HEADER GENE REGULATION 17-MAY-18 5ZWX
TITLE CRYSTAL STRUCTURE OF RAPHANUS SATIVUS AGDP1 AGD12 IN COMPLEX WITH AN
TITLE 2 H3K9ME2 PEPTIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DUF724 DOMAIN-CONTAINING PROTEIN 6-LIKE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: AGDP1 AGD12 CASSETTE;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: H3(1-15)K9ME2 PEPTIDE;
COMPND 9 CHAIN: P, Q;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RAPHANUS SATIVUS;
SOURCE 3 ORGANISM_TAXID: 3726;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VARIANT: RIL;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PMBP;
SOURCE 10 MOL_ID: 2;
SOURCE 11 SYNTHETIC: YES;
SOURCE 12 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;
SOURCE 13 ORGANISM_COMMON: MOUSE-EAR CRESS;
SOURCE 14 ORGANISM_TAXID: 3702
KEYWDS AGENET DOMAIN, AGDP1, EPIGENETICS, H3K9ME2, GENE REGULATION
EXPDTA X-RAY DIFFRACTION
AUTHOR X.DU,J.DU
REVDAT 1 14-NOV-18 5ZWX 0
JRNL AUTH C.ZHANG,X.DU,K.TANG,Z.YANG,L.PAN,P.ZHU,J.LUO,Y.JIANG,
JRNL AUTH 2 H.ZHANG,H.WAN,X.WANG,F.WU,W.A.TAO,X.J.HE,H.ZHANG,
JRNL AUTH 3 R.A.BRESSAN,J.DU,J.K.ZHU
JRNL TITL ARABIDOPSIS AGDP1 LINKS H3K9ME2 TO DNA METHYLATION IN
JRNL TITL 2 HETEROCHROMATIN
JRNL REF NAT COMMUN V. 9 4547 2018
JRNL REFN ESSN 2041-1723
JRNL PMID 30382101
JRNL DOI 10.1038/S41467-018-06965-W
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.19
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.050
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 33643
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.183
REMARK 3 R VALUE (WORKING SET) : 0.182
REMARK 3 FREE R VALUE : 0.211
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.070
REMARK 3 FREE R VALUE TEST SET COUNT : 1705
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 41.1974 - 5.4766 0.99 2533 158 0.1938 0.2123
REMARK 3 2 5.4766 - 4.3485 0.99 2613 125 0.1555 0.1645
REMARK 3 3 4.3485 - 3.7993 1.00 2611 136 0.1492 0.1988
REMARK 3 4 3.7993 - 3.4521 1.00 2569 129 0.1623 0.1967
REMARK 3 5 3.4521 - 3.2048 1.00 2594 152 0.1667 0.1923
REMARK 3 6 3.2048 - 3.0159 1.00 2618 141 0.1778 0.1975
REMARK 3 7 3.0159 - 2.8649 1.00 2631 133 0.1875 0.2145
REMARK 3 8 2.8649 - 2.7402 1.00 2619 119 0.1889 0.2139
REMARK 3 9 2.7402 - 2.6347 1.00 2548 174 0.1857 0.1970
REMARK 3 10 2.6347 - 2.5438 1.00 2621 140 0.1988 0.2102
REMARK 3 11 2.5438 - 2.4643 0.99 2583 138 0.1891 0.2487
REMARK 3 12 2.4643 - 2.3939 1.00 2565 130 0.1979 0.2165
REMARK 3 13 2.3939 - 2.3308 1.00 2638 162 0.1963 0.2416
REMARK 3 14 2.3308 - 2.2740 1.00 2566 100 0.1975 0.3284
REMARK 3 15 2.2740 - 2.2223 1.00 2651 144 0.1980 0.2123
REMARK 3 16 2.2223 - 2.1750 1.00 2603 130 0.2048 0.2139
REMARK 3 17 2.1750 - 2.1315 1.00 2612 135 0.2090 0.2254
REMARK 3 18 2.1315 - 2.0913 1.00 2612 133 0.2056 0.2673
REMARK 3 19 2.0913 - 2.0539 1.00 2646 116 0.2153 0.2363
REMARK 3 20 2.0539 - 2.0191 1.00 2559 161 0.2211 0.2498
REMARK 3 21 2.0191 - 1.9865 1.00 2570 166 0.2266 0.2939
REMARK 3 22 1.9865 - 1.9560 1.00 2606 143 0.2337 0.3348
REMARK 3 23 1.9560 - 1.9272 0.99 2570 125 0.2462 0.2292
REMARK 3 24 1.9272 - 1.9001 1.00 2571 138 0.2519 0.3178
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.210
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.950
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 : 0.012 2626
REMARK 3 ANGLE : 1.422 3540
REMARK 3 CHIRALITY : 0.065 362
REMARK 3 PLANARITY : 0.006 462
REMARK 3 DIHEDRAL : 15.559 1000
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 21
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 26 THROUGH 37 )
REMARK 3 ORIGIN FOR THE GROUP (A): 10.4963 36.4198 -12.2428
REMARK 3 T TENSOR
REMARK 3 T11: 0.5035 T22: 0.4805
REMARK 3 T33: 0.3883 T12: -0.0909
REMARK 3 T13: -0.1007 T23: 0.0780
REMARK 3 L TENSOR
REMARK 3 L11: 7.9560 L22: 3.5626
REMARK 3 L33: 2.3298 L12: 2.0319
REMARK 3 L13: -1.4182 L23: -1.3167
REMARK 3 S TENSOR
REMARK 3 S11: -0.6247 S12: 0.5696 S13: 0.5223
REMARK 3 S21: -1.1746 S22: 0.7640 S23: 0.2124
REMARK 3 S31: 0.4584 S32: -0.6333 S33: -0.1334
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 38 THROUGH 45 )
REMARK 3 ORIGIN FOR THE GROUP (A): 13.7305 34.0153 2.7465
REMARK 3 T TENSOR
REMARK 3 T11: 0.3898 T22: 0.3153
REMARK 3 T33: 0.2546 T12: -0.0404
REMARK 3 T13: -0.0322 T23: 0.0733
REMARK 3 L TENSOR
REMARK 3 L11: 9.1174 L22: 8.6961
REMARK 3 L33: 2.3907 L12: 3.5443
REMARK 3 L13: 3.9050 L23: 1.1364
REMARK 3 S TENSOR
REMARK 3 S11: -0.3543 S12: 0.2667 S13: 0.6203
REMARK 3 S21: 0.7517 S22: 0.4603 S23: 0.1578
REMARK 3 S31: -0.7350 S32: -0.0607 S33: -0.0362
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 46 THROUGH 59 )
REMARK 3 ORIGIN FOR THE GROUP (A): 12.2894 32.5591 4.2885
REMARK 3 T TENSOR
REMARK 3 T11: 0.2500 T22: 0.3183
REMARK 3 T33: 0.2686 T12: -0.0019
REMARK 3 T13: -0.0087 T23: 0.0854
REMARK 3 L TENSOR
REMARK 3 L11: 2.8948 L22: 2.9351
REMARK 3 L33: 6.7379 L12: -2.2841
REMARK 3 L13: 1.5256 L23: -2.9872
REMARK 3 S TENSOR
REMARK 3 S11: -0.2389 S12: 0.2133 S13: -0.0595
REMARK 3 S21: 0.1069 S22: 0.4409 S23: 0.3624
REMARK 3 S31: -0.1174 S32: -0.5700 S33: -0.1497
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 60 THROUGH 98 )
REMARK 3 ORIGIN FOR THE GROUP (A): 5.8868 38.1525 1.3892
REMARK 3 T TENSOR
REMARK 3 T11: 0.1895 T22: 0.5803
REMARK 3 T33: 0.4248 T12: 0.1239
REMARK 3 T13: -0.0154 T23: 0.2076
REMARK 3 L TENSOR
REMARK 3 L11: 3.5547 L22: 4.0168
REMARK 3 L33: 3.4352 L12: -0.7628
REMARK 3 L13: -0.1706 L23: 1.0717
REMARK 3 S TENSOR
REMARK 3 S11: -0.2960 S12: -0.1084 S13: 0.3747
REMARK 3 S21: -0.4736 S22: 0.5766 S23: 0.8143
REMARK 3 S31: -0.3975 S32: -1.1698 S33: -0.0504
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 99 THROUGH 109 )
REMARK 3 ORIGIN FOR THE GROUP (A): 15.9200 11.6496 -3.0527
REMARK 3 T TENSOR
REMARK 3 T11: 1.3051 T22: 0.5419
REMARK 3 T33: 1.0807 T12: -0.1314
REMARK 3 T13: -0.1557 T23: -0.0154
REMARK 3 L TENSOR
REMARK 3 L11: 1.3487 L22: 2.0047
REMARK 3 L33: 7.1535 L12: -2.8155
REMARK 3 L13: 1.6288 L23: 1.1515
REMARK 3 S TENSOR
REMARK 3 S11: 0.2922 S12: 0.6215 S13: -1.8943
REMARK 3 S21: 0.1197 S22: 0.5536 S23: 0.2442
REMARK 3 S31: 2.7381 S32: 1.1197 S33: -0.6026
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 110 THROUGH 116 )
REMARK 3 ORIGIN FOR THE GROUP (A): 25.6481 11.2437 6.2236
REMARK 3 T TENSOR
REMARK 3 T11: 0.7412 T22: 0.4520
REMARK 3 T33: 0.3318 T12: 0.1036
REMARK 3 T13: -0.0918 T23: -0.1354
REMARK 3 L TENSOR
REMARK 3 L11: 2.4647 L22: 5.8086
REMARK 3 L33: 4.1984 L12: 1.3488
REMARK 3 L13: 0.0258 L23: -4.5926
REMARK 3 S TENSOR
REMARK 3 S11: 0.1957 S12: 1.0759 S13: -0.7567
REMARK 3 S21: -1.8053 S22: 0.1567 S23: 0.9141
REMARK 3 S31: 1.8060 S32: 0.0571 S33: -0.4844
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 117 THROUGH 135 )
REMARK 3 ORIGIN FOR THE GROUP (A): 19.5412 20.7633 11.2348
REMARK 3 T TENSOR
REMARK 3 T11: 0.2539 T22: 0.2166
REMARK 3 T33: 0.1869 T12: -0.0333
REMARK 3 T13: 0.0167 T23: -0.0041
REMARK 3 L TENSOR
REMARK 3 L11: 7.2565 L22: 5.4632
REMARK 3 L33: 3.5602 L12: -3.4663
REMARK 3 L13: 0.1965 L23: 1.1385
REMARK 3 S TENSOR
REMARK 3 S11: -0.3219 S12: 0.0215 S13: -0.0707
REMARK 3 S21: 0.2006 S22: 0.3388 S23: -0.0464
REMARK 3 S31: 0.4001 S32: 0.0027 S33: -0.0200
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 136 THROUGH 148 )
REMARK 3 ORIGIN FOR THE GROUP (A): 23.3544 19.6058 15.1988
REMARK 3 T TENSOR
REMARK 3 T11: 0.3486 T22: 0.3151
REMARK 3 T33: 0.1933 T12: 0.0372
REMARK 3 T13: 0.0031 T23: 0.0035
REMARK 3 L TENSOR
REMARK 3 L11: 7.7613 L22: 3.0413
REMARK 3 L33: 7.9062 L12: 0.9774
REMARK 3 L13: 0.2894 L23: -0.0482
REMARK 3 S TENSOR
REMARK 3 S11: 0.3412 S12: -0.1546 S13: -0.4378
REMARK 3 S21: 0.0927 S22: -0.2574 S23: -0.9325
REMARK 3 S31: 1.0514 S32: -0.1133 S33: 0.0390
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 149 THROUGH 160 )
REMARK 3 ORIGIN FOR THE GROUP (A): 18.0957 17.1880 12.6374
REMARK 3 T TENSOR
REMARK 3 T11: 0.2895 T22: 0.1813
REMARK 3 T33: 0.2425 T12: -0.0204
REMARK 3 T13: 0.0054 T23: -0.0042
REMARK 3 L TENSOR
REMARK 3 L11: 2.7591 L22: 3.2418
REMARK 3 L33: 5.9658 L12: -0.3666
REMARK 3 L13: 0.3685 L23: 0.0362
REMARK 3 S TENSOR
REMARK 3 S11: 0.0497 S12: 0.0319 S13: -0.1940
REMARK 3 S21: 0.0591 S22: 0.1081 S23: 0.0294
REMARK 3 S31: 0.7961 S32: -0.2269 S33: -0.1087
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 161 THROUGH 173 )
REMARK 3 ORIGIN FOR THE GROUP (A): 21.3622 23.9464 -6.5205
REMARK 3 T TENSOR
REMARK 3 T11: 0.5748 T22: 0.3992
REMARK 3 T33: 0.3066 T12: -0.0259
REMARK 3 T13: 0.0801 T23: -0.0032
REMARK 3 L TENSOR
REMARK 3 L11: 5.5971 L22: 2.2731
REMARK 3 L33: 9.5185 L12: -2.0702
REMARK 3 L13: 0.9399 L23: -4.0221
REMARK 3 S TENSOR
REMARK 3 S11: 0.0174 S12: 0.7520 S13: -0.2787
REMARK 3 S21: -1.2323 S22: 0.0835 S23: -0.3212
REMARK 3 S31: 1.0390 S32: 0.4320 S33: -0.0500
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'P' AND (RESID 1 THROUGH 10 )
REMARK 3 ORIGIN FOR THE GROUP (A): 10.6106 34.2088 15.6737
REMARK 3 T TENSOR
REMARK 3 T11: 0.3849 T22: 0.3401
REMARK 3 T33: 0.3035 T12: 0.0914
REMARK 3 T13: 0.0292 T23: 0.0650
REMARK 3 L TENSOR
REMARK 3 L11: 2.1243 L22: 4.5960
REMARK 3 L33: 5.1318 L12: -1.1387
REMARK 3 L13: 2.1856 L23: -1.9252
REMARK 3 S TENSOR
REMARK 3 S11: -0.5734 S12: -0.3128 S13: 0.3549
REMARK 3 S21: 0.4927 S22: 0.4493 S23: 0.1870
REMARK 3 S31: -0.5411 S32: -0.6795 S33: -0.0004
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 26 THROUGH 37 )
REMARK 3 ORIGIN FOR THE GROUP (A): 0.0741 10.0210 48.2189
REMARK 3 T TENSOR
REMARK 3 T11: 0.4166 T22: 0.5062
REMARK 3 T33: 0.4407 T12: 0.0402
REMARK 3 T13: 0.1161 T23: 0.0592
REMARK 3 L TENSOR
REMARK 3 L11: 5.2211 L22: 9.8638
REMARK 3 L33: 5.0461 L12: -0.5393
REMARK 3 L13: 2.4576 L23: -1.9114
REMARK 3 S TENSOR
REMARK 3 S11: -0.1513 S12: -0.4730 S13: -1.0590
REMARK 3 S21: 0.8894 S22: 0.5658 S23: -0.0173
REMARK 3 S31: -0.2362 S32: -0.8561 S33: -0.2487
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 38 THROUGH 45 )
REMARK 3 ORIGIN FOR THE GROUP (A): 8.1443 12.4415 35.3260
REMARK 3 T TENSOR
REMARK 3 T11: 0.3583 T22: 0.2449
REMARK 3 T33: 0.3574 T12: 0.0158
REMARK 3 T13: 0.0848 T23: 0.0150
REMARK 3 L TENSOR
REMARK 3 L11: 2.3094 L22: 7.1227
REMARK 3 L33: 7.1423 L12: -3.4603
REMARK 3 L13: -1.8463 L23: 0.6746
REMARK 3 S TENSOR
REMARK 3 S11: -0.3100 S12: 0.2395 S13: -0.4456
REMARK 3 S21: -0.5560 S22: 0.1623 S23: -0.0880
REMARK 3 S31: 0.6224 S32: -0.1609 S33: 0.0772
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 46 THROUGH 59 )
REMARK 3 ORIGIN FOR THE GROUP (A): 7.3866 13.9806 33.2130
REMARK 3 T TENSOR
REMARK 3 T11: 0.2485 T22: 0.2504
REMARK 3 T33: 0.2040 T12: 0.0186
REMARK 3 T13: -0.0136 T23: 0.0382
REMARK 3 L TENSOR
REMARK 3 L11: 4.5460 L22: 5.1416
REMARK 3 L33: 6.4491 L12: 2.2964
REMARK 3 L13: -1.6365 L23: -1.6723
REMARK 3 S TENSOR
REMARK 3 S11: -0.1822 S12: -0.2848 S13: 0.2404
REMARK 3 S21: -0.0956 S22: 0.2586 S23: 0.1019
REMARK 3 S31: 0.1082 S32: -0.5804 S33: -0.1137
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 60 THROUGH 98 )
REMARK 3 ORIGIN FOR THE GROUP (A): 0.2023 8.3169 33.8013
REMARK 3 T TENSOR
REMARK 3 T11: 0.2733 T22: 0.4187
REMARK 3 T33: 0.3573 T12: -0.0848
REMARK 3 T13: -0.0106 T23: 0.0710
REMARK 3 L TENSOR
REMARK 3 L11: 3.6399 L22: 3.8105
REMARK 3 L33: 2.8096 L12: -0.1047
REMARK 3 L13: 0.2750 L23: 0.2670
REMARK 3 S TENSOR
REMARK 3 S11: 0.1250 S12: 0.1208 S13: -0.5165
REMARK 3 S21: 0.1267 S22: 0.1858 S23: 0.5755
REMARK 3 S31: 0.6105 S32: -0.8721 S33: -0.2245
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 99 THROUGH 116 )
REMARK 3 ORIGIN FOR THE GROUP (A): 12.9569 34.8443 39.0113
REMARK 3 T TENSOR
REMARK 3 T11: 0.9101 T22: 0.5195
REMARK 3 T33: 0.7881 T12: 0.0650
REMARK 3 T13: 0.2334 T23: -0.1080
REMARK 3 L TENSOR
REMARK 3 L11: 4.0469 L22: 4.2275
REMARK 3 L33: 1.6366 L12: 4.0356
REMARK 3 L13: -2.3946 L23: -2.0653
REMARK 3 S TENSOR
REMARK 3 S11: 1.1956 S12: -0.6848 S13: 2.3235
REMARK 3 S21: 0.7380 S22: 0.0365 S23: 1.6724
REMARK 3 S31: -1.5675 S32: -0.0253 S33: -0.2025
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 117 THROUGH 135 )
REMARK 3 ORIGIN FOR THE GROUP (A): 16.5160 25.6819 29.2113
REMARK 3 T TENSOR
REMARK 3 T11: 0.2938 T22: 0.2027
REMARK 3 T33: 0.1803 T12: 0.0833
REMARK 3 T13: -0.0127 T23: -0.0018
REMARK 3 L TENSOR
REMARK 3 L11: 7.3952 L22: 4.8779
REMARK 3 L33: 3.0670 L12: 3.4795
REMARK 3 L13: 0.6829 L23: 1.9789
REMARK 3 S TENSOR
REMARK 3 S11: -0.2299 S12: -0.0004 S13: 0.1843
REMARK 3 S21: -0.1319 S22: 0.2385 S23: 0.0412
REMARK 3 S31: -0.3869 S32: 0.0282 S33: -0.1811
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 136 THROUGH 148 )
REMARK 3 ORIGIN FOR THE GROUP (A): 21.3331 26.9066 26.7588
REMARK 3 T TENSOR
REMARK 3 T11: 0.4002 T22: 0.2755
REMARK 3 T33: 0.1961 T12: 0.0052
REMARK 3 T13: 0.0261 T23: -0.0038
REMARK 3 L TENSOR
REMARK 3 L11: 7.0145 L22: 3.7051
REMARK 3 L33: 6.8435 L12: -1.4364
REMARK 3 L13: -0.1309 L23: -2.0352
REMARK 3 S TENSOR
REMARK 3 S11: 0.5517 S12: 0.3850 S13: 0.6374
REMARK 3 S21: 0.0101 S22: -0.5029 S23: -1.2052
REMARK 3 S31: -0.8889 S32: 0.0669 S33: -0.0576
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 149 THROUGH 160 )
REMARK 3 ORIGIN FOR THE GROUP (A): 15.5962 29.2762 27.4224
REMARK 3 T TENSOR
REMARK 3 T11: 0.3490 T22: 0.1988
REMARK 3 T33: 0.2550 T12: 0.0681
REMARK 3 T13: 0.0031 T23: 0.0058
REMARK 3 L TENSOR
REMARK 3 L11: 2.5875 L22: 3.0228
REMARK 3 L33: 3.1410 L12: 0.1835
REMARK 3 L13: -1.8859 L23: 0.2513
REMARK 3 S TENSOR
REMARK 3 S11: 0.3764 S12: 0.0990 S13: 0.3723
REMARK 3 S21: -0.0072 S22: 0.0123 S23: 0.0840
REMARK 3 S31: -0.7640 S32: -0.2967 S33: -0.3005
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 161 THROUGH 173 )
REMARK 3 ORIGIN FOR THE GROUP (A): 12.3156 22.4683 46.5952
REMARK 3 T TENSOR
REMARK 3 T11: 0.6287 T22: 0.3380
REMARK 3 T33: 0.2775 T12: 0.0505
REMARK 3 T13: -0.0080 T23: 0.0108
REMARK 3 L TENSOR
REMARK 3 L11: 5.9207 L22: 1.4849
REMARK 3 L33: 7.5682 L12: 2.8858
REMARK 3 L13: -2.8213 L23: -1.2241
REMARK 3 S TENSOR
REMARK 3 S11: 0.0644 S12: -0.5965 S13: 0.2811
REMARK 3 S21: 1.0461 S22: 0.0559 S23: -0.0759
REMARK 3 S31: -0.4512 S32: 0.4019 S33: -0.1727
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: CHAIN 'Q' AND (RESID 1 THROUGH 10 )
REMARK 3 ORIGIN FOR THE GROUP (A): 9.7011 12.3666 21.9420
REMARK 3 T TENSOR
REMARK 3 T11: 0.2794 T22: 0.3147
REMARK 3 T33: 0.2872 T12: -0.0208
REMARK 3 T13: 0.0067 T23: 0.0084
REMARK 3 L TENSOR
REMARK 3 L11: 2.5950 L22: 3.5940
REMARK 3 L33: 7.2636 L12: 1.8059
REMARK 3 L13: 3.1562 L23: -0.3929
REMARK 3 S TENSOR
REMARK 3 S11: -0.2788 S12: 0.1821 S13: -0.3606
REMARK 3 S21: -0.4683 S22: 0.2686 S23: 0.0861
REMARK 3 S31: 0.3329 S32: -0.5910 S33: 0.0031
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 5ZWX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 25-MAY-18.
REMARK 100 THE DEPOSITION ID IS D_1300007805.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-DEC-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL18U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9778
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 33643
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 6.700
REMARK 200 R MERGE (I) : 0.08200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 21.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.97
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6
REMARK 200 DATA REDUNDANCY IN SHELL : 6.80
REMARK 200 R MERGE FOR SHELL (I) : 0.56700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.21
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.69
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15% PEG 20000, 0.1M MES, PH 6.5, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 27.49050
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1330 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9470 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, P
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1320 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9610 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, Q
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 20
REMARK 465 ASN A 21
REMARK 465 SER A 22
REMARK 465 PHE A 23
REMARK 465 ALA A 24
REMARK 465 PRO A 25
REMARK 465 GLU A 174
REMARK 465 GLU A 175
REMARK 465 THR A 176
REMARK 465 GLU A 177
REMARK 465 VAL A 178
REMARK 465 ASP A 179
REMARK 465 GLU A 180
REMARK 465 THR P 11
REMARK 465 GLY P 12
REMARK 465 GLY P 13
REMARK 465 LYS P 14
REMARK 465 ALA P 15
REMARK 465 SER B 20
REMARK 465 ASN B 21
REMARK 465 SER B 22
REMARK 465 PHE B 23
REMARK 465 ALA B 24
REMARK 465 PRO B 25
REMARK 465 GLU B 174
REMARK 465 GLU B 175
REMARK 465 THR B 176
REMARK 465 GLU B 177
REMARK 465 VAL B 178
REMARK 465 ASP B 179
REMARK 465 GLU B 180
REMARK 465 THR Q 11
REMARK 465 GLY Q 12
REMARK 465 GLY Q 13
REMARK 465 LYS Q 14
REMARK 465 ALA Q 15
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 ASP A 64 66.54 -100.13
REMARK 500 SER A 104 -165.64 -69.00
REMARK 500 ASP B 137 23.87 81.35
REMARK 500
REMARK 500 REMARK: NULL
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 SEQUENCE OF ENTITY 1 HAS BEEN DEPOSITED TO NCBI WITH ACCESSION
REMARK 999 NUMBER XP_018485729. RESIDUES L54M/L135M/L140M REPRESENT MUTATIONS.
DBREF 5ZWX A 20 180 PDB 5ZWX 5ZWX 20 180
DBREF 5ZWX P 1 15 UNP P59226 H32_ARATH 2 16
DBREF 5ZWX B 20 180 PDB 5ZWX 5ZWX 20 180
DBREF 5ZWX Q 1 15 UNP P59226 H32_ARATH 2 16
SEQRES 1 A 161 SER ASN SER PHE ALA PRO ARG ILE ARG LEU PRO PRO PHE
SEQRES 2 A 161 LEU LYS PRO GLY ALA ALA VAL GLU ILE SER SER ASN GLU
SEQRES 3 A 161 SER GLY PHE ARG GLY SER TRP TYR MSE GLY LYS VAL VAL
SEQRES 4 A 161 ALA VAL PRO SER SER ASP SER THR THR THR LYS CYS GLU
SEQRES 5 A 161 VAL GLU TYR THR THR LEU PHE PHE ASP LYS GLU GLY ARG
SEQRES 6 A 161 LYS ARG LEU ARG GLU VAL VAL ASP VAL GLY GLN LEU ARG
SEQRES 7 A 161 PRO PRO ALA PRO ALA VAL SER GLU ARG GLU LYS ARG ARG
SEQRES 8 A 161 GLU VAL ALA VAL GLY ASP ASP VAL ASP ALA PHE TYR SER
SEQRES 9 A 161 ASP GLY TRP TRP GLU GLY THR VAL THR GLU VAL MSE GLY
SEQRES 10 A 161 ASP GLY ARG MSE SER VAL TYR PHE ARG ALA SER LYS GLU
SEQRES 11 A 161 GLN ILE ARG PHE ARG ARG ASP GLU LEU ARG PHE HIS ARG
SEQRES 12 A 161 GLU TRP VAL ASN GLY ALA TRP ARG PRO PRO ILE GLU GLU
SEQRES 13 A 161 THR GLU VAL ASP GLU
SEQRES 1 P 15 ALA ARG THR LYS GLN THR ALA ARG MLY SER THR GLY GLY
SEQRES 2 P 15 LYS ALA
SEQRES 1 B 161 SER ASN SER PHE ALA PRO ARG ILE ARG LEU PRO PRO PHE
SEQRES 2 B 161 LEU LYS PRO GLY ALA ALA VAL GLU ILE SER SER ASN GLU
SEQRES 3 B 161 SER GLY PHE ARG GLY SER TRP TYR MSE GLY LYS VAL VAL
SEQRES 4 B 161 ALA VAL PRO SER SER ASP SER THR THR THR LYS CYS GLU
SEQRES 5 B 161 VAL GLU TYR THR THR LEU PHE PHE ASP LYS GLU GLY ARG
SEQRES 6 B 161 LYS ARG LEU ARG GLU VAL VAL ASP VAL GLY GLN LEU ARG
SEQRES 7 B 161 PRO PRO ALA PRO ALA VAL SER GLU ARG GLU LYS ARG ARG
SEQRES 8 B 161 GLU VAL ALA VAL GLY ASP ASP VAL ASP ALA PHE TYR SER
SEQRES 9 B 161 ASP GLY TRP TRP GLU GLY THR VAL THR GLU VAL MSE GLY
SEQRES 10 B 161 ASP GLY ARG MSE SER VAL TYR PHE ARG ALA SER LYS GLU
SEQRES 11 B 161 GLN ILE ARG PHE ARG ARG ASP GLU LEU ARG PHE HIS ARG
SEQRES 12 B 161 GLU TRP VAL ASN GLY ALA TRP ARG PRO PRO ILE GLU GLU
SEQRES 13 B 161 THR GLU VAL ASP GLU
SEQRES 1 Q 15 ALA ARG THR LYS GLN THR ALA ARG MLY SER THR GLY GLY
SEQRES 2 Q 15 LYS ALA
MODRES 5ZWX MLY P 9 LYS MODIFIED RESIDUE
MODRES 5ZWX MLY Q 9 LYS MODIFIED RESIDUE
HET MSE A 54 8
HET MSE A 135 8
HET MSE A 140 8
HET MLY P 9 11
HET MSE B 54 8
HET MSE B 135 8
HET MSE B 140 8
HET MLY Q 9 11
HETNAM MSE SELENOMETHIONINE
HETNAM MLY N-DIMETHYL-LYSINE
FORMUL 1 MSE 6(C5 H11 N O2 SE)
FORMUL 2 MLY 2(C8 H18 N2 O2)
FORMUL 5 HOH *248(H2 O)
HELIX 1 AA1 GLU A 45 ARG A 49 5 5
HELIX 2 AA2 ASP A 92 GLY A 94 5 3
HELIX 3 AA3 SER A 104 ARG A 110 1 7
HELIX 4 AA4 THR P 3 ARG P 8 1 6
HELIX 5 AA5 GLU B 45 ARG B 49 5 5
HELIX 6 AA6 ASP B 92 GLY B 94 5 3
HELIX 7 AA7 GLU B 105 ARG B 110 1 6
HELIX 8 AA8 THR Q 3 ARG Q 8 1 6
SHEET 1 AA1 6 ARG A 86 VAL A 91 0
SHEET 2 AA1 6 CYS A 70 PHE A 78 -1 N CYS A 70 O VAL A 91
SHEET 3 AA1 6 SER A 51 ALA A 59 -1 N VAL A 58 O GLU A 71
SHEET 4 AA1 6 GLY A 125 MSE A 135 -1 O TRP A 126 N TRP A 52
SHEET 5 AA1 6 ARG A 139 PHE A 144 -1 O ARG A 139 N MSE A 135
SHEET 6 AA1 6 GLU A 149 ARG A 154 -1 O GLU A 149 N PHE A 144
SHEET 1 AA2 6 LEU A 96 ARG A 97 0
SHEET 2 AA2 6 ALA A 38 ILE A 41 -1 N GLU A 40 O ARG A 97
SHEET 3 AA2 6 SER A 51 ALA A 59 -1 O TYR A 53 N ILE A 41
SHEET 4 AA2 6 GLY A 125 MSE A 135 -1 O TRP A 126 N TRP A 52
SHEET 5 AA2 6 ASP A 117 TYR A 122 -1 N TYR A 122 O GLY A 125
SHEET 6 AA2 6 LEU A 158 PHE A 160 -1 O ARG A 159 N ASP A 119
SHEET 1 AA3 2 GLU A 163 VAL A 165 0
SHEET 2 AA3 2 ALA A 168 ARG A 170 -1 O ALA A 168 N VAL A 165
SHEET 1 AA4 6 ARG B 86 VAL B 91 0
SHEET 2 AA4 6 CYS B 70 PHE B 78 -1 N CYS B 70 O VAL B 91
SHEET 3 AA4 6 SER B 51 ALA B 59 -1 N VAL B 58 O GLU B 71
SHEET 4 AA4 6 GLY B 125 MSE B 135 -1 O TRP B 126 N TRP B 52
SHEET 5 AA4 6 ARG B 139 PHE B 144 -1 O ARG B 139 N MSE B 135
SHEET 6 AA4 6 GLU B 149 ARG B 154 -1 O GLU B 149 N PHE B 144
SHEET 1 AA5 6 LEU B 96 ARG B 97 0
SHEET 2 AA5 6 ALA B 38 ILE B 41 -1 N GLU B 40 O ARG B 97
SHEET 3 AA5 6 SER B 51 ALA B 59 -1 O TYR B 53 N ILE B 41
SHEET 4 AA5 6 GLY B 125 MSE B 135 -1 O TRP B 126 N TRP B 52
SHEET 5 AA5 6 ASP B 117 TYR B 122 -1 N VAL B 118 O GLY B 129
SHEET 6 AA5 6 LEU B 158 PHE B 160 -1 O ARG B 159 N ASP B 119
SHEET 1 AA6 2 GLU B 163 VAL B 165 0
SHEET 2 AA6 2 ALA B 168 ARG B 170 -1 O ALA B 168 N VAL B 165
LINK C TYR A 53 N MSE A 54 1555 1555 1.33
LINK C MSE A 54 N GLY A 55 1555 1555 1.34
LINK C VAL A 134 N MSE A 135 1555 1555 1.33
LINK C MSE A 135 N GLY A 136 1555 1555 1.33
LINK C ARG A 139 N MSE A 140 1555 1555 1.33
LINK C MSE A 140 N SER A 141 1555 1555 1.33
LINK C ARG P 8 N MLY P 9 1555 1555 1.33
LINK C MLY P 9 N SER P 10 1555 1555 1.32
LINK C TYR B 53 N MSE B 54 1555 1555 1.33
LINK C MSE B 54 N GLY B 55 1555 1555 1.33
LINK C VAL B 134 N MSE B 135 1555 1555 1.31
LINK C MSE B 135 N GLY B 136 1555 1555 1.31
LINK C ARG B 139 N MSE B 140 1555 1555 1.33
LINK C MSE B 140 N SER B 141 1555 1555 1.33
LINK C ARG Q 8 N MLY Q 9 1555 1555 1.33
LINK C MLY Q 9 N SER Q 10 1555 1555 1.32
CISPEP 1 ARG A 170 PRO A 171 0 -3.57
CISPEP 2 ARG B 170 PRO B 171 0 -2.13
CRYST1 47.653 54.981 83.576 90.00 99.72 90.00 P 1 21 1 4
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 0.020985 0.000000 0.003596 0.00000
SCALE2 0.000000 0.018188 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012140 0.00000
(ATOM LINES ARE NOT SHOWN.)
END