HEADER HYDROLASE/DNA 06-OCT-11 3U3Y
TITLE MOUSE TREX1 D200H MUTANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THREE PRIME REPAIR EXONUCLEASE 1;
COMPND 3 CHAIN: B, A;
COMPND 4 SYNONYM: 3'-5' EXONUCLEASE TREX1;
COMPND 5 EC: 3.1.11.2;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: 5'-D(*GP*AP*CP*G)-3';
COMPND 10 CHAIN: C, D;
COMPND 11 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: TREX1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PET28;
SOURCE 9 MOL_ID: 2;
SOURCE 10 SYNTHETIC: YES;
SOURCE 11 OTHER_DETAILS: CHEMICALLY SYNTHESIZED DNA OLIGONUCLEOTIDE
KEYWDS RNASE H FOLD, 3' EXONUCLEASE, HOMODIMER, HYDROLASE-DNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR S.L.BAILEY,S.HARVEY,F.W.PERRINO,T.HOLLIS
REVDAT 3 28-FEB-24 3U3Y 1 REMARK SEQADV LINK
REVDAT 2 18-APR-12 3U3Y 1 JRNL
REVDAT 1 28-DEC-11 3U3Y 0
JRNL AUTH S.L.BAILEY,S.HARVEY,F.W.PERRINO,T.HOLLIS
JRNL TITL DEFECTS IN DNA DEGRADATION REVEALED IN CRYSTAL STRUCTURES OF
JRNL TITL 2 TREX1 EXONUCLEASE MUTATIONS LINKED TO AUTOIMMUNE DISEASE.
JRNL REF DNA REPAIR V. 11 65 2012
JRNL REFN ISSN 1568-7864
JRNL PMID 22071149
JRNL DOI 10.1016/J.DNAREP.2011.10.007
REMARK 2
REMARK 2 RESOLUTION. 2.28 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7.1_743)
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) : 2.28
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 22.72
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 22013
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.216
REMARK 3 R VALUE (WORKING SET) : 0.213
REMARK 3 FREE R VALUE : 0.275
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.160
REMARK 3 FREE R VALUE TEST SET COUNT : 1136
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 22.7247 - 4.5493 0.97 2623 146 0.1965 0.2249
REMARK 3 2 4.5493 - 3.6156 0.99 2628 135 0.2069 0.2536
REMARK 3 3 3.6156 - 3.1600 1.00 2657 134 0.2198 0.3042
REMARK 3 4 3.1600 - 2.8717 1.00 2622 126 0.2053 0.2881
REMARK 3 5 2.8717 - 2.6662 1.00 2626 148 0.2109 0.2914
REMARK 3 6 2.6662 - 2.5092 1.00 2559 131 0.2287 0.2973
REMARK 3 7 2.5092 - 2.3837 0.99 2618 157 0.2393 0.3536
REMARK 3 8 2.3837 - 2.2800 0.99 2544 159 0.2702 0.3276
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.00
REMARK 3 SHRINKAGE RADIUS : 0.89
REMARK 3 K_SOL : 0.40
REMARK 3 B_SOL : 51.13
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.740
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.880
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) : -7.90290
REMARK 3 B22 (A**2) : 4.21740
REMARK 3 B33 (A**2) : 3.68550
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -2.59510
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.007 3655
REMARK 3 ANGLE : 1.096 5011
REMARK 3 CHIRALITY : 0.057 567
REMARK 3 PLANARITY : 0.006 624
REMARK 3 DIHEDRAL : 17.269 1372
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 40
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN A AND RESID 6:21)
REMARK 3 ORIGIN FOR THE GROUP (A): -6.6582 -19.8561 12.2934
REMARK 3 T TENSOR
REMARK 3 T11: 0.1977 T22: 0.2263
REMARK 3 T33: 0.3560 T12: -0.0070
REMARK 3 T13: -0.0634 T23: 0.0249
REMARK 3 L TENSOR
REMARK 3 L11: 2.1109 L22: 4.2769
REMARK 3 L33: 1.9352 L12: 0.9881
REMARK 3 L13: 0.1874 L23: 0.6496
REMARK 3 S TENSOR
REMARK 3 S11: 0.2670 S12: -0.0161 S13: -0.7955
REMARK 3 S21: -0.3465 S22: -0.2817 S23: -0.1388
REMARK 3 S31: 0.0651 S32: -0.1676 S33: 0.0165
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN A AND RESID 22:41)
REMARK 3 ORIGIN FOR THE GROUP (A): -7.5011 -7.6182 12.1270
REMARK 3 T TENSOR
REMARK 3 T11: 0.1885 T22: 0.2080
REMARK 3 T33: 0.1132 T12: -0.0380
REMARK 3 T13: -0.0383 T23: -0.0229
REMARK 3 L TENSOR
REMARK 3 L11: 3.0415 L22: 3.9776
REMARK 3 L33: 1.6868 L12: -0.4610
REMARK 3 L13: 0.1147 L23: -0.7292
REMARK 3 S TENSOR
REMARK 3 S11: 0.0388 S12: -0.2918 S13: -0.4587
REMARK 3 S21: -0.2270 S22: -0.0263 S23: 0.3244
REMARK 3 S31: 0.1321 S32: -0.1538 S33: -0.0357
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN A AND RESID 42:52)
REMARK 3 ORIGIN FOR THE GROUP (A): -0.2224 -29.1945 24.1080
REMARK 3 T TENSOR
REMARK 3 T11: 0.3797 T22: 0.5421
REMARK 3 T33: 1.2128 T12: -0.1351
REMARK 3 T13: 0.0753 T23: 0.1405
REMARK 3 L TENSOR
REMARK 3 L11: 6.9754 L22: 0.2430
REMARK 3 L33: 8.3443 L12: -1.0297
REMARK 3 L13: -6.4957 L23: 0.4960
REMARK 3 S TENSOR
REMARK 3 S11: -0.3804 S12: -0.5709 S13: -0.5748
REMARK 3 S21: 0.1679 S22: -0.3802 S23: 0.7378
REMARK 3 S31: 0.7507 S32: -0.3102 S33: 0.7472
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN A AND RESID 53:59)
REMARK 3 ORIGIN FOR THE GROUP (A): -1.1640 -21.4248 34.0004
REMARK 3 T TENSOR
REMARK 3 T11: 0.4560 T22: 0.6543
REMARK 3 T33: 0.4456 T12: -0.0256
REMARK 3 T13: -0.1106 T23: 0.2392
REMARK 3 L TENSOR
REMARK 3 L11: 4.9463 L22: 5.9313
REMARK 3 L33: 2.8358 L12: -1.5495
REMARK 3 L13: 2.9601 L23: -1.8494
REMARK 3 S TENSOR
REMARK 3 S11: 0.4392 S12: 0.2019 S13: -0.3192
REMARK 3 S21: 0.2928 S22: -0.4921 S23: -0.3834
REMARK 3 S31: 0.3637 S32: 0.1978 S33: -0.0851
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: (CHAIN A AND RESID 60:66)
REMARK 3 ORIGIN FOR THE GROUP (A): 6.9576 -18.7531 18.3358
REMARK 3 T TENSOR
REMARK 3 T11: 0.2322 T22: 0.4195
REMARK 3 T33: 0.2004 T12: -0.1060
REMARK 3 T13: -0.0464 T23: 0.0794
REMARK 3 L TENSOR
REMARK 3 L11: 0.4419 L22: 0.2803
REMARK 3 L33: 3.2002 L12: 0.1066
REMARK 3 L13: -1.1835 L23: -0.3736
REMARK 3 S TENSOR
REMARK 3 S11: 0.2405 S12: -0.9075 S13: -0.3546
REMARK 3 S21: 0.3715 S22: -0.0627 S23: -0.0739
REMARK 3 S31: -0.0431 S32: -0.3032 S33: -0.0759
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: (CHAIN A AND RESID 67:83)
REMARK 3 ORIGIN FOR THE GROUP (A): -5.7539 2.8089 12.8030
REMARK 3 T TENSOR
REMARK 3 T11: 0.2732 T22: 0.1819
REMARK 3 T33: 0.1696 T12: 0.0016
REMARK 3 T13: -0.0346 T23: -0.0180
REMARK 3 L TENSOR
REMARK 3 L11: 3.1863 L22: 3.7914
REMARK 3 L33: 1.6094 L12: -1.7370
REMARK 3 L13: -0.2435 L23: 0.4264
REMARK 3 S TENSOR
REMARK 3 S11: -0.1964 S12: -0.3159 S13: 0.2039
REMARK 3 S21: 0.3182 S22: 0.0011 S23: 0.0267
REMARK 3 S31: -0.0225 S32: -0.2100 S33: 0.2016
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: (CHAIN A AND RESID 84:90)
REMARK 3 ORIGIN FOR THE GROUP (A): -4.4877 5.7038 15.6246
REMARK 3 T TENSOR
REMARK 3 T11: 0.2061 T22: 0.3118
REMARK 3 T33: 0.2276 T12: -0.0066
REMARK 3 T13: -0.0102 T23: -0.0402
REMARK 3 L TENSOR
REMARK 3 L11: 2.9306 L22: 7.2051
REMARK 3 L33: 3.9421 L12: -2.8171
REMARK 3 L13: 2.1045 L23: -1.0260
REMARK 3 S TENSOR
REMARK 3 S11: -0.4579 S12: -0.2316 S13: 0.4317
REMARK 3 S21: 0.4728 S22: 0.4165 S23: 0.3365
REMARK 3 S31: 0.3597 S32: -0.6536 S33: -0.0806
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: (CHAIN A AND RESID 91:99)
REMARK 3 ORIGIN FOR THE GROUP (A): 1.9061 6.0552 7.6238
REMARK 3 T TENSOR
REMARK 3 T11: 0.3891 T22: 0.2666
REMARK 3 T33: 0.2848 T12: -0.0319
REMARK 3 T13: -0.0310 T23: 0.0818
REMARK 3 L TENSOR
REMARK 3 L11: 6.5628 L22: 6.0641
REMARK 3 L33: 4.5742 L12: -0.2956
REMARK 3 L13: -3.3978 L23: 4.1376
REMARK 3 S TENSOR
REMARK 3 S11: 0.2157 S12: 0.6098 S13: 0.8937
REMARK 3 S21: 0.3852 S22: 0.0283 S23: -0.1202
REMARK 3 S31: -0.1953 S32: -0.4331 S33: -0.0853
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: (CHAIN A AND RESID 100:112)
REMARK 3 ORIGIN FOR THE GROUP (A): 0.7004 -9.7666 1.3743
REMARK 3 T TENSOR
REMARK 3 T11: 0.3001 T22: 0.4841
REMARK 3 T33: 0.1398 T12: 0.1550
REMARK 3 T13: -0.1509 T23: -0.1396
REMARK 3 L TENSOR
REMARK 3 L11: 0.2363 L22: 0.1978
REMARK 3 L33: 0.2672 L12: -0.2015
REMARK 3 L13: 0.1186 L23: -0.1776
REMARK 3 S TENSOR
REMARK 3 S11: 0.1178 S12: 0.2413 S13: -0.1589
REMARK 3 S21: -0.1036 S22: 0.0233 S23: -0.0230
REMARK 3 S31: 0.0829 S32: 0.0580 S33: 0.1926
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: (CHAIN A AND RESID 113:134)
REMARK 3 ORIGIN FOR THE GROUP (A): -8.1542 -15.8062 10.3664
REMARK 3 T TENSOR
REMARK 3 T11: 0.2612 T22: 0.1655
REMARK 3 T33: 0.3266 T12: -0.0387
REMARK 3 T13: -0.0833 T23: 0.0012
REMARK 3 L TENSOR
REMARK 3 L11: 3.1458 L22: 3.1956
REMARK 3 L33: 1.5772 L12: -0.0962
REMARK 3 L13: 0.5227 L23: 0.9975
REMARK 3 S TENSOR
REMARK 3 S11: -0.0328 S12: -0.0643 S13: -0.5481
REMARK 3 S21: -0.1690 S22: 0.0943 S23: 0.3289
REMARK 3 S31: 0.0129 S32: 0.1229 S33: -0.0160
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: (CHAIN A AND RESID 135:142)
REMARK 3 ORIGIN FOR THE GROUP (A): -9.9075 -5.9315 -0.2104
REMARK 3 T TENSOR
REMARK 3 T11: 0.3936 T22: 0.3826
REMARK 3 T33: 0.3990 T12: 0.0613
REMARK 3 T13: -0.1279 T23: -0.1315
REMARK 3 L TENSOR
REMARK 3 L11: 3.6449 L22: 4.1987
REMARK 3 L33: 7.2025 L12: -3.1443
REMARK 3 L13: 1.4359 L23: 1.6230
REMARK 3 S TENSOR
REMARK 3 S11: 0.3985 S12: 0.4054 S13: 0.4251
REMARK 3 S21: -1.1012 S22: -0.2625 S23: 0.4406
REMARK 3 S31: -0.0385 S32: 0.2546 S33: 0.1600
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: (CHAIN A AND RESID 143:153)
REMARK 3 ORIGIN FOR THE GROUP (A): -7.9445 -17.1896 2.2253
REMARK 3 T TENSOR
REMARK 3 T11: 0.2310 T22: 0.3716
REMARK 3 T33: 0.5288 T12: -0.0589
REMARK 3 T13: -0.0819 T23: 0.0430
REMARK 3 L TENSOR
REMARK 3 L11: 5.4597 L22: 3.9686
REMARK 3 L33: 5.2451 L12: 1.2447
REMARK 3 L13: -3.8093 L23: 0.3790
REMARK 3 S TENSOR
REMARK 3 S11: -0.3935 S12: -0.2751 S13: -0.2565
REMARK 3 S21: -0.5717 S22: 0.0112 S23: 0.1544
REMARK 3 S31: -0.1672 S32: 0.3784 S33: 0.3705
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: (CHAIN A AND RESID 154:161)
REMARK 3 ORIGIN FOR THE GROUP (A): -15.7392 -19.7831 21.5721
REMARK 3 T TENSOR
REMARK 3 T11: 0.2566 T22: 0.4973
REMARK 3 T33: 0.5098 T12: -0.0787
REMARK 3 T13: 0.0332 T23: 0.1937
REMARK 3 L TENSOR
REMARK 3 L11: 0.1927 L22: 5.4022
REMARK 3 L33: 4.5440 L12: 0.6993
REMARK 3 L13: -0.7681 L23: -0.7292
REMARK 3 S TENSOR
REMARK 3 S11: -0.1000 S12: -0.0394 S13: -0.3800
REMARK 3 S21: 0.1641 S22: -0.1723 S23: 0.4487
REMARK 3 S31: 0.1107 S32: -0.1250 S33: 0.2427
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: (CHAIN A AND RESID 162:174)
REMARK 3 ORIGIN FOR THE GROUP (A): -17.2690 -23.4724 29.0479
REMARK 3 T TENSOR
REMARK 3 T11: 0.4955 T22: 0.6969
REMARK 3 T33: 1.1553 T12: -0.1811
REMARK 3 T13: 0.2228 T23: 0.1715
REMARK 3 L TENSOR
REMARK 3 L11: 2.2559 L22: 2.1709
REMARK 3 L33: 2.5937 L12: 2.0276
REMARK 3 L13: -1.4264 L23: -0.5131
REMARK 3 S TENSOR
REMARK 3 S11: -0.1373 S12: 0.0147 S13: -0.7233
REMARK 3 S21: 0.1107 S22: -0.1789 S23: -0.2923
REMARK 3 S31: 0.4760 S32: -0.2041 S33: 0.2813
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: (CHAIN A AND RESID 175:188)
REMARK 3 ORIGIN FOR THE GROUP (A): -11.6608 -14.9223 31.3060
REMARK 3 T TENSOR
REMARK 3 T11: 0.2713 T22: 0.6070
REMARK 3 T33: 0.4626 T12: -0.0907
REMARK 3 T13: 0.0638 T23: 0.2345
REMARK 3 L TENSOR
REMARK 3 L11: 0.3140 L22: 1.7795
REMARK 3 L33: 0.4484 L12: -0.2522
REMARK 3 L13: 0.0250 L23: 0.8183
REMARK 3 S TENSOR
REMARK 3 S11: 0.0878 S12: -0.1296 S13: -0.0634
REMARK 3 S21: 0.4188 S22: -0.1223 S23: 0.5985
REMARK 3 S31: 0.1200 S32: -0.2418 S33: -0.1716
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: (CHAIN A AND RESID 189:194)
REMARK 3 ORIGIN FOR THE GROUP (A): -3.2234 -7.9610 29.9944
REMARK 3 T TENSOR
REMARK 3 T11: 0.4716 T22: 0.7274
REMARK 3 T33: 0.3691 T12: -0.0961
REMARK 3 T13: -0.0890 T23: 0.2188
REMARK 3 L TENSOR
REMARK 3 L11: 3.8084 L22: 1.8874
REMARK 3 L33: 4.0278 L12: 1.6453
REMARK 3 L13: 0.1896 L23: 2.2565
REMARK 3 S TENSOR
REMARK 3 S11: -0.6994 S12: -0.4226 S13: 0.0559
REMARK 3 S21: -0.0071 S22: -0.2081 S23: -0.2314
REMARK 3 S31: -0.1633 S32: 0.3750 S33: 0.7300
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: (CHAIN A AND RESID 195:204)
REMARK 3 ORIGIN FOR THE GROUP (A): -2.7314 -8.5701 21.7094
REMARK 3 T TENSOR
REMARK 3 T11: 0.2503 T22: 0.3436
REMARK 3 T33: 0.0965 T12: -0.0108
REMARK 3 T13: 0.0228 T23: 0.0082
REMARK 3 L TENSOR
REMARK 3 L11: 6.9197 L22: 3.2355
REMARK 3 L33: 2.8824 L12: 2.2530
REMARK 3 L13: 0.1667 L23: -2.4087
REMARK 3 S TENSOR
REMARK 3 S11: -0.0761 S12: -0.4495 S13: -0.0600
REMARK 3 S21: 0.4063 S22: 0.1874 S23: 0.1683
REMARK 3 S31: -0.4603 S32: -0.0214 S33: -0.1461
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: (CHAIN A AND RESID 205:210)
REMARK 3 ORIGIN FOR THE GROUP (A): -5.3046 -20.5354 25.9116
REMARK 3 T TENSOR
REMARK 3 T11: 0.3287 T22: 0.5371
REMARK 3 T33: 0.4219 T12: -0.0175
REMARK 3 T13: 0.0873 T23: 0.1919
REMARK 3 L TENSOR
REMARK 3 L11: 2.0469 L22: 1.4016
REMARK 3 L33: 3.1915 L12: 1.6417
REMARK 3 L13: -2.4254 L23: -1.7804
REMARK 3 S TENSOR
REMARK 3 S11: -0.0075 S12: -0.3889 S13: -0.4559
REMARK 3 S21: 0.4116 S22: -0.0203 S23: 0.3835
REMARK 3 S31: 0.0751 S32: 0.2149 S33: 0.0989
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: (CHAIN A AND RESID 211:222)
REMARK 3 ORIGIN FOR THE GROUP (A): -10.5874 -28.2102 18.9041
REMARK 3 T TENSOR
REMARK 3 T11: 0.2810 T22: 0.3404
REMARK 3 T33: 0.9105 T12: -0.0571
REMARK 3 T13: -0.1148 T23: 0.0633
REMARK 3 L TENSOR
REMARK 3 L11: 4.8412 L22: 0.5067
REMARK 3 L33: 5.2744 L12: 0.1787
REMARK 3 L13: 2.0384 L23: 1.5622
REMARK 3 S TENSOR
REMARK 3 S11: 0.1271 S12: 0.0894 S13: -1.5775
REMARK 3 S21: 0.1561 S22: 0.0130 S23: -0.0653
REMARK 3 S31: 0.7158 S32: -0.1751 S33: -0.5105
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: (CHAIN A AND RESID 223:234)
REMARK 3 ORIGIN FOR THE GROUP (A): -16.2368 -13.6770 4.7846
REMARK 3 T TENSOR
REMARK 3 T11: 0.3162 T22: 0.3003
REMARK 3 T33: 0.5616 T12: -0.0668
REMARK 3 T13: -0.1947 T23: -0.0238
REMARK 3 L TENSOR
REMARK 3 L11: 0.0060 L22: 0.5723
REMARK 3 L33: 1.3943 L12: -0.0588
REMARK 3 L13: -0.0968 L23: 0.8889
REMARK 3 S TENSOR
REMARK 3 S11: -0.1749 S12: 0.0823 S13: -0.2852
REMARK 3 S21: -0.4399 S22: -0.0161 S23: 0.6524
REMARK 3 S31: -0.2206 S32: -0.2928 S33: 0.2996
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: (CHAIN B AND RESID 6:11)
REMARK 3 ORIGIN FOR THE GROUP (A): 22.3918 8.9163 4.0834
REMARK 3 T TENSOR
REMARK 3 T11: 0.5942 T22: 0.5871
REMARK 3 T33: 0.7240 T12: -0.2368
REMARK 3 T13: 0.2892 T23: 0.3040
REMARK 3 L TENSOR
REMARK 3 L11: 2.7827 L22: 0.0914
REMARK 3 L33: 0.3356 L12: -0.5025
REMARK 3 L13: -0.9676 L23: 0.1751
REMARK 3 S TENSOR
REMARK 3 S11: -0.0943 S12: 0.1001 S13: -0.0396
REMARK 3 S21: -0.3188 S22: 0.0380 S23: -0.2937
REMARK 3 S31: -0.3082 S32: 0.4766 S33: -0.1285
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: (CHAIN B AND RESID 12:25)
REMARK 3 ORIGIN FOR THE GROUP (A): 19.7196 -9.6488 13.3070
REMARK 3 T TENSOR
REMARK 3 T11: 0.1726 T22: 0.3301
REMARK 3 T33: 0.1907 T12: -0.0504
REMARK 3 T13: 0.0178 T23: -0.0242
REMARK 3 L TENSOR
REMARK 3 L11: 7.4954 L22: 7.4817
REMARK 3 L33: 3.1169 L12: -5.4750
REMARK 3 L13: 0.6876 L23: -0.4113
REMARK 3 S TENSOR
REMARK 3 S11: 0.3674 S12: -0.1015 S13: 0.4792
REMARK 3 S21: -0.3411 S22: -0.3065 S23: 0.1523
REMARK 3 S31: -0.0762 S32: -0.0519 S33: -0.1109
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: (CHAIN B AND RESID 26:40)
REMARK 3 ORIGIN FOR THE GROUP (A): 18.7294 -13.3414 11.5296
REMARK 3 T TENSOR
REMARK 3 T11: 0.2375 T22: 0.2441
REMARK 3 T33: 0.1029 T12: 0.0814
REMARK 3 T13: 0.0267 T23: 0.0359
REMARK 3 L TENSOR
REMARK 3 L11: 3.4362 L22: 0.9844
REMARK 3 L33: 1.5839 L12: 1.0401
REMARK 3 L13: -0.3204 L23: 0.8047
REMARK 3 S TENSOR
REMARK 3 S11: 0.1973 S12: 0.4105 S13: -0.1913
REMARK 3 S21: -0.4241 S22: -0.3714 S23: -0.2226
REMARK 3 S31: 0.3237 S32: 0.2445 S33: 0.1078
REMARK 3 TLS GROUP : 24
REMARK 3 SELECTION: (CHAIN B AND RESID 41:45)
REMARK 3 ORIGIN FOR THE GROUP (A): 12.4031 9.5235 14.1595
REMARK 3 T TENSOR
REMARK 3 T11: 0.4717 T22: 0.4417
REMARK 3 T33: 0.9813 T12: -0.1478
REMARK 3 T13: -0.3843 T23: 0.0613
REMARK 3 L TENSOR
REMARK 3 L11: 2.1703 L22: 1.5839
REMARK 3 L33: 0.8537 L12: 0.9369
REMARK 3 L13: 0.4368 L23: 0.0528
REMARK 3 S TENSOR
REMARK 3 S11: -0.1530 S12: -0.0683 S13: 0.5439
REMARK 3 S21: -0.0639 S22: -0.0134 S23: 0.0354
REMARK 3 S31: -0.2752 S32: 0.0744 S33: 0.3603
REMARK 3 TLS GROUP : 25
REMARK 3 SELECTION: (CHAIN B AND RESID 46:58)
REMARK 3 ORIGIN FOR THE GROUP (A): 14.0064 7.1764 31.6897
REMARK 3 T TENSOR
REMARK 3 T11: 0.4341 T22: 0.6481
REMARK 3 T33: 0.5235 T12: 0.1092
REMARK 3 T13: -0.2277 T23: -0.2513
REMARK 3 L TENSOR
REMARK 3 L11: 3.5509 L22: 0.4570
REMARK 3 L33: 4.0332 L12: 1.2664
REMARK 3 L13: 2.2626 L23: 0.6749
REMARK 3 S TENSOR
REMARK 3 S11: -0.2780 S12: -0.2796 S13: 0.4639
REMARK 3 S21: -0.1246 S22: 0.0579 S23: 0.1964
REMARK 3 S31: -0.3210 S32: -0.6689 S33: 0.6617
REMARK 3 TLS GROUP : 26
REMARK 3 SELECTION: (CHAIN B AND RESID 59:64)
REMARK 3 ORIGIN FOR THE GROUP (A): 5.5208 1.9640 19.9324
REMARK 3 T TENSOR
REMARK 3 T11: 0.3026 T22: 0.5514
REMARK 3 T33: 0.2623 T12: 0.1003
REMARK 3 T13: -0.0197 T23: -0.0535
REMARK 3 L TENSOR
REMARK 3 L11: 4.8304 L22: 3.3687
REMARK 3 L33: 5.2245 L12: 2.0920
REMARK 3 L13: 1.0345 L23: -3.0625
REMARK 3 S TENSOR
REMARK 3 S11: 0.1209 S12: -0.7983 S13: 0.2918
REMARK 3 S21: 0.4721 S22: 0.0465 S23: 0.0732
REMARK 3 S31: -0.7935 S32: 0.1654 S33: -0.2747
REMARK 3 TLS GROUP : 27
REMARK 3 SELECTION: (CHAIN B AND RESID 65:90)
REMARK 3 ORIGIN FOR THE GROUP (A): 16.9503 -21.6571 15.7439
REMARK 3 T TENSOR
REMARK 3 T11: 0.2860 T22: 0.2289
REMARK 3 T33: 0.2254 T12: -0.0272
REMARK 3 T13: -0.0751 T23: 0.0436
REMARK 3 L TENSOR
REMARK 3 L11: 3.9945 L22: 2.9350
REMARK 3 L33: 2.6629 L12: -2.0837
REMARK 3 L13: 1.4121 L23: -1.8477
REMARK 3 S TENSOR
REMARK 3 S11: 0.1809 S12: -0.0908 S13: -0.6228
REMARK 3 S21: -0.0064 S22: -0.1870 S23: -0.0678
REMARK 3 S31: 0.5333 S32: 0.2292 S33: -0.1324
REMARK 3 TLS GROUP : 28
REMARK 3 SELECTION: (CHAIN B AND RESID 91:100)
REMARK 3 ORIGIN FOR THE GROUP (A): 11.2536 -26.3559 10.5150
REMARK 3 T TENSOR
REMARK 3 T11: 0.3970 T22: 0.2560
REMARK 3 T33: 0.5589 T12: 0.0659
REMARK 3 T13: -0.1443 T23: -0.0206
REMARK 3 L TENSOR
REMARK 3 L11: 3.3039 L22: 7.3523
REMARK 3 L33: 0.7811 L12: -0.4796
REMARK 3 L13: 1.3761 L23: -1.4303
REMARK 3 S TENSOR
REMARK 3 S11: 0.4606 S12: 0.0790 S13: -1.3375
REMARK 3 S21: -0.4590 S22: -0.0426 S23: 0.3784
REMARK 3 S31: 0.3110 S32: 0.0066 S33: -0.1838
REMARK 3 TLS GROUP : 29
REMARK 3 SELECTION: (CHAIN B AND RESID 101:117)
REMARK 3 ORIGIN FOR THE GROUP (A): 10.2040 -8.1895 1.7380
REMARK 3 T TENSOR
REMARK 3 T11: 0.4052 T22: 0.4072
REMARK 3 T33: 0.1537 T12: 0.1148
REMARK 3 T13: 0.0341 T23: 0.0492
REMARK 3 L TENSOR
REMARK 3 L11: 1.9765 L22: 1.7777
REMARK 3 L33: 1.8264 L12: 0.0428
REMARK 3 L13: -0.1475 L23: 0.7696
REMARK 3 S TENSOR
REMARK 3 S11: 0.2123 S12: 0.4744 S13: 0.1185
REMARK 3 S21: -0.7486 S22: 0.1633 S23: 0.0787
REMARK 3 S31: -0.0478 S32: 0.2033 S33: -0.0525
REMARK 3 TLS GROUP : 30
REMARK 3 SELECTION: (CHAIN B AND RESID 118:127)
REMARK 3 ORIGIN FOR THE GROUP (A): 22.7001 -3.0670 11.0907
REMARK 3 T TENSOR
REMARK 3 T11: 0.1761 T22: 0.3529
REMARK 3 T33: 0.3247 T12: -0.0348
REMARK 3 T13: 0.1278 T23: 0.0370
REMARK 3 L TENSOR
REMARK 3 L11: 5.5118 L22: 4.5678
REMARK 3 L33: 4.9501 L12: 0.3538
REMARK 3 L13: 1.5741 L23: -1.7043
REMARK 3 S TENSOR
REMARK 3 S11: 0.3464 S12: 0.4173 S13: 0.2837
REMARK 3 S21: 0.1351 S22: 0.0889 S23: -0.1263
REMARK 3 S31: -0.4137 S32: 0.1164 S33: -0.1867
REMARK 3 TLS GROUP : 31
REMARK 3 SELECTION: (CHAIN B AND RESID 128:139)
REMARK 3 ORIGIN FOR THE GROUP (A): 25.2336 -13.0077 7.0213
REMARK 3 T TENSOR
REMARK 3 T11: 0.3337 T22: 0.4538
REMARK 3 T33: 0.1907 T12: 0.1028
REMARK 3 T13: 0.0538 T23: 0.0782
REMARK 3 L TENSOR
REMARK 3 L11: 1.7235 L22: 6.8659
REMARK 3 L33: 8.8936 L12: -0.9645
REMARK 3 L13: -3.7093 L23: -0.2916
REMARK 3 S TENSOR
REMARK 3 S11: 0.2416 S12: 0.3393 S13: 0.1615
REMARK 3 S21: -0.0980 S22: -0.4746 S23: -0.1788
REMARK 3 S31: -0.0722 S32: 0.9566 S33: 0.0826
REMARK 3 TLS GROUP : 32
REMARK 3 SELECTION: (CHAIN B AND RESID 140:145)
REMARK 3 ORIGIN FOR THE GROUP (A): 18.9177 -16.5261 -3.6273
REMARK 3 T TENSOR
REMARK 3 T11: 0.5777 T22: 0.8282
REMARK 3 T33: 0.3284 T12: 0.2702
REMARK 3 T13: 0.1014 T23: -0.0786
REMARK 3 L TENSOR
REMARK 3 L11: 0.1829 L22: 1.9307
REMARK 3 L33: 0.8192 L12: 0.0083
REMARK 3 L13: -0.2524 L23: -0.9668
REMARK 3 S TENSOR
REMARK 3 S11: 0.0189 S12: 0.2116 S13: -0.1375
REMARK 3 S21: -0.6738 S22: -0.2415 S23: -0.2448
REMARK 3 S31: 0.4456 S32: 0.1255 S33: 0.1416
REMARK 3 TLS GROUP : 33
REMARK 3 SELECTION: (CHAIN B AND RESID 146:157)
REMARK 3 ORIGIN FOR THE GROUP (A): 23.2567 -2.5979 6.9194
REMARK 3 T TENSOR
REMARK 3 T11: 0.1896 T22: 0.5462
REMARK 3 T33: 0.4545 T12: 0.0734
REMARK 3 T13: 0.0889 T23: 0.1330
REMARK 3 L TENSOR
REMARK 3 L11: 5.5307 L22: 2.8581
REMARK 3 L33: 2.2524 L12: 1.1071
REMARK 3 L13: 1.1717 L23: -1.3281
REMARK 3 S TENSOR
REMARK 3 S11: 0.0318 S12: 0.6540 S13: 0.6541
REMARK 3 S21: -0.4677 S22: -0.1159 S23: -0.4519
REMARK 3 S31: 0.1678 S32: 0.4959 S33: -0.2931
REMARK 3 TLS GROUP : 34
REMARK 3 SELECTION: (CHAIN B AND RESID 158:175)
REMARK 3 ORIGIN FOR THE GROUP (A): 30.4868 4.6939 24.1183
REMARK 3 T TENSOR
REMARK 3 T11: 0.3495 T22: 0.4880
REMARK 3 T33: 1.3879 T12: -0.0296
REMARK 3 T13: -0.2640 T23: 0.0526
REMARK 3 L TENSOR
REMARK 3 L11: 6.5176 L22: 0.2518
REMARK 3 L33: 3.1427 L12: 1.2396
REMARK 3 L13: 2.4446 L23: 0.6545
REMARK 3 S TENSOR
REMARK 3 S11: -0.1318 S12: -0.0819 S13: 0.7187
REMARK 3 S21: 0.0720 S22: 0.1372 S23: -0.1956
REMARK 3 S31: -0.1604 S32: 0.2136 S33: 0.1555
REMARK 3 TLS GROUP : 35
REMARK 3 SELECTION: (CHAIN B AND RESID 176:187)
REMARK 3 ORIGIN FOR THE GROUP (A): 24.5159 -2.7169 28.1841
REMARK 3 T TENSOR
REMARK 3 T11: 0.1653 T22: 0.6136
REMARK 3 T33: 0.4063 T12: 0.1019
REMARK 3 T13: -0.3778 T23: -0.2344
REMARK 3 L TENSOR
REMARK 3 L11: 0.1874 L22: 0.0059
REMARK 3 L33: 0.3445 L12: 0.0098
REMARK 3 L13: 0.2546 L23: 0.0168
REMARK 3 S TENSOR
REMARK 3 S11: -0.0206 S12: -0.0670 S13: 0.0978
REMARK 3 S21: 0.0682 S22: 0.0272 S23: -0.0633
REMARK 3 S31: -0.0320 S32: 0.0921 S33: 0.2375
REMARK 3 TLS GROUP : 36
REMARK 3 SELECTION: (CHAIN B AND RESID 188:191)
REMARK 3 ORIGIN FOR THE GROUP (A): 18.9235 -3.8140 34.2798
REMARK 3 T TENSOR
REMARK 3 T11: 0.6122 T22: 0.4125
REMARK 3 T33: 0.3621 T12: 0.0147
REMARK 3 T13: -0.0170 T23: -0.2126
REMARK 3 L TENSOR
REMARK 3 L11: 0.3221 L22: 3.5995
REMARK 3 L33: 1.1922 L12: -0.7497
REMARK 3 L13: 0.1982 L23: 0.9442
REMARK 3 S TENSOR
REMARK 3 S11: 0.1584 S12: -0.3571 S13: 0.4729
REMARK 3 S21: 0.2013 S22: -0.1794 S23: 0.0847
REMARK 3 S31: -0.3815 S32: -0.0740 S33: 0.2315
REMARK 3 TLS GROUP : 37
REMARK 3 SELECTION: (CHAIN B AND RESID 192:208)
REMARK 3 ORIGIN FOR THE GROUP (A): 15.9297 -7.9615 22.4308
REMARK 3 T TENSOR
REMARK 3 T11: 0.2189 T22: 0.3740
REMARK 3 T33: 0.1544 T12: -0.0571
REMARK 3 T13: -0.0617 T23: -0.0254
REMARK 3 L TENSOR
REMARK 3 L11: 4.7553 L22: 2.3367
REMARK 3 L33: 4.1666 L12: -2.1910
REMARK 3 L13: -0.3652 L23: -0.5599
REMARK 3 S TENSOR
REMARK 3 S11: -0.0120 S12: -0.5461 S13: 0.3834
REMARK 3 S21: 0.4057 S22: 0.2311 S23: -0.2428
REMARK 3 S31: 0.2845 S32: -0.0698 S33: -0.1481
REMARK 3 TLS GROUP : 38
REMARK 3 SELECTION: (CHAIN B AND RESID 209:214)
REMARK 3 ORIGIN FOR THE GROUP (A): 19.8060 8.0339 22.3534
REMARK 3 T TENSOR
REMARK 3 T11: 0.3004 T22: 0.2797
REMARK 3 T33: 0.8543 T12: 0.0254
REMARK 3 T13: -0.2536 T23: -0.1659
REMARK 3 L TENSOR
REMARK 3 L11: 1.3248 L22: 1.6477
REMARK 3 L33: 0.6907 L12: 1.4685
REMARK 3 L13: -0.6055 L23: -0.5754
REMARK 3 S TENSOR
REMARK 3 S11: -0.2242 S12: -0.1040 S13: 0.6881
REMARK 3 S21: 0.1354 S22: -0.0588 S23: -0.2011
REMARK 3 S31: -0.3188 S32: 0.1124 S33: 0.3214
REMARK 3 TLS GROUP : 39
REMARK 3 SELECTION: (CHAIN B AND RESID 215:224)
REMARK 3 ORIGIN FOR THE GROUP (A): 25.1553 6.5284 11.0519
REMARK 3 T TENSOR
REMARK 3 T11: 0.3798 T22: 0.3103
REMARK 3 T33: 1.0664 T12: -0.1556
REMARK 3 T13: 0.1226 T23: 0.1717
REMARK 3 L TENSOR
REMARK 3 L11: 0.1286 L22: 0.1517
REMARK 3 L33: 0.3357 L12: 0.1397
REMARK 3 L13: -0.2068 L23: -0.2263
REMARK 3 S TENSOR
REMARK 3 S11: 0.0655 S12: -0.0584 S13: 0.4202
REMARK 3 S21: 0.0780 S22: -0.1382 S23: 0.1531
REMARK 3 S31: -0.2103 S32: 0.1043 S33: -0.4754
REMARK 3 TLS GROUP : 40
REMARK 3 SELECTION: (CHAIN B AND RESID 225:234)
REMARK 3 ORIGIN FOR THE GROUP (A): 28.6297 -10.5387 2.8528
REMARK 3 T TENSOR
REMARK 3 T11: 0.3675 T22: 0.6880
REMARK 3 T33: 0.3164 T12: 0.2287
REMARK 3 T13: 0.1774 T23: 0.2198
REMARK 3 L TENSOR
REMARK 3 L11: 2.0124 L22: 0.6982
REMARK 3 L33: 1.3522 L12: -0.0582
REMARK 3 L13: -0.7945 L23: -0.8297
REMARK 3 S TENSOR
REMARK 3 S11: 0.2829 S12: 0.6828 S13: 0.5602
REMARK 3 S21: -0.2899 S22: -0.0884 S23: -0.1473
REMARK 3 S31: -0.3242 S32: -0.3717 S33: 0.0552
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 3U3Y COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-OCT-11.
REMARK 100 THE DEPOSITION ID IS D_1000068275.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-OCT-08
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : OSMIC
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU SATURN 92
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21089
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.280
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : 0.07200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> 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
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 29.57
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.75
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 16% PEG 4000, 0.1 M MES PH 6.0, 2% 1,4
REMARK 280 -BUTANEDIOL, VAPOR DIFFUSION, TEMPERATURE 298K
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 28.93050
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6280 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18170 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -32.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, A, C, 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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET B 1
REMARK 465 GLY B 2
REMARK 465 SER B 3
REMARK 465 GLN B 4
REMARK 465 THR B 5
REMARK 465 THR B 47
REMARK 465 SER B 48
REMARK 465 SER B 167
REMARK 465 PRO B 168
REMARK 465 SER B 169
REMARK 465 GLY B 170
REMARK 465 ASN B 171
REMARK 465 GLY B 172
REMARK 465 SER B 173
REMARK 465 THR B 235
REMARK 465 PRO B 236
REMARK 465 ALA B 237
REMARK 465 THR B 238
REMARK 465 THR B 239
REMARK 465 GLY B 240
REMARK 465 THR B 241
REMARK 465 THR B 242
REMARK 465 ASN B 243
REMARK 465 LEU B 244
REMARK 465 ARG B 245
REMARK 465 PRO B 246
REMARK 465 HIS B 247
REMARK 465 ALA B 248
REMARK 465 ALA B 249
REMARK 465 THR B 250
REMARK 465 ALA B 251
REMARK 465 THR B 252
REMARK 465 THR B 253
REMARK 465 PRO B 254
REMARK 465 LEU B 255
REMARK 465 ALA B 256
REMARK 465 THR B 257
REMARK 465 ALA B 258
REMARK 465 ASN B 259
REMARK 465 GLY B 260
REMARK 465 SER B 261
REMARK 465 PRO B 262
REMARK 465 SER B 263
REMARK 465 ASN B 264
REMARK 465 GLY B 265
REMARK 465 ARG B 266
REMARK 465 SER B 267
REMARK 465 ARG B 268
REMARK 465 ARG B 269
REMARK 465 PRO B 270
REMARK 465 LYS B 271
REMARK 465 SER B 272
REMARK 465 PRO B 273
REMARK 465 PRO B 274
REMARK 465 PRO B 275
REMARK 465 GLU B 276
REMARK 465 LYS B 277
REMARK 465 VAL B 278
REMARK 465 PRO B 279
REMARK 465 GLU B 280
REMARK 465 ALA B 281
REMARK 465 PRO B 282
REMARK 465 SER B 283
REMARK 465 GLN B 284
REMARK 465 GLU B 285
REMARK 465 GLY B 286
REMARK 465 LEU B 287
REMARK 465 LEU B 288
REMARK 465 ALA B 289
REMARK 465 PRO B 290
REMARK 465 LEU B 291
REMARK 465 SER B 292
REMARK 465 LEU B 293
REMARK 465 LEU B 294
REMARK 465 THR B 295
REMARK 465 LEU B 296
REMARK 465 LEU B 297
REMARK 465 THR B 298
REMARK 465 LEU B 299
REMARK 465 ALA B 300
REMARK 465 ILE B 301
REMARK 465 ALA B 302
REMARK 465 THR B 303
REMARK 465 LEU B 304
REMARK 465 TYR B 305
REMARK 465 GLY B 306
REMARK 465 LEU B 307
REMARK 465 PHE B 308
REMARK 465 LEU B 309
REMARK 465 ALA B 310
REMARK 465 SER B 311
REMARK 465 PRO B 312
REMARK 465 GLY B 313
REMARK 465 GLN B 314
REMARK 465 MET A 1
REMARK 465 GLY A 2
REMARK 465 SER A 3
REMARK 465 GLN A 4
REMARK 465 THR A 5
REMARK 465 ASN A 46
REMARK 465 THR A 47
REMARK 465 SER A 48
REMARK 465 ILE A 49
REMARK 465 SER A 50
REMARK 465 ALA A 165
REMARK 465 SER A 166
REMARK 465 SER A 167
REMARK 465 PRO A 168
REMARK 465 SER A 169
REMARK 465 GLY A 170
REMARK 465 ASN A 171
REMARK 465 GLY A 172
REMARK 465 SER A 173
REMARK 465 THR A 235
REMARK 465 PRO A 236
REMARK 465 ALA A 237
REMARK 465 THR A 238
REMARK 465 THR A 239
REMARK 465 GLY A 240
REMARK 465 THR A 241
REMARK 465 THR A 242
REMARK 465 ASN A 243
REMARK 465 LEU A 244
REMARK 465 ARG A 245
REMARK 465 PRO A 246
REMARK 465 HIS A 247
REMARK 465 ALA A 248
REMARK 465 ALA A 249
REMARK 465 THR A 250
REMARK 465 ALA A 251
REMARK 465 THR A 252
REMARK 465 THR A 253
REMARK 465 PRO A 254
REMARK 465 LEU A 255
REMARK 465 ALA A 256
REMARK 465 THR A 257
REMARK 465 ALA A 258
REMARK 465 ASN A 259
REMARK 465 GLY A 260
REMARK 465 SER A 261
REMARK 465 PRO A 262
REMARK 465 SER A 263
REMARK 465 ASN A 264
REMARK 465 GLY A 265
REMARK 465 ARG A 266
REMARK 465 SER A 267
REMARK 465 ARG A 268
REMARK 465 ARG A 269
REMARK 465 PRO A 270
REMARK 465 LYS A 271
REMARK 465 SER A 272
REMARK 465 PRO A 273
REMARK 465 PRO A 274
REMARK 465 PRO A 275
REMARK 465 GLU A 276
REMARK 465 LYS A 277
REMARK 465 VAL A 278
REMARK 465 PRO A 279
REMARK 465 GLU A 280
REMARK 465 ALA A 281
REMARK 465 PRO A 282
REMARK 465 SER A 283
REMARK 465 GLN A 284
REMARK 465 GLU A 285
REMARK 465 GLY A 286
REMARK 465 LEU A 287
REMARK 465 LEU A 288
REMARK 465 ALA A 289
REMARK 465 PRO A 290
REMARK 465 LEU A 291
REMARK 465 SER A 292
REMARK 465 LEU A 293
REMARK 465 LEU A 294
REMARK 465 THR A 295
REMARK 465 LEU A 296
REMARK 465 LEU A 297
REMARK 465 THR A 298
REMARK 465 LEU A 299
REMARK 465 ALA A 300
REMARK 465 ILE A 301
REMARK 465 ALA A 302
REMARK 465 THR A 303
REMARK 465 LEU A 304
REMARK 465 TYR A 305
REMARK 465 GLY A 306
REMARK 465 LEU A 307
REMARK 465 PHE A 308
REMARK 465 LEU A 309
REMARK 465 ALA A 310
REMARK 465 SER A 311
REMARK 465 PRO A 312
REMARK 465 GLY A 313
REMARK 465 GLN A 314
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 ILE B 49 CG1 CG2 CD1
REMARK 470 ARG B 174 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 174 CG CD NE CZ NH1 NH2
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 OE1 GLU B 198 HZ3 LYS A 66 1.57
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 DG C 1 O4' - C1' - N9 ANGL. DEV. = 1.8 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 TYR B 129 -80.84 -127.78
REMARK 500 HIS A 53 69.61 67.66
REMARK 500 TYR A 129 -74.24 -127.00
REMARK 500 PRO A 146 4.59 -68.68
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 A 99 0.14 SIDE CHAIN
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 CA D 5 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 18 OD1
REMARK 620 2 HOH B 331 O 90.0
REMARK 620 3 HOH B 355 O 99.0 83.8
REMARK 620 4 HOH B 386 O 90.8 168.3 84.6
REMARK 620 5 DC D 3 O3' 149.3 85.3 110.5 99.8
REMARK 620 6 DG D 4 OP1 91.6 96.1 169.4 95.5 59.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 5 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 18 OD1
REMARK 620 2 HOH A 344 O 96.1
REMARK 620 3 HOH A 349 O 87.6 89.4
REMARK 620 4 DC C 3 O3' 154.5 109.4 91.0
REMARK 620 5 DG C 4 OP1 98.8 163.6 98.2 56.2
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BU1 A 315
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 5
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 5
DBREF 3U3Y B 1 314 UNP Q91XB0 TREX1_MOUSE 1 314
DBREF 3U3Y A 1 314 UNP Q91XB0 TREX1_MOUSE 1 314
DBREF 3U3Y C 1 4 PDB 3U3Y 3U3Y 1 4
DBREF 3U3Y D 1 4 PDB 3U3Y 3U3Y 1 4
SEQADV 3U3Y HIS B 200 UNP Q91XB0 ASP 200 ENGINEERED MUTATION
SEQADV 3U3Y HIS A 200 UNP Q91XB0 ASP 200 ENGINEERED MUTATION
SEQRES 1 B 314 MET GLY SER GLN THR LEU PRO HIS GLY HIS MET GLN THR
SEQRES 2 B 314 LEU ILE PHE LEU ASP LEU GLU ALA THR GLY LEU PRO SER
SEQRES 3 B 314 SER ARG PRO GLU VAL THR GLU LEU CYS LEU LEU ALA VAL
SEQRES 4 B 314 HIS ARG ARG ALA LEU GLU ASN THR SER ILE SER GLN GLY
SEQRES 5 B 314 HIS PRO PRO PRO VAL PRO ARG PRO PRO ARG VAL VAL ASP
SEQRES 6 B 314 LYS LEU SER LEU CYS ILE ALA PRO GLY LYS ALA CYS SER
SEQRES 7 B 314 PRO GLY ALA SER GLU ILE THR GLY LEU SER LYS ALA GLU
SEQRES 8 B 314 LEU GLU VAL GLN GLY ARG GLN ARG PHE ASP ASP ASN LEU
SEQRES 9 B 314 ALA ILE LEU LEU ARG ALA PHE LEU GLN ARG GLN PRO GLN
SEQRES 10 B 314 PRO CYS CYS LEU VAL ALA HIS ASN GLY ASP ARG TYR ASP
SEQRES 11 B 314 PHE PRO LEU LEU GLN THR GLU LEU ALA ARG LEU SER THR
SEQRES 12 B 314 PRO SER PRO LEU ASP GLY THR PHE CYS VAL ASP SER ILE
SEQRES 13 B 314 ALA ALA LEU LYS ALA LEU GLU GLN ALA SER SER PRO SER
SEQRES 14 B 314 GLY ASN GLY SER ARG LYS SER TYR SER LEU GLY SER ILE
SEQRES 15 B 314 TYR THR ARG LEU TYR TRP GLN ALA PRO THR ASP SER HIS
SEQRES 16 B 314 THR ALA GLU GLY HIS VAL LEU THR LEU LEU SER ILE CYS
SEQRES 17 B 314 GLN TRP LYS PRO GLN ALA LEU LEU GLN TRP VAL ASP GLU
SEQRES 18 B 314 HIS ALA ARG PRO PHE SER THR VAL LYS PRO MET TYR GLY
SEQRES 19 B 314 THR PRO ALA THR THR GLY THR THR ASN LEU ARG PRO HIS
SEQRES 20 B 314 ALA ALA THR ALA THR THR PRO LEU ALA THR ALA ASN GLY
SEQRES 21 B 314 SER PRO SER ASN GLY ARG SER ARG ARG PRO LYS SER PRO
SEQRES 22 B 314 PRO PRO GLU LYS VAL PRO GLU ALA PRO SER GLN GLU GLY
SEQRES 23 B 314 LEU LEU ALA PRO LEU SER LEU LEU THR LEU LEU THR LEU
SEQRES 24 B 314 ALA ILE ALA THR LEU TYR GLY LEU PHE LEU ALA SER PRO
SEQRES 25 B 314 GLY GLN
SEQRES 1 A 314 MET GLY SER GLN THR LEU PRO HIS GLY HIS MET GLN THR
SEQRES 2 A 314 LEU ILE PHE LEU ASP LEU GLU ALA THR GLY LEU PRO SER
SEQRES 3 A 314 SER ARG PRO GLU VAL THR GLU LEU CYS LEU LEU ALA VAL
SEQRES 4 A 314 HIS ARG ARG ALA LEU GLU ASN THR SER ILE SER GLN GLY
SEQRES 5 A 314 HIS PRO PRO PRO VAL PRO ARG PRO PRO ARG VAL VAL ASP
SEQRES 6 A 314 LYS LEU SER LEU CYS ILE ALA PRO GLY LYS ALA CYS SER
SEQRES 7 A 314 PRO GLY ALA SER GLU ILE THR GLY LEU SER LYS ALA GLU
SEQRES 8 A 314 LEU GLU VAL GLN GLY ARG GLN ARG PHE ASP ASP ASN LEU
SEQRES 9 A 314 ALA ILE LEU LEU ARG ALA PHE LEU GLN ARG GLN PRO GLN
SEQRES 10 A 314 PRO CYS CYS LEU VAL ALA HIS ASN GLY ASP ARG TYR ASP
SEQRES 11 A 314 PHE PRO LEU LEU GLN THR GLU LEU ALA ARG LEU SER THR
SEQRES 12 A 314 PRO SER PRO LEU ASP GLY THR PHE CYS VAL ASP SER ILE
SEQRES 13 A 314 ALA ALA LEU LYS ALA LEU GLU GLN ALA SER SER PRO SER
SEQRES 14 A 314 GLY ASN GLY SER ARG LYS SER TYR SER LEU GLY SER ILE
SEQRES 15 A 314 TYR THR ARG LEU TYR TRP GLN ALA PRO THR ASP SER HIS
SEQRES 16 A 314 THR ALA GLU GLY HIS VAL LEU THR LEU LEU SER ILE CYS
SEQRES 17 A 314 GLN TRP LYS PRO GLN ALA LEU LEU GLN TRP VAL ASP GLU
SEQRES 18 A 314 HIS ALA ARG PRO PHE SER THR VAL LYS PRO MET TYR GLY
SEQRES 19 A 314 THR PRO ALA THR THR GLY THR THR ASN LEU ARG PRO HIS
SEQRES 20 A 314 ALA ALA THR ALA THR THR PRO LEU ALA THR ALA ASN GLY
SEQRES 21 A 314 SER PRO SER ASN GLY ARG SER ARG ARG PRO LYS SER PRO
SEQRES 22 A 314 PRO PRO GLU LYS VAL PRO GLU ALA PRO SER GLN GLU GLY
SEQRES 23 A 314 LEU LEU ALA PRO LEU SER LEU LEU THR LEU LEU THR LEU
SEQRES 24 A 314 ALA ILE ALA THR LEU TYR GLY LEU PHE LEU ALA SER PRO
SEQRES 25 A 314 GLY GLN
SEQRES 1 C 4 DG DA DC DG
SEQRES 1 D 4 DG DA DC DG
HET BU1 A 315 16
HET CA C 5 1
HET CA D 5 1
HETNAM BU1 1,4-BUTANEDIOL
HETNAM CA CALCIUM ION
FORMUL 5 BU1 C4 H10 O2
FORMUL 6 CA 2(CA 2+)
FORMUL 8 HOH *183(H2 O)
HELIX 1 1 LEU B 24 ARG B 28 5 5
HELIX 2 2 ARG B 41 ASN B 46 1 6
HELIX 3 3 SER B 78 GLY B 86 1 9
HELIX 4 4 SER B 88 GLN B 95 1 8
HELIX 5 5 ASP B 101 ARG B 114 1 14
HELIX 6 6 TYR B 129 ARG B 140 1 12
HELIX 7 7 SER B 155 GLN B 164 1 10
HELIX 8 8 SER B 178 TRP B 188 1 11
HELIX 9 9 THR B 196 TRP B 210 1 15
HELIX 10 10 LYS B 211 ALA B 223 1 13
HELIX 11 11 SER B 227 VAL B 229 5 3
HELIX 12 12 LEU A 24 ARG A 28 5 5
HELIX 13 13 ARG A 41 GLU A 45 1 5
HELIX 14 14 SER A 78 GLY A 86 1 9
HELIX 15 15 SER A 88 GLN A 95 1 8
HELIX 16 16 ASP A 101 ARG A 114 1 14
HELIX 17 17 TYR A 129 ARG A 140 1 12
HELIX 18 18 SER A 155 GLU A 163 1 9
HELIX 19 19 SER A 178 TRP A 188 1 11
HELIX 20 20 THR A 196 GLN A 209 1 14
HELIX 21 21 LYS A 211 ALA A 223 1 13
HELIX 22 22 SER A 227 VAL A 229 5 3
SHEET 1 A12 ARG B 224 PRO B 225 0
SHEET 2 A12 PHE B 151 ASP B 154 -1 N CYS B 152 O ARG B 224
SHEET 3 A12 CYS B 119 ALA B 123 1 N LEU B 121 O PHE B 151
SHEET 4 A12 THR B 13 ALA B 21 1 N LEU B 17 O VAL B 122
SHEET 5 A12 VAL B 31 HIS B 40 -1 O VAL B 39 N LEU B 14
SHEET 6 A12 ASP B 65 CYS B 70 -1 O LEU B 67 N LEU B 36
SHEET 7 A12 ASP A 65 CYS A 70 -1 O SER A 68 N LYS B 66
SHEET 8 A12 VAL A 31 HIS A 40 -1 N LEU A 36 O LEU A 67
SHEET 9 A12 THR A 13 ALA A 21 -1 N LEU A 14 O VAL A 39
SHEET 10 A12 CYS A 119 ALA A 123 1 O VAL A 122 N ILE A 15
SHEET 11 A12 PHE A 151 ASP A 154 1 O PHE A 151 N LEU A 121
SHEET 12 A12 ARG A 224 PRO A 225 -1 O ARG A 224 N CYS A 152
LINK OD1 ASP B 18 CA CA D 5 1555 1555 2.57
LINK O HOH B 331 CA CA D 5 1555 1555 2.59
LINK O HOH B 355 CA CA D 5 1555 1555 2.61
LINK O HOH B 386 CA CA D 5 1555 1555 2.74
LINK OD1 ASP A 18 CA CA C 5 1555 1555 2.53
LINK O HOH A 344 CA CA C 5 1555 1555 2.63
LINK O HOH A 349 CA CA C 5 1555 1555 2.72
LINK O3' DC C 3 CA CA C 5 1555 1555 2.72
LINK OP1 DG C 4 CA CA C 5 1555 1555 2.52
LINK O3' DC D 3 CA CA D 5 1555 1555 2.53
LINK OP1 DG D 4 CA CA D 5 1555 1555 2.53
CISPEP 1 HIS B 53 PRO B 54 0 -5.61
CISPEP 2 GLN B 117 PRO B 118 0 7.07
CISPEP 3 GLN A 51 GLY A 52 0 1.04
CISPEP 4 HIS A 53 PRO A 54 0 -18.15
CISPEP 5 GLN A 117 PRO A 118 0 3.02
SITE 1 AC1 7 THR A 192 ASP A 193 GLU A 198 GLY A 199
SITE 2 AC1 7 LEU A 202 THR A 203 HOH A 387
SITE 1 AC2 5 ASP A 18 HOH A 344 HOH A 349 DC C 3
SITE 2 AC2 5 DG C 4
SITE 1 AC3 6 ASP B 18 HOH B 331 HOH B 355 HOH B 386
SITE 2 AC3 6 DC D 3 DG D 4
CRYST1 65.066 57.861 68.227 90.00 108.11 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 0.015369 0.000000 0.005026 0.00000
SCALE2 0.000000 0.017283 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015421 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
