HEADER VIRAL PROTEIN/SIGNALLING PROTEIN 22-JAN-15 4XT1
TITLE STRUCTURE OF A NANOBODY-BOUND VIRAL GPCR BOUND TO HUMAN CHEMOKINE
TITLE 2 CX3CL1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: G-PROTEIN COUPLED RECEPTOR HOMOLOG US28;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: HHRF3;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: FRACTALKINE;
COMPND 8 CHAIN: B;
COMPND 9 FRAGMENT: UNP RESIDUES 25-101;
COMPND 10 SYNONYM: C-X3-C MOTIF CHEMOKINE 1,CX3C MEMBRANE-ANCHORED CHEMOKINE,
COMPND 11 NEUROTACTIN,SMALL-INDUCIBLE CYTOKINE D1;
COMPND 12 ENGINEERED: YES;
COMPND 13 MUTATION: YES;
COMPND 14 MOL_ID: 3;
COMPND 15 MOLECULE: NANOBODY 7;
COMPND 16 CHAIN: C;
COMPND 17 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CYTOMEGALOVIRUS;
SOURCE 3 ORGANISM_TAXID: 10358;
SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 5 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 7 EXPRESSION_SYSTEM_CELL_LINE: HEK293S GNTI-;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 10 ORGANISM_COMMON: HUMAN;
SOURCE 11 ORGANISM_TAXID: 9606;
SOURCE 12 GENE: CX3CL1, FKN, NTT, SCYD1, A-152E5.2;
SOURCE 13 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 14 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 16 EXPRESSION_SYSTEM_CELL_LINE: HEK293S GNTI-;
SOURCE 17 MOL_ID: 3;
SOURCE 18 ORGANISM_SCIENTIFIC: VICUGNA PACOS;
SOURCE 19 ORGANISM_TAXID: 30538;
SOURCE 20 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 21 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 22 EXPRESSION_SYSTEM_STRAIN: BL21
KEYWDS GPCR, CHEMOKINE, MEMBRANE PROTEIN, COMPLEX, VIRAL PROTEIN-SIGNALLING
KEYWDS 2 PROTEIN COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.S.BURG,K.M.JUDE,D.WAGHRAY,K.C.GARCIA
REVDAT 3 27-SEP-23 4XT1 1 SOURCE JRNL REMARK SEQRES
REVDAT 2 18-MAR-15 4XT1 1 JRNL
REVDAT 1 04-MAR-15 4XT1 0
JRNL AUTH J.S.BURG,J.R.INGRAM,A.J.VENKATAKRISHNAN,K.M.JUDE,
JRNL AUTH 2 A.DUKKIPATI,E.N.FEINBERG,A.ANGELINI,D.WAGHRAY,R.O.DROR,
JRNL AUTH 3 H.L.PLOEGH,K.C.GARCIA
JRNL TITL STRUCTURAL BIOLOGY. STRUCTURAL BASIS FOR CHEMOKINE
JRNL TITL 2 RECOGNITION AND ACTIVATION OF A VIRAL G PROTEIN-COUPLED
JRNL TITL 3 RECEPTOR.
JRNL REF SCIENCE V. 347 1113 2015
JRNL REFN ESSN 1095-9203
JRNL PMID 25745166
JRNL DOI 10.1126/SCIENCE.AAA5026
REMARK 2
REMARK 2 RESOLUTION. 2.89 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX DEV_1839
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.89
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.23
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 16629
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.204
REMARK 3 R VALUE (WORKING SET) : 0.199
REMARK 3 FREE R VALUE : 0.249
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.980
REMARK 3 FREE R VALUE TEST SET COUNT : 1659
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 38.2374 - 6.5960 1.00 1273 143 0.1846 0.2083
REMARK 3 2 6.5960 - 5.2397 1.00 1247 145 0.2212 0.2534
REMARK 3 3 5.2397 - 4.5786 1.00 1265 134 0.1699 0.2022
REMARK 3 4 4.5786 - 4.1606 1.00 1261 135 0.1573 0.2179
REMARK 3 5 4.1606 - 3.8627 1.00 1251 137 0.1999 0.2280
REMARK 3 6 3.8627 - 3.6351 1.00 1260 142 0.1904 0.2472
REMARK 3 7 3.6351 - 3.4532 1.00 1233 145 0.2020 0.3041
REMARK 3 8 3.4532 - 3.3029 1.00 1264 140 0.2338 0.2984
REMARK 3 9 3.3029 - 3.1759 1.00 1245 139 0.2307 0.3373
REMARK 3 10 3.1759 - 3.0663 1.00 1253 137 0.2341 0.2838
REMARK 3 11 3.0663 - 2.9705 1.00 1237 137 0.2562 0.3219
REMARK 3 12 2.9705 - 2.8856 0.95 1181 125 0.2723 0.3354
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) : 0.430
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.330
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 58.12
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 67.00
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 : 0.002 4044
REMARK 3 ANGLE : 0.605 5461
REMARK 3 CHIRALITY : 0.021 630
REMARK 3 PLANARITY : 0.003 649
REMARK 3 DIHEDRAL : 12.801 1462
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 1 THROUGH 66 )
REMARK 3 ORIGIN FOR THE GROUP (A): 97.8340 17.9238 277.5957
REMARK 3 T TENSOR
REMARK 3 T11: 0.7263 T22: 0.7106
REMARK 3 T33: 0.4480 T12: -0.1552
REMARK 3 T13: 0.1093 T23: -0.0240
REMARK 3 L TENSOR
REMARK 3 L11: 3.6181 L22: 7.7641
REMARK 3 L33: 4.4286 L12: 0.2164
REMARK 3 L13: -0.4889 L23: -4.0143
REMARK 3 S TENSOR
REMARK 3 S11: 0.2541 S12: -1.0191 S13: -0.1501
REMARK 3 S21: 0.5337 S22: -0.2781 S23: -0.0937
REMARK 3 S31: 0.7752 S32: -0.2718 S33: 0.0552
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 67 THROUGH 72 )
REMARK 3 ORIGIN FOR THE GROUP (A): 90.1610 21.1182 275.9458
REMARK 3 T TENSOR
REMARK 3 T11: 0.6665 T22: 0.9599
REMARK 3 T33: 0.4348 T12: -0.1040
REMARK 3 T13: 0.2870 T23: -0.0122
REMARK 3 L TENSOR
REMARK 3 L11: 9.5434 L22: 7.0106
REMARK 3 L33: 4.0699 L12: -5.9422
REMARK 3 L13: 2.6683 L23: 1.5195
REMARK 3 S TENSOR
REMARK 3 S11: 0.8410 S12: 0.3912 S13: 0.4446
REMARK 3 S21: 0.2966 S22: -0.2147 S23: 0.9728
REMARK 3 S31: -0.9919 S32: -1.3048 S33: -1.0979
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 73 THROUGH 116 )
REMARK 3 ORIGIN FOR THE GROUP (A): 99.5792 18.4164 278.1598
REMARK 3 T TENSOR
REMARK 3 T11: 0.8674 T22: 0.6620
REMARK 3 T33: 0.2987 T12: -0.1589
REMARK 3 T13: 0.0638 T23: 0.0675
REMARK 3 L TENSOR
REMARK 3 L11: 6.6941 L22: 3.7743
REMARK 3 L33: 7.1639 L12: 2.0050
REMARK 3 L13: -4.2132 L23: -3.4989
REMARK 3 S TENSOR
REMARK 3 S11: 0.0082 S12: -0.6647 S13: -0.6379
REMARK 3 S21: 0.6593 S22: 0.0400 S23: -0.0901
REMARK 3 S31: 0.7415 S32: -0.5307 S33: 0.0046
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 16 THROUGH 33 )
REMARK 3 ORIGIN FOR THE GROUP (A): 110.2833 23.3554 207.6492
REMARK 3 T TENSOR
REMARK 3 T11: 0.6672 T22: 0.6745
REMARK 3 T33: 0.5254 T12: -0.0585
REMARK 3 T13: 0.1004 T23: 0.0131
REMARK 3 L TENSOR
REMARK 3 L11: 6.0571 L22: 3.2809
REMARK 3 L33: 6.4363 L12: 0.0943
REMARK 3 L13: 0.5272 L23: 1.0416
REMARK 3 S TENSOR
REMARK 3 S11: -0.1704 S12: 0.9867 S13: 0.5568
REMARK 3 S21: -0.4851 S22: 0.4170 S23: 0.1129
REMARK 3 S31: -0.7431 S32: -0.4589 S33: -0.0335
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 34 THROUGH 103 )
REMARK 3 ORIGIN FOR THE GROUP (A): 103.0991 10.5731 240.6328
REMARK 3 T TENSOR
REMARK 3 T11: 0.3570 T22: 0.2609
REMARK 3 T33: 0.4665 T12: -0.0585
REMARK 3 T13: 0.0052 T23: -0.0455
REMARK 3 L TENSOR
REMARK 3 L11: 2.3303 L22: 1.7464
REMARK 3 L33: 3.9634 L12: -0.6707
REMARK 3 L13: -1.7244 L23: 0.1946
REMARK 3 S TENSOR
REMARK 3 S11: -0.2586 S12: 0.1193 S13: -0.4502
REMARK 3 S21: -0.0147 S22: 0.0722 S23: 0.1727
REMARK 3 S31: 0.7907 S32: -0.3102 S33: 0.1915
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 104 THROUGH 169 )
REMARK 3 ORIGIN FOR THE GROUP (A): 92.4756 22.3415 242.3529
REMARK 3 T TENSOR
REMARK 3 T11: 0.1923 T22: 0.3210
REMARK 3 T33: 0.4229 T12: 0.0114
REMARK 3 T13: -0.0223 T23: 0.0353
REMARK 3 L TENSOR
REMARK 3 L11: 2.9439 L22: 1.4595
REMARK 3 L33: 8.8955 L12: 0.3258
REMARK 3 L13: -0.3839 L23: 1.6012
REMARK 3 S TENSOR
REMARK 3 S11: -0.2236 S12: 0.2217 S13: 0.0628
REMARK 3 S21: -0.1167 S22: -0.1545 S23: 0.4046
REMARK 3 S31: -0.0129 S32: -0.6211 S33: 0.3990
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 170 THROUGH 183 )
REMARK 3 ORIGIN FOR THE GROUP (A): 92.3407 20.5767 214.9800
REMARK 3 T TENSOR
REMARK 3 T11: 0.8177 T22: 1.0753
REMARK 3 T33: 0.6612 T12: -0.0693
REMARK 3 T13: -0.1480 T23: -0.2003
REMARK 3 L TENSOR
REMARK 3 L11: 3.4908 L22: 8.5694
REMARK 3 L33: 8.4630 L12: -2.8670
REMARK 3 L13: -1.4758 L23: 5.6972
REMARK 3 S TENSOR
REMARK 3 S11: 0.3479 S12: 1.4016 S13: -0.1867
REMARK 3 S21: -1.3734 S22: -1.3732 S23: 1.9016
REMARK 3 S31: -0.4287 S32: -0.8483 S33: 1.0144
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 184 THROUGH 290 )
REMARK 3 ORIGIN FOR THE GROUP (A): 106.3190 29.7905 237.0153
REMARK 3 T TENSOR
REMARK 3 T11: 0.3088 T22: 0.2787
REMARK 3 T33: 0.3940 T12: -0.0511
REMARK 3 T13: 0.0069 T23: 0.0360
REMARK 3 L TENSOR
REMARK 3 L11: 0.9490 L22: 0.5389
REMARK 3 L33: 5.3558 L12: -0.0388
REMARK 3 L13: -0.0274 L23: 0.1635
REMARK 3 S TENSOR
REMARK 3 S11: -0.0709 S12: 0.0897 S13: -0.0460
REMARK 3 S21: -0.1062 S22: 0.0317 S23: 0.0247
REMARK 3 S31: -0.1538 S32: -0.0703 S33: 0.0276
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 291 THROUGH 310 )
REMARK 3 ORIGIN FOR THE GROUP (A): 109.6962 9.3779 257.7165
REMARK 3 T TENSOR
REMARK 3 T11: 0.3843 T22: 0.4173
REMARK 3 T33: 0.6507 T12: 0.0627
REMARK 3 T13: -0.0727 T23: -0.0791
REMARK 3 L TENSOR
REMARK 3 L11: 7.7503 L22: 5.3358
REMARK 3 L33: 8.0326 L12: -1.3482
REMARK 3 L13: 3.2667 L23: -4.8988
REMARK 3 S TENSOR
REMARK 3 S11: 0.4807 S12: -0.1203 S13: -0.6189
REMARK 3 S21: -0.2217 S22: -0.5434 S23: -0.6009
REMARK 3 S31: 0.8659 S32: 0.4113 S33: 0.1423
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 2 THROUGH 16 )
REMARK 3 ORIGIN FOR THE GROUP (A): 102.8725 21.5940 212.1990
REMARK 3 T TENSOR
REMARK 3 T11: 0.5954 T22: 0.8527
REMARK 3 T33: 0.5501 T12: 0.0365
REMARK 3 T13: -0.0628 T23: -0.0573
REMARK 3 L TENSOR
REMARK 3 L11: 4.5598 L22: 6.5817
REMARK 3 L33: 9.6518 L12: 2.3673
REMARK 3 L13: -3.1025 L23: -1.9082
REMARK 3 S TENSOR
REMARK 3 S11: 0.3271 S12: 0.9673 S13: -0.0434
REMARK 3 S21: -0.6332 S22: -0.3916 S23: 1.6379
REMARK 3 S31: -0.8714 S32: 0.1197 S33: -0.1066
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 17 THROUGH 23 )
REMARK 3 ORIGIN FOR THE GROUP (A): 101.4834 24.0413 188.1388
REMARK 3 T TENSOR
REMARK 3 T11: 1.2398 T22: 1.6698
REMARK 3 T33: 0.7576 T12: -0.1170
REMARK 3 T13: -0.1320 T23: -0.0828
REMARK 3 L TENSOR
REMARK 3 L11: 0.4372 L22: 2.0615
REMARK 3 L33: 4.7053 L12: -0.8465
REMARK 3 L13: -1.4104 L23: 2.9888
REMARK 3 S TENSOR
REMARK 3 S11: -1.0461 S12: 0.9625 S13: -0.1861
REMARK 3 S21: 1.7639 S22: 0.0976 S23: 0.8073
REMARK 3 S31: 0.9873 S32: -3.3418 S33: 1.1414
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 24 THROUGH 29 )
REMARK 3 ORIGIN FOR THE GROUP (A): 102.3993 14.3923 196.3178
REMARK 3 T TENSOR
REMARK 3 T11: 1.8237 T22: 1.6473
REMARK 3 T33: 0.8598 T12: -0.4539
REMARK 3 T13: -0.1482 T23: -0.3401
REMARK 3 L TENSOR
REMARK 3 L11: 3.7392 L22: 1.2740
REMARK 3 L33: 5.7859 L12: -1.8308
REMARK 3 L13: -3.6685 L23: 0.8875
REMARK 3 S TENSOR
REMARK 3 S11: -0.7249 S12: 1.4117 S13: -1.2002
REMARK 3 S21: 0.5817 S22: 1.1974 S23: -0.7236
REMARK 3 S31: 2.0070 S32: -2.3345 S33: -0.1025
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 30 THROUGH 57 )
REMARK 3 ORIGIN FOR THE GROUP (A): 100.9478 20.6617 199.6775
REMARK 3 T TENSOR
REMARK 3 T11: 1.0706 T22: 1.9454
REMARK 3 T33: 0.4560 T12: -0.0774
REMARK 3 T13: -0.1322 T23: -0.0630
REMARK 3 L TENSOR
REMARK 3 L11: 1.9495 L22: 2.9397
REMARK 3 L33: 3.0594 L12: 1.8877
REMARK 3 L13: -1.5929 L23: -1.1735
REMARK 3 S TENSOR
REMARK 3 S11: -0.4506 S12: 0.2093 S13: -0.2632
REMARK 3 S21: -1.1037 S22: 0.2179 S23: 0.1150
REMARK 3 S31: 0.5901 S32: -0.1105 S33: -0.3604
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 58 THROUGH 69 )
REMARK 3 ORIGIN FOR THE GROUP (A): 96.0353 13.8865 190.4050
REMARK 3 T TENSOR
REMARK 3 T11: 1.2548 T22: 2.1225
REMARK 3 T33: 1.1028 T12: -0.7648
REMARK 3 T13: -0.0630 T23: -0.0347
REMARK 3 L TENSOR
REMARK 3 L11: 9.6854 L22: 5.9922
REMARK 3 L33: 6.3853 L12: -7.6140
REMARK 3 L13: -1.4100 L23: 1.3203
REMARK 3 S TENSOR
REMARK 3 S11: 0.1889 S12: 3.4295 S13: -2.5020
REMARK 3 S21: -0.6080 S22: -0.3263 S23: 2.1531
REMARK 3 S31: 1.5941 S32: -2.3030 S33: 0.6776
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 4XT1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-JAN-15.
REMARK 100 THE DEPOSITION ID IS D_1000206261.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-OCT-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.3
REMARK 200 NUMBER OF CRYSTALS USED : 2
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) : 1.033
REMARK 200 MONOCHROMATOR : NULL
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 : 16648
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.880
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 200 DATA REDUNDANCY : 8.500
REMARK 200 R MERGE (I) : 0.20000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.88
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.93
REMARK 200 COMPLETENESS FOR SHELL (%) : 74.8
REMARK 200 DATA REDUNDANCY IN SHELL : 6.80
REMARK 200 R MERGE FOR SHELL (I) : 0.87200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 4MBS, 1F2L, 3ONA, 4B41
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.80
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.85
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 300, MES, SODIUM SUCCINATE,
REMARK 280 POLYPROPYLENE GLYCOL 400, PH 6.3, LIPIDIC CUBIC PHASE,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -Y,X,Z
REMARK 290 4555 Y,-X,Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -Y+1/2,X+1/2,Z+1/2
REMARK 290 8555 Y+1/2,-X+1/2,Z+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 40.51200
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 40.51200
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 115.65150
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 40.51200
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 40.51200
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 115.65150
REMARK 290 SMTRY1 7 0.000000 -1.000000 0.000000 40.51200
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 40.51200
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 115.65150
REMARK 290 SMTRY1 8 0.000000 1.000000 0.000000 40.51200
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 40.51200
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 115.65150
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7910 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23920 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -40.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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 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 ASP A -7
REMARK 465 TYR A -6
REMARK 465 LYS A -5
REMARK 465 ASP A -4
REMARK 465 ASP A -3
REMARK 465 ASP A -2
REMARK 465 ASP A -1
REMARK 465 ALA A 0
REMARK 465 MET A 1
REMARK 465 THR A 2
REMARK 465 PRO A 3
REMARK 465 THR A 4
REMARK 465 THR A 5
REMARK 465 THR A 6
REMARK 465 THR A 7
REMARK 465 ALA A 8
REMARK 465 GLU A 9
REMARK 465 LEU A 10
REMARK 465 THR A 11
REMARK 465 THR A 12
REMARK 465 GLU A 13
REMARK 465 PHE A 14
REMARK 465 HIS A 96
REMARK 465 ASN A 97
REMARK 465 SER A 98
REMARK 465 LEU A 99
REMARK 465 ALA A 100
REMARK 465 GLN A 311
REMARK 465 ARG A 312
REMARK 465 LEU A 313
REMARK 465 PHE A 314
REMARK 465 SER A 315
REMARK 465 ARG A 316
REMARK 465 ASP A 317
REMARK 465 VAL A 318
REMARK 465 SER A 319
REMARK 465 TRP A 320
REMARK 465 TYR A 321
REMARK 465 HIS A 322
REMARK 465 SER A 323
REMARK 465 MET A 324
REMARK 465 SER A 325
REMARK 465 PHE A 326
REMARK 465 SER A 327
REMARK 465 ARG A 328
REMARK 465 ARG A 329
REMARK 465 SER A 330
REMARK 465 SER A 331
REMARK 465 PRO A 332
REMARK 465 SER A 333
REMARK 465 ARG A 334
REMARK 465 ARG A 335
REMARK 465 GLU A 336
REMARK 465 THR A 337
REMARK 465 SER A 338
REMARK 465 SER A 339
REMARK 465 ASP A 340
REMARK 465 THR A 341
REMARK 465 LEU A 342
REMARK 465 SER A 343
REMARK 465 ASP A 344
REMARK 465 GLU A 345
REMARK 465 VAL A 346
REMARK 465 CYS A 347
REMARK 465 ARG A 348
REMARK 465 VAL A 349
REMARK 465 SER A 350
REMARK 465 GLN A 351
REMARK 465 ILE A 352
REMARK 465 ILE A 353
REMARK 465 PRO A 354
REMARK 465 ALA B 69
REMARK 465 ALA B 70
REMARK 465 ALA B 71
REMARK 465 LEU B 72
REMARK 465 THR B 73
REMARK 465 ARG B 74
REMARK 465 ASN B 75
REMARK 465 GLY B 76
REMARK 465 GLY B 77
REMARK 465 SER B 78
REMARK 465 GLY B 79
REMARK 465 SER B 80
REMARK 465 GLY B 81
REMARK 465 SER B 82
REMARK 465 ALA B 83
REMARK 465 ALA B 84
REMARK 465 ALA B 85
REMARK 465 LEU B 86
REMARK 465 GLU B 87
REMARK 465 VAL B 88
REMARK 465 LEU B 89
REMARK 465 PHE B 90
REMARK 465 GLN B 91
REMARK 465 GLY C -3
REMARK 465 PRO C -2
REMARK 465 GLY C -1
REMARK 465 SER C 0
REMARK 465 SER C 117
REMARK 465 SER C 118
REMARK 465 ARG C 119
REMARK 465 ALA C 120
REMARK 465 ALA C 121
REMARK 465 ALA C 122
REMARK 465 HIS C 123
REMARK 465 HIS C 124
REMARK 465 HIS C 125
REMARK 465 HIS C 126
REMARK 465 HIS C 127
REMARK 465 HIS C 128
REMARK 465 HIS C 129
REMARK 465 HIS C 130
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ARG A 62 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 63 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 65 CG CD OE1 NE2
REMARK 470 GLN A 91 CG CD OE1 NE2
REMARK 470 ARG A 137 CD NE CZ NH1 NH2
REMARK 470 LYS A 297 CG CD CE NZ
REMARK 470 LYS B 14 CG CD CE NZ
REMARK 470 LEU B 23 CG CD1 CD2
REMARK 470 HIS B 26 CG ND1 CD2 CE1 NE2
REMARK 470 LYS B 36 CG CD CE NZ
REMARK 470 ARG B 37 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 44 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 47 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 54 CG CD CE NZ
REMARK 470 GLN B 56 CG CD OE1 NE2
REMARK 470 LYS B 59 CG CD CE NZ
REMARK 470 MET B 62 CG SD CE
REMARK 470 GLN B 63 CG CD OE1 NE2
REMARK 470 HIS B 64 CG ND1 CD2 CE1 NE2
REMARK 470 ASP B 66 CG OD1 OD2
REMARK 470 ARG B 67 CG CD NE CZ NH1 NH2
REMARK 470 GLN B 68 CG CD OE1 NE2
REMARK 470 GLN C 1 CG CD OE1 NE2
REMARK 470 ARG C 13 CG CD NE CZ NH1 NH2
REMARK 470 ASP C 61 CG OD1 OD2
REMARK 470 LYS C 64 CG CD CE NZ
REMARK 470 GLN C 110 CG CD OE1 NE2
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 OH TYR A 209 O19 OLC A 407 1.26
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 ASP A 17 96.42 -54.09
REMARK 500 TRP A 60 -73.74 -60.65
REMARK 500 GLN A 65 -61.76 -96.13
REMARK 500 VAL A 102 81.35 31.07
REMARK 500 PHE A 197 -64.82 -124.15
REMARK 500 TYR A 291 -54.60 -126.12
REMARK 500 ILE B 19 102.29 -162.85
REMARK 500 LYS B 54 37.20 -91.32
REMARK 500 ALA C 74 -29.69 69.72
REMARK 500 ILE C 101 -61.95 61.47
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 OLC A 403
REMARK 610 OLC A 404
REMARK 610 OLC A 405
REMARK 610 OLC A 406
REMARK 610 OLC A 408
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLR A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLR A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SIN A 416
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4XT3 RELATED DB: PDB
DBREF 4XT1 A 1 354 UNP P69332 US28_HCMVA 1 354
DBREF 4XT1 B 1 77 UNP P78423 X3CL1_HUMAN 25 101
DBREF 4XT1 C -3 130 PDB 4XT1 4XT1 -3 130
SEQADV 4XT1 ASP A -7 UNP P69332 EXPRESSION TAG
SEQADV 4XT1 TYR A -6 UNP P69332 EXPRESSION TAG
SEQADV 4XT1 LYS A -5 UNP P69332 EXPRESSION TAG
SEQADV 4XT1 ASP A -4 UNP P69332 EXPRESSION TAG
SEQADV 4XT1 ASP A -3 UNP P69332 EXPRESSION TAG
SEQADV 4XT1 ASP A -2 UNP P69332 EXPRESSION TAG
SEQADV 4XT1 ASP A -1 UNP P69332 EXPRESSION TAG
SEQADV 4XT1 ALA A 0 UNP P69332 EXPRESSION TAG
SEQADV 4XT1 ALA B 9 UNP P78423 ASN 33 ENGINEERED MUTATION
SEQADV 4XT1 SER B 78 UNP P78423 EXPRESSION TAG
SEQADV 4XT1 GLY B 79 UNP P78423 EXPRESSION TAG
SEQADV 4XT1 SER B 80 UNP P78423 EXPRESSION TAG
SEQADV 4XT1 GLY B 81 UNP P78423 EXPRESSION TAG
SEQADV 4XT1 SER B 82 UNP P78423 EXPRESSION TAG
SEQADV 4XT1 ALA B 83 UNP P78423 EXPRESSION TAG
SEQADV 4XT1 ALA B 84 UNP P78423 EXPRESSION TAG
SEQADV 4XT1 ALA B 85 UNP P78423 EXPRESSION TAG
SEQADV 4XT1 LEU B 86 UNP P78423 EXPRESSION TAG
SEQADV 4XT1 GLU B 87 UNP P78423 EXPRESSION TAG
SEQADV 4XT1 VAL B 88 UNP P78423 EXPRESSION TAG
SEQADV 4XT1 LEU B 89 UNP P78423 EXPRESSION TAG
SEQADV 4XT1 PHE B 90 UNP P78423 EXPRESSION TAG
SEQADV 4XT1 GLN B 91 UNP P78423 EXPRESSION TAG
SEQRES 1 A 362 ASP TYR LYS ASP ASP ASP ASP ALA MET THR PRO THR THR
SEQRES 2 A 362 THR THR ALA GLU LEU THR THR GLU PHE ASP TYR ASP GLU
SEQRES 3 A 362 ASP ALA THR PRO CYS VAL PHE THR ASP VAL LEU ASN GLN
SEQRES 4 A 362 SER LYS PRO VAL THR LEU PHE LEU TYR GLY VAL VAL PHE
SEQRES 5 A 362 LEU PHE GLY SER ILE GLY ASN PHE LEU VAL ILE PHE THR
SEQRES 6 A 362 ILE THR TRP ARG ARG ARG ILE GLN CYS SER GLY ASP VAL
SEQRES 7 A 362 TYR PHE ILE ASN LEU ALA ALA ALA ASP LEU LEU PHE VAL
SEQRES 8 A 362 CYS THR LEU PRO LEU TRP MET GLN TYR LEU LEU ASP HIS
SEQRES 9 A 362 ASN SER LEU ALA SER VAL PRO CYS THR LEU LEU THR ALA
SEQRES 10 A 362 CYS PHE TYR VAL ALA MET PHE ALA SER LEU CYS PHE ILE
SEQRES 11 A 362 THR GLU ILE ALA LEU ASP ARG TYR TYR ALA ILE VAL TYR
SEQRES 12 A 362 MET ARG TYR ARG PRO VAL LYS GLN ALA CYS LEU PHE SER
SEQRES 13 A 362 ILE PHE TRP TRP ILE PHE ALA VAL ILE ILE ALA ILE PRO
SEQRES 14 A 362 HIS PHE MET VAL VAL THR LYS LYS ASP ASN GLN CYS MET
SEQRES 15 A 362 THR ASP TYR ASP TYR LEU GLU VAL SER TYR PRO ILE ILE
SEQRES 16 A 362 LEU ASN VAL GLU LEU MET LEU GLY ALA PHE VAL ILE PRO
SEQRES 17 A 362 LEU SER VAL ILE SER TYR CYS TYR TYR ARG ILE SER ARG
SEQRES 18 A 362 ILE VAL ALA VAL SER GLN SER ARG HIS LYS GLY ARG ILE
SEQRES 19 A 362 VAL ARG VAL LEU ILE ALA VAL VAL LEU VAL PHE ILE ILE
SEQRES 20 A 362 PHE TRP LEU PRO TYR HIS LEU THR LEU PHE VAL ASP THR
SEQRES 21 A 362 LEU LYS LEU LEU LYS TRP ILE SER SER SER CYS GLU PHE
SEQRES 22 A 362 GLU ARG SER LEU LYS ARG ALA LEU ILE LEU THR GLU SER
SEQRES 23 A 362 LEU ALA PHE CYS HIS CYS CYS LEU ASN PRO LEU LEU TYR
SEQRES 24 A 362 VAL PHE VAL GLY THR LYS PHE ARG GLN GLU LEU HIS CYS
SEQRES 25 A 362 LEU LEU ALA GLU PHE ARG GLN ARG LEU PHE SER ARG ASP
SEQRES 26 A 362 VAL SER TRP TYR HIS SER MET SER PHE SER ARG ARG SER
SEQRES 27 A 362 SER PRO SER ARG ARG GLU THR SER SER ASP THR LEU SER
SEQRES 28 A 362 ASP GLU VAL CYS ARG VAL SER GLN ILE ILE PRO
SEQRES 1 B 91 PCA HIS HIS GLY VAL THR LYS CYS ALA ILE THR CYS SER
SEQRES 2 B 91 LYS MET THR SER LYS ILE PRO VAL ALA LEU LEU ILE HIS
SEQRES 3 B 91 TYR GLN GLN ASN GLN ALA SER CYS GLY LYS ARG ALA ILE
SEQRES 4 B 91 ILE LEU GLU THR ARG GLN HIS ARG LEU PHE CYS ALA ASP
SEQRES 5 B 91 PRO LYS GLU GLN TRP VAL LYS ASP ALA MET GLN HIS LEU
SEQRES 6 B 91 ASP ARG GLN ALA ALA ALA LEU THR ARG ASN GLY GLY SER
SEQRES 7 B 91 GLY SER GLY SER ALA ALA ALA LEU GLU VAL LEU PHE GLN
SEQRES 1 C 134 GLY PRO GLY SER GLN VAL GLN LEU VAL GLU SER GLY GLY
SEQRES 2 C 134 GLY LEU VAL ARG PRO GLY GLY SER LEU ARG LEU SER CYS
SEQRES 3 C 134 ALA ALA SER GLY SER ILE PHE THR ILE TYR ALA MET GLY
SEQRES 4 C 134 TRP TYR ARG GLN ALA PRO GLY LYS GLN ARG GLU LEU VAL
SEQRES 5 C 134 ALA ARG ILE THR PHE GLY GLY ASP THR ASN TYR ALA ASP
SEQRES 6 C 134 SER VAL LYS GLY ARG PHE THR ILE SER ARG ASP ASN ALA
SEQRES 7 C 134 LYS ASN ALA VAL TYR LEU GLN MET ASN SER LEU LYS PRO
SEQRES 8 C 134 GLU ASP THR ALA VAL TYR TYR CYS ASN ALA GLU GLU THR
SEQRES 9 C 134 ILE VAL GLU GLU ALA ASP TYR TRP GLY GLN GLY THR GLN
SEQRES 10 C 134 VAL THR VAL SER SER ARG ALA ALA ALA HIS HIS HIS HIS
SEQRES 11 C 134 HIS HIS HIS HIS
MODRES 4XT1 PCA B 1 GLN MODIFIED RESIDUE
HET PCA B 1 8
HET CLR A 401 28
HET CLR A 402 28
HET OLC A 403 20
HET OLC A 404 20
HET OLC A 405 16
HET OLC A 406 21
HET OLC A 407 25
HET OLC A 408 14
HET UNL A 409 7
HET UNL A 410 12
HET UNL A 411 10
HET UNL A 412 12
HET UNL A 413 10
HET UNL A 414 12
HET UNL A 415 12
HET SIN A 416 8
HETNAM PCA PYROGLUTAMIC ACID
HETNAM CLR CHOLESTEROL
HETNAM OLC (2R)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE
HETNAM UNL UNKNOWN LIGAND
HETNAM SIN SUCCINIC ACID
HETSYN OLC 1-OLEOYL-R-GLYCEROL
FORMUL 2 PCA C5 H7 N O3
FORMUL 4 CLR 2(C27 H46 O)
FORMUL 6 OLC 6(C21 H40 O4)
FORMUL 19 SIN C4 H6 O4
FORMUL 20 HOH *23(H2 O)
HELIX 1 AA1 PHE A 25 TRP A 60 1 36
HELIX 2 AA2 CYS A 66 CYS A 84 1 19
HELIX 3 AA3 THR A 85 ASP A 95 1 11
HELIX 4 AA4 PRO A 103 VAL A 134 1 32
HELIX 5 AA5 PRO A 140 ILE A 158 1 19
HELIX 6 AA6 ALA A 159 MET A 164 1 6
HELIX 7 AA7 SER A 183 PHE A 197 1 15
HELIX 8 AA8 PHE A 197 ALA A 216 1 20
HELIX 9 AA9 HIS A 222 LEU A 256 1 35
HELIX 10 AB1 SER A 262 PHE A 281 1 20
HELIX 11 AB2 CYS A 282 TYR A 291 1 10
HELIX 12 AB3 GLY A 295 PHE A 309 1 15
HELIX 13 AB4 GLN B 31 GLY B 35 5 5
HELIX 14 AB5 GLU B 55 GLN B 68 1 14
HELIX 15 AB6 LYS C 86 THR C 90 5 5
SHEET 1 AA1 2 CYS A 23 VAL A 24 0
SHEET 2 AA1 2 ILE B 10 THR B 11 -1 O THR B 11 N CYS A 23
SHEET 1 AA2 2 VAL A 166 LYS A 169 0
SHEET 2 AA2 2 GLN A 172 THR A 175 -1 O GLN A 172 N LYS A 169
SHEET 1 AA3 3 LEU B 24 GLN B 29 0
SHEET 2 AA3 3 ILE B 39 THR B 43 -1 O ILE B 40 N GLN B 28
SHEET 3 AA3 3 LEU B 48 ALA B 51 -1 O ALA B 51 N ILE B 39
SHEET 1 AA4 4 LEU C 4 SER C 7 0
SHEET 2 AA4 4 SER C 17 ALA C 24 -1 O SER C 21 N SER C 7
SHEET 3 AA4 4 ALA C 77 ASN C 83 -1 O MET C 82 N LEU C 18
SHEET 4 AA4 4 PHE C 67 ASP C 72 -1 N ASP C 72 O ALA C 77
SHEET 1 AA5 6 GLY C 10 LEU C 11 0
SHEET 2 AA5 6 THR C 112 THR C 115 1 O THR C 115 N GLY C 10
SHEET 3 AA5 6 ALA C 91 GLU C 99 -1 N TYR C 93 O THR C 112
SHEET 4 AA5 6 ILE C 31 GLN C 39 -1 N TYR C 37 O TYR C 94
SHEET 5 AA5 6 ARG C 45 THR C 52 -1 O ALA C 49 N TRP C 36
SHEET 6 AA5 6 THR C 57 TYR C 59 -1 O ASN C 58 N ARG C 50
SHEET 1 AA6 4 GLY C 10 LEU C 11 0
SHEET 2 AA6 4 THR C 112 THR C 115 1 O THR C 115 N GLY C 10
SHEET 3 AA6 4 ALA C 91 GLU C 99 -1 N TYR C 93 O THR C 112
SHEET 4 AA6 4 TYR C 107 TRP C 108 -1 O TYR C 107 N ALA C 97
SSBOND 1 CYS A 23 CYS A 263 1555 1555 2.03
SSBOND 2 CYS A 104 CYS A 173 1555 1555 2.03
SSBOND 3 CYS B 8 CYS B 34 1555 1555 2.03
SSBOND 4 CYS B 12 CYS B 50 1555 1555 2.03
SSBOND 5 CYS C 22 CYS C 95 1555 1555 2.03
LINK C PCA B 1 N HIS B 2 1555 1555 1.33
SITE 1 AC1 3 PRO A 243 LEU A 246 CLR A 402
SITE 1 AC2 6 PHE A 249 LEU A 253 SER A 268 ARG A 271
SITE 2 AC2 6 LEU A 279 CLR A 401
SITE 1 AC3 2 PRO A 34 PHE A 38
SITE 1 AC4 6 GLY A 224 ARG A 228 ILE A 231 LEU A 235
SITE 2 AC4 6 OLC A 406 OLC A 407
SITE 1 AC5 6 PHE A 46 ILE A 49 LEU A 289 PHE A 293
SITE 2 AC5 6 ARG A 299 LEU A 302
SITE 1 AC6 5 TYR A 209 ARG A 213 ILE A 231 VAL A 234
SITE 2 AC6 5 OLC A 404
SITE 1 AC7 8 SER A 202 TYR A 209 ARG A 210 ARG A 213
SITE 2 AC7 8 ARG A 225 ARG A 228 OLC A 404 OLC A 408
SITE 1 AC8 3 LEU A 289 LEU A 290 OLC A 407
SITE 1 AC9 3 LEU A 119 THR A 123 GLY A 195
CRYST1 81.024 81.024 231.303 90.00 90.00 90.00 I 4 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 0.012342 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012342 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004323 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
