HEADER DNA BINDING PROTEIN 15-FEB-18 6CFN
TITLE CRYSTAL STRUCTURE OF THE DNA-FREE GLUCOCORTICOID RECEPTOR DNA BINDING
TITLE 2 DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUCOCORTICOID RECEPTOR;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H;
COMPND 4 SYNONYM: GR,NUCLEAR RECEPTOR SUBFAMILY 3 GROUP C MEMBER 1;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: NR3C1, GRL;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PSMT3
KEYWDS DNA BINDING DOMAIN, NUCLEAR RECEPTOR, GLUCOCORTICOID RECEPTOR, DNA
KEYWDS 2 BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR F.FRANK,C.D.OKAFOR,E.A.ORTLUND
REVDAT 2 04-OCT-23 6CFN 1 REMARK
REVDAT 1 26-SEP-18 6CFN 0
JRNL AUTH F.FRANK,C.D.OKAFOR,E.A.ORTLUND
JRNL TITL THE FIRST CRYSTAL STRUCTURE OF A DNA-FREE NUCLEAR RECEPTOR
JRNL TITL 2 DNA BINDING DOMAIN SHEDS LIGHT ON DNA-DRIVEN ALLOSTERY IN
JRNL TITL 3 THE GLUCOCORTICOID RECEPTOR.
JRNL REF SCI REP V. 8 13497 2018
JRNL REFN ESSN 2045-2322
JRNL PMID 30201977
JRNL DOI 10.1038/S41598-018-31812-9
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.11.1_2575: ???)
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) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.04
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.970
REMARK 3 COMPLETENESS FOR RANGE (%) : 89.5
REMARK 3 NUMBER OF REFLECTIONS : 33027
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.197
REMARK 3 R VALUE (WORKING SET) : 0.195
REMARK 3 FREE R VALUE : 0.248
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 1654
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 36.0454 - 5.7168 0.95 2787 146 0.1861 0.2551
REMARK 3 2 5.7168 - 4.5405 0.98 2858 150 0.1618 0.1962
REMARK 3 3 4.5405 - 3.9674 0.98 2876 152 0.1423 0.1824
REMARK 3 4 3.9674 - 3.6050 0.98 2862 150 0.1745 0.2230
REMARK 3 5 3.6050 - 3.3468 0.98 2866 152 0.2085 0.2742
REMARK 3 6 3.3468 - 3.1496 0.97 2830 149 0.2228 0.2708
REMARK 3 7 3.1496 - 2.9919 0.97 2843 150 0.2293 0.3003
REMARK 3 8 2.9919 - 2.8618 0.95 2774 147 0.2634 0.3285
REMARK 3 9 2.8618 - 2.7516 0.90 2643 139 0.2636 0.2972
REMARK 3 10 2.7516 - 2.6567 0.81 2389 126 0.2704 0.3823
REMARK 3 11 2.6567 - 2.5737 0.70 2032 107 0.2769 0.3049
REMARK 3 12 2.5737 - 2.5001 0.56 1613 86 0.3016 0.3771
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) : 0.340
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.360
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 : 0.009 4663
REMARK 3 ANGLE : 1.159 6207
REMARK 3 CHIRALITY : 0.061 663
REMARK 3 PLANARITY : 0.005 795
REMARK 3 DIHEDRAL : 9.828 2895
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 44
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 419 THROUGH 429 )
REMARK 3 ORIGIN FOR THE GROUP (A): 3.0826 -9.1037 -20.9016
REMARK 3 T TENSOR
REMARK 3 T11: 0.4397 T22: 0.7531
REMARK 3 T33: 0.6157 T12: -0.0551
REMARK 3 T13: 0.0495 T23: 0.1342
REMARK 3 L TENSOR
REMARK 3 L11: 2.5993 L22: 6.5898
REMARK 3 L33: 2.3080 L12: -3.7721
REMARK 3 L13: 1.8634 L23: -1.6526
REMARK 3 S TENSOR
REMARK 3 S11: -0.0506 S12: 0.8831 S13: 1.6007
REMARK 3 S21: -0.4074 S22: 0.0159 S23: -0.1943
REMARK 3 S31: -0.9490 S32: 0.1146 S33: 0.2626
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 430 THROUGH 449 )
REMARK 3 ORIGIN FOR THE GROUP (A): 4.6878 -16.4782 -12.4939
REMARK 3 T TENSOR
REMARK 3 T11: 0.4031 T22: 0.6770
REMARK 3 T33: 0.6151 T12: 0.0667
REMARK 3 T13: 0.1623 T23: 0.1070
REMARK 3 L TENSOR
REMARK 3 L11: 5.9198 L22: 8.9884
REMARK 3 L33: 6.0514 L12: 2.0837
REMARK 3 L13: 1.0318 L23: -2.3862
REMARK 3 S TENSOR
REMARK 3 S11: -0.5107 S12: -0.7491 S13: -0.7197
REMARK 3 S21: -0.3185 S22: -0.0365 S23: -1.5165
REMARK 3 S31: 0.1124 S32: 1.4399 S33: 0.4259
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 450 THROUGH 464 )
REMARK 3 ORIGIN FOR THE GROUP (A): -10.5231 -20.7494 -11.4248
REMARK 3 T TENSOR
REMARK 3 T11: 0.4663 T22: 0.5210
REMARK 3 T33: 0.4791 T12: -0.0174
REMARK 3 T13: 0.1166 T23: -0.0036
REMARK 3 L TENSOR
REMARK 3 L11: 2.0061 L22: 7.2452
REMARK 3 L33: 5.0895 L12: 1.5996
REMARK 3 L13: -0.5683 L23: -1.5865
REMARK 3 S TENSOR
REMARK 3 S11: 0.3445 S12: -0.4796 S13: -0.2807
REMARK 3 S21: 0.2397 S22: -0.7577 S23: -0.2998
REMARK 3 S31: -0.1216 S32: 0.4789 S33: 0.1131
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 465 THROUGH 484 )
REMARK 3 ORIGIN FOR THE GROUP (A): -6.1176 -14.9201 -15.9403
REMARK 3 T TENSOR
REMARK 3 T11: 0.2966 T22: 0.5165
REMARK 3 T33: 0.3968 T12: -0.0193
REMARK 3 T13: 0.0943 T23: -0.0924
REMARK 3 L TENSOR
REMARK 3 L11: 6.1827 L22: 8.0624
REMARK 3 L33: 4.3400 L12: -0.1089
REMARK 3 L13: -1.6253 L23: -1.9174
REMARK 3 S TENSOR
REMARK 3 S11: -0.3153 S12: 0.1860 S13: -0.3876
REMARK 3 S21: -0.4798 S22: 0.1528 S23: -0.3279
REMARK 3 S31: -0.0691 S32: 0.1599 S33: 0.1606
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 485 THROUGH 498 )
REMARK 3 ORIGIN FOR THE GROUP (A): 13.0595 -24.3639 -12.8435
REMARK 3 T TENSOR
REMARK 3 T11: 0.8289 T22: 1.1685
REMARK 3 T33: 1.0553 T12: 0.1181
REMARK 3 T13: 0.3723 T23: 0.3180
REMARK 3 L TENSOR
REMARK 3 L11: 7.2808 L22: 1.9619
REMARK 3 L33: 0.3416 L12: -3.7530
REMARK 3 L13: -0.2948 L23: 0.2922
REMARK 3 S TENSOR
REMARK 3 S11: -0.3922 S12: 0.1459 S13: -1.3787
REMARK 3 S21: 0.7461 S22: -0.4937 S23: 0.4366
REMARK 3 S31: 0.1748 S32: 0.8529 S33: 0.7096
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 419 THROUGH 438 )
REMARK 3 ORIGIN FOR THE GROUP (A): 5.5423 -43.9340 -22.2968
REMARK 3 T TENSOR
REMARK 3 T11: 0.6298 T22: 0.4898
REMARK 3 T33: 0.7344 T12: 0.2165
REMARK 3 T13: 0.0861 T23: -0.1177
REMARK 3 L TENSOR
REMARK 3 L11: 7.2111 L22: 7.8024
REMARK 3 L33: 8.0904 L12: 7.3907
REMARK 3 L13: 0.3950 L23: -0.6501
REMARK 3 S TENSOR
REMARK 3 S11: 0.1959 S12: -0.2914 S13: -0.0998
REMARK 3 S21: 0.6208 S22: 0.0674 S23: -0.9575
REMARK 3 S31: 0.1775 S32: 0.0962 S33: -0.2744
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 439 THROUGH 449 )
REMARK 3 ORIGIN FOR THE GROUP (A): -4.6371 -47.5182 -18.0662
REMARK 3 T TENSOR
REMARK 3 T11: 1.0236 T22: 0.4035
REMARK 3 T33: 0.7390 T12: 0.0647
REMARK 3 T13: 0.3373 T23: 0.0524
REMARK 3 L TENSOR
REMARK 3 L11: 4.5976 L22: 7.3682
REMARK 3 L33: 8.4770 L12: 4.6703
REMARK 3 L13: -3.3196 L23: -1.0997
REMARK 3 S TENSOR
REMARK 3 S11: -0.1022 S12: -0.9225 S13: -0.2118
REMARK 3 S21: 0.2388 S22: -0.2955 S23: 0.6427
REMARK 3 S31: 1.3554 S32: 0.6566 S33: 0.3065
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 450 THROUGH 459 )
REMARK 3 ORIGIN FOR THE GROUP (A): -14.8898 -43.4037 -21.5610
REMARK 3 T TENSOR
REMARK 3 T11: 0.8849 T22: 0.4666
REMARK 3 T33: 0.6971 T12: 0.1976
REMARK 3 T13: 0.1524 T23: 0.0962
REMARK 3 L TENSOR
REMARK 3 L11: 2.4910 L22: 9.2929
REMARK 3 L33: 5.2909 L12: 2.4546
REMARK 3 L13: -0.1799 L23: -4.0016
REMARK 3 S TENSOR
REMARK 3 S11: -0.0143 S12: 0.2693 S13: -0.9721
REMARK 3 S21: 0.4836 S22: -0.3216 S23: 0.9520
REMARK 3 S31: 0.8672 S32: 0.2963 S33: 0.0517
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 460 THROUGH 464 )
REMARK 3 ORIGIN FOR THE GROUP (A): -9.5677 -30.8161 -28.0815
REMARK 3 T TENSOR
REMARK 3 T11: 0.7904 T22: 0.5110
REMARK 3 T33: 0.6831 T12: 0.1380
REMARK 3 T13: 0.3298 T23: 0.0381
REMARK 3 L TENSOR
REMARK 3 L11: 3.0738 L22: 1.2753
REMARK 3 L33: 3.9756 L12: -0.7620
REMARK 3 L13: 3.3843 L23: -1.3375
REMARK 3 S TENSOR
REMARK 3 S11: 1.8074 S12: 1.3452 S13: 1.6688
REMARK 3 S21: -0.4454 S22: -1.2559 S23: 0.0550
REMARK 3 S31: 0.8311 S32: 0.6262 S33: -0.3515
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 465 THROUGH 473 )
REMARK 3 ORIGIN FOR THE GROUP (A): -2.8361 -33.6953 -18.4551
REMARK 3 T TENSOR
REMARK 3 T11: 0.6649 T22: 0.4650
REMARK 3 T33: 0.5961 T12: 0.1412
REMARK 3 T13: 0.1426 T23: -0.0275
REMARK 3 L TENSOR
REMARK 3 L11: 4.6391 L22: 4.1652
REMARK 3 L33: 3.4329 L12: -2.8893
REMARK 3 L13: 1.7594 L23: 1.3579
REMARK 3 S TENSOR
REMARK 3 S11: -0.6187 S12: -0.7462 S13: 1.6084
REMARK 3 S21: 0.0364 S22: 0.6670 S23: -0.6964
REMARK 3 S31: -0.2728 S32: -0.1534 S33: -0.4347
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 474 THROUGH 488 )
REMARK 3 ORIGIN FOR THE GROUP (A): -5.5538 -43.8374 -26.4868
REMARK 3 T TENSOR
REMARK 3 T11: 0.7312 T22: 0.4154
REMARK 3 T33: 0.4702 T12: 0.1411
REMARK 3 T13: 0.0709 T23: -0.0409
REMARK 3 L TENSOR
REMARK 3 L11: 8.4068 L22: 8.6440
REMARK 3 L33: 4.1035 L12: -4.0292
REMARK 3 L13: -4.0701 L23: 5.7709
REMARK 3 S TENSOR
REMARK 3 S11: 0.9712 S12: 1.6017 S13: -0.8592
REMARK 3 S21: -0.9810 S22: -1.1950 S23: 0.1285
REMARK 3 S31: -0.0804 S32: -0.2802 S33: 0.0656
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 420 THROUGH 429 )
REMARK 3 ORIGIN FOR THE GROUP (A): 19.3083 -51.1648 -26.7485
REMARK 3 T TENSOR
REMARK 3 T11: 0.7251 T22: 0.5420
REMARK 3 T33: 0.8975 T12: 0.0674
REMARK 3 T13: 0.2323 T23: 0.0822
REMARK 3 L TENSOR
REMARK 3 L11: 6.0813 L22: 4.2217
REMARK 3 L33: 4.9051 L12: -4.2799
REMARK 3 L13: -0.9944 L23: 3.0521
REMARK 3 S TENSOR
REMARK 3 S11: -0.0749 S12: -0.4177 S13: 1.3588
REMARK 3 S21: 0.2198 S22: 0.4201 S23: 0.5711
REMARK 3 S31: -1.8426 S32: 0.3150 S33: -0.3567
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 430 THROUGH 438 )
REMARK 3 ORIGIN FOR THE GROUP (A): 11.2233 -52.3663 -29.8579
REMARK 3 T TENSOR
REMARK 3 T11: 0.8294 T22: 0.7214
REMARK 3 T33: 0.7234 T12: 0.2583
REMARK 3 T13: 0.1905 T23: -0.1291
REMARK 3 L TENSOR
REMARK 3 L11: 5.2245 L22: 7.5350
REMARK 3 L33: 8.7670 L12: 2.3616
REMARK 3 L13: 6.1018 L23: -0.5050
REMARK 3 S TENSOR
REMARK 3 S11: -1.5438 S12: -0.0878 S13: -0.8822
REMARK 3 S21: 1.0381 S22: 0.2974 S23: 1.5764
REMARK 3 S31: -0.6544 S32: -0.9976 S33: 0.9558
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 439 THROUGH 450 )
REMARK 3 ORIGIN FOR THE GROUP (A): 14.5808 -57.0521 -38.4225
REMARK 3 T TENSOR
REMARK 3 T11: 0.9159 T22: 0.7971
REMARK 3 T33: 0.7945 T12: 0.2044
REMARK 3 T13: -0.1216 T23: -0.1560
REMARK 3 L TENSOR
REMARK 3 L11: 4.2781 L22: 3.1287
REMARK 3 L33: 3.4877 L12: 1.8764
REMARK 3 L13: 3.5884 L23: 0.7108
REMARK 3 S TENSOR
REMARK 3 S11: 0.0862 S12: 2.7283 S13: -0.1036
REMARK 3 S21: -0.8525 S22: 0.0282 S23: 2.2353
REMARK 3 S31: -1.0970 S32: 0.2804 S33: -0.1295
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 451 THROUGH 465 )
REMARK 3 ORIGIN FOR THE GROUP (A): 22.6637 -67.8675 -34.2582
REMARK 3 T TENSOR
REMARK 3 T11: 0.2806 T22: 0.4250
REMARK 3 T33: 0.2715 T12: 0.0336
REMARK 3 T13: 0.0509 T23: 0.0707
REMARK 3 L TENSOR
REMARK 3 L11: 8.8071 L22: 8.4084
REMARK 3 L33: 8.0657 L12: 0.7321
REMARK 3 L13: 1.0297 L23: 3.4045
REMARK 3 S TENSOR
REMARK 3 S11: 0.1452 S12: -0.3062 S13: 0.2259
REMARK 3 S21: 0.2147 S22: 0.0263 S23: 0.5238
REMARK 3 S31: -0.4514 S32: -0.9616 S33: -0.0801
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 466 THROUGH 487 )
REMARK 3 ORIGIN FOR THE GROUP (A): 20.6033 -60.8749 -31.0949
REMARK 3 T TENSOR
REMARK 3 T11: 0.4261 T22: 0.3631
REMARK 3 T33: 0.3969 T12: 0.0846
REMARK 3 T13: 0.0930 T23: -0.0473
REMARK 3 L TENSOR
REMARK 3 L11: 6.9827 L22: 7.7414
REMARK 3 L33: 6.9436 L12: -4.5299
REMARK 3 L13: -1.9053 L23: 2.2283
REMARK 3 S TENSOR
REMARK 3 S11: 0.1263 S12: -0.8031 S13: -0.0092
REMARK 3 S21: 0.6936 S22: -0.1338 S23: 0.7112
REMARK 3 S31: -0.5240 S32: 0.1120 S33: 0.0072
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 488 THROUGH 500 )
REMARK 3 ORIGIN FOR THE GROUP (A): -0.7856 -52.9451 -35.3860
REMARK 3 T TENSOR
REMARK 3 T11: 0.7750 T22: 1.0550
REMARK 3 T33: 1.0833 T12: 0.2050
REMARK 3 T13: -0.1171 T23: -0.3485
REMARK 3 L TENSOR
REMARK 3 L11: 6.9627 L22: 3.1861
REMARK 3 L33: 5.1728 L12: -4.4075
REMARK 3 L13: 0.6465 L23: 0.6623
REMARK 3 S TENSOR
REMARK 3 S11: 0.2928 S12: 1.2753 S13: -1.3266
REMARK 3 S21: -0.4238 S22: -0.3402 S23: 1.3755
REMARK 3 S31: 0.1711 S32: 0.6600 S33: -0.1344
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 420 THROUGH 429 )
REMARK 3 ORIGIN FOR THE GROUP (A): 19.9128 -10.4482 -25.3482
REMARK 3 T TENSOR
REMARK 3 T11: 0.5494 T22: 0.6385
REMARK 3 T33: 0.7831 T12: 0.0546
REMARK 3 T13: 0.1929 T23: 0.0831
REMARK 3 L TENSOR
REMARK 3 L11: 4.8691 L22: 6.3994
REMARK 3 L33: 9.2125 L12: 4.4412
REMARK 3 L13: 1.4185 L23: 5.8198
REMARK 3 S TENSOR
REMARK 3 S11: 0.1638 S12: -0.0482 S13: 0.7435
REMARK 3 S21: -0.8555 S22: -0.4567 S23: 0.6070
REMARK 3 S31: -0.6186 S32: -0.4952 S33: 0.2320
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 430 THROUGH 438 )
REMARK 3 ORIGIN FOR THE GROUP (A): 15.5829 -18.0145 -24.2258
REMARK 3 T TENSOR
REMARK 3 T11: 0.4310 T22: 0.7699
REMARK 3 T33: 0.8292 T12: -0.0633
REMARK 3 T13: 0.1657 T23: 0.0731
REMARK 3 L TENSOR
REMARK 3 L11: 5.8983 L22: 9.2476
REMARK 3 L33: 7.2240 L12: -0.0801
REMARK 3 L13: 5.1516 L23: -2.4572
REMARK 3 S TENSOR
REMARK 3 S11: -0.3474 S12: 0.2237 S13: -1.2360
REMARK 3 S21: -0.2544 S22: -0.1169 S23: 1.6713
REMARK 3 S31: 1.0998 S32: -1.4166 S33: 0.2801
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 439 THROUGH 451 )
REMARK 3 ORIGIN FOR THE GROUP (A): 22.9439 -24.1702 -29.1595
REMARK 3 T TENSOR
REMARK 3 T11: 0.5643 T22: 0.6510
REMARK 3 T33: 0.7681 T12: -0.1054
REMARK 3 T13: 0.1036 T23: -0.1664
REMARK 3 L TENSOR
REMARK 3 L11: 3.8957 L22: 8.2150
REMARK 3 L33: 3.8595 L12: -4.1797
REMARK 3 L13: 3.8406 L23: -4.6073
REMARK 3 S TENSOR
REMARK 3 S11: 0.1577 S12: 1.1053 S13: -1.2871
REMARK 3 S21: -1.2916 S22: -0.5691 S23: 0.6553
REMARK 3 S31: 1.4331 S32: -0.5992 S33: 0.2677
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 452 THROUGH 461 )
REMARK 3 ORIGIN FOR THE GROUP (A): 36.1624 -23.8381 -23.0230
REMARK 3 T TENSOR
REMARK 3 T11: 0.4277 T22: 0.4669
REMARK 3 T33: 0.4731 T12: 0.0456
REMARK 3 T13: 0.1054 T23: -0.0932
REMARK 3 L TENSOR
REMARK 3 L11: 6.4193 L22: 5.7251
REMARK 3 L33: 7.7799 L12: 3.8778
REMARK 3 L13: 1.8359 L23: 0.0962
REMARK 3 S TENSOR
REMARK 3 S11: -0.1212 S12: -0.6722 S13: -0.5361
REMARK 3 S21: -0.5388 S22: -0.5393 S23: -0.2710
REMARK 3 S31: 0.5842 S32: -0.4319 S33: 0.5671
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 462 THROUGH 466 )
REMARK 3 ORIGIN FOR THE GROUP (A): 33.2732 -11.4748 -22.4414
REMARK 3 T TENSOR
REMARK 3 T11: 0.6249 T22: 0.7347
REMARK 3 T33: 0.6423 T12: -0.0632
REMARK 3 T13: 0.2171 T23: -0.1733
REMARK 3 L TENSOR
REMARK 3 L11: 3.6945 L22: 2.8298
REMARK 3 L33: 8.5215 L12: -1.0978
REMARK 3 L13: -4.7793 L23: -0.3898
REMARK 3 S TENSOR
REMARK 3 S11: 0.7138 S12: -1.6414 S13: 0.9090
REMARK 3 S21: 0.5473 S22: 0.0831 S23: 0.5779
REMARK 3 S31: -1.9511 S32: 0.8014 S33: -0.0507
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 467 THROUGH 473 )
REMARK 3 ORIGIN FOR THE GROUP (A): 31.3722 -12.0604 -29.6342
REMARK 3 T TENSOR
REMARK 3 T11: 0.5052 T22: 0.6572
REMARK 3 T33: 0.5309 T12: 0.0330
REMARK 3 T13: 0.2216 T23: -0.0347
REMARK 3 L TENSOR
REMARK 3 L11: 9.4427 L22: 6.6576
REMARK 3 L33: 4.4679 L12: -3.0246
REMARK 3 L13: 0.1696 L23: -0.9547
REMARK 3 S TENSOR
REMARK 3 S11: 0.5539 S12: 1.5797 S13: 0.2971
REMARK 3 S21: -0.5877 S22: -0.4024 S23: -0.1684
REMARK 3 S31: -0.1108 S32: 0.0455 S33: -0.0768
REMARK 3 TLS GROUP : 24
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 474 THROUGH 487 )
REMARK 3 ORIGIN FOR THE GROUP (A): 26.4869 -20.4621 -20.5167
REMARK 3 T TENSOR
REMARK 3 T11: 0.4101 T22: 0.5108
REMARK 3 T33: 0.5258 T12: -0.0487
REMARK 3 T13: 0.1653 T23: 0.0120
REMARK 3 L TENSOR
REMARK 3 L11: 8.8142 L22: 6.8349
REMARK 3 L33: 6.3960 L12: -1.9485
REMARK 3 L13: -2.1304 L23: -1.3052
REMARK 3 S TENSOR
REMARK 3 S11: -0.6574 S12: -1.3972 S13: -1.0412
REMARK 3 S21: 0.3114 S22: 0.2480 S23: 0.6835
REMARK 3 S31: 0.4088 S32: -0.4973 S33: 0.2732
REMARK 3 TLS GROUP : 25
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 419 THROUGH 429 )
REMARK 3 ORIGIN FOR THE GROUP (A): 43.0748 -33.1099 -42.1209
REMARK 3 T TENSOR
REMARK 3 T11: 1.0006 T22: 0.5027
REMARK 3 T33: 0.7259 T12: 0.0860
REMARK 3 T13: 0.1843 T23: -0.1344
REMARK 3 L TENSOR
REMARK 3 L11: 4.2885 L22: 8.3817
REMARK 3 L33: 3.2936 L12: -5.4485
REMARK 3 L13: -1.9431 L23: 4.0348
REMARK 3 S TENSOR
REMARK 3 S11: 0.1633 S12: -0.2885 S13: -0.9400
REMARK 3 S21: 0.5297 S22: -0.1876 S23: -0.0495
REMARK 3 S31: 1.8690 S32: -0.1148 S33: -0.0954
REMARK 3 TLS GROUP : 26
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 430 THROUGH 449 )
REMARK 3 ORIGIN FOR THE GROUP (A): 37.2122 -24.2980 -45.5882
REMARK 3 T TENSOR
REMARK 3 T11: 0.9178 T22: 0.6600
REMARK 3 T33: 0.4687 T12: 0.0863
REMARK 3 T13: 0.0254 T23: -0.1483
REMARK 3 L TENSOR
REMARK 3 L11: 9.5988 L22: 2.8560
REMARK 3 L33: 6.4979 L12: 3.3781
REMARK 3 L13: 3.4092 L23: -1.5345
REMARK 3 S TENSOR
REMARK 3 S11: -0.0255 S12: 1.4250 S13: -1.0003
REMARK 3 S21: -2.0666 S22: -0.2626 S23: -0.1072
REMARK 3 S31: -1.1514 S32: -1.3519 S33: 0.2371
REMARK 3 TLS GROUP : 27
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 450 THROUGH 464 )
REMARK 3 ORIGIN FOR THE GROUP (A): 40.7383 -15.1772 -33.3045
REMARK 3 T TENSOR
REMARK 3 T11: 0.5284 T22: 0.5268
REMARK 3 T33: 0.2843 T12: 0.0706
REMARK 3 T13: 0.0506 T23: 0.0130
REMARK 3 L TENSOR
REMARK 3 L11: 8.0356 L22: 6.0861
REMARK 3 L33: 3.7321 L12: 2.8548
REMARK 3 L13: -1.0427 L23: 3.9352
REMARK 3 S TENSOR
REMARK 3 S11: -0.2086 S12: 1.2946 S13: 0.2766
REMARK 3 S21: -1.0122 S22: -0.3127 S23: 0.3622
REMARK 3 S31: -0.3201 S32: -0.1548 S33: 0.7358
REMARK 3 TLS GROUP : 28
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 465 THROUGH 483 )
REMARK 3 ORIGIN FOR THE GROUP (A): 41.9075 -23.2866 -35.0760
REMARK 3 T TENSOR
REMARK 3 T11: 0.7137 T22: 0.4182
REMARK 3 T33: 0.3153 T12: 0.0917
REMARK 3 T13: 0.1638 T23: -0.0390
REMARK 3 L TENSOR
REMARK 3 L11: 7.2147 L22: 4.2558
REMARK 3 L33: 7.9223 L12: 0.6121
REMARK 3 L13: -0.8406 L23: -1.2414
REMARK 3 S TENSOR
REMARK 3 S11: -0.3286 S12: 0.0674 S13: -0.9832
REMARK 3 S21: -1.1065 S22: -0.4265 S23: -0.9465
REMARK 3 S31: 0.9643 S32: 0.3401 S33: 0.6466
REMARK 3 TLS GROUP : 29
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 484 THROUGH 497 )
REMARK 3 ORIGIN FOR THE GROUP (A): 38.7110 -19.7302 -55.3625
REMARK 3 T TENSOR
REMARK 3 T11: 1.2468 T22: 0.8858
REMARK 3 T33: 0.6620 T12: 0.2810
REMARK 3 T13: 0.2044 T23: -0.0591
REMARK 3 L TENSOR
REMARK 3 L11: 1.4073 L22: 2.4410
REMARK 3 L33: 2.4549 L12: -1.5045
REMARK 3 L13: 1.7157 L23: -1.7125
REMARK 3 S TENSOR
REMARK 3 S11: 0.0502 S12: -0.2330 S13: -0.0958
REMARK 3 S21: -0.2621 S22: 0.3172 S23: 0.6038
REMARK 3 S31: -1.8860 S32: 0.5945 S33: -0.4835
REMARK 3 TLS GROUP : 30
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 418 THROUGH 449 )
REMARK 3 ORIGIN FOR THE GROUP (A): 45.8174 -39.8620 -2.4227
REMARK 3 T TENSOR
REMARK 3 T11: 0.8373 T22: 0.6640
REMARK 3 T33: 0.6074 T12: -0.1129
REMARK 3 T13: 0.2989 T23: 0.0757
REMARK 3 L TENSOR
REMARK 3 L11: 6.8169 L22: 5.1505
REMARK 3 L33: 5.9441 L12: 0.0357
REMARK 3 L13: 1.5674 L23: -0.8054
REMARK 3 S TENSOR
REMARK 3 S11: 0.0628 S12: -0.5193 S13: -0.5790
REMARK 3 S21: 0.3530 S22: 0.0400 S23: 0.2710
REMARK 3 S31: 0.4552 S32: 0.1435 S33: -0.1649
REMARK 3 TLS GROUP : 31
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 450 THROUGH 454 )
REMARK 3 ORIGIN FOR THE GROUP (A): 61.3004 -32.2555 -6.7372
REMARK 3 T TENSOR
REMARK 3 T11: 0.8706 T22: 1.4069
REMARK 3 T33: 1.0766 T12: -0.0985
REMARK 3 T13: 0.2644 T23: 0.2578
REMARK 3 L TENSOR
REMARK 3 L11: 3.9907 L22: 4.5752
REMARK 3 L33: 3.5215 L12: -3.7108
REMARK 3 L13: 3.4211 L23: -3.5357
REMARK 3 S TENSOR
REMARK 3 S11: 0.5733 S12: -2.9643 S13: 1.5876
REMARK 3 S21: -0.4035 S22: 1.5542 S23: -0.2843
REMARK 3 S31: 0.5359 S32: 0.5196 S33: -2.5748
REMARK 3 TLS GROUP : 32
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 455 THROUGH 464 )
REMARK 3 ORIGIN FOR THE GROUP (A): 49.7526 -28.4765 -17.5338
REMARK 3 T TENSOR
REMARK 3 T11: 0.4499 T22: 0.4236
REMARK 3 T33: 0.5644 T12: -0.0021
REMARK 3 T13: 0.2513 T23: 0.0304
REMARK 3 L TENSOR
REMARK 3 L11: 9.4280 L22: 5.3118
REMARK 3 L33: 6.1796 L12: 0.3033
REMARK 3 L13: 3.4481 L23: 3.3258
REMARK 3 S TENSOR
REMARK 3 S11: -1.4025 S12: 0.5412 S13: 0.2034
REMARK 3 S21: -0.7833 S22: 0.0745 S23: 0.1095
REMARK 3 S31: 0.4251 S32: -0.7413 S33: 0.6902
REMARK 3 TLS GROUP : 33
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 465 THROUGH 484 )
REMARK 3 ORIGIN FOR THE GROUP (A): 47.0221 -34.8308 -11.5428
REMARK 3 T TENSOR
REMARK 3 T11: 0.3535 T22: 0.4691
REMARK 3 T33: 0.4500 T12: 0.1432
REMARK 3 T13: 0.1518 T23: 0.0037
REMARK 3 L TENSOR
REMARK 3 L11: 6.7409 L22: 8.3538
REMARK 3 L33: 8.0890 L12: 6.7412
REMARK 3 L13: -1.6866 L23: -4.3568
REMARK 3 S TENSOR
REMARK 3 S11: -0.1009 S12: -0.3522 S13: 0.0049
REMARK 3 S21: -0.0375 S22: -0.6159 S23: 0.9358
REMARK 3 S31: 0.0591 S32: -0.3589 S33: 0.4691
REMARK 3 TLS GROUP : 34
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 485 THROUGH 495 )
REMARK 3 ORIGIN FOR THE GROUP (A): 51.8747 -34.3509 7.6559
REMARK 3 T TENSOR
REMARK 3 T11: 0.8712 T22: 1.1065
REMARK 3 T33: 0.7926 T12: -0.0566
REMARK 3 T13: 0.2025 T23: -0.0471
REMARK 3 L TENSOR
REMARK 3 L11: 3.9040 L22: 0.6803
REMARK 3 L33: 9.4149 L12: 0.5950
REMARK 3 L13: 3.6070 L23: -0.6615
REMARK 3 S TENSOR
REMARK 3 S11: -0.6709 S12: -0.3983 S13: -1.2973
REMARK 3 S21: 0.0527 S22: 0.7901 S23: -1.4312
REMARK 3 S31: -0.9860 S32: 0.5838 S33: 0.3340
REMARK 3 TLS GROUP : 35
REMARK 3 SELECTION: CHAIN 'G' AND (RESID 418 THROUGH 429 )
REMARK 3 ORIGIN FOR THE GROUP (A): 43.5852 -38.9572 -57.3976
REMARK 3 T TENSOR
REMARK 3 T11: 1.0869 T22: 0.5125
REMARK 3 T33: 0.4521 T12: -0.0188
REMARK 3 T13: 0.2356 T23: -0.0386
REMARK 3 L TENSOR
REMARK 3 L11: 7.3371 L22: 9.3468
REMARK 3 L33: 2.9100 L12: 3.6949
REMARK 3 L13: -4.6199 L23: -2.2178
REMARK 3 S TENSOR
REMARK 3 S11: 0.0450 S12: 0.1197 S13: -0.8213
REMARK 3 S21: 0.6084 S22: -0.4461 S23: 0.1927
REMARK 3 S31: -0.6299 S32: 0.5093 S33: 0.5817
REMARK 3 TLS GROUP : 36
REMARK 3 SELECTION: CHAIN 'G' AND (RESID 430 THROUGH 438 )
REMARK 3 ORIGIN FOR THE GROUP (A): 46.2718 -30.3741 -57.2977
REMARK 3 T TENSOR
REMARK 3 T11: 0.9186 T22: 0.8345
REMARK 3 T33: 0.5048 T12: 0.0390
REMARK 3 T13: 0.2069 T23: -0.2286
REMARK 3 L TENSOR
REMARK 3 L11: 1.4641 L22: 8.7876
REMARK 3 L33: 3.4497 L12: 0.0535
REMARK 3 L13: 0.0068 L23: -5.4226
REMARK 3 S TENSOR
REMARK 3 S11: -0.1953 S12: -1.2003 S13: 0.8907
REMARK 3 S21: 2.0896 S22: 0.0150 S23: -0.5904
REMARK 3 S31: -1.1131 S32: 0.1971 S33: -0.2149
REMARK 3 TLS GROUP : 37
REMARK 3 SELECTION: CHAIN 'G' AND (RESID 439 THROUGH 450 )
REMARK 3 ORIGIN FOR THE GROUP (A): 51.3949 -29.0649 -66.3062
REMARK 3 T TENSOR
REMARK 3 T11: 0.8124 T22: 0.7481
REMARK 3 T33: 0.8316 T12: -0.0706
REMARK 3 T13: 0.1897 T23: -0.2617
REMARK 3 L TENSOR
REMARK 3 L11: 2.1263 L22: 2.2942
REMARK 3 L33: 7.5522 L12: 0.4719
REMARK 3 L13: 0.6101 L23: -3.7144
REMARK 3 S TENSOR
REMARK 3 S11: 0.3382 S12: -1.1828 S13: 1.1498
REMARK 3 S21: -1.6336 S22: -0.0873 S23: -1.1007
REMARK 3 S31: -0.5396 S32: 1.8094 S33: -0.1317
REMARK 3 TLS GROUP : 38
REMARK 3 SELECTION: CHAIN 'G' AND (RESID 451 THROUGH 455 )
REMARK 3 ORIGIN FOR THE GROUP (A): 49.3325 -25.4776 -75.9942
REMARK 3 T TENSOR
REMARK 3 T11: 0.6894 T22: 0.6053
REMARK 3 T33: 0.5264 T12: -0.1057
REMARK 3 T13: 0.1092 T23: -0.0169
REMARK 3 L TENSOR
REMARK 3 L11: 6.4459 L22: 1.9690
REMARK 3 L33: 6.2567 L12: -0.7166
REMARK 3 L13: 3.1760 L23: -2.4200
REMARK 3 S TENSOR
REMARK 3 S11: -0.9432 S12: 1.2757 S13: 0.3731
REMARK 3 S21: -0.5396 S22: 0.2854 S23: -0.5360
REMARK 3 S31: -0.9159 S32: -0.4160 S33: 0.6986
REMARK 3 TLS GROUP : 39
REMARK 3 SELECTION: CHAIN 'G' AND (RESID 456 THROUGH 465 )
REMARK 3 ORIGIN FOR THE GROUP (A): 38.0018 -36.8493 -77.0500
REMARK 3 T TENSOR
REMARK 3 T11: 0.5807 T22: 0.6671
REMARK 3 T33: 0.5227 T12: -0.0364
REMARK 3 T13: 0.1581 T23: -0.1488
REMARK 3 L TENSOR
REMARK 3 L11: 3.3159 L22: 3.8787
REMARK 3 L33: 9.6053 L12: -1.6996
REMARK 3 L13: -1.6069 L23: -4.3424
REMARK 3 S TENSOR
REMARK 3 S11: -0.3240 S12: 0.1036 S13: -0.1244
REMARK 3 S21: 0.2462 S22: -0.1252 S23: 0.1283
REMARK 3 S31: 0.4216 S32: -2.1291 S33: 0.0703
REMARK 3 TLS GROUP : 40
REMARK 3 SELECTION: CHAIN 'G' AND (RESID 466 THROUGH 487 )
REMARK 3 ORIGIN FOR THE GROUP (A): 43.2385 -34.7836 -68.7050
REMARK 3 T TENSOR
REMARK 3 T11: 0.6250 T22: 0.5814
REMARK 3 T33: 0.4370 T12: -0.0711
REMARK 3 T13: 0.1691 T23: -0.2064
REMARK 3 L TENSOR
REMARK 3 L11: 8.9160 L22: 7.1816
REMARK 3 L33: 3.4107 L12: -4.1569
REMARK 3 L13: 0.3615 L23: 0.3144
REMARK 3 S TENSOR
REMARK 3 S11: -0.6046 S12: -0.3162 S13: -0.1290
REMARK 3 S21: 0.9907 S22: 0.2375 S23: 0.7633
REMARK 3 S31: -0.1057 S32: -0.0453 S33: 0.3236
REMARK 3 TLS GROUP : 41
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 419 THROUGH 438 )
REMARK 3 ORIGIN FOR THE GROUP (A): 36.6896 -41.8884 10.7001
REMARK 3 T TENSOR
REMARK 3 T11: 0.8315 T22: 0.7383
REMARK 3 T33: 0.5380 T12: -0.0310
REMARK 3 T13: 0.2257 T23: 0.0870
REMARK 3 L TENSOR
REMARK 3 L11: 5.7842 L22: 8.4759
REMARK 3 L33: 8.6861 L12: 1.2140
REMARK 3 L13: 1.4515 L23: 2.9478
REMARK 3 S TENSOR
REMARK 3 S11: 0.0518 S12: 0.1878 S13: 0.3243
REMARK 3 S21: -1.2217 S22: -0.0020 S23: 0.3972
REMARK 3 S31: -0.2843 S32: -0.5824 S33: 0.0464
REMARK 3 TLS GROUP : 42
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 439 THROUGH 451 )
REMARK 3 ORIGIN FOR THE GROUP (A): 36.2620 -32.9082 19.9317
REMARK 3 T TENSOR
REMARK 3 T11: 1.1563 T22: 0.6030
REMARK 3 T33: 0.8816 T12: -0.0953
REMARK 3 T13: 0.3388 T23: 0.0725
REMARK 3 L TENSOR
REMARK 3 L11: 4.0348 L22: 7.9593
REMARK 3 L33: 3.6265 L12: 0.8920
REMARK 3 L13: 3.4562 L23: -1.3880
REMARK 3 S TENSOR
REMARK 3 S11: 0.4316 S12: -0.1756 S13: 1.4921
REMARK 3 S21: 0.5301 S22: -0.6597 S23: -0.1018
REMARK 3 S31: -1.4373 S32: 0.0154 S33: 0.1036
REMARK 3 TLS GROUP : 43
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 452 THROUGH 461 )
REMARK 3 ORIGIN FOR THE GROUP (A): 40.8250 -40.4440 31.4533
REMARK 3 T TENSOR
REMARK 3 T11: 0.7493 T22: 0.7720
REMARK 3 T33: 0.7059 T12: 0.0248
REMARK 3 T13: 0.1562 T23: 0.1218
REMARK 3 L TENSOR
REMARK 3 L11: 4.9244 L22: 2.1540
REMARK 3 L33: 3.6572 L12: -3.2339
REMARK 3 L13: 4.2001 L23: -2.7253
REMARK 3 S TENSOR
REMARK 3 S11: 0.0073 S12: 0.3574 S13: 0.0484
REMARK 3 S21: 0.1353 S22: -1.0457 S23: -0.5644
REMARK 3 S31: -0.3097 S32: 1.1853 S33: 1.2529
REMARK 3 TLS GROUP : 44
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 462 THROUGH 487 )
REMARK 3 ORIGIN FOR THE GROUP (A): 38.1457 -44.0698 22.3766
REMARK 3 T TENSOR
REMARK 3 T11: 0.6610 T22: 0.5750
REMARK 3 T33: 0.5719 T12: -0.0392
REMARK 3 T13: 0.2699 T23: 0.0881
REMARK 3 L TENSOR
REMARK 3 L11: 2.9000 L22: 7.2026
REMARK 3 L33: 5.1181 L12: 1.6979
REMARK 3 L13: 0.4194 L23: 0.9498
REMARK 3 S TENSOR
REMARK 3 S11: -0.4261 S12: 0.7748 S13: -0.7611
REMARK 3 S21: 0.2038 S22: 0.2564 S23: -0.4301
REMARK 3 S31: 0.5368 S32: 0.0493 S33: 0.3184
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 6CFN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-FEB-18.
REMARK 100 THE DEPOSITION ID IS D_1000232664.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-MAR-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 33141
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 36.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 89.5
REMARK 200 DATA REDUNDANCY : 2.400
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 56.9
REMARK 200 DATA REDUNDANCY IN SHELL : 1.40
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.300
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: 4HN5
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG3350, 50 MM TRIS PH8.5, AND 200
REMARK 280 MM DI-SODIUM TARTRATE, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6, 7, 8
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 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 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 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 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 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 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 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 350
REMARK 350 BIOMOLECULE: 8
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: H
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 SER A 417
REMARK 465 PRO A 418
REMARK 465 GLY A 499
REMARK 465 ILE A 500
REMARK 465 GLN A 501
REMARK 465 GLN A 502
REMARK 465 ALA A 503
REMARK 465 THR A 504
REMARK 465 THR A 505
REMARK 465 GLY A 506
REMARK 465 SER B 417
REMARK 465 PRO B 418
REMARK 465 GLU B 489
REMARK 465 ALA B 490
REMARK 465 ARG B 491
REMARK 465 LYS B 492
REMARK 465 THR B 493
REMARK 465 LYS B 494
REMARK 465 LYS B 495
REMARK 465 LYS B 496
REMARK 465 ILE B 497
REMARK 465 LYS B 498
REMARK 465 GLY B 499
REMARK 465 ILE B 500
REMARK 465 GLN B 501
REMARK 465 GLN B 502
REMARK 465 ALA B 503
REMARK 465 THR B 504
REMARK 465 THR B 505
REMARK 465 GLY B 506
REMARK 465 SER C 417
REMARK 465 PRO C 418
REMARK 465 LYS C 419
REMARK 465 GLN C 501
REMARK 465 GLN C 502
REMARK 465 ALA C 503
REMARK 465 THR C 504
REMARK 465 THR C 505
REMARK 465 GLY C 506
REMARK 465 SER D 417
REMARK 465 PRO D 418
REMARK 465 LYS D 419
REMARK 465 LEU D 488
REMARK 465 GLU D 489
REMARK 465 ALA D 490
REMARK 465 ARG D 491
REMARK 465 LYS D 492
REMARK 465 THR D 493
REMARK 465 LYS D 494
REMARK 465 LYS D 495
REMARK 465 LYS D 496
REMARK 465 ILE D 497
REMARK 465 LYS D 498
REMARK 465 GLY D 499
REMARK 465 ILE D 500
REMARK 465 GLN D 501
REMARK 465 GLN D 502
REMARK 465 ALA D 503
REMARK 465 THR D 504
REMARK 465 THR D 505
REMARK 465 GLY D 506
REMARK 465 SER E 417
REMARK 465 PRO E 418
REMARK 465 LYS E 498
REMARK 465 GLY E 499
REMARK 465 ILE E 500
REMARK 465 GLN E 501
REMARK 465 GLN E 502
REMARK 465 ALA E 503
REMARK 465 THR E 504
REMARK 465 THR E 505
REMARK 465 GLY E 506
REMARK 465 SER F 417
REMARK 465 LYS F 496
REMARK 465 ILE F 497
REMARK 465 LYS F 498
REMARK 465 GLY F 499
REMARK 465 ILE F 500
REMARK 465 GLN F 501
REMARK 465 GLN F 502
REMARK 465 ALA F 503
REMARK 465 THR F 504
REMARK 465 THR F 505
REMARK 465 GLY F 506
REMARK 465 SER G 417
REMARK 465 LEU G 488
REMARK 465 GLU G 489
REMARK 465 ALA G 490
REMARK 465 ARG G 491
REMARK 465 LYS G 492
REMARK 465 THR G 493
REMARK 465 LYS G 494
REMARK 465 LYS G 495
REMARK 465 LYS G 496
REMARK 465 ILE G 497
REMARK 465 LYS G 498
REMARK 465 GLY G 499
REMARK 465 ILE G 500
REMARK 465 GLN G 501
REMARK 465 GLN G 502
REMARK 465 ALA G 503
REMARK 465 THR G 504
REMARK 465 THR G 505
REMARK 465 GLY G 506
REMARK 465 SER H 417
REMARK 465 PRO H 418
REMARK 465 LEU H 488
REMARK 465 GLU H 489
REMARK 465 ALA H 490
REMARK 465 ARG H 491
REMARK 465 LYS H 492
REMARK 465 THR H 493
REMARK 465 LYS H 494
REMARK 465 LYS H 495
REMARK 465 LYS H 496
REMARK 465 ILE H 497
REMARK 465 LYS H 498
REMARK 465 GLY H 499
REMARK 465 ILE H 500
REMARK 465 GLN H 501
REMARK 465 GLN H 502
REMARK 465 ALA H 503
REMARK 465 THR H 504
REMARK 465 THR H 505
REMARK 465 GLY H 506
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 VAL A 449 NE2 GLN A 452 2.18
REMARK 500 ND2 ASN E 461 O HOH E 701 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 NH1 ARG C 479 O CYS E 457 1545 2.10
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 CYS E 424 CB CYS E 424 SG -0.106
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASN A 454 49.40 -87.63
REMARK 500 CYS A 473 87.53 -153.67
REMARK 500 GLN B 452 107.15 -54.36
REMARK 500 LYS C 498 2.66 -59.88
REMARK 500 ASP E 426 -177.46 -64.33
REMARK 500 GLN E 452 88.66 -67.80
REMARK 500 ARG E 470 -59.75 -24.76
REMARK 500 LYS F 419 -24.92 -142.01
REMARK 500 ASN F 454 34.07 -49.31
REMARK 500 TYR F 455 105.98 -52.68
REMARK 500 ARG F 470 157.99 -49.63
REMARK 500 LYS F 471 -23.80 80.20
REMARK 500 ASN F 487 141.95 -171.93
REMARK 500 LYS F 492 -75.11 -32.15
REMARK 500 ASN G 454 62.24 -118.13
REMARK 500 ASN G 461 30.18 70.63
REMARK 500 GLN H 452 77.61 35.89
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 LYS E 492 THR E 493 148.92
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 601 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 421 SG
REMARK 620 2 CYS A 424 SG 112.1
REMARK 620 3 CYS A 438 SG 110.2 114.5
REMARK 620 4 CYS A 441 SG 104.7 115.8 98.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 602 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 457 SG
REMARK 620 2 CYS A 463 SG 119.7
REMARK 620 3 CYS A 473 SG 118.1 107.9
REMARK 620 4 CYS A 476 SG 109.2 93.2 104.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 601 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 421 SG
REMARK 620 2 CYS B 424 SG 102.5
REMARK 620 3 CYS B 438 SG 119.2 115.7
REMARK 620 4 CYS B 441 SG 109.0 119.0 92.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 602 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 457 SG
REMARK 620 2 CYS B 463 SG 119.7
REMARK 620 3 CYS B 473 SG 111.2 113.2
REMARK 620 4 CYS B 476 SG 106.1 95.1 109.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C 601 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 421 SG
REMARK 620 2 CYS C 424 SG 118.0
REMARK 620 3 CYS C 438 SG 106.5 112.5
REMARK 620 4 CYS C 441 SG 108.2 119.4 87.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C 602 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 457 SG
REMARK 620 2 CYS C 463 SG 112.1
REMARK 620 3 CYS C 473 SG 114.6 118.2
REMARK 620 4 CYS C 476 SG 99.2 105.2 104.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D 601 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 421 SG
REMARK 620 2 CYS D 424 SG 107.8
REMARK 620 3 CYS D 438 SG 112.3 105.0
REMARK 620 4 CYS D 441 SG 106.8 121.9 103.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D 602 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 457 SG
REMARK 620 2 CYS D 463 SG 103.1
REMARK 620 3 CYS D 473 SG 119.2 117.9
REMARK 620 4 CYS D 476 SG 99.1 105.5 109.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN E 601 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS E 421 SG
REMARK 620 2 CYS E 424 SG 113.5
REMARK 620 3 CYS E 438 SG 112.8 111.5
REMARK 620 4 CYS E 441 SG 105.6 116.7 95.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN E 602 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS E 457 SG
REMARK 620 2 CYS E 463 SG 118.3
REMARK 620 3 CYS E 473 SG 119.1 105.9
REMARK 620 4 CYS E 476 SG 106.7 101.1 103.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN F 601 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS F 421 SG
REMARK 620 2 CYS F 424 SG 107.8
REMARK 620 3 CYS F 438 SG 115.9 108.0
REMARK 620 4 CYS F 441 SG 110.9 117.8 96.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN F 602 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS F 457 SG
REMARK 620 2 CYS F 463 SG 114.2
REMARK 620 3 CYS F 473 SG 117.6 110.8
REMARK 620 4 CYS F 476 SG 113.5 95.8 102.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN G 601 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS G 421 SG
REMARK 620 2 CYS G 424 SG 110.4
REMARK 620 3 CYS G 438 SG 115.4 115.9
REMARK 620 4 CYS G 441 SG 97.3 115.9 100.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN G 602 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS G 457 SG
REMARK 620 2 CYS G 463 SG 111.7
REMARK 620 3 CYS G 473 SG 116.8 117.8
REMARK 620 4 CYS G 476 SG 101.0 100.8 105.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN H 601 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS H 421 SG
REMARK 620 2 CYS H 424 SG 99.9
REMARK 620 3 CYS H 438 SG 112.4 100.0
REMARK 620 4 CYS H 441 SG 120.7 120.7 101.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN H 602 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS H 457 SG
REMARK 620 2 CYS H 463 SG 112.5
REMARK 620 3 CYS H 473 SG 113.3 120.2
REMARK 620 4 CYS H 476 SG 98.8 105.1 103.7
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN C 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN C 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN D 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN D 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN E 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN E 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN F 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN F 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN G 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN G 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN H 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN H 602
DBREF 6CFN A 418 506 UNP P04150 GCR_HUMAN 418 506
DBREF 6CFN B 418 506 UNP P04150 GCR_HUMAN 418 506
DBREF 6CFN C 418 506 UNP P04150 GCR_HUMAN 418 506
DBREF 6CFN D 418 506 UNP P04150 GCR_HUMAN 418 506
DBREF 6CFN E 418 506 UNP P04150 GCR_HUMAN 418 506
DBREF 6CFN F 418 506 UNP P04150 GCR_HUMAN 418 506
DBREF 6CFN G 418 506 UNP P04150 GCR_HUMAN 418 506
DBREF 6CFN H 418 506 UNP P04150 GCR_HUMAN 418 506
SEQADV 6CFN SER A 417 UNP P04150 EXPRESSION TAG
SEQADV 6CFN SER B 417 UNP P04150 EXPRESSION TAG
SEQADV 6CFN SER C 417 UNP P04150 EXPRESSION TAG
SEQADV 6CFN SER D 417 UNP P04150 EXPRESSION TAG
SEQADV 6CFN SER E 417 UNP P04150 EXPRESSION TAG
SEQADV 6CFN SER F 417 UNP P04150 EXPRESSION TAG
SEQADV 6CFN SER G 417 UNP P04150 EXPRESSION TAG
SEQADV 6CFN SER H 417 UNP P04150 EXPRESSION TAG
SEQRES 1 A 90 SER PRO LYS LEU CYS LEU VAL CYS SER ASP GLU ALA SER
SEQRES 2 A 90 GLY CYS HIS TYR GLY VAL LEU THR CYS GLY SER CYS LYS
SEQRES 3 A 90 VAL PHE PHE LYS ARG ALA VAL GLU GLY GLN HIS ASN TYR
SEQRES 4 A 90 LEU CYS ALA GLY ARG ASN ASP CYS ILE ILE ASP LYS ILE
SEQRES 5 A 90 ARG ARG LYS ASN CYS PRO ALA CYS ARG TYR ARG LYS CYS
SEQRES 6 A 90 LEU GLN ALA GLY MET ASN LEU GLU ALA ARG LYS THR LYS
SEQRES 7 A 90 LYS LYS ILE LYS GLY ILE GLN GLN ALA THR THR GLY
SEQRES 1 B 90 SER PRO LYS LEU CYS LEU VAL CYS SER ASP GLU ALA SER
SEQRES 2 B 90 GLY CYS HIS TYR GLY VAL LEU THR CYS GLY SER CYS LYS
SEQRES 3 B 90 VAL PHE PHE LYS ARG ALA VAL GLU GLY GLN HIS ASN TYR
SEQRES 4 B 90 LEU CYS ALA GLY ARG ASN ASP CYS ILE ILE ASP LYS ILE
SEQRES 5 B 90 ARG ARG LYS ASN CYS PRO ALA CYS ARG TYR ARG LYS CYS
SEQRES 6 B 90 LEU GLN ALA GLY MET ASN LEU GLU ALA ARG LYS THR LYS
SEQRES 7 B 90 LYS LYS ILE LYS GLY ILE GLN GLN ALA THR THR GLY
SEQRES 1 C 90 SER PRO LYS LEU CYS LEU VAL CYS SER ASP GLU ALA SER
SEQRES 2 C 90 GLY CYS HIS TYR GLY VAL LEU THR CYS GLY SER CYS LYS
SEQRES 3 C 90 VAL PHE PHE LYS ARG ALA VAL GLU GLY GLN HIS ASN TYR
SEQRES 4 C 90 LEU CYS ALA GLY ARG ASN ASP CYS ILE ILE ASP LYS ILE
SEQRES 5 C 90 ARG ARG LYS ASN CYS PRO ALA CYS ARG TYR ARG LYS CYS
SEQRES 6 C 90 LEU GLN ALA GLY MET ASN LEU GLU ALA ARG LYS THR LYS
SEQRES 7 C 90 LYS LYS ILE LYS GLY ILE GLN GLN ALA THR THR GLY
SEQRES 1 D 90 SER PRO LYS LEU CYS LEU VAL CYS SER ASP GLU ALA SER
SEQRES 2 D 90 GLY CYS HIS TYR GLY VAL LEU THR CYS GLY SER CYS LYS
SEQRES 3 D 90 VAL PHE PHE LYS ARG ALA VAL GLU GLY GLN HIS ASN TYR
SEQRES 4 D 90 LEU CYS ALA GLY ARG ASN ASP CYS ILE ILE ASP LYS ILE
SEQRES 5 D 90 ARG ARG LYS ASN CYS PRO ALA CYS ARG TYR ARG LYS CYS
SEQRES 6 D 90 LEU GLN ALA GLY MET ASN LEU GLU ALA ARG LYS THR LYS
SEQRES 7 D 90 LYS LYS ILE LYS GLY ILE GLN GLN ALA THR THR GLY
SEQRES 1 E 90 SER PRO LYS LEU CYS LEU VAL CYS SER ASP GLU ALA SER
SEQRES 2 E 90 GLY CYS HIS TYR GLY VAL LEU THR CYS GLY SER CYS LYS
SEQRES 3 E 90 VAL PHE PHE LYS ARG ALA VAL GLU GLY GLN HIS ASN TYR
SEQRES 4 E 90 LEU CYS ALA GLY ARG ASN ASP CYS ILE ILE ASP LYS ILE
SEQRES 5 E 90 ARG ARG LYS ASN CYS PRO ALA CYS ARG TYR ARG LYS CYS
SEQRES 6 E 90 LEU GLN ALA GLY MET ASN LEU GLU ALA ARG LYS THR LYS
SEQRES 7 E 90 LYS LYS ILE LYS GLY ILE GLN GLN ALA THR THR GLY
SEQRES 1 F 90 SER PRO LYS LEU CYS LEU VAL CYS SER ASP GLU ALA SER
SEQRES 2 F 90 GLY CYS HIS TYR GLY VAL LEU THR CYS GLY SER CYS LYS
SEQRES 3 F 90 VAL PHE PHE LYS ARG ALA VAL GLU GLY GLN HIS ASN TYR
SEQRES 4 F 90 LEU CYS ALA GLY ARG ASN ASP CYS ILE ILE ASP LYS ILE
SEQRES 5 F 90 ARG ARG LYS ASN CYS PRO ALA CYS ARG TYR ARG LYS CYS
SEQRES 6 F 90 LEU GLN ALA GLY MET ASN LEU GLU ALA ARG LYS THR LYS
SEQRES 7 F 90 LYS LYS ILE LYS GLY ILE GLN GLN ALA THR THR GLY
SEQRES 1 G 90 SER PRO LYS LEU CYS LEU VAL CYS SER ASP GLU ALA SER
SEQRES 2 G 90 GLY CYS HIS TYR GLY VAL LEU THR CYS GLY SER CYS LYS
SEQRES 3 G 90 VAL PHE PHE LYS ARG ALA VAL GLU GLY GLN HIS ASN TYR
SEQRES 4 G 90 LEU CYS ALA GLY ARG ASN ASP CYS ILE ILE ASP LYS ILE
SEQRES 5 G 90 ARG ARG LYS ASN CYS PRO ALA CYS ARG TYR ARG LYS CYS
SEQRES 6 G 90 LEU GLN ALA GLY MET ASN LEU GLU ALA ARG LYS THR LYS
SEQRES 7 G 90 LYS LYS ILE LYS GLY ILE GLN GLN ALA THR THR GLY
SEQRES 1 H 90 SER PRO LYS LEU CYS LEU VAL CYS SER ASP GLU ALA SER
SEQRES 2 H 90 GLY CYS HIS TYR GLY VAL LEU THR CYS GLY SER CYS LYS
SEQRES 3 H 90 VAL PHE PHE LYS ARG ALA VAL GLU GLY GLN HIS ASN TYR
SEQRES 4 H 90 LEU CYS ALA GLY ARG ASN ASP CYS ILE ILE ASP LYS ILE
SEQRES 5 H 90 ARG ARG LYS ASN CYS PRO ALA CYS ARG TYR ARG LYS CYS
SEQRES 6 H 90 LEU GLN ALA GLY MET ASN LEU GLU ALA ARG LYS THR LYS
SEQRES 7 H 90 LYS LYS ILE LYS GLY ILE GLN GLN ALA THR THR GLY
HET ZN A 601 1
HET ZN A 602 1
HET ZN B 601 1
HET ZN B 602 1
HET ZN C 601 1
HET ZN C 602 1
HET ZN D 601 1
HET ZN D 602 1
HET ZN E 601 1
HET ZN E 602 1
HET ZN F 601 1
HET ZN F 602 1
HET ZN G 601 1
HET ZN G 602 1
HET ZN H 601 1
HET ZN H 602 1
HETNAM ZN ZINC ION
FORMUL 9 ZN 16(ZN 2+)
FORMUL 25 HOH *26(H2 O)
HELIX 1 AA1 CYS A 438 GLN A 452 1 15
HELIX 2 AA2 ARG A 469 ASN A 472 5 4
HELIX 3 AA3 CYS A 473 GLY A 485 1 13
HELIX 4 AA4 ASN A 487 LYS A 498 1 12
HELIX 5 AA5 CYS B 438 GLU B 450 1 13
HELIX 6 AA6 CYS B 473 ALA B 484 1 12
HELIX 7 AA7 CYS C 438 GLN C 452 1 15
HELIX 8 AA8 CYS C 473 GLY C 485 1 13
HELIX 9 AA9 ASN C 487 LYS C 498 1 12
HELIX 10 AB1 CYS D 438 GLY D 451 1 14
HELIX 11 AB2 ARG D 469 ASN D 472 5 4
HELIX 12 AB3 CYS D 473 ALA D 484 1 12
HELIX 13 AB4 CYS E 438 GLU E 450 1 13
HELIX 14 AB5 ILE E 468 ASN E 472 5 5
HELIX 15 AB6 CYS E 473 ALA E 484 1 12
HELIX 16 AB7 LEU E 488 ILE E 497 1 10
HELIX 17 AB8 CYS F 438 GLU F 450 1 13
HELIX 18 AB9 CYS F 473 GLY F 485 1 13
HELIX 19 AC1 LEU F 488 LYS F 495 1 8
HELIX 20 AC2 CYS G 438 GLY G 451 1 14
HELIX 21 AC3 ARG G 469 ASN G 472 5 4
HELIX 22 AC4 CYS G 473 ALA G 484 1 12
HELIX 23 AC5 CYS H 438 GLN H 452 1 15
HELIX 24 AC6 ARG H 469 ASN H 472 5 4
HELIX 25 AC7 CYS H 473 GLY H 485 1 13
SHEET 1 AA1 2 GLY A 430 HIS A 432 0
SHEET 2 AA1 2 VAL A 435 THR A 437 -1 O VAL A 435 N HIS A 432
SHEET 1 AA2 2 GLY B 430 HIS B 432 0
SHEET 2 AA2 2 VAL B 435 THR B 437 -1 O VAL B 435 N HIS B 432
SHEET 1 AA3 2 GLY C 430 HIS C 432 0
SHEET 2 AA3 2 VAL C 435 THR C 437 -1 O VAL C 435 N HIS C 432
SHEET 1 AA4 2 GLY D 430 HIS D 432 0
SHEET 2 AA4 2 VAL D 435 THR D 437 -1 O VAL D 435 N HIS D 432
SHEET 1 AA5 2 GLY E 430 HIS E 432 0
SHEET 2 AA5 2 VAL E 435 THR E 437 -1 O VAL E 435 N HIS E 432
SHEET 1 AA6 2 GLY F 430 HIS F 432 0
SHEET 2 AA6 2 VAL F 435 THR F 437 -1 O VAL F 435 N HIS F 432
SHEET 1 AA7 2 GLY G 430 HIS G 432 0
SHEET 2 AA7 2 VAL G 435 THR G 437 -1 O THR G 437 N GLY G 430
SHEET 1 AA8 2 GLY H 430 HIS H 432 0
SHEET 2 AA8 2 VAL H 435 THR H 437 -1 O VAL H 435 N HIS H 432
SSBOND 1 CYS A 431 CYS D 431 1555 1555 2.03
SSBOND 2 CYS B 431 CYS C 431 1555 1555 2.04
SSBOND 3 CYS E 431 CYS G 431 1555 1555 2.03
SSBOND 4 CYS F 431 CYS H 431 1555 1555 2.03
LINK SG CYS A 421 ZN ZN A 601 1555 1555 2.53
LINK SG CYS A 424 ZN ZN A 601 1555 1555 2.16
LINK SG CYS A 438 ZN ZN A 601 1555 1555 2.37
LINK SG CYS A 441 ZN ZN A 601 1555 1555 2.32
LINK SG CYS A 457 ZN ZN A 602 1555 1555 2.48
LINK SG CYS A 463 ZN ZN A 602 1555 1555 2.28
LINK SG CYS A 473 ZN ZN A 602 1555 1555 2.39
LINK SG CYS A 476 ZN ZN A 602 1555 1555 2.52
LINK SG CYS B 421 ZN ZN B 601 1555 1555 2.53
LINK SG CYS B 424 ZN ZN B 601 1555 1555 2.35
LINK SG CYS B 438 ZN ZN B 601 1555 1555 2.40
LINK SG CYS B 441 ZN ZN B 601 1555 1555 2.17
LINK SG CYS B 457 ZN ZN B 602 1555 1555 2.35
LINK SG CYS B 463 ZN ZN B 602 1555 1555 2.19
LINK SG CYS B 473 ZN ZN B 602 1555 1555 2.14
LINK SG CYS B 476 ZN ZN B 602 1555 1555 2.58
LINK SG CYS C 421 ZN ZN C 601 1555 1555 2.38
LINK SG CYS C 424 ZN ZN C 601 1555 1555 2.17
LINK SG CYS C 438 ZN ZN C 601 1555 1555 2.32
LINK SG CYS C 441 ZN ZN C 601 1555 1555 2.39
LINK SG CYS C 457 ZN ZN C 602 1555 1555 2.44
LINK SG CYS C 463 ZN ZN C 602 1555 1555 2.30
LINK SG CYS C 473 ZN ZN C 602 1555 1555 2.33
LINK SG CYS C 476 ZN ZN C 602 1555 1555 2.50
LINK SG CYS D 421 ZN ZN D 601 1555 1555 2.35
LINK SG CYS D 424 ZN ZN D 601 1555 1555 2.24
LINK SG CYS D 438 ZN ZN D 601 1555 1555 2.21
LINK SG CYS D 441 ZN ZN D 601 1555 1555 2.24
LINK SG CYS D 457 ZN ZN D 602 1555 1555 2.36
LINK SG CYS D 463 ZN ZN D 602 1555 1555 2.23
LINK SG CYS D 473 ZN ZN D 602 1555 1555 2.26
LINK SG CYS D 476 ZN ZN D 602 1555 1555 2.35
LINK SG CYS E 421 ZN ZN E 601 1555 1555 2.43
LINK SG CYS E 424 ZN ZN E 601 1555 1555 2.35
LINK SG CYS E 438 ZN ZN E 601 1555 1555 2.20
LINK SG CYS E 441 ZN ZN E 601 1555 1555 2.35
LINK SG CYS E 457 ZN ZN E 602 1555 1555 2.26
LINK SG CYS E 463 ZN ZN E 602 1555 1555 2.32
LINK SG CYS E 473 ZN ZN E 602 1555 1555 2.26
LINK SG CYS E 476 ZN ZN E 602 1555 1555 2.45
LINK SG CYS F 421 ZN ZN F 601 1555 1555 2.46
LINK SG CYS F 424 ZN ZN F 601 1555 1555 2.21
LINK SG CYS F 438 ZN ZN F 601 1555 1555 2.44
LINK SG CYS F 441 ZN ZN F 601 1555 1555 2.36
LINK SG CYS F 457 ZN ZN F 602 1555 1555 2.30
LINK SG CYS F 463 ZN ZN F 602 1555 1555 2.20
LINK SG CYS F 473 ZN ZN F 602 1555 1555 2.22
LINK SG CYS F 476 ZN ZN F 602 1555 1555 2.29
LINK SG CYS G 421 ZN ZN G 601 1555 1555 2.58
LINK SG CYS G 424 ZN ZN G 601 1555 1555 2.28
LINK SG CYS G 438 ZN ZN G 601 1555 1555 2.22
LINK SG CYS G 441 ZN ZN G 601 1555 1555 2.26
LINK SG CYS G 457 ZN ZN G 602 1555 1555 2.24
LINK SG CYS G 463 ZN ZN G 602 1555 1555 2.27
LINK SG CYS G 473 ZN ZN G 602 1555 1555 2.25
LINK SG CYS G 476 ZN ZN G 602 1555 1555 2.56
LINK SG CYS H 421 ZN ZN H 601 1555 1555 2.48
LINK SG CYS H 424 ZN ZN H 601 1555 1555 2.22
LINK SG CYS H 438 ZN ZN H 601 1555 1555 2.39
LINK SG CYS H 441 ZN ZN H 601 1555 1555 2.25
LINK SG CYS H 457 ZN ZN H 602 1555 1555 2.37
LINK SG CYS H 463 ZN ZN H 602 1555 1555 2.25
LINK SG CYS H 473 ZN ZN H 602 1555 1555 2.31
LINK SG CYS H 476 ZN ZN H 602 1555 1555 2.45
SITE 1 AC1 4 CYS A 421 CYS A 424 CYS A 438 CYS A 441
SITE 1 AC2 4 CYS A 457 CYS A 463 CYS A 473 CYS A 476
SITE 1 AC3 5 CYS B 421 VAL B 423 CYS B 424 CYS B 438
SITE 2 AC3 5 CYS B 441
SITE 1 AC4 4 CYS B 457 CYS B 463 CYS B 473 CYS B 476
SITE 1 AC5 4 CYS C 421 CYS C 424 CYS C 438 CYS C 441
SITE 1 AC6 4 CYS C 457 CYS C 463 CYS C 473 CYS C 476
SITE 1 AC7 4 CYS D 421 CYS D 424 CYS D 438 CYS D 441
SITE 1 AC8 4 CYS D 457 CYS D 463 CYS D 473 CYS D 476
SITE 1 AC9 4 CYS E 421 CYS E 424 CYS E 438 CYS E 441
SITE 1 AD1 4 CYS E 457 CYS E 463 CYS E 473 CYS E 476
SITE 1 AD2 4 CYS F 421 CYS F 424 CYS F 438 CYS F 441
SITE 1 AD3 4 CYS F 457 CYS F 463 CYS F 473 CYS F 476
SITE 1 AD4 4 CYS G 421 CYS G 424 CYS G 438 CYS G 441
SITE 1 AD5 4 CYS G 457 CYS G 463 CYS G 473 CYS G 476
SITE 1 AD6 4 CYS H 421 CYS H 424 CYS H 438 CYS H 441
SITE 1 AD7 4 CYS H 457 CYS H 463 CYS H 473 CYS H 476
CRYST1 65.803 65.432 72.659 71.27 84.96 68.44 P 1 8
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 0.015197 -0.006005 0.000561 0.00000
SCALE2 0.000000 0.016433 -0.005393 0.00000
SCALE3 0.000000 0.000000 0.014541 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
