HEADER MEMBRANE PROTEIN 03-FEB-11 3QLU
TITLE CRYSTAL STRUCTURE OF THE GLUK2/GLUK5 (GLUR6/KA2) ATD DIMER ASSEMBLY
CAVEAT 3QLU NAG C 398 HAS WRONG CHIRALITY AT ATOM C1 NAG D 397 HAS WRONG
CAVEAT 2 3QLU CHIRALITY AT ATOM C1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUTAMATE RECEPTOR, IONOTROPIC KAINATE 5;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: GLUTAMATE RECEPTOR KA-2, KA2;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: GLUTAMATE RECEPTOR, IONOTROPIC KAINATE 2;
COMPND 8 CHAIN: C, D;
COMPND 9 SYNONYM: GLUTAMATE RECEPTOR 6, GLUR-6, GLUR6;
COMPND 10 ENGINEERED: YES;
COMPND 11 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: BROWN RAT,RAT,RATS;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 GENE: GRIK5;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: HEK 293 GNTI(-);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PRK-IRES_EGFP;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 13 ORGANISM_COMMON: BROWN RAT,RAT,RATS;
SOURCE 14 ORGANISM_TAXID: 10116;
SOURCE 15 GENE: GLUR6, GRIK2;
SOURCE 16 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 18 EXPRESSION_SYSTEM_CELL_LINE: HEK 293 GNTI(-);
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PRK-IRES_EGFP
KEYWDS MEMBRANE PROTEIN, GLYCOSYLATION
EXPDTA X-RAY DIFFRACTION
AUTHOR J.KUMAR,M.L.MAYER
REVDAT 5 13-SEP-23 3QLU 1 REMARK
REVDAT 4 31-MAR-21 3QLU 1 SOURCE HETSYN
REVDAT 3 29-JUL-20 3QLU 1 CAVEAT COMPND REMARK SEQADV
REVDAT 3 2 1 HETNAM LINK SITE
REVDAT 2 10-OCT-12 3QLU 1 JRNL
REVDAT 1 03-AUG-11 3QLU 0
JRNL AUTH J.KUMAR,P.SCHUCK,M.L.MAYER
JRNL TITL STRUCTURE AND ASSEMBLY MECHANISM FOR HETEROMERIC KAINATE
JRNL TITL 2 RECEPTORS.
JRNL REF NEURON V. 71 319 2011
JRNL REFN ISSN 0896-6273
JRNL PMID 21791290
JRNL DOI 10.1016/J.NEURON.2011.05.038
REMARK 2
REMARK 2 RESOLUTION. 2.91 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.6.1_357)
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 : MLHL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.91
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.97
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 3 NUMBER OF REFLECTIONS : 39761
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.200
REMARK 3 R VALUE (WORKING SET) : 0.197
REMARK 3 FREE R VALUE : 0.256
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 1991
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 29.9712 - 6.9774 1.00 2919 158 0.1929 0.2139
REMARK 3 2 6.9774 - 5.5497 1.00 2796 153 0.1937 0.2642
REMARK 3 3 5.5497 - 4.8515 1.00 2767 163 0.1541 0.2042
REMARK 3 4 4.8515 - 4.4095 1.00 2729 147 0.1327 0.2123
REMARK 3 5 4.4095 - 4.0943 1.00 2723 142 0.1510 0.2136
REMARK 3 6 4.0943 - 3.8534 1.00 2707 158 0.1633 0.2191
REMARK 3 7 3.8534 - 3.6608 1.00 2715 137 0.1775 0.2328
REMARK 3 8 3.6608 - 3.5017 1.00 2703 133 0.1957 0.2876
REMARK 3 9 3.5017 - 3.3670 0.99 2735 128 0.2022 0.2641
REMARK 3 10 3.3670 - 3.2510 0.99 2679 131 0.2114 0.2825
REMARK 3 11 3.2510 - 3.1495 0.98 2647 136 0.2347 0.2809
REMARK 3 12 3.1495 - 3.0595 0.98 2665 144 0.2470 0.3754
REMARK 3 13 3.0595 - 2.9790 0.97 2593 133 0.2614 0.3451
REMARK 3 14 2.9790 - 2.9064 0.89 2392 128 0.2675 0.3536
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.00
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : 0.36
REMARK 3 B_SOL : 13.21
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.360
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 41.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.91310
REMARK 3 B22 (A**2) : 6.02280
REMARK 3 B33 (A**2) : -4.10970
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.006 12268
REMARK 3 ANGLE : 0.918 16626
REMARK 3 CHIRALITY : 0.049 1926
REMARK 3 PLANARITY : 0.004 2094
REMARK 3 DIHEDRAL : 13.787 4549
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 14
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN A AND RESID 3:53)
REMARK 3 ORIGIN FOR THE GROUP (A): 14.6146 7.7746 26.3172
REMARK 3 T TENSOR
REMARK 3 T11: 0.0646 T22: 0.1718
REMARK 3 T33: 0.1448 T12: -0.0358
REMARK 3 T13: -0.0437 T23: 0.0763
REMARK 3 L TENSOR
REMARK 3 L11: 1.3427 L22: 0.4190
REMARK 3 L33: 1.0259 L12: -0.2687
REMARK 3 L13: -0.0713 L23: -0.5616
REMARK 3 S TENSOR
REMARK 3 S11: -0.0102 S12: 0.2949 S13: -0.3545
REMARK 3 S21: 0.0015 S22: -0.2837 S23: -0.2982
REMARK 3 S31: -0.0785 S32: 0.2080 S33: 0.1900
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN A AND RESID 54:120)
REMARK 3 ORIGIN FOR THE GROUP (A): 0.4522 3.0400 17.6521
REMARK 3 T TENSOR
REMARK 3 T11: 0.0186 T22: 0.0083
REMARK 3 T33: 0.1239 T12: -0.0391
REMARK 3 T13: 0.0095 T23: 0.0008
REMARK 3 L TENSOR
REMARK 3 L11: 2.1099 L22: 0.7285
REMARK 3 L33: 1.0166 L12: 0.2775
REMARK 3 L13: 0.1893 L23: 0.2143
REMARK 3 S TENSOR
REMARK 3 S11: -0.3884 S12: 0.1016 S13: -0.2232
REMARK 3 S21: 0.0231 S22: 0.1887 S23: 0.0356
REMARK 3 S31: -0.1307 S32: 0.3205 S33: 0.1266
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN A AND RESID 121:247) OR (CHAIN G AND RESID 1)
REMARK 3 ORIGIN FOR THE GROUP (A): 4.6626 25.3132 -3.5580
REMARK 3 T TENSOR
REMARK 3 T11: 0.0996 T22: 0.0353
REMARK 3 T33: 0.1340 T12: -0.0246
REMARK 3 T13: -0.0075 T23: 0.0478
REMARK 3 L TENSOR
REMARK 3 L11: 1.0429 L22: 0.8870
REMARK 3 L33: 2.1125 L12: 1.0159
REMARK 3 L13: 0.3549 L23: -0.2445
REMARK 3 S TENSOR
REMARK 3 S11: -0.0117 S12: -0.0424 S13: -0.3178
REMARK 3 S21: 0.0943 S22: 0.0373 S23: -0.2775
REMARK 3 S31: -0.3143 S32: -0.1191 S33: -0.0348
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN A AND RESID 248:375) OR (CHAIN G AND RESID
REMARK 3 2:5)
REMARK 3 ORIGIN FOR THE GROUP (A): 7.5248 18.3010 22.6754
REMARK 3 T TENSOR
REMARK 3 T11: 0.0642 T22: 0.0331
REMARK 3 T33: 0.0638 T12: -0.0345
REMARK 3 T13: -0.0494 T23: 0.0075
REMARK 3 L TENSOR
REMARK 3 L11: 0.7483 L22: 0.9644
REMARK 3 L33: 1.0980 L12: -0.6065
REMARK 3 L13: 0.2134 L23: -0.8575
REMARK 3 S TENSOR
REMARK 3 S11: -0.0067 S12: 0.0291 S13: 0.2386
REMARK 3 S21: 0.1497 S22: -0.1236 S23: 0.2383
REMARK 3 S31: -0.2486 S32: 0.1435 S33: 0.0155
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: (CHAIN B AND RESID 3:105)
REMARK 3 ORIGIN FOR THE GROUP (A): 33.7478 -2.7532 29.9242
REMARK 3 T TENSOR
REMARK 3 T11: 0.0510 T22: 0.0908
REMARK 3 T33: 0.1221 T12: -0.0075
REMARK 3 T13: -0.0467 T23: 0.0044
REMARK 3 L TENSOR
REMARK 3 L11: 0.8267 L22: 0.6310
REMARK 3 L33: 1.0826 L12: 0.3099
REMARK 3 L13: 0.5295 L23: 0.2583
REMARK 3 S TENSOR
REMARK 3 S11: -0.1320 S12: 0.0216 S13: -0.0673
REMARK 3 S21: -0.0581 S22: 0.1518 S23: -0.0845
REMARK 3 S31: -0.0149 S32: -0.0886 S33: -0.1336
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: (CHAIN B AND RESID 110:153)
REMARK 3 ORIGIN FOR THE GROUP (A): 45.2972 -11.7328 51.2242
REMARK 3 T TENSOR
REMARK 3 T11: 0.0730 T22: 0.1170
REMARK 3 T33: 0.0866 T12: 0.0286
REMARK 3 T13: 0.0279 T23: -0.0225
REMARK 3 L TENSOR
REMARK 3 L11: 0.7022 L22: 0.2978
REMARK 3 L33: 1.3607 L12: 0.0256
REMARK 3 L13: -0.6173 L23: 0.0036
REMARK 3 S TENSOR
REMARK 3 S11: -0.0418 S12: 0.0448 S13: -0.0228
REMARK 3 S21: 0.1149 S22: 0.0905 S23: 0.0640
REMARK 3 S31: 0.0850 S32: -0.2401 S33: -0.0647
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: (CHAIN B AND RESID 154:231) OR (CHAIN H AND RESID 1)
REMARK 3 ORIGIN FOR THE GROUP (A): 36.7708 -23.2158 57.9400
REMARK 3 T TENSOR
REMARK 3 T11: 0.2000 T22: 0.2574
REMARK 3 T33: 0.0593 T12: -0.0976
REMARK 3 T13: 0.0299 T23: 0.0077
REMARK 3 L TENSOR
REMARK 3 L11: 2.1162 L22: 1.4071
REMARK 3 L33: 0.5506 L12: -0.0783
REMARK 3 L13: -1.2511 L23: 0.5360
REMARK 3 S TENSOR
REMARK 3 S11: 0.0741 S12: 0.2978 S13: 0.0228
REMARK 3 S21: 0.4190 S22: -0.2089 S23: 0.2283
REMARK 3 S31: 0.1938 S32: -0.3477 S33: 0.1218
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: (CHAIN B AND RESID 232:382) OR (CHAIN H AND RESID
REMARK 3 2:6)
REMARK 3 ORIGIN FOR THE GROUP (A): 33.4743 0.2916 45.6937
REMARK 3 T TENSOR
REMARK 3 T11: 0.0214 T22: 0.1183
REMARK 3 T33: 0.1163 T12: 0.0306
REMARK 3 T13: 0.0457 T23: -0.0573
REMARK 3 L TENSOR
REMARK 3 L11: 0.3714 L22: 0.8195
REMARK 3 L33: 0.8242 L12: -0.0880
REMARK 3 L13: 0.9294 L23: -0.2846
REMARK 3 S TENSOR
REMARK 3 S11: -0.0521 S12: -0.3904 S13: -0.0904
REMARK 3 S21: 0.1985 S22: -0.0058 S23: 0.0326
REMARK 3 S31: -0.2660 S32: -0.1799 S33: 0.0284
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: (CHAIN C AND RESID 2:119) OR (CHAIN I AND RESID 1)
REMARK 3 OR (CHAIN E)
REMARK 3 ORIGIN FOR THE GROUP (A): -8.1159 -14.0300 0.7416
REMARK 3 T TENSOR
REMARK 3 T11: 0.3377 T22: 0.0489
REMARK 3 T33: 0.0446 T12: -0.0591
REMARK 3 T13: 0.0636 T23: -0.0126
REMARK 3 L TENSOR
REMARK 3 L11: 1.4025 L22: 0.5439
REMARK 3 L33: 0.9359 L12: 0.2533
REMARK 3 L13: 0.4123 L23: -0.4427
REMARK 3 S TENSOR
REMARK 3 S11: -0.2674 S12: -0.2096 S13: 0.1444
REMARK 3 S21: -0.2792 S22: 0.0928 S23: -0.0739
REMARK 3 S31: 0.2982 S32: -0.1455 S33: 0.1127
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: (CHAIN C AND RESID 120:267)
REMARK 3 ORIGIN FOR THE GROUP (A): -21.9564 9.9418 -10.3106
REMARK 3 T TENSOR
REMARK 3 T11: 0.0275 T22: 0.1100
REMARK 3 T33: 0.0937 T12: -0.0420
REMARK 3 T13: 0.0075 T23: 0.0340
REMARK 3 L TENSOR
REMARK 3 L11: 0.4406 L22: 0.9679
REMARK 3 L33: 0.4505 L12: 0.1550
REMARK 3 L13: 0.0720 L23: 0.0958
REMARK 3 S TENSOR
REMARK 3 S11: 0.1104 S12: 0.1345 S13: -0.1457
REMARK 3 S21: 0.0852 S22: -0.0476 S23: 0.0474
REMARK 3 S31: 0.0303 S32: -0.2118 S33: -0.0267
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: (CHAIN C AND RESID 278:383) OR (CHAIN I AND RESID
REMARK 3 3:4)
REMARK 3 ORIGIN FOR THE GROUP (A): -8.7723 -9.5818 -12.0899
REMARK 3 T TENSOR
REMARK 3 T11: 0.2498 T22: 0.1251
REMARK 3 T33: 0.0112 T12: -0.1173
REMARK 3 T13: 0.0120 T23: -0.0548
REMARK 3 L TENSOR
REMARK 3 L11: 0.5850 L22: 0.0197
REMARK 3 L33: 0.6237 L12: -0.1075
REMARK 3 L13: 0.3353 L23: -0.9550
REMARK 3 S TENSOR
REMARK 3 S11: -0.0102 S12: 0.3917 S13: -0.3473
REMARK 3 S21: -0.4632 S22: -0.1672 S23: 0.4282
REMARK 3 S31: 0.3979 S32: 0.3165 S33: -0.0131
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: (CHAIN D AND RESID 2:120) OR (CHAIN J AND RESID 1)
REMARK 3 OR (CHAIN F)
REMARK 3 ORIGIN FOR THE GROUP (A): 52.5705 -28.3190 20.8831
REMARK 3 T TENSOR
REMARK 3 T11: 0.2776 T22: 0.0001
REMARK 3 T33: 0.1083 T12: -0.0368
REMARK 3 T13: 0.1042 T23: -0.0091
REMARK 3 L TENSOR
REMARK 3 L11: 0.7185 L22: 1.3182
REMARK 3 L33: 0.1852 L12: -0.8693
REMARK 3 L13: 0.4735 L23: -0.1171
REMARK 3 S TENSOR
REMARK 3 S11: -0.0890 S12: -0.0262 S13: 0.2020
REMARK 3 S21: -0.1145 S22: 0.0231 S23: -0.2911
REMARK 3 S31: 0.2206 S32: 0.0930 S33: 0.0555
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: (CHAIN D AND RESID 121:268) OR (CHAIN J AND RESID 2)
REMARK 3 ORIGIN FOR THE GROUP (A): 65.4942 -29.8096 47.6003
REMARK 3 T TENSOR
REMARK 3 T11: 0.1380 T22: 0.1517
REMARK 3 T33: 0.1163 T12: 0.0489
REMARK 3 T13: 0.0126 T23: 0.0564
REMARK 3 L TENSOR
REMARK 3 L11: 0.6629 L22: 0.2562
REMARK 3 L33: 0.2216 L12: -0.3905
REMARK 3 L13: -0.1465 L23: 0.4119
REMARK 3 S TENSOR
REMARK 3 S11: 0.0184 S12: -0.1355 S13: -0.1894
REMARK 3 S21: 0.0846 S22: -0.1713 S23: -0.0854
REMARK 3 S31: 0.1063 S32: 0.0124 S33: 0.0758
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: (CHAIN D AND RESID 279:383) OR (CHAIN J AND RESID 3)
REMARK 3 ORIGIN FOR THE GROUP (A): 53.4008 -38.8614 28.9885
REMARK 3 T TENSOR
REMARK 3 T11: 0.3635 T22: 0.0192
REMARK 3 T33: 0.3085 T12: 0.0159
REMARK 3 T13: 0.1166 T23: 0.0167
REMARK 3 L TENSOR
REMARK 3 L11: 0.6464 L22: 0.3188
REMARK 3 L33: 0.7814 L12: -0.1418
REMARK 3 L13: 0.2622 L23: 0.2647
REMARK 3 S TENSOR
REMARK 3 S11: -0.1386 S12: -0.1286 S13: -0.4545
REMARK 3 S21: 0.0818 S22: 0.1317 S23: 0.0543
REMARK 3 S31: 0.6896 S32: 0.1189 S33: 0.0405
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 2
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN C AND (RESSEQ 10:104 OR RESSEQ
REMARK 3 114:174 OR RESSEQ 181:266 OR RESSEQ 279:
REMARK 3 305 OR RESSEQ 324:383 ) AND (NOT ELEMENT
REMARK 3 H)
REMARK 3 SELECTION : CHAIN D AND (RESSEQ 10:104 OR RESSEQ
REMARK 3 114:174 OR RESSEQ 181:266 OR RESSEQ 279:
REMARK 3 305 OR RESSEQ 324:383 ) AND (NOT ELEMENT
REMARK 3 H)
REMARK 3 ATOM PAIRS NUMBER : 2616
REMARK 3 RMSD : 0.028
REMARK 3 NCS GROUP : 2
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 2:10 OR RESSEQ 22:37
REMARK 3 OR RESSEQ 40:98 OR RESSEQ 118:172 OR
REMARK 3 RESSEQ 179:270 OR RESSEQ 278:356 ) AND
REMARK 3 (NOT ELEMENT H)
REMARK 3 SELECTION : CHAIN B AND (RESSEQ 2:10 OR RESSEQ 22:37
REMARK 3 OR RESSEQ 40:98 OR RESSEQ 118:172 OR
REMARK 3 RESSEQ 179:270 OR RESSEQ 278:356 ) AND
REMARK 3 (NOT ELEMENT H)
REMARK 3 ATOM PAIRS NUMBER : 2376
REMARK 3 RMSD : 0.043
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3QLU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-MAR-11.
REMARK 100 THE DEPOSITION ID IS D_1000063807.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-NOV-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.20
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 23-ID-B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.03320
REMARK 200 MONOCHROMATOR : SI(111) DOUBLE CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 40232
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 200 DATA REDUNDANCY : 4.100
REMARK 200 R MERGE (I) : 0.11400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.1
REMARK 200 DATA REDUNDANCY IN SHELL : 3.90
REMARK 200 R MERGE FOR SHELL (I) : 0.45000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 3OM0 AND 3H6H
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.27
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.52
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.15 M AMMONIUM SULFATE; 0.1 M TRIS;
REMARK 280 18% PEG 4K, PH 8.20, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 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 32.81300
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 97.70500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 69.77400
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 97.70500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 32.81300
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 69.77400
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: 5340 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 32250 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -4.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C
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: 5170 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 33000 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 8.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 VAL A 1
REMARK 465 ASP A 176
REMARK 465 SER A 177
REMARK 465 ARG A 376
REMARK 465 THR A 377
REMARK 465 LEU A 378
REMARK 465 ALA A 379
REMARK 465 MET A 380
REMARK 465 ASN A 381
REMARK 465 ALA A 382
REMARK 465 THR A 383
REMARK 465 THR A 384
REMARK 465 LEU A 385
REMARK 465 ASP A 386
REMARK 465 ILE A 387
REMARK 465 LEU A 388
REMARK 465 GLU A 389
REMARK 465 LEU A 390
REMARK 465 VAL A 391
REMARK 465 PRO A 392
REMARK 465 ARG A 393
REMARK 465 VAL B 1
REMARK 465 THR B 383
REMARK 465 THR B 384
REMARK 465 LEU B 385
REMARK 465 ASP B 386
REMARK 465 ILE B 387
REMARK 465 LEU B 388
REMARK 465 GLU B 389
REMARK 465 LEU B 390
REMARK 465 VAL B 391
REMARK 465 PRO B 392
REMARK 465 ARG B 393
REMARK 465 THR C 1
REMARK 465 GLU C 268
REMARK 465 ARG C 269
REMARK 465 LEU C 270
REMARK 465 GLN C 271
REMARK 465 ALA C 272
REMARK 465 PRO C 273
REMARK 465 PRO C 274
REMARK 465 LYS C 275
REMARK 465 PRO C 276
REMARK 465 ASP C 277
REMARK 465 GLU C 384
REMARK 465 SER C 385
REMARK 465 GLN C 386
REMARK 465 LYS C 387
REMARK 465 GLY C 388
REMARK 465 LYS C 389
REMARK 465 LEU C 390
REMARK 465 GLU C 391
REMARK 465 LEU C 392
REMARK 465 VAL C 393
REMARK 465 PRO C 394
REMARK 465 ARG C 395
REMARK 465 THR D 1
REMARK 465 ARG D 269
REMARK 465 LEU D 270
REMARK 465 GLN D 271
REMARK 465 ALA D 272
REMARK 465 PRO D 273
REMARK 465 PRO D 274
REMARK 465 LYS D 275
REMARK 465 PRO D 276
REMARK 465 ASP D 277
REMARK 465 GLU D 384
REMARK 465 SER D 385
REMARK 465 GLN D 386
REMARK 465 LYS D 387
REMARK 465 GLY D 388
REMARK 465 LYS D 389
REMARK 465 LEU D 390
REMARK 465 GLU D 391
REMARK 465 LEU D 392
REMARK 465 VAL D 393
REMARK 465 PRO D 394
REMARK 465 ARG D 395
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 LEU A 2 CG CD1 CD2
REMARK 470 SER A 3 OG
REMARK 470 VAL A 38 CG1 CG2
REMARK 470 GLN A 110 CG CD OE1 NE2
REMARK 470 ARG A 178 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 263 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 271 CG CD OE1 OE2
REMARK 470 SER B 3 OG
REMARK 470 ARG B 108 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 178 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 263 CG CD NE CZ NH1 NH2
REMARK 470 GLN B 364 CG CD OE1 NE2
REMARK 470 THR C 2 OG1 CG2
REMARK 470 ASP C 176 CG OD1 OD2
REMARK 470 LYS C 178 CG CD CE NZ
REMARK 470 MET C 267 CG SD CE
REMARK 470 GLU C 366 CG CD OE1 OE2
REMARK 470 LYS D 181 CG CD CE NZ
REMARK 470 GLU D 268 CG CD OE1 OE2
REMARK 470 SER D 278 OG
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 GLU A 45 CA CB CG CD OE1 OE2
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 ND2 ASN C 347 C2 NAG C 397 2.03
REMARK 500 ND2 ASN B 266 C2 NAG B 396 2.17
REMARK 500 ND2 ASN D 347 C2 NAG D 398 2.18
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 THR B 277 O7 NAG D 397 1455 2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 270 NE - CZ - NH1 ANGL. DEV. = -6.5 DEGREES
REMARK 500 ARG A 270 NE - CZ - NH2 ANGL. DEV. = 6.3 DEGREES
REMARK 500 ARG B 270 NE - CZ - NH1 ANGL. DEV. = 6.0 DEGREES
REMARK 500 ARG B 270 NE - CZ - NH2 ANGL. DEV. = -6.0 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 TYR A 111 36.71 -96.47
REMARK 500 THR A 168 -73.47 -115.50
REMARK 500 SER A 218 -159.57 -79.16
REMARK 500 ASP A 229 45.92 -98.35
REMARK 500 ILE A 238 -46.65 -132.61
REMARK 500 ASN A 272 -34.93 -132.30
REMARK 500 ARG B 108 176.67 -54.60
REMARK 500 THR B 168 -75.35 -115.13
REMARK 500 ASP B 176 -9.36 79.73
REMARK 500 SER B 218 -160.18 -77.71
REMARK 500 ASP B 229 46.15 -97.38
REMARK 500 ILE B 238 -47.72 -132.46
REMARK 500 ALA B 379 123.42 -178.43
REMARK 500 LEU C 40 74.37 45.42
REMARK 500 TYR C 55 3.70 82.78
REMARK 500 ASP C 121 134.21 -38.35
REMARK 500 MET C 217 76.25 -107.69
REMARK 500 PHE C 306 63.01 -150.39
REMARK 500 ARG C 318 -59.39 -148.30
REMARK 500 ILE C 371 18.19 -145.77
REMARK 500 LEU D 40 73.96 45.95
REMARK 500 TYR D 55 2.86 83.52
REMARK 500 MET D 217 75.97 -106.62
REMARK 500 MET D 267 46.31 -155.74
REMARK 500 ARG D 318 -45.00 -150.36
REMARK 500 ASN D 350 6.42 -150.02
REMARK 500 ILE D 371 19.72 -145.47
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3GLV RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE GLUK2/GLUK5 (GLUR6/KA2) ATD TETRAMER
REMARK 900 ASSEMBLY
REMARK 900 RELATED ID: 3QLT RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF A GLUK2 (GLUR6) GLYCAN WEDGE HOMODIMER ASSEMBLY
REMARK 900 RELATED ID: 3OM0 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE GLUK5 (KA2) ATD
REMARK 900 RELATED ID: 3H6G RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE GLUK2 (GLUR6) ATD
REMARK 900 RELATED ID: 3OLZ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE GLUK3 (GLUR7) ATD
DBREF 3QLU A 1 387 UNP Q63273 GRIK5_RAT 20 406
DBREF 3QLU B 1 387 UNP Q63273 GRIK5_RAT 20 406
DBREF 3QLU C 1 389 UNP P42260 GRIK2_RAT 32 420
DBREF 3QLU D 1 389 UNP P42260 GRIK2_RAT 32 420
SEQADV 3QLU LEU A 388 UNP Q63273 EXPRESSION TAG
SEQADV 3QLU GLU A 389 UNP Q63273 EXPRESSION TAG
SEQADV 3QLU LEU A 390 UNP Q63273 EXPRESSION TAG
SEQADV 3QLU VAL A 391 UNP Q63273 EXPRESSION TAG
SEQADV 3QLU PRO A 392 UNP Q63273 EXPRESSION TAG
SEQADV 3QLU ARG A 393 UNP Q63273 EXPRESSION TAG
SEQADV 3QLU LEU B 388 UNP Q63273 EXPRESSION TAG
SEQADV 3QLU GLU B 389 UNP Q63273 EXPRESSION TAG
SEQADV 3QLU LEU B 390 UNP Q63273 EXPRESSION TAG
SEQADV 3QLU VAL B 391 UNP Q63273 EXPRESSION TAG
SEQADV 3QLU PRO B 392 UNP Q63273 EXPRESSION TAG
SEQADV 3QLU ARG B 393 UNP Q63273 EXPRESSION TAG
SEQADV 3QLU ASN C 213 UNP P42260 ALA 244 ENGINEERED MUTATION
SEQADV 3QLU SER C 215 UNP P42260 GLY 246 ENGINEERED MUTATION
SEQADV 3QLU LEU C 390 UNP P42260 EXPRESSION TAG
SEQADV 3QLU GLU C 391 UNP P42260 EXPRESSION TAG
SEQADV 3QLU LEU C 392 UNP P42260 EXPRESSION TAG
SEQADV 3QLU VAL C 393 UNP P42260 EXPRESSION TAG
SEQADV 3QLU PRO C 394 UNP P42260 EXPRESSION TAG
SEQADV 3QLU ARG C 395 UNP P42260 EXPRESSION TAG
SEQADV 3QLU ASN D 213 UNP P42260 ALA 244 ENGINEERED MUTATION
SEQADV 3QLU SER D 215 UNP P42260 GLY 246 ENGINEERED MUTATION
SEQADV 3QLU LEU D 390 UNP P42260 EXPRESSION TAG
SEQADV 3QLU GLU D 391 UNP P42260 EXPRESSION TAG
SEQADV 3QLU LEU D 392 UNP P42260 EXPRESSION TAG
SEQADV 3QLU VAL D 393 UNP P42260 EXPRESSION TAG
SEQADV 3QLU PRO D 394 UNP P42260 EXPRESSION TAG
SEQADV 3QLU ARG D 395 UNP P42260 EXPRESSION TAG
SEQRES 1 A 393 VAL LEU SER SER LEU ARG MET ALA ALA ILE LEU ASP ASP
SEQRES 2 A 393 GLN THR VAL CYS GLY ARG GLY GLU ARG LEU ALA LEU ALA
SEQRES 3 A 393 LEU ALA ARG GLU GLN ILE ASN GLY ILE ILE GLU VAL PRO
SEQRES 4 A 393 ALA LYS ALA ARG VAL GLU VAL ASP ILE PHE GLU LEU GLN
SEQRES 5 A 393 ARG ASP SER GLN TYR GLU THR THR ASP THR MET CYS GLN
SEQRES 6 A 393 ILE LEU PRO LYS GLY VAL VAL SER VAL LEU GLY PRO SER
SEQRES 7 A 393 SER SER PRO ALA SER ALA SER THR VAL SER HIS ILE CYS
SEQRES 8 A 393 GLY GLU LYS GLU ILE PRO HIS ILE LYS VAL GLY PRO GLU
SEQRES 9 A 393 GLU THR PRO ARG LEU GLN TYR LEU ARG PHE ALA SER VAL
SEQRES 10 A 393 SER LEU TYR PRO SER ASN GLU ASP VAL SER LEU ALA VAL
SEQRES 11 A 393 SER ARG ILE LEU LYS SER PHE ASN TYR PRO SER ALA SER
SEQRES 12 A 393 LEU ILE CYS ALA LYS ALA GLU CYS LEU LEU ARG LEU GLU
SEQRES 13 A 393 GLU LEU VAL ARG GLY PHE LEU ILE SER LYS GLU THR LEU
SEQRES 14 A 393 SER VAL ARG MET LEU ASP ASP SER ARG ASP PRO THR PRO
SEQRES 15 A 393 LEU LEU LYS GLU ILE ARG ASP ASP LYS VAL SER THR ILE
SEQRES 16 A 393 ILE ILE ASP ALA ASN ALA SER ILE SER HIS LEU VAL LEU
SEQRES 17 A 393 ARG LYS ALA SER GLU LEU GLY MET THR SER ALA PHE TYR
SEQRES 18 A 393 LYS TYR ILE LEU THR THR MET ASP PHE PRO ILE LEU HIS
SEQRES 19 A 393 LEU ASP GLY ILE VAL GLU ASP SER SER ASN ILE LEU GLY
SEQRES 20 A 393 PHE SER MET PHE ASN THR SER HIS PRO PHE TYR PRO GLU
SEQRES 21 A 393 PHE VAL ARG SER LEU ASN MET SER TRP ARG GLU ASN CYS
SEQRES 22 A 393 GLU ALA SER THR TYR PRO GLY PRO ALA LEU SER ALA ALA
SEQRES 23 A 393 LEU MET PHE ASP ALA VAL HIS VAL VAL VAL SER ALA VAL
SEQRES 24 A 393 ARG GLU LEU ASN ARG SER GLN GLU ILE GLY VAL LYS PRO
SEQRES 25 A 393 LEU ALA CYS THR SER ALA ASN ILE TRP PRO HIS GLY THR
SEQRES 26 A 393 SER LEU MET ASN TYR LEU ARG MET VAL GLU TYR ASP GLY
SEQRES 27 A 393 LEU THR GLY ARG VAL GLU PHE ASN SER LYS GLY GLN ARG
SEQRES 28 A 393 THR ASN TYR THR LEU ARG ILE LEU GLU LYS SER ARG GLN
SEQRES 29 A 393 GLY HIS ARG GLU ILE GLY VAL TRP TYR SER ASN ARG THR
SEQRES 30 A 393 LEU ALA MET ASN ALA THR THR LEU ASP ILE LEU GLU LEU
SEQRES 31 A 393 VAL PRO ARG
SEQRES 1 B 393 VAL LEU SER SER LEU ARG MET ALA ALA ILE LEU ASP ASP
SEQRES 2 B 393 GLN THR VAL CYS GLY ARG GLY GLU ARG LEU ALA LEU ALA
SEQRES 3 B 393 LEU ALA ARG GLU GLN ILE ASN GLY ILE ILE GLU VAL PRO
SEQRES 4 B 393 ALA LYS ALA ARG VAL GLU VAL ASP ILE PHE GLU LEU GLN
SEQRES 5 B 393 ARG ASP SER GLN TYR GLU THR THR ASP THR MET CYS GLN
SEQRES 6 B 393 ILE LEU PRO LYS GLY VAL VAL SER VAL LEU GLY PRO SER
SEQRES 7 B 393 SER SER PRO ALA SER ALA SER THR VAL SER HIS ILE CYS
SEQRES 8 B 393 GLY GLU LYS GLU ILE PRO HIS ILE LYS VAL GLY PRO GLU
SEQRES 9 B 393 GLU THR PRO ARG LEU GLN TYR LEU ARG PHE ALA SER VAL
SEQRES 10 B 393 SER LEU TYR PRO SER ASN GLU ASP VAL SER LEU ALA VAL
SEQRES 11 B 393 SER ARG ILE LEU LYS SER PHE ASN TYR PRO SER ALA SER
SEQRES 12 B 393 LEU ILE CYS ALA LYS ALA GLU CYS LEU LEU ARG LEU GLU
SEQRES 13 B 393 GLU LEU VAL ARG GLY PHE LEU ILE SER LYS GLU THR LEU
SEQRES 14 B 393 SER VAL ARG MET LEU ASP ASP SER ARG ASP PRO THR PRO
SEQRES 15 B 393 LEU LEU LYS GLU ILE ARG ASP ASP LYS VAL SER THR ILE
SEQRES 16 B 393 ILE ILE ASP ALA ASN ALA SER ILE SER HIS LEU VAL LEU
SEQRES 17 B 393 ARG LYS ALA SER GLU LEU GLY MET THR SER ALA PHE TYR
SEQRES 18 B 393 LYS TYR ILE LEU THR THR MET ASP PHE PRO ILE LEU HIS
SEQRES 19 B 393 LEU ASP GLY ILE VAL GLU ASP SER SER ASN ILE LEU GLY
SEQRES 20 B 393 PHE SER MET PHE ASN THR SER HIS PRO PHE TYR PRO GLU
SEQRES 21 B 393 PHE VAL ARG SER LEU ASN MET SER TRP ARG GLU ASN CYS
SEQRES 22 B 393 GLU ALA SER THR TYR PRO GLY PRO ALA LEU SER ALA ALA
SEQRES 23 B 393 LEU MET PHE ASP ALA VAL HIS VAL VAL VAL SER ALA VAL
SEQRES 24 B 393 ARG GLU LEU ASN ARG SER GLN GLU ILE GLY VAL LYS PRO
SEQRES 25 B 393 LEU ALA CYS THR SER ALA ASN ILE TRP PRO HIS GLY THR
SEQRES 26 B 393 SER LEU MET ASN TYR LEU ARG MET VAL GLU TYR ASP GLY
SEQRES 27 B 393 LEU THR GLY ARG VAL GLU PHE ASN SER LYS GLY GLN ARG
SEQRES 28 B 393 THR ASN TYR THR LEU ARG ILE LEU GLU LYS SER ARG GLN
SEQRES 29 B 393 GLY HIS ARG GLU ILE GLY VAL TRP TYR SER ASN ARG THR
SEQRES 30 B 393 LEU ALA MET ASN ALA THR THR LEU ASP ILE LEU GLU LEU
SEQRES 31 B 393 VAL PRO ARG
SEQRES 1 C 395 THR THR HIS VAL LEU ARG PHE GLY GLY ILE PHE GLU TYR
SEQRES 2 C 395 VAL GLU SER GLY PRO MET GLY ALA GLU GLU LEU ALA PHE
SEQRES 3 C 395 ARG PHE ALA VAL ASN THR ILE ASN ARG ASN ARG THR LEU
SEQRES 4 C 395 LEU PRO ASN THR THR LEU THR TYR ASP THR GLN LYS ILE
SEQRES 5 C 395 ASN LEU TYR ASP SER PHE GLU ALA SER LYS LYS ALA CYS
SEQRES 6 C 395 ASP GLN LEU SER LEU GLY VAL ALA ALA ILE PHE GLY PRO
SEQRES 7 C 395 SER HIS SER SER SER ALA ASN ALA VAL GLN SER ILE CYS
SEQRES 8 C 395 ASN ALA LEU GLY VAL PRO HIS ILE GLN THR ARG TRP LYS
SEQRES 9 C 395 HIS GLN VAL SER ASP ASN LYS ASP SER PHE TYR VAL SER
SEQRES 10 C 395 LEU TYR PRO ASP PHE SER SER LEU SER ARG ALA ILE LEU
SEQRES 11 C 395 ASP LEU VAL GLN PHE PHE LYS TRP LYS THR VAL THR VAL
SEQRES 12 C 395 VAL TYR ASP ASP SER THR GLY LEU ILE ARG LEU GLN GLU
SEQRES 13 C 395 LEU ILE LYS ALA PRO SER ARG TYR ASN LEU ARG LEU LYS
SEQRES 14 C 395 ILE ARG GLN LEU PRO ALA ASP THR LYS ASP ALA LYS PRO
SEQRES 15 C 395 LEU LEU LYS GLU MET LYS ARG GLY LYS GLU PHE HIS VAL
SEQRES 16 C 395 ILE PHE ASP CYS SER HIS GLU MET ALA ALA GLY ILE LEU
SEQRES 17 C 395 LYS GLN ALA LEU ASN MET SER MET MET THR GLU TYR TYR
SEQRES 18 C 395 HIS TYR ILE PHE THR THR LEU ASP LEU PHE ALA LEU ASP
SEQRES 19 C 395 VAL GLU PRO TYR ARG TYR SER GLY VAL ASN MET THR GLY
SEQRES 20 C 395 PHE ARG ILE LEU ASN THR GLU ASN THR GLN VAL SER SER
SEQRES 21 C 395 ILE ILE GLU LYS TRP SER MET GLU ARG LEU GLN ALA PRO
SEQRES 22 C 395 PRO LYS PRO ASP SER GLY LEU LEU ASP GLY PHE MET THR
SEQRES 23 C 395 THR ASP ALA ALA LEU MET TYR ASP ALA VAL HIS VAL VAL
SEQRES 24 C 395 SER VAL ALA VAL GLN GLN PHE PRO GLN MET THR VAL SER
SEQRES 25 C 395 SER LEU GLN CYS ASN ARG HIS LYS PRO TRP ARG PHE GLY
SEQRES 26 C 395 THR ARG PHE MET SER LEU ILE LYS GLU ALA HIS TRP GLU
SEQRES 27 C 395 GLY LEU THR GLY ARG ILE THR PHE ASN LYS THR ASN GLY
SEQRES 28 C 395 LEU ARG THR ASP PHE ASP LEU ASP VAL ILE SER LEU LYS
SEQRES 29 C 395 GLU GLU GLY LEU GLU LYS ILE GLY THR TRP ASP PRO ALA
SEQRES 30 C 395 SER GLY LEU ASN MET THR GLU SER GLN LYS GLY LYS LEU
SEQRES 31 C 395 GLU LEU VAL PRO ARG
SEQRES 1 D 395 THR THR HIS VAL LEU ARG PHE GLY GLY ILE PHE GLU TYR
SEQRES 2 D 395 VAL GLU SER GLY PRO MET GLY ALA GLU GLU LEU ALA PHE
SEQRES 3 D 395 ARG PHE ALA VAL ASN THR ILE ASN ARG ASN ARG THR LEU
SEQRES 4 D 395 LEU PRO ASN THR THR LEU THR TYR ASP THR GLN LYS ILE
SEQRES 5 D 395 ASN LEU TYR ASP SER PHE GLU ALA SER LYS LYS ALA CYS
SEQRES 6 D 395 ASP GLN LEU SER LEU GLY VAL ALA ALA ILE PHE GLY PRO
SEQRES 7 D 395 SER HIS SER SER SER ALA ASN ALA VAL GLN SER ILE CYS
SEQRES 8 D 395 ASN ALA LEU GLY VAL PRO HIS ILE GLN THR ARG TRP LYS
SEQRES 9 D 395 HIS GLN VAL SER ASP ASN LYS ASP SER PHE TYR VAL SER
SEQRES 10 D 395 LEU TYR PRO ASP PHE SER SER LEU SER ARG ALA ILE LEU
SEQRES 11 D 395 ASP LEU VAL GLN PHE PHE LYS TRP LYS THR VAL THR VAL
SEQRES 12 D 395 VAL TYR ASP ASP SER THR GLY LEU ILE ARG LEU GLN GLU
SEQRES 13 D 395 LEU ILE LYS ALA PRO SER ARG TYR ASN LEU ARG LEU LYS
SEQRES 14 D 395 ILE ARG GLN LEU PRO ALA ASP THR LYS ASP ALA LYS PRO
SEQRES 15 D 395 LEU LEU LYS GLU MET LYS ARG GLY LYS GLU PHE HIS VAL
SEQRES 16 D 395 ILE PHE ASP CYS SER HIS GLU MET ALA ALA GLY ILE LEU
SEQRES 17 D 395 LYS GLN ALA LEU ASN MET SER MET MET THR GLU TYR TYR
SEQRES 18 D 395 HIS TYR ILE PHE THR THR LEU ASP LEU PHE ALA LEU ASP
SEQRES 19 D 395 VAL GLU PRO TYR ARG TYR SER GLY VAL ASN MET THR GLY
SEQRES 20 D 395 PHE ARG ILE LEU ASN THR GLU ASN THR GLN VAL SER SER
SEQRES 21 D 395 ILE ILE GLU LYS TRP SER MET GLU ARG LEU GLN ALA PRO
SEQRES 22 D 395 PRO LYS PRO ASP SER GLY LEU LEU ASP GLY PHE MET THR
SEQRES 23 D 395 THR ASP ALA ALA LEU MET TYR ASP ALA VAL HIS VAL VAL
SEQRES 24 D 395 SER VAL ALA VAL GLN GLN PHE PRO GLN MET THR VAL SER
SEQRES 25 D 395 SER LEU GLN CYS ASN ARG HIS LYS PRO TRP ARG PHE GLY
SEQRES 26 D 395 THR ARG PHE MET SER LEU ILE LYS GLU ALA HIS TRP GLU
SEQRES 27 D 395 GLY LEU THR GLY ARG ILE THR PHE ASN LYS THR ASN GLY
SEQRES 28 D 395 LEU ARG THR ASP PHE ASP LEU ASP VAL ILE SER LEU LYS
SEQRES 29 D 395 GLU GLU GLY LEU GLU LYS ILE GLY THR TRP ASP PRO ALA
SEQRES 30 D 395 SER GLY LEU ASN MET THR GLU SER GLN LYS GLY LYS LEU
SEQRES 31 D 395 GLU LEU VAL PRO ARG
MODRES 3QLU ASN C 347 ASN GLYCOSYLATION SITE
MODRES 3QLU ASN D 213 ASN GLYCOSYLATION SITE
MODRES 3QLU ASN A 303 ASN GLYCOSYLATION SITE
MODRES 3QLU ASN C 36 ASN GLYCOSYLATION SITE
MODRES 3QLU ASN D 36 ASN GLYCOSYLATION SITE
MODRES 3QLU ASN A 252 ASN GLYCOSYLATION SITE
MODRES 3QLU ASN A 266 ASN GLYCOSYLATION SITE
MODRES 3QLU ASN A 353 ASN GLYCOSYLATION SITE
MODRES 3QLU ASN D 347 ASN GLYCOSYLATION SITE
MODRES 3QLU ASN B 266 ASN GLYCOSYLATION SITE
MODRES 3QLU ASN C 381 ASN GLYCOSYLATION SITE
MODRES 3QLU ASN B 375 ASN GLYCOSYLATION SITE
MODRES 3QLU ASN B 353 ASN GLYCOSYLATION SITE
MODRES 3QLU ASN B 252 ASN GLYCOSYLATION SITE
MODRES 3QLU ASN A 200 ASN GLYCOSYLATION SITE
MODRES 3QLU ASN B 200 ASN GLYCOSYLATION SITE
HET NAG A 394 27
HET NAG A 395 27
HET NAG A 396 27
HET NAG A 397 27
HET NAG A 398 27
HET NAG B 394 27
HET NAG B 395 27
HET NAG B 396 27
HET NAG B 397 27
HET NAG B 398 27
HET CL B 399 1
HET GOL B 400 14
HET NAG C 396 27
HET NAG C 397 27
HET NAG C 398 27
HET CL C 399 1
HET NAG D 396 27
HET NAG D 397 27
HET NAG D 398 27
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM CL CHLORIDE ION
HETNAM GOL GLYCEROL
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 5 NAG 16(C8 H15 N O6)
FORMUL 15 CL 2(CL 1-)
FORMUL 16 GOL C3 H8 O3
FORMUL 24 HOH *6(H2 O)
HELIX 1 1 GLY A 20 ILE A 35 1 16
HELIX 2 2 SER A 55 LEU A 67 1 13
HELIX 3 3 PRO A 68 GLY A 70 5 3
HELIX 4 4 SER A 80 GLU A 95 1 16
HELIX 5 5 SER A 122 PHE A 137 1 16
HELIX 6 6 GLU A 150 LEU A 155 1 6
HELIX 7 7 LEU A 155 PHE A 162 1 8
HELIX 8 8 PRO A 180 ASP A 190 1 11
HELIX 9 9 ASN A 200 LEU A 214 1 15
HELIX 10 10 PHE A 257 GLU A 271 1 15
HELIX 11 11 ALA A 282 ARG A 304 1 23
HELIX 12 12 HIS A 323 MET A 333 1 11
HELIX 13 13 GLY B 20 ILE B 35 1 16
HELIX 14 14 SER B 55 LEU B 67 1 13
HELIX 15 15 PRO B 68 GLY B 70 5 3
HELIX 16 16 SER B 80 GLU B 95 1 16
HELIX 17 17 SER B 122 PHE B 137 1 16
HELIX 18 18 GLU B 150 LEU B 155 1 6
HELIX 19 19 LEU B 155 ARG B 160 1 6
HELIX 20 20 PRO B 180 ASP B 190 1 11
HELIX 21 21 ASN B 200 LEU B 214 1 15
HELIX 22 22 PHE B 257 CYS B 273 1 17
HELIX 23 23 ALA B 282 ARG B 304 1 23
HELIX 24 24 HIS B 323 MET B 333 1 11
HELIX 25 25 GLY C 20 ASN C 36 1 17
HELIX 26 26 ASP C 56 GLY C 71 1 16
HELIX 27 27 HIS C 80 LEU C 94 1 15
HELIX 28 28 ASP C 121 PHE C 136 1 16
HELIX 29 29 LEU C 151 ARG C 153 5 3
HELIX 30 30 LEU C 154 LYS C 159 1 6
HELIX 31 31 ALA C 160 ARG C 163 5 4
HELIX 32 32 ALA C 180 GLY C 190 1 11
HELIX 33 33 SER C 200 ASN C 213 1 14
HELIX 34 34 ASP C 229 LEU C 233 5 5
HELIX 35 35 VAL C 235 ARG C 239 5 5
HELIX 36 36 ASN C 255 SER C 266 1 12
HELIX 37 37 THR C 286 GLN C 305 1 20
HELIX 38 38 PHE C 324 GLU C 334 1 11
HELIX 39 39 GLY D 20 ASN D 36 1 17
HELIX 40 40 ASP D 56 GLY D 71 1 16
HELIX 41 41 HIS D 80 LEU D 94 1 15
HELIX 42 42 ASP D 121 PHE D 136 1 16
HELIX 43 43 LEU D 151 ARG D 153 5 3
HELIX 44 44 LEU D 154 LYS D 159 1 6
HELIX 45 45 ALA D 160 ARG D 163 5 4
HELIX 46 46 ALA D 180 GLY D 190 1 11
HELIX 47 47 SER D 200 ASN D 213 1 14
HELIX 48 48 ASP D 229 LEU D 233 5 5
HELIX 49 49 VAL D 235 ARG D 239 5 5
HELIX 50 50 ASN D 255 SER D 266 1 12
HELIX 51 51 THR D 286 GLN D 305 1 20
HELIX 52 52 PHE D 324 GLU D 334 1 11
SHEET 1 A 5 VAL A 44 GLU A 50 0
SHEET 2 A 5 LEU A 5 LEU A 11 1 N LEU A 5 O GLU A 45
SHEET 3 A 5 VAL A 74 LEU A 75 1 O LEU A 75 N ALA A 8
SHEET 4 A 5 HIS A 98 LYS A 100 1 O ILE A 99 N VAL A 74
SHEET 5 A 5 SER A 116 SER A 118 1 O VAL A 117 N LYS A 100
SHEET 1 B 7 LEU A 169 MET A 173 0
SHEET 2 B 7 ALA A 142 CYS A 146 1 N CYS A 146 O ARG A 172
SHEET 3 B 7 THR A 194 ASP A 198 1 O ILE A 196 N ILE A 145
SHEET 4 B 7 LYS A 222 LEU A 225 1 O LYS A 222 N ILE A 195
SHEET 5 B 7 ASN A 244 SER A 249 1 O LEU A 246 N TYR A 223
SHEET 6 B 7 LEU A 356 LYS A 361 -1 O ARG A 357 N SER A 249
SHEET 7 B 7 HIS A 366 TRP A 372 -1 O GLY A 370 N ILE A 358
SHEET 1 C 2 TYR A 336 GLY A 338 0
SHEET 2 C 2 GLY A 341 VAL A 343 -1 O VAL A 343 N TYR A 336
SHEET 1 D 5 VAL B 44 GLU B 50 0
SHEET 2 D 5 LEU B 5 LEU B 11 1 N LEU B 5 O GLU B 45
SHEET 3 D 5 VAL B 74 LEU B 75 1 O LEU B 75 N ILE B 10
SHEET 4 D 5 HIS B 98 LYS B 100 1 O ILE B 99 N VAL B 74
SHEET 5 D 5 SER B 116 SER B 118 1 O VAL B 117 N LYS B 100
SHEET 1 E 7 LEU B 169 MET B 173 0
SHEET 2 E 7 ALA B 142 CYS B 146 1 N LEU B 144 O ARG B 172
SHEET 3 E 7 THR B 194 ASP B 198 1 O ILE B 196 N ILE B 145
SHEET 4 E 7 LYS B 222 LEU B 225 1 O LYS B 222 N ILE B 195
SHEET 5 E 7 ASN B 244 SER B 249 1 O LEU B 246 N TYR B 223
SHEET 6 E 7 THR B 355 GLU B 360 -1 O ARG B 357 N SER B 249
SHEET 7 E 7 GLU B 368 TYR B 373 -1 O TRP B 372 N LEU B 356
SHEET 1 F 2 TYR B 336 GLY B 338 0
SHEET 2 F 2 GLY B 341 VAL B 343 -1 O VAL B 343 N TYR B 336
SHEET 1 G 5 THR C 43 ILE C 52 0
SHEET 2 G 5 HIS C 3 GLU C 12 1 N PHE C 7 O THR C 46
SHEET 3 G 5 ILE C 75 PHE C 76 1 O PHE C 76 N ILE C 10
SHEET 4 G 5 HIS C 98 GLN C 100 1 O ILE C 99 N ILE C 75
SHEET 5 G 5 TYR C 115 SER C 117 1 O VAL C 116 N GLN C 100
SHEET 1 H 8 ARG C 167 LEU C 173 0
SHEET 2 H 8 THR C 140 ASP C 146 1 N VAL C 143 O ARG C 171
SHEET 3 H 8 HIS C 194 ASP C 198 1 O ASP C 198 N VAL C 144
SHEET 4 H 8 HIS C 222 PHE C 225 1 O ILE C 224 N PHE C 197
SHEET 5 H 8 ASN C 244 ARG C 249 1 O THR C 246 N TYR C 223
SHEET 6 H 8 LEU C 358 LYS C 364 -1 O ASP C 359 N ARG C 249
SHEET 7 H 8 GLY C 367 ASP C 375 -1 O ILE C 371 N VAL C 360
SHEET 8 H 8 GLY C 379 MET C 382 -1 O ASN C 381 N THR C 373
SHEET 1 I 2 HIS C 336 GLY C 339 0
SHEET 2 I 2 GLY C 342 THR C 345 -1 O ILE C 344 N TRP C 337
SHEET 1 J 5 THR D 43 ILE D 52 0
SHEET 2 J 5 HIS D 3 GLU D 12 1 N GLY D 9 O ASP D 48
SHEET 3 J 5 ILE D 75 PHE D 76 1 O PHE D 76 N ILE D 10
SHEET 4 J 5 HIS D 98 GLN D 100 1 O ILE D 99 N ILE D 75
SHEET 5 J 5 TYR D 115 SER D 117 1 O VAL D 116 N GLN D 100
SHEET 1 K 8 ARG D 167 LEU D 173 0
SHEET 2 K 8 THR D 140 ASP D 146 1 N VAL D 143 O ARG D 171
SHEET 3 K 8 HIS D 194 ASP D 198 1 O ASP D 198 N VAL D 144
SHEET 4 K 8 HIS D 222 PHE D 225 1 O ILE D 224 N PHE D 197
SHEET 5 K 8 ASN D 244 ARG D 249 1 O THR D 246 N TYR D 223
SHEET 6 K 8 LEU D 358 LYS D 364 -1 O ASP D 359 N ARG D 249
SHEET 7 K 8 GLY D 367 ASP D 375 -1 O GLU D 369 N SER D 362
SHEET 8 K 8 GLY D 379 MET D 382 -1 O ASN D 381 N THR D 373
SHEET 1 L 2 HIS D 336 GLY D 339 0
SHEET 2 L 2 GLY D 342 THR D 345 -1 O ILE D 344 N TRP D 337
SSBOND 1 CYS A 17 CYS A 273 1555 1555 2.03
SSBOND 2 CYS A 64 CYS A 315 1555 1555 2.04
SSBOND 3 CYS A 146 CYS A 151 1555 1555 2.02
SSBOND 4 CYS B 17 CYS B 273 1555 1555 2.04
SSBOND 5 CYS B 64 CYS B 315 1555 1555 2.03
SSBOND 6 CYS B 146 CYS B 151 1555 1555 2.02
SSBOND 7 CYS C 65 CYS C 316 1555 1555 2.05
SSBOND 8 CYS D 65 CYS D 316 1555 1555 2.02
LINK ND2 ASN A 200 C1 NAG A 394 1555 1555 1.45
LINK ND2 ASN A 252 C1 NAG A 395 1555 1555 1.44
LINK ND2 ASN A 266 C1 NAG A 396 1555 1555 1.44
LINK ND2 ASN A 303 C1 NAG A 397 1555 1555 1.44
LINK ND2 ASN A 353 C1 NAG A 398 1555 1555 1.44
LINK ND2 ASN B 200 C1 NAG B 394 1555 1555 1.46
LINK ND2 ASN B 252 C1 NAG B 395 1555 1555 1.45
LINK ND2 ASN B 266 C1 NAG B 396 1555 1555 1.44
LINK ND2 ASN B 353 C1 NAG B 397 1555 1555 1.45
LINK ND2 ASN B 375 C1 NAG B 398 1555 1555 1.45
LINK ND2 ASN C 36 C1 NAG C 396 1555 1555 1.44
LINK ND2 ASN C 347 C1 NAG C 397 1555 1555 1.43
LINK ND2 ASN C 381 C1 NAG C 398 1555 1555 1.44
LINK ND2 ASN D 36 C1 NAG D 396 1555 1555 1.44
LINK ND2 ASN D 213 C1 NAG D 397 1555 1555 1.44
LINK ND2 ASN D 347 C1 NAG D 398 1555 1555 1.44
CISPEP 1 VAL A 38 PRO A 39 0 7.01
CISPEP 2 GLY A 76 PRO A 77 0 1.41
CISPEP 3 PRO A 107 ARG A 108 0 -12.12
CISPEP 4 VAL B 38 PRO B 39 0 3.79
CISPEP 5 GLY B 76 PRO B 77 0 2.64
CISPEP 6 GLY C 77 PRO C 78 0 -3.51
CISPEP 7 GLY D 77 PRO D 78 0 -3.08
CRYST1 65.626 139.548 195.410 90.00 90.00 90.00 P 21 21 21 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 0.015238 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007166 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005117 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
