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HEADER TRANSFERASE 12-AUG-15 5D6O
TITLE ORTHORHOMBIC CRYSTAL STRUCTURE OF AN ACETYLESTER HYDROLASE FROM
TITLE 2 CORYNEBACTERIUM GLUTAMICUM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HOMOSERINE O-ACETYLTRANSFERASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 EC: 2.3.1.-,2.3.1.31;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CORYNEBACTERIUM GLUTAMICUM (STRAIN ATCC 13032 /
SOURCE 3 DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025);
SOURCE 4 ORGANISM_TAXID: 196627;
SOURCE 5 STRAIN: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025;
SOURCE 6 GENE: CG0961, CGL0839;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: JM109;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PHWG771
KEYWDS ACETYLESTER HYDROLASE, ALPHA/BETA HYDROLASE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.NIEFIND,C.TOELZER,J.ALTENBUCHNER,H.WATZLAWICK
REVDAT 1 09-DEC-15 5D6O 0
JRNL AUTH C.TOELZER,S.PAL,H.WATZLAWICK,J.ALTENBUCHNER,K.NIEFIND
JRNL TITL A NOVEL ESTERASE SUBFAMILY WITH ALPHA/BETA-HYDROLASE FOLD
JRNL TITL 2 SUGGESTED BY STRUCTURES OF TWO BACTERIAL ENZYMES HOMOLOGOUS
JRNL TITL 3 TO L-HOMOSERINE O-ACETYLTRANSFERASES
JRNL REF FEBS LETT. 2015
JRNL REFN ISSN 0014-5793
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.93
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.990
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 120181
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.175
REMARK 3 R VALUE (WORKING SET) : 0.175
REMARK 3 FREE R VALUE : 0.210
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.970
REMARK 3 FREE R VALUE TEST SET COUNT : 2370
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 19.9260 - 4.6103 1.00 7406 149 0.1889 0.2147
REMARK 3 2 4.6103 - 3.6667 1.00 7080 136 0.1416 0.1563
REMARK 3 3 3.6667 - 3.2054 1.00 7015 144 0.1493 0.1772
REMARK 3 4 3.2054 - 2.9133 1.00 6970 150 0.1579 0.1774
REMARK 3 5 2.9133 - 2.7051 1.00 6931 151 0.1670 0.1927
REMARK 3 6 2.7051 - 2.5459 1.00 6926 144 0.1709 0.2196
REMARK 3 7 2.5459 - 2.4186 1.00 6871 149 0.1698 0.2209
REMARK 3 8 2.4186 - 2.3135 1.00 6875 151 0.1746 0.1931
REMARK 3 9 2.3135 - 2.2246 1.00 6877 136 0.1735 0.2298
REMARK 3 10 2.2246 - 2.1479 1.00 6948 128 0.1741 0.2437
REMARK 3 11 2.1479 - 2.0808 1.00 6812 125 0.1765 0.2341
REMARK 3 12 2.0808 - 2.0214 1.00 6878 132 0.1882 0.2216
REMARK 3 13 2.0214 - 1.9682 1.00 6859 132 0.1919 0.2450
REMARK 3 14 1.9682 - 1.9202 1.00 6770 151 0.2033 0.2631
REMARK 3 15 1.9202 - 1.8766 1.00 6915 125 0.2190 0.2866
REMARK 3 16 1.8766 - 1.8367 1.00 6808 125 0.2338 0.3071
REMARK 3 17 1.8367 - 1.8000 1.00 6870 142 0.2374 0.2672
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) : 18.370
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 : 0.003 11333
REMARK 3 ANGLE : 0.719 15373
REMARK 3 CHIRALITY : 0.029 1640
REMARK 3 PLANARITY : 0.003 2020
REMARK 3 DIHEDRAL : 11.153 4042
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 27
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 19 )
REMARK 3 ORIGIN FOR THE GROUP (A): 47.3482 14.2120 357.8705
REMARK 3 T TENSOR
REMARK 3 T11: 0.1574 T22: 0.1534
REMARK 3 T33: 0.1193 T12: 0.0028
REMARK 3 T13: 0.0449 T23: -0.0007
REMARK 3 L TENSOR
REMARK 3 L11: 2.3882 L22: 0.3692
REMARK 3 L33: 2.8004 L12: -0.8613
REMARK 3 L13: 0.8922 L23: -0.6999
REMARK 3 S TENSOR
REMARK 3 S11: 0.0035 S12: -0.0811 S13: 0.2641
REMARK 3 S21: 0.2731 S22: -0.0241 S23: 0.1014
REMARK 3 S31: -0.2557 S32: -0.2368 S33: 0.0043
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 20 THROUGH 81 )
REMARK 3 ORIGIN FOR THE GROUP (A): 57.2891 3.6944 361.7229
REMARK 3 T TENSOR
REMARK 3 T11: 0.0735 T22: 0.1329
REMARK 3 T33: 0.0722 T12: 0.0105
REMARK 3 T13: 0.0124 T23: -0.0165
REMARK 3 L TENSOR
REMARK 3 L11: 0.6078 L22: 1.4336
REMARK 3 L33: 1.1979 L12: 0.1069
REMARK 3 L13: 0.2330 L23: -0.2445
REMARK 3 S TENSOR
REMARK 3 S11: 0.0093 S12: -0.1637 S13: 0.0567
REMARK 3 S21: 0.0979 S22: 0.0070 S23: 0.0798
REMARK 3 S31: -0.0369 S32: 0.0811 S33: -0.0143
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 82 THROUGH 199 )
REMARK 3 ORIGIN FOR THE GROUP (A): 62.0957 8.6617 352.7780
REMARK 3 T TENSOR
REMARK 3 T11: 0.0980 T22: 0.1340
REMARK 3 T33: 0.0811 T12: -0.0214
REMARK 3 T13: -0.0021 T23: -0.0013
REMARK 3 L TENSOR
REMARK 3 L11: 0.3892 L22: 0.4636
REMARK 3 L33: 1.0381 L12: -0.1045
REMARK 3 L13: 0.1973 L23: -0.2361
REMARK 3 S TENSOR
REMARK 3 S11: -0.0042 S12: -0.0212 S13: 0.0535
REMARK 3 S21: 0.0738 S22: -0.0011 S23: -0.0530
REMARK 3 S31: -0.1050 S32: 0.1420 S33: 0.0184
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 200 THROUGH 253 )
REMARK 3 ORIGIN FOR THE GROUP (A): 44.3901 2.9800 337.9247
REMARK 3 T TENSOR
REMARK 3 T11: 0.0753 T22: 0.1098
REMARK 3 T33: 0.0815 T12: 0.0321
REMARK 3 T13: 0.0040 T23: 0.0003
REMARK 3 L TENSOR
REMARK 3 L11: 0.7344 L22: 0.8936
REMARK 3 L33: 0.8727 L12: 0.4664
REMARK 3 L13: -0.0177 L23: 0.4665
REMARK 3 S TENSOR
REMARK 3 S11: 0.0152 S12: 0.0230 S13: 0.0427
REMARK 3 S21: 0.0637 S22: -0.0148 S23: 0.1267
REMARK 3 S31: 0.0129 S32: -0.1558 S33: 0.0218
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 254 THROUGH 310 )
REMARK 3 ORIGIN FOR THE GROUP (A): 67.2999 -1.1370 346.7173
REMARK 3 T TENSOR
REMARK 3 T11: 0.0988 T22: 0.0961
REMARK 3 T33: 0.0611 T12: 0.0201
REMARK 3 T13: -0.0100 T23: 0.0009
REMARK 3 L TENSOR
REMARK 3 L11: 0.5271 L22: 0.6115
REMARK 3 L33: 0.5529 L12: -0.0011
REMARK 3 L13: -0.1015 L23: -0.0993
REMARK 3 S TENSOR
REMARK 3 S11: -0.0330 S12: -0.0625 S13: -0.0303
REMARK 3 S21: -0.0585 S22: 0.0292 S23: -0.0667
REMARK 3 S31: 0.0207 S32: 0.1518 S33: 0.0007
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 311 THROUGH 349 )
REMARK 3 ORIGIN FOR THE GROUP (A): 55.8748 -12.2145 351.4528
REMARK 3 T TENSOR
REMARK 3 T11: 0.1542 T22: 0.0792
REMARK 3 T33: 0.0762 T12: -0.0079
REMARK 3 T13: 0.0007 T23: 0.0101
REMARK 3 L TENSOR
REMARK 3 L11: 2.2505 L22: 0.7994
REMARK 3 L33: 1.3514 L12: 0.0827
REMARK 3 L13: -0.1466 L23: 0.1068
REMARK 3 S TENSOR
REMARK 3 S11: 0.0122 S12: -0.0951 S13: -0.2317
REMARK 3 S21: 0.0352 S22: -0.0336 S23: 0.0110
REMARK 3 S31: 0.3128 S32: -0.0293 S33: -0.0164
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 19 )
REMARK 3 ORIGIN FOR THE GROUP (A): 58.3372 11.5515 302.6799
REMARK 3 T TENSOR
REMARK 3 T11: 0.1426 T22: 0.0806
REMARK 3 T33: 0.0980 T12: 0.0026
REMARK 3 T13: 0.0280 T23: 0.0035
REMARK 3 L TENSOR
REMARK 3 L11: 1.9694 L22: 0.7432
REMARK 3 L33: 2.9325 L12: -0.4197
REMARK 3 L13: 1.5455 L23: -0.0708
REMARK 3 S TENSOR
REMARK 3 S11: 0.0262 S12: 0.0306 S13: 0.1971
REMARK 3 S21: -0.2909 S22: -0.0762 S23: -0.0593
REMARK 3 S31: -0.3519 S32: 0.1156 S33: 0.0163
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 20 THROUGH 81 )
REMARK 3 ORIGIN FOR THE GROUP (A): 55.6043 -3.0143 301.5239
REMARK 3 T TENSOR
REMARK 3 T11: 0.0806 T22: 0.0773
REMARK 3 T33: 0.0686 T12: -0.0024
REMARK 3 T13: 0.0055 T23: -0.0090
REMARK 3 L TENSOR
REMARK 3 L11: 0.8146 L22: 0.8986
REMARK 3 L33: 1.1954 L12: -0.3159
REMARK 3 L13: 0.0435 L23: 0.1283
REMARK 3 S TENSOR
REMARK 3 S11: -0.0087 S12: 0.1251 S13: 0.0212
REMARK 3 S21: -0.0573 S22: -0.0411 S23: 0.0413
REMARK 3 S31: -0.0538 S32: -0.0194 S33: 0.0500
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 82 THROUGH 199 )
REMARK 3 ORIGIN FOR THE GROUP (A): 48.3383 0.3676 309.5025
REMARK 3 T TENSOR
REMARK 3 T11: 0.0886 T22: 0.0920
REMARK 3 T33: 0.0756 T12: 0.0264
REMARK 3 T13: -0.0066 T23: -0.0066
REMARK 3 L TENSOR
REMARK 3 L11: 0.4722 L22: 0.4934
REMARK 3 L33: 0.5275 L12: -0.0340
REMARK 3 L13: -0.1102 L23: 0.2256
REMARK 3 S TENSOR
REMARK 3 S11: -0.0113 S12: 0.0672 S13: 0.0079
REMARK 3 S21: -0.0693 S22: -0.0567 S23: 0.0726
REMARK 3 S31: -0.0651 S32: -0.0933 S33: 0.0607
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 200 THROUGH 253 )
REMARK 3 ORIGIN FOR THE GROUP (A): 65.4951 7.3773 324.3155
REMARK 3 T TENSOR
REMARK 3 T11: 0.0894 T22: 0.0803
REMARK 3 T33: 0.0808 T12: -0.0080
REMARK 3 T13: 0.0049 T23: -0.0148
REMARK 3 L TENSOR
REMARK 3 L11: 1.5846 L22: 1.3320
REMARK 3 L33: 1.5509 L12: -0.6678
REMARK 3 L13: 0.5869 L23: -1.0016
REMARK 3 S TENSOR
REMARK 3 S11: -0.0072 S12: 0.0020 S13: 0.0774
REMARK 3 S21: 0.0297 S22: -0.0176 S23: -0.0954
REMARK 3 S31: -0.1405 S32: 0.1752 S33: 0.0269
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 254 THROUGH 310 )
REMARK 3 ORIGIN FOR THE GROUP (A): 48.4234 -9.3650 317.5265
REMARK 3 T TENSOR
REMARK 3 T11: 0.0865 T22: 0.0977
REMARK 3 T33: 0.0871 T12: -0.0018
REMARK 3 T13: 0.0156 T23: -0.0196
REMARK 3 L TENSOR
REMARK 3 L11: 0.7349 L22: 0.9933
REMARK 3 L33: 0.5584 L12: 0.1429
REMARK 3 L13: 0.0436 L23: 0.0613
REMARK 3 S TENSOR
REMARK 3 S11: -0.0266 S12: 0.0091 S13: -0.0986
REMARK 3 S21: 0.0049 S22: 0.0173 S23: 0.0855
REMARK 3 S31: 0.0678 S32: -0.1345 S33: 0.0231
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 311 THROUGH 349 )
REMARK 3 ORIGIN FOR THE GROUP (A): 64.1662 -13.9174 314.5293
REMARK 3 T TENSOR
REMARK 3 T11: 0.0761 T22: 0.0789
REMARK 3 T33: 0.0851 T12: 0.0287
REMARK 3 T13: 0.0036 T23: 0.0041
REMARK 3 L TENSOR
REMARK 3 L11: 1.5184 L22: 1.4981
REMARK 3 L33: 1.3932 L12: 0.7306
REMARK 3 L13: 0.1512 L23: 0.3348
REMARK 3 S TENSOR
REMARK 3 S11: 0.0035 S12: 0.1106 S13: -0.1250
REMARK 3 S21: 0.0315 S22: -0.0023 S23: -0.0985
REMARK 3 S31: 0.1054 S32: 0.1856 S33: 0.0109
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 1 THROUGH 19 )
REMARK 3 ORIGIN FOR THE GROUP (A): 62.9352 -48.3563 424.6328
REMARK 3 T TENSOR
REMARK 3 T11: 0.1292 T22: 0.2501
REMARK 3 T33: 0.0810 T12: -0.0142
REMARK 3 T13: -0.0108 T23: 0.0429
REMARK 3 L TENSOR
REMARK 3 L11: 2.0312 L22: 1.2854
REMARK 3 L33: 3.1037 L12: -0.5277
REMARK 3 L13: -1.5012 L23: 0.4787
REMARK 3 S TENSOR
REMARK 3 S11: -0.0315 S12: -0.2993 S13: -0.0182
REMARK 3 S21: 0.1118 S22: -0.0132 S23: -0.0428
REMARK 3 S31: 0.3466 S32: 0.2825 S33: 0.0114
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 20 THROUGH 81 )
REMARK 3 ORIGIN FOR THE GROUP (A): 52.9606 -37.4311 426.4881
REMARK 3 T TENSOR
REMARK 3 T11: 0.1225 T22: 0.1423
REMARK 3 T33: 0.0793 T12: -0.0038
REMARK 3 T13: -0.0036 T23: 0.0148
REMARK 3 L TENSOR
REMARK 3 L11: 0.8465 L22: 0.8261
REMARK 3 L33: 1.3732 L12: 0.1114
REMARK 3 L13: 0.0761 L23: -0.1172
REMARK 3 S TENSOR
REMARK 3 S11: 0.0116 S12: -0.2126 S13: -0.0485
REMARK 3 S21: 0.1105 S22: -0.0697 S23: -0.0205
REMARK 3 S31: -0.0515 S32: 0.0938 S33: 0.0475
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 82 THROUGH 199 )
REMARK 3 ORIGIN FOR THE GROUP (A): 48.1415 -43.9092 418.6231
REMARK 3 T TENSOR
REMARK 3 T11: 0.0839 T22: 0.1219
REMARK 3 T33: 0.0845 T12: -0.0118
REMARK 3 T13: 0.0002 T23: 0.0171
REMARK 3 L TENSOR
REMARK 3 L11: 0.6484 L22: 0.4932
REMARK 3 L33: 1.0825 L12: -0.0227
REMARK 3 L13: -0.2959 L23: 0.1753
REMARK 3 S TENSOR
REMARK 3 S11: -0.0033 S12: -0.1089 S13: -0.0863
REMARK 3 S21: 0.0940 S22: -0.0357 S23: 0.0395
REMARK 3 S31: 0.1121 S32: -0.0752 S33: 0.0278
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 200 THROUGH 253 )
REMARK 3 ORIGIN FOR THE GROUP (A): 65.8462 -40.9143 402.9789
REMARK 3 T TENSOR
REMARK 3 T11: 0.0600 T22: 0.1302
REMARK 3 T33: 0.0785 T12: 0.0061
REMARK 3 T13: 0.0017 T23: -0.0077
REMARK 3 L TENSOR
REMARK 3 L11: 1.1583 L22: 1.1448
REMARK 3 L33: 0.9414 L12: 0.3532
REMARK 3 L13: 0.1248 L23: -0.0748
REMARK 3 S TENSOR
REMARK 3 S11: -0.0878 S12: -0.0663 S13: -0.1090
REMARK 3 S21: -0.0113 S22: 0.1010 S23: -0.1157
REMARK 3 S31: 0.0143 S32: 0.1330 S33: -0.0000
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 254 THROUGH 310 )
REMARK 3 ORIGIN FOR THE GROUP (A): 42.9270 -35.3863 410.9432
REMARK 3 T TENSOR
REMARK 3 T11: 0.0915 T22: 0.1233
REMARK 3 T33: 0.0577 T12: 0.0049
REMARK 3 T13: -0.0032 T23: -0.0087
REMARK 3 L TENSOR
REMARK 3 L11: 0.7802 L22: 0.7246
REMARK 3 L33: 0.5677 L12: -0.2413
REMARK 3 L13: 0.0331 L23: 0.0982
REMARK 3 S TENSOR
REMARK 3 S11: 0.0071 S12: -0.0131 S13: 0.0503
REMARK 3 S21: -0.0284 S22: -0.0276 S23: 0.0190
REMARK 3 S31: -0.0595 S32: -0.1893 S33: 0.0377
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 311 THROUGH 349 )
REMARK 3 ORIGIN FOR THE GROUP (A): 54.3009 -23.5418 413.6485
REMARK 3 T TENSOR
REMARK 3 T11: 0.1288 T22: 0.0985
REMARK 3 T33: 0.0735 T12: -0.0126
REMARK 3 T13: -0.0122 T23: -0.0073
REMARK 3 L TENSOR
REMARK 3 L11: 2.4489 L22: 1.4265
REMARK 3 L33: 1.2346 L12: -0.2751
REMARK 3 L13: -0.2984 L23: 0.2871
REMARK 3 S TENSOR
REMARK 3 S11: 0.0723 S12: -0.0400 S13: 0.1695
REMARK 3 S21: 0.0553 S22: -0.0619 S23: -0.1866
REMARK 3 S31: -0.2939 S32: 0.0238 S33: -0.0844
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 1 THROUGH 19 )
REMARK 3 ORIGIN FOR THE GROUP (A): 51.2859 -54.9234 369.5205
REMARK 3 T TENSOR
REMARK 3 T11: 0.1383 T22: 0.1492
REMARK 3 T33: 0.1544 T12: -0.0118
REMARK 3 T13: -0.0347 T23: -0.0552
REMARK 3 L TENSOR
REMARK 3 L11: 1.8540 L22: 1.7198
REMARK 3 L33: 2.7110 L12: 0.1542
REMARK 3 L13: -1.7826 L23: -0.3627
REMARK 3 S TENSOR
REMARK 3 S11: -0.0611 S12: 0.3526 S13: -0.2625
REMARK 3 S21: -0.1129 S22: 0.0591 S23: 0.1412
REMARK 3 S31: 0.3860 S32: -0.2743 S33: 0.0036
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 20 THROUGH 50 )
REMARK 3 ORIGIN FOR THE GROUP (A): 62.5868 -43.7913 362.6419
REMARK 3 T TENSOR
REMARK 3 T11: 0.1279 T22: 0.2450
REMARK 3 T33: 0.0989 T12: -0.0164
REMARK 3 T13: 0.0243 T23: -0.0470
REMARK 3 L TENSOR
REMARK 3 L11: 2.0761 L22: 1.7318
REMARK 3 L33: 1.5415 L12: -1.0402
REMARK 3 L13: 1.4332 L23: -1.1545
REMARK 3 S TENSOR
REMARK 3 S11: 0.0155 S12: 0.1612 S13: 0.0623
REMARK 3 S21: -0.1367 S22: -0.0902 S23: -0.2171
REMARK 3 S31: 0.1007 S32: 0.3645 S33: 0.0731
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 51 THROUGH 114 )
REMARK 3 ORIGIN FOR THE GROUP (A): 54.5661 -44.4903 370.5083
REMARK 3 T TENSOR
REMARK 3 T11: 0.0745 T22: 0.1002
REMARK 3 T33: 0.0808 T12: -0.0279
REMARK 3 T13: 0.0009 T23: -0.0209
REMARK 3 L TENSOR
REMARK 3 L11: 1.2278 L22: 1.2687
REMARK 3 L33: 1.1507 L12: -0.6925
REMARK 3 L13: 0.3377 L23: -0.2763
REMARK 3 S TENSOR
REMARK 3 S11: -0.0360 S12: 0.1516 S13: -0.0727
REMARK 3 S21: 0.0180 S22: 0.0095 S23: 0.0124
REMARK 3 S31: 0.0321 S32: 0.0380 S33: 0.0184
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 115 THROUGH 137 )
REMARK 3 ORIGIN FOR THE GROUP (A): 62.4067 -38.4455 362.2238
REMARK 3 T TENSOR
REMARK 3 T11: 0.0960 T22: 0.1838
REMARK 3 T33: 0.0927 T12: -0.0438
REMARK 3 T13: 0.0111 T23: -0.0209
REMARK 3 L TENSOR
REMARK 3 L11: 2.1401 L22: 0.7072
REMARK 3 L33: 1.4596 L12: -0.3541
REMARK 3 L13: 0.5467 L23: 0.3162
REMARK 3 S TENSOR
REMARK 3 S11: 0.0530 S12: 0.2617 S13: -0.1629
REMARK 3 S21: -0.1519 S22: 0.0476 S23: -0.1201
REMARK 3 S31: 0.0002 S32: 0.2083 S33: -0.0716
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 138 THROUGH 199 )
REMARK 3 ORIGIN FOR THE GROUP (A): 61.1353 -40.4520 380.3459
REMARK 3 T TENSOR
REMARK 3 T11: 0.0638 T22: 0.1242
REMARK 3 T33: 0.0864 T12: -0.0105
REMARK 3 T13: -0.0103 T23: -0.0082
REMARK 3 L TENSOR
REMARK 3 L11: 0.6374 L22: 0.5836
REMARK 3 L33: 0.7678 L12: 0.2546
REMARK 3 L13: 0.0970 L23: -0.1771
REMARK 3 S TENSOR
REMARK 3 S11: -0.0099 S12: 0.0894 S13: -0.0463
REMARK 3 S21: -0.0121 S22: 0.0188 S23: -0.0593
REMARK 3 S31: -0.0174 S32: 0.1062 S33: 0.0104
REMARK 3 TLS GROUP : 24
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 200 THROUGH 232 )
REMARK 3 ORIGIN FOR THE GROUP (A): 45.7019 -45.6872 391.2831
REMARK 3 T TENSOR
REMARK 3 T11: 0.0976 T22: 0.0844
REMARK 3 T33: 0.0633 T12: -0.0321
REMARK 3 T13: -0.0077 T23: 0.0018
REMARK 3 L TENSOR
REMARK 3 L11: 1.5186 L22: 2.2252
REMARK 3 L33: 0.7990 L12: -0.7408
REMARK 3 L13: -0.1375 L23: 0.6810
REMARK 3 S TENSOR
REMARK 3 S11: -0.0139 S12: -0.0711 S13: -0.0930
REMARK 3 S21: 0.0175 S22: 0.0296 S23: 0.1112
REMARK 3 S31: 0.0920 S32: -0.0572 S33: 0.0010
REMARK 3 TLS GROUP : 25
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 233 THROUGH 253 )
REMARK 3 ORIGIN FOR THE GROUP (A): 42.7012 -50.4297 388.5010
REMARK 3 T TENSOR
REMARK 3 T11: 0.1086 T22: 0.1423
REMARK 3 T33: 0.1634 T12: -0.0342
REMARK 3 T13: -0.0062 T23: -0.0124
REMARK 3 L TENSOR
REMARK 3 L11: 2.5087 L22: 1.4315
REMARK 3 L33: 1.7708 L12: -1.7163
REMARK 3 L13: -1.0504 L23: 0.9935
REMARK 3 S TENSOR
REMARK 3 S11: -0.1932 S12: 0.2787 S13: -0.2031
REMARK 3 S21: 0.1497 S22: -0.1177 S23: 0.2543
REMARK 3 S31: 0.1234 S32: -0.2646 S33: 0.2060
REMARK 3 TLS GROUP : 26
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 254 THROUGH 310 )
REMARK 3 ORIGIN FOR THE GROUP (A): 61.8646 -32.1946 380.8567
REMARK 3 T TENSOR
REMARK 3 T11: 0.0895 T22: 0.1166
REMARK 3 T33: 0.0789 T12: -0.0317
REMARK 3 T13: -0.0164 T23: -0.0142
REMARK 3 L TENSOR
REMARK 3 L11: 0.8435 L22: 0.8312
REMARK 3 L33: 0.4837 L12: -0.0960
REMARK 3 L13: -0.0893 L23: 0.0713
REMARK 3 S TENSOR
REMARK 3 S11: -0.0717 S12: -0.0153 S13: 0.0541
REMARK 3 S21: -0.0551 S22: 0.0874 S23: -0.0619
REMARK 3 S31: -0.0540 S32: 0.1652 S33: -0.0099
REMARK 3 TLS GROUP : 27
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 311 THROUGH 349 )
REMARK 3 ORIGIN FOR THE GROUP (A): 46.2133 -27.9847 377.2508
REMARK 3 T TENSOR
REMARK 3 T11: 0.1258 T22: 0.1367
REMARK 3 T33: 0.0815 T12: -0.0100
REMARK 3 T13: -0.0393 T23: -0.0003
REMARK 3 L TENSOR
REMARK 3 L11: 1.0486 L22: 0.9807
REMARK 3 L33: 1.4725 L12: -0.0886
REMARK 3 L13: -0.2089 L23: -0.1111
REMARK 3 S TENSOR
REMARK 3 S11: -0.0578 S12: 0.1333 S13: 0.1491
REMARK 3 S21: -0.0904 S22: -0.0109 S23: 0.1705
REMARK 3 S31: -0.1447 S32: -0.2068 S33: 0.0281
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 5D6O COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-AUG-15.
REMARK 100 THE DEPOSITION ID IS D_1000212743.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-JUL-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : BESSY
REMARK 200 BEAMLINE : 14.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.91841
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 120186
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 19.930
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 13.10
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.21960
REMARK 200 FOR THE DATA SET : 12.7300
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) : 1.86
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 13.10
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.280
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: TRIGONAL STRUCTURE OF THE SAME PROTEIN
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.05
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: RESERVOIR: 24 %(W/V) PEG4000, 20
REMARK 280 %(V/V) GLYCEROL, 0.16 M MAGNESIUM CHLORIDE, 80 MM TRIS/HCL, PH
REMARK 280 8.5. DROP BEFORE EQUILIBRATION: 0.4 MIKROLITER RESERVOIR
REMARK 280 SOLUTION PLUT 0.8 MIKROLITER ENZYME SOLUTION (PROTEIN
REMARK 280 CONCENTRATION: 5 MG/ML), VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-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 22.07050
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 161.39400
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 44.80600
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 161.39400
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 22.07050
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 44.80600
REMARK 290 SMTRY3 4 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: 5950 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23730 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -84.0 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: 5340 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23670 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -88.0 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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH C 761 O HOH C 869 1.56
REMARK 500 O HOH B 815 O HOH B 817 1.57
REMARK 500 MG MG A 403 O HOH A 540 1.60
REMARK 500 O HOH A 667 O HOH A 898 1.60
REMARK 500 O HOH B 795 O HOH B 1062 1.69
REMARK 500 O HOH C 742 O HOH C 754 1.70
REMARK 500 O HOH B 707 O HOH B 820 1.71
REMARK 500 O HOH B 813 O HOH B 904 1.71
REMARK 500 O HOH B 773 O HOH B 837 1.74
REMARK 500 O HOH D 513 O HOH D 708 1.74
REMARK 500 O HOH A 1026 O HOH A 1056 1.74
REMARK 500 O HOH B 680 O HOH B 940 1.74
REMARK 500 O HOH B 986 O HOH B 996 1.74
REMARK 500 O HOH C 825 O HOH C 892 1.76
REMARK 500 O HOH D 615 O HOH D 846 1.76
REMARK 500 O HOH C 719 O HOH C 905 1.76
REMARK 500 O HOH A 882 O HOH A 1034 1.76
REMARK 500 O HOH A 828 O HOH A 857 1.77
REMARK 500 O HOH B 997 O HOH B 1127 1.78
REMARK 500 O HOH B 812 O HOH B 844 1.78
REMARK 500 O HOH B 811 O HOH B 819 1.78
REMARK 500 O HOH D 1102 O HOH D 1109 1.79
REMARK 500 O HOH C 605 O HOH C 682 1.79
REMARK 500 O HOH C 567 O HOH C 958 1.79
REMARK 500 O HOH C 511 O HOH C 809 1.79
REMARK 500 O HOH A 733 O HOH A 883 1.79
REMARK 500 O HOH B 763 O HOH B 896 1.79
REMARK 500 O HOH A 876 O HOH A 1030 1.79
REMARK 500 O HOH B 1032 O HOH B 1126 1.80
REMARK 500 O HOH B 722 O HOH B 840 1.81
REMARK 500 O HOH C 602 O HOH C 739 1.81
REMARK 500 O HOH A 971 O HOH D 853 1.82
REMARK 500 O HOH D 782 O HOH D 919 1.82
REMARK 500 O HOH C 1102 O HOH D 1109 1.82
REMARK 500 O HOH D 775 O HOH D 797 1.83
REMARK 500 O HOH A 638 O HOH A 842 1.83
REMARK 500 O HOH A 825 O HOH A 995 1.84
REMARK 500 O HOH D 876 O HOH D 955 1.84
REMARK 500 O HOH A 1061 O HOH A 1069 1.85
REMARK 500 O HOH C 980 O HOH C 1029 1.85
REMARK 500 O HOH C 686 O HOH C 784 1.86
REMARK 500 O HOH C 903 O HOH C 1003 1.87
REMARK 500 O HOH B 568 O HOH B 717 1.87
REMARK 500 O HOH A 814 O HOH A 1009 1.87
REMARK 500 O HOH B 790 O HOH B 1080 1.87
REMARK 500 O HOH B 582 O HOH B 876 1.88
REMARK 500 O HOH C 983 O HOH D 969 1.88
REMARK 500 O HOH D 785 O HOH D 918 1.88
REMARK 500 O GLU C 46 O HOH C 501 1.88
REMARK 500 O HOH C 756 O HOH C 967 1.89
REMARK 500
REMARK 500 THIS ENTRY HAS 329 CLOSE CONTACTS
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 774 O HOH B 617 4557 1.64
REMARK 500 O HOH B 936 O HOH B 942 4457 1.75
REMARK 500 O HOH A 891 O HOH B 889 4447 1.76
REMARK 500 O HOH C 763 O HOH D 840 3757 1.77
REMARK 500 O HOH B 995 O HOH D 694 4547 1.80
REMARK 500 O HOH C 762 O HOH D 812 3747 1.80
REMARK 500 O HOH A 1043 O HOH A 1059 1455 1.80
REMARK 500 O HOH B 769 O HOH D 874 4447 1.86
REMARK 500 O HOH A 774 O HOH B 732 4557 1.86
REMARK 500 O HOH B 1094 O HOH D 994 4547 1.87
REMARK 500 O HOH A 852 O HOH C 538 3757 1.87
REMARK 500 O HOH A 718 O HOH C 879 3757 1.92
REMARK 500 O HOH A 553 O HOH B 766 4557 1.94
REMARK 500 O HOH B 1036 O HOH D 1022 4447 1.95
REMARK 500 O HOH A 887 O HOH A 998 1455 1.96
REMARK 500 O HOH B 934 O HOH B 964 4447 1.97
REMARK 500 O HOH A 907 O HOH A 952 1655 1.98
REMARK 500 O HOH B 931 O HOH D 827 4547 2.01
REMARK 500 O HOH B 583 O HOH D 802 4547 2.02
REMARK 500 O HOH C 881 O HOH D 1038 1655 2.02
REMARK 500 O HOH B 986 O HOH B 1137 4547 2.06
REMARK 500 O HOH B 743 O HOH D 972 4547 2.07
REMARK 500 O HOH D 883 O HOH D 901 1455 2.07
REMARK 500 O HOH C 649 O HOH D 840 3757 2.08
REMARK 500 O HOH A 1052 O HOH B 1023 4547 2.09
REMARK 500 O HOH B 1003 O HOH D 985 4447 2.11
REMARK 500 O HOH C 940 O HOH D 590 1655 2.11
REMARK 500 O HOH B 992 O HOH D 994 4547 2.11
REMARK 500 O HOH A 996 O HOH B 552 4457 2.11
REMARK 500 O HOH B 976 O HOH B 1050 4557 2.12
REMARK 500 O HOH C 707 O HOH D 748 3757 2.12
REMARK 500 O HOH A 569 O HOH B 952 4447 2.13
REMARK 500 O HOH C 647 O HOH D 828 3857 2.13
REMARK 500 O HOH A 943 O HOH B 717 1455 2.13
REMARK 500 O HOH A 943 O HOH B 519 1455 2.13
REMARK 500 O HOH C 860 O HOH D 902 3747 2.13
REMARK 500 O HOH A 869 O HOH C 773 3757 2.14
REMARK 500 O HOH A 774 O HOH B 501 4557 2.15
REMARK 500 O HOH B 996 O HOH B 1137 4547 2.16
REMARK 500 O HOH C 929 O HOH D 1010 3757 2.16
REMARK 500 O HOH C 704 O HOH D 840 3757 2.17
REMARK 500 O HOH B 953 O HOH B 974 1455 2.17
REMARK 500 O HOH A 1039 O HOH D 1115 1565 2.17
REMARK 500 O HOH B 851 O HOH D 874 4447 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 TYR A 7 58.82 -97.23
REMARK 500 THR A 61 -153.06 -138.92
REMARK 500 MET A 107 -116.07 54.58
REMARK 500 SER A 142 -111.62 60.78
REMARK 500 PHE A 219 -121.04 -114.49
REMARK 500 PHE A 244 -66.21 -131.54
REMARK 500 ASP A 268 100.00 -165.42
REMARK 500 PHE A 299 63.22 -118.23
REMARK 500 ASN A 330 71.12 60.09
REMARK 500 TYR B 7 59.42 -96.57
REMARK 500 THR B 61 -153.93 -138.32
REMARK 500 MET B 107 -114.48 54.75
REMARK 500 SER B 142 -111.96 59.52
REMARK 500 PHE B 219 -121.66 -114.40
REMARK 500 PHE B 244 -65.89 -131.01
REMARK 500 ASP B 268 99.40 -164.45
REMARK 500 PHE B 299 62.32 -118.65
REMARK 500 ASN B 330 70.36 59.97
REMARK 500 THR C 61 -153.39 -138.48
REMARK 500 MET C 107 -114.92 53.78
REMARK 500 SER C 142 -111.49 59.96
REMARK 500 PHE C 219 -121.43 -114.35
REMARK 500 PHE C 244 -65.70 -131.72
REMARK 500 ASP C 268 100.98 -165.24
REMARK 500 ASN C 330 70.67 59.52
REMARK 500 TYR D 7 58.90 -96.75
REMARK 500 THR D 61 -152.81 -138.15
REMARK 500 MET D 107 -115.77 55.05
REMARK 500 SER D 142 -112.11 60.18
REMARK 500 PHE D 219 -122.03 -113.99
REMARK 500 PHE D 244 -65.69 -130.87
REMARK 500 ASP D 268 99.74 -164.59
REMARK 500 PHE D 299 64.03 -118.60
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 A1062 DISTANCE = 5.81 ANGSTROMS
REMARK 525 HOH A1063 DISTANCE = 5.92 ANGSTROMS
REMARK 525 HOH A1064 DISTANCE = 6.01 ANGSTROMS
REMARK 525 HOH A1065 DISTANCE = 6.06 ANGSTROMS
REMARK 525 HOH A1066 DISTANCE = 6.12 ANGSTROMS
REMARK 525 HOH A1067 DISTANCE = 6.24 ANGSTROMS
REMARK 525 HOH A1068 DISTANCE = 6.26 ANGSTROMS
REMARK 525 HOH A1069 DISTANCE = 6.38 ANGSTROMS
REMARK 525 HOH A1070 DISTANCE = 6.45 ANGSTROMS
REMARK 525 HOH A1071 DISTANCE = 6.79 ANGSTROMS
REMARK 525 HOH A1072 DISTANCE = 7.60 ANGSTROMS
REMARK 525 HOH B1151 DISTANCE = 5.81 ANGSTROMS
REMARK 525 HOH B1152 DISTANCE = 5.85 ANGSTROMS
REMARK 525 HOH B1153 DISTANCE = 5.92 ANGSTROMS
REMARK 525 HOH B1154 DISTANCE = 5.95 ANGSTROMS
REMARK 525 HOH B1155 DISTANCE = 5.96 ANGSTROMS
REMARK 525 HOH B1156 DISTANCE = 5.99 ANGSTROMS
REMARK 525 HOH B1157 DISTANCE = 5.99 ANGSTROMS
REMARK 525 HOH B1158 DISTANCE = 6.12 ANGSTROMS
REMARK 525 HOH B1159 DISTANCE = 6.16 ANGSTROMS
REMARK 525 HOH B1160 DISTANCE = 6.22 ANGSTROMS
REMARK 525 HOH B1161 DISTANCE = 6.38 ANGSTROMS
REMARK 525 HOH B1162 DISTANCE = 6.43 ANGSTROMS
REMARK 525 HOH B1163 DISTANCE = 6.46 ANGSTROMS
REMARK 525 HOH B1164 DISTANCE = 6.77 ANGSTROMS
REMARK 525 HOH B1165 DISTANCE = 6.80 ANGSTROMS
REMARK 525 HOH B1166 DISTANCE = 6.98 ANGSTROMS
REMARK 525 HOH B1167 DISTANCE = 7.01 ANGSTROMS
REMARK 525 HOH B1168 DISTANCE = 7.10 ANGSTROMS
REMARK 525 HOH B1169 DISTANCE = 7.22 ANGSTROMS
REMARK 525 HOH B1170 DISTANCE = 7.33 ANGSTROMS
REMARK 525 HOH B1171 DISTANCE = 7.36 ANGSTROMS
REMARK 525 HOH B1172 DISTANCE = 7.45 ANGSTROMS
REMARK 525 HOH B1173 DISTANCE = 7.50 ANGSTROMS
REMARK 525 HOH B1174 DISTANCE = 7.78 ANGSTROMS
REMARK 525 HOH B1175 DISTANCE = 7.83 ANGSTROMS
REMARK 525 HOH B1176 DISTANCE = 7.99 ANGSTROMS
REMARK 525 HOH B1177 DISTANCE = 8.00 ANGSTROMS
REMARK 525 HOH B1178 DISTANCE = 8.30 ANGSTROMS
REMARK 525 HOH B1179 DISTANCE = 8.68 ANGSTROMS
REMARK 525 HOH B1180 DISTANCE = 8.83 ANGSTROMS
REMARK 525 HOH B1181 DISTANCE = 8.91 ANGSTROMS
REMARK 525 HOH B1182 DISTANCE = 8.98 ANGSTROMS
REMARK 525 HOH B1183 DISTANCE = 9.01 ANGSTROMS
REMARK 525 HOH B1184 DISTANCE = 10.07 ANGSTROMS
REMARK 525 HOH B1185 DISTANCE = 10.11 ANGSTROMS
REMARK 525 HOH C1072 DISTANCE = 5.82 ANGSTROMS
REMARK 525 HOH C1073 DISTANCE = 6.05 ANGSTROMS
REMARK 525 HOH C1074 DISTANCE = 6.07 ANGSTROMS
REMARK 525 HOH C1075 DISTANCE = 6.07 ANGSTROMS
REMARK 525 HOH C1076 DISTANCE = 6.16 ANGSTROMS
REMARK 525 HOH C1077 DISTANCE = 6.22 ANGSTROMS
REMARK 525 HOH C1078 DISTANCE = 6.24 ANGSTROMS
REMARK 525 HOH C1079 DISTANCE = 6.26 ANGSTROMS
REMARK 525 HOH C1080 DISTANCE = 6.32 ANGSTROMS
REMARK 525 HOH C1081 DISTANCE = 6.43 ANGSTROMS
REMARK 525 HOH C1082 DISTANCE = 6.50 ANGSTROMS
REMARK 525 HOH C1083 DISTANCE = 6.50 ANGSTROMS
REMARK 525 HOH C1084 DISTANCE = 6.53 ANGSTROMS
REMARK 525 HOH C1085 DISTANCE = 6.55 ANGSTROMS
REMARK 525 HOH C1086 DISTANCE = 6.56 ANGSTROMS
REMARK 525 HOH C1087 DISTANCE = 6.61 ANGSTROMS
REMARK 525 HOH C1088 DISTANCE = 6.65 ANGSTROMS
REMARK 525 HOH C1089 DISTANCE = 6.66 ANGSTROMS
REMARK 525 HOH C1090 DISTANCE = 6.68 ANGSTROMS
REMARK 525 HOH C1091 DISTANCE = 6.72 ANGSTROMS
REMARK 525 HOH C1092 DISTANCE = 6.74 ANGSTROMS
REMARK 525 HOH C1093 DISTANCE = 6.82 ANGSTROMS
REMARK 525 HOH C1094 DISTANCE = 6.91 ANGSTROMS
REMARK 525 HOH C1095 DISTANCE = 6.94 ANGSTROMS
REMARK 525 HOH C1096 DISTANCE = 7.13 ANGSTROMS
REMARK 525 HOH C1097 DISTANCE = 7.15 ANGSTROMS
REMARK 525 HOH C1098 DISTANCE = 7.41 ANGSTROMS
REMARK 525 HOH C1099 DISTANCE = 7.43 ANGSTROMS
REMARK 525 HOH C1100 DISTANCE = 7.49 ANGSTROMS
REMARK 525 HOH C1101 DISTANCE = 7.61 ANGSTROMS
REMARK 525 HOH C1102 DISTANCE = 7.69 ANGSTROMS
REMARK 525 HOH C1103 DISTANCE = 7.82 ANGSTROMS
REMARK 525 HOH C1104 DISTANCE = 7.82 ANGSTROMS
REMARK 525 HOH C1105 DISTANCE = 7.90 ANGSTROMS
REMARK 525 HOH C1106 DISTANCE = 7.92 ANGSTROMS
REMARK 525 HOH C1107 DISTANCE = 8.27 ANGSTROMS
REMARK 525 HOH C1108 DISTANCE = 8.85 ANGSTROMS
REMARK 525 HOH C1109 DISTANCE = 8.87 ANGSTROMS
REMARK 525 HOH C1110 DISTANCE = 8.93 ANGSTROMS
REMARK 525 HOH C1111 DISTANCE = 9.22 ANGSTROMS
REMARK 525 HOH C1112 DISTANCE = 9.45 ANGSTROMS
REMARK 525 HOH C1113 DISTANCE = 9.49 ANGSTROMS
REMARK 525 HOH C1114 DISTANCE = 9.75 ANGSTROMS
REMARK 525 HOH C1115 DISTANCE = 9.99 ANGSTROMS
REMARK 525 HOH C1116 DISTANCE = 10.80 ANGSTROMS
REMARK 525 HOH D1089 DISTANCE = 5.81 ANGSTROMS
REMARK 525 HOH D1090 DISTANCE = 5.83 ANGSTROMS
REMARK 525 HOH D1091 DISTANCE = 5.84 ANGSTROMS
REMARK 525 HOH D1092 DISTANCE = 5.92 ANGSTROMS
REMARK 525 HOH D1093 DISTANCE = 5.99 ANGSTROMS
REMARK 525 HOH D1094 DISTANCE = 6.07 ANGSTROMS
REMARK 525 HOH D1095 DISTANCE = 6.16 ANGSTROMS
REMARK 525 HOH D1096 DISTANCE = 6.24 ANGSTROMS
REMARK 525 HOH D1097 DISTANCE = 6.29 ANGSTROMS
REMARK 525 HOH D1098 DISTANCE = 6.30 ANGSTROMS
REMARK 525 HOH D1099 DISTANCE = 6.34 ANGSTROMS
REMARK 525 HOH D1100 DISTANCE = 6.43 ANGSTROMS
REMARK 525 HOH D1101 DISTANCE = 6.81 ANGSTROMS
REMARK 525 HOH D1102 DISTANCE = 6.85 ANGSTROMS
REMARK 525 HOH D1103 DISTANCE = 6.87 ANGSTROMS
REMARK 525 HOH D1104 DISTANCE = 6.91 ANGSTROMS
REMARK 525 HOH D1105 DISTANCE = 6.97 ANGSTROMS
REMARK 525 HOH D1106 DISTANCE = 7.14 ANGSTROMS
REMARK 525 HOH D1107 DISTANCE = 7.56 ANGSTROMS
REMARK 525 HOH D1108 DISTANCE = 7.62 ANGSTROMS
REMARK 525 HOH D1109 DISTANCE = 7.68 ANGSTROMS
REMARK 525 HOH D1110 DISTANCE = 7.72 ANGSTROMS
REMARK 525 HOH D1111 DISTANCE = 7.73 ANGSTROMS
REMARK 525 HOH D1112 DISTANCE = 7.82 ANGSTROMS
REMARK 525 HOH D1113 DISTANCE = 8.02 ANGSTROMS
REMARK 525 HOH D1114 DISTANCE = 8.14 ANGSTROMS
REMARK 525 HOH D1115 DISTANCE = 9.06 ANGSTROMS
REMARK 525 HOH D1116 DISTANCE = 9.84 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 403 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 572 O
REMARK 620 2 HOH A 892 O 131.4
REMARK 620 3 HOH A 905 O 82.7 51.6
REMARK 620 4 HOH A 534 O 168.7 46.0 90.5
REMARK 620 5 HOH A 672 O 86.2 104.4 86.8 84.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 403 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B 599 O
REMARK 620 2 HOH B 624 O 88.6
REMARK 620 3 HOH B 715 O 93.4 175.9
REMARK 620 4 HOH B 580 O 176.6 91.1 86.8
REMARK 620 5 HOH B 894 O 92.7 85.7 90.7 83.9
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C 403 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH C 556 O
REMARK 620 2 HOH C 580 O 165.0
REMARK 620 3 HOH C 718 O 87.5 86.8
REMARK 620 4 HOH C 519 O 87.3 94.9 165.6
REMARK 620 5 HOH C 726 O 98.4 66.7 73.3 94.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D 403 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH D 684 O
REMARK 620 2 HOH D 911 O 81.9
REMARK 620 3 HOH D 549 O 77.8 86.2
REMARK 620 4 HOH D 678 O 97.4 88.4 173.3
REMARK 620 5 HOH D 605 O 166.8 88.6 92.4 91.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D 404 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH D 810 O
REMARK 620 2 HOH D 823 O 91.8
REMARK 620 3 HOH D 973 O 88.3 55.9
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 410
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 411
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL C 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG C 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL D 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL D 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG D 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG D 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 408
DBREF 5D6O A 1 349 UNP Q8NS43 Q8NS43_CORGL 1 349
DBREF 5D6O B 1 349 UNP Q8NS43 Q8NS43_CORGL 1 349
DBREF 5D6O C 1 349 UNP Q8NS43 Q8NS43_CORGL 1 349
DBREF 5D6O D 1 349 UNP Q8NS43 Q8NS43_CORGL 1 349
SEQRES 1 A 349 MET LEU ASP ASN SER PHE TYR THR ALA GLU VAL GLN GLY
SEQRES 2 A 349 PRO TYR GLU THR ALA SER ILE GLY ARG LEU GLU LEU GLU
SEQRES 3 A 349 GLU GLY GLY VAL ILE GLU ASP CYS TRP LEU ALA TYR ALA
SEQRES 4 A 349 THR ALA GLY THR LEU ASN GLU ASP LYS SER ASN ALA ILE
SEQRES 5 A 349 LEU ILE PRO THR TRP TYR SER GLY THR HIS GLN THR TRP
SEQRES 6 A 349 PHE GLN GLN TYR ILE GLY THR ASP HIS ALA LEU ASP PRO
SEQRES 7 A 349 SER LYS TYR PHE ILE ILE SER ILE ASN GLN ILE GLY ASN
SEQRES 8 A 349 GLY LEU SER VAL SER PRO ALA ASN THR ALA ASP ASP SER
SEQRES 9 A 349 ILE SER MET SER LYS PHE PRO ASN VAL ARG ILE GLY ASP
SEQRES 10 A 349 ASP VAL VAL ALA GLN ASP ARG LEU LEU ARG GLN GLU PHE
SEQRES 11 A 349 GLY ILE THR GLU LEU PHE ALA VAL VAL GLY GLY SER MET
SEQRES 12 A 349 GLY ALA GLN GLN THR TYR GLU TRP ILE VAL ARG PHE PRO
SEQRES 13 A 349 ASP GLN VAL HIS ARG ALA ALA PRO ILE ALA GLY THR ALA
SEQRES 14 A 349 LYS ASN THR PRO HIS ASP PHE ILE PHE THR GLN THR LEU
SEQRES 15 A 349 ASN GLU THR VAL GLU ALA ASP PRO GLY PHE ASN GLY GLY
SEQRES 16 A 349 GLU TYR SER SER HIS GLU GLU VAL ALA ASP GLY LEU ARG
SEQRES 17 A 349 ARG GLN SER HIS LEU TRP ALA ALA MET GLY PHE SER THR
SEQRES 18 A 349 GLU PHE TRP LYS GLN GLU ALA TRP ARG ARG LEU GLY LEU
SEQRES 19 A 349 GLU SER LYS GLU SER VAL LEU ALA ASP PHE LEU ASP PRO
SEQRES 20 A 349 LEU PHE MET SER MET ASP PRO ASN THR LEU LEU ASN ASN
SEQRES 21 A 349 ALA TRP LYS TRP GLN HIS GLY ASP VAL SER ARG HIS THR
SEQRES 22 A 349 GLY GLY ASP LEU ALA ALA ALA LEU GLY ARG VAL LYS ALA
SEQRES 23 A 349 LYS THR PHE VAL MET PRO ILE SER GLU ASP MET PHE PHE
SEQRES 24 A 349 PRO VAL ARG ASP CYS ALA ALA GLU GLN ALA LEU ILE PRO
SEQRES 25 A 349 GLY SER GLU LEU ARG VAL ILE GLU ASP ILE ALA GLY HIS
SEQRES 26 A 349 LEU GLY LEU PHE ASN VAL SER GLU ASN TYR ILE PRO GLN
SEQRES 27 A 349 ILE ASP LYS ASN LEU LYS GLU LEU PHE GLU SER
SEQRES 1 B 349 MET LEU ASP ASN SER PHE TYR THR ALA GLU VAL GLN GLY
SEQRES 2 B 349 PRO TYR GLU THR ALA SER ILE GLY ARG LEU GLU LEU GLU
SEQRES 3 B 349 GLU GLY GLY VAL ILE GLU ASP CYS TRP LEU ALA TYR ALA
SEQRES 4 B 349 THR ALA GLY THR LEU ASN GLU ASP LYS SER ASN ALA ILE
SEQRES 5 B 349 LEU ILE PRO THR TRP TYR SER GLY THR HIS GLN THR TRP
SEQRES 6 B 349 PHE GLN GLN TYR ILE GLY THR ASP HIS ALA LEU ASP PRO
SEQRES 7 B 349 SER LYS TYR PHE ILE ILE SER ILE ASN GLN ILE GLY ASN
SEQRES 8 B 349 GLY LEU SER VAL SER PRO ALA ASN THR ALA ASP ASP SER
SEQRES 9 B 349 ILE SER MET SER LYS PHE PRO ASN VAL ARG ILE GLY ASP
SEQRES 10 B 349 ASP VAL VAL ALA GLN ASP ARG LEU LEU ARG GLN GLU PHE
SEQRES 11 B 349 GLY ILE THR GLU LEU PHE ALA VAL VAL GLY GLY SER MET
SEQRES 12 B 349 GLY ALA GLN GLN THR TYR GLU TRP ILE VAL ARG PHE PRO
SEQRES 13 B 349 ASP GLN VAL HIS ARG ALA ALA PRO ILE ALA GLY THR ALA
SEQRES 14 B 349 LYS ASN THR PRO HIS ASP PHE ILE PHE THR GLN THR LEU
SEQRES 15 B 349 ASN GLU THR VAL GLU ALA ASP PRO GLY PHE ASN GLY GLY
SEQRES 16 B 349 GLU TYR SER SER HIS GLU GLU VAL ALA ASP GLY LEU ARG
SEQRES 17 B 349 ARG GLN SER HIS LEU TRP ALA ALA MET GLY PHE SER THR
SEQRES 18 B 349 GLU PHE TRP LYS GLN GLU ALA TRP ARG ARG LEU GLY LEU
SEQRES 19 B 349 GLU SER LYS GLU SER VAL LEU ALA ASP PHE LEU ASP PRO
SEQRES 20 B 349 LEU PHE MET SER MET ASP PRO ASN THR LEU LEU ASN ASN
SEQRES 21 B 349 ALA TRP LYS TRP GLN HIS GLY ASP VAL SER ARG HIS THR
SEQRES 22 B 349 GLY GLY ASP LEU ALA ALA ALA LEU GLY ARG VAL LYS ALA
SEQRES 23 B 349 LYS THR PHE VAL MET PRO ILE SER GLU ASP MET PHE PHE
SEQRES 24 B 349 PRO VAL ARG ASP CYS ALA ALA GLU GLN ALA LEU ILE PRO
SEQRES 25 B 349 GLY SER GLU LEU ARG VAL ILE GLU ASP ILE ALA GLY HIS
SEQRES 26 B 349 LEU GLY LEU PHE ASN VAL SER GLU ASN TYR ILE PRO GLN
SEQRES 27 B 349 ILE ASP LYS ASN LEU LYS GLU LEU PHE GLU SER
SEQRES 1 C 349 MET LEU ASP ASN SER PHE TYR THR ALA GLU VAL GLN GLY
SEQRES 2 C 349 PRO TYR GLU THR ALA SER ILE GLY ARG LEU GLU LEU GLU
SEQRES 3 C 349 GLU GLY GLY VAL ILE GLU ASP CYS TRP LEU ALA TYR ALA
SEQRES 4 C 349 THR ALA GLY THR LEU ASN GLU ASP LYS SER ASN ALA ILE
SEQRES 5 C 349 LEU ILE PRO THR TRP TYR SER GLY THR HIS GLN THR TRP
SEQRES 6 C 349 PHE GLN GLN TYR ILE GLY THR ASP HIS ALA LEU ASP PRO
SEQRES 7 C 349 SER LYS TYR PHE ILE ILE SER ILE ASN GLN ILE GLY ASN
SEQRES 8 C 349 GLY LEU SER VAL SER PRO ALA ASN THR ALA ASP ASP SER
SEQRES 9 C 349 ILE SER MET SER LYS PHE PRO ASN VAL ARG ILE GLY ASP
SEQRES 10 C 349 ASP VAL VAL ALA GLN ASP ARG LEU LEU ARG GLN GLU PHE
SEQRES 11 C 349 GLY ILE THR GLU LEU PHE ALA VAL VAL GLY GLY SER MET
SEQRES 12 C 349 GLY ALA GLN GLN THR TYR GLU TRP ILE VAL ARG PHE PRO
SEQRES 13 C 349 ASP GLN VAL HIS ARG ALA ALA PRO ILE ALA GLY THR ALA
SEQRES 14 C 349 LYS ASN THR PRO HIS ASP PHE ILE PHE THR GLN THR LEU
SEQRES 15 C 349 ASN GLU THR VAL GLU ALA ASP PRO GLY PHE ASN GLY GLY
SEQRES 16 C 349 GLU TYR SER SER HIS GLU GLU VAL ALA ASP GLY LEU ARG
SEQRES 17 C 349 ARG GLN SER HIS LEU TRP ALA ALA MET GLY PHE SER THR
SEQRES 18 C 349 GLU PHE TRP LYS GLN GLU ALA TRP ARG ARG LEU GLY LEU
SEQRES 19 C 349 GLU SER LYS GLU SER VAL LEU ALA ASP PHE LEU ASP PRO
SEQRES 20 C 349 LEU PHE MET SER MET ASP PRO ASN THR LEU LEU ASN ASN
SEQRES 21 C 349 ALA TRP LYS TRP GLN HIS GLY ASP VAL SER ARG HIS THR
SEQRES 22 C 349 GLY GLY ASP LEU ALA ALA ALA LEU GLY ARG VAL LYS ALA
SEQRES 23 C 349 LYS THR PHE VAL MET PRO ILE SER GLU ASP MET PHE PHE
SEQRES 24 C 349 PRO VAL ARG ASP CYS ALA ALA GLU GLN ALA LEU ILE PRO
SEQRES 25 C 349 GLY SER GLU LEU ARG VAL ILE GLU ASP ILE ALA GLY HIS
SEQRES 26 C 349 LEU GLY LEU PHE ASN VAL SER GLU ASN TYR ILE PRO GLN
SEQRES 27 C 349 ILE ASP LYS ASN LEU LYS GLU LEU PHE GLU SER
SEQRES 1 D 349 MET LEU ASP ASN SER PHE TYR THR ALA GLU VAL GLN GLY
SEQRES 2 D 349 PRO TYR GLU THR ALA SER ILE GLY ARG LEU GLU LEU GLU
SEQRES 3 D 349 GLU GLY GLY VAL ILE GLU ASP CYS TRP LEU ALA TYR ALA
SEQRES 4 D 349 THR ALA GLY THR LEU ASN GLU ASP LYS SER ASN ALA ILE
SEQRES 5 D 349 LEU ILE PRO THR TRP TYR SER GLY THR HIS GLN THR TRP
SEQRES 6 D 349 PHE GLN GLN TYR ILE GLY THR ASP HIS ALA LEU ASP PRO
SEQRES 7 D 349 SER LYS TYR PHE ILE ILE SER ILE ASN GLN ILE GLY ASN
SEQRES 8 D 349 GLY LEU SER VAL SER PRO ALA ASN THR ALA ASP ASP SER
SEQRES 9 D 349 ILE SER MET SER LYS PHE PRO ASN VAL ARG ILE GLY ASP
SEQRES 10 D 349 ASP VAL VAL ALA GLN ASP ARG LEU LEU ARG GLN GLU PHE
SEQRES 11 D 349 GLY ILE THR GLU LEU PHE ALA VAL VAL GLY GLY SER MET
SEQRES 12 D 349 GLY ALA GLN GLN THR TYR GLU TRP ILE VAL ARG PHE PRO
SEQRES 13 D 349 ASP GLN VAL HIS ARG ALA ALA PRO ILE ALA GLY THR ALA
SEQRES 14 D 349 LYS ASN THR PRO HIS ASP PHE ILE PHE THR GLN THR LEU
SEQRES 15 D 349 ASN GLU THR VAL GLU ALA ASP PRO GLY PHE ASN GLY GLY
SEQRES 16 D 349 GLU TYR SER SER HIS GLU GLU VAL ALA ASP GLY LEU ARG
SEQRES 17 D 349 ARG GLN SER HIS LEU TRP ALA ALA MET GLY PHE SER THR
SEQRES 18 D 349 GLU PHE TRP LYS GLN GLU ALA TRP ARG ARG LEU GLY LEU
SEQRES 19 D 349 GLU SER LYS GLU SER VAL LEU ALA ASP PHE LEU ASP PRO
SEQRES 20 D 349 LEU PHE MET SER MET ASP PRO ASN THR LEU LEU ASN ASN
SEQRES 21 D 349 ALA TRP LYS TRP GLN HIS GLY ASP VAL SER ARG HIS THR
SEQRES 22 D 349 GLY GLY ASP LEU ALA ALA ALA LEU GLY ARG VAL LYS ALA
SEQRES 23 D 349 LYS THR PHE VAL MET PRO ILE SER GLU ASP MET PHE PHE
SEQRES 24 D 349 PRO VAL ARG ASP CYS ALA ALA GLU GLN ALA LEU ILE PRO
SEQRES 25 D 349 GLY SER GLU LEU ARG VAL ILE GLU ASP ILE ALA GLY HIS
SEQRES 26 D 349 LEU GLY LEU PHE ASN VAL SER GLU ASN TYR ILE PRO GLN
SEQRES 27 D 349 ILE ASP LYS ASN LEU LYS GLU LEU PHE GLU SER
HET CL A 401 1
HET CL A 402 1
HET MG A 403 1
HET GOL A 404 6
HET GOL A 405 6
HET GOL A 406 6
HET GOL A 407 6
HET GOL A 408 6
HET GOL A 409 6
HET GOL A 410 6
HET GOL A 411 6
HET CL B 401 1
HET CL B 402 1
HET MG B 403 1
HET GOL B 404 6
HET GOL B 405 6
HET GOL B 406 6
HET CL C 401 1
HET CL C 402 1
HET MG C 403 1
HET GOL C 404 6
HET GOL C 405 6
HET CL D 401 1
HET CL D 402 1
HET MG D 403 1
HET MG D 404 1
HET GOL D 405 6
HET GOL D 406 6
HET GOL D 407 6
HET GOL D 408 6
HETNAM CL CHLORIDE ION
HETNAM MG MAGNESIUM ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 5 CL 8(CL 1-)
FORMUL 7 MG 5(MG 2+)
FORMUL 8 GOL 17(C3 H8 O3)
FORMUL 35 HOH *2489(H2 O)
HELIX 1 AA1 ASN A 4 TYR A 7 5 4
HELIX 2 AA2 THR A 8 GLY A 13 1 6
HELIX 3 AA3 HIS A 62 TYR A 69 1 8
HELIX 4 AA4 ASP A 102 PHE A 110 5 9
HELIX 5 AA5 ARG A 114 GLY A 131 1 18
HELIX 6 AA6 SER A 142 PHE A 155 1 14
HELIX 7 AA7 PRO A 156 VAL A 159 5 4
HELIX 8 AA8 THR A 172 ALA A 188 1 17
HELIX 9 AA9 ASP A 189 GLU A 196 5 8
HELIX 10 AB1 SER A 199 GLU A 202 5 4
HELIX 11 AB2 VAL A 203 GLY A 218 1 16
HELIX 12 AB3 SER A 220 GLN A 226 1 7
HELIX 13 AB4 GLU A 227 GLY A 233 5 7
HELIX 14 AB5 SER A 236 PHE A 244 1 9
HELIX 15 AB6 PHE A 244 SER A 251 1 8
HELIX 16 AB7 ASP A 253 HIS A 266 1 14
HELIX 17 AB8 ASP A 268 GLY A 274 5 7
HELIX 18 AB9 ASP A 276 ARG A 283 1 8
HELIX 19 AC1 PRO A 300 ALA A 309 1 10
HELIX 20 AC2 ALA A 323 ASN A 330 5 8
HELIX 21 AC3 ASN A 334 GLU A 348 1 15
HELIX 22 AC4 THR B 8 GLY B 13 1 6
HELIX 23 AC5 HIS B 62 TYR B 69 1 8
HELIX 24 AC6 ASP B 102 PHE B 110 5 9
HELIX 25 AC7 ARG B 114 GLY B 131 1 18
HELIX 26 AC8 SER B 142 PHE B 155 1 14
HELIX 27 AC9 PRO B 156 VAL B 159 5 4
HELIX 28 AD1 THR B 172 ALA B 188 1 17
HELIX 29 AD2 ASP B 189 GLU B 196 5 8
HELIX 30 AD3 SER B 199 GLU B 202 5 4
HELIX 31 AD4 VAL B 203 GLY B 218 1 16
HELIX 32 AD5 SER B 220 GLN B 226 1 7
HELIX 33 AD6 GLU B 227 GLY B 233 5 7
HELIX 34 AD7 SER B 236 PHE B 244 1 9
HELIX 35 AD8 PHE B 244 MET B 250 1 7
HELIX 36 AD9 ASP B 253 HIS B 266 1 14
HELIX 37 AE1 ASP B 268 GLY B 274 5 7
HELIX 38 AE2 ASP B 276 GLY B 282 1 7
HELIX 39 AE3 PRO B 300 ALA B 309 1 10
HELIX 40 AE4 ALA B 323 ASN B 330 5 8
HELIX 41 AE5 ASN B 334 GLU B 348 1 15
HELIX 42 AE6 THR C 8 GLY C 13 1 6
HELIX 43 AE7 HIS C 62 TYR C 69 1 8
HELIX 44 AE8 ASP C 102 PHE C 110 5 9
HELIX 45 AE9 ARG C 114 GLY C 131 1 18
HELIX 46 AF1 SER C 142 PHE C 155 1 14
HELIX 47 AF2 PRO C 156 VAL C 159 5 4
HELIX 48 AF3 THR C 172 ALA C 188 1 17
HELIX 49 AF4 ASP C 189 GLU C 196 5 8
HELIX 50 AF5 SER C 199 GLU C 202 5 4
HELIX 51 AF6 VAL C 203 GLY C 218 1 16
HELIX 52 AF7 SER C 220 GLN C 226 1 7
HELIX 53 AF8 GLU C 227 GLY C 233 5 7
HELIX 54 AF9 SER C 236 PHE C 244 1 9
HELIX 55 AG1 PHE C 244 MET C 250 1 7
HELIX 56 AG2 ASP C 253 HIS C 266 1 14
HELIX 57 AG3 ASP C 268 GLY C 274 5 7
HELIX 58 AG4 ASP C 276 GLY C 282 1 7
HELIX 59 AG5 PRO C 300 ALA C 309 1 10
HELIX 60 AG6 ALA C 323 ASN C 330 5 8
HELIX 61 AG7 ASN C 334 GLU C 348 1 15
HELIX 62 AG8 ASN D 4 TYR D 7 5 4
HELIX 63 AG9 THR D 8 GLY D 13 1 6
HELIX 64 AH1 HIS D 62 TYR D 69 1 8
HELIX 65 AH2 ASP D 102 PHE D 110 5 9
HELIX 66 AH3 ARG D 114 GLY D 131 1 18
HELIX 67 AH4 SER D 142 PHE D 155 1 14
HELIX 68 AH5 PRO D 156 VAL D 159 5 4
HELIX 69 AH6 THR D 172 ALA D 188 1 17
HELIX 70 AH7 ASP D 189 GLU D 196 5 8
HELIX 71 AH8 SER D 199 GLU D 202 5 4
HELIX 72 AH9 VAL D 203 GLY D 218 1 16
HELIX 73 AI1 SER D 220 GLN D 226 1 7
HELIX 74 AI2 GLU D 227 GLY D 233 5 7
HELIX 75 AI3 SER D 236 PHE D 244 1 9
HELIX 76 AI4 PHE D 244 SER D 251 1 8
HELIX 77 AI5 ASP D 253 HIS D 266 1 14
HELIX 78 AI6 ASP D 268 GLY D 274 5 7
HELIX 79 AI7 ASP D 276 GLY D 282 1 7
HELIX 80 AI8 PRO D 300 ALA D 309 1 10
HELIX 81 AI9 ALA D 323 ASN D 330 5 8
HELIX 82 AJ1 ASN D 334 GLU D 348 1 15
SHEET 1 AA1 8 GLU A 16 SER A 19 0
SHEET 2 AA1 8 TRP A 35 ALA A 41 -1 O TYR A 38 N GLU A 16
SHEET 3 AA1 8 PHE A 82 ILE A 86 -1 O ILE A 83 N ALA A 41
SHEET 4 AA1 8 ALA A 51 PRO A 55 1 N ILE A 52 O ILE A 84
SHEET 5 AA1 8 ALA A 137 GLY A 141 1 O VAL A 139 N LEU A 53
SHEET 6 AA1 8 ARG A 161 ILE A 165 1 O ILE A 165 N GLY A 140
SHEET 7 AA1 8 LYS A 287 VAL A 290 1 O LYS A 287 N ALA A 162
SHEET 8 AA1 8 GLU A 315 LEU A 316 1 O GLU A 315 N VAL A 290
SHEET 1 AA2 2 LEU A 23 GLU A 24 0
SHEET 2 AA2 2 VAL A 30 ILE A 31 -1 O ILE A 31 N LEU A 23
SHEET 1 AA3 8 GLU B 16 SER B 19 0
SHEET 2 AA3 8 TRP B 35 ALA B 41 -1 O TYR B 38 N GLU B 16
SHEET 3 AA3 8 PHE B 82 ILE B 86 -1 O ILE B 83 N ALA B 41
SHEET 4 AA3 8 ALA B 51 PRO B 55 1 N ILE B 52 O ILE B 84
SHEET 5 AA3 8 ALA B 137 GLY B 141 1 O VAL B 139 N LEU B 53
SHEET 6 AA3 8 ARG B 161 ILE B 165 1 O ILE B 165 N GLY B 140
SHEET 7 AA3 8 LYS B 287 VAL B 290 1 O LYS B 287 N ALA B 162
SHEET 8 AA3 8 GLU B 315 LEU B 316 1 O GLU B 315 N VAL B 290
SHEET 1 AA4 2 LEU B 23 GLU B 24 0
SHEET 2 AA4 2 VAL B 30 ILE B 31 -1 O ILE B 31 N LEU B 23
SHEET 1 AA5 8 GLU C 16 SER C 19 0
SHEET 2 AA5 8 TRP C 35 ALA C 41 -1 O TYR C 38 N GLU C 16
SHEET 3 AA5 8 PHE C 82 ILE C 86 -1 O ILE C 83 N ALA C 41
SHEET 4 AA5 8 ALA C 51 PRO C 55 1 N ILE C 52 O PHE C 82
SHEET 5 AA5 8 ALA C 137 GLY C 141 1 O VAL C 139 N LEU C 53
SHEET 6 AA5 8 ARG C 161 ILE C 165 1 O ILE C 165 N GLY C 140
SHEET 7 AA5 8 LYS C 287 VAL C 290 1 O LYS C 287 N ALA C 162
SHEET 8 AA5 8 GLU C 315 LEU C 316 1 O GLU C 315 N VAL C 290
SHEET 1 AA6 2 LEU C 23 GLU C 24 0
SHEET 2 AA6 2 VAL C 30 ILE C 31 -1 O ILE C 31 N LEU C 23
SHEET 1 AA7 8 GLU D 16 SER D 19 0
SHEET 2 AA7 8 TRP D 35 ALA D 41 -1 O TYR D 38 N GLU D 16
SHEET 3 AA7 8 PHE D 82 ILE D 86 -1 O SER D 85 N ALA D 39
SHEET 4 AA7 8 ALA D 51 PRO D 55 1 N ILE D 52 O ILE D 84
SHEET 5 AA7 8 ALA D 137 GLY D 141 1 O VAL D 139 N LEU D 53
SHEET 6 AA7 8 ARG D 161 ILE D 165 1 O ILE D 165 N GLY D 140
SHEET 7 AA7 8 LYS D 287 VAL D 290 1 O LYS D 287 N ALA D 162
SHEET 8 AA7 8 GLU D 315 LEU D 316 1 O GLU D 315 N VAL D 290
SHEET 1 AA8 2 LEU D 23 GLU D 24 0
SHEET 2 AA8 2 VAL D 30 ILE D 31 -1 O ILE D 31 N LEU D 23
LINK MG MG A 403 O HOH A 572 1555 1555 2.29
LINK MG MG A 403 O HOH A 892 1555 1555 2.96
LINK MG MG A 403 O HOH A 905 1555 1555 2.33
LINK MG MG A 403 O HOH A 534 1555 1555 2.18
LINK MG MG A 403 O HOH A 672 1555 1555 2.20
LINK MG MG B 403 O HOH B 599 1555 1555 2.07
LINK MG MG B 403 O HOH B 624 1555 1555 2.17
LINK MG MG B 403 O HOH B 715 1555 1555 2.10
LINK MG MG B 403 O HOH B 580 1555 1555 2.07
LINK MG MG B 403 O HOH B 894 1555 1555 2.18
LINK MG MG C 403 O HOH C 556 1555 1555 2.02
LINK MG MG C 403 O HOH C 580 1555 1555 2.34
LINK MG MG C 403 O HOH C 718 1555 1555 2.12
LINK MG MG C 403 O HOH C 519 1555 1555 2.48
LINK MG MG C 403 O HOH C 726 1555 1555 2.70
LINK MG MG D 403 O HOH D 684 1555 1555 2.21
LINK MG MG D 403 O HOH D 911 1555 1555 2.22
LINK MG MG D 403 O HOH D 549 1555 1555 2.35
LINK MG MG D 403 O HOH D 678 1555 1555 2.03
LINK MG MG D 403 O HOH D 605 1555 1555 2.18
LINK MG MG D 404 O HOH D 810 1555 1555 1.98
LINK MG MG D 404 O HOH D 823 1555 1555 2.42
LINK MG MG D 404 O HOH D 973 1555 1555 2.41
SITE 1 AC1 5 TRP A 57 TYR A 58 SER A 142 MET A 143
SITE 2 AC1 5 GOL A 407
SITE 1 AC2 3 THR A 61 THR A 64 GOL A 410
SITE 1 AC3 7 HIS A 74 HOH A 534 HOH A 540 HOH A 572
SITE 2 AC3 7 HOH A 672 HOH A 892 HOH A 905
SITE 1 AC4 8 LEU A 2 ASN A 4 TYR A 7 GLY A 92
SITE 2 AC4 8 SER A 96 ALA A 98 ASN A 99 HOH A 614
SITE 1 AC5 7 GLU A 227 ARG A 230 GLU A 235 HOH A 513
SITE 2 AC5 7 HOH A 730 HOH A 760 GLN B 226
SITE 1 AC6 8 PRO A 14 TYR A 15 GLU A 16 THR A 40
SITE 2 AC6 8 HOH A 588 ARG C 127 THR C 133 HOH C 665
SITE 1 AC7 9 TRP A 57 TYR A 58 SER A 59 SER A 142
SITE 2 AC7 9 TRP A 214 HIS A 325 LEU A 326 PHE A 329
SITE 3 AC7 9 CL A 401
SITE 1 AC8 2 ARG A 127 HOH A 542
SITE 1 AC9 8 GLY A 13 PRO A 14 THR A 40 PHE A 66
SITE 2 AC9 8 HOH A 573 HOH A 580 HOH A 751 HOH C 665
SITE 1 AD1 5 GLN A 63 THR A 64 CL A 402 HOH A 510
SITE 2 AD1 5 HOH A 530
SITE 1 AD2 7 GLY A 233 GLU A 235 ALA A 306 LEU A 310
SITE 2 AD2 7 HOH A 501 HOH A 546 HOH A 615
SITE 1 AD3 5 TRP B 57 TYR B 58 SER B 142 MET B 143
SITE 2 AD3 5 HOH B 597
SITE 1 AD4 3 THR B 61 THR B 64 HOH B 700
SITE 1 AD5 6 HIS B 74 HOH B 580 HOH B 599 HOH B 624
SITE 2 AD5 6 HOH B 715 HOH B 894
SITE 1 AD6 6 PRO B 97 MET B 107 SER B 108 PHE B 110
SITE 2 AD6 6 ASN B 255 ASN B 259
SITE 1 AD7 7 LEU B 2 ASN B 4 TYR B 7 GLY B 92
SITE 2 AD7 7 ALA B 98 ASN B 99 HOH B 535
SITE 1 AD8 8 PRO A 173 GLU A 235 SER A 239 ASP A 243
SITE 2 AD8 8 HOH A 613 LYS B 225 GLU B 227 HOH B 741
SITE 1 AD9 5 TRP C 57 TYR C 58 SER C 142 MET C 143
SITE 2 AD9 5 GOL C 404
SITE 1 AE1 4 GLY C 60 THR C 61 THR C 64 HOH C 676
SITE 1 AE2 7 ASP C 73 HIS C 74 HOH C 519 HOH C 556
SITE 2 AE2 7 HOH C 580 HOH C 718 HOH C 726
SITE 1 AE3 7 TRP C 57 TYR C 58 SER C 142 HIS C 325
SITE 2 AE3 7 LEU C 326 PHE C 329 CL C 401
SITE 1 AE4 6 ARG C 114 HIS C 266 ASP C 268 ARG C 271
SITE 2 AE4 6 HOH C 605 HOH C 624
SITE 1 AE5 5 TRP D 57 TYR D 58 SER D 142 MET D 143
SITE 2 AE5 5 GOL D 406
SITE 1 AE6 4 GLY D 60 THR D 61 THR D 64 HOH D 666
SITE 1 AE7 6 HIS D 74 HOH D 549 HOH D 605 HOH D 678
SITE 2 AE7 6 HOH D 684 HOH D 911
SITE 1 AE8 5 VAL D 11 GLN D 63 HOH D 810 HOH D 823
SITE 2 AE8 5 HOH D 973
SITE 1 AE9 7 PRO C 173 LEU C 234 GLU C 235 SER C 239
SITE 2 AE9 7 LYS D 225 GLU D 227 HOH D 676
SITE 1 AF1 9 TRP D 57 TYR D 58 SER D 59 SER D 142
SITE 2 AF1 9 TRP D 214 HIS D 325 LEU D 326 PHE D 329
SITE 3 AF1 9 CL D 401
SITE 1 AF2 6 PRO D 97 MET D 107 PHE D 110 ASN D 255
SITE 2 AF2 6 ASN D 259 HOH D 631
SITE 1 AF3 8 LEU C 2 ASN C 4 TYR C 7 GLY C 92
SITE 2 AF3 8 ALA C 98 ASN C 99 ASP C 253 HOH D 511
CRYST1 44.141 89.612 322.788 90.00 90.00 90.00 P 21 21 21 16
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 0.022655 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011159 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003098 0.00000
TER 2743 SER A 349
TER 5486 SER B 349
TER 8229 SER C 349
TER 10972 SER D 349
MASTER 1106 0 30 82 40 0 57 613572 4 134 108
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