HEADER LYASE 07-OCT-14 4RJ0
TITLE THE CRYSTAL STRUCTURE OF Y333N MUTANT PYRIDOXAL-DEPENDENT
TITLE 2 DECARBOXYLASE FROM SPHAEROBACTER THERMOPHILUS DSM 20745
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PYRIDOXAL-DEPENDENT DECARBOXYLASE;
COMPND 3 CHAIN: B, A, C, D;
COMPND 4 EC: 4.1.1.15;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SPHAEROBACTER THERMOPHILUS DSM 20745;
SOURCE 3 ORGANISM_TAXID: 479434;
SOURCE 4 GENE: STHE_2364;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)MAGIC;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PMCSG7
KEYWDS STRUCTURAL GENOMICS, PSI-BIOLOGY, MIDWEST CENTER FOR STRUCTURAL
KEYWDS 2 GENOMICS, MCSG, A/B/A FOLD, LYASE, CYTOSOLIC
EXPDTA X-RAY DIFFRACTION
AUTHOR R.WU,S.CLANCY,A.JOACHIMIAK,MIDWEST CENTER FOR STRUCTURAL GENOMICS
AUTHOR 2 (MCSG)
REVDAT 3 06-DEC-23 4RJ0 1 REMARK
REVDAT 2 20-SEP-23 4RJ0 1 REMARK SEQADV LINK
REVDAT 1 12-NOV-14 4RJ0 0
JRNL AUTH R.WU,S.CLANCY,A.JOACHIMIAK,
JRNL AUTH 2 MIDWEST CENTER FOR STRUCTURAL GENOMICS (MCSG)
JRNL TITL THE CRYSTAL STRUCTURE OF Y333N MUTANT PYRIDOXAL-DEPENDENT
JRNL TITL 2 DECARBOXYLASE FROM SPHAEROBACTER THERMOPHILUS DSM 20745
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.4_1496)
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) : 1.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 32.56
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 91.0
REMARK 3 NUMBER OF REFLECTIONS : 142776
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.169
REMARK 3 R VALUE (WORKING SET) : 0.168
REMARK 3 FREE R VALUE : 0.193
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 7159
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 32.5626 - 6.0466 0.91 4646 226 0.1525 0.1588
REMARK 3 2 6.0466 - 4.8043 0.94 4729 239 0.1596 0.1864
REMARK 3 3 4.8043 - 4.1984 0.95 4695 268 0.1368 0.1423
REMARK 3 4 4.1984 - 3.8152 0.94 4699 240 0.1395 0.1591
REMARK 3 5 3.8152 - 3.5421 0.94 4708 234 0.1494 0.1595
REMARK 3 6 3.5421 - 3.3335 0.93 4653 242 0.1663 0.1721
REMARK 3 7 3.3335 - 3.1667 0.94 4686 231 0.1692 0.1912
REMARK 3 8 3.1667 - 3.0290 0.93 4588 235 0.1689 0.2043
REMARK 3 9 3.0290 - 2.9124 0.92 4612 240 0.1780 0.1799
REMARK 3 10 2.9124 - 2.8120 0.92 4592 239 0.1786 0.2026
REMARK 3 11 2.8120 - 2.7241 0.92 4568 250 0.1805 0.2053
REMARK 3 12 2.7241 - 2.6463 0.93 4554 260 0.1705 0.1992
REMARK 3 13 2.6463 - 2.5766 0.92 4539 257 0.1739 0.2033
REMARK 3 14 2.5766 - 2.5138 0.92 4609 254 0.1677 0.2082
REMARK 3 15 2.5138 - 2.4567 0.93 4566 242 0.1736 0.2003
REMARK 3 16 2.4567 - 2.4044 0.92 4556 249 0.1778 0.2213
REMARK 3 17 2.4044 - 2.3563 0.92 4596 238 0.1725 0.2263
REMARK 3 18 2.3563 - 2.3119 0.92 4531 237 0.1760 0.2267
REMARK 3 19 2.3119 - 2.2706 0.91 4542 235 0.1764 0.2360
REMARK 3 20 2.2706 - 2.2321 0.91 4535 223 0.1840 0.2197
REMARK 3 21 2.2321 - 2.1961 0.89 4404 255 0.1816 0.2143
REMARK 3 22 2.1961 - 2.1623 0.91 4433 260 0.1770 0.2257
REMARK 3 23 2.1623 - 2.1305 0.89 4435 228 0.1768 0.2045
REMARK 3 24 2.1305 - 2.1005 0.90 4475 241 0.1814 0.2152
REMARK 3 25 2.1005 - 2.0722 0.89 4387 245 0.1869 0.2308
REMARK 3 26 2.0722 - 2.0452 0.88 4372 217 0.1987 0.2431
REMARK 3 27 2.0452 - 2.0197 0.88 4398 232 0.1985 0.2275
REMARK 3 28 2.0197 - 1.9954 0.87 4283 203 0.1995 0.2305
REMARK 3 29 1.9954 - 1.9722 0.86 4186 221 0.2018 0.2412
REMARK 3 30 1.9722 - 1.9500 0.81 4040 218 0.2140 0.2437
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) : 0.180
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.240
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 18.15
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 : 0.017 14671
REMARK 3 ANGLE : 1.425 19960
REMARK 3 CHIRALITY : 0.123 2250
REMARK 3 PLANARITY : 0.009 2619
REMARK 3 DIHEDRAL : 15.070 5352
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 32
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'B' AND (RESID -1 THROUGH 38 )
REMARK 3 ORIGIN FOR THE GROUP (A): -13.9380 24.5720 29.4545
REMARK 3 T TENSOR
REMARK 3 T11: 0.1528 T22: 0.1665
REMARK 3 T33: 0.0851 T12: 0.0134
REMARK 3 T13: 0.0138 T23: 0.0287
REMARK 3 L TENSOR
REMARK 3 L11: 1.8149 L22: 2.6724
REMARK 3 L33: 1.6355 L12: -1.0388
REMARK 3 L13: 0.1397 L23: 0.2950
REMARK 3 S TENSOR
REMARK 3 S11: 0.1437 S12: 0.2894 S13: 0.0412
REMARK 3 S21: -0.4607 S22: -0.1990 S23: 0.0576
REMARK 3 S31: -0.2145 S32: -0.0957 S33: 0.0355
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 39 THROUGH 64 )
REMARK 3 ORIGIN FOR THE GROUP (A): 3.6400 21.8945 37.7121
REMARK 3 T TENSOR
REMARK 3 T11: 0.1346 T22: 0.2067
REMARK 3 T33: 0.2265 T12: -0.0323
REMARK 3 T13: 0.0962 T23: 0.0745
REMARK 3 L TENSOR
REMARK 3 L11: 1.3371 L22: 3.7221
REMARK 3 L33: 0.6932 L12: -1.6816
REMARK 3 L13: 0.4708 L23: -0.0857
REMARK 3 S TENSOR
REMARK 3 S11: 0.1277 S12: 0.0521 S13: 0.3307
REMARK 3 S21: -0.3252 S22: -0.0739 S23: -0.6755
REMARK 3 S31: -0.0868 S32: 0.1122 S33: -0.0626
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 65 THROUGH 136 )
REMARK 3 ORIGIN FOR THE GROUP (A): -9.7311 9.2368 42.4744
REMARK 3 T TENSOR
REMARK 3 T11: 0.0688 T22: 0.1164
REMARK 3 T33: 0.0781 T12: -0.0055
REMARK 3 T13: 0.0124 T23: -0.0046
REMARK 3 L TENSOR
REMARK 3 L11: 0.6482 L22: 1.4227
REMARK 3 L33: 0.5235 L12: -0.1912
REMARK 3 L13: 0.2125 L23: -0.2935
REMARK 3 S TENSOR
REMARK 3 S11: 0.0122 S12: 0.0445 S13: -0.0278
REMARK 3 S21: -0.1687 S22: -0.0345 S23: -0.0186
REMARK 3 S31: 0.0473 S32: 0.0597 S33: 0.0170
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 137 THROUGH 191 )
REMARK 3 ORIGIN FOR THE GROUP (A): -11.7944 2.6841 68.1097
REMARK 3 T TENSOR
REMARK 3 T11: 0.0646 T22: 0.0950
REMARK 3 T33: 0.1209 T12: -0.0187
REMARK 3 T13: 0.0125 T23: 0.0382
REMARK 3 L TENSOR
REMARK 3 L11: 1.2985 L22: 1.8455
REMARK 3 L33: 1.8603 L12: -0.7078
REMARK 3 L13: 0.0718 L23: 0.1278
REMARK 3 S TENSOR
REMARK 3 S11: -0.0533 S12: -0.1123 S13: -0.0301
REMARK 3 S21: 0.1819 S22: 0.0598 S23: -0.0025
REMARK 3 S31: -0.0412 S32: 0.0006 S33: -0.0150
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 192 THROUGH 264 )
REMARK 3 ORIGIN FOR THE GROUP (A): -1.1866 -4.4225 70.2652
REMARK 3 T TENSOR
REMARK 3 T11: 0.0870 T22: 0.1340
REMARK 3 T33: 0.1381 T12: -0.0054
REMARK 3 T13: -0.0316 T23: 0.0400
REMARK 3 L TENSOR
REMARK 3 L11: 0.9886 L22: 1.6799
REMARK 3 L33: 0.7467 L12: -0.3687
REMARK 3 L13: -0.2737 L23: 0.5070
REMARK 3 S TENSOR
REMARK 3 S11: -0.0143 S12: -0.1015 S13: -0.0811
REMARK 3 S21: 0.2582 S22: -0.0205 S23: -0.2415
REMARK 3 S31: 0.0543 S32: 0.1510 S33: 0.0362
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 265 THROUGH 312 )
REMARK 3 ORIGIN FOR THE GROUP (A): -6.9554 -6.4462 54.9798
REMARK 3 T TENSOR
REMARK 3 T11: 0.0488 T22: 0.0830
REMARK 3 T33: 0.1262 T12: -0.0026
REMARK 3 T13: 0.0118 T23: 0.0046
REMARK 3 L TENSOR
REMARK 3 L11: 0.8600 L22: 1.2123
REMARK 3 L33: 3.1564 L12: -0.0209
REMARK 3 L13: -0.7388 L23: -1.5181
REMARK 3 S TENSOR
REMARK 3 S11: -0.0172 S12: 0.0447 S13: -0.0827
REMARK 3 S21: -0.0699 S22: -0.0070 S23: -0.0068
REMARK 3 S31: 0.1447 S32: 0.0440 S33: 0.0234
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 313 THROUGH 354 )
REMARK 3 ORIGIN FOR THE GROUP (A): -23.6717 5.6742 59.3318
REMARK 3 T TENSOR
REMARK 3 T11: 0.0717 T22: 0.1868
REMARK 3 T33: 0.2178 T12: 0.0159
REMARK 3 T13: 0.0424 T23: 0.0339
REMARK 3 L TENSOR
REMARK 3 L11: 0.4588 L22: 1.0092
REMARK 3 L33: 1.2031 L12: 0.2281
REMARK 3 L13: 0.5761 L23: -0.3494
REMARK 3 S TENSOR
REMARK 3 S11: -0.0280 S12: -0.0699 S13: -0.0239
REMARK 3 S21: 0.1629 S22: 0.0864 S23: 0.3331
REMARK 3 S31: -0.0689 S32: -0.3600 S33: -0.0216
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 355 THROUGH 433 )
REMARK 3 ORIGIN FOR THE GROUP (A): 10.6769 -4.9213 48.3917
REMARK 3 T TENSOR
REMARK 3 T11: -0.0148 T22: 0.2360
REMARK 3 T33: 0.2760 T12: 0.0543
REMARK 3 T13: 0.1103 T23: 0.0897
REMARK 3 L TENSOR
REMARK 3 L11: 2.5058 L22: 1.4170
REMARK 3 L33: 1.3691 L12: -0.0036
REMARK 3 L13: 0.1841 L23: -0.8418
REMARK 3 S TENSOR
REMARK 3 S11: 0.1549 S12: 0.0492 S13: -0.1937
REMARK 3 S21: -0.2697 S22: -0.3424 S23: -0.4521
REMARK 3 S31: 0.2582 S32: 0.4220 S33: 0.1348
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 434 THROUGH 476 )
REMARK 3 ORIGIN FOR THE GROUP (A): 15.7122 -1.3175 45.9128
REMARK 3 T TENSOR
REMARK 3 T11: 0.1119 T22: 0.2841
REMARK 3 T33: 0.3146 T12: 0.0327
REMARK 3 T13: 0.0804 T23: 0.0905
REMARK 3 L TENSOR
REMARK 3 L11: 1.9331 L22: 1.1530
REMARK 3 L33: 1.7311 L12: -0.2420
REMARK 3 L13: 0.8045 L23: -0.3220
REMARK 3 S TENSOR
REMARK 3 S11: 0.0463 S12: 0.1266 S13: -0.0438
REMARK 3 S21: -0.1597 S22: -0.2628 S23: -0.3888
REMARK 3 S31: 0.1395 S32: 0.5280 S33: 0.1685
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 4 THROUGH 38 )
REMARK 3 ORIGIN FOR THE GROUP (A): -8.4701 4.1495 28.5389
REMARK 3 T TENSOR
REMARK 3 T11: 0.1814 T22: 0.1574
REMARK 3 T33: 0.1182 T12: -0.0060
REMARK 3 T13: 0.0039 T23: -0.0342
REMARK 3 L TENSOR
REMARK 3 L11: 4.4072 L22: 3.4631
REMARK 3 L33: 1.9640 L12: -2.8157
REMARK 3 L13: 0.0311 L23: -0.0171
REMARK 3 S TENSOR
REMARK 3 S11: 0.1671 S12: 0.3670 S13: -0.3177
REMARK 3 S21: -0.4877 S22: -0.1558 S23: 0.0752
REMARK 3 S31: 0.1757 S32: 0.0671 S33: -0.0195
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 39 THROUGH 96 )
REMARK 3 ORIGIN FOR THE GROUP (A): -24.8180 10.3106 38.2328
REMARK 3 T TENSOR
REMARK 3 T11: 0.1104 T22: 0.1730
REMARK 3 T33: 0.1479 T12: -0.0241
REMARK 3 T13: -0.0357 T23: -0.0178
REMARK 3 L TENSOR
REMARK 3 L11: 1.1040 L22: 4.0763
REMARK 3 L33: 0.6242 L12: -1.0994
REMARK 3 L13: -0.0865 L23: 0.9235
REMARK 3 S TENSOR
REMARK 3 S11: 0.0601 S12: 0.1533 S13: -0.2421
REMARK 3 S21: -0.3092 S22: -0.0868 S23: 0.4200
REMARK 3 S31: 0.0953 S32: -0.1048 S33: 0.0175
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 97 THROUGH 167 )
REMARK 3 ORIGIN FOR THE GROUP (A): -3.5152 21.4916 53.3245
REMARK 3 T TENSOR
REMARK 3 T11: 0.0444 T22: 0.1156
REMARK 3 T33: 0.1367 T12: -0.0253
REMARK 3 T13: 0.0094 T23: 0.0010
REMARK 3 L TENSOR
REMARK 3 L11: 0.1406 L22: 0.5222
REMARK 3 L33: 1.2566 L12: -0.2181
REMARK 3 L13: -0.3526 L23: -0.0273
REMARK 3 S TENSOR
REMARK 3 S11: 0.0073 S12: -0.0084 S13: 0.1009
REMARK 3 S21: 0.0020 S22: -0.0102 S23: -0.1409
REMARK 3 S31: -0.0204 S32: 0.1139 S33: 0.0039
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 168 THROUGH 191 )
REMARK 3 ORIGIN FOR THE GROUP (A): -13.4639 19.7879 75.1258
REMARK 3 T TENSOR
REMARK 3 T11: 0.1615 T22: 0.1361
REMARK 3 T33: 0.1213 T12: -0.0264
REMARK 3 T13: 0.0208 T23: 0.0056
REMARK 3 L TENSOR
REMARK 3 L11: 5.4295 L22: 3.8433
REMARK 3 L33: 2.9399 L12: -4.0533
REMARK 3 L13: 2.2864 L23: -1.6987
REMARK 3 S TENSOR
REMARK 3 S11: -0.2144 S12: -0.5295 S13: -0.2527
REMARK 3 S21: 0.4124 S22: 0.3571 S23: 0.1644
REMARK 3 S31: 0.0418 S32: -0.1973 S33: -0.1595
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 192 THROUGH 264 )
REMARK 3 ORIGIN FOR THE GROUP (A): -20.3064 29.1636 71.3826
REMARK 3 T TENSOR
REMARK 3 T11: 0.0952 T22: 0.1353
REMARK 3 T33: 0.1013 T12: -0.0087
REMARK 3 T13: 0.0404 T23: -0.0138
REMARK 3 L TENSOR
REMARK 3 L11: 1.0634 L22: 1.8796
REMARK 3 L33: 0.3657 L12: -0.4065
REMARK 3 L13: 0.1357 L23: -0.4051
REMARK 3 S TENSOR
REMARK 3 S11: -0.0441 S12: -0.1635 S13: 0.0528
REMARK 3 S21: 0.3095 S22: 0.0473 S23: 0.1602
REMARK 3 S31: -0.0022 S32: -0.0778 S33: -0.0000
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 265 THROUGH 312 )
REMARK 3 ORIGIN FOR THE GROUP (A): -14.5941 31.8888 56.1668
REMARK 3 T TENSOR
REMARK 3 T11: 0.0420 T22: 0.0810
REMARK 3 T33: 0.1106 T12: -0.0236
REMARK 3 T13: 0.0078 T23: 0.0028
REMARK 3 L TENSOR
REMARK 3 L11: 0.8365 L22: 0.9973
REMARK 3 L33: 2.6366 L12: -0.3254
REMARK 3 L13: 0.6441 L23: 1.0963
REMARK 3 S TENSOR
REMARK 3 S11: 0.0069 S12: 0.0045 S13: 0.0668
REMARK 3 S21: 0.0015 S22: -0.0279 S23: -0.0632
REMARK 3 S31: -0.0572 S32: -0.0428 S33: 0.0259
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 313 THROUGH 354 )
REMARK 3 ORIGIN FOR THE GROUP (A): 2.1128 19.6230 59.6957
REMARK 3 T TENSOR
REMARK 3 T11: 0.0723 T22: 0.1879
REMARK 3 T33: 0.2040 T12: 0.0022
REMARK 3 T13: -0.0127 T23: 0.0143
REMARK 3 L TENSOR
REMARK 3 L11: 0.6684 L22: 0.8956
REMARK 3 L33: 1.2476 L12: 0.3919
REMARK 3 L13: -0.6230 L23: 0.1066
REMARK 3 S TENSOR
REMARK 3 S11: -0.0740 S12: -0.0951 S13: -0.0229
REMARK 3 S21: 0.0056 S22: 0.0481 S23: -0.4228
REMARK 3 S31: 0.0569 S32: 0.3281 S33: 0.0205
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 355 THROUGH 435 )
REMARK 3 ORIGIN FOR THE GROUP (A): -32.4446 30.5855 49.4561
REMARK 3 T TENSOR
REMARK 3 T11: 0.0487 T22: 0.1411
REMARK 3 T33: 0.1304 T12: 0.0106
REMARK 3 T13: -0.0143 T23: 0.0008
REMARK 3 L TENSOR
REMARK 3 L11: 2.8311 L22: 1.1268
REMARK 3 L33: 1.0781 L12: -0.1785
REMARK 3 L13: -0.5512 L23: 0.2712
REMARK 3 S TENSOR
REMARK 3 S11: 0.0490 S12: -0.0644 S13: 0.1627
REMARK 3 S21: -0.0371 S22: -0.0514 S23: 0.2662
REMARK 3 S31: -0.0995 S32: -0.2225 S33: -0.0224
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 436 THROUGH 476 )
REMARK 3 ORIGIN FOR THE GROUP (A): -37.0820 27.4826 47.3742
REMARK 3 T TENSOR
REMARK 3 T11: 0.0513 T22: 0.1640
REMARK 3 T33: 0.1975 T12: -0.0118
REMARK 3 T13: -0.0213 T23: -0.0091
REMARK 3 L TENSOR
REMARK 3 L11: 1.6397 L22: 1.0016
REMARK 3 L33: 1.9186 L12: 0.0091
REMARK 3 L13: -1.2889 L23: -0.0691
REMARK 3 S TENSOR
REMARK 3 S11: 0.0870 S12: -0.0571 S13: -0.0085
REMARK 3 S21: -0.0999 S22: -0.0807 S23: 0.3016
REMARK 3 S31: -0.1087 S32: -0.2301 S33: -0.0134
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 5 THROUGH 38 )
REMARK 3 ORIGIN FOR THE GROUP (A): -10.3653 76.2905 26.6002
REMARK 3 T TENSOR
REMARK 3 T11: 0.4252 T22: 0.2743
REMARK 3 T33: 0.1994 T12: -0.0293
REMARK 3 T13: -0.1198 T23: -0.0115
REMARK 3 L TENSOR
REMARK 3 L11: 1.8518 L22: 2.1297
REMARK 3 L33: 1.7717 L12: 1.2760
REMARK 3 L13: -0.7397 L23: -1.2315
REMARK 3 S TENSOR
REMARK 3 S11: 0.1960 S12: -0.3324 S13: 0.0096
REMARK 3 S21: 0.5757 S22: -0.2744 S23: -0.2797
REMARK 3 S31: -0.3089 S32: 0.3779 S33: 0.0722
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 39 THROUGH 96 )
REMARK 3 ORIGIN FOR THE GROUP (A): -29.5446 70.7070 29.0470
REMARK 3 T TENSOR
REMARK 3 T11: 0.4449 T22: 0.2177
REMARK 3 T33: 0.1493 T12: 0.0083
REMARK 3 T13: 0.0150 T23: -0.0268
REMARK 3 L TENSOR
REMARK 3 L11: 0.8474 L22: 4.2705
REMARK 3 L33: 0.3460 L12: 1.6738
REMARK 3 L13: -0.2304 L23: -0.0997
REMARK 3 S TENSOR
REMARK 3 S11: 0.1874 S12: -0.1544 S13: 0.2629
REMARK 3 S21: 0.6942 S22: -0.1261 S23: 0.3594
REMARK 3 S31: -0.1596 S32: 0.0437 S33: -0.0584
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 97 THROUGH 167 )
REMARK 3 ORIGIN FOR THE GROUP (A): -21.8303 59.5020 3.8151
REMARK 3 T TENSOR
REMARK 3 T11: 0.2480 T22: 0.1106
REMARK 3 T33: 0.0988 T12: 0.0298
REMARK 3 T13: -0.0005 T23: -0.0037
REMARK 3 L TENSOR
REMARK 3 L11: 1.4004 L22: 1.0233
REMARK 3 L33: 0.9411 L12: 0.2764
REMARK 3 L13: 0.8231 L23: -0.1710
REMARK 3 S TENSOR
REMARK 3 S11: -0.0353 S12: 0.1534 S13: -0.0596
REMARK 3 S21: -0.1322 S22: 0.0240 S23: -0.0360
REMARK 3 S31: 0.0470 S32: 0.1483 S33: 0.0166
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 168 THROUGH 191 )
REMARK 3 ORIGIN FOR THE GROUP (A): -43.4587 60.8932 -6.8218
REMARK 3 T TENSOR
REMARK 3 T11: 0.4300 T22: 0.1831
REMARK 3 T33: 0.2339 T12: -0.0237
REMARK 3 T13: -0.1371 T23: 0.0059
REMARK 3 L TENSOR
REMARK 3 L11: 2.0545 L22: 3.0759
REMARK 3 L33: 5.0260 L12: 1.7126
REMARK 3 L13: -1.5747 L23: -2.9899
REMARK 3 S TENSOR
REMARK 3 S11: -0.0679 S12: 0.3558 S13: 0.0793
REMARK 3 S21: -0.5019 S22: 0.3312 S23: 0.4129
REMARK 3 S31: 0.1450 S32: -0.3085 S33: -0.2602
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 192 THROUGH 281 )
REMARK 3 ORIGIN FOR THE GROUP (A): -43.9999 50.8411 1.0242
REMARK 3 T TENSOR
REMARK 3 T11: 0.2655 T22: 0.1270
REMARK 3 T33: 0.1927 T12: -0.0263
REMARK 3 T13: -0.0859 T23: 0.0031
REMARK 3 L TENSOR
REMARK 3 L11: 0.6511 L22: 1.6232
REMARK 3 L33: 1.0437 L12: -0.1466
REMARK 3 L13: -0.4742 L23: -0.5133
REMARK 3 S TENSOR
REMARK 3 S11: -0.0598 S12: 0.1000 S13: 0.0039
REMARK 3 S21: -0.2365 S22: 0.0836 S23: 0.3609
REMARK 3 S31: 0.1351 S32: -0.2193 S33: -0.0179
REMARK 3 TLS GROUP : 24
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 282 THROUGH 354 )
REMARK 3 ORIGIN FOR THE GROUP (A): -27.0595 55.0733 3.4111
REMARK 3 T TENSOR
REMARK 3 T11: 0.2358 T22: 0.1137
REMARK 3 T33: 0.1151 T12: 0.0331
REMARK 3 T13: -0.0129 T23: -0.0067
REMARK 3 L TENSOR
REMARK 3 L11: 0.9839 L22: 2.3170
REMARK 3 L33: 1.6051 L12: 0.5382
REMARK 3 L13: 0.3149 L23: -0.0863
REMARK 3 S TENSOR
REMARK 3 S11: -0.0136 S12: 0.1331 S13: -0.0914
REMARK 3 S21: -0.1934 S22: 0.0104 S23: -0.1050
REMARK 3 S31: 0.1726 S32: 0.1386 S33: 0.0158
REMARK 3 TLS GROUP : 25
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 355 THROUGH 476 )
REMARK 3 ORIGIN FOR THE GROUP (A): -42.3012 50.4942 26.7615
REMARK 3 T TENSOR
REMARK 3 T11: 0.3323 T22: 0.1776
REMARK 3 T33: 0.1592 T12: 0.0420
REMARK 3 T13: 0.0152 T23: 0.0144
REMARK 3 L TENSOR
REMARK 3 L11: 2.2424 L22: 1.0061
REMARK 3 L33: 1.2943 L12: 0.5835
REMARK 3 L13: -0.2453 L23: -0.1259
REMARK 3 S TENSOR
REMARK 3 S11: 0.0615 S12: -0.2587 S13: -0.0292
REMARK 3 S21: 0.2672 S22: -0.0290 S23: 0.2352
REMARK 3 S31: -0.0499 S32: -0.2462 S33: -0.0246
REMARK 3 TLS GROUP : 26
REMARK 3 SELECTION: CHAIN 'D' AND (RESID -1 THROUGH 38 )
REMARK 3 ORIGIN FOR THE GROUP (A): -14.7498 56.2471 28.7883
REMARK 3 T TENSOR
REMARK 3 T11: 0.4076 T22: 0.2246
REMARK 3 T33: 0.1892 T12: 0.0198
REMARK 3 T13: -0.1079 T23: 0.0104
REMARK 3 L TENSOR
REMARK 3 L11: 0.6659 L22: 2.1753
REMARK 3 L33: 1.3212 L12: 0.5368
REMARK 3 L13: -0.0675 L23: -0.5931
REMARK 3 S TENSOR
REMARK 3 S11: 0.2428 S12: -0.3014 S13: -0.2285
REMARK 3 S21: 0.7145 S22: -0.2780 S23: -0.3361
REMARK 3 S31: -0.0151 S32: 0.1512 S33: 0.0489
REMARK 3 TLS GROUP : 27
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 39 THROUGH 96 )
REMARK 3 ORIGIN FOR THE GROUP (A): -6.9792 64.5772 10.5845
REMARK 3 T TENSOR
REMARK 3 T11: 0.2238 T22: 0.2267
REMARK 3 T33: 0.1971 T12: 0.0397
REMARK 3 T13: -0.0116 T23: 0.0022
REMARK 3 L TENSOR
REMARK 3 L11: 0.5817 L22: 5.6820
REMARK 3 L33: 1.0636 L12: 0.6754
REMARK 3 L13: -0.3254 L23: -2.2112
REMARK 3 S TENSOR
REMARK 3 S11: -0.0465 S12: 0.0281 S13: -0.2075
REMARK 3 S21: -0.2560 S22: -0.1038 S23: -0.5549
REMARK 3 S31: 0.1778 S32: 0.1722 S33: 0.1056
REMARK 3 TLS GROUP : 28
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 97 THROUGH 167 )
REMARK 3 ORIGIN FOR THE GROUP (A): -33.1504 76.5715 13.4368
REMARK 3 T TENSOR
REMARK 3 T11: 0.2643 T22: 0.1290
REMARK 3 T33: 0.1157 T12: 0.0207
REMARK 3 T13: 0.0148 T23: -0.0098
REMARK 3 L TENSOR
REMARK 3 L11: 0.7074 L22: 1.2495
REMARK 3 L33: 1.6115 L12: -0.1249
REMARK 3 L13: 0.6452 L23: -0.4273
REMARK 3 S TENSOR
REMARK 3 S11: 0.0575 S12: -0.1048 S13: 0.0481
REMARK 3 S21: 0.1176 S22: 0.0462 S23: 0.1672
REMARK 3 S31: -0.0544 S32: -0.0695 S33: -0.1098
REMARK 3 TLS GROUP : 29
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 168 THROUGH 191 )
REMARK 3 ORIGIN FOR THE GROUP (A): -39.2551 76.0186 -9.6742
REMARK 3 T TENSOR
REMARK 3 T11: 0.4483 T22: 0.1968
REMARK 3 T33: 0.1913 T12: 0.0197
REMARK 3 T13: -0.0943 T23: 0.0136
REMARK 3 L TENSOR
REMARK 3 L11: 5.3658 L22: 3.1905
REMARK 3 L33: 1.5838 L12: 3.1257
REMARK 3 L13: -1.3278 L23: -1.4706
REMARK 3 S TENSOR
REMARK 3 S11: -0.1226 S12: 0.5059 S13: -0.2759
REMARK 3 S21: -0.4973 S22: 0.2348 S23: 0.1764
REMARK 3 S31: 0.1095 S32: -0.2927 S33: -0.1342
REMARK 3 TLS GROUP : 30
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 192 THROUGH 281 )
REMARK 3 ORIGIN FOR THE GROUP (A): -31.1464 85.8301 -8.3323
REMARK 3 T TENSOR
REMARK 3 T11: 0.3706 T22: 0.1402
REMARK 3 T33: 0.1314 T12: 0.0299
REMARK 3 T13: -0.0465 T23: 0.0297
REMARK 3 L TENSOR
REMARK 3 L11: 0.9901 L22: 0.9931
REMARK 3 L33: 0.4929 L12: 0.3058
REMARK 3 L13: -0.1065 L23: 0.2921
REMARK 3 S TENSOR
REMARK 3 S11: 0.0775 S12: 0.1748 S13: 0.0820
REMARK 3 S21: -0.3608 S22: -0.0280 S23: 0.1215
REMARK 3 S31: 0.0134 S32: -0.0405 S33: -0.0470
REMARK 3 TLS GROUP : 31
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 282 THROUGH 354 )
REMARK 3 ORIGIN FOR THE GROUP (A): -31.9376 81.4899 8.2776
REMARK 3 T TENSOR
REMARK 3 T11: 0.2458 T22: 0.1095
REMARK 3 T33: 0.0876 T12: 0.0285
REMARK 3 T13: 0.0039 T23: -0.0173
REMARK 3 L TENSOR
REMARK 3 L11: 1.7927 L22: 1.6447
REMARK 3 L33: 0.8294 L12: 0.3133
REMARK 3 L13: 0.3470 L23: -0.2578
REMARK 3 S TENSOR
REMARK 3 S11: -0.0240 S12: -0.1172 S13: 0.1304
REMARK 3 S21: 0.0376 S22: 0.0341 S23: 0.1492
REMARK 3 S31: -0.1152 S32: -0.0501 S33: -0.0174
REMARK 3 TLS GROUP : 32
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 355 THROUGH 476 )
REMARK 3 ORIGIN FOR THE GROUP (A): -6.4910 85.0021 -1.3500
REMARK 3 T TENSOR
REMARK 3 T11: 0.2467 T22: 0.1812
REMARK 3 T33: 0.1530 T12: 0.0228
REMARK 3 T13: 0.0169 T23: -0.0066
REMARK 3 L TENSOR
REMARK 3 L11: 1.7320 L22: 1.1904
REMARK 3 L33: 1.8710 L12: -0.0375
REMARK 3 L13: -0.7944 L23: -0.8958
REMARK 3 S TENSOR
REMARK 3 S11: 0.1976 S12: 0.1938 S13: 0.1095
REMARK 3 S21: -0.1670 S22: -0.1819 S23: -0.2327
REMARK 3 S31: -0.0401 S32: 0.2189 S33: -0.0204
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 4RJ0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-OCT-14.
REMARK 100 THE DEPOSITION ID IS D_1000087405.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JAN-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97924
REMARK 200 MONOCHROMATOR : SI 111, CHANNEL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 144197
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.950
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 (%) : 93.1
REMARK 200 DATA REDUNDANCY : 3.100
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.98
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.00
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.59300
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MLPHARE
REMARK 200 STARTING MODEL: 4RIT
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.43
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.59
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.04M KPO4, 16% PEG8K, 20% GLYCEROL,
REMARK 280 PH 7.5, VAPOR DIFFUSION, SITTING DROP, 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 62.09900
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: 13790 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 29800 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -107.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 14180 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 29870 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -119.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 SER B -2
REMARK 465 THR B 49
REMARK 465 VAL B 50
REMARK 465 ASP B 51
REMARK 465 LEU B 52
REMARK 465 PRO B 53
REMARK 465 GLY B 54
REMARK 465 PRO B 55
REMARK 465 ARG B 477
REMARK 465 GLU B 478
REMARK 465 ARG B 479
REMARK 465 GLY B 480
REMARK 465 GLN B 481
REMARK 465 GLU B 482
REMARK 465 ARG B 483
REMARK 465 SER A -2
REMARK 465 ASN A -1
REMARK 465 ALA A 0
REMARK 465 MET A 1
REMARK 465 ASP A 2
REMARK 465 SER A 3
REMARK 465 THR A 49
REMARK 465 VAL A 50
REMARK 465 ASP A 51
REMARK 465 LEU A 52
REMARK 465 PRO A 53
REMARK 465 GLY A 54
REMARK 465 ARG A 477
REMARK 465 GLU A 478
REMARK 465 ARG A 479
REMARK 465 GLY A 480
REMARK 465 GLN A 481
REMARK 465 GLU A 482
REMARK 465 ARG A 483
REMARK 465 SER C -2
REMARK 465 ASN C -1
REMARK 465 ALA C 0
REMARK 465 MET C 1
REMARK 465 ASP C 2
REMARK 465 SER C 3
REMARK 465 ARG C 4
REMARK 465 VAL C 50
REMARK 465 ASP C 51
REMARK 465 LEU C 52
REMARK 465 ASN C 333
REMARK 465 MET C 334
REMARK 465 ARG C 335
REMARK 465 ALA C 336
REMARK 465 THR C 337
REMARK 465 ASP C 338
REMARK 465 ARG C 477
REMARK 465 GLU C 478
REMARK 465 ARG C 479
REMARK 465 GLY C 480
REMARK 465 GLN C 481
REMARK 465 GLU C 482
REMARK 465 ARG C 483
REMARK 465 SER D -2
REMARK 465 ASP D 51
REMARK 465 LEU D 52
REMARK 465 ALA D 331
REMARK 465 PRO D 332
REMARK 465 ASN D 333
REMARK 465 MET D 334
REMARK 465 ARG D 335
REMARK 465 ALA D 336
REMARK 465 THR D 337
REMARK 465 ASP D 338
REMARK 465 ARG D 477
REMARK 465 GLU D 478
REMARK 465 ARG D 479
REMARK 465 GLY D 480
REMARK 465 GLN D 481
REMARK 465 GLU D 482
REMARK 465 ARG D 483
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 ASN B -1 CG OD1 ND2
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 OG1 THR B 351 OP1 LLP A 304 2.16
REMARK 500 NH1 ARG C 373 OD1 ASP C 377 2.17
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 LEU B 193 O - C - N ANGL. DEV. = -9.6 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 MET B 91 46.16 -83.16
REMARK 500 SER B 119 59.04 -151.50
REMARK 500 LLP B 304 -98.49 -92.96
REMARK 500 PHE B 327 -59.87 -155.49
REMARK 500 ASN B 404 49.43 -82.23
REMARK 500 MET A 91 48.25 -82.35
REMARK 500 SER A 119 65.14 -154.62
REMARK 500 LLP A 304 -95.66 -87.32
REMARK 500 PHE A 327 -58.99 -156.70
REMARK 500 ASN A 404 47.18 -82.53
REMARK 500 PRO C 55 136.84 -38.64
REMARK 500 MET C 91 45.85 -82.18
REMARK 500 ALA C 273 40.60 -107.12
REMARK 500 LLP C 304 -91.40 -92.38
REMARK 500 PHE C 327 -55.97 -143.59
REMARK 500 ASN C 404 43.18 -80.68
REMARK 500 MET D 91 46.68 -82.71
REMARK 500 LLP D 304 -75.79 -95.14
REMARK 500 PHE D 327 -55.62 -144.17
REMARK 500 ASN D 404 38.48 -84.48
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PMP D 2001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 2002
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: MCSG-APC100677 RELATED DB: TARGETTRACK
DBREF 4RJ0 B 1 483 UNP D1C7D8 D1C7D8_SPHTD 1 483
DBREF 4RJ0 A 1 483 UNP D1C7D8 D1C7D8_SPHTD 1 483
DBREF 4RJ0 C 1 483 UNP D1C7D8 D1C7D8_SPHTD 1 483
DBREF 4RJ0 D 1 483 UNP D1C7D8 D1C7D8_SPHTD 1 483
SEQADV 4RJ0 SER B -2 UNP D1C7D8 EXPRESSION TAG
SEQADV 4RJ0 ASN B -1 UNP D1C7D8 EXPRESSION TAG
SEQADV 4RJ0 ALA B 0 UNP D1C7D8 EXPRESSION TAG
SEQADV 4RJ0 ASN B 333 UNP D1C7D8 TYR 333 ENGINEERED MUTATION
SEQADV 4RJ0 SER A -2 UNP D1C7D8 EXPRESSION TAG
SEQADV 4RJ0 ASN A -1 UNP D1C7D8 EXPRESSION TAG
SEQADV 4RJ0 ALA A 0 UNP D1C7D8 EXPRESSION TAG
SEQADV 4RJ0 ASN A 333 UNP D1C7D8 TYR 333 ENGINEERED MUTATION
SEQADV 4RJ0 SER C -2 UNP D1C7D8 EXPRESSION TAG
SEQADV 4RJ0 ASN C -1 UNP D1C7D8 EXPRESSION TAG
SEQADV 4RJ0 ALA C 0 UNP D1C7D8 EXPRESSION TAG
SEQADV 4RJ0 ASN C 333 UNP D1C7D8 TYR 333 ENGINEERED MUTATION
SEQADV 4RJ0 SER D -2 UNP D1C7D8 EXPRESSION TAG
SEQADV 4RJ0 ASN D -1 UNP D1C7D8 EXPRESSION TAG
SEQADV 4RJ0 ALA D 0 UNP D1C7D8 EXPRESSION TAG
SEQADV 4RJ0 ASN D 333 UNP D1C7D8 TYR 333 ENGINEERED MUTATION
SEQRES 1 B 486 SER ASN ALA MET ASP SER ARG PHE LEU PRO ALA THR ALA
SEQRES 2 B 486 PHE ILE ASP PRO GLU GLY ARG ASN ARG ASN GLU VAL GLU
SEQRES 3 B 486 ARG LEU VAL GLN GLN VAL VAL ASP LEU ILE LEU ALA LYS
SEQRES 4 B 486 LEU THR GLY ALA ALA GLU ARG PRO PRO MET PRO GLU THR
SEQRES 5 B 486 VAL ASP LEU PRO GLY PRO ILE THR ILE PRO GLU ALA ALA
SEQRES 6 B 486 ALA THR GLU ALA THR LEU LEU GLN ALA ILE ARG ASP MET
SEQRES 7 B 486 VAL ASP GLY SER MET ASN PRO ALA ASN PRO GLY TYR ILE
SEQRES 8 B 486 GLY HIS MET ASP PRO MET PRO ALA THR MET ALA ILE LEU
SEQRES 9 B 486 GLY ASP LEU VAL ALA ALA ALA VAL ASN ASN ASN MET LEU
SEQRES 10 B 486 SER LEU GLU MET SER PRO SER PHE SER ARG LEU GLU THR
SEQRES 11 B 486 LEU LEU LEU ARG ALA ILE ALA GLY LEU PHE GLY LEU GLY
SEQRES 12 B 486 GLU GLN ALA GLY GLY VAL LEU THR SER GLY GLY SER LEU
SEQRES 13 B 486 ALA ASN LEU GLN ALA LEU ALA VAL ALA ARG ASN VAL ALA
SEQRES 14 B 486 PHE ASP SER VAL GLU PRO GLY ILE THR GLY LEU ALA GLN
SEQRES 15 B 486 ARG PRO VAL ILE PHE ALA SER GLU ALA ALA HIS THR SER
SEQRES 16 B 486 LEU GLN LYS ALA ALA MET LEU LEU GLY LEU GLY THR ALA
SEQRES 17 B 486 ALA VAL ILE PRO VAL ARG ALA THR ALA ASP SER ARG MET
SEQRES 18 B 486 ASP PRO GLU ASP LEU ARG ALA ARG ILE ASP GLN ALA ARG
SEQRES 19 B 486 GLY ALA GLY GLN HIS PRO PHE CYS VAL VAL ALA THR ALA
SEQRES 20 B 486 GLY THR THR THR THR GLY ASN ILE ASP PRO LEU ALA GLU
SEQRES 21 B 486 ILE GLY ALA ILE ALA ARG GLU HIS GLY LEU TRP PHE HIS
SEQRES 22 B 486 VAL ASP ALA ALA TYR GLY GLY ALA LEU VAL PHE SER GLU
SEQRES 23 B 486 ARG HIS ARG TRP ARG LEU ALA GLY ILE GLU GLN ALA ASP
SEQRES 24 B 486 SER ILE THR PHE ASN PRO GLN LLP TRP LEU TYR VAL ALA
SEQRES 25 B 486 LYS THR CYS ALA MET VAL LEU PHE ARG ASP ALA GLY VAL
SEQRES 26 B 486 LEU GLU ARG ALA PHE ARG ILE PRO ALA PRO ASN MET ARG
SEQRES 27 B 486 ALA THR ASP GLY PHE ILE ASN LEU GLY GLU ILE GLY VAL
SEQRES 28 B 486 GLN GLY THR ARG HIS ALA ASP VAL VAL LYS LEU TRP LEU
SEQRES 29 B 486 THR LEU GLN HIS ILE GLY GLN GLN GLY TYR ALA ARG LEU
SEQRES 30 B 486 ILE ASP ASP GLY TYR ARG LEU ALA GLU ARG VAL VAL GLU
SEQRES 31 B 486 GLY VAL ARG GLN ARG PRO PHE LEU ARG LEU ALA GLY GLU
SEQRES 32 B 486 ILE ASP THR ASN ILE VAL CYS PHE ARG GLY GLU PRO ASP
SEQRES 33 B 486 TRP LEU PRO ALA GLU ARG TRP ASP ASP TRP ASN ALA ALA
SEQRES 34 B 486 LEU GLN ALA LEU LEU LEU ARG GLU GLY LYS ILE PHE LEU
SEQRES 35 B 486 SER LEU PRO VAL TYR ARG GLY GLY ARG TRP LEU ARG ALA
SEQRES 36 B 486 VAL LEU LEU ASN PRO TYR THR THR ASP ALA VAL ILE ASP
SEQRES 37 B 486 ALA MET PHE LYS GLN ILE ASP ARG PHE ALA GLY ARG GLU
SEQRES 38 B 486 ARG GLY GLN GLU ARG
SEQRES 1 A 486 SER ASN ALA MET ASP SER ARG PHE LEU PRO ALA THR ALA
SEQRES 2 A 486 PHE ILE ASP PRO GLU GLY ARG ASN ARG ASN GLU VAL GLU
SEQRES 3 A 486 ARG LEU VAL GLN GLN VAL VAL ASP LEU ILE LEU ALA LYS
SEQRES 4 A 486 LEU THR GLY ALA ALA GLU ARG PRO PRO MET PRO GLU THR
SEQRES 5 A 486 VAL ASP LEU PRO GLY PRO ILE THR ILE PRO GLU ALA ALA
SEQRES 6 A 486 ALA THR GLU ALA THR LEU LEU GLN ALA ILE ARG ASP MET
SEQRES 7 A 486 VAL ASP GLY SER MET ASN PRO ALA ASN PRO GLY TYR ILE
SEQRES 8 A 486 GLY HIS MET ASP PRO MET PRO ALA THR MET ALA ILE LEU
SEQRES 9 A 486 GLY ASP LEU VAL ALA ALA ALA VAL ASN ASN ASN MET LEU
SEQRES 10 A 486 SER LEU GLU MET SER PRO SER PHE SER ARG LEU GLU THR
SEQRES 11 A 486 LEU LEU LEU ARG ALA ILE ALA GLY LEU PHE GLY LEU GLY
SEQRES 12 A 486 GLU GLN ALA GLY GLY VAL LEU THR SER GLY GLY SER LEU
SEQRES 13 A 486 ALA ASN LEU GLN ALA LEU ALA VAL ALA ARG ASN VAL ALA
SEQRES 14 A 486 PHE ASP SER VAL GLU PRO GLY ILE THR GLY LEU ALA GLN
SEQRES 15 A 486 ARG PRO VAL ILE PHE ALA SER GLU ALA ALA HIS THR SER
SEQRES 16 A 486 LEU GLN LYS ALA ALA MET LEU LEU GLY LEU GLY THR ALA
SEQRES 17 A 486 ALA VAL ILE PRO VAL ARG ALA THR ALA ASP SER ARG MET
SEQRES 18 A 486 ASP PRO GLU ASP LEU ARG ALA ARG ILE ASP GLN ALA ARG
SEQRES 19 A 486 GLY ALA GLY GLN HIS PRO PHE CYS VAL VAL ALA THR ALA
SEQRES 20 A 486 GLY THR THR THR THR GLY ASN ILE ASP PRO LEU ALA GLU
SEQRES 21 A 486 ILE GLY ALA ILE ALA ARG GLU HIS GLY LEU TRP PHE HIS
SEQRES 22 A 486 VAL ASP ALA ALA TYR GLY GLY ALA LEU VAL PHE SER GLU
SEQRES 23 A 486 ARG HIS ARG TRP ARG LEU ALA GLY ILE GLU GLN ALA ASP
SEQRES 24 A 486 SER ILE THR PHE ASN PRO GLN LLP TRP LEU TYR VAL ALA
SEQRES 25 A 486 LYS THR CYS ALA MET VAL LEU PHE ARG ASP ALA GLY VAL
SEQRES 26 A 486 LEU GLU ARG ALA PHE ARG ILE PRO ALA PRO ASN MET ARG
SEQRES 27 A 486 ALA THR ASP GLY PHE ILE ASN LEU GLY GLU ILE GLY VAL
SEQRES 28 A 486 GLN GLY THR ARG HIS ALA ASP VAL VAL LYS LEU TRP LEU
SEQRES 29 A 486 THR LEU GLN HIS ILE GLY GLN GLN GLY TYR ALA ARG LEU
SEQRES 30 A 486 ILE ASP ASP GLY TYR ARG LEU ALA GLU ARG VAL VAL GLU
SEQRES 31 A 486 GLY VAL ARG GLN ARG PRO PHE LEU ARG LEU ALA GLY GLU
SEQRES 32 A 486 ILE ASP THR ASN ILE VAL CYS PHE ARG GLY GLU PRO ASP
SEQRES 33 A 486 TRP LEU PRO ALA GLU ARG TRP ASP ASP TRP ASN ALA ALA
SEQRES 34 A 486 LEU GLN ALA LEU LEU LEU ARG GLU GLY LYS ILE PHE LEU
SEQRES 35 A 486 SER LEU PRO VAL TYR ARG GLY GLY ARG TRP LEU ARG ALA
SEQRES 36 A 486 VAL LEU LEU ASN PRO TYR THR THR ASP ALA VAL ILE ASP
SEQRES 37 A 486 ALA MET PHE LYS GLN ILE ASP ARG PHE ALA GLY ARG GLU
SEQRES 38 A 486 ARG GLY GLN GLU ARG
SEQRES 1 C 486 SER ASN ALA MET ASP SER ARG PHE LEU PRO ALA THR ALA
SEQRES 2 C 486 PHE ILE ASP PRO GLU GLY ARG ASN ARG ASN GLU VAL GLU
SEQRES 3 C 486 ARG LEU VAL GLN GLN VAL VAL ASP LEU ILE LEU ALA LYS
SEQRES 4 C 486 LEU THR GLY ALA ALA GLU ARG PRO PRO MET PRO GLU THR
SEQRES 5 C 486 VAL ASP LEU PRO GLY PRO ILE THR ILE PRO GLU ALA ALA
SEQRES 6 C 486 ALA THR GLU ALA THR LEU LEU GLN ALA ILE ARG ASP MET
SEQRES 7 C 486 VAL ASP GLY SER MET ASN PRO ALA ASN PRO GLY TYR ILE
SEQRES 8 C 486 GLY HIS MET ASP PRO MET PRO ALA THR MET ALA ILE LEU
SEQRES 9 C 486 GLY ASP LEU VAL ALA ALA ALA VAL ASN ASN ASN MET LEU
SEQRES 10 C 486 SER LEU GLU MET SER PRO SER PHE SER ARG LEU GLU THR
SEQRES 11 C 486 LEU LEU LEU ARG ALA ILE ALA GLY LEU PHE GLY LEU GLY
SEQRES 12 C 486 GLU GLN ALA GLY GLY VAL LEU THR SER GLY GLY SER LEU
SEQRES 13 C 486 ALA ASN LEU GLN ALA LEU ALA VAL ALA ARG ASN VAL ALA
SEQRES 14 C 486 PHE ASP SER VAL GLU PRO GLY ILE THR GLY LEU ALA GLN
SEQRES 15 C 486 ARG PRO VAL ILE PHE ALA SER GLU ALA ALA HIS THR SER
SEQRES 16 C 486 LEU GLN LYS ALA ALA MET LEU LEU GLY LEU GLY THR ALA
SEQRES 17 C 486 ALA VAL ILE PRO VAL ARG ALA THR ALA ASP SER ARG MET
SEQRES 18 C 486 ASP PRO GLU ASP LEU ARG ALA ARG ILE ASP GLN ALA ARG
SEQRES 19 C 486 GLY ALA GLY GLN HIS PRO PHE CYS VAL VAL ALA THR ALA
SEQRES 20 C 486 GLY THR THR THR THR GLY ASN ILE ASP PRO LEU ALA GLU
SEQRES 21 C 486 ILE GLY ALA ILE ALA ARG GLU HIS GLY LEU TRP PHE HIS
SEQRES 22 C 486 VAL ASP ALA ALA TYR GLY GLY ALA LEU VAL PHE SER GLU
SEQRES 23 C 486 ARG HIS ARG TRP ARG LEU ALA GLY ILE GLU GLN ALA ASP
SEQRES 24 C 486 SER ILE THR PHE ASN PRO GLN LLP TRP LEU TYR VAL ALA
SEQRES 25 C 486 LYS THR CYS ALA MET VAL LEU PHE ARG ASP ALA GLY VAL
SEQRES 26 C 486 LEU GLU ARG ALA PHE ARG ILE PRO ALA PRO ASN MET ARG
SEQRES 27 C 486 ALA THR ASP GLY PHE ILE ASN LEU GLY GLU ILE GLY VAL
SEQRES 28 C 486 GLN GLY THR ARG HIS ALA ASP VAL VAL LYS LEU TRP LEU
SEQRES 29 C 486 THR LEU GLN HIS ILE GLY GLN GLN GLY TYR ALA ARG LEU
SEQRES 30 C 486 ILE ASP ASP GLY TYR ARG LEU ALA GLU ARG VAL VAL GLU
SEQRES 31 C 486 GLY VAL ARG GLN ARG PRO PHE LEU ARG LEU ALA GLY GLU
SEQRES 32 C 486 ILE ASP THR ASN ILE VAL CYS PHE ARG GLY GLU PRO ASP
SEQRES 33 C 486 TRP LEU PRO ALA GLU ARG TRP ASP ASP TRP ASN ALA ALA
SEQRES 34 C 486 LEU GLN ALA LEU LEU LEU ARG GLU GLY LYS ILE PHE LEU
SEQRES 35 C 486 SER LEU PRO VAL TYR ARG GLY GLY ARG TRP LEU ARG ALA
SEQRES 36 C 486 VAL LEU LEU ASN PRO TYR THR THR ASP ALA VAL ILE ASP
SEQRES 37 C 486 ALA MET PHE LYS GLN ILE ASP ARG PHE ALA GLY ARG GLU
SEQRES 38 C 486 ARG GLY GLN GLU ARG
SEQRES 1 D 486 SER ASN ALA MET ASP SER ARG PHE LEU PRO ALA THR ALA
SEQRES 2 D 486 PHE ILE ASP PRO GLU GLY ARG ASN ARG ASN GLU VAL GLU
SEQRES 3 D 486 ARG LEU VAL GLN GLN VAL VAL ASP LEU ILE LEU ALA LYS
SEQRES 4 D 486 LEU THR GLY ALA ALA GLU ARG PRO PRO MET PRO GLU THR
SEQRES 5 D 486 VAL ASP LEU PRO GLY PRO ILE THR ILE PRO GLU ALA ALA
SEQRES 6 D 486 ALA THR GLU ALA THR LEU LEU GLN ALA ILE ARG ASP MET
SEQRES 7 D 486 VAL ASP GLY SER MET ASN PRO ALA ASN PRO GLY TYR ILE
SEQRES 8 D 486 GLY HIS MET ASP PRO MET PRO ALA THR MET ALA ILE LEU
SEQRES 9 D 486 GLY ASP LEU VAL ALA ALA ALA VAL ASN ASN ASN MET LEU
SEQRES 10 D 486 SER LEU GLU MET SER PRO SER PHE SER ARG LEU GLU THR
SEQRES 11 D 486 LEU LEU LEU ARG ALA ILE ALA GLY LEU PHE GLY LEU GLY
SEQRES 12 D 486 GLU GLN ALA GLY GLY VAL LEU THR SER GLY GLY SER LEU
SEQRES 13 D 486 ALA ASN LEU GLN ALA LEU ALA VAL ALA ARG ASN VAL ALA
SEQRES 14 D 486 PHE ASP SER VAL GLU PRO GLY ILE THR GLY LEU ALA GLN
SEQRES 15 D 486 ARG PRO VAL ILE PHE ALA SER GLU ALA ALA HIS THR SER
SEQRES 16 D 486 LEU GLN LYS ALA ALA MET LEU LEU GLY LEU GLY THR ALA
SEQRES 17 D 486 ALA VAL ILE PRO VAL ARG ALA THR ALA ASP SER ARG MET
SEQRES 18 D 486 ASP PRO GLU ASP LEU ARG ALA ARG ILE ASP GLN ALA ARG
SEQRES 19 D 486 GLY ALA GLY GLN HIS PRO PHE CYS VAL VAL ALA THR ALA
SEQRES 20 D 486 GLY THR THR THR THR GLY ASN ILE ASP PRO LEU ALA GLU
SEQRES 21 D 486 ILE GLY ALA ILE ALA ARG GLU HIS GLY LEU TRP PHE HIS
SEQRES 22 D 486 VAL ASP ALA ALA TYR GLY GLY ALA LEU VAL PHE SER GLU
SEQRES 23 D 486 ARG HIS ARG TRP ARG LEU ALA GLY ILE GLU GLN ALA ASP
SEQRES 24 D 486 SER ILE THR PHE ASN PRO GLN LLP TRP LEU TYR VAL ALA
SEQRES 25 D 486 LYS THR CYS ALA MET VAL LEU PHE ARG ASP ALA GLY VAL
SEQRES 26 D 486 LEU GLU ARG ALA PHE ARG ILE PRO ALA PRO ASN MET ARG
SEQRES 27 D 486 ALA THR ASP GLY PHE ILE ASN LEU GLY GLU ILE GLY VAL
SEQRES 28 D 486 GLN GLY THR ARG HIS ALA ASP VAL VAL LYS LEU TRP LEU
SEQRES 29 D 486 THR LEU GLN HIS ILE GLY GLN GLN GLY TYR ALA ARG LEU
SEQRES 30 D 486 ILE ASP ASP GLY TYR ARG LEU ALA GLU ARG VAL VAL GLU
SEQRES 31 D 486 GLY VAL ARG GLN ARG PRO PHE LEU ARG LEU ALA GLY GLU
SEQRES 32 D 486 ILE ASP THR ASN ILE VAL CYS PHE ARG GLY GLU PRO ASP
SEQRES 33 D 486 TRP LEU PRO ALA GLU ARG TRP ASP ASP TRP ASN ALA ALA
SEQRES 34 D 486 LEU GLN ALA LEU LEU LEU ARG GLU GLY LYS ILE PHE LEU
SEQRES 35 D 486 SER LEU PRO VAL TYR ARG GLY GLY ARG TRP LEU ARG ALA
SEQRES 36 D 486 VAL LEU LEU ASN PRO TYR THR THR ASP ALA VAL ILE ASP
SEQRES 37 D 486 ALA MET PHE LYS GLN ILE ASP ARG PHE ALA GLY ARG GLU
SEQRES 38 D 486 ARG GLY GLN GLU ARG
MODRES 4RJ0 LLP B 304 LYS
MODRES 4RJ0 LLP A 304 LYS
MODRES 4RJ0 LLP C 304 LYS
MODRES 4RJ0 LLP D 304 LYS
HET LLP B 304 24
HET LLP A 304 24
HET LLP C 304 24
HET LLP D 304 24
HET GOL A 501 6
HET GOL A 502 6
HET PO4 C 501 5
HET PMP D2001 16
HET GOL D2002 6
HETNAM LLP (2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-
HETNAM 2 LLP (PHOSPHONOOXYMETHYL)PYRIDIN-4-
HETNAM 3 LLP YL]METHYLIDENEAMINO]HEXANOIC ACID
HETNAM GOL GLYCEROL
HETNAM PO4 PHOSPHATE ION
HETNAM PMP 4'-DEOXY-4'-AMINOPYRIDOXAL-5'-PHOSPHATE
HETSYN LLP N'-PYRIDOXYL-LYSINE-5'-MONOPHOSPHATE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
HETSYN PMP PYRIDOXAMINE-5'-PHOSPHATE
FORMUL 1 LLP 4(C14 H22 N3 O7 P)
FORMUL 5 GOL 3(C3 H8 O3)
FORMUL 7 PO4 O4 P 3-
FORMUL 8 PMP C8 H13 N2 O5 P
FORMUL 10 HOH *741(H2 O)
HELIX 1 1 ASN B -1 SER B 3 5 5
HELIX 2 2 ASN B 18 GLY B 39 1 22
HELIX 3 3 ALA B 40 ARG B 43 5 4
HELIX 4 4 THR B 64 GLY B 78 1 15
HELIX 5 5 ALA B 96 ASN B 110 1 15
HELIX 6 6 SER B 115 MET B 118 5 4
HELIX 7 7 SER B 119 PHE B 137 1 19
HELIX 8 8 GLY B 150 ASP B 168 1 19
HELIX 9 9 THR B 191 LEU B 200 1 10
HELIX 10 10 GLY B 203 ALA B 205 5 3
HELIX 11 11 ASP B 219 ALA B 233 1 15
HELIX 12 12 PRO B 254 HIS B 265 1 12
HELIX 13 13 TYR B 275 SER B 282 5 8
HELIX 14 14 HIS B 285 ALA B 290 5 6
HELIX 15 15 GLY B 291 ALA B 295 5 5
HELIX 16 16 GLY B 321 ALA B 326 1 6
HELIX 17 17 ASN B 342 GLY B 347 5 6
HELIX 18 18 ASP B 355 ARG B 392 1 38
HELIX 19 19 PRO B 416 GLU B 418 5 3
HELIX 20 20 ARG B 419 GLU B 434 1 16
HELIX 21 21 THR B 460 ALA B 475 1 16
HELIX 22 22 ASN A 18 GLY A 39 1 22
HELIX 23 23 ALA A 40 ARG A 43 5 4
HELIX 24 24 THR A 64 GLY A 78 1 15
HELIX 25 25 ALA A 96 ASN A 110 1 15
HELIX 26 26 SER A 119 PHE A 137 1 19
HELIX 27 27 GLY A 150 ASP A 168 1 19
HELIX 28 28 THR A 191 LEU A 200 1 10
HELIX 29 29 GLY A 203 ALA A 205 5 3
HELIX 30 30 ASP A 219 ALA A 233 1 15
HELIX 31 31 PRO A 254 HIS A 265 1 12
HELIX 32 32 TYR A 275 SER A 282 5 8
HELIX 33 33 HIS A 285 ALA A 290 5 6
HELIX 34 34 GLY A 291 ALA A 295 5 5
HELIX 35 35 GLY A 321 ALA A 326 1 6
HELIX 36 36 ASN A 342 GLY A 347 5 6
HELIX 37 37 ASP A 355 GLN A 391 1 37
HELIX 38 38 PRO A 416 GLU A 418 5 3
HELIX 39 39 ARG A 419 LYS A 436 1 18
HELIX 40 40 THR A 460 GLY A 476 1 17
HELIX 41 41 ASN C 18 GLY C 39 1 22
HELIX 42 42 ALA C 40 ARG C 43 5 4
HELIX 43 43 THR C 64 GLY C 78 1 15
HELIX 44 44 ALA C 96 ASN C 110 1 15
HELIX 45 45 SER C 115 MET C 118 5 4
HELIX 46 46 SER C 119 GLY C 138 1 20
HELIX 47 47 GLY C 150 ASP C 168 1 19
HELIX 48 48 THR C 191 LEU C 200 1 10
HELIX 49 49 GLY C 203 ALA C 205 5 3
HELIX 50 50 ASP C 219 ALA C 233 1 15
HELIX 51 51 PRO C 254 HIS C 265 1 12
HELIX 52 52 TYR C 275 SER C 282 5 8
HELIX 53 53 HIS C 285 ALA C 290 5 6
HELIX 54 54 GLY C 291 ALA C 295 5 5
HELIX 55 55 ASN C 301 LEU C 306 1 6
HELIX 56 56 GLY C 321 PHE C 327 1 7
HELIX 57 57 ASN C 342 GLY C 347 5 6
HELIX 58 58 ASP C 355 ARG C 392 1 38
HELIX 59 59 PRO C 416 GLU C 434 1 19
HELIX 60 60 THR C 460 GLY C 476 1 17
HELIX 61 61 ASN D 18 GLY D 39 1 22
HELIX 62 62 ALA D 40 ARG D 43 5 4
HELIX 63 63 THR D 64 GLY D 78 1 15
HELIX 64 64 ALA D 96 ASN D 110 1 15
HELIX 65 65 SER D 119 GLY D 138 1 20
HELIX 66 66 GLY D 150 ASP D 168 1 19
HELIX 67 67 THR D 191 LEU D 200 1 10
HELIX 68 68 GLY D 203 ALA D 205 5 3
HELIX 69 69 ASP D 219 ALA D 233 1 15
HELIX 70 70 PRO D 254 HIS D 265 1 12
HELIX 71 71 TYR D 275 SER D 282 5 8
HELIX 72 72 HIS D 285 ALA D 290 5 6
HELIX 73 73 GLY D 291 ALA D 295 5 5
HELIX 74 74 ASN D 301 LEU D 306 1 6
HELIX 75 75 GLY D 321 ALA D 326 1 6
HELIX 76 76 ASN D 342 GLY D 347 5 6
HELIX 77 77 ASP D 355 ARG D 392 1 38
HELIX 78 78 PRO D 416 GLU D 418 5 3
HELIX 79 79 ARG D 419 GLU D 434 1 16
HELIX 80 80 THR D 460 GLY D 476 1 17
SHEET 1 A 7 GLY B 144 THR B 148 0
SHEET 2 A 7 ALA B 313 PHE B 317 -1 O PHE B 317 N GLY B 144
SHEET 3 A 7 SER B 297 PHE B 300 -1 N PHE B 300 O MET B 314
SHEET 4 A 7 TRP B 268 ALA B 273 1 N VAL B 271 O SER B 297
SHEET 5 A 7 HIS B 236 THR B 243 1 N ALA B 242 O ASP B 272
SHEET 6 A 7 PRO B 181 SER B 186 1 N PHE B 184 O VAL B 241
SHEET 7 A 7 VAL B 207 VAL B 210 1 O VAL B 210 N ALA B 185
SHEET 1 B 3 LEU B 395 LEU B 397 0
SHEET 2 B 3 ILE B 405 GLY B 410 -1 O ARG B 409 N ARG B 396
SHEET 3 B 3 LEU B 450 VAL B 453 -1 O ALA B 452 N VAL B 406
SHEET 1 C 2 VAL B 443 TYR B 444 0
SHEET 2 C 2 GLY B 447 ARG B 448 -1 O GLY B 447 N TYR B 444
SHEET 1 D 7 GLY A 144 THR A 148 0
SHEET 2 D 7 ALA A 313 PHE A 317 -1 O PHE A 317 N GLY A 144
SHEET 3 D 7 SER A 297 PHE A 300 -1 N ILE A 298 O LEU A 316
SHEET 4 D 7 TRP A 268 ASP A 272 1 N VAL A 271 O SER A 297
SHEET 5 D 7 HIS A 236 THR A 243 1 N ALA A 242 O ASP A 272
SHEET 6 D 7 PRO A 181 SER A 186 1 N PHE A 184 O VAL A 241
SHEET 7 D 7 VAL A 207 VAL A 210 1 O ILE A 208 N ILE A 183
SHEET 1 E 3 LEU A 395 LEU A 397 0
SHEET 2 E 3 ILE A 405 GLY A 410 -1 O ARG A 409 N ARG A 396
SHEET 3 E 3 LEU A 450 VAL A 453 -1 O ALA A 452 N VAL A 406
SHEET 1 F 2 VAL A 443 TYR A 444 0
SHEET 2 F 2 GLY A 447 ARG A 448 -1 O GLY A 447 N TYR A 444
SHEET 1 G 7 GLY C 144 THR C 148 0
SHEET 2 G 7 ALA C 313 PHE C 317 -1 O PHE C 317 N GLY C 144
SHEET 3 G 7 SER C 297 PHE C 300 -1 N ILE C 298 O LEU C 316
SHEET 4 G 7 TRP C 268 ALA C 273 1 N VAL C 271 O SER C 297
SHEET 5 G 7 HIS C 236 THR C 243 1 N ALA C 242 O ASP C 272
SHEET 6 G 7 PRO C 181 SER C 186 1 N PHE C 184 O VAL C 241
SHEET 7 G 7 VAL C 207 VAL C 210 1 O ILE C 208 N ILE C 183
SHEET 1 H 3 LEU C 395 LEU C 397 0
SHEET 2 H 3 ILE C 405 GLY C 410 -1 O ARG C 409 N ARG C 396
SHEET 3 H 3 LEU C 450 VAL C 453 -1 O ALA C 452 N VAL C 406
SHEET 1 I 2 VAL C 443 TYR C 444 0
SHEET 2 I 2 GLY C 447 ARG C 448 -1 O GLY C 447 N TYR C 444
SHEET 1 J 7 GLY D 144 THR D 148 0
SHEET 2 J 7 ALA D 313 PHE D 317 -1 O PHE D 317 N GLY D 144
SHEET 3 J 7 SER D 297 PHE D 300 -1 N ILE D 298 O LEU D 316
SHEET 4 J 7 TRP D 268 ASP D 272 1 N VAL D 271 O SER D 297
SHEET 5 J 7 HIS D 236 THR D 243 1 N ALA D 242 O ASP D 272
SHEET 6 J 7 PRO D 181 SER D 186 1 N PHE D 184 O VAL D 241
SHEET 7 J 7 VAL D 207 VAL D 210 1 O ILE D 208 N ILE D 183
SHEET 1 K 3 LEU D 395 LEU D 397 0
SHEET 2 K 3 ILE D 405 GLY D 410 -1 O ARG D 409 N ARG D 396
SHEET 3 K 3 LEU D 450 VAL D 453 -1 O ALA D 452 N VAL D 406
SHEET 1 L 2 VAL D 443 TYR D 444 0
SHEET 2 L 2 GLY D 447 ARG D 448 -1 O GLY D 447 N TYR D 444
LINK C GLN B 303 N LLP B 304 1555 1555 1.30
LINK C LLP B 304 N TRP B 305 1555 1555 1.31
LINK C GLN A 303 N LLP A 304 1555 1555 1.31
LINK C LLP A 304 N TRP A 305 1555 1555 1.31
LINK C GLN C 303 N LLP C 304 1555 1555 1.32
LINK C LLP C 304 N TRP C 305 1555 1555 1.31
LINK C GLN D 303 N ALLP D 304 1555 1555 1.23
LINK C ALLP D 304 N TRP D 305 1555 1555 1.29
CISPEP 1 LYS B 310 THR B 311 0 0.93
CISPEP 2 LYS A 310 THR A 311 0 -3.88
CISPEP 3 LYS C 310 THR C 311 0 -0.38
CISPEP 4 LYS D 310 THR D 311 0 -2.03
SITE 1 AC1 6 LEU A 6 PRO A 7 ALA A 8 ALA A 10
SITE 2 AC1 6 PHE A 11 TYR B 458
SITE 1 AC2 4 LEU A 136 PHE A 137 ARG A 286 GLU A 293
SITE 1 AC3 4 LEU C 136 PHE C 137 ARG C 286 GLU C 293
SITE 1 AC4 15 THR C 351 MET D 91 GLY D 150 GLY D 151
SITE 2 AC4 15 SER D 152 HIS D 190 GLY D 245 THR D 247
SITE 3 AC4 15 ASP D 272 ALA D 274 ASN D 301 GLN D 303
SITE 4 AC4 15 HOH D2153 HOH D2169 HOH D2183
SITE 1 AC5 3 PHE D 137 ARG D 286 ALA D 290
CRYST1 68.984 124.198 129.942 90.00 99.56 90.00 P 1 21 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 0.014496 0.000000 0.002441 0.00000
SCALE2 0.000000 0.008052 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007804 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
