HEADER SIGNALING PROTEIN 08-FEB-16 5I2C
TITLE ARGININE-BOUND CASTOR1 FROM HOMO SAPIENS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GATS-LIKE PROTEIN 3;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: GATSL3;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VARIANT: LOBSTR
KEYWDS SIGNALING, ARGININE, ACT, MTOR, SIGNALING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR R.A.SAXTON,K.E.KNOCKENHAUER,T.U.SCHWARTZ
REVDAT 7 06-MAR-24 5I2C 1 REMARK
REVDAT 6 27-NOV-19 5I2C 1 REMARK
REVDAT 5 10-APR-19 5I2C 1 REMARK
REVDAT 4 27-SEP-17 5I2C 1 JRNL REMARK
REVDAT 3 24-AUG-16 5I2C 1 JRNL
REVDAT 2 17-AUG-16 5I2C 1 JRNL
REVDAT 1 10-AUG-16 5I2C 0
JRNL AUTH R.A.SAXTON,L.CHANTRANUPONG,K.E.KNOCKENHAUER,T.U.SCHWARTZ,
JRNL AUTH 2 D.M.SABATINI
JRNL TITL MECHANISM OF ARGININE SENSING BY CASTOR1 UPSTREAM OF MTORC1.
JRNL REF NATURE V. 536 229 2016
JRNL REFN ESSN 1476-4687
JRNL PMID 27487210
JRNL DOI 10.1038/NATURE19079
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.10_2155: ???)
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) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 86.71
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 3 NUMBER OF REFLECTIONS : 116806
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.172
REMARK 3 R VALUE (WORKING SET) : 0.172
REMARK 3 FREE R VALUE : 0.204
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.710
REMARK 3 FREE R VALUE TEST SET COUNT : 2002
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 86.8127 - 4.3395 0.98 8362 147 0.1590 0.1810
REMARK 3 2 4.3395 - 3.4443 0.99 8373 144 0.1527 0.1860
REMARK 3 3 3.4443 - 3.0089 0.98 8206 142 0.1635 0.1784
REMARK 3 4 3.0089 - 2.7338 0.99 8314 147 0.1733 0.2167
REMARK 3 5 2.7338 - 2.5378 0.99 8281 151 0.1754 0.1962
REMARK 3 6 2.5378 - 2.3882 0.97 8179 138 0.1761 0.2307
REMARK 3 7 2.3882 - 2.2686 0.98 8171 143 0.1738 0.2275
REMARK 3 8 2.2686 - 2.1698 0.99 8245 145 0.1798 0.2371
REMARK 3 9 2.1698 - 2.0863 0.99 8269 142 0.1904 0.2408
REMARK 3 10 2.0863 - 2.0143 0.97 8066 147 0.1954 0.2270
REMARK 3 11 2.0143 - 1.9513 0.98 8208 137 0.2067 0.2462
REMARK 3 12 1.9513 - 1.8955 0.98 8193 148 0.2242 0.2925
REMARK 3 13 1.8955 - 1.8456 0.99 8243 136 0.2543 0.3030
REMARK 3 14 1.8456 - 1.8006 0.92 7694 135 0.2827 0.2966
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) : 0.210
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.880
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) : 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 : 0.007 9288
REMARK 3 ANGLE : 0.846 12667
REMARK 3 CHIRALITY : 0.057 1509
REMARK 3 PLANARITY : 0.006 1602
REMARK 3 DIHEDRAL : 15.344 5528
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 23
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 137 )
REMARK 3 ORIGIN FOR THE GROUP (A): 50.7590 69.6786 79.4332
REMARK 3 T TENSOR
REMARK 3 T11: 0.1893 T22: 0.1188
REMARK 3 T33: 0.1667 T12: -0.0206
REMARK 3 T13: -0.0084 T23: -0.0025
REMARK 3 L TENSOR
REMARK 3 L11: 2.8730 L22: 1.3736
REMARK 3 L33: 2.9632 L12: -0.3730
REMARK 3 L13: -1.6349 L23: 0.1952
REMARK 3 S TENSOR
REMARK 3 S11: -0.0817 S12: -0.0021 S13: -0.1002
REMARK 3 S21: 0.0964 S22: 0.0506 S23: 0.0316
REMARK 3 S31: 0.1608 S32: 0.0382 S33: 0.0337
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 138 THROUGH 175 )
REMARK 3 ORIGIN FOR THE GROUP (A): 40.9220 68.6026 90.3116
REMARK 3 T TENSOR
REMARK 3 T11: 0.3436 T22: 0.3374
REMARK 3 T33: 0.2685 T12: 0.0171
REMARK 3 T13: -0.0267 T23: -0.0125
REMARK 3 L TENSOR
REMARK 3 L11: 1.3315 L22: 5.2918
REMARK 3 L33: 1.7618 L12: 1.3761
REMARK 3 L13: -0.2712 L23: -0.8904
REMARK 3 S TENSOR
REMARK 3 S11: 0.1206 S12: -0.2234 S13: 0.0812
REMARK 3 S21: 0.9435 S22: -0.0535 S23: -0.0682
REMARK 3 S31: -0.1087 S32: -0.2454 S33: -0.0973
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 176 THROUGH 268 )
REMARK 3 ORIGIN FOR THE GROUP (A): 48.5347 74.6362 62.5024
REMARK 3 T TENSOR
REMARK 3 T11: 0.1681 T22: 0.2114
REMARK 3 T33: 0.1718 T12: -0.0092
REMARK 3 T13: -0.0024 T23: 0.0160
REMARK 3 L TENSOR
REMARK 3 L11: 2.6691 L22: 3.9009
REMARK 3 L33: 2.9735 L12: -2.4239
REMARK 3 L13: -0.7722 L23: 1.0631
REMARK 3 S TENSOR
REMARK 3 S11: 0.1786 S12: 0.2376 S13: -0.0600
REMARK 3 S21: -0.3215 S22: -0.1300 S23: 0.1286
REMARK 3 S31: -0.0916 S32: -0.2233 S33: -0.0396
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 269 THROUGH 322 )
REMARK 3 ORIGIN FOR THE GROUP (A): 42.0341 84.3527 75.7607
REMARK 3 T TENSOR
REMARK 3 T11: 0.1992 T22: 0.1105
REMARK 3 T33: 0.2320 T12: -0.0201
REMARK 3 T13: 0.0210 T23: 0.0086
REMARK 3 L TENSOR
REMARK 3 L11: 7.3272 L22: 2.4173
REMARK 3 L33: 4.3665 L12: -2.0852
REMARK 3 L13: 1.2535 L23: -0.4870
REMARK 3 S TENSOR
REMARK 3 S11: 0.0248 S12: 0.3134 S13: 0.4040
REMARK 3 S21: -0.0273 S22: -0.0819 S23: 0.0348
REMARK 3 S31: -0.2528 S32: -0.2013 S33: 0.0581
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 75 )
REMARK 3 ORIGIN FOR THE GROUP (A): 76.4859 64.2757 52.6292
REMARK 3 T TENSOR
REMARK 3 T11: 0.2315 T22: 0.2088
REMARK 3 T33: 0.2528 T12: -0.0284
REMARK 3 T13: 0.0330 T23: -0.0538
REMARK 3 L TENSOR
REMARK 3 L11: 2.9607 L22: 1.5813
REMARK 3 L33: 3.4998 L12: -0.5780
REMARK 3 L13: -2.1659 L23: 0.6405
REMARK 3 S TENSOR
REMARK 3 S11: 0.0923 S12: -0.1677 S13: 0.2782
REMARK 3 S21: -0.0045 S22: 0.0398 S23: -0.1289
REMARK 3 S31: -0.0967 S32: -0.0287 S33: -0.1263
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 76 THROUGH 137 )
REMARK 3 ORIGIN FOR THE GROUP (A): 86.1407 55.1472 37.6620
REMARK 3 T TENSOR
REMARK 3 T11: 0.2612 T22: 0.1793
REMARK 3 T33: 0.1958 T12: 0.0241
REMARK 3 T13: 0.0280 T23: -0.0446
REMARK 3 L TENSOR
REMARK 3 L11: 4.4473 L22: 2.0556
REMARK 3 L33: 3.6610 L12: -0.6801
REMARK 3 L13: -1.4989 L23: -0.4646
REMARK 3 S TENSOR
REMARK 3 S11: 0.0747 S12: 0.2532 S13: -0.1510
REMARK 3 S21: -0.3175 S22: -0.0154 S23: -0.1214
REMARK 3 S31: 0.2093 S32: 0.1423 S33: -0.0758
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 138 THROUGH 153 )
REMARK 3 ORIGIN FOR THE GROUP (A): 82.1946 63.3138 27.3981
REMARK 3 T TENSOR
REMARK 3 T11: 0.5508 T22: 0.4775
REMARK 3 T33: 0.4284 T12: 0.0682
REMARK 3 T13: 0.0859 T23: 0.0531
REMARK 3 L TENSOR
REMARK 3 L11: 9.7737 L22: 4.1839
REMARK 3 L33: 2.5052 L12: -6.1463
REMARK 3 L13: -1.8244 L23: 1.9621
REMARK 3 S TENSOR
REMARK 3 S11: -0.2858 S12: 0.4925 S13: 0.8815
REMARK 3 S21: -0.0638 S22: 0.6293 S23: -0.3498
REMARK 3 S31: -0.6820 S32: -0.6796 S33: -0.4432
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 154 THROUGH 190 )
REMARK 3 ORIGIN FOR THE GROUP (A): 79.3931 46.2081 48.5247
REMARK 3 T TENSOR
REMARK 3 T11: 0.3267 T22: 0.1002
REMARK 3 T33: 0.2387 T12: -0.0230
REMARK 3 T13: -0.0025 T23: -0.0913
REMARK 3 L TENSOR
REMARK 3 L11: 4.3314 L22: 2.4910
REMARK 3 L33: 3.0480 L12: -0.2061
REMARK 3 L13: -0.1323 L23: -0.1649
REMARK 3 S TENSOR
REMARK 3 S11: -0.3026 S12: -0.4362 S13: -0.3639
REMARK 3 S21: 0.2524 S22: 0.0952 S23: -0.0700
REMARK 3 S31: 0.3174 S32: -0.2185 S33: 0.2041
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 191 THROUGH 248 )
REMARK 3 ORIGIN FOR THE GROUP (A): 66.3426 52.7604 53.5804
REMARK 3 T TENSOR
REMARK 3 T11: 0.3014 T22: 0.1943
REMARK 3 T33: 0.2792 T12: -0.0372
REMARK 3 T13: 0.0138 T23: -0.0575
REMARK 3 L TENSOR
REMARK 3 L11: 3.4378 L22: 1.5921
REMARK 3 L33: 2.3143 L12: -0.4255
REMARK 3 L13: -1.5298 L23: 1.1274
REMARK 3 S TENSOR
REMARK 3 S11: -0.1663 S12: 0.0469 S13: -0.3731
REMARK 3 S21: 0.2048 S22: -0.0391 S23: 0.1963
REMARK 3 S31: 0.3518 S32: -0.1416 S33: 0.1888
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 249 THROUGH 279 )
REMARK 3 ORIGIN FOR THE GROUP (A): 76.9449 46.2695 49.7933
REMARK 3 T TENSOR
REMARK 3 T11: 0.4065 T22: 0.2780
REMARK 3 T33: 0.2054 T12: -0.0055
REMARK 3 T13: 0.0324 T23: -0.0264
REMARK 3 L TENSOR
REMARK 3 L11: 4.3340 L22: 3.8421
REMARK 3 L33: 2.1304 L12: -0.0831
REMARK 3 L13: -2.1827 L23: -0.1290
REMARK 3 S TENSOR
REMARK 3 S11: -0.2505 S12: 0.0144 S13: -0.5461
REMARK 3 S21: 0.1055 S22: 0.0383 S23: 0.2768
REMARK 3 S31: 0.3798 S32: -0.2550 S33: 0.2043
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 280 THROUGH 322 )
REMARK 3 ORIGIN FOR THE GROUP (A): 84.9996 41.5512 45.8756
REMARK 3 T TENSOR
REMARK 3 T11: 0.3264 T22: 0.1780
REMARK 3 T33: 0.2453 T12: 0.0792
REMARK 3 T13: -0.0045 T23: 0.0040
REMARK 3 L TENSOR
REMARK 3 L11: 3.0724 L22: 4.1408
REMARK 3 L33: 4.0496 L12: 1.9354
REMARK 3 L13: -0.2618 L23: 1.1886
REMARK 3 S TENSOR
REMARK 3 S11: -0.1045 S12: -0.0565 S13: -0.4759
REMARK 3 S21: 0.1579 S22: 0.0725 S23: -0.1122
REMARK 3 S31: 0.6635 S32: 0.2634 S33: 0.0304
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 2 THROUGH 137 )
REMARK 3 ORIGIN FOR THE GROUP (A): 45.6758 43.0261 30.1148
REMARK 3 T TENSOR
REMARK 3 T11: 0.1454 T22: 0.2189
REMARK 3 T33: 0.2720 T12: -0.0089
REMARK 3 T13: -0.0460 T23: 0.0407
REMARK 3 L TENSOR
REMARK 3 L11: 2.1294 L22: 1.6224
REMARK 3 L33: 4.6857 L12: -0.1761
REMARK 3 L13: -1.1335 L23: -1.0552
REMARK 3 S TENSOR
REMARK 3 S11: -0.0525 S12: 0.1284 S13: 0.2570
REMARK 3 S21: 0.0799 S22: -0.0693 S23: -0.1931
REMARK 3 S31: -0.1829 S32: 0.2287 S33: 0.1066
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 138 THROUGH 173 )
REMARK 3 ORIGIN FOR THE GROUP (A): 57.1224 46.7534 19.4281
REMARK 3 T TENSOR
REMARK 3 T11: 0.4480 T22: 0.6390
REMARK 3 T33: 0.4974 T12: -0.1024
REMARK 3 T13: 0.0586 T23: 0.2065
REMARK 3 L TENSOR
REMARK 3 L11: 1.8044 L22: 6.3517
REMARK 3 L33: 0.3598 L12: 0.8100
REMARK 3 L13: 0.4709 L23: 1.1191
REMARK 3 S TENSOR
REMARK 3 S11: 0.3602 S12: 0.0923 S13: 0.2941
REMARK 3 S21: 0.4630 S22: -0.4941 S23: -0.5222
REMARK 3 S31: -0.0064 S32: -0.0324 S33: 0.1495
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 174 THROUGH 268 )
REMARK 3 ORIGIN FOR THE GROUP (A): 29.1381 47.6213 30.2735
REMARK 3 T TENSOR
REMARK 3 T11: 0.2877 T22: 0.3422
REMARK 3 T33: 0.2807 T12: 0.1148
REMARK 3 T13: -0.0406 T23: -0.0060
REMARK 3 L TENSOR
REMARK 3 L11: 1.8090 L22: 0.7396
REMARK 3 L33: 4.0090 L12: 0.2113
REMARK 3 L13: 0.2080 L23: 0.3270
REMARK 3 S TENSOR
REMARK 3 S11: -0.0650 S12: 0.1245 S13: 0.1984
REMARK 3 S21: 0.0846 S22: -0.0229 S23: 0.1644
REMARK 3 S31: -0.5318 S32: -0.5779 S33: 0.0986
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 269 THROUGH 322 )
REMARK 3 ORIGIN FOR THE GROUP (A): 36.2291 40.5112 14.8393
REMARK 3 T TENSOR
REMARK 3 T11: 0.1800 T22: 0.3860
REMARK 3 T33: 0.2175 T12: 0.0232
REMARK 3 T13: -0.0043 T23: 0.0257
REMARK 3 L TENSOR
REMARK 3 L11: 4.4613 L22: 2.8871
REMARK 3 L33: 4.0779 L12: -1.3365
REMARK 3 L13: 0.7308 L23: -0.1423
REMARK 3 S TENSOR
REMARK 3 S11: 0.1766 S12: 0.7842 S13: 0.0743
REMARK 3 S21: -0.2523 S22: -0.3252 S23: 0.1082
REMARK 3 S31: -0.1543 S32: -0.1626 S33: 0.0968
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 2 THROUGH 32 )
REMARK 3 ORIGIN FOR THE GROUP (A): 25.1647 36.5621 60.0165
REMARK 3 T TENSOR
REMARK 3 T11: 0.2869 T22: 0.3079
REMARK 3 T33: 0.2359 T12: -0.0702
REMARK 3 T13: -0.0296 T23: -0.0297
REMARK 3 L TENSOR
REMARK 3 L11: 2.1074 L22: 2.1968
REMARK 3 L33: 3.6706 L12: -0.5979
REMARK 3 L13: -1.1019 L23: -0.0449
REMARK 3 S TENSOR
REMARK 3 S11: 0.3653 S12: 0.0738 S13: -0.0543
REMARK 3 S21: -0.0888 S22: -0.2142 S23: 0.2088
REMARK 3 S31: 0.3820 S32: -0.4948 S33: -0.1351
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 33 THROUGH 153 )
REMARK 3 ORIGIN FOR THE GROUP (A): 18.4941 36.3347 69.7488
REMARK 3 T TENSOR
REMARK 3 T11: 0.3341 T22: 0.4278
REMARK 3 T33: 0.3895 T12: -0.1812
REMARK 3 T13: -0.0058 T23: -0.0333
REMARK 3 L TENSOR
REMARK 3 L11: 1.7209 L22: 1.8490
REMARK 3 L33: 2.6140 L12: 0.1826
REMARK 3 L13: -0.2607 L23: -0.3464
REMARK 3 S TENSOR
REMARK 3 S11: 0.1036 S12: 0.0475 S13: -0.2136
REMARK 3 S21: 0.0767 S22: -0.1410 S23: 0.4573
REMARK 3 S31: 0.5482 S32: -0.6842 S33: 0.0452
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 154 THROUGH 262 )
REMARK 3 ORIGIN FOR THE GROUP (A): 29.0638 51.2928 64.7839
REMARK 3 T TENSOR
REMARK 3 T11: 0.2306 T22: 0.2625
REMARK 3 T33: 0.2536 T12: -0.0024
REMARK 3 T13: -0.0148 T23: 0.0018
REMARK 3 L TENSOR
REMARK 3 L11: 1.2723 L22: 2.5002
REMARK 3 L33: 4.1685 L12: 0.0555
REMARK 3 L13: -0.6227 L23: -0.2441
REMARK 3 S TENSOR
REMARK 3 S11: 0.1519 S12: 0.0885 S13: 0.1432
REMARK 3 S21: -0.1268 S22: -0.0990 S23: 0.0203
REMARK 3 S31: -0.4451 S32: -0.2493 S33: -0.0483
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 263 THROUGH 323 )
REMARK 3 ORIGIN FOR THE GROUP (A): 28.5263 45.7923 81.1081
REMARK 3 T TENSOR
REMARK 3 T11: 0.2314 T22: 0.2296
REMARK 3 T33: 0.2229 T12: -0.0690
REMARK 3 T13: 0.0254 T23: 0.0294
REMARK 3 L TENSOR
REMARK 3 L11: 1.4946 L22: 5.8761
REMARK 3 L33: 2.2400 L12: 0.0765
REMARK 3 L13: 0.3309 L23: 2.0761
REMARK 3 S TENSOR
REMARK 3 S11: 0.0448 S12: -0.1448 S13: -0.0829
REMARK 3 S21: 0.3759 S22: -0.1545 S23: 0.2829
REMARK 3 S31: 0.3077 S32: -0.3009 S33: 0.0992
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 401 THROUGH 401 )
REMARK 3 ORIGIN FOR THE GROUP (A): 48.8410 80.6941 82.5773
REMARK 3 T TENSOR
REMARK 3 T11: 0.2537 T22: 0.2067
REMARK 3 T33: 0.2330 T12: -0.0114
REMARK 3 T13: 0.0498 T23: 0.0041
REMARK 3 L TENSOR
REMARK 3 L11: 2.0001 L22: 4.3059
REMARK 3 L33: 2.0000 L12: -2.4227
REMARK 3 L13: 2.0000 L23: 6.2022
REMARK 3 S TENSOR
REMARK 3 S11: 0.4445 S12: 0.1588 S13: 0.5961
REMARK 3 S21: -0.1467 S22: -0.1581 S23: 0.0333
REMARK 3 S31: -0.5616 S32: -0.1915 S33: -0.2560
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 401 THROUGH 401 )
REMARK 3 ORIGIN FOR THE GROUP (A): 90.1798 53.3970 48.0665
REMARK 3 T TENSOR
REMARK 3 T11: 0.3170 T22: 0.3535
REMARK 3 T33: 0.2614 T12: 0.0414
REMARK 3 T13: 0.0141 T23: -0.0880
REMARK 3 L TENSOR
REMARK 3 L11: 2.0002 L22: 5.0281
REMARK 3 L33: 2.0000 L12: -8.0795
REMARK 3 L13: 2.0000 L23: 2.0000
REMARK 3 S TENSOR
REMARK 3 S11: -0.6326 S12: -0.2687 S13: -0.4714
REMARK 3 S21: 0.4203 S22: 0.3514 S23: -0.0420
REMARK 3 S31: 1.4005 S32: 0.7512 S33: 0.2808
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 401 THROUGH 401 )
REMARK 3 ORIGIN FOR THE GROUP (A): 44.3135 36.4408 19.6315
REMARK 3 T TENSOR
REMARK 3 T11: 0.2506 T22: 0.3838
REMARK 3 T33: 0.2745 T12: 0.0185
REMARK 3 T13: -0.0152 T23: 0.0417
REMARK 3 L TENSOR
REMARK 3 L11: 1.9999 L22: 6.9242
REMARK 3 L33: 2.0001 L12: 7.9442
REMARK 3 L13: 2.0000 L23: -7.2568
REMARK 3 S TENSOR
REMARK 3 S11: 0.2075 S12: 0.4806 S13: 0.2287
REMARK 3 S21: -0.4026 S22: -0.0049 S23: 0.0703
REMARK 3 S31: 0.6382 S32: -1.4230 S33: -0.2270
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 401 THROUGH 401 )
REMARK 3 ORIGIN FOR THE GROUP (A): 26.5351 35.5112 78.1782
REMARK 3 T TENSOR
REMARK 3 T11: 0.3091 T22: 0.3434
REMARK 3 T33: 0.3085 T12: -0.1918
REMARK 3 T13: -0.0085 T23: 0.0568
REMARK 3 L TENSOR
REMARK 3 L11: 2.2041 L22: 7.9131
REMARK 3 L33: 1.6980 L12: -0.4490
REMARK 3 L13: 1.7385 L23: -1.3782
REMARK 3 S TENSOR
REMARK 3 S11: 0.3002 S12: -0.6368 S13: 0.0090
REMARK 3 S21: 0.2508 S22: 0.1818 S23: -0.0266
REMARK 3 S31: -0.3099 S32: 0.5994 S33: -0.4930
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 5I2C COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-FEB-16.
REMARK 100 THE DEPOSITION ID IS D_1000218060.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-OCT-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.0-5.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 24-ID-C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9792
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 116806
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 86.720
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 200 DATA REDUNDANCY : 3.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.07200
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 25.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.85
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) : 0.07200
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.42
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.25
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM ACETATE, 0.25 M AMMONIUM
REMARK 280 ACETATE, 22.5% PEG 3350, PH 5.0, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 291.15K
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 41.30050
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: 2330 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25220 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 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: 2290 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24100 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 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 A 85
REMARK 465 GLY A 86
REMARK 465 ALA A 87
REMARK 465 ALA A 88
REMARK 465 VAL A 89
REMARK 465 ASP A 157
REMARK 465 ASP A 158
REMARK 465 SER A 159
REMARK 465 SER A 160
REMARK 465 ASN A 161
REMARK 465 GLY A 162
REMARK 465 PHE A 163
REMARK 465 PRO A 164
REMARK 465 ARG A 165
REMARK 465 THR A 166
REMARK 465 GLN A 167
REMARK 465 SER A 257
REMARK 465 SER A 258
REMARK 465 SER A 259
REMARK 465 GLY A 260
REMARK 465 GLU A 261
REMARK 465 ARG A 323
REMARK 465 GLN A 324
REMARK 465 GLU A 325
REMARK 465 GLY A 326
REMARK 465 LEU A 327
REMARK 465 ALA A 328
REMARK 465 SER A 329
REMARK 465 SER B 83
REMARK 465 HIS B 84
REMARK 465 SER B 85
REMARK 465 GLY B 86
REMARK 465 ALA B 87
REMARK 465 ALA B 88
REMARK 465 ASP B 157
REMARK 465 ASP B 158
REMARK 465 SER B 159
REMARK 465 SER B 160
REMARK 465 ASN B 161
REMARK 465 GLY B 162
REMARK 465 PHE B 163
REMARK 465 PRO B 164
REMARK 465 ARG B 165
REMARK 465 THR B 166
REMARK 465 GLN B 167
REMARK 465 HIS B 168
REMARK 465 GLY B 169
REMARK 465 PRO B 170
REMARK 465 SER B 171
REMARK 465 PRO B 172
REMARK 465 HIS B 209
REMARK 465 SER B 210
REMARK 465 THR B 211
REMARK 465 PRO B 212
REMARK 465 LYS B 213
REMARK 465 GLU B 214
REMARK 465 ALA B 215
REMARK 465 ALA B 216
REMARK 465 SER B 217
REMARK 465 SER B 218
REMARK 465 SER B 219
REMARK 465 PRO B 220
REMARK 465 GLU B 221
REMARK 465 PRO B 222
REMARK 465 SER B 223
REMARK 465 SER B 224
REMARK 465 ILE B 225
REMARK 465 ARG B 323
REMARK 465 GLN B 324
REMARK 465 GLU B 325
REMARK 465 GLY B 326
REMARK 465 LEU B 327
REMARK 465 ALA B 328
REMARK 465 SER B 329
REMARK 465 MET C 1
REMARK 465 SER C 83
REMARK 465 HIS C 84
REMARK 465 SER C 85
REMARK 465 GLY C 86
REMARK 465 ALA C 87
REMARK 465 ALA C 88
REMARK 465 VAL C 89
REMARK 465 THR C 155
REMARK 465 ARG C 156
REMARK 465 ASP C 157
REMARK 465 ASP C 158
REMARK 465 SER C 159
REMARK 465 SER C 160
REMARK 465 ASN C 161
REMARK 465 GLY C 162
REMARK 465 PHE C 163
REMARK 465 HIS C 209
REMARK 465 SER C 210
REMARK 465 THR C 211
REMARK 465 PRO C 212
REMARK 465 LYS C 213
REMARK 465 GLU C 214
REMARK 465 ALA C 215
REMARK 465 ALA C 216
REMARK 465 SER C 217
REMARK 465 SER C 218
REMARK 465 SER C 219
REMARK 465 PRO C 220
REMARK 465 GLU C 221
REMARK 465 PRO C 222
REMARK 465 SER C 223
REMARK 465 SER C 224
REMARK 465 SER C 257
REMARK 465 SER C 258
REMARK 465 SER C 259
REMARK 465 GLY C 260
REMARK 465 ARG C 323
REMARK 465 GLN C 324
REMARK 465 GLU C 325
REMARK 465 GLY C 326
REMARK 465 LEU C 327
REMARK 465 ALA C 328
REMARK 465 SER C 329
REMARK 465 MET D 1
REMARK 465 SER D 82
REMARK 465 SER D 83
REMARK 465 HIS D 84
REMARK 465 SER D 85
REMARK 465 GLY D 86
REMARK 465 ALA D 87
REMARK 465 ALA D 88
REMARK 465 VAL D 89
REMARK 465 THR D 155
REMARK 465 ARG D 156
REMARK 465 ASP D 157
REMARK 465 ASP D 158
REMARK 465 SER D 159
REMARK 465 SER D 160
REMARK 465 ASN D 161
REMARK 465 GLY D 162
REMARK 465 PHE D 163
REMARK 465 PRO D 164
REMARK 465 ARG D 165
REMARK 465 THR D 166
REMARK 465 GLN D 167
REMARK 465 HIS D 168
REMARK 465 GLY D 169
REMARK 465 SER D 210
REMARK 465 THR D 211
REMARK 465 PRO D 212
REMARK 465 LYS D 213
REMARK 465 GLU D 214
REMARK 465 ALA D 215
REMARK 465 ALA D 216
REMARK 465 SER D 217
REMARK 465 SER D 218
REMARK 465 SER D 219
REMARK 465 PRO D 220
REMARK 465 GLU D 221
REMARK 465 GLN D 324
REMARK 465 GLU D 325
REMARK 465 GLY D 326
REMARK 465 LEU D 327
REMARK 465 ALA D 328
REMARK 465 SER D 329
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 ARG A 35 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 38 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 67 CG CD OE1 OE2
REMARK 470 LYS A 96 CG CD CE NZ
REMARK 470 GLU A 192 CG CD OE1 OE2
REMARK 470 GLU B 107 CG CD OE1 OE2
REMARK 470 ARG B 156 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 192 CG CD OE1 OE2
REMARK 470 GLU B 318 CG CD OE1 OE2
REMARK 470 ARG C 99 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 192 CG CD OE1 OE2
REMARK 470 GLU C 318 CG CD OE1 OE2
REMARK 470 ARG D 35 CG CD NE CZ NH1 NH2
REMARK 470 ARG D 38 CG CD NE CZ NH1 NH2
REMARK 470 GLN D 90 CG CD OE1 NE2
REMARK 470 ARG D 99 CG CD NE CZ NH1 NH2
REMARK 470 GLU D 107 CG CD OE1 OE2
REMARK 470 GLN D 139 CG CD OE1 NE2
REMARK 470 GLU D 140 CG CD OE1 OE2
REMARK 470 GLU D 150 CG CD OE1 OE2
REMARK 470 GLU D 244 CG CD OE1 OE2
REMARK 470 ARG D 323 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 NH2 ARG C 38 OE1 GLU C 58 2.06
REMARK 500 O HOH D 556 O HOH D 621 2.15
REMARK 500 O PHE C 249 O HOH C 501 2.16
REMARK 500 O HOH A 696 O HOH A 724 2.17
REMARK 500 O SER D 179 O HOH D 501 2.17
REMARK 500 O VAL B 89 O HOH B 501 2.17
REMARK 500 OE1 GLU A 234 NE2 GLN D 181 2.18
REMARK 500 O HOH D 509 O HOH D 633 2.18
REMARK 500 O HOH C 549 O HOH C 618 2.18
REMARK 500 O HOH D 651 O HOH D 657 2.18
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 GLU A 7 57.97 -91.12
REMARK 500 VAL A 101 -55.17 -122.02
REMARK 500 ASP B 50 -176.49 -172.64
REMARK 500 ALA B 74 153.33 83.72
REMARK 500 VAL B 101 -53.22 -121.25
REMARK 500 THR B 155 -159.34 -122.53
REMARK 500 GLU C 7 57.13 -92.77
REMARK 500 ASP C 50 -174.95 -176.91
REMARK 500 VAL C 101 -55.59 -124.80
REMARK 500 ARG C 165 -106.60 55.88
REMARK 500 VAL D 101 -58.35 -120.79
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH B 704 DISTANCE = 5.81 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ARG A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ARG B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ARG C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT C 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ARG D 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT D 402
DBREF 5I2C A 1 329 UNP Q8WTX7 GATL3_HUMAN 1 329
DBREF 5I2C B 1 329 UNP Q8WTX7 GATL3_HUMAN 1 329
DBREF 5I2C C 1 329 UNP Q8WTX7 GATL3_HUMAN 1 329
DBREF 5I2C D 1 329 UNP Q8WTX7 GATL3_HUMAN 1 329
SEQRES 1 A 329 MET GLU LEU HIS ILE LEU GLU HIS ARG VAL ARG VAL LEU
SEQRES 2 A 329 SER VAL ALA ARG PRO GLY LEU TRP LEU TYR THR HIS PRO
SEQRES 3 A 329 LEU ILE LYS LEU LEU PHE LEU PRO ARG ARG SER ARG CYS
SEQRES 4 A 329 LYS PHE PHE SER LEU THR GLU THR PRO GLU ASP TYR THR
SEQRES 5 A 329 LEU MET VAL ASP GLU GLU GLY PHE LYS GLU LEU PRO PRO
SEQRES 6 A 329 SER GLU PHE LEU GLN VAL ALA GLU ALA THR TRP LEU VAL
SEQRES 7 A 329 LEU ASN VAL SER SER HIS SER GLY ALA ALA VAL GLN ALA
SEQRES 8 A 329 ALA GLY VAL THR LYS ILE ALA ARG SER VAL ILE ALA PRO
SEQRES 9 A 329 LEU ALA GLU HIS HIS VAL SER VAL LEU MET LEU SER THR
SEQRES 10 A 329 TYR GLN THR ASP PHE ILE LEU VAL ARG GLU GLN ASP LEU
SEQRES 11 A 329 SER VAL VAL ILE HIS THR LEU ALA GLN GLU PHE ASP ILE
SEQRES 12 A 329 TYR ARG GLU VAL GLY GLY GLU PRO VAL PRO VAL THR ARG
SEQRES 13 A 329 ASP ASP SER SER ASN GLY PHE PRO ARG THR GLN HIS GLY
SEQRES 14 A 329 PRO SER PRO THR VAL HIS PRO ILE GLN SER PRO GLN ASN
SEQRES 15 A 329 ARG PHE CYS VAL LEU THR LEU ASP PRO GLU THR LEU PRO
SEQRES 16 A 329 ALA ILE ALA THR THR LEU ILE ASP VAL LEU PHE TYR SER
SEQRES 17 A 329 HIS SER THR PRO LYS GLU ALA ALA SER SER SER PRO GLU
SEQRES 18 A 329 PRO SER SER ILE THR PHE PHE ALA PHE SER LEU ILE GLU
SEQRES 19 A 329 GLY TYR ILE SER ILE VAL MET ASP ALA GLU THR GLN LYS
SEQRES 20 A 329 LYS PHE PRO SER ASP LEU LEU LEU THR SER SER SER GLY
SEQRES 21 A 329 GLU LEU TRP ARG MET VAL ARG ILE GLY GLY GLN PRO LEU
SEQRES 22 A 329 GLY PHE ASP GLU CYS GLY ILE VAL ALA GLN ILE ALA GLY
SEQRES 23 A 329 PRO LEU ALA ALA ALA ASP ILE SER ALA TYR TYR ILE SER
SEQRES 24 A 329 THR PHE ASN PHE ASP HIS ALA LEU VAL PRO GLU ASP GLY
SEQRES 25 A 329 ILE GLY SER VAL ILE GLU VAL LEU GLN ARG ARG GLN GLU
SEQRES 26 A 329 GLY LEU ALA SER
SEQRES 1 B 329 MET GLU LEU HIS ILE LEU GLU HIS ARG VAL ARG VAL LEU
SEQRES 2 B 329 SER VAL ALA ARG PRO GLY LEU TRP LEU TYR THR HIS PRO
SEQRES 3 B 329 LEU ILE LYS LEU LEU PHE LEU PRO ARG ARG SER ARG CYS
SEQRES 4 B 329 LYS PHE PHE SER LEU THR GLU THR PRO GLU ASP TYR THR
SEQRES 5 B 329 LEU MET VAL ASP GLU GLU GLY PHE LYS GLU LEU PRO PRO
SEQRES 6 B 329 SER GLU PHE LEU GLN VAL ALA GLU ALA THR TRP LEU VAL
SEQRES 7 B 329 LEU ASN VAL SER SER HIS SER GLY ALA ALA VAL GLN ALA
SEQRES 8 B 329 ALA GLY VAL THR LYS ILE ALA ARG SER VAL ILE ALA PRO
SEQRES 9 B 329 LEU ALA GLU HIS HIS VAL SER VAL LEU MET LEU SER THR
SEQRES 10 B 329 TYR GLN THR ASP PHE ILE LEU VAL ARG GLU GLN ASP LEU
SEQRES 11 B 329 SER VAL VAL ILE HIS THR LEU ALA GLN GLU PHE ASP ILE
SEQRES 12 B 329 TYR ARG GLU VAL GLY GLY GLU PRO VAL PRO VAL THR ARG
SEQRES 13 B 329 ASP ASP SER SER ASN GLY PHE PRO ARG THR GLN HIS GLY
SEQRES 14 B 329 PRO SER PRO THR VAL HIS PRO ILE GLN SER PRO GLN ASN
SEQRES 15 B 329 ARG PHE CYS VAL LEU THR LEU ASP PRO GLU THR LEU PRO
SEQRES 16 B 329 ALA ILE ALA THR THR LEU ILE ASP VAL LEU PHE TYR SER
SEQRES 17 B 329 HIS SER THR PRO LYS GLU ALA ALA SER SER SER PRO GLU
SEQRES 18 B 329 PRO SER SER ILE THR PHE PHE ALA PHE SER LEU ILE GLU
SEQRES 19 B 329 GLY TYR ILE SER ILE VAL MET ASP ALA GLU THR GLN LYS
SEQRES 20 B 329 LYS PHE PRO SER ASP LEU LEU LEU THR SER SER SER GLY
SEQRES 21 B 329 GLU LEU TRP ARG MET VAL ARG ILE GLY GLY GLN PRO LEU
SEQRES 22 B 329 GLY PHE ASP GLU CYS GLY ILE VAL ALA GLN ILE ALA GLY
SEQRES 23 B 329 PRO LEU ALA ALA ALA ASP ILE SER ALA TYR TYR ILE SER
SEQRES 24 B 329 THR PHE ASN PHE ASP HIS ALA LEU VAL PRO GLU ASP GLY
SEQRES 25 B 329 ILE GLY SER VAL ILE GLU VAL LEU GLN ARG ARG GLN GLU
SEQRES 26 B 329 GLY LEU ALA SER
SEQRES 1 C 329 MET GLU LEU HIS ILE LEU GLU HIS ARG VAL ARG VAL LEU
SEQRES 2 C 329 SER VAL ALA ARG PRO GLY LEU TRP LEU TYR THR HIS PRO
SEQRES 3 C 329 LEU ILE LYS LEU LEU PHE LEU PRO ARG ARG SER ARG CYS
SEQRES 4 C 329 LYS PHE PHE SER LEU THR GLU THR PRO GLU ASP TYR THR
SEQRES 5 C 329 LEU MET VAL ASP GLU GLU GLY PHE LYS GLU LEU PRO PRO
SEQRES 6 C 329 SER GLU PHE LEU GLN VAL ALA GLU ALA THR TRP LEU VAL
SEQRES 7 C 329 LEU ASN VAL SER SER HIS SER GLY ALA ALA VAL GLN ALA
SEQRES 8 C 329 ALA GLY VAL THR LYS ILE ALA ARG SER VAL ILE ALA PRO
SEQRES 9 C 329 LEU ALA GLU HIS HIS VAL SER VAL LEU MET LEU SER THR
SEQRES 10 C 329 TYR GLN THR ASP PHE ILE LEU VAL ARG GLU GLN ASP LEU
SEQRES 11 C 329 SER VAL VAL ILE HIS THR LEU ALA GLN GLU PHE ASP ILE
SEQRES 12 C 329 TYR ARG GLU VAL GLY GLY GLU PRO VAL PRO VAL THR ARG
SEQRES 13 C 329 ASP ASP SER SER ASN GLY PHE PRO ARG THR GLN HIS GLY
SEQRES 14 C 329 PRO SER PRO THR VAL HIS PRO ILE GLN SER PRO GLN ASN
SEQRES 15 C 329 ARG PHE CYS VAL LEU THR LEU ASP PRO GLU THR LEU PRO
SEQRES 16 C 329 ALA ILE ALA THR THR LEU ILE ASP VAL LEU PHE TYR SER
SEQRES 17 C 329 HIS SER THR PRO LYS GLU ALA ALA SER SER SER PRO GLU
SEQRES 18 C 329 PRO SER SER ILE THR PHE PHE ALA PHE SER LEU ILE GLU
SEQRES 19 C 329 GLY TYR ILE SER ILE VAL MET ASP ALA GLU THR GLN LYS
SEQRES 20 C 329 LYS PHE PRO SER ASP LEU LEU LEU THR SER SER SER GLY
SEQRES 21 C 329 GLU LEU TRP ARG MET VAL ARG ILE GLY GLY GLN PRO LEU
SEQRES 22 C 329 GLY PHE ASP GLU CYS GLY ILE VAL ALA GLN ILE ALA GLY
SEQRES 23 C 329 PRO LEU ALA ALA ALA ASP ILE SER ALA TYR TYR ILE SER
SEQRES 24 C 329 THR PHE ASN PHE ASP HIS ALA LEU VAL PRO GLU ASP GLY
SEQRES 25 C 329 ILE GLY SER VAL ILE GLU VAL LEU GLN ARG ARG GLN GLU
SEQRES 26 C 329 GLY LEU ALA SER
SEQRES 1 D 329 MET GLU LEU HIS ILE LEU GLU HIS ARG VAL ARG VAL LEU
SEQRES 2 D 329 SER VAL ALA ARG PRO GLY LEU TRP LEU TYR THR HIS PRO
SEQRES 3 D 329 LEU ILE LYS LEU LEU PHE LEU PRO ARG ARG SER ARG CYS
SEQRES 4 D 329 LYS PHE PHE SER LEU THR GLU THR PRO GLU ASP TYR THR
SEQRES 5 D 329 LEU MET VAL ASP GLU GLU GLY PHE LYS GLU LEU PRO PRO
SEQRES 6 D 329 SER GLU PHE LEU GLN VAL ALA GLU ALA THR TRP LEU VAL
SEQRES 7 D 329 LEU ASN VAL SER SER HIS SER GLY ALA ALA VAL GLN ALA
SEQRES 8 D 329 ALA GLY VAL THR LYS ILE ALA ARG SER VAL ILE ALA PRO
SEQRES 9 D 329 LEU ALA GLU HIS HIS VAL SER VAL LEU MET LEU SER THR
SEQRES 10 D 329 TYR GLN THR ASP PHE ILE LEU VAL ARG GLU GLN ASP LEU
SEQRES 11 D 329 SER VAL VAL ILE HIS THR LEU ALA GLN GLU PHE ASP ILE
SEQRES 12 D 329 TYR ARG GLU VAL GLY GLY GLU PRO VAL PRO VAL THR ARG
SEQRES 13 D 329 ASP ASP SER SER ASN GLY PHE PRO ARG THR GLN HIS GLY
SEQRES 14 D 329 PRO SER PRO THR VAL HIS PRO ILE GLN SER PRO GLN ASN
SEQRES 15 D 329 ARG PHE CYS VAL LEU THR LEU ASP PRO GLU THR LEU PRO
SEQRES 16 D 329 ALA ILE ALA THR THR LEU ILE ASP VAL LEU PHE TYR SER
SEQRES 17 D 329 HIS SER THR PRO LYS GLU ALA ALA SER SER SER PRO GLU
SEQRES 18 D 329 PRO SER SER ILE THR PHE PHE ALA PHE SER LEU ILE GLU
SEQRES 19 D 329 GLY TYR ILE SER ILE VAL MET ASP ALA GLU THR GLN LYS
SEQRES 20 D 329 LYS PHE PRO SER ASP LEU LEU LEU THR SER SER SER GLY
SEQRES 21 D 329 GLU LEU TRP ARG MET VAL ARG ILE GLY GLY GLN PRO LEU
SEQRES 22 D 329 GLY PHE ASP GLU CYS GLY ILE VAL ALA GLN ILE ALA GLY
SEQRES 23 D 329 PRO LEU ALA ALA ALA ASP ILE SER ALA TYR TYR ILE SER
SEQRES 24 D 329 THR PHE ASN PHE ASP HIS ALA LEU VAL PRO GLU ASP GLY
SEQRES 25 D 329 ILE GLY SER VAL ILE GLU VAL LEU GLN ARG ARG GLN GLU
SEQRES 26 D 329 GLY LEU ALA SER
HET ARG A 401 12
HET ACT A 402 4
HET ARG B 401 12
HET ACT B 402 4
HET ARG C 401 12
HET ACT C 402 4
HET ARG D 401 12
HET ACT D 402 4
HETNAM ARG ARGININE
HETNAM ACT ACETATE ION
FORMUL 5 ARG 4(C6 H15 N4 O2 1+)
FORMUL 6 ACT 4(C2 H3 O2 1-)
FORMUL 13 HOH *796(H2 O)
HELIX 1 AA1 GLY A 19 LEU A 33 1 15
HELIX 2 AA2 PRO A 34 SER A 37 5 4
HELIX 3 AA3 GLU A 57 LYS A 61 1 5
HELIX 4 AA4 ALA A 92 ALA A 98 5 7
HELIX 5 AA5 VAL A 101 HIS A 108 1 8
HELIX 6 AA6 ASP A 129 ALA A 138 1 10
HELIX 7 AA7 ASP A 190 ALA A 196 5 7
HELIX 8 AA8 ILE A 197 TYR A 207 1 11
HELIX 9 AA9 GLU A 244 PHE A 249 5 6
HELIX 10 AB1 GLY A 279 ALA A 291 1 13
HELIX 11 AB2 GLY A 312 GLN A 321 1 10
HELIX 12 AB3 ARG B 17 LEU B 22 5 6
HELIX 13 AB4 TYR B 23 LEU B 33 1 11
HELIX 14 AB5 PRO B 34 SER B 37 5 4
HELIX 15 AB6 GLU B 57 LYS B 61 1 5
HELIX 16 AB7 ALA B 92 ALA B 98 5 7
HELIX 17 AB8 VAL B 101 HIS B 108 1 8
HELIX 18 AB9 ASP B 129 ALA B 138 1 10
HELIX 19 AC1 ASP B 190 ALA B 196 5 7
HELIX 20 AC2 ILE B 197 TYR B 207 1 11
HELIX 21 AC3 ALA B 243 LYS B 247 1 5
HELIX 22 AC4 GLY B 279 ASP B 292 1 14
HELIX 23 AC5 GLY B 312 GLN B 321 1 10
HELIX 24 AC6 ARG C 17 LEU C 22 5 6
HELIX 25 AC7 TYR C 23 LEU C 33 1 11
HELIX 26 AC8 PRO C 34 SER C 37 5 4
HELIX 27 AC9 GLU C 57 LYS C 61 1 5
HELIX 28 AD1 VAL C 94 ALA C 98 5 5
HELIX 29 AD2 VAL C 101 HIS C 108 1 8
HELIX 30 AD3 ASP C 129 ALA C 138 1 10
HELIX 31 AD4 ASP C 190 GLU C 192 5 3
HELIX 32 AD5 THR C 193 SER C 208 1 16
HELIX 33 AD6 ALA C 243 LYS C 247 1 5
HELIX 34 AD7 GLY C 279 ALA C 291 1 13
HELIX 35 AD8 GLY C 312 ARG C 322 1 11
HELIX 36 AD9 ARG D 17 LEU D 22 5 6
HELIX 37 AE1 TYR D 23 LEU D 33 1 11
HELIX 38 AE2 PRO D 34 SER D 37 5 4
HELIX 39 AE3 GLU D 57 LYS D 61 1 5
HELIX 40 AE4 VAL D 94 ALA D 98 5 5
HELIX 41 AE5 VAL D 101 HIS D 108 1 8
HELIX 42 AE6 ASP D 129 ALA D 138 1 10
HELIX 43 AE7 ASP D 190 ALA D 196 5 7
HELIX 44 AE8 ILE D 197 TYR D 207 1 11
HELIX 45 AE9 ALA D 243 LYS D 247 1 5
HELIX 46 AF1 GLY D 279 ALA D 291 1 13
HELIX 47 AF2 GLY D 312 ARG D 322 1 11
SHEET 1 AA1 4 LEU A 69 VAL A 71 0
SHEET 2 AA1 4 GLU A 2 ALA A 16 -1 N SER A 14 O GLN A 70
SHEET 3 AA1 4 ASP A 142 VAL A 147 1 O GLU A 146 N ILE A 5
SHEET 4 AA1 4 GLU A 150 PRO A 153 -1 O VAL A 152 N ARG A 145
SHEET 1 AA2 9 VAL A 112 SER A 116 0
SHEET 2 AA2 9 ASP A 121 ARG A 126 -1 O LEU A 124 N LEU A 113
SHEET 3 AA2 9 TRP A 76 VAL A 81 -1 N LEU A 77 O VAL A 125
SHEET 4 AA2 9 GLU A 2 ALA A 16 -1 N VAL A 10 O TRP A 76
SHEET 5 AA2 9 ASP A 50 ASP A 56 -1 O VAL A 55 N ARG A 11
SHEET 6 AA2 9 PHE A 41 GLU A 46 -1 N THR A 45 O THR A 52
SHEET 7 AA2 9 PHE A 228 ILE A 233 -1 O PHE A 230 N LEU A 44
SHEET 8 AA2 9 TYR A 236 ASP A 242 -1 O VAL A 240 N ALA A 229
SHEET 9 AA2 9 PHE A 184 LEU A 187 -1 N CYS A 185 O MET A 241
SHEET 1 AA3 4 ILE A 177 GLN A 178 0
SHEET 2 AA3 4 TRP A 263 ILE A 268 -1 O ARG A 267 N GLN A 178
SHEET 3 AA3 4 ASP A 304 PRO A 309 -1 O VAL A 308 N ARG A 264
SHEET 4 AA3 4 TYR A 296 SER A 299 -1 N TYR A 296 O LEU A 307
SHEET 1 AA4 9 ILE B 177 GLN B 178 0
SHEET 2 AA4 9 TRP B 263 ILE B 268 -1 O ARG B 267 N GLN B 178
SHEET 3 AA4 9 ARG B 183 LEU B 189 -1 N PHE B 184 O TRP B 263
SHEET 4 AA4 9 TYR B 236 ASP B 242 -1 O ILE B 239 N LEU B 187
SHEET 5 AA4 9 PHE B 228 ILE B 233 -1 N SER B 231 O SER B 238
SHEET 6 AA4 9 PHE B 41 GLU B 46 -1 N GLU B 46 O PHE B 228
SHEET 7 AA4 9 TYR B 51 ASP B 56 -1 O THR B 52 N THR B 45
SHEET 8 AA4 9 GLU B 2 VAL B 15 -1 N LEU B 13 O LEU B 53
SHEET 9 AA4 9 LEU B 69 VAL B 71 -1 O GLN B 70 N SER B 14
SHEET 1 AA5 9 GLU B 150 PRO B 153 0
SHEET 2 AA5 9 ASP B 142 VAL B 147 -1 N ARG B 145 O VAL B 152
SHEET 3 AA5 9 GLU B 2 VAL B 15 1 N ILE B 5 O TYR B 144
SHEET 4 AA5 9 TRP B 76 SER B 82 -1 O SER B 82 N GLU B 2
SHEET 5 AA5 9 ASP B 121 ARG B 126 -1 O VAL B 125 N LEU B 77
SHEET 6 AA5 9 VAL B 112 SER B 116 -1 N LEU B 113 O LEU B 124
SHEET 7 AA5 9 TYR B 296 SER B 299 -1 O SER B 299 N MET B 114
SHEET 8 AA5 9 ASP B 304 PRO B 309 -1 O LEU B 307 N TYR B 296
SHEET 9 AA5 9 TRP B 263 ILE B 268 -1 N VAL B 266 O ALA B 306
SHEET 1 AA6 4 LEU C 69 VAL C 71 0
SHEET 2 AA6 4 LEU C 3 VAL C 15 -1 N SER C 14 O GLN C 70
SHEET 3 AA6 4 ILE C 143 VAL C 147 1 O TYR C 144 N ILE C 5
SHEET 4 AA6 4 GLU C 150 PRO C 153 -1 O VAL C 152 N ARG C 145
SHEET 1 AA7 9 VAL C 112 SER C 116 0
SHEET 2 AA7 9 ASP C 121 ARG C 126 -1 O LEU C 124 N LEU C 113
SHEET 3 AA7 9 TRP C 76 VAL C 81 -1 N LEU C 77 O VAL C 125
SHEET 4 AA7 9 LEU C 3 VAL C 15 -1 N LEU C 6 O VAL C 78
SHEET 5 AA7 9 TYR C 51 ASP C 56 -1 O VAL C 55 N ARG C 11
SHEET 6 AA7 9 PHE C 41 GLU C 46 -1 N THR C 45 O THR C 52
SHEET 7 AA7 9 PHE C 228 ILE C 233 -1 O PHE C 228 N GLU C 46
SHEET 8 AA7 9 TYR C 236 ASP C 242 -1 O SER C 238 N SER C 231
SHEET 9 AA7 9 PHE C 184 LEU C 187 -1 N CYS C 185 O MET C 241
SHEET 1 AA8 4 ILE C 177 GLN C 178 0
SHEET 2 AA8 4 TRP C 263 ILE C 268 -1 O ARG C 267 N GLN C 178
SHEET 3 AA8 4 ASP C 304 PRO C 309 -1 O VAL C 308 N ARG C 264
SHEET 4 AA8 4 TYR C 296 SER C 299 -1 N ILE C 298 O HIS C 305
SHEET 1 AA9 9 ILE D 177 GLN D 178 0
SHEET 2 AA9 9 TRP D 263 ILE D 268 -1 O ARG D 267 N GLN D 178
SHEET 3 AA9 9 ARG D 183 LEU D 187 -1 N PHE D 184 O TRP D 263
SHEET 4 AA9 9 TYR D 236 ASP D 242 -1 O ILE D 239 N LEU D 187
SHEET 5 AA9 9 PHE D 228 ILE D 233 -1 N SER D 231 O SER D 238
SHEET 6 AA9 9 PHE D 41 GLU D 46 -1 N GLU D 46 O PHE D 228
SHEET 7 AA9 9 TYR D 51 ASP D 56 -1 O THR D 52 N THR D 45
SHEET 8 AA9 9 LEU D 3 VAL D 15 -1 N ARG D 11 O VAL D 55
SHEET 9 AA9 9 LEU D 69 VAL D 71 -1 O GLN D 70 N SER D 14
SHEET 1 AB1 9 GLU D 150 PRO D 153 0
SHEET 2 AB1 9 ILE D 143 VAL D 147 -1 N ARG D 145 O VAL D 152
SHEET 3 AB1 9 LEU D 3 VAL D 15 1 N LEU D 3 O TYR D 144
SHEET 4 AB1 9 TRP D 76 ASN D 80 -1 O ASN D 80 N HIS D 4
SHEET 5 AB1 9 ASP D 121 ARG D 126 -1 O VAL D 125 N LEU D 77
SHEET 6 AB1 9 VAL D 112 SER D 116 -1 N LEU D 113 O LEU D 124
SHEET 7 AB1 9 TYR D 296 SER D 299 -1 O SER D 299 N MET D 114
SHEET 8 AB1 9 ASP D 304 PRO D 309 -1 O HIS D 305 N ILE D 298
SHEET 9 AB1 9 TRP D 263 ILE D 268 -1 N VAL D 266 O ALA D 306
SITE 1 AC1 16 SER A 111 VAL A 112 LEU A 273 GLY A 274
SITE 2 AC1 16 GLU A 277 CYS A 278 GLY A 279 ILE A 280
SITE 3 AC1 16 VAL A 281 THR A 300 PHE A 301 PHE A 303
SITE 4 AC1 16 ASP A 304 HOH A 577 HOH A 594 HOH A 623
SITE 1 AC2 9 LEU A 115 SER A 116 THR A 117 ALA A 229
SITE 2 AC2 9 SER A 231 SER A 238 VAL A 240 ILE A 298
SITE 3 AC2 9 HOH A 513
SITE 1 AC3 17 SER B 111 VAL B 112 LEU B 273 GLY B 274
SITE 2 AC3 17 GLU B 277 CYS B 278 GLY B 279 ILE B 280
SITE 3 AC3 17 VAL B 281 SER B 299 THR B 300 PHE B 301
SITE 4 AC3 17 PHE B 303 ASP B 304 HOH B 549 HOH B 552
SITE 5 AC3 17 HOH B 577
SITE 1 AC4 7 LEU B 115 SER B 116 THR B 117 ALA B 229
SITE 2 AC4 7 SER B 231 SER B 238 ILE B 298
SITE 1 AC5 17 SER C 111 VAL C 112 LEU C 273 GLY C 274
SITE 2 AC5 17 GLU C 277 CYS C 278 GLY C 279 ILE C 280
SITE 3 AC5 17 VAL C 281 SER C 299 THR C 300 PHE C 301
SITE 4 AC5 17 PHE C 303 ASP C 304 HOH C 566 HOH C 572
SITE 5 AC5 17 HOH C 592
SITE 1 AC6 7 SER C 116 THR C 117 SER C 231 SER C 238
SITE 2 AC6 7 VAL C 240 ILE C 298 HOH C 506
SITE 1 AC7 16 SER D 111 VAL D 112 LEU D 273 GLY D 274
SITE 2 AC7 16 GLU D 277 CYS D 278 GLY D 279 ILE D 280
SITE 3 AC7 16 VAL D 281 THR D 300 PHE D 301 PHE D 303
SITE 4 AC7 16 ASP D 304 HOH D 529 HOH D 540 HOH D 581
SITE 1 AC8 6 LEU D 115 SER D 116 SER D 231 SER D 238
SITE 2 AC8 6 ILE D 298 HOH D 514
CRYST1 91.393 82.601 96.666 90.00 116.23 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 0.010942 0.000000 0.005391 0.00000
SCALE2 0.000000 0.012106 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011532 0.00000
(ATOM LINES ARE NOT SHOWN.)
END