13: 0.4175 L23: 0.4279
REMARK 3 S TENSOR
REMARK 3 S11: -0.0176 S12: -0.5486 S13: -0.5091
REMARK 3 S21: 0.0198 S22: -0.0973 S23: 0.0378
REMARK 3 S31: -0.0255 S32: -0.9456 S33: 0.1298
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 325 THROUGH 450 )
REMARK 3 ORIGIN FOR THE GROUP (A): -3.7631 -90.0114 -19.0975
REMARK 3 T TENSOR
REMARK 3 T11: 0.4068 T22: 0.7487
REMARK 3 T33: 0.6844 T12: 0.1840
REMARK 3 T13: 0.1846 T23: 0.3108
REMARK 3 L TENSOR
REMARK 3 L11: 2.3724 L22: 1.8361
REMARK 3 L33: 1.5504 L12: 0.1892
REMARK 3 L13: -0.5172 L23: 1.2399
REMARK 3 S TENSOR
REMARK 3 S11: 0.0926 S12: -0.5576 S13: -0.5503
REMARK 3 S21: -0.0070 S22: -0.0454 S23: -0.2966
REMARK 3 S31: -0.0718 S32: -0.5219 S33: -0.0333
REMARK 3 TLS GROUP : 24
REMARK 3 SELECTION: CHAIN 'E' AND (RESID -1 THROUGH 200 )
REMARK 3 ORIGIN FOR THE GROUP (A): 14.6544-118.2462 -47.0123
REMARK 3 T TENSOR
REMARK 3 T11: 0.3505 T22: 0.4116
REMARK 3 T33: 1.7293 T12: -0.0839
REMARK 3 T13: 0.3901 T23: -0.2613
REMARK 3 L TENSOR
REMARK 3 L11: 0.5736 L22: 0.4530
REMARK 3 L33: 0.2342 L12: -0.2425
REMARK 3 L13: -0.1749 L23: 0.0940
REMARK 3 S TENSOR
REMARK 3 S11: -0.1306 S12: 0.1023 S13: -0.7640
REMARK 3 S21: -0.0419 S22: 0.0162 S23: 0.2806
REMARK 3 S31: 0.3045 S32: -0.1859 S33: 0.1562
REMARK 3 TLS GROUP : 25
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 201 THROUGH 239 )
REMARK 3 ORIGIN FOR THE GROUP (A): 7.3502-113.4881 -62.6898
REMARK 3 T TENSOR
REMARK 3 T11: 0.5448 T22: 0.8028
REMARK 3 T33: 1.5649 T12: -0.1221
REMARK 3 T13: 0.2187 T23: -0.5195
REMARK 3 L TENSOR
REMARK 3 L11: 0.0414 L22: 0.4928
REMARK 3 L33: 0.4930 L12: -0.1414
REMARK 3 L13: 0.1414 L23: -0.4922
REMARK 3 S TENSOR
REMARK 3 S11: -0.0131 S12: 0.7202 S13: -0.7334
REMARK 3 S21: -0.2141 S22: -0.0636 S23: 0.3167
REMARK 3 S31: 0.4080 S32: -0.3617 S33: 0.0924
REMARK 3 TLS GROUP : 26
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 240 THROUGH 285 )
REMARK 3 ORIGIN FOR THE GROUP (A): 9.6160-124.5826 -67.6503
REMARK 3 T TENSOR
REMARK 3 T11: 0.7805 T22: 0.8678
REMARK 3 T33: 1.7336 T12: -0.2254
REMARK 3 T13: 0.2630 T23: -0.5642
REMARK 3 L TENSOR
REMARK 3 L11: 0.3811 L22: 1.4436
REMARK 3 L33: 0.3758 L12: 0.6496
REMARK 3 L13: 0.0479 L23: -0.2662
REMARK 3 S TENSOR
REMARK 3 S11: -0.3144 S12: 0.2798 S13: -0.4802
REMARK 3 S21: -0.3931 S22: 0.1716 S23: 0.1980
REMARK 3 S31: 0.3355 S32: -0.1245 S33: 0.1207
REMARK 3 TLS GROUP : 27
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 286 THROUGH 314 )
REMARK 3 ORIGIN FOR THE GROUP (A): 24.0202-106.4979 -65.2359
REMARK 3 T TENSOR
REMARK 3 T11: 0.4317 T22: 0.4463
REMARK 3 T33: 1.1493 T12: -0.0590
REMARK 3 T13: 0.1601 T23: -0.2845
REMARK 3 L TENSOR
REMARK 3 L11: 2.3928 L22: 2.6977
REMARK 3 L33: 2.2628 L12: -1.9773
REMARK 3 L13: -1.0003 L23: 0.5428
REMARK 3 S TENSOR
REMARK 3 S11: 0.1452 S12: 0.3668 S13: -0.3495
REMARK 3 S21: -0.4346 S22: -0.1381 S23: 0.3042
REMARK 3 S31: 0.0241 S32: -0.1191 S33: -0.0024
REMARK 3 TLS GROUP : 28
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 315 THROUGH 336 )
REMARK 3 ORIGIN FOR THE GROUP (A): 21.6224-109.8455 -81.2521
REMARK 3 T TENSOR
REMARK 3 T11: 0.8115 T22: 0.6750
REMARK 3 T33: 1.1385 T12: 0.0608
REMARK 3 T13: -0.0027 T23: -0.3317
REMARK 3 L TENSOR
REMARK 3 L11: 0.9616 L22: 4.4376
REMARK 3 L33: 2.4763 L12: -1.5308
REMARK 3 L13: 0.8600 L23: 0.4797
REMARK 3 S TENSOR
REMARK 3 S11: 0.2187 S12: 0.6658 S13: -1.0449
REMARK 3 S21: -0.7698 S22: -0.4635 S23: 0.8499
REMARK 3 S31: 0.5790 S32: -0.3008 S33: 0.2419
REMARK 3 TLS GROUP : 29
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 337 THROUGH 363 )
REMARK 3 ORIGIN FOR THE GROUP (A): 21.3911-100.7043 -68.7473
REMARK 3 T TENSOR
REMARK 3 T11: 0.6085 T22: 0.4992
REMARK 3 T33: 1.1104 T12: -0.0579
REMARK 3 T13: 0.0535 T23: -0.3107
REMARK 3 L TENSOR
REMARK 3 L11: 3.1506 L22: 4.3384
REMARK 3 L33: 2.3009 L12: -3.5215
REMARK 3 L13: -2.3372 L23: 2.2840
REMARK 3 S TENSOR
REMARK 3 S11: -0.0877 S12: 0.3228 S13: -0.3993
REMARK 3 S21: -0.2571 S22: -0.0667 S23: 0.7090
REMARK 3 S31: 0.1035 S32: -0.0319 S33: 0.1516
REMARK 3 TLS GROUP : 30
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 364 THROUGH 450 )
REMARK 3 ORIGIN FOR THE GROUP (A): 31.1510-102.5789 -54.4866
REMARK 3 T TENSOR
REMARK 3 T11: 0.3840 T22: 0.3844
REMARK 3 T33: 1.0620 T12: -0.0801
REMARK 3 T13: 0.2518 T23: -0.2535
REMARK 3 L TENSOR
REMARK 3 L11: 1.4536 L22: 1.4856
REMARK 3 L33: 1.7192 L12: -0.7826
REMARK 3 L13: 0.3243 L23: 0.0840
REMARK 3 S TENSOR
REMARK 3 S11: -0.0299 S12: 0.0780 S13: -0.0380
REMARK 3 S21: -0.0764 S22: 0.0269 S23: 0.0676
REMARK 3 S31: -0.1231 S32: 0.1651 S33: -0.0093
REMARK 3 TLS GROUP : 31
REMARK 3 SELECTION: CHAIN 'F' AND (RESID -1 THROUGH 49 )
REMARK 3 ORIGIN FOR THE GROUP (A): -19.9058 -36.6046 29.9016
REMARK 3 T TENSOR
REMARK 3 T11: 0.8133 T22: 1.3412
REMARK 3 T33: 0.4566 T12: 0.6763
REMARK 3 T13: 0.0262 T23: 0.0274
REMARK 3 L TENSOR
REMARK 3 L11: 0.3639 L22: 0.9415
REMARK 3 L33: 1.3535 L12: 0.3086
REMARK 3 L13: -0.5595 L23: -0.6510
REMARK 3 S TENSOR
REMARK 3 S11: 0.0447 S12: -0.1831 S13: 0.0784
REMARK 3 S21: -0.0247 S22: -0.0746 S23: -0.1670
REMARK 3 S31: -0.1558 S32: 0.0632 S33: 0.0585
REMARK 3 TLS GROUP : 32
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 50 THROUGH 209 )
REMARK 3 ORIGIN FOR THE GROUP (A): -28.0126 -44.9153 24.0116
REMARK 3 T TENSOR
REMARK 3 T11: 0.7187 T22: 1.2751
REMARK 3 T33: 0.4254 T12: 1.1664
REMARK 3 T13: 0.1647 T23: 0.0702
REMARK 3 L TENSOR
REMARK 3 L11: 0.3823 L22: 0.1504
REMARK 3 L33: 0.2353 L12: -0.0721
REMARK 3 L13: -0.0089 L23: -0.0374
REMARK 3 S TENSOR
REMARK 3 S11: 0.0093 S12: -0.2741 S13: -0.1747
REMARK 3 S21: 0.0237 S22: -0.0459 S23: -0.0405
REMARK 3 S31: 0.1708 S32: 0.0266 S33: 0.0628
REMARK 3 TLS GROUP : 33
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 210 THROUGH 241 )
REMARK 3 ORIGIN FOR THE GROUP (A): -33.5293 -63.3581 32.6610
REMARK 3 T TENSOR
REMARK 3 T11: 1.2160 T22: 1.5333
REMARK 3 T33: 0.6701 T12: 0.7294
REMARK 3 T13: 0.1097 T23: 0.2392
REMARK 3 L TENSOR
REMARK 3 L11: 1.1951 L22: 0.4973
REMARK 3 L33: 0.8068 L12: 0.3912
REMARK 3 L13: 0.9059 L23: 0.0754
REMARK 3 S TENSOR
REMARK 3 S11: 0.0923 S12: -0.3453 S13: -0.5111
REMARK 3 S21: 0.2024 S22: 0.0279 S23: -0.1088
REMARK 3 S31: 0.4432 S32: -0.1149 S33: -0.1339
REMARK 3 TLS GROUP : 34
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 242 THROUGH 314 )
REMARK 3 ORIGIN FOR THE GROUP (A): -32.7750 -61.0357 25.0604
REMARK 3 T TENSOR
REMARK 3 T11: 1.0972 T22: 1.4507
REMARK 3 T33: 0.6638 T12: 0.7383
REMARK 3 T13: 0.1964 T23: 0.3064
REMARK 3 L TENSOR
REMARK 3 L11: 0.8509 L22: 0.2653
REMARK 3 L33: 1.0075 L12: -0.2985
REMARK 3 L13: 0.9050 L23: -0.3977
REMARK 3 S TENSOR
REMARK 3 S11: 0.0543 S12: -0.2844 S13: -0.3355
REMARK 3 S21: -0.0917 S22: -0.1166 S23: -0.0076
REMARK 3 S31: 0.4430 S32: 0.0103 S33: 0.0321
REMARK 3 TLS GROUP : 35
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 315 THROUGH 363 )
REMARK 3 ORIGIN FOR THE GROUP (A): -45.0656 -64.2289 16.0316
REMARK 3 T TENSOR
REMARK 3 T11: 1.4234 T22: 1.2340
REMARK 3 T33: 0.7618 T12: 0.5979
REMARK 3 T13: 0.2601 T23: 0.2899
REMARK 3 L TENSOR
REMARK 3 L11: 2.1552 L22: 1.0618
REMARK 3 L33: 2.8843 L12: 0.3600
REMARK 3 L13: 1.5192 L23: -1.0925
REMARK 3 S TENSOR
REMARK 3 S11: -0.6346 S12: -0.9725 S13: -0.8344
REMARK 3 S21: 0.6835 S22: 0.3316 S23: -0.0784
REMARK 3 S31: 1.2777 S32: 0.1847 S33: 0.2904
REMARK 3 TLS GROUP : 36
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 364 THROUGH 450 )
REMARK 3 ORIGIN FOR THE GROUP (A): -37.5262 -48.0370 4.7548
REMARK 3 T TENSOR
REMARK 3 T11: 0.9470 T22: 1.0031
REMARK 3 T33: 0.4587 T12: 0.7803
REMARK 3 T13: 0.0003 T23: 0.1261
REMARK 3 L TENSOR
REMARK 3 L11: 1.0097 L22: 1.0510
REMARK 3 L33: 0.7477 L12: -0.7373
REMARK 3 L13: -0.0529 L23: -0.1010
REMARK 3 S TENSOR
REMARK 3 S11: -0.0275 S12: -0.0660 S13: -0.2440
REMARK 3 S21: -0.1679 S22: -0.0320 S23: 0.2394
REMARK 3 S31: 0.0548 S32: -0.1224 S33: 0.0235
REMARK 3 TLS GROUP : 37
REMARK 3 SELECTION: CHAIN 'G' AND (RESID -1 THROUGH 200 )
REMARK 3 ORIGIN FOR THE GROUP (A): -25.8010 -58.3234 -37.7762
REMARK 3 T TENSOR
REMARK 3 T11: 1.3356 T22: 0.9362
REMARK 3 T33: 0.5427 T12: 0.8021
REMARK 3 T13: -0.0304 T23: -0.1056
REMARK 3 L TENSOR
REMARK 3 L11: 0.4570 L22: 0.4895
REMARK 3 L33: 0.0382 L12: -0.1485
REMARK 3 L13: -0.0590 L23: 0.1198
REMARK 3 S TENSOR
REMARK 3 S11: 0.1610 S12: 0.3752 S13: -0.2861
REMARK 3 S21: -0.5638 S22: -0.1956 S23: 0.1773
REMARK 3 S31: -0.0949 S32: -0.3426 S33: 0.0547
REMARK 3 TLS GROUP : 38
REMARK 3 SELECTION: CHAIN 'G' AND (RESID 201 THROUGH 241 )
REMARK 3 ORIGIN FOR THE GROUP (A): -21.6397 -45.6417 -50.3826
REMARK 3 T TENSOR
REMARK 3 T11: 1.5584 T22: 1.1509
REMARK 3 T33: 0.5616 T12: 0.7065
REMARK 3 T13: 0.1423 T23: 0.0885
REMARK 3 L TENSOR
REMARK 3 L11: 0.9944 L22: 0.4369
REMARK 3 L33: 0.0360 L12: 0.6589
REMARK 3 L13: 0.1883 L23: 0.1241
REMARK 3 S TENSOR
REMARK 3 S11: -0.0748 S12: 0.5382 S13: -0.0533
REMARK 3 S21: -0.5708 S22: 0.0265 S23: -0.0562
REMARK 3 S31: -0.1068 S32: -0.0359 S33: 0.0281
REMARK 3 TLS GROUP : 39
REMARK 3 SELECTION: CHAIN 'G' AND (RESID 242 THROUGH 285 )
REMARK 3 ORIGIN FOR THE GROUP (A): -18.4716 -50.8775 -57.0616
REMARK 3 T TENSOR
REMARK 3 T11: 1.7254 T22: 1.2304
REMARK 3 T33: 0.5662 T12: 0.7157
REMARK 3 T13: 0.1096 T23: 0.0062
REMARK 3 L TENSOR
REMARK 3 L11: 0.6275 L22: 0.5889
REMARK 3 L33: 1.2561 L12: 0.4523
REMARK 3 L13: 0.1145 L23: 0.3959
REMARK 3 S TENSOR
REMARK 3 S11: -0.0540 S12: 0.3625 S13: -0.0830
REMARK 3 S21: -0.3865 S22: 0.0694 S23: -0.0395
REMARK 3 S31: -0.2909 S32: -0.0149 S33: -0.0158
REMARK 3 TLS GROUP : 40
REMARK 3 SELECTION: CHAIN 'G' AND (RESID 286 THROUGH 336 )
REMARK 3 ORIGIN FOR THE GROUP (A): -3.5561 -42.8502 -45.4143
REMARK 3 T TENSOR
REMARK 3 T11: 1.6471 T22: 0.8727
REMARK 3 T33: 0.6134 T12: 0.5108
REMARK 3 T13: 0.3408 T23: 0.1331
REMARK 3 L TENSOR
REMARK 3 L11: 0.2008 L22: 0.2149
REMARK 3 L33: 0.9107 L12: 0.2069
REMARK 3 L13: 0.4287 L23: 0.4377
REMARK 3 S TENSOR
REMARK 3 S11: 0.1358 S12: 0.4969 S13: 0.3113
REMARK 3 S21: -0.6655 S22: -0.0785 S23: -0.2972
REMARK 3 S31: -0.5865 S32: 0.0066 S33: -0.0775
REMARK 3 TLS GROUP : 41
REMARK 3 SELECTION: CHAIN 'G' AND (RESID 337 THROUGH 411 )
REMARK 3 ORIGIN FOR THE GROUP (A): -4.6363 -48.0344 -33.6530
REMARK 3 T TENSOR
REMARK 3 T11: 1.3450 T22: 0.7650
REMARK 3 T33: 0.4595 T12: 0.6044
REMARK 3 T13: 0.2907 T23: 0.0826
REMARK 3 L TENSOR
REMARK 3 L11: 0.5652 L22: 1.0123
REMARK 3 L33: 0.2356 L12: -0.6819
REMARK 3 L13: -0.0516 L23: 0.2594
REMARK 3 S TENSOR
REMARK 3 S11: 0.1941 S12: 0.2468 S13: 0.2165
REMARK 3 S21: -0.6788 S22: -0.2266 S23: -0.3155
REMARK 3 S31: -0.4875 S32: -0.0855 S33: 0.0099
REMARK 3 TLS GROUP : 42
REMARK 3 SELECTION: CHAIN 'G' AND (RESID 412 THROUGH 450 )
REMARK 3 ORIGIN FOR THE GROUP (A): -8.9430 -45.4431 -22.2403
REMARK 3 T TENSOR
REMARK 3 T11: 1.1077 T22: 0.7341
REMARK 3 T33: 0.3982 T12: 0.5580
REMARK 3 T13: 0.1719 T23: 0.0927
REMARK 3 L TENSOR
REMARK 3 L11: 1.4938 L22: 1.7713
REMARK 3 L33: 1.2087 L12: -0.9589
REMARK 3 L13: -0.5683 L23: 0.3944
REMARK 3 S TENSOR
REMARK 3 S11: 0.0781 S12: -0.0193 S13: 0.1080
REMARK 3 S21: -0.2317 S22: -0.0857 S23: -0.1441
REMARK 3 S31: -0.3018 S32: -0.0678 S33: -0.0000
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 8S9J COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-MAR-23.
REMARK 100 THE DEPOSITION ID IS D_1000273255.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-FEB-23
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9537
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS 20220220
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.7.8
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 212752
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.250
REMARK 200 RESOLUTION RANGE LOW (A) : 49.500
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 200 DATA REDUNDANCY : 7.800
REMARK 200 R MERGE (I) : 0.12200
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 11.0000
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) : 2.28
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : 7.40
REMARK 200 R MERGE FOR SHELL (I) : 1.43500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.8.3
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.45
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.11
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2UL 7.1 MG/ML FPHA (10MM HEPES PH 7.5,
REMARK 280 100MM NACL) WERE MIXED WITH 1UL OF RESERVOIR SOLUTION. SITTING
REMARK 280 DROP RESERVOIR CONTAINED 30UL OF 1.35M AMMONIUM SULFATE, 0.09M
REMARK 280 SODIUM ACETATE PH 4.6, 4% V/V ACETONE. CRYSTAL APPEARED AFTER 30
REMARK 280 DAYS AT 16C AND GREW LARGER FOR ANOTHER 2 MONTHS WHEN IT WAS
REMARK 280 FROZEN IN A SOLUTION OF ~25% GLYCEROL, 75% RESERVOIR., VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 289.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 41 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 3555 -Y,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X,Z+3/4
REMARK 290 5555 -X+1/2,Y,-Z+3/4
REMARK 290 6555 X,-Y+1/2,-Z+1/4
REMARK 290 7555 Y+1/2,X+1/2,-Z+1/2
REMARK 290 8555 -Y,-X,-Z
REMARK 290 9555 X+1/2,Y+1/2,Z+1/2
REMARK 290 10555 -X,-Y,Z
REMARK 290 11555 -Y+1/2,X,Z+3/4
REMARK 290 12555 Y,-X+1/2,Z+1/4
REMARK 290 13555 -X,Y+1/2,-Z+1/4
REMARK 290 14555 X+1/2,-Y,-Z+3/4
REMARK 290 15555 Y,X,-Z
REMARK 290 16555 -Y+1/2,-X+1/2,-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 156.52100
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 156.52100
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 92.83600
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 156.52100
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 46.41800
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 156.52100
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 139.25400
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 156.52100
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 139.25400
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 156.52100
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 46.41800
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 156.52100
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 156.52100
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 92.83600
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 0.00000
REMARK 290 SMTRY1 9 1.000000 0.000000 0.000000 156.52100
REMARK 290 SMTRY2 9 0.000000 1.000000 0.000000 156.52100
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 92.83600
REMARK 290 SMTRY1 10 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 11 0.000000 -1.000000 0.000000 156.52100
REMARK 290 SMTRY2 11 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 1.000000 139.25400
REMARK 290 SMTRY1 12 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 12 -1.000000 0.000000 0.000000 156.52100
REMARK 290 SMTRY3 12 0.000000 0.000000 1.000000 46.41800
REMARK 290 SMTRY1 13 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 156.52100
REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 46.41800
REMARK 290 SMTRY1 14 1.000000 0.000000 0.000000 156.52100
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 139.25400
REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 15 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 156.52100
REMARK 290 SMTRY2 16 -1.000000 0.000000 0.000000 156.52100
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 92.83600
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6, 7
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 5
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E
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: 6
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350
REMARK 350 BIOMOLECULE: 7
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 616 LIES ON A SPECIAL POSITION.
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 GLY A -2
REMARK 465 GLY B -2
REMARK 465 GLY C -2
REMARK 465 GLY D -2
REMARK 465 PRO D -1
REMARK 465 GLY E -2
REMARK 465 GLY F -2
REMARK 465 GLY G -2
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 GLN B 15 CG CD OE1 NE2
REMARK 470 PHE B 36 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG B 227 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 442 CG CD OE1 OE2
REMARK 470 ASP C 203 CG OD1 OD2
REMARK 470 ASP C 281 CG OD1 OD2
REMARK 470 GLN C 310 CG CD OE1 NE2
REMARK 470 LYS C 312 CG CD CE NZ
REMARK 470 LYS C 330 CG CD CE NZ
REMARK 470 GLN C 335 CG CD OE1 NE2
REMARK 470 GLN D 15 CG CD OE1 NE2
REMARK 470 LYS D 64 CG CD CE NZ
REMARK 470 GLU D 224 CG CD OE1 OE2
REMARK 470 ARG D 227 CG CD NE CZ NH1 NH2
REMARK 470 GLN D 231 CG CD OE1 NE2
REMARK 470 SER D 248 OG
REMARK 470 GLN D 355 CG CD OE1 NE2
REMARK 470 HIS E 11 CG ND1 CD2 CE1 NE2
REMARK 470 ASP E 33 CG OD1 OD2
REMARK 470 PHE E 36 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU E 47 CG CD OE1 OE2
REMARK 470 ASN E 150 CG OD1 ND2
REMARK 470 LYS E 151 CG CD CE NZ
REMARK 470 ARG E 227 CG CD NE CZ NH1 NH2
REMARK 470 GLN E 231 CG CD OE1 NE2
REMARK 470 HIS E 232 CG ND1 CD2 CE1 NE2
REMARK 470 LYS E 235 CG CD CE NZ
REMARK 470 MET E 236 CG SD CE
REMARK 470 LEU E 238 CG CD1 CD2
REMARK 470 ASP E 239 CG OD1 OD2
REMARK 470 LEU E 241 CG CD1 CD2
REMARK 470 ASP E 242 CG OD1 OD2
REMARK 470 THR E 243 OG1 CG2
REMARK 470 ASP E 244 CG OD1 OD2
REMARK 470 SER E 248 OG
REMARK 470 ASP E 253 CG OD1 OD2
REMARK 470 LYS E 262 CG CD CE NZ
REMARK 470 ARG E 265 CG CD NE CZ NH1 NH2
REMARK 470 TYR E 275 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLN E 284 CG CD OE1 NE2
REMARK 470 GLN E 310 CG CD OE1 NE2
REMARK 470 LYS E 311 CG CD CE NZ
REMARK 470 TYR E 331 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLN E 359 CG CD OE1 NE2
REMARK 470 ASP F 67 CG OD1 OD2
REMARK 470 TRP F 146 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP F 146 CZ3 CH2
REMARK 470 SER F 264 OG
REMARK 470 TYR F 275 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ILE F 306 CG1 CG2 CD1
REMARK 470 THR F 307 OG1 CG2
REMARK 470 SER F 308 OG
REMARK 470 GLN F 310 CG CD OE1 NE2
REMARK 470 LYS F 312 CG CD CE NZ
REMARK 470 LEU F 313 CG CD1 CD2
REMARK 470 SER F 314 OG
REMARK 470 PRO F 315 CG CD
REMARK 470 GLN F 316 CG CD OE1 NE2
REMARK 470 ARG F 317 CG CD NE CZ NH1 NH2
REMARK 470 ILE F 319 CG1 CG2 CD1
REMARK 470 ASP F 320 CG OD1 OD2
REMARK 470 ASP F 326 CG OD1 OD2
REMARK 470 LEU F 329 CG CD1 CD2
REMARK 470 LYS F 330 CG CD CE NZ
REMARK 470 TYR F 331 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU F 332 CG CD OE1 OE2
REMARK 470 ASP F 333 CG OD1 OD2
REMARK 470 VAL F 334 CG1 CG2
REMARK 470 GLN F 335 CG CD OE1 NE2
REMARK 470 THR F 336 OG1 CG2
REMARK 470 LYS F 338 CG CD CE NZ
REMARK 470 GLN F 339 CG CD OE1 NE2
REMARK 470 GLN F 340 CG CD OE1 NE2
REMARK 470 GLN F 351 CG CD OE1 NE2
REMARK 470 GLN F 407 CG CD OE1 NE2
REMARK 470 LYS F 430 CG CD CE NZ
REMARK 470 ASP G 33 CG OD1 OD2
REMARK 470 LYS G 37 CG CD CE NZ
REMARK 470 GLU G 80 CG CD OE1 OE2
REMARK 470 GLN G 119 CG CD OE1 NE2
REMARK 470 LYS G 151 CG CD CE NZ
REMARK 470 ARG G 219 CG CD NE CZ NH1 NH2
REMARK 470 LEU G 223 CG CD1 CD2
REMARK 470 GLU G 224 CG CD OE1 OE2
REMARK 470 ARG G 227 CG CD NE CZ NH1 NH2
REMARK 470 GLN G 231 CG CD OE1 NE2
REMARK 470 MET G 236 CG SD CE
REMARK 470 ASP G 244 CG OD1 OD2
REMARK 470 ASP G 245 CG OD1 OD2
REMARK 470 VAL G 246 CG1 CG2
REMARK 470 THR G 251 OG1 CG2
REMARK 470 SER G 264 OG
REMARK 470 SER G 268 OG
REMARK 470 GLN G 310 CG CD OE1 NE2
REMARK 470 LEU G 324 CG CD1 CD2
REMARK 470 LYS G 330 CG CD CE NZ
REMARK 470 GLU G 332 CG CD OE1 OE2
REMARK 470 GLN G 335 CG CD OE1 NE2
REMARK 470 LYS G 354 CG CD CE NZ
REMARK 470 GLU G 442 CG CD OE1 OE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH D 616 O HOH D 664 2.10
REMARK 500 O HOH A 714 O HOH A 721 2.11
REMARK 500 O ALA G 190 OG SER G 194 2.12
REMARK 500 O HOH F 613 O HOH F 630 2.14
REMARK 500 O HOH A 601 O HOH A 602 2.17
REMARK 500 O HOH A 648 O HOH A 688 2.17
REMARK 500 O PHE G 208 NZ LYS G 291 2.17
REMARK 500 OG SER F 215 OE2 GLU F 301 2.17
REMARK 500 O HOH C 657 O HOH D 631 2.17
REMARK 500 O HOH A 724 O HOH A 729 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 PRO F 277 CD PRO F 277 N 0.134
REMARK 500 PRO G 202 CD PRO G 202 N 0.087
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 PRO F 277 CA - N - CD ANGL. DEV. = -9.8 DEGREES
REMARK 500 ILE F 390 CB - CA - C ANGL. DEV. = -15.9 DEGREES
REMARK 500 ILE F 390 N - CA - C ANGL. DEV. = 22.4 DEGREES
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 HIS A 32 -128.26 55.03
REMARK 500 PHE A 69 38.98 -90.80
REMARK 500 TYR A 143 -4.03 -144.91
REMARK 500 ASN A 150 131.06 -170.87
REMARK 500 SER A 189 -125.76 60.07
REMARK 500 SER A 268 -4.86 -150.81
REMARK 500 PHE A 349 -60.98 -120.05
REMARK 500 ILE A 390 -31.47 81.14
REMARK 500 ASN A 399 53.66 -99.01
REMARK 500 PRO A 435 37.62 -85.79
REMARK 500 HIS B 32 -119.99 40.02
REMARK 500 PHE B 69 44.15 -99.95
REMARK 500 TYR B 143 -4.24 -140.26
REMARK 500 SER B 189 -116.54 47.60
REMARK 500 SER B 268 -3.41 -160.07
REMARK 500 ASP B 300 56.23 -119.17
REMARK 500 HIS B 377 -178.42 -173.25
REMARK 500 ILE B 390 -26.06 85.48
REMARK 500 ASN B 399 57.46 -93.02
REMARK 500 HIS B 406 44.99 -140.32
REMARK 500 PRO B 435 40.29 -84.79
REMARK 500 MET B 438 151.23 -48.83
REMARK 500 HIS C 32 -125.11 59.47
REMARK 500 SER C 46 -71.52 -65.70
REMARK 500 PHE C 69 35.61 -95.46
REMARK 500 HIS C 112 149.36 -179.29
REMARK 500 ASN C 150 124.91 -172.14
REMARK 500 SER C 189 -121.62 60.50
REMARK 500 ARG C 219 78.60 -119.13
REMARK 500 ASP C 242 59.51 34.65
REMARK 500 SER C 308 -179.59 -171.67
REMARK 500 ASN C 325 20.11 -76.16
REMARK 500 PHE C 349 -66.57 -120.99
REMARK 500 HIS C 389 133.76 -38.66
REMARK 500 ILE C 390 -26.61 84.46
REMARK 500 ASN C 399 54.97 -94.14
REMARK 500 PRO C 435 47.72 -83.46
REMARK 500 HIS D 32 -120.50 48.83
REMARK 500 PHE D 69 36.84 -99.13
REMARK 500 ASP D 81 86.04 -69.85
REMARK 500 HIS D 112 148.52 -175.09
REMARK 500 TYR D 143 -9.41 -140.10
REMARK 500 ASP D 145 81.41 -67.04
REMARK 500 SER D 189 -120.43 56.92
REMARK 500 SER D 268 -3.82 -151.09
REMARK 500 THR D 280 -163.68 -118.41
REMARK 500 LYS D 311 41.12 -77.50
REMARK 500 HIS D 377 -179.05 -172.62
REMARK 500 ILE D 390 -25.01 81.00
REMARK 500 ASN D 399 58.98 -90.33
REMARK 500
REMARK 500 THIS ENTRY HAS 99 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG F 137 0.08 SIDE CHAIN
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 731 DISTANCE = 5.93 ANGSTROMS
DBREF1 8S9J A 1 450 UNP A0A0D6GYZ4_STAAU
DBREF2 8S9J A A0A0D6GYZ4 1 450
DBREF1 8S9J B 1 450 UNP A0A0D6GYZ4_STAAU
DBREF2 8S9J B A0A0D6GYZ4 1 450
DBREF1 8S9J C 1 450 UNP A0A0D6GYZ4_STAAU
DBREF2 8S9J C A0A0D6GYZ4 1 450
DBREF1 8S9J D 1 450 UNP A0A0D6GYZ4_STAAU
DBREF2 8S9J D A0A0D6GYZ4 1 450
DBREF1 8S9J E 1 450 UNP A0A0D6GYZ4_STAAU
DBREF2 8S9J E A0A0D6GYZ4 1 450
DBREF1 8S9J F 1 450 UNP A0A0D6GYZ4_STAAU
DBREF2 8S9J F A0A0D6GYZ4 1 450
DBREF1 8S9J G 1 450 UNP A0A0D6GYZ4_STAAU
DBREF2 8S9J G A0A0D6GYZ4 1 450
SEQADV 8S9J GLY A -2 UNP A0A0D6GYZ EXPRESSION TAG
SEQADV 8S9J PRO A -1 UNP A0A0D6GYZ EXPRESSION TAG
SEQADV 8S9J GLY A 0 UNP A0A0D6GYZ EXPRESSION TAG
SEQADV 8S9J GLY B -2 UNP A0A0D6GYZ EXPRESSION TAG
SEQADV 8S9J PRO B -1 UNP A0A0D6GYZ EXPRESSION TAG
SEQADV 8S9J GLY B 0 UNP A0A0D6GYZ EXPRESSION TAG
SEQADV 8S9J GLY C -2 UNP A0A0D6GYZ EXPRESSION TAG
SEQADV 8S9J PRO C -1 UNP A0A0D6GYZ EXPRESSION TAG
SEQADV 8S9J GLY C 0 UNP A0A0D6GYZ EXPRESSION TAG
SEQADV 8S9J GLY D -2 UNP A0A0D6GYZ EXPRESSION TAG
SEQADV 8S9J PRO D -1 UNP A0A0D6GYZ EXPRESSION TAG
SEQADV 8S9J GLY D 0 UNP A0A0D6GYZ EXPRESSION TAG
SEQADV 8S9J GLY E -2 UNP A0A0D6GYZ EXPRESSION TAG
SEQADV 8S9J PRO E -1 UNP A0A0D6GYZ EXPRESSION TAG
SEQADV 8S9J GLY E 0 UNP A0A0D6GYZ EXPRESSION TAG
SEQADV 8S9J GLY F -2 UNP A0A0D6GYZ EXPRESSION TAG
SEQADV 8S9J PRO F -1 UNP A0A0D6GYZ EXPRESSION TAG
SEQADV 8S9J GLY F 0 UNP A0A0D6GYZ EXPRESSION TAG
SEQADV 8S9J GLY G -2 UNP A0A0D6GYZ EXPRESSION TAG
SEQADV 8S9J PRO G -1 UNP A0A0D6GYZ EXPRESSION TAG
SEQADV 8S9J GLY G 0 UNP A0A0D6GYZ EXPRESSION TAG
SEQRES 1 A 453 GLY PRO GLY MET LYS ILE ASN THR THR GLY GLY GLN ILE
SEQRES 2 A 453 HIS GLY ILE THR GLN ASP GLY LEU ASP ILE PHE LEU GLY
SEQRES 3 A 453 ILE PRO TYR ALA GLU PRO PRO VAL HIS ASP ASN ARG PHE
SEQRES 4 A 453 LYS HIS SER THR LEU LYS THR GLN TRP SER GLU PRO ILE
SEQRES 5 A 453 ASP ALA THR GLU ILE GLN PRO ILE PRO PRO GLN PRO ASP
SEQRES 6 A 453 ASN LYS LEU GLU ASP PHE PHE SER SER GLN SER THR THR
SEQRES 7 A 453 PHE THR GLU HIS GLU ASP CYS LEU TYR LEU ASN ILE TRP
SEQRES 8 A 453 LYS GLN HIS ASN ASP GLN THR LYS LYS PRO VAL ILE ILE
SEQRES 9 A 453 TYR PHE TYR GLY GLY SER PHE GLU ASN GLY HIS GLY THR
SEQRES 10 A 453 ALA GLU LEU TYR GLN PRO ALA HIS LEU VAL GLN ASN ASN
SEQRES 11 A 453 ASP ILE ILE VAL ILE THR CYS ASN TYR ARG LEU GLY ALA
SEQRES 12 A 453 LEU GLY TYR LEU ASP TRP SER TYR PHE ASN LYS ASP PHE
SEQRES 13 A 453 HIS SER ASN ASN GLY LEU SER ASP GLN ILE ASN VAL ILE
SEQRES 14 A 453 LYS TRP VAL HIS GLN PHE ILE GLU SER PHE GLY GLY ASP
SEQRES 15 A 453 ALA ASN ASN ILE THR LEU MET GLY GLN SER ALA GLY SER
SEQRES 16 A 453 MET SER ILE LEU THR LEU LEU LYS ILE PRO ASP ILE GLU
SEQRES 17 A 453 PRO TYR PHE HIS LYS VAL VAL LEU LEU SER GLY ALA LEU
SEQRES 18 A 453 ARG LEU ASP THR LEU GLU SER ALA ARG ASN LYS ALA GLN
SEQRES 19 A 453 HIS PHE GLN LYS MET MET LEU ASP TYR LEU ASP THR ASP
SEQRES 20 A 453 ASP VAL THR SER LEU SER THR ASN ASP ILE LEU MET LEU
SEQRES 21 A 453 MET ALA LYS LEU LYS GLN SER ARG GLY PRO SER LYS GLY
SEQRES 22 A 453 LEU ASP LEU ILE TYR ALA PRO ILE LYS THR ASP TYR ILE
SEQRES 23 A 453 GLN ASN ASN TYR PRO THR THR LYS PRO ILE PHE ALA CYS
SEQRES 24 A 453 TYR THR LYS ASP GLU GLY ASP ILE TYR ILE THR SER GLU
SEQRES 25 A 453 GLN LYS LYS LEU SER PRO GLN ARG PHE ILE ASP ILE MET
SEQRES 26 A 453 GLU LEU ASN ASP ILE PRO LEU LYS TYR GLU ASP VAL GLN
SEQRES 27 A 453 THR ALA LYS GLN GLN SER LEU ALA ILE THR HIS CYS TYR
SEQRES 28 A 453 PHE LYS GLN PRO MET LYS GLN PHE LEU GLN GLN LEU ASN
SEQRES 29 A 453 ILE GLN ASP SER ASN ALA GLN LEU TRP LEU ALA GLU PHE
SEQRES 30 A 453 ALA TRP HIS ASP THR SER SER ALA HIS TYR ARG SER ALA
SEQRES 31 A 453 TYR HIS ILE LEU ASP MET VAL PHE TRP PHE GLY ASN LEU
SEQRES 32 A 453 GLN ILE LEU ALA ALA HIS GLN TYR PRO THR THR ALA HIS
SEQRES 33 A 453 LEU LYS PHE LEU SER ARG GLN MET GLN ASN ASP LEU ALA
SEQRES 34 A 453 ASN PHE ALA LYS SER GLY LYS MET PRO TRP PRO MET TYR
SEQRES 35 A 453 HIS ASN GLU ARG ARG TYR TYR ARG THR TYR GLN
SEQRES 1 B 453 GLY PRO GLY MET LYS ILE ASN THR THR GLY GLY GLN ILE
SEQRES 2 B 453 HIS GLY ILE THR GLN ASP GLY LEU ASP ILE PHE LEU GLY
SEQRES 3 B 453 ILE PRO TYR ALA GLU PRO PRO VAL HIS ASP ASN ARG PHE
SEQRES 4 B 453 LYS HIS SER THR LEU LYS THR GLN TRP SER GLU PRO ILE
SEQRES 5 B 453 ASP ALA THR GLU ILE GLN PRO ILE PRO PRO GLN PRO ASP
SEQRES 6 B 453 ASN LYS LEU GLU ASP PHE PHE SER SER GLN SER THR THR
SEQRES 7 B 453 PHE THR GLU HIS GLU ASP CYS LEU TYR LEU ASN ILE TRP
SEQRES 8 B 453 LYS GLN HIS ASN ASP GLN THR LYS LYS PRO VAL ILE ILE
SEQRES 9 B 453 TYR PHE TYR GLY GLY SER PHE GLU ASN GLY HIS GLY THR
SEQRES 10 B 453 ALA GLU LEU TYR GLN PRO ALA HIS LEU VAL GLN ASN ASN
SEQRES 11 B 453 ASP ILE ILE VAL ILE THR CYS ASN TYR ARG LEU GLY ALA
SEQRES 12 B 453 LEU GLY TYR LEU ASP TRP SER TYR PHE ASN LYS ASP PHE
SEQRES 13 B 453 HIS SER ASN ASN GLY LEU SER ASP GLN ILE ASN VAL ILE
SEQRES 14 B 453 LYS TRP VAL HIS GLN PHE ILE GLU SER PHE GLY GLY ASP
SEQRES 15 B 453 ALA ASN ASN ILE THR LEU MET GLY GLN SER ALA GLY SER
SEQRES 16 B 453 MET SER ILE LEU THR LEU LEU LYS ILE PRO ASP ILE GLU
SEQRES 17 B 453 PRO TYR PHE HIS LYS VAL VAL LEU LEU SER GLY ALA LEU
SEQRES 18 B 453 ARG LEU ASP THR LEU GLU SER ALA ARG ASN LYS ALA GLN
SEQRES 19 B 453 HIS PHE GLN LYS MET MET LEU ASP TYR LEU ASP THR ASP
SEQRES 20 B 453 ASP VAL THR SER LEU SER THR ASN ASP ILE LEU MET LEU
SEQRES 21 B 453 MET ALA LYS LEU LYS GLN SER ARG GLY PRO SER LYS GLY
SEQRES 22 B 453 LEU ASP LEU ILE TYR ALA PRO ILE LYS THR ASP TYR ILE
SEQRES 23 B 453 GLN ASN ASN TYR PRO THR THR LYS PRO ILE PHE ALA CYS
SEQRES 24 B 453 TYR THR LYS ASP GLU GLY ASP ILE TYR ILE THR SER GLU
SEQRES 25 B 453 GLN LYS LYS LEU SER PRO GLN ARG PHE ILE ASP ILE MET
SEQRES 26 B 453 GLU LEU ASN ASP ILE PRO LEU LYS TYR GLU ASP VAL GLN
SEQRES 27 B 453 THR ALA LYS GLN GLN SER LEU ALA ILE THR HIS CYS TYR
SEQRES 28 B 453 PHE LYS GLN PRO MET LYS GLN PHE LEU GLN GLN LEU ASN
SEQRES 29 B 453 ILE GLN ASP SER ASN ALA GLN LEU TRP LEU ALA GLU PHE
SEQRES 30 B 453 ALA TRP HIS ASP THR SER SER ALA HIS TYR ARG SER ALA
SEQRES 31 B 453 TYR HIS ILE LEU ASP MET VAL PHE TRP PHE GLY ASN LEU
SEQRES 32 B 453 GLN ILE LEU ALA ALA HIS GLN TYR PRO THR THR ALA HIS
SEQRES 33 B 453 LEU LYS PHE LEU SER ARG GLN MET GLN ASN ASP LEU ALA
SEQRES 34 B 453 ASN PHE ALA LYS SER GLY LYS MET PRO TRP PRO MET TYR
SEQRES 35 B 453 HIS ASN GLU ARG ARG TYR TYR ARG THR TYR GLN
SEQRES 1 C 453 GLY PRO GLY MET LYS ILE ASN THR THR GLY GLY GLN ILE
SEQRES 2 C 453 HIS GLY ILE THR GLN ASP GLY LEU ASP ILE PHE LEU GLY
SEQRES 3 C 453 ILE PRO TYR ALA GLU PRO PRO VAL HIS ASP ASN ARG PHE
SEQRES 4 C 453 LYS HIS SER THR LEU LYS THR GLN TRP SER GLU PRO ILE
SEQRES 5 C 453 ASP ALA THR GLU ILE GLN PRO ILE PRO PRO GLN PRO ASP
SEQRES 6 C 453 ASN LYS LEU GLU ASP PHE PHE SER SER GLN SER THR THR
SEQRES 7 C 453 PHE THR GLU HIS GLU ASP CYS LEU TYR LEU ASN ILE TRP
SEQRES 8 C 453 LYS GLN HIS ASN ASP GLN THR LYS LYS PRO VAL ILE ILE
SEQRES 9 C 453 TYR PHE TYR GLY GLY SER PHE GLU ASN GLY HIS GLY THR
SEQRES 10 C 453 ALA GLU LEU TYR GLN PRO ALA HIS LEU VAL GLN ASN ASN
SEQRES 11 C 453 ASP ILE ILE VAL ILE THR CYS ASN TYR ARG LEU GLY ALA
SEQRES 12 C 453 LEU GLY TYR LEU ASP TRP SER TYR PHE ASN LYS ASP PHE
SEQRES 13 C 453 HIS SER ASN ASN GLY LEU SER ASP GLN ILE ASN VAL ILE
SEQRES 14 C 453 LYS TRP VAL HIS GLN PHE ILE GLU SER PHE GLY GLY ASP
SEQRES 15 C 453 ALA ASN ASN ILE THR LEU MET GLY GLN SER ALA GLY SER
SEQRES 16 C 453 MET SER ILE LEU THR LEU LEU LYS ILE PRO ASP ILE GLU
SEQRES 17 C 453 PRO TYR PHE HIS LYS VAL VAL LEU LEU SER GLY ALA LEU
SEQRES 18 C 453 ARG LEU ASP THR LEU GLU SER ALA ARG ASN LYS ALA GLN
SEQRES 19 C 453 HIS PHE GLN LYS MET MET LEU ASP TYR LEU ASP THR ASP
SEQRES 20 C 453 ASP VAL THR SER LEU SER THR ASN ASP ILE LEU MET LEU
SEQRES 21 C 453 MET ALA LYS LEU LYS GLN SER ARG GLY PRO SER LYS GLY
SEQRES 22 C 453 LEU ASP LEU ILE TYR ALA PRO ILE LYS THR ASP TYR ILE
SEQRES 23 C 453 GLN ASN ASN TYR PRO THR THR LYS PRO ILE PHE ALA CYS
SEQRES 24 C 453 TYR THR LYS ASP GLU GLY ASP ILE TYR ILE THR SER GLU
SEQRES 25 C 453 GLN LYS LYS LEU SER PRO GLN ARG PHE ILE ASP ILE MET
SEQRES 26 C 453 GLU LEU ASN ASP ILE PRO LEU LYS TYR GLU ASP VAL GLN
SEQRES 27 C 453 THR ALA LYS GLN GLN SER LEU ALA ILE THR HIS CYS TYR
SEQRES 28 C 453 PHE LYS GLN PRO MET LYS GLN PHE LEU GLN GLN LEU ASN
SEQRES 29 C 453 ILE GLN ASP SER ASN ALA GLN LEU TRP LEU ALA GLU PHE
SEQRES 30 C 453 ALA TRP HIS ASP THR SER SER ALA HIS TYR ARG SER ALA
SEQRES 31 C 453 TYR HIS ILE LEU ASP MET VAL PHE TRP PHE GLY ASN LEU
SEQRES 32 C 453 GLN ILE LEU ALA ALA HIS GLN TYR PRO THR THR ALA HIS
SEQRES 33 C 453 LEU LYS PHE LEU SER ARG GLN MET GLN ASN ASP LEU ALA
SEQRES 34 C 453 ASN PHE ALA LYS SER GLY LYS MET PRO TRP PRO MET TYR
SEQRES 35 C 453 HIS ASN GLU ARG ARG TYR TYR ARG THR TYR GLN
SEQRES 1 D 453 GLY PRO GLY MET LYS ILE ASN THR THR GLY GLY GLN ILE
SEQRES 2 D 453 HIS GLY ILE THR GLN ASP GLY LEU ASP ILE PHE LEU GLY
SEQRES 3 D 453 ILE PRO TYR ALA GLU PRO PRO VAL HIS ASP ASN ARG PHE
SEQRES 4 D 453 LYS HIS SER THR LEU LYS THR GLN TRP SER GLU PRO ILE
SEQRES 5 D 453 ASP ALA THR GLU ILE GLN PRO ILE PRO PRO GLN PRO ASP
SEQRES 6 D 453 ASN LYS LEU GLU ASP PHE PHE SER SER GLN SER THR THR
SEQRES 7 D 453 PHE THR GLU HIS GLU ASP CYS LEU TYR LEU ASN ILE TRP
SEQRES 8 D 453 LYS GLN HIS ASN ASP GLN THR LYS LYS PRO VAL ILE ILE
SEQRES 9 D 453 TYR PHE TYR GLY GLY SER PHE GLU ASN GLY HIS GLY THR
SEQRES 10 D 453 ALA GLU LEU TYR GLN PRO ALA HIS LEU VAL GLN ASN ASN
SEQRES 11 D 453 ASP ILE ILE VAL ILE THR CYS ASN TYR ARG LEU GLY ALA
SEQRES 12 D 453 LEU GLY TYR LEU ASP TRP SER TYR PHE ASN LYS ASP PHE
SEQRES 13 D 453 HIS SER ASN ASN GLY LEU SER ASP GLN ILE ASN VAL ILE
SEQRES 14 D 453 LYS TRP VAL HIS GLN PHE ILE GLU SER PHE GLY GLY ASP
SEQRES 15 D 453 ALA ASN ASN ILE THR LEU MET GLY GLN SER ALA GLY SER
SEQRES 16 D 453 MET SER ILE LEU THR LEU LEU LYS ILE PRO ASP ILE GLU
SEQRES 17 D 453 PRO TYR PHE HIS LYS VAL VAL LEU LEU SER GLY ALA LEU
SEQRES 18 D 453 ARG LEU ASP THR LEU GLU SER ALA ARG ASN LYS ALA GLN
SEQRES 19 D 453 HIS PHE GLN LYS MET MET LEU ASP TYR LEU ASP THR ASP
SEQRES 20 D 453 ASP VAL THR SER LEU SER THR ASN ASP ILE LEU MET LEU
SEQRES 21 D 453 MET ALA LYS LEU LYS GLN SER ARG GLY PRO SER LYS GLY
SEQRES 22 D 453 LEU ASP LEU ILE TYR ALA PRO ILE LYS THR ASP TYR ILE
SEQRES 23 D 453 GLN ASN ASN TYR PRO THR THR LYS PRO ILE PHE ALA CYS
SEQRES 24 D 453 TYR THR LYS ASP GLU GLY ASP ILE TYR ILE THR SER GLU
SEQRES 25 D 453 GLN LYS LYS LEU SER PRO GLN ARG PHE ILE ASP ILE MET
SEQRES 26 D 453 GLU LEU ASN ASP ILE PRO LEU LYS TYR GLU ASP VAL GLN
SEQRES 27 D 453 THR ALA LYS GLN GLN SER LEU ALA ILE THR HIS CYS TYR
SEQRES 28 D 453 PHE LYS GLN PRO MET LYS GLN PHE LEU GLN GLN LEU ASN
SEQRES 29 D 453 ILE GLN ASP SER ASN ALA GLN LEU TRP LEU ALA GLU PHE
SEQRES 30 D 453 ALA TRP HIS ASP THR SER SER ALA HIS TYR ARG SER ALA
SEQRES 31 D 453 TYR HIS ILE LEU ASP MET VAL PHE TRP PHE GLY ASN LEU
SEQRES 32 D 453 GLN ILE LEU ALA ALA HIS GLN TYR PRO THR THR ALA HIS
SEQRES 33 D 453 LEU LYS PHE LEU SER ARG GLN MET GLN ASN ASP LEU ALA
SEQRES 34 D 453 ASN PHE ALA LYS SER GLY LYS MET PRO TRP PRO MET TYR
SEQRES 35 D 453 HIS ASN GLU ARG ARG TYR TYR ARG THR TYR GLN
SEQRES 1 E 453 GLY PRO GLY MET LYS ILE ASN THR THR GLY GLY GLN ILE
SEQRES 2 E 453 HIS GLY ILE THR GLN ASP GLY LEU ASP ILE PHE LEU GLY
SEQRES 3 E 453 ILE PRO TYR ALA GLU PRO PRO VAL HIS ASP ASN ARG PHE
SEQRES 4 E 453 LYS HIS SER THR LEU LYS THR GLN TRP SER GLU PRO ILE
SEQRES 5 E 453 ASP ALA THR GLU ILE GLN PRO ILE PRO PRO GLN PRO ASP
SEQRES 6 E 453 ASN LYS LEU GLU ASP PHE PHE SER SER GLN SER THR THR
SEQRES 7 E 453 PHE THR GLU HIS GLU ASP CYS LEU TYR LEU ASN ILE TRP
SEQRES 8 E 453 LYS GLN HIS ASN ASP GLN THR LYS LYS PRO VAL ILE ILE
SEQRES 9 E 453 TYR PHE TYR GLY GLY SER PHE GLU ASN GLY HIS GLY THR
SEQRES 10 E 453 ALA GLU LEU TYR GLN PRO ALA HIS LEU VAL GLN ASN ASN
SEQRES 11 E 453 ASP ILE ILE VAL ILE THR CYS ASN TYR ARG LEU GLY ALA
SEQRES 12 E 453 LEU GLY TYR LEU ASP TRP SER TYR PHE ASN LYS ASP PHE
SEQRES 13 E 453 HIS SER ASN ASN GLY LEU SER ASP GLN ILE ASN VAL ILE
SEQRES 14 E 453 LYS TRP VAL HIS GLN PHE ILE GLU SER PHE GLY GLY ASP
SEQRES 15 E 453 ALA ASN ASN ILE THR LEU MET GLY GLN SER ALA GLY SER
SEQRES 16 E 453 MET SER ILE LEU THR LEU LEU LYS ILE PRO ASP ILE GLU
SEQRES 17 E 453 PRO TYR PHE HIS LYS VAL VAL LEU LEU SER GLY ALA LEU
SEQRES 18 E 453 ARG LEU ASP THR LEU GLU SER ALA ARG ASN LYS ALA GLN
SEQRES 19 E 453 HIS PHE GLN LYS MET MET LEU ASP TYR LEU ASP THR ASP
SEQRES 20 E 453 ASP VAL THR SER LEU SER THR ASN ASP ILE LEU MET LEU
SEQRES 21 E 453 MET ALA LYS LEU LYS GLN SER ARG GLY PRO SER LYS GLY
SEQRES 22 E 453 LEU ASP LEU ILE TYR ALA PRO ILE LYS THR ASP TYR ILE
SEQRES 23 E 453 GLN ASN ASN TYR PRO THR THR LYS PRO ILE PHE ALA CYS
SEQRES 24 E 453 TYR THR LYS ASP GLU GLY ASP ILE TYR ILE THR SER GLU
SEQRES 25 E 453 GLN LYS LYS LEU SER PRO GLN ARG PHE ILE ASP ILE MET
SEQRES 26 E 453 GLU LEU ASN ASP ILE PRO LEU LYS TYR GLU ASP VAL GLN
SEQRES 27 E 453 THR ALA LYS GLN GLN SER LEU ALA ILE THR HIS CYS TYR
SEQRES 28 E 453 PHE LYS GLN PRO MET LYS GLN PHE LEU GLN GLN LEU ASN
SEQRES 29 E 453 ILE GLN ASP SER ASN ALA GLN LEU TRP LEU ALA GLU PHE
SEQRES 30 E 453 ALA TRP HIS ASP THR SER SER ALA HIS TYR ARG SER ALA
SEQRES 31 E 453 TYR HIS ILE LEU ASP MET VAL PHE TRP PHE GLY ASN LEU
SEQRES 32 E 453 GLN ILE LEU ALA ALA HIS GLN TYR PRO THR THR ALA HIS
SEQRES 33 E 453 LEU LYS PHE LEU SER ARG GLN MET GLN ASN ASP LEU ALA
SEQRES 34 E 453 ASN PHE ALA LYS SER GLY LYS MET PRO TRP PRO MET TYR
SEQRES 35 E 453 HIS ASN GLU ARG ARG TYR TYR ARG THR TYR GLN
SEQRES 1 F 453 GLY PRO GLY MET LYS ILE ASN THR THR GLY GLY GLN ILE
SEQRES 2 F 453 HIS GLY ILE THR GLN ASP GLY LEU ASP ILE PHE LEU GLY
SEQRES 3 F 453 ILE PRO TYR ALA GLU PRO PRO VAL HIS ASP ASN ARG PHE
SEQRES 4 F 453 LYS HIS SER THR LEU LYS THR GLN TRP SER GLU PRO ILE
SEQRES 5 F 453 ASP ALA THR GLU ILE GLN PRO ILE PRO PRO GLN PRO ASP
SEQRES 6 F 453 ASN LYS LEU GLU ASP PHE PHE SER SER GLN SER THR THR
SEQRES 7 F 453 PHE THR GLU HIS GLU ASP CYS LEU TYR LEU ASN ILE TRP
SEQRES 8 F 453 LYS GLN HIS ASN ASP GLN THR LYS LYS PRO VAL ILE ILE
SEQRES 9 F 453 TYR PHE TYR GLY GLY SER PHE GLU ASN GLY HIS GLY THR
SEQRES 10 F 453 ALA GLU LEU TYR GLN PRO ALA HIS LEU VAL GLN ASN ASN
SEQRES 11 F 453 ASP ILE ILE VAL ILE THR CYS ASN TYR ARG LEU GLY ALA
SEQRES 12 F 453 LEU GLY TYR LEU ASP TRP SER TYR PHE ASN LYS ASP PHE
SEQRES 13 F 453 HIS SER ASN ASN GLY LEU SER ASP GLN ILE ASN VAL ILE
SEQRES 14 F 453 LYS TRP VAL HIS GLN PHE ILE GLU SER PHE GLY GLY ASP
SEQRES 15 F 453 ALA ASN ASN ILE THR LEU MET GLY GLN SER ALA GLY SER
SEQRES 16 F 453 MET SER ILE LEU THR LEU LEU LYS ILE PRO ASP ILE GLU
SEQRES 17 F 453 PRO TYR PHE HIS LYS VAL VAL LEU LEU SER GLY ALA LEU
SEQRES 18 F 453 ARG LEU ASP THR LEU GLU SER ALA ARG ASN LYS ALA GLN
SEQRES 19 F 453 HIS PHE GLN LYS MET MET LEU ASP TYR LEU ASP THR ASP
SEQRES 20 F 453 ASP VAL THR SER LEU SER THR ASN ASP ILE LEU MET LEU
SEQRES 21 F 453 MET ALA LYS LEU LYS GLN SER ARG GLY PRO SER LYS GLY
SEQRES 22 F 453 LEU ASP LEU ILE TYR ALA PRO ILE LYS THR ASP TYR ILE
SEQRES 23 F 453 GLN ASN ASN TYR PRO THR THR LYS PRO ILE PHE ALA CYS
SEQRES 24 F 453 TYR THR LYS ASP GLU GLY ASP ILE TYR ILE THR SER GLU
SEQRES 25 F 453 GLN LYS LYS LEU SER PRO GLN ARG PHE ILE ASP ILE MET
SEQRES 26 F 453 GLU LEU ASN ASP ILE PRO LEU LYS TYR GLU ASP VAL GLN
SEQRES 27 F 453 THR ALA LYS GLN GLN SER LEU ALA ILE THR HIS CYS TYR
SEQRES 28 F 453 PHE LYS GLN PRO MET LYS GLN PHE LEU GLN GLN LEU ASN
SEQRES 29 F 453 ILE GLN ASP SER ASN ALA GLN LEU TRP LEU ALA GLU PHE
SEQRES 30 F 453 ALA TRP HIS ASP THR SER SER ALA HIS TYR ARG SER ALA
SEQRES 31 F 453 TYR HIS ILE LEU ASP MET VAL PHE TRP PHE GLY ASN LEU
SEQRES 32 F 453 GLN ILE LEU ALA ALA HIS GLN TYR PRO THR THR ALA HIS
SEQRES 33 F 453 LEU LYS PHE LEU SER ARG GLN MET GLN ASN ASP LEU ALA
SEQRES 34 F 453 ASN PHE ALA LYS SER GLY LYS MET PRO TRP PRO MET TYR
SEQRES 35 F 453 HIS ASN GLU ARG ARG TYR TYR ARG THR TYR GLN
SEQRES 1 G 453 GLY PRO GLY MET LYS ILE ASN THR THR GLY GLY GLN ILE
SEQRES 2 G 453 HIS GLY ILE THR GLN ASP GLY LEU ASP ILE PHE LEU GLY
SEQRES 3 G 453 ILE PRO TYR ALA GLU PRO PRO VAL HIS ASP ASN ARG PHE
SEQRES 4 G 453 LYS HIS SER THR LEU LYS THR GLN TRP SER GLU PRO ILE
SEQRES 5 G 453 ASP ALA THR GLU ILE GLN PRO ILE PRO PRO GLN PRO ASP
SEQRES 6 G 453 ASN LYS LEU GLU ASP PHE PHE SER SER GLN SER THR THR
SEQRES 7 G 453 PHE THR GLU HIS GLU ASP CYS LEU TYR LEU ASN ILE TRP
SEQRES 8 G 453 LYS GLN HIS ASN ASP GLN THR LYS LYS PRO VAL ILE ILE
SEQRES 9 G 453 TYR PHE TYR GLY GLY SER PHE GLU ASN GLY HIS GLY THR
SEQRES 10 G 453 ALA GLU LEU TYR GLN PRO ALA HIS LEU VAL GLN ASN ASN
SEQRES 11 G 453 ASP ILE ILE VAL ILE THR CYS ASN TYR ARG LEU GLY ALA
SEQRES 12 G 453 LEU GLY TYR LEU ASP TRP SER TYR PHE ASN LYS ASP PHE
SEQRES 13 G 453 HIS SER ASN ASN GLY LEU SER ASP GLN ILE ASN VAL ILE
SEQRES 14 G 453 LYS TRP VAL HIS GLN PHE ILE GLU SER PHE GLY GLY ASP
SEQRES 15 G 453 ALA ASN ASN ILE THR LEU MET GLY GLN SER ALA GLY SER
SEQRES 16 G 453 MET SER ILE LEU THR LEU LEU LYS ILE PRO ASP ILE GLU
SEQRES 17 G 453 PRO TYR PHE HIS LYS VAL VAL LEU LEU SER GLY ALA LEU
SEQRES 18 G 453 ARG LEU ASP THR LEU GLU SER ALA ARG ASN LYS ALA GLN
SEQRES 19 G 453 HIS PHE GLN LYS MET MET LEU ASP TYR LEU ASP THR ASP
SEQRES 20 G 453 ASP VAL THR SER LEU SER THR ASN ASP ILE LEU MET LEU
SEQRES 21 G 453 MET ALA LYS LEU LYS GLN SER ARG GLY PRO SER LYS GLY
SEQRES 22 G 453 LEU ASP LEU ILE TYR ALA PRO ILE LYS THR ASP TYR ILE
SEQRES 23 G 453 GLN ASN ASN TYR PRO THR THR LYS PRO ILE PHE ALA CYS
SEQRES 24 G 453 TYR THR LYS ASP GLU GLY ASP ILE TYR ILE THR SER GLU
SEQRES 25 G 453 GLN LYS LYS LEU SER PRO GLN ARG PHE ILE ASP ILE MET
SEQRES 26 G 453 GLU LEU ASN ASP ILE PRO LEU LYS TYR GLU ASP VAL GLN
SEQRES 27 G 453 THR ALA LYS GLN GLN SER LEU ALA ILE THR HIS CYS TYR
SEQRES 28 G 453 PHE LYS GLN PRO MET LYS GLN PHE LEU GLN GLN LEU ASN
SEQRES 29 G 453 ILE GLN ASP SER ASN ALA GLN LEU TRP LEU ALA GLU PHE
SEQRES 30 G 453 ALA TRP HIS ASP THR SER SER ALA HIS TYR ARG SER ALA
SEQRES 31 G 453 TYR HIS ILE LEU ASP MET VAL PHE TRP PHE GLY ASN LEU
SEQRES 32 G 453 GLN ILE LEU ALA ALA HIS GLN TYR PRO THR THR ALA HIS
SEQRES 33 G 453 LEU LYS PHE LEU SER ARG GLN MET GLN ASN ASP LEU ALA
SEQRES 34 G 453 ASN PHE ALA LYS SER GLY LYS MET PRO TRP PRO MET TYR
SEQRES 35 G 453 HIS ASN GLU ARG ARG TYR TYR ARG THR TYR GLN
HET SO4 A 501 5
HET SO4 A 502 5
HET SO4 A 503 5
HET SO4 A 504 5
HET SO4 A 505 5
HET SO4 A 506 5
HET SO4 B 501 5
HET SO4 B 502 5
HET SO4 B 503 5
HET SO4 B 504 5
HET SO4 C 501 5
HET SO4 C 502 5
HET SO4 C 503 5
HET SO4 C 504 5
HET SO4 C 505 5
HET SO4 D 501 5
HET SO4 D 502 5
HET SO4 D 503 5
HET SO4 D 504 5
HET SO4 E 501 5
HET SO4 E 502 5
HET SO4 E 503 5
HET SO4 E 504 5
HET SO4 F 501 5
HET SO4 F 502 5
HET SO4 F 503 5
HET SO4 G 501 5
HET SO4 G 502 5
HETNAM SO4 SULFATE ION
FORMUL 8 SO4 28(O4 S 2-)
FORMUL 36 HOH *400(H2 O)
HELIX 1 AA1 VAL A 31 ARG A 35 5 5
HELIX 2 AA2 ASN A 63 PHE A 69 1 7
HELIX 3 AA3 ALA A 115 GLN A 119 5 5
HELIX 4 AA4 PRO A 120 ASN A 127 1 8
HELIX 5 AA5 LEU A 138 LEU A 144 1 7
HELIX 6 AA6 ASP A 145 PHE A 149 5 5
HELIX 7 AA7 ASN A 156 ILE A 173 1 18
HELIX 8 AA8 GLU A 174 PHE A 176 5 3
HELIX 9 AA9 SER A 189 LYS A 200 1 12
HELIX 10 AB1 ILE A 204 PHE A 208 5 5
HELIX 11 AB2 THR A 222 ASP A 242 1 21
HELIX 12 AB3 ASP A 245 LEU A 249 5 5
HELIX 13 AB4 SER A 250 GLY A 266 1 17
HELIX 14 AB5 ASP A 300 TYR A 305 5 6
HELIX 15 AB6 SER A 308 LYS A 312 5 5
HELIX 16 AB7 SER A 314 ASN A 325 1 12
HELIX 17 AB8 LYS A 330 GLN A 335 5 6
HELIX 18 AB9 THR A 336 PHE A 349 1 14
HELIX 19 AC1 PHE A 349 ASP A 364 1 16
HELIX 20 AC2 ILE A 390 PHE A 397 1 8
HELIX 21 AC3 LEU A 400 ALA A 405 1 6
HELIX 22 AC4 THR A 411 GLY A 432 1 22
HELIX 23 AC5 VAL B 31 ARG B 35 5 5
HELIX 24 AC6 ALA B 115 GLN B 119 5 5
HELIX 25 AC7 PRO B 120 ASN B 127 1 8
HELIX 26 AC8 LEU B 138 LEU B 144 1 7
HELIX 27 AC9 ASP B 145 PHE B 149 5 5
HELIX 28 AD1 ASN B 156 ILE B 173 1 18
HELIX 29 AD2 GLU B 174 PHE B 176 5 3
HELIX 30 AD3 SER B 189 LYS B 200 1 12
HELIX 31 AD4 ILE B 204 PHE B 208 5 5
HELIX 32 AD5 THR B 222 ASP B 242 1 21
HELIX 33 AD6 ASP B 245 LEU B 249 5 5
HELIX 34 AD7 SER B 250 GLY B 266 1 17
HELIX 35 AD8 ASP B 300 TYR B 305 5 6
HELIX 36 AD9 SER B 314 ASN B 325 1 12
HELIX 37 AE1 LYS B 330 GLN B 335 5 6
HELIX 38 AE2 THR B 336 PHE B 349 1 14
HELIX 39 AE3 PHE B 349 ASP B 364 1 16
HELIX 40 AE4 ILE B 390 PHE B 397 1 8
HELIX 41 AE5 LEU B 400 ALA B 405 1 6
HELIX 42 AE6 THR B 411 GLY B 432 1 22
HELIX 43 AE7 VAL C 31 ARG C 35 5 5
HELIX 44 AE8 LYS C 64 PHE C 69 1 6
HELIX 45 AE9 ALA C 115 GLN C 119 5 5
HELIX 46 AF1 PRO C 120 ASN C 127 1 8
HELIX 47 AF2 LEU C 138 LEU C 144 1 7
HELIX 48 AF3 ASP C 145 PHE C 149 5 5
HELIX 49 AF4 ASN C 156 ILE C 173 1 18
HELIX 50 AF5 GLU C 174 PHE C 176 5 3
HELIX 51 AF6 SER C 189 LEU C 199 1 11
HELIX 52 AF7 ILE C 204 PHE C 208 5 5
HELIX 53 AF8 THR C 222 ASP C 242 1 21
HELIX 54 AF9 ASP C 245 LEU C 249 5 5
HELIX 55 AG1 SER C 250 GLY C 266 1 17
HELIX 56 AG2 ASP C 300 TYR C 305 5 6
HELIX 57 AG3 SER C 314 ASN C 325 1 12
HELIX 58 AG4 LYS C 330 VAL C 334 5 5
HELIX 59 AG5 THR C 336 TYR C 348 1 13
HELIX 60 AG6 PHE C 349 ASP C 364 1 16
HELIX 61 AG7 ILE C 390 PHE C 397 1 8
HELIX 62 AG8 LEU C 400 ALA C 405 1 6
HELIX 63 AG9 THR C 411 GLY C 432 1 22
HELIX 64 AH1 VAL D 31 ARG D 35 5 5
HELIX 65 AH2 ALA D 115 GLN D 119 5 5
HELIX 66 AH3 PRO D 120 ASN D 127 1 8
HELIX 67 AH4 LEU D 138 LEU D 144 1 7
HELIX 68 AH5 ASP D 145 PHE D 149 5 5
HELIX 69 AH6 ASN D 156 ILE D 173 1 18
HELIX 70 AH7 GLU D 174 PHE D 176 5 3
HELIX 71 AH8 SER D 189 LEU D 199 1 11
HELIX 72 AH9 ILE D 204 PHE D 208 5 5
HELIX 73 AI1 THR D 222 ASP D 242 1 21
HELIX 74 AI2 ASP D 245 LEU D 249 5 5
HELIX 75 AI3 SER D 250 GLY D 266 1 17
HELIX 76 AI4 ASP D 300 TYR D 305 5 6
HELIX 77 AI5 SER D 314 ASN D 325 1 12
HELIX 78 AI6 LYS D 330 GLN D 335 5 6
HELIX 79 AI7 THR D 336 PHE D 349 1 14
HELIX 80 AI8 PHE D 349 ASP D 364 1 16
HELIX 81 AI9 LEU D 391 PHE D 397 1 7
HELIX 82 AJ1 LEU D 400 ALA D 405 1 6
HELIX 83 AJ2 THR D 411 GLY D 432 1 22
HELIX 84 AJ3 VAL E 31 ARG E 35 5 5
HELIX 85 AJ4 ALA E 115 GLN E 119 5 5
HELIX 86 AJ5 PRO E 120 ASN E 127 1 8
HELIX 87 AJ6 LEU E 138 LEU E 144 1 7
HELIX 88 AJ7 ASN E 156 ILE E 173 1 18
HELIX 89 AJ8 GLU E 174 PHE E 176 5 3
HELIX 90 AJ9 SER E 189 LYS E 200 1 12
HELIX 91 AK1 ILE E 204 PHE E 208 5 5
HELIX 92 AK2 THR E 222 TYR E 240 1 19
HELIX 93 AK3 ASP E 245 LEU E 249 5 5
HELIX 94 AK4 SER E 250 GLY E 266 1 17
HELIX 95 AK5 ASP E 300 TYR E 305 5 6
HELIX 96 AK6 SER E 314 ASN E 325 1 12
HELIX 97 AK7 LYS E 330 GLN E 335 5 6
HELIX 98 AK8 THR E 336 PHE E 349 1 14
HELIX 99 AK9 PHE E 349 ASP E 364 1 16
HELIX 100 AL1 ILE E 390 PHE E 397 1 8
HELIX 101 AL2 LEU E 400 ALA E 405 1 6
HELIX 102 AL3 THR E 411 GLY E 432 1 22
HELIX 103 AL4 VAL F 31 ARG F 35 5 5
HELIX 104 AL5 LYS F 64 PHE F 69 1 6
HELIX 105 AL6 ALA F 115 GLN F 119 5 5
HELIX 106 AL7 PRO F 120 ASN F 127 1 8
HELIX 107 AL8 GLY F 139 LEU F 144 1 6
HELIX 108 AL9 ASP F 145 PHE F 149 5 5
HELIX 109 AM1 ASN F 156 ILE F 173 1 18
HELIX 110 AM2 GLU F 174 PHE F 176 5 3
HELIX 111 AM3 SER F 189 LYS F 200 1 12
HELIX 112 AM4 ILE F 204 PHE F 208 5 5
HELIX 113 AM5 THR F 222 ASP F 242 1 21
HELIX 114 AM6 ASP F 245 LEU F 249 5 5
HELIX 115 AM7 SER F 250 GLY F 266 1 17
HELIX 116 AM8 ASP F 300 TYR F 305 5 6
HELIX 117 AM9 SER F 308 LYS F 312 5 5
HELIX 118 AN1 SER F 314 ASN F 325 1 12
HELIX 119 AN2 LYS F 330 GLN F 335 5 6
HELIX 120 AN3 THR F 336 PHE F 349 1 14
HELIX 121 AN4 PHE F 349 ASP F 364 1 16
HELIX 122 AN5 LEU F 391 PHE F 397 1 7
HELIX 123 AN6 LEU F 400 ALA F 405 1 6
HELIX 124 AN7 THR F 411 GLY F 432 1 22
HELIX 125 AN8 VAL G 31 ARG G 35 5 5
HELIX 126 AN9 ALA G 115 GLN G 119 5 5
HELIX 127 AO1 PRO G 120 ASN G 127 1 8
HELIX 128 AO2 LEU G 138 LEU G 144 1 7
HELIX 129 AO3 ASP G 145 PHE G 149 5 5
HELIX 130 AO4 ASN G 156 ILE G 173 1 18
HELIX 131 AO5 GLU G 174 PHE G 176 5 3
HELIX 132 AO6 SER G 189 LEU G 199 1 11
HELIX 133 AO7 ILE G 204 PHE G 208 5 5
HELIX 134 AO8 THR G 222 ASP G 242 1 21
HELIX 135 AO9 SER G 250 GLY G 266 1 17
HELIX 136 AP1 ASP G 300 TYR G 305 5 6
HELIX 137 AP2 SER G 314 ASN G 325 1 12
HELIX 138 AP3 LYS G 330 VAL G 334 5 5
HELIX 139 AP4 THR G 336 PHE G 349 1 14
HELIX 140 AP5 PHE G 349 ASP G 364 1 16
HELIX 141 AP6 ILE G 390 PHE G 397 1 8
HELIX 142 AP7 LEU G 400 ALA G 405 1 6
HELIX 143 AP8 THR G 411 GLY G 432 1 22
SHEET 1 AA1 3 GLY A 0 ASN A 4 0
SHEET 2 AA1 3 GLN A 9 GLN A 15 -1 O GLY A 12 N MET A 1
SHEET 3 AA1 3 ILE A 49 ASP A 50 1 O ILE A 49 N HIS A 11
SHEET 1 AA211 GLY A 0 ASN A 4 0
SHEET 2 AA211 GLN A 9 GLN A 15 -1 O GLY A 12 N MET A 1
SHEET 3 AA211 LEU A 18 PRO A 25 -1 O ILE A 20 N ILE A 13
SHEET 4 AA211 TYR A 84 GLN A 90 -1 O LYS A 89 N ASP A 19
SHEET 5 AA211 ILE A 130 CYS A 134 -1 O THR A 133 N ASN A 86
SHEET 6 AA211 LYS A 97 PHE A 103 1 N TYR A 102 O ILE A 132
SHEET 7 AA211 GLY A 178 GLN A 188 1 O THR A 184 N VAL A 99
SHEET 8 AA211 LYS A 210 LEU A 214 1 O LEU A 214 N GLY A 187
SHEET 9 AA211 ILE A 293 THR A 298 1 O PHE A 294 N LEU A 213
SHEET 10 AA211 LEU A 369 PHE A 374 1 O TRP A 370 N ALA A 295
SHEET 11 AA211 ARG A 447 TYR A 449 1 O ARG A 447 N GLU A 373
SHEET 1 AA3 3 GLY B 0 THR B 5 0
SHEET 2 AA3 3 GLY B 8 GLN B 15 -1 O GLY B 12 N MET B 1
SHEET 3 AA3 3 ILE B 49 ASP B 50 1 O ILE B 49 N GLN B 9
SHEET 1 AA411 GLY B 0 THR B 5 0
SHEET 2 AA411 GLY B 8 GLN B 15 -1 O GLY B 12 N MET B 1
SHEET 3 AA411 LEU B 18 PRO B 25 -1 O ILE B 20 N ILE B 13
SHEET 4 AA411 TYR B 84 GLN B 90 -1 O LYS B 89 N ASP B 19
SHEET 5 AA411 ILE B 130 CYS B 134 -1 O THR B 133 N ASN B 86
SHEET 6 AA411 LYS B 97 PHE B 103 1 N TYR B 102 O ILE B 132
SHEET 7 AA411 GLY B 178 GLN B 188 1 O THR B 184 N VAL B 99
SHEET 8 AA411 LYS B 210 LEU B 214 1 O LEU B 214 N GLY B 187
SHEET 9 AA411 ILE B 293 THR B 298 1 O CYS B 296 N LEU B 213
SHEET 10 AA411 LEU B 369 PHE B 374 1 O TRP B 370 N ALA B 295
SHEET 11 AA411 ARG B 447 TYR B 449 1 O ARG B 447 N GLU B 373
SHEET 1 AA5 3 GLY C 0 THR C 5 0
SHEET 2 AA5 3 GLY C 8 GLN C 15 -1 O GLY C 12 N MET C 1
SHEET 3 AA5 3 ILE C 49 ASP C 50 1 O ILE C 49 N HIS C 11
SHEET 1 AA611 GLY C 0 THR C 5 0
SHEET 2 AA611 GLY C 8 GLN C 15 -1 O GLY C 12 N MET C 1
SHEET 3 AA611 LEU C 18 PRO C 25 -1 O ILE C 20 N ILE C 13
SHEET 4 AA611 TYR C 84 GLN C 90 -1 O LYS C 89 N ASP C 19
SHEET 5 AA611 ILE C 130 CYS C 134 -1 O THR C 133 N ASN C 86
SHEET 6 AA611 LYS C 97 PHE C 103 1 N PRO C 98 O ILE C 130
SHEET 7 AA611 GLY C 178 GLN C 188 1 O THR C 184 N VAL C 99
SHEET 8 AA611 LYS C 210 LEU C 214 1 O LEU C 214 N GLY C 187
SHEET 9 AA611 ILE C 293 THR C 298 1 O PHE C 294 N LEU C 213
SHEET 10 AA611 LEU C 369 PHE C 374 1 O TRP C 370 N ALA C 295
SHEET 11 AA611 ARG C 447 TYR C 449 1 O ARG C 447 N GLU C 373
SHEET 1 AA7 3 MET D 1 THR D 5 0
SHEET 2 AA7 3 GLY D 8 GLN D 15 -1 O GLY D 12 N MET D 1
SHEET 3 AA7 3 ILE D 49 ASP D 50 1 O ILE D 49 N HIS D 11
SHEET 1 AA811 MET D 1 THR D 5 0
SHEET 2 AA811 GLY D 8 GLN D 15 -1 O GLY D 12 N MET D 1
SHEET 3 AA811 LEU D 18 PRO D 25 -1 O ILE D 20 N ILE D 13
SHEET 4 AA811 TYR D 84 GLN D 90 -1 O LYS D 89 N ASP D 19
SHEET 5 AA811 ILE D 130 CYS D 134 -1 O THR D 133 N ASN D 86
SHEET 6 AA811 LYS D 97 PHE D 103 1 N ILE D 100 O ILE D 132
SHEET 7 AA811 GLY D 178 GLN D 188 1 O THR D 184 N VAL D 99
SHEET 8 AA811 LYS D 210 LEU D 214 1 O LEU D 214 N GLY D 187
SHEET 9 AA811 ILE D 293 THR D 298 1 O PHE D 294 N LEU D 213
SHEET 10 AA811 LEU D 369 PHE D 374 1 O PHE D 374 N TYR D 297
SHEET 11 AA811 ARG D 447 TYR D 449 1 O ARG D 447 N GLU D 373
SHEET 1 AA9 3 GLY E 0 THR E 5 0
SHEET 2 AA9 3 GLY E 8 GLN E 15 -1 O GLY E 12 N MET E 1
SHEET 3 AA9 3 ILE E 49 ASP E 50 1 O ILE E 49 N HIS E 11
SHEET 1 AB111 GLY E 0 THR E 5 0
SHEET 2 AB111 GLY E 8 GLN E 15 -1 O GLY E 12 N MET E 1
SHEET 3 AB111 LEU E 18 PRO E 25 -1 O ILE E 20 N ILE E 13
SHEET 4 AB111 TYR E 84 GLN E 90 -1 O LYS E 89 N ASP E 19
SHEET 5 AB111 ILE E 130 CYS E 134 -1 O THR E 133 N ASN E 86
SHEET 6 AB111 LYS E 97 PHE E 103 1 N TYR E 102 O ILE E 132
SHEET 7 AB111 GLY E 178 GLN E 188 1 O MET E 186 N ILE E 101
SHEET 8 AB111 LYS E 210 LEU E 214 1 O LEU E 214 N GLY E 187
SHEET 9 AB111 ILE E 293 THR E 298 1 O PHE E 294 N LEU E 213
SHEET 10 AB111 LEU E 369 PHE E 374 1 O TRP E 370 N ALA E 295
SHEET 11 AB111 ARG E 447 TYR E 449 1 O ARG E 447 N GLU E 373
SHEET 1 AB2 3 GLY F 0 THR F 5 0
SHEET 2 AB2 3 GLY F 8 GLN F 15 -1 O GLY F 8 N THR F 5
SHEET 3 AB2 3 ILE F 49 ASP F 50 1 O ILE F 49 N GLN F 9
SHEET 1 AB311 GLY F 0 THR F 5 0
SHEET 2 AB311 GLY F 8 GLN F 15 -1 O GLY F 8 N THR F 5
SHEET 3 AB311 LEU F 18 PRO F 25 -1 O ILE F 20 N ILE F 13
SHEET 4 AB311 TYR F 84 GLN F 90 -1 O LYS F 89 N ASP F 19
SHEET 5 AB311 ILE F 130 CYS F 134 -1 O THR F 133 N ASN F 86
SHEET 6 AB311 LYS F 97 PHE F 103 1 N ILE F 100 O ILE F 130
SHEET 7 AB311 GLY F 178 GLN F 188 1 O THR F 184 N VAL F 99
SHEET 8 AB311 LYS F 210 LEU F 214 1 O LEU F 214 N GLY F 187
SHEET 9 AB311 ILE F 293 THR F 298 1 O PHE F 294 N LEU F 213
SHEET 10 AB311 LEU F 369 PHE F 374 1 O TRP F 370 N ALA F 295
SHEET 11 AB311 ARG F 447 TYR F 449 1 O ARG F 447 N GLU F 373
SHEET 1 AB4 3 GLY G 0 THR G 5 0
SHEET 2 AB4 3 GLY G 8 GLN G 15 -1 O GLY G 12 N MET G 1
SHEET 3 AB4 3 ILE G 49 ASP G 50 1 O ILE G 49 N GLN G 9
SHEET 1 AB511 GLY G 0 THR G 5 0
SHEET 2 AB511 GLY G 8 GLN G 15 -1 O GLY G 12 N MET G 1
SHEET 3 AB511 LEU G 18 PRO G 25 -1 O ILE G 20 N ILE G 13
SHEET 4 AB511 TYR G 84 GLN G 90 -1 O LYS G 89 N ASP G 19
SHEET 5 AB511 ILE G 130 CYS G 134 -1 O THR G 133 N ASN G 86
SHEET 6 AB511 LYS G 97 PHE G 103 1 N TYR G 102 O ILE G 132
SHEET 7 AB511 GLY G 178 GLN G 188 1 O THR G 184 N VAL G 99
SHEET 8 AB511 LYS G 210 LEU G 214 1 O LEU G 214 N GLY G 187
SHEET 9 AB511 ILE G 293 THR G 298 1 O PHE G 294 N LEU G 213
SHEET 10 AB511 LEU G 369 PHE G 374 1 O TRP G 370 N ALA G 295
SHEET 11 AB511 ARG G 447 TYR G 449 1 O ARG G 447 N GLU G 373
CRYST1 313.042 313.042 185.672 90.00 90.00 90.00 I 41 2 2 112
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 0.003194 0.000000 0.000000 0.00000
SCALE2 0.000000 0.003194 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005386 0.00000
TER 3706 GLN A 450
TER 7375 GLN B 450
TER 11062 GLN C 450
TER 14727 GLN D 450
TER 18309 GLN E 450
TER 21887 GLN F 450
TER 25493 GLN G 450
MASTER 1242 0 28 143 98 0 0 625920 7 140 245
END |