HEADER VIRAL PROTEIN/ISOMERASE 08-JUN-10 2XGY
TITLE COMPLEX OF RABBIT ENDOGENOUS LENTIVIRUS (RELIK)CAPSID WITH
TITLE 2 CYCLOPHILIN A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RELIK CAPSID N-TERMINAL DOMAIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: PEPTIDYL-PROLYL CIS-TRANS ISOMERASE A;
COMPND 7 CHAIN: B;
COMPND 8 SYNONYM: PPIASE A, ROTAMASE A, CYCLOPHILIN A, CYCLOSPORIN A-BINDING
COMPND 9 PROTEIN;
COMPND 10 EC: 5.2.1.8;
COMPND 11 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ORYCTOLAGUS CUNICULUS;
SOURCE 3 ORGANISM_COMMON: RABBIT;
SOURCE 4 ORGANISM_TAXID: 9986;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET22B;
SOURCE 9 OTHER_DETAILS: SYNTHESISED RECONSTRUCTED GENE;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 12 ORGANISM_COMMON: HUMAN;
SOURCE 13 ORGANISM_TAXID: 9606;
SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 16 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 17 EXPRESSION_SYSTEM_PLASMID: PGEX-6P1
KEYWDS VIRAL PROTEIN-ISOMERASE COMPLEX, RETROVIRAL CAPSID, ENDOGENOUS
EXPDTA X-RAY DIFFRACTION
AUTHOR D.C.GOLDSTONE,L.E.ROBERTSON,L.F.HAIRE,J.P.STOYE,I.A.TAYLOR
REVDAT 1 22-SEP-10 2XGY 0
JRNL AUTH D.C.GOLDSTONE,M.W.YAP,L.E.ROBERTSON,L.F.HAIRE,W.R.TAYLOR,
JRNL AUTH 2 A.KATZOURAKIS,J.P.STOYE,I.A.TAYLOR
JRNL TITL STRUCTURAL AND FUNCTIONAL ANALYSIS OF PREHISTORIC
JRNL TITL 2 LENTIVIRUSES UNCOVERS AN ANCIENT MOLECULAR INTERFACE.
JRNL REF CELL HOST MICROBE V. 8 248 2010
JRNL REFN ISSN 1931-3128
JRNL PMID 20833376
JRNL DOI 10.1016/J.CHOM.2010.08.006
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT 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) : 1.800
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.482
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.34
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.86
REMARK 3 NUMBER OF REFLECTIONS : 35141
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.1574
REMARK 3 R VALUE (WORKING SET) : 0.1558
REMARK 3 FREE R VALUE : 0.1874
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.0
REMARK 3 FREE R VALUE TEST SET COUNT : 1756
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 24.4845 - 4.2257 1.00 2728 151 0.1575 0.1712
REMARK 3 2 4.2257 - 3.3568 0.99 2666 131 0.1303 0.1655
REMARK 3 3 3.3568 - 2.9333 0.99 2621 146 0.1542 0.1858
REMARK 3 4 2.9333 - 2.6655 0.98 2607 135 0.1508 0.1963
REMARK 3 5 2.6655 - 2.4746 0.98 2600 138 0.1546 0.1959
REMARK 3 6 2.4746 - 2.3288 0.97 2565 137 0.1487 0.1814
REMARK 3 7 2.3288 - 2.2123 0.97 2554 142 0.1450 0.1791
REMARK 3 8 2.2123 - 2.1160 0.97 2533 139 0.1445 0.2015
REMARK 3 9 2.1160 - 2.0346 0.96 2545 115 0.1473 0.1658
REMARK 3 10 2.0346 - 1.9644 0.95 2491 129 0.1486 0.1913
REMARK 3 11 1.9644 - 1.9030 0.96 2533 128 0.1539 0.2054
REMARK 3 12 1.9030 - 1.8487 0.94 2463 139 0.1728 0.1914
REMARK 3 13 1.8487 - 1.8000 0.93 2479 126 0.2100 0.2844
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 : 0.366
REMARK 3 B_SOL : 57.894
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.31
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.24
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 30.39
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.1
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.6015
REMARK 3 B22 (A**2) : 1.6015
REMARK 3 B33 (A**2) : -3.2031
REMARK 3 B12 (A**2) : -0.0000
REMARK 3 B13 (A**2) : -0.0000
REMARK 3 B23 (A**2) : -0.0000
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 : 0.005 2300
REMARK 3 ANGLE : 0.931 3108
REMARK 3 CHIRALITY : 0.063 337
REMARK 3 PLANARITY : 0.004 405
REMARK 3 DIHEDRAL : 15.660 828
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 18
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN A AND RESID 1:14)
REMARK 3 ORIGIN FOR THE GROUP (A): 43.4717 -22.9068 6.5899
REMARK 3 T TENSOR
REMARK 3 T11: 0.4612 T22: 0.3595
REMARK 3 T33: 0.6405 T12: -0.2357
REMARK 3 T13: -0.1071 T23: 0.0608
REMARK 3 L TENSOR
REMARK 3 L11: 2.0359 L22: 5.4402
REMARK 3 L33: 2.8044 L12: 2.0048
REMARK 3 L13: -1.5261 L23: 1.2639
REMARK 3 S TENSOR
REMARK 3 S11: 0.0468 S12: 0.5799 S13: -0.4278
REMARK 3 S21: 1.2256 S22: -0.5864 S23: -1.3691
REMARK 3 S31: -1.2714 S32: 0.1146 S33: 0.8172
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN A AND RESID 15:29)
REMARK 3 ORIGIN FOR THE GROUP (A): 28.7404 -11.4715 4.7440
REMARK 3 T TENSOR
REMARK 3 T11: 0.5874 T22: 0.2021
REMARK 3 T33: 0.4411 T12: -0.0446
REMARK 3 T13: 0.1388 T23: -0.0252
REMARK 3 L TENSOR
REMARK 3 L11: 4.0056 L22: -1.6366
REMARK 3 L33: 1.3569 L12: 2.2023
REMARK 3 L13: 0.8577 L23: 1.0772
REMARK 3 S TENSOR
REMARK 3 S11: 0.3663 S12: -0.1571 S13: 1.0296
REMARK 3 S21: 0.1998 S22: -0.2299 S23: 0.3070
REMARK 3 S31: -0.4961 S32: -0.1128 S33: -0.0797
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN A AND RESID 30:45)
REMARK 3 ORIGIN FOR THE GROUP (A): 27.4403 -18.4287 -2.2514
REMARK 3 T TENSOR
REMARK 3 T11: 0.3961 T22: 0.2212
REMARK 3 T33: 0.2876 T12: -0.0127
REMARK 3 T13: 0.0778 T23: 0.0622
REMARK 3 L TENSOR
REMARK 3 L11: 1.7247 L22: 1.9118
REMARK 3 L33: 0.1027 L12: -0.9471
REMARK 3 L13: 0.0442 L23: -0.1182
REMARK 3 S TENSOR
REMARK 3 S11: -0.0868 S12: 0.2772 S13: -0.2254
REMARK 3 S21: -0.2230 S22: 0.0402 S23: 0.1692
REMARK 3 S31: -0.2040 S32: -0.0039 S33: 0.0312
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN A AND RESID 46:52)
REMARK 3 ORIGIN FOR THE GROUP (A): 35.7494 -25.6124 5.6862
REMARK 3 T TENSOR
REMARK 3 T11: 0.3210 T22: 0.3018
REMARK 3 T33: 0.2757 T12: -0.0936
REMARK 3 T13: 0.0449 T23: 0.0257
REMARK 3 L TENSOR
REMARK 3 L11: 3.9741 L22: 3.9525
REMARK 3 L33: 2.8932 L12: 1.8723
REMARK 3 L13: -1.1503 L23: -5.0118
REMARK 3 S TENSOR
REMARK 3 S11: -0.1948 S12: 0.5239 S13: -0.0539
REMARK 3 S21: 0.0366 S22: -0.1351 S23: -0.6505
REMARK 3 S31: -0.3575 S32: 0.5450 S33: 0.2776
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: (CHAIN A AND RESID 53:60)
REMARK 3 ORIGIN FOR THE GROUP (A): 27.6935 -20.2554 10.3625
REMARK 3 T TENSOR
REMARK 3 T11: 0.4635 T22: 0.3179
REMARK 3 T33: 0.3109 T12: -0.0445
REMARK 3 T13: 0.1236 T23: -0.0467
REMARK 3 L TENSOR
REMARK 3 L11: 5.8112 L22: 6.9662
REMARK 3 L33: 4.1186 L12: -2.4543
REMARK 3 L13: -2.1150 L23: 2.5718
REMARK 3 S TENSOR
REMARK 3 S11: -0.2231 S12: -0.7687 S13: 0.5398
REMARK 3 S21: 1.4475 S22: -0.0250 S23: 0.4816
REMARK 3 S31: -0.3538 S32: 0.2041 S33: 0.1201
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: (CHAIN A AND RESID 61:69)
REMARK 3 ORIGIN FOR THE GROUP (A): 16.9115 -21.7086 7.4965
REMARK 3 T TENSOR
REMARK 3 T11: 0.3412 T22: 0.3284
REMARK 3 T33: 0.5565 T12: 0.0240
REMARK 3 T13: 0.1903 T23: 0.0120
REMARK 3 L TENSOR
REMARK 3 L11: 3.4981 L22: 4.0327
REMARK 3 L33: 3.7206 L12: -2.2358
REMARK 3 L13: -4.2353 L23: 0.7333
REMARK 3 S TENSOR
REMARK 3 S11: 0.7864 S12: 0.3930 S13: 1.0540
REMARK 3 S21: 0.2230 S22: -0.1265 S23: 0.9789
REMARK 3 S31: -0.1259 S32: -0.9991 S33: -0.6273
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: (CHAIN A AND RESID 70:85)
REMARK 3 ORIGIN FOR THE GROUP (A): 21.0842 -37.9000 5.2292
REMARK 3 T TENSOR
REMARK 3 T11: 0.2347 T22: 0.2986
REMARK 3 T33: 0.2764 T12: -0.0559
REMARK 3 T13: 0.0221 T23: 0.0010
REMARK 3 L TENSOR
REMARK 3 L11: -0.4805 L22: 7.2978
REMARK 3 L33: 1.0687 L12: 1.5853
REMARK 3 L13: -0.4765 L23: -0.9843
REMARK 3 S TENSOR
REMARK 3 S11: -0.0837 S12: 0.0941 S13: -0.0579
REMARK 3 S21: 0.0437 S22: 0.1557 S23: 0.8639
REMARK 3 S31: 0.1671 S32: -0.3510 S33: -0.0642
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: (CHAIN A AND RESID 86:109)
REMARK 3 ORIGIN FOR THE GROUP (A): 31.6601 -42.6074 11.4796
REMARK 3 T TENSOR
REMARK 3 T11: 0.3335 T22: 0.3060
REMARK 3 T33: 0.2618 T12: -0.0372
REMARK 3 T13: 0.0374 T23: 0.0475
REMARK 3 L TENSOR
REMARK 3 L11: -0.1985 L22: 2.9527
REMARK 3 L33: -0.7823 L12: -0.5627
REMARK 3 L13: -0.0796 L23: 1.2942
REMARK 3 S TENSOR
REMARK 3 S11: -0.0305 S12: -0.2074 S13: -0.1126
REMARK 3 S21: 0.7342 S22: -0.0664 S23: -0.0004
REMARK 3 S31: 0.1022 S32: 0.0978 S33: 0.0765
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: (CHAIN A AND RESID 110:118)
REMARK 3 ORIGIN FOR THE GROUP (A): 41.0684 -35.1320 7.6854
REMARK 3 T TENSOR
REMARK 3 T11: 0.2041 T22: 0.3120
REMARK 3 T33: 0.4201 T12: -0.0728
REMARK 3 T13: -0.0269 T23: -0.0270
REMARK 3 L TENSOR
REMARK 3 L11: -4.3971 L22: 7.7166
REMARK 3 L33: 2.5416 L12: -1.6483
REMARK 3 L13: -3.4906 L23: 2.1686
REMARK 3 S TENSOR
REMARK 3 S11: 0.1832 S12: -0.0315 S13: -0.1844
REMARK 3 S21: -0.1505 S22: 0.1590 S23: -1.7432
REMARK 3 S31: 0.1733 S32: 0.7560 S33: -0.3026
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: (CHAIN A AND RESID 119:136)
REMARK 3 ORIGIN FOR THE GROUP (A): 26.3751 -29.1643 -0.7039
REMARK 3 T TENSOR
REMARK 3 T11: 0.2602 T22: 0.2234
REMARK 3 T33: 0.2389 T12: -0.0455
REMARK 3 T13: 0.0385 T23: 0.0280
REMARK 3 L TENSOR
REMARK 3 L11: -0.0498 L22: 1.3808
REMARK 3 L33: 0.1862 L12: -0.4217
REMARK 3 L13: 0.0406 L23: 0.5652
REMARK 3 S TENSOR
REMARK 3 S11: -0.0152 S12: 0.0409 S13: 0.0745
REMARK 3 S21: -0.3192 S22: 0.1018 S23: 0.0992
REMARK 3 S31: -0.1256 S32: -0.0909 S33: -0.0818
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: (CHAIN B AND RESID 2:42)
REMARK 3 ORIGIN FOR THE GROUP (A): 46.1666 -64.5887 0.4794
REMARK 3 T TENSOR
REMARK 3 T11: 0.2166 T22: 0.3197
REMARK 3 T33: 0.2482 T12: 0.0192
REMARK 3 T13: -0.0345 T23: 0.0164
REMARK 3 L TENSOR
REMARK 3 L11: -1.0731 L22: 0.9011
REMARK 3 L33: 1.9632 L12: -1.2260
REMARK 3 L13: 0.0952 L23: -0.2531
REMARK 3 S TENSOR
REMARK 3 S11: 0.1381 S12: 0.1231 S13: -0.1976
REMARK 3 S21: -0.0728 S22: -0.0895 S23: -0.2419
REMARK 3 S31: 0.1934 S32: 0.4533 S33: -0.0449
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: (CHAIN B AND RESID 43:65)
REMARK 3 ORIGIN FOR THE GROUP (A): 36.6696 -62.8791 5.4094
REMARK 3 T TENSOR
REMARK 3 T11: 0.2580 T22: 0.2089
REMARK 3 T33: 0.2447 T12: -0.0371
REMARK 3 T13: -0.0637 T23: 0.0279
REMARK 3 L TENSOR
REMARK 3 L11: 0.9995 L22: -0.1178
REMARK 3 L33: 0.6356 L12: -0.2469
REMARK 3 L13: 0.2871 L23: 0.4708
REMARK 3 S TENSOR
REMARK 3 S11: 0.1271 S12: -0.1340 S13: -0.1384
REMARK 3 S21: 0.0064 S22: -0.0459 S23: 0.0151
REMARK 3 S31: 0.0708 S32: -0.0438 S33: -0.0863
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: (CHAIN B AND RESID 66:79)
REMARK 3 ORIGIN FOR THE GROUP (A): 38.4237 -65.3979 14.5070
REMARK 3 T TENSOR
REMARK 3 T11: 0.2566 T22: 0.3316
REMARK 3 T33: 0.2633 T12: -0.1005
REMARK 3 T13: -0.0421 T23: 0.0394
REMARK 3 L TENSOR
REMARK 3 L11: -0.2585 L22: 0.3220
REMARK 3 L33: 1.4365 L12: -0.1509
REMARK 3 L13: -0.0280 L23: -0.2361
REMARK 3 S TENSOR
REMARK 3 S11: -0.0073 S12: -0.1239 S13: -0.2062
REMARK 3 S21: -0.0147 S22: 0.0925 S23: 0.0014
REMARK 3 S31: 0.1827 S32: -0.0884 S33: -0.0707
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: (CHAIN B AND RESID 80:85)
REMARK 3 ORIGIN FOR THE GROUP (A): 46.5584 -58.0831 17.7927
REMARK 3 T TENSOR
REMARK 3 T11: 0.3254 T22: 0.4171
REMARK 3 T33: 0.2589 T12: -0.1012
REMARK 3 T13: -0.0543 T23: 0.0383
REMARK 3 L TENSOR
REMARK 3 L11: 1.8823 L22: 2.3001
REMARK 3 L33: -0.1266 L12: 1.3604
REMARK 3 L13: 0.8637 L23: 0.6897
REMARK 3 S TENSOR
REMARK 3 S11: 0.0982 S12: -0.4194 S13: -0.0942
REMARK 3 S21: 0.5991 S22: -0.3796 S23: -0.1199
REMARK 3 S31: -0.2153 S32: 0.0953 S33: 0.2181
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: (CHAIN B AND RESID 86:117)
REMARK 3 ORIGIN FOR THE GROUP (A): 43.4762 -52.9226 6.6253
REMARK 3 T TENSOR
REMARK 3 T11: 0.2777 T22: 0.2614
REMARK 3 T33: 0.2457 T12: -0.0583
REMARK 3 T13: -0.0329 T23: 0.0208
REMARK 3 L TENSOR
REMARK 3 L11: 0.5200 L22: 0.2917
REMARK 3 L33: -0.5205 L12: -0.1911
REMARK 3 L13: -0.0826 L23: 0.0156
REMARK 3 S TENSOR
REMARK 3 S11: 0.1116 S12: -0.0029 S13: 0.0968
REMARK 3 S21: 0.0991 S22: -0.1596 S23: -0.0679
REMARK 3 S31: -0.0616 S32: 0.1064 S33: 0.0406
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: (CHAIN B AND RESID 118:126)
REMARK 3 ORIGIN FOR THE GROUP (A): 40.4610 -45.1229 5.4279
REMARK 3 T TENSOR
REMARK 3 T11: 0.2856 T22: 0.2426
REMARK 3 T33: 0.3146 T12: -0.0506
REMARK 3 T13: 0.0079 T23: -0.0017
REMARK 3 L TENSOR
REMARK 3 L11: 1.2396 L22: 0.5246
REMARK 3 L33: 2.7522 L12: -0.1461
REMARK 3 L13: -0.8699 L23: 1.2807
REMARK 3 S TENSOR
REMARK 3 S11: 0.3963 S12: -0.1244 S13: 0.1039
REMARK 3 S21: 0.2497 S22: 0.0152 S23: -0.3716
REMARK 3 S31: -0.4564 S32: 0.0988 S33: -0.3067
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: (CHAIN B AND RESID 127:144)
REMARK 3 ORIGIN FOR THE GROUP (A): 39.6530 -58.3713 -5.2308
REMARK 3 T TENSOR
REMARK 3 T11: 0.2588 T22: 0.2863
REMARK 3 T33: 0.2144 T12: -0.0021
REMARK 3 T13: -0.0395 T23: 0.0001
REMARK 3 L TENSOR
REMARK 3 L11: 0.0177 L22: 0.7069
REMARK 3 L33: -0.4244 L12: -0.1115
REMARK 3 L13: 0.0408 L23: -0.3134
REMARK 3 S TENSOR
REMARK 3 S11: 0.0999 S12: 0.0950 S13: -0.1189
REMARK 3 S21: -0.1897 S22: -0.1078 S23: -0.0834
REMARK 3 S31: -0.0115 S32: 0.1431 S33: 0.0219
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: (CHAIN B AND RESID 145:165)
REMARK 3 ORIGIN FOR THE GROUP (A): 32.7857 -64.4882 0.0579
REMARK 3 T TENSOR
REMARK 3 T11: 0.2470 T22: 0.2226
REMARK 3 T33: 0.2651 T12: 0.0019
REMARK 3 T13: -0.0487 T23: -0.0178
REMARK 3 L TENSOR
REMARK 3 L11: 1.2025 L22: 0.7805
REMARK 3 L33: 0.7863 L12: -0.3025
REMARK 3 L13: 0.5157 L23: -0.0862
REMARK 3 S TENSOR
REMARK 3 S11: 0.2848 S12: 0.1081 S13: -0.1854
REMARK 3 S21: -0.0687 S22: -0.1908 S23: 0.1771
REMARK 3 S31: 0.0710 S32: 0.0240 S33: -0.0859
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 2XGY COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 08-JUN-10.
REMARK 100 THE PDBE ID CODE IS EBI-44183.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 35238
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.80
REMARK 200 RESOLUTION RANGE LOW (A) : 25.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.8
REMARK 200 DATA REDUNDANCY : 21.2
REMARK 200 R MERGE (I) : 0.05
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 71.40
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 (%) : 94.1
REMARK 200 DATA REDUNDANCY IN SHELL : 11.8
REMARK 200 R MERGE FOR SHELL (I) : 0.60
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.40
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: NULL
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.07
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 16-26% PEG3350, 0.1M HEPES PH 7.5
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 16.55167
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 33.10333
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 24.82750
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 41.37917
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 8.27583
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1890 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13280 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -5.1 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 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 LEU A 4
REMARK 465 ARG A 5
REMARK 465 GLY A 6
REMARK 465 GLY A 7
REMARK 465 ARG A 8
REMARK 465 GLN A 9
REMARK 465 PHE A 62
REMARK 465 ALA A 63
REMARK 465 THR A 138
REMARK 465 ILE A 139
REMARK 465 SER A 140
REMARK 465 PRO A 141
REMARK 465 LEU A 142
REMARK 465 GLU A 143
REMARK 465 HIS A 144
REMARK 465 HIS A 145
REMARK 465 HIS A 146
REMARK 465 HIS A 147
REMARK 465 HIS A 148
REMARK 465 HIS A 149
REMARK 465 GLY B -7
REMARK 465 PRO B -6
REMARK 465 LEU B -5
REMARK 465 GLY B -4
REMARK 465 SER B -3
REMARK 465 PRO B -2
REMARK 465 GLU B -1
REMARK 465 PHE B 0
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 GLU A 10 CG CD OE1 OE2
REMARK 470 GLU A 110 CG CD OE1 OE2
REMARK 470 ARG A 137 CG CD NE CZ NH1 NH2
REMARK 470 MET B 1 CG SD CE
REMARK 470 LYS B 155 CD CE NZ
REMARK 470 GLU B 165 CG CD OE1 OE2
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 90 -8.52 85.65
REMARK 500 PHE B 60 -77.66 -131.62
REMARK 500 LYS B 133 -74.87 -101.96
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1138
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B1166
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1VBS RELATED DB: PDB
REMARK 900 STRUCTURE OF CYCLOPHILIN COMPLEXED WITH (D)
REMARK 900 ALA CONTAINING TETRAPEPTIDE
REMARK 900 RELATED ID: 1OCA RELATED DB: PDB
REMARK 900 HUMAN CYCLOPHILIN A, UNLIGATED, NMR, 20
REMARK 900 STRUCTURES
REMARK 900 RELATED ID: 1MF8 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN CALCINEURIN
REMARK 900 COMPLEXED WITHCYCLOSPORIN A AND HUMAN
REMARK 900 CYCLOPHILIN
REMARK 900 RELATED ID: 2CYH RELATED DB: PDB
REMARK 900 CYCLOPHILIN A COMPLEXED WITH DIPEPTIDE ALA-
REMARK 900 PRO
REMARK 900 RELATED ID: 1CWB RELATED DB: PDB
REMARK 900 MOL_ID: 1; MOLECULE: CYCLOPHILIN A; CHAIN: A
REMARK 900 ; ENGINEERED: YES; MOL_ID: 2; MOLECULE: [4
REMARK 900 -[(E)-2-BUTENYL]-4,4,N-TRIMETHYL-L-
REMARK 900 THREONINE]1- CYCLOSPORIN; CHAIN: C; ENGINEERED
REMARK 900 : YES
REMARK 900 RELATED ID: 1VBT RELATED DB: PDB
REMARK 900 STRUCTURE OF CYCLOPHILIN COMPLEXED WITH SULFUR
REMARK 900 -SUBSTITUTED TETRAPEPTIDE AAPF
REMARK 900 RELATED ID: 1CWL RELATED DB: PDB
REMARK 900 HUMAN CYCLOPHILIN A COMPLEXED WITH 4 4-
REMARK 900 HYDROXY-MELEU CYCLOSPORIN
REMARK 900 RELATED ID: 1M9E RELATED DB: PDB
REMARK 900 X-RAY CRYSTAL STRUCTURE OF CYCLOPHILIN A/
REMARK 900 HIV-1 CA N-TERMINAL DOMAIN (1-146) M-
REMARK 900 TYPE H87A COMPLEX.
REMARK 900 RELATED ID: 1CWC RELATED DB: PDB
REMARK 900 MOL_ID: 1; MOLECULE: CYCLOPHILIN A; CHAIN: A
REMARK 900 ; ENGINEERED: YES; MOL_ID: 2; MOLECULE: [4,
REMARK 900 N-DIMETHYLNORLEUCINE]4-CYCLOSPORIN; CHAIN: C
REMARK 900 ; ENGINEERED: YES
REMARK 900 RELATED ID: 1CWO RELATED DB: PDB
REMARK 900 HUMAN CYCLOPHILIN A COMPLEXED WITH THR2,
REMARK 900 LEU5, D-HIV8, LEU10 CYCLOSPORIN
REMARK 900 RELATED ID: 1CWI RELATED DB: PDB
REMARK 900 HUMAN CYCLOPHILIN A COMPLEXED WITH 2-VAL 3
REMARK 900 -(N-METHYL)-D-ALANINE CYCLOSPORIN
REMARK 900 RELATED ID: 2X2C RELATED DB: PDB
REMARK 900 ACETYL-CYPA:CYCLOSPORINE COMPLEX
REMARK 900 RELATED ID: 1RMH RELATED DB: PDB
REMARK 900 RECOMBINANT CYCLOPHILIN A FROM HUMAN T CELL
REMARK 900 RELATED ID: 1CWJ RELATED DB: PDB
REMARK 900 HUMAN CYCLOPHILIN A COMPLEXED WITH 2-VAL 3
REMARK 900 -S-METHYL-SARCOSINE CYCLOSPORIN
REMARK 900 RELATED ID: 2RMB RELATED DB: PDB
REMARK 900 CYCLOPHILIN A COMPLEXED WITH DIMETHYL-
REMARK 900 CYCLOSPORIN A
REMARK 900 RELATED ID: 1M9C RELATED DB: PDB
REMARK 900 X-RAY CRYSTAL STRUCTURE OF CYCLOPHILIN A/
REMARK 900 HIV-1 CA N-TERMINAL DOMAIN (1-146) M-
REMARK 900 TYPE COMPLEX.
REMARK 900 RELATED ID: 1CWA RELATED DB: PDB
REMARK 900 MOL_ID: 1; MOLECULE: CYCLOPHILIN A; CHAIN: A
REMARK 900 ; ENGINEERED: YES; MOL_ID: 2; MOLECULE:
REMARK 900 CYCLOSPORIN A; CHAIN: C; ENGINEERED: YES
REMARK 900 RELATED ID: 1CWF RELATED DB: PDB
REMARK 900 HUMAN CYCLOPHILIN A COMPLEXED WITH 2-VAL
REMARK 900 CYCLOSPORIN
REMARK 900 RELATED ID: 3CYH RELATED DB: PDB
REMARK 900 CYCLOPHILIN A COMPLEXED WITH DIPEPTIDE SER-
REMARK 900 PRO
REMARK 900 RELATED ID: 1M9Y RELATED DB: PDB
REMARK 900 X-RAY CRYSTAL STRUCTURE OF CYCLOPHILIN A/
REMARK 900 HIV-1 CA N-TERMINAL DOMAIN (1-146) M-
REMARK 900 TYPE H87A,G89A COMPLEX.
REMARK 900 RELATED ID: 4CYH RELATED DB: PDB
REMARK 900 CYCLOPHILIN A COMPLEXED WITH DIPEPTIDE HIS-
REMARK 900 PRO
REMARK 900 RELATED ID: 1M9F RELATED DB: PDB
REMARK 900 X-RAY CRYSTAL STRUCTURE OF CYCLOPHILIN A/
REMARK 900 HIV-1 CA N-TERMINAL DOMAIN (1-146) M-
REMARK 900 TYPE H87A,A88M COMPLEX.
REMARK 900 RELATED ID: 1CWH RELATED DB: PDB
REMARK 900 HUMAN CYCLOPHILIN A COMPLEXED WITH 3-D-SER
REMARK 900 CYCLOSPORIN
REMARK 900 RELATED ID: 1BCK RELATED DB: PDB
REMARK 900 HUMAN CYCLOPHILIN A COMPLEXED WITH 2-THR
REMARK 900 CYCLOSPORIN
REMARK 900 RELATED ID: 1W8V RELATED DB: PDB
REMARK 900 ENZYMATIC AND STRUCTURAL CHARACTERIZATION OF
REMARK 900 NON PEPTIDE LIGAND CYCLOPHILIN COMPLEXES
REMARK 900 RELATED ID: 1AWR RELATED DB: PDB
REMARK 900 CYPA COMPLEXED WITH HAGPIA
REMARK 900 RELATED ID: 1NMK RELATED DB: PDB
REMARK 900 THE SANGLIFEHRIN-CYCLOPHILIN INTERACTION:
REMARK 900 DEGRADATION WORK,SYNTHETIC MACROCYCLIC ANALOGUES
REMARK 900 , X-RAY CRYSTAL STRUCTUREAND BINDING DATA
REMARK 900 RELATED ID: 1MIK RELATED DB: PDB
REMARK 900 MOL_ID: 1; MOLECULE: CYCLOPHILIN A; CHAIN: A
REMARK 900 ; ENGINEERED: YES; MOL_ID: 2; MOLECULE: [(5-
REMARK 900 HYDROXY)NORVALINE2]-CYCLOSPORIN; CHAIN: B;
REMARK 900 ENGINEERED: YES
REMARK 900 RELATED ID: 1AWV RELATED DB: PDB
REMARK 900 CYPA COMPLEXED WITH HVGPIA
REMARK 900 RELATED ID: 1M9D RELATED DB: PDB
REMARK 900 X-RAY CRYSTAL STRUCTURE OF CYCLOPHILIN A/
REMARK 900 HIV-1 CA N-TERMINAL DOMAIN (1-146) O-
REMARK 900 TYPE CHIMERA COMPLEX.
REMARK 900 RELATED ID: 1AWT RELATED DB: PDB
REMARK 900 SECYPA COMPLEXED WITH HAGPIA
REMARK 900 RELATED ID: 2CPL RELATED DB: PDB
REMARK 900 CYCLOPHILIN A
REMARK 900 RELATED ID: 1FGL RELATED DB: PDB
REMARK 900 CYCLOPHILIN A COMPLEXED WITH A FRAGMENT OF
REMARK 900 HIV-1 GAGPROTEIN
REMARK 900 RELATED ID: 2X2A RELATED DB: PDB
REMARK 900 FREE ACETYL-CYPA TRIGONAL FORM
REMARK 900 RELATED ID: 1M9X RELATED DB: PDB
REMARK 900 X-RAY CRYSTAL STRUCTURE OF CYCLOPHILIN A/
REMARK 900 HIV-1 CA N-TERMINAL DOMAIN (1-146) M-
REMARK 900 TYPE H87A,A88M,G89A COMPLEX.
REMARK 900 RELATED ID: 1CWK RELATED DB: PDB
REMARK 900 HUMAN CYCLOPHILIN A COMPLEXED WITH 1-(6,7
REMARK 900 -DIHYDRO)MEBMT 2-VAL 3-D-(2-S-METHYL)
REMARK 900 SARCOSINE CYCLOSPORIN
REMARK 900 RELATED ID: 1M63 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CALCINEURIN-CYCLOPHILIN-
REMARK 900 CYCLOSPORINSHOWS COMMON BUT DISTINCT RECOGNITION
REMARK 900 OF IMMUNOPHILIN-DRUGCOMPLEXES
REMARK 900 RELATED ID: 5CYH RELATED DB: PDB
REMARK 900 CYCLOPHILIN A COMPLEXED WITH DIPEPTIDE GLY-
REMARK 900 PRO
REMARK 900 RELATED ID: 2X2D RELATED DB: PDB
REMARK 900 ACETYL-CYPA:HIV-1 N-TERM CAPSID DOMAIN
REMARK 900 COMPLEX
REMARK 900 RELATED ID: 1AK4 RELATED DB: PDB
REMARK 900 HUMAN CYCLOPHILIN A BOUND TO THE AMINO-
REMARK 900 TERMINAL DOMAIN OF HIV-1 CAPSID
REMARK 900 RELATED ID: 1AWS RELATED DB: PDB
REMARK 900 SECYPA COMPLEXED WITH HAGPIA (PSEUDO-SYMMETRIC
REMARK 900 MONOMER)
REMARK 900 RELATED ID: 2ALF RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN CYPA MUTANT K131A
REMARK 900 RELATED ID: 3CYS RELATED DB: PDB
REMARK 900 CYCLOPHILIN A COMPLEXED WITH CYCLOSPORIN A (
REMARK 900 NMR, 22 STRUCTURES)
REMARK 900 RELATED ID: 1W8L RELATED DB: PDB
REMARK 900 ENZYMATIC AND STRUCTURAL CHARACTERIZATION OF
REMARK 900 NON PEPTIDE LIGAND CYCLOPHILIN COMPLEXES
REMARK 900 RELATED ID: 2X25 RELATED DB: PDB
REMARK 900 FREE ACETYL-CYPA ORTHORHOMBIC FORM
REMARK 900 RELATED ID: 1W8M RELATED DB: PDB
REMARK 900 ENZYMATIC AND STRUCTURAL CHARACTERISATION OF
REMARK 900 NON PEPTIDE LIGAND CYCLOPHILIN COMPLEXES
REMARK 900 RELATED ID: 1AWU RELATED DB: PDB
REMARK 900 CYPA COMPLEXED WITH HVGPIA (PSEUDO-SYMMETRIC
REMARK 900 MONOMER)
REMARK 900 RELATED ID: 2RMA RELATED DB: PDB
REMARK 900 CYCLOPHILIN A COMPLEXED WITH CYCLOSPORIN A
REMARK 900 RELATED ID: 1CWM RELATED DB: PDB
REMARK 900 HUMAN CYCLOPHILIN A COMPLEXED WITH 4 MEILE
REMARK 900 CYCLOSPORIN
REMARK 900 RELATED ID: 1AWQ RELATED DB: PDB
REMARK 900 CYPA COMPLEXED WITH HAGPIA (PSEUDO-SYMMETRIC
REMARK 900 MONOMER)
REMARK 900 RELATED ID: 2XGU RELATED DB: PDB
REMARK 900 STRUCTURE OF THE N-TERMINAL DOMAIN OF
REMARK 900 CAPSID PROTEIN FROM RABBIT ENDOGENOUS
REMARK 900 LENTIVIRUS (RELIK)
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 RESIDUES 141-149 ARE AN EXPRESSION TAG.
DBREF 2XGY A 1 140 PDB 2XGY 2XGY 1 140
DBREF 2XGY A 141 149 PDB 2XGY 2XGY 141 149
DBREF 2XGY B 1 165 UNP P62937 PPIA_HUMAN 1 165
SEQADV 2XGY GLY B -7 UNP P62937 EXPRESSION TAG
SEQADV 2XGY PRO B -6 UNP P62937 EXPRESSION TAG
SEQADV 2XGY LEU B -5 UNP P62937 EXPRESSION TAG
SEQADV 2XGY GLY B -4 UNP P62937 EXPRESSION TAG
SEQADV 2XGY SER B -3 UNP P62937 EXPRESSION TAG
SEQADV 2XGY PRO B -2 UNP P62937 EXPRESSION TAG
SEQADV 2XGY GLU B -1 UNP P62937 EXPRESSION TAG
SEQADV 2XGY PHE B 0 UNP P62937 EXPRESSION TAG
SEQRES 1 A 149 PRO ILE MET LEU ARG GLY GLY ARG GLN GLU TYR GLU PRO
SEQRES 2 A 149 VAL GLY PRO GLY LEU ILE ALA ALA TRP LEU LYS GLN VAL
SEQRES 3 A 149 GLN GLU HIS GLY LEU THR HIS PRO ALA THR ILE THR TYR
SEQRES 4 A 149 PHE GLY VAL ILE SER ILE ASN PHE THR SER VAL ASP ILE
SEQRES 5 A 149 ASN MET LEU LEU ASN VAL THR PRO GLY PHE ALA ALA GLU
SEQRES 6 A 149 LYS GLN LEU VAL ILE ASP LYS ILE LYS GLU LYS ALA ILE
SEQRES 7 A 149 ALA TRP ASP GLU MET HIS PRO PRO PRO PRO ALA ASP ALA
SEQRES 8 A 149 ALA GLY PRO VAL PRO LEU THR SER ASP GLN ILE ARG GLY
SEQRES 9 A 149 ILE GLY LEU SER PRO GLU GLU ALA ALA GLY PRO ARG PHE
SEQRES 10 A 149 ALA ASP ALA ARG THR LEU TYR ARG THR TRP VAL LEU GLU
SEQRES 11 A 149 ALA LEU GLN GLU CYS GLN ARG THR ILE SER PRO LEU GLU
SEQRES 12 A 149 HIS HIS HIS HIS HIS HIS
SEQRES 1 B 173 GLY PRO LEU GLY SER PRO GLU PHE MET VAL ASN PRO THR
SEQRES 2 B 173 VAL PHE PHE ASP ILE ALA VAL ASP GLY GLU PRO LEU GLY
SEQRES 3 B 173 ARG VAL SER PHE GLU LEU PHE ALA ASP LYS VAL PRO LYS
SEQRES 4 B 173 THR ALA GLU ASN PHE ARG ALA LEU SER THR GLY GLU LYS
SEQRES 5 B 173 GLY PHE GLY TYR LYS GLY SER CYS PHE HIS ARG ILE ILE
SEQRES 6 B 173 PRO GLY PHE MET CYS GLN GLY GLY ASP PHE THR ARG HIS
SEQRES 7 B 173 ASN GLY THR GLY GLY LYS SER ILE TYR GLY GLU LYS PHE
SEQRES 8 B 173 GLU ASP GLU ASN PHE ILE LEU LYS HIS THR GLY PRO GLY
SEQRES 9 B 173 ILE LEU SER MET ALA ASN ALA GLY PRO ASN THR ASN GLY
SEQRES 10 B 173 SER GLN PHE PHE ILE CYS THR ALA LYS THR GLU TRP LEU
SEQRES 11 B 173 ASP GLY LYS HIS VAL VAL PHE GLY LYS VAL LYS GLU GLY
SEQRES 12 B 173 MET ASN ILE VAL GLU ALA MET GLU ARG PHE GLY SER ARG
SEQRES 13 B 173 ASN GLY LYS THR SER LYS LYS ILE THR ILE ALA ASP CYS
SEQRES 14 B 173 GLY GLN LEU GLU
HET GOL A1138 6
HET GOL B1166 6
HETNAM GOL GLYCEROL
FORMUL 3 GOL 2(C3 H8 O3)
FORMUL 4 HOH *367(H2 O)
HELIX 1 1 GLY A 15 GLY A 30 1 16
HELIX 2 2 HIS A 33 SER A 44 1 12
HELIX 3 3 THR A 48 THR A 59 1 12
HELIX 4 4 ALA A 64 HIS A 84 1 21
HELIX 5 5 THR A 98 ARG A 103 1 6
HELIX 6 6 SER A 108 ALA A 113 1 6
HELIX 7 7 GLY A 114 ARG A 116 5 3
HELIX 8 8 PHE A 117 CYS A 135 1 19
HELIX 9 9 VAL B 29 GLY B 42 1 14
HELIX 10 10 THR B 119 ASP B 123 5 5
HELIX 11 11 GLY B 135 ARG B 144 1 10
SHEET 1 BA 8 ARG B 55 ILE B 57 0
SHEET 2 BA 8 MET B 61 GLY B 64 -1 O MET B 61 N ILE B 57
SHEET 3 BA 8 PHE B 112 CYS B 115 -1 O PHE B 112 N GLY B 64
SHEET 4 BA 8 ILE B 97 MET B 100 -1 O ILE B 97 N CYS B 115
SHEET 5 BA 8 VAL B 128 VAL B 132 -1 N PHE B 129 O LEU B 98
SHEET 6 BA 8 GLU B 15 LEU B 24 -1 O GLU B 23 N LYS B 131
SHEET 7 BA 8 THR B 5 VAL B 12 -1 O VAL B 6 N PHE B 22
SHEET 8 BA 8 ILE B 156 LEU B 164 -1 O THR B 157 N ALA B 11
CISPEP 1 GLY A 93 PRO A 94 0 18.86
SITE 1 AC1 7 ASN A 53 ASN A 57 ILE A 70 ILE A 73
SITE 2 AC1 7 ARG A 103 TYR A 124 HOH A2136
SITE 1 AC2 8 HIS A 84 ASP A 90 HOH A2100 GLY B 59
SITE 2 AC2 8 PHE B 60 TRP B 121 HOH B2229 HOH B2230
CRYST1 117.158 117.158 49.655 90.00 90.00 120.00 P 61 6
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 0.008535 0.004928 0.000000 0.00000
SCALE2 0.000000 0.009856 0.000000 0.00000
SCALE3 0.000000 0.000000 0.020139 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
