HEADER IMMUNE SYSTEM 15-JUL-15 5CKG
TITLE HUMAN BETA-2 MICROGLOBULIN MUTANT V85E
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BETA-2-MICROGLOBULIN;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RESIDUES 21-119;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: B2M, CDABP0092, HDCMA22P;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET29B
KEYWDS AGGREGATION PROPENSITY, AMYLOID, BETA-SANDWITCH, FOLD STABILITY,
KEYWDS 2 IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR B.M.SALA,M.DE ROSA,M.BOLOGNESI,S.RICAGNO
REVDAT 2 10-JAN-24 5CKG 1 REMARK
REVDAT 1 18-MAY-16 5CKG 0
JRNL AUTH C.CAMILLONI,B.M.SALA,P.SORMANNI,R.PORCARI,A.CORAZZA,
JRNL AUTH 2 M.DE ROSA,S.ZANINI,A.BARBIROLI,G.ESPOSITO,M.BOLOGNESI,
JRNL AUTH 3 V.BELLOTTI,M.VENDRUSCOLO,S.RICAGNO
JRNL TITL RATIONAL DESIGN OF MUTATIONS THAT CHANGE THE AGGREGATION
JRNL TITL 2 RATE OF A PROTEIN WHILE MAINTAINING ITS NATIVE STRUCTURE AND
JRNL TITL 3 STABILITY.
JRNL REF SCI REP V. 6 25559 2016
JRNL REFN ESSN 2045-2322
JRNL PMID 27150430
JRNL DOI 10.1038/SREP25559
REMARK 2
REMARK 2 RESOLUTION. 1.75 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.8.4_1496
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 27.71
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.3
REMARK 3 NUMBER OF REFLECTIONS : 20722
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.188
REMARK 3 R VALUE (WORKING SET) : 0.183
REMARK 3 FREE R VALUE : 0.232
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.630
REMARK 3 FREE R VALUE TEST SET COUNT : 1995
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 27.7127 - 4.2131 0.96 1411 150 0.1643 0.1979
REMARK 3 2 4.2131 - 3.3459 0.96 1370 147 0.1538 0.2198
REMARK 3 3 3.3459 - 2.9235 0.97 1341 142 0.1809 0.2354
REMARK 3 4 2.9235 - 2.6564 0.97 1361 145 0.1985 0.2355
REMARK 3 5 2.6564 - 2.4662 0.97 1337 143 0.2057 0.2304
REMARK 3 6 2.4662 - 2.3208 0.98 1357 145 0.1989 0.2667
REMARK 3 7 2.3208 - 2.2047 0.94 1286 137 0.1978 0.2797
REMARK 3 8 2.2047 - 2.1087 0.97 1341 142 0.1911 0.2787
REMARK 3 9 2.1087 - 2.0276 0.97 1336 143 0.1962 0.2244
REMARK 3 10 2.0276 - 1.9576 0.97 1346 145 0.1944 0.2351
REMARK 3 11 1.9576 - 1.8964 0.95 1301 139 0.1956 0.2414
REMARK 3 12 1.8964 - 1.8422 0.94 1285 137 0.2150 0.2819
REMARK 3 13 1.8422 - 1.7937 0.97 1314 138 0.2468 0.2554
REMARK 3 14 1.7937 - 1.7500 0.96 1341 142 0.2792 0.3226
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.210
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.270
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.018 1825
REMARK 3 ANGLE : 1.789 2495
REMARK 3 CHIRALITY : 0.095 264
REMARK 3 PLANARITY : 0.009 328
REMARK 3 DIHEDRAL : 14.321 697
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 0 THROUGH 11 )
REMARK 3 ORIGIN FOR THE GROUP (A): 14.8261 7.2752 0.2253
REMARK 3 T TENSOR
REMARK 3 T11: 0.3370 T22: 0.2532
REMARK 3 T33: 0.2174 T12: 0.0381
REMARK 3 T13: 0.0428 T23: 0.0295
REMARK 3 L TENSOR
REMARK 3 L11: 6.0814 L22: 4.8299
REMARK 3 L33: 4.9578 L12: 4.0012
REMARK 3 L13: -5.0995 L23: -3.6658
REMARK 3 S TENSOR
REMARK 3 S11: 0.1650 S12: 0.4150 S13: 0.1519
REMARK 3 S21: -0.1353 S22: 0.1636 S23: 0.0046
REMARK 3 S31: -0.3783 S32: -0.5392 S33: -0.3944
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 12 THROUGH 19 )
REMARK 3 ORIGIN FOR THE GROUP (A): -6.8371 -2.5125 13.5967
REMARK 3 T TENSOR
REMARK 3 T11: 0.2820 T22: 0.9004
REMARK 3 T33: 0.8162 T12: 0.0866
REMARK 3 T13: 0.2734 T23: 0.4344
REMARK 3 L TENSOR
REMARK 3 L11: 7.3070 L22: 1.7610
REMARK 3 L33: 2.0223 L12: -1.1469
REMARK 3 L13: -3.8492 L23: -2.2594
REMARK 3 S TENSOR
REMARK 3 S11: 0.5230 S12: -0.7219 S13: 0.4631
REMARK 3 S21: 0.5125 S22: 0.8309 S23: 1.9455
REMARK 3 S31: 1.5183 S32: -1.8381 S33: 0.4752
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 20 THROUGH 35 )
REMARK 3 ORIGIN FOR THE GROUP (A): 10.6651 0.0410 3.8551
REMARK 3 T TENSOR
REMARK 3 T11: 0.2413 T22: 0.2070
REMARK 3 T33: 0.1408 T12: -0.0301
REMARK 3 T13: 0.0099 T23: -0.0069
REMARK 3 L TENSOR
REMARK 3 L11: 6.5201 L22: 4.6644
REMARK 3 L33: 8.3999 L12: 2.4432
REMARK 3 L13: -6.1040 L23: -4.3703
REMARK 3 S TENSOR
REMARK 3 S11: -0.2211 S12: 0.7602 S13: -0.0289
REMARK 3 S21: -0.1321 S22: 0.4524 S23: 0.1072
REMARK 3 S31: 0.2244 S32: -1.0477 S33: -0.2205
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 36 THROUGH 50 )
REMARK 3 ORIGIN FOR THE GROUP (A): 11.9042 -5.1428 15.3734
REMARK 3 T TENSOR
REMARK 3 T11: 0.4083 T22: 0.3359
REMARK 3 T33: 0.3114 T12: 0.0048
REMARK 3 T13: -0.0099 T23: 0.0591
REMARK 3 L TENSOR
REMARK 3 L11: 8.2339 L22: 5.9545
REMARK 3 L33: 4.6333 L12: 1.7999
REMARK 3 L13: -5.3712 L23: -1.4790
REMARK 3 S TENSOR
REMARK 3 S11: -0.2069 S12: -0.7004 S13: -0.9536
REMARK 3 S21: -0.0680 S22: -0.3003 S23: -0.1722
REMARK 3 S31: 1.2384 S32: 0.6819 S33: 0.3652
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 51 THROUGH 71 )
REMARK 3 ORIGIN FOR THE GROUP (A): 10.3379 -2.4663 0.0144
REMARK 3 T TENSOR
REMARK 3 T11: 0.3906 T22: 0.4553
REMARK 3 T33: 0.3056 T12: -0.0572
REMARK 3 T13: -0.0251 T23: 0.0136
REMARK 3 L TENSOR
REMARK 3 L11: 4.1828 L22: 6.8465
REMARK 3 L33: 5.4869 L12: 2.9061
REMARK 3 L13: -4.2253 L23: -5.0568
REMARK 3 S TENSOR
REMARK 3 S11: -0.6248 S12: 1.1455 S13: -0.5086
REMARK 3 S21: -0.7810 S22: 0.5674 S23: -0.0012
REMARK 3 S31: 0.9857 S32: -1.5096 S33: 0.1250
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 72 THROUGH 83 )
REMARK 3 ORIGIN FOR THE GROUP (A): 6.8196 1.2482 17.8662
REMARK 3 T TENSOR
REMARK 3 T11: 0.3622 T22: 0.4676
REMARK 3 T33: 0.2703 T12: 0.1113
REMARK 3 T13: 0.0653 T23: 0.0520
REMARK 3 L TENSOR
REMARK 3 L11: 7.5593 L22: 3.7284
REMARK 3 L33: 7.2542 L12: 1.4216
REMARK 3 L13: -5.1174 L23: -0.7486
REMARK 3 S TENSOR
REMARK 3 S11: -0.2138 S12: -1.1234 S13: -0.0974
REMARK 3 S21: 0.4207 S22: 0.1072 S23: 0.3544
REMARK 3 S31: -0.3120 S32: -0.3395 S33: -0.0599
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 84 THROUGH 90 )
REMARK 3 ORIGIN FOR THE GROUP (A): 22.3704 8.2474 8.4635
REMARK 3 T TENSOR
REMARK 3 T11: 0.4557 T22: 0.2209
REMARK 3 T33: 0.2545 T12: -0.0687
REMARK 3 T13: 0.0762 T23: -0.0233
REMARK 3 L TENSOR
REMARK 3 L11: 8.6940 L22: 3.6699
REMARK 3 L33: 2.9786 L12: 4.5217
REMARK 3 L13: -2.2928 L23: -2.9994
REMARK 3 S TENSOR
REMARK 3 S11: 0.2118 S12: -0.8019 S13: -0.1007
REMARK 3 S21: 0.8078 S22: -0.4647 S23: 0.2163
REMARK 3 S31: -0.3563 S32: 0.2507 S33: -0.0900
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 91 THROUGH 99 )
REMARK 3 ORIGIN FOR THE GROUP (A): 4.1503 7.0623 14.4056
REMARK 3 T TENSOR
REMARK 3 T11: 0.5088 T22: 0.4128
REMARK 3 T33: 0.4898 T12: 0.1177
REMARK 3 T13: 0.1078 T23: -0.0267
REMARK 3 L TENSOR
REMARK 3 L11: 4.5347 L22: 5.9403
REMARK 3 L33: 4.4092 L12: 4.2833
REMARK 3 L13: -4.1498 L23: -3.0101
REMARK 3 S TENSOR
REMARK 3 S11: 0.0461 S12: 0.5767 S13: 2.5245
REMARK 3 S21: 0.5718 S22: 0.9125 S23: 1.4065
REMARK 3 S31: -1.2551 S32: -1.4709 S33: -0.4316
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 0 THROUGH 11 )
REMARK 3 ORIGIN FOR THE GROUP (A): 29.5223 19.3515 -40.1714
REMARK 3 T TENSOR
REMARK 3 T11: 0.1987 T22: 0.1215
REMARK 3 T33: 0.2179 T12: 0.0445
REMARK 3 T13: -0.0376 T23: -0.0118
REMARK 3 L TENSOR
REMARK 3 L11: 4.1598 L22: 3.2323
REMARK 3 L33: 6.1443 L12: 4.4203
REMARK 3 L13: -2.9761 L23: -2.5532
REMARK 3 S TENSOR
REMARK 3 S11: 0.3745 S12: -0.1562 S13: 0.3016
REMARK 3 S21: 0.1000 S22: -0.1594 S23: 0.0683
REMARK 3 S31: -0.2856 S32: -0.0491 S33: -0.1245
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 12 THROUGH 19 )
REMARK 3 ORIGIN FOR THE GROUP (A): 7.5659 11.1292 -29.6757
REMARK 3 T TENSOR
REMARK 3 T11: 0.2213 T22: 0.6615
REMARK 3 T33: 0.3188 T12: -0.0125
REMARK 3 T13: 0.0121 T23: -0.0481
REMARK 3 L TENSOR
REMARK 3 L11: 4.1488 L22: 8.8091
REMARK 3 L33: 6.7661 L12: -1.1527
REMARK 3 L13: -2.1084 L23: -2.0153
REMARK 3 S TENSOR
REMARK 3 S11: 0.0968 S12: -0.8481 S13: 0.2412
REMARK 3 S21: 0.6161 S22: -0.0633 S23: 0.7257
REMARK 3 S31: -0.0087 S32: -0.8123 S33: -0.0592
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 20 THROUGH 35 )
REMARK 3 ORIGIN FOR THE GROUP (A): 25.4233 12.3459 -38.1375
REMARK 3 T TENSOR
REMARK 3 T11: 0.1756 T22: 0.2106
REMARK 3 T33: 0.1699 T12: -0.0164
REMARK 3 T13: -0.0490 T23: -0.0219
REMARK 3 L TENSOR
REMARK 3 L11: 9.6838 L22: 1.8911
REMARK 3 L33: 2.2436 L12: 1.4858
REMARK 3 L13: -2.8129 L23: -0.4016
REMARK 3 S TENSOR
REMARK 3 S11: -0.0417 S12: -0.1936 S13: -0.2492
REMARK 3 S21: 0.1035 S22: -0.0018 S23: -0.1560
REMARK 3 S31: 0.0453 S32: -0.3198 S33: 0.0702
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 36 THROUGH 41 )
REMARK 3 ORIGIN FOR THE GROUP (A): 28.1619 9.5737 -28.6991
REMARK 3 T TENSOR
REMARK 3 T11: 0.2658 T22: 0.3803
REMARK 3 T33: 0.2287 T12: -0.0076
REMARK 3 T13: -0.0935 T23: 0.0344
REMARK 3 L TENSOR
REMARK 3 L11: 5.9700 L22: 3.0086
REMARK 3 L33: 3.1100 L12: 2.8984
REMARK 3 L13: -3.9222 L23: -2.9152
REMARK 3 S TENSOR
REMARK 3 S11: 0.1337 S12: -0.9679 S13: 0.0028
REMARK 3 S21: 0.0575 S22: -0.0780 S23: -0.0127
REMARK 3 S31: 0.1789 S32: 0.0096 S33: -0.0107
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 42 THROUGH 50 )
REMARK 3 ORIGIN FOR THE GROUP (A): 24.6415 4.0858 -26.0297
REMARK 3 T TENSOR
REMARK 3 T11: 0.7528 T22: 0.5640
REMARK 3 T33: 0.5508 T12: -0.0166
REMARK 3 T13: 0.0629 T23: 0.0707
REMARK 3 L TENSOR
REMARK 3 L11: 2.0630 L22: 8.4601
REMARK 3 L33: 3.3012 L12: -0.9624
REMARK 3 L13: -0.3083 L23: 4.6956
REMARK 3 S TENSOR
REMARK 3 S11: -0.2447 S12: -1.0754 S13: -2.3197
REMARK 3 S21: -0.0051 S22: -0.3164 S23: 0.3355
REMARK 3 S31: 1.6695 S32: -0.1102 S33: 0.5172
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 51 THROUGH 60 )
REMARK 3 ORIGIN FOR THE GROUP (A): 29.1399 11.1250 -48.0717
REMARK 3 T TENSOR
REMARK 3 T11: 0.2634 T22: 0.2836
REMARK 3 T33: 0.1875 T12: -0.0254
REMARK 3 T13: -0.0498 T23: -0.0177
REMARK 3 L TENSOR
REMARK 3 L11: 8.8853 L22: 9.8595
REMARK 3 L33: 3.1392 L12: 4.7383
REMARK 3 L13: -4.4279 L23: -3.4033
REMARK 3 S TENSOR
REMARK 3 S11: -0.4063 S12: 0.4568 S13: -0.1064
REMARK 3 S21: -0.8507 S22: 0.0301 S23: 0.1223
REMARK 3 S31: 0.2945 S32: -0.0208 S33: 0.3732
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 61 THROUGH 71 )
REMARK 3 ORIGIN FOR THE GROUP (A): 21.8502 8.7582 -37.2922
REMARK 3 T TENSOR
REMARK 3 T11: 0.1854 T22: 0.2602
REMARK 3 T33: 0.1838 T12: -0.0464
REMARK 3 T13: -0.0282 T23: 0.0088
REMARK 3 L TENSOR
REMARK 3 L11: 7.1887 L22: 3.7163
REMARK 3 L33: 4.1464 L12: 3.0919
REMARK 3 L13: -5.1090 L23: -2.5509
REMARK 3 S TENSOR
REMARK 3 S11: -0.2367 S12: 0.3407 S13: -0.1939
REMARK 3 S21: 0.0780 S22: 0.1343 S23: 0.2268
REMARK 3 S31: 0.1769 S32: -0.7295 S33: 0.1196
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 72 THROUGH 77 )
REMARK 3 ORIGIN FOR THE GROUP (A): 13.6377 12.2889 -19.3094
REMARK 3 T TENSOR
REMARK 3 T11: 0.5343 T22: 0.7802
REMARK 3 T33: 0.3977 T12: 0.0614
REMARK 3 T13: -0.0177 T23: -0.0147
REMARK 3 L TENSOR
REMARK 3 L11: 4.2088 L22: 5.4649
REMARK 3 L33: 8.5243 L12: -1.4438
REMARK 3 L13: -4.9982 L23: -1.8328
REMARK 3 S TENSOR
REMARK 3 S11: -0.0094 S12: -1.4629 S13: 1.4657
REMARK 3 S21: 0.6761 S22: -0.0521 S23: 0.0394
REMARK 3 S31: -0.7692 S32: -0.4637 S33: -0.0727
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 78 THROUGH 90 )
REMARK 3 ORIGIN FOR THE GROUP (A): 32.6828 16.6382 -30.8694
REMARK 3 T TENSOR
REMARK 3 T11: 0.2396 T22: 0.2557
REMARK 3 T33: 0.2425 T12: -0.0507
REMARK 3 T13: -0.0827 T23: -0.0090
REMARK 3 L TENSOR
REMARK 3 L11: 5.1988 L22: 1.0771
REMARK 3 L33: 5.8270 L12: 1.9272
REMARK 3 L13: -2.0314 L23: -0.9894
REMARK 3 S TENSOR
REMARK 3 S11: 0.3172 S12: -0.7160 S13: 0.1386
REMARK 3 S21: 0.2955 S22: -0.2803 S23: -0.2047
REMARK 3 S31: -0.6957 S32: 0.5655 S33: 0.0178
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 91 THROUGH 99 )
REMARK 3 ORIGIN FOR THE GROUP (A): 19.2791 18.9832 -27.5458
REMARK 3 T TENSOR
REMARK 3 T11: 0.3575 T22: 0.3924
REMARK 3 T33: 0.3909 T12: 0.0865
REMARK 3 T13: -0.0090 T23: -0.1542
REMARK 3 L TENSOR
REMARK 3 L11: 2.8044 L22: 7.5454
REMARK 3 L33: 8.3563 L12: 4.5612
REMARK 3 L13: -1.7686 L23: -1.5665
REMARK 3 S TENSOR
REMARK 3 S11: 0.3727 S12: -0.7559 S13: 2.4337
REMARK 3 S21: 0.5885 S22: -0.1686 S23: 1.0270
REMARK 3 S31: -1.1201 S32: -0.9227 S33: -0.0078
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 5CKG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-JUL-15.
REMARK 100 THE DEPOSITION ID IS D_1000211695.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-MAR-14
REMARK 200 TEMPERATURE (KELVIN) : 110
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID29
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.99
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20777
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.750
REMARK 200 RESOLUTION RANGE LOW (A) : 27.710
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.0
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : 0.06400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.84
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.9
REMARK 200 DATA REDUNDANCY IN SHELL : 3.70
REMARK 200 R MERGE FOR SHELL (I) : 0.32000
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: MOLREP
REMARK 200 STARTING MODEL: 2Z9T
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.35
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.21
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM ACETATE, 30% W/V PEG
REMARK 280 4000, 15% GLYCEROL, 0.2 M AMMONIUM ACETATE, PH 5.5, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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 X+1/2,Y+1/2,Z
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 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 1.000000 0.000000 0.000000 44.28900
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 14.43000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 44.28900
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 14.43000
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH B 269 LIES ON A SPECIAL POSITION.
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 LYS A 19 CG CD CE NZ
REMARK 470 LYS A 48 CG CD CE NZ
REMARK 470 MET A 99 CG SD CE
REMARK 470 LYS B 19 CG CD CE NZ
REMARK 470 GLU B 50 CG CD OE1 OE2
REMARK 470 ASP B 98 CG OD1 OD2
REMARK 470 MET B 99 CG SD CE
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH A 226 O HOH A 230 2.02
REMARK 500 O HOH B 265 O HOH B 274 2.13
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH B 223 O HOH B 252 4554 2.03
REMARK 500 O HOH B 257 O HOH B 257 2554 2.11
REMARK 500 O HOH B 261 O HOH B 272 4544 2.13
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 CYS A 80 CB CYS A 80 SG 0.140
REMARK 500 CYS B 80 CB CYS B 80 SG 0.172
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 CYS B 80 CA - CB - SG ANGL. DEV. = 6.8 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 PRO A 32 -169.12 -77.23
REMARK 500 LYS A 48 120.40 -39.81
REMARK 500 VAL A 49 133.68 1.39
REMARK 500 TRP A 60 69.05 77.00
REMARK 500 PRO B 32 -173.56 -67.82
REMARK 500 TRP B 60 66.75 70.72
REMARK 500 ASP B 98 46.26 -97.94
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 ACT A 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT B 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 102
DBREF 5CKG A 1 99 UNP P61769 B2MG_HUMAN 21 119
DBREF 5CKG B 1 99 UNP P61769 B2MG_HUMAN 21 119
SEQADV 5CKG MET A 0 UNP P61769 INITIATING METHIONINE
SEQADV 5CKG GLU A 85 UNP P61769 VAL 105 ENGINEERED MUTATION
SEQADV 5CKG MET B 0 UNP P61769 INITIATING METHIONINE
SEQADV 5CKG GLU B 85 UNP P61769 VAL 105 ENGINEERED MUTATION
SEQRES 1 A 100 MET ILE GLN ARG THR PRO LYS ILE GLN VAL TYR SER ARG
SEQRES 2 A 100 HIS PRO ALA GLU ASN GLY LYS SER ASN PHE LEU ASN CYS
SEQRES 3 A 100 TYR VAL SER GLY PHE HIS PRO SER ASP ILE GLU VAL ASP
SEQRES 4 A 100 LEU LEU LYS ASN GLY GLU ARG ILE GLU LYS VAL GLU HIS
SEQRES 5 A 100 SER ASP LEU SER PHE SER LYS ASP TRP SER PHE TYR LEU
SEQRES 6 A 100 LEU TYR TYR THR GLU PHE THR PRO THR GLU LYS ASP GLU
SEQRES 7 A 100 TYR ALA CYS ARG VAL ASN HIS GLU THR LEU SER GLN PRO
SEQRES 8 A 100 LYS ILE VAL LYS TRP ASP ARG ASP MET
SEQRES 1 B 100 MET ILE GLN ARG THR PRO LYS ILE GLN VAL TYR SER ARG
SEQRES 2 B 100 HIS PRO ALA GLU ASN GLY LYS SER ASN PHE LEU ASN CYS
SEQRES 3 B 100 TYR VAL SER GLY PHE HIS PRO SER ASP ILE GLU VAL ASP
SEQRES 4 B 100 LEU LEU LYS ASN GLY GLU ARG ILE GLU LYS VAL GLU HIS
SEQRES 5 B 100 SER ASP LEU SER PHE SER LYS ASP TRP SER PHE TYR LEU
SEQRES 6 B 100 LEU TYR TYR THR GLU PHE THR PRO THR GLU LYS ASP GLU
SEQRES 7 B 100 TYR ALA CYS ARG VAL ASN HIS GLU THR LEU SER GLN PRO
SEQRES 8 B 100 LYS ILE VAL LYS TRP ASP ARG ASP MET
HET ACT A 101 4
HET ACT B 101 4
HET GOL B 102 6
HETNAM ACT ACETATE ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 ACT 2(C2 H3 O2 1-)
FORMUL 5 GOL C3 H8 O3
FORMUL 6 HOH *120(H2 O)
SHEET 1 AA1 4 LYS A 6 SER A 11 0
SHEET 2 AA1 4 ASN A 21 PHE A 30 -1 O SER A 28 N LYS A 6
SHEET 3 AA1 4 SER A 61 PHE A 70 -1 O TYR A 66 N CYS A 25
SHEET 4 AA1 4 HIS A 51 SER A 57 -1 N SER A 57 O SER A 61
SHEET 1 AA2 4 GLU A 44 ARG A 45 0
SHEET 2 AA2 4 GLU A 36 LYS A 41 -1 N LYS A 41 O GLU A 44
SHEET 3 AA2 4 TYR A 78 ASN A 83 -1 O ARG A 81 N ASP A 38
SHEET 4 AA2 4 LYS A 91 LYS A 94 -1 O VAL A 93 N CYS A 80
SHEET 1 AA3 4 LYS B 6 SER B 11 0
SHEET 2 AA3 4 ASN B 21 PHE B 30 -1 O TYR B 26 N GLN B 8
SHEET 3 AA3 4 SER B 61 PHE B 70 -1 O TYR B 66 N CYS B 25
SHEET 4 AA3 4 HIS B 51 SER B 57 -1 N ASP B 53 O LEU B 65
SHEET 1 AA4 4 GLU B 44 ARG B 45 0
SHEET 2 AA4 4 GLU B 36 LYS B 41 -1 N LYS B 41 O GLU B 44
SHEET 3 AA4 4 TYR B 78 ASN B 83 -1 O ALA B 79 N LEU B 40
SHEET 4 AA4 4 LYS B 91 LYS B 94 -1 O LYS B 91 N VAL B 82
SSBOND 1 CYS A 25 CYS A 80 1555 1555 2.07
SSBOND 2 CYS B 25 CYS B 80 1555 1555 2.06
CISPEP 1 HIS A 31 PRO A 32 0 -0.08
CISPEP 2 HIS B 31 PRO B 32 0 -4.75
SITE 1 AC1 1 GLN A 8
SITE 1 AC2 2 TYR B 10 ARG B 12
SITE 1 AC3 4 GLU B 36 ASN B 83 HIS B 84 GLU B 85
CRYST1 88.578 28.860 87.719 90.00 110.11 90.00 C 1 2 1 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.011289 0.000000 0.004134 0.00000
SCALE2 0.000000 0.034650 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012140 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
