HEADER DNA BINDING PROTEIN 08-JUN-11 3B0B
TITLE CRYSTAL STRUCTURE OF THE CHICKEN CENP-S/CENP-X COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CENTROMERE PROTEIN S;
COMPND 3 CHAIN: B, A;
COMPND 4 SYNONYM: CENP-S;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: CENTROMERE PROTEIN X;
COMPND 8 CHAIN: C, D;
COMPND 9 SYNONYM: CENP-X;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GALLUS GALLUS;
SOURCE 3 ORGANISM_TAXID: 9031;
SOURCE 4 GENE: CENP-S;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PRSFDUET;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: GALLUS GALLUS;
SOURCE 12 ORGANISM_TAXID: 9031;
SOURCE 13 GENE: CENP-X;
SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 16 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 18 EXPRESSION_SYSTEM_PLASMID: PRSFDUET
KEYWDS HISTONE FOLD, DNA BINDING, DNA, NUCLEUS, DNA BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR T.NISHINO,K.TAKEUCHI,K.E.GASCOIGNE,A.SUZUKI,T.HORI,T.OYAMA,
AUTHOR 2 K.MORIKAWA,I.M.CHEESEMAN,T.FUKAGAWA
REVDAT 1 07-MAR-12 3B0B 0
JRNL AUTH T.NISHINO,K.TAKEUCHI,K.E.GASCOIGNE,A.SUZUKI,T.HORI,T.OYAMA,
JRNL AUTH 2 K.MORIKAWA,I.M.CHEESEMAN,T.FUKAGAWA
JRNL TITL CENP-T-W-S-X FORMS A UNIQUE CENTROMERIC CHROMATIN STRUCTURE
JRNL TITL 2 WITH A HISTONE-LIKE FOLD.
JRNL REF CELL(CAMBRIDGE,MASS.) V. 148 487 2012
JRNL REFN ISSN 0092-8674
JRNL PMID 22304917
JRNL DOI 10.1016/J.CELL.2011.11.061
REMARK 2
REMARK 2 RESOLUTION. 2.15 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.6.4_486)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.15
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.21
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 3 NUMBER OF REFLECTIONS : 24657
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.190
REMARK 3 R VALUE (WORKING SET) : 0.186
REMARK 3 FREE R VALUE : 0.235
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.960
REMARK 3 FREE R VALUE TEST SET COUNT : 1963
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 42.2191 - 4.6302 0.99 2294 202 0.1756 0.2107
REMARK 3 2 4.6302 - 3.6758 1.00 2291 202 0.1532 0.2009
REMARK 3 3 3.6758 - 3.2113 1.00 2317 197 0.1935 0.2263
REMARK 3 4 3.2113 - 2.9178 0.99 2288 201 0.2096 0.2912
REMARK 3 5 2.9178 - 2.7087 0.99 2274 195 0.2204 0.2585
REMARK 3 6 2.7087 - 2.5490 0.99 2307 195 0.2067 0.2842
REMARK 3 7 2.5490 - 2.4214 0.99 2260 198 0.2045 0.2617
REMARK 3 8 2.4214 - 2.3160 0.98 2256 191 0.1998 0.2772
REMARK 3 9 2.3160 - 2.2268 0.97 2223 195 0.2087 0.2708
REMARK 3 10 2.2268 - 2.1500 0.93 2184 187 0.2180 0.2758
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
REMARK 3 SHRINKAGE RADIUS : 0.83
REMARK 3 K_SOL : 0.33
REMARK 3 B_SOL : 54.79
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.550
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.030
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) : 5.30910
REMARK 3 B22 (A**2) : 5.30910
REMARK 3 B33 (A**2) : -20.06620
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 : 0.007 2781
REMARK 3 ANGLE : 0.959 3729
REMARK 3 CHIRALITY : 0.068 435
REMARK 3 PLANARITY : 0.003 483
REMARK 3 DIHEDRAL : 14.839 1067
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 15
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 8:35)
REMARK 3 ORIGIN FOR THE GROUP (A): -3.5624 0.1355 32.0144
REMARK 3 T TENSOR
REMARK 3 T11: 0.6690 T22: 0.2618
REMARK 3 T33: 0.3467 T12: -0.0329
REMARK 3 T13: 0.0885 T23: 0.0337
REMARK 3 L TENSOR
REMARK 3 L11: 2.4412 L22: 2.6905
REMARK 3 L33: 4.9176 L12: 0.5815
REMARK 3 L13: 1.6933 L23: 1.6199
REMARK 3 S TENSOR
REMARK 3 S11: -0.2799 S12: -0.5695 S13: -0.3773
REMARK 3 S21: 0.2334 S22: 0.1507 S23: 0.2485
REMARK 3 S31: 0.4735 S32: -0.0378 S33: 0.1527
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 36:75)
REMARK 3 ORIGIN FOR THE GROUP (A): 2.3786 4.2969 21.0190
REMARK 3 T TENSOR
REMARK 3 T11: 0.5081 T22: 0.3184
REMARK 3 T33: 0.3439 T12: -0.1698
REMARK 3 T13: 0.0433 T23: -0.0728
REMARK 3 L TENSOR
REMARK 3 L11: 2.3514 L22: 3.1932
REMARK 3 L33: 2.2495 L12: 0.7623
REMARK 3 L13: -0.7412 L23: -0.6162
REMARK 3 S TENSOR
REMARK 3 S11: -0.2808 S12: -0.0979 S13: -0.2477
REMARK 3 S21: -0.0543 S22: 0.1418 S23: -0.3631
REMARK 3 S31: 0.3074 S32: 0.4012 S33: 0.0460
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 76:86)
REMARK 3 ORIGIN FOR THE GROUP (A): -0.8929 12.4615 12.2426
REMARK 3 T TENSOR
REMARK 3 T11: 0.6390 T22: 0.4674
REMARK 3 T33: 0.4878 T12: -0.2859
REMARK 3 T13: 0.0492 T23: 0.0225
REMARK 3 L TENSOR
REMARK 3 L11: 2.6857 L22: 1.8897
REMARK 3 L33: 1.8171 L12: -2.1533
REMARK 3 L13: 0.9433 L23: -0.7752
REMARK 3 S TENSOR
REMARK 3 S11: -0.8393 S12: 0.6741 S13: -0.0017
REMARK 3 S21: -0.4068 S22: 1.0662 S23: 0.2054
REMARK 3 S31: 0.0744 S32: 0.1479 S33: -0.2650
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 87:104)
REMARK 3 ORIGIN FOR THE GROUP (A): -9.5793 17.8308 16.5707
REMARK 3 T TENSOR
REMARK 3 T11: 0.8240 T22: 0.5805
REMARK 3 T33: 0.8608 T12: -0.0707
REMARK 3 T13: -0.0820 T23: 0.1485
REMARK 3 L TENSOR
REMARK 3 L11: 9.0786 L22: 7.9276
REMARK 3 L33: 7.7223 L12: -1.6101
REMARK 3 L13: -0.3400 L23: 5.6816
REMARK 3 S TENSOR
REMARK 3 S11: -0.0838 S12: -0.5337 S13: 0.6547
REMARK 3 S21: -0.5689 S22: -0.4343 S23: 1.0866
REMARK 3 S31: -1.2794 S32: -1.2842 S33: -0.0560
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN C AND (RESSEQ 6:29)
REMARK 3 ORIGIN FOR THE GROUP (A): 6.5999 11.5332 27.2914
REMARK 3 T TENSOR
REMARK 3 T11: 0.6593 T22: 0.4438
REMARK 3 T33: 0.4405 T12: -0.1190
REMARK 3 T13: -0.0526 T23: -0.0935
REMARK 3 L TENSOR
REMARK 3 L11: 8.4414 L22: 3.5628
REMARK 3 L33: 4.5713 L12: 0.9242
REMARK 3 L13: -1.8172 L23: -1.3983
REMARK 3 S TENSOR
REMARK 3 S11: -0.1418 S12: -0.9451 S13: 0.4821
REMARK 3 S21: 0.7610 S22: 0.2288 S23: -0.2744
REMARK 3 S31: -0.2767 S32: 0.5128 S33: -0.1437
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN C AND (RESSEQ 30:57)
REMARK 3 ORIGIN FOR THE GROUP (A): -8.7635 3.4963 20.7270
REMARK 3 T TENSOR
REMARK 3 T11: 0.4787 T22: 0.3880
REMARK 3 T33: 0.5016 T12: -0.1538
REMARK 3 T13: 0.0053 T23: 0.0762
REMARK 3 L TENSOR
REMARK 3 L11: 5.5287 L22: 3.4261
REMARK 3 L33: 3.5774 L12: 2.7750
REMARK 3 L13: 1.8707 L23: 3.1293
REMARK 3 S TENSOR
REMARK 3 S11: -0.3974 S12: 0.3332 S13: 0.3872
REMARK 3 S21: -0.1556 S22: 0.5928 S23: 0.8768
REMARK 3 S31: -0.0480 S32: 0.1421 S33: -0.1474
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN C AND (RESSEQ 58:64)
REMARK 3 ORIGIN FOR THE GROUP (A): -17.3068 -14.4783 21.9420
REMARK 3 T TENSOR
REMARK 3 T11: 0.8885 T22: 0.3859
REMARK 3 T33: 0.8068 T12: -0.2589
REMARK 3 T13: 0.0853 T23: -0.0613
REMARK 3 L TENSOR
REMARK 3 L11: 1.8052 L22: 2.7391
REMARK 3 L33: 0.7188 L12: 2.0753
REMARK 3 L13: 0.3067 L23: 0.8240
REMARK 3 S TENSOR
REMARK 3 S11: 0.2203 S12: -0.4438 S13: -0.6798
REMARK 3 S21: 0.0549 S22: -0.3319 S23: 0.7257
REMARK 3 S31: 0.2865 S32: -0.2501 S33: -0.2643
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN C AND (RESSEQ 65:80)
REMARK 3 ORIGIN FOR THE GROUP (A): -5.3675 -6.6569 15.2433
REMARK 3 T TENSOR
REMARK 3 T11: 0.7846 T22: 0.3349
REMARK 3 T33: 0.4552 T12: -0.2324
REMARK 3 T13: 0.0715 T23: -0.0632
REMARK 3 L TENSOR
REMARK 3 L11: 7.1842 L22: 4.2284
REMARK 3 L33: 3.0997 L12: 0.9835
REMARK 3 L13: 0.1614 L23: 0.6573
REMARK 3 S TENSOR
REMARK 3 S11: 0.1979 S12: 0.9170 S13: 0.1328
REMARK 3 S21: -0.2301 S22: 0.5604 S23: -0.4491
REMARK 3 S31: 0.4198 S32: 0.3578 S33: -0.3741
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 5:40)
REMARK 3 ORIGIN FOR THE GROUP (A): 4.7214 -5.8965 -12.6704
REMARK 3 T TENSOR
REMARK 3 T11: 0.5564 T22: 0.7030
REMARK 3 T33: 0.3867 T12: -0.2319
REMARK 3 T13: -0.0452 T23: -0.0364
REMARK 3 L TENSOR
REMARK 3 L11: 8.0930 L22: 4.4806
REMARK 3 L33: 5.4508 L12: -2.8073
REMARK 3 L13: 2.8719 L23: -3.0006
REMARK 3 S TENSOR
REMARK 3 S11: 0.7435 S12: -0.0526 S13: -1.0834
REMARK 3 S21: 0.0230 S22: -0.4908 S23: 0.6066
REMARK 3 S31: 0.4212 S32: 0.1719 S33: -0.1435
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 41:69)
REMARK 3 ORIGIN FOR THE GROUP (A): 2.1538 2.7111 -1.9415
REMARK 3 T TENSOR
REMARK 3 T11: 0.5833 T22: 0.5270
REMARK 3 T33: 0.3289 T12: -0.2506
REMARK 3 T13: 0.0114 T23: 0.0192
REMARK 3 L TENSOR
REMARK 3 L11: 1.6540 L22: 9.1084
REMARK 3 L33: 3.3937 L12: -0.4966
REMARK 3 L13: 0.3874 L23: 3.1834
REMARK 3 S TENSOR
REMARK 3 S11: 0.4484 S12: 0.0527 S13: 0.0459
REMARK 3 S21: 0.7903 S22: -0.6855 S23: 0.5137
REMARK 3 S31: 0.1915 S32: -0.3940 S33: 0.1771
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 70:102)
REMARK 3 ORIGIN FOR THE GROUP (A): 15.9061 8.4988 2.9884
REMARK 3 T TENSOR
REMARK 3 T11: 0.6079 T22: 0.7320
REMARK 3 T33: 0.7004 T12: -0.2553
REMARK 3 T13: -0.0175 T23: -0.1222
REMARK 3 L TENSOR
REMARK 3 L11: 3.7042 L22: 7.7305
REMARK 3 L33: 4.3775 L12: -1.1633
REMARK 3 L13: 0.2245 L23: 0.0200
REMARK 3 S TENSOR
REMARK 3 S11: -0.0046 S12: 0.4787 S13: -0.2650
REMARK 3 S21: 0.4318 S22: 0.3655 S23: -1.5713
REMARK 3 S31: -0.3027 S32: 1.2063 S33: -0.3450
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN D AND (RESSEQ 6:18)
REMARK 3 ORIGIN FOR THE GROUP (A): 7.7935 6.3529 -12.1383
REMARK 3 T TENSOR
REMARK 3 T11: 0.7075 T22: 0.7325
REMARK 3 T33: 0.4296 T12: -0.2978
REMARK 3 T13: 0.0374 T23: -0.0143
REMARK 3 L TENSOR
REMARK 3 L11: 7.9342 L22: 9.3189
REMARK 3 L33: 9.7367 L12: -5.9947
REMARK 3 L13: -3.1744 L23: 2.3887
REMARK 3 S TENSOR
REMARK 3 S11: 0.1229 S12: 1.3470 S13: 0.5674
REMARK 3 S21: -1.0932 S22: -0.2115 S23: -0.0496
REMARK 3 S31: -0.7294 S32: -0.1022 S33: -0.0635
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN D AND (RESSEQ 19:29)
REMARK 3 ORIGIN FOR THE GROUP (A): 1.8110 15.5297 -5.2253
REMARK 3 T TENSOR
REMARK 3 T11: 0.8528 T22: 0.6985
REMARK 3 T33: 0.3573 T12: -0.2816
REMARK 3 T13: 0.0809 T23: 0.0241
REMARK 3 L TENSOR
REMARK 3 L11: 3.9243 L22: 9.5072
REMARK 3 L33: 5.5459 L12: -3.2188
REMARK 3 L13: 1.7555 L23: 4.0161
REMARK 3 S TENSOR
REMARK 3 S11: 0.0642 S12: 0.7091 S13: 0.5243
REMARK 3 S21: -0.2746 S22: 0.0097 S23: -0.2983
REMARK 3 S31: -1.1411 S32: -0.1905 S33: 0.0365
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN D AND (RESSEQ 30:58)
REMARK 3 ORIGIN FOR THE GROUP (A): 11.4751 -5.9158 -1.7297
REMARK 3 T TENSOR
REMARK 3 T11: 0.6470 T22: 0.8600
REMARK 3 T33: 0.4452 T12: -0.0652
REMARK 3 T13: -0.1129 T23: -0.0145
REMARK 3 L TENSOR
REMARK 3 L11: 4.8677 L22: 2.0298
REMARK 3 L33: 4.0593 L12: 1.1948
REMARK 3 L13: -1.0722 L23: -1.4875
REMARK 3 S TENSOR
REMARK 3 S11: 0.1554 S12: -0.4507 S13: -0.4345
REMARK 3 S21: 1.3384 S22: 0.2700 S23: -0.8761
REMARK 3 S31: -0.0640 S32: 0.4978 S33: -0.3790
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN D AND (RESSEQ 59:80)
REMARK 3 ORIGIN FOR THE GROUP (A): 3.8472 -14.1675 1.7979
REMARK 3 T TENSOR
REMARK 3 T11: 1.0145 T22: 0.7844
REMARK 3 T33: 0.5938 T12: -0.2411
REMARK 3 T13: -0.0507 T23: 0.1510
REMARK 3 L TENSOR
REMARK 3 L11: 6.6296 L22: 9.4103
REMARK 3 L33: 6.6682 L12: -2.4853
REMARK 3 L13: -0.8450 L23: 1.7735
REMARK 3 S TENSOR
REMARK 3 S11: -0.2951 S12: -0.7401 S13: -1.1211
REMARK 3 S21: 0.9685 S22: 0.7281 S23: 0.4245
REMARK 3 S31: 1.0514 S32: 0.4545 S33: -0.2809
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 3B0B COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 16-JUN-11.
REMARK 100 THE RCSB ID CODE IS RCSB029917.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-OCT-10; 14-NOV-10
REMARK 200 TEMPERATURE (KELVIN) : 100; 100
REMARK 200 PH : 9.5
REMARK 200 NUMBER OF CRYSTALS USED : 2
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; Y
REMARK 200 RADIATION SOURCE : SPRING-8; SPRING-8
REMARK 200 BEAMLINE : BL38B1; BL44XU
REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9642, 0.97944, 0.97889,
REMARK 200 0.9951; 0.9
REMARK 200 MONOCHROMATOR : GRAPHITE; GRAPHITE
REMARK 200 OPTICS : NULL; NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD; CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315; ADSC QUANTUM
REMARK 200 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25152
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.150
REMARK 200 RESOLUTION RANGE LOW (A) : 42.211
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.23
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD; SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.43
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.76
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM CITRATE-BISPROPANE PH 9.5, 500MM
REMARK 280 NACL, 100MM MGSO4, AND 30% PEG 600, VAPOR DIFFUSION, TEMPERATURE
REMARK 280 293K
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 115.21100
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 230.42200
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 172.81650
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 288.02750
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 57.60550
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C, A, 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4920 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9380 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -40.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4740 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9480 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -43.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 GLY B 0
REMARK 465 SER B 1
REMARK 465 GLU B 2
REMARK 465 ALA B 3
REMARK 465 ALA B 4
REMARK 465 GLY B 5
REMARK 465 GLY B 6
REMARK 465 GLU B 7
REMARK 465 MSE B 105
REMARK 465 GLU B 106
REMARK 465 GLY C 0
REMARK 465 TYR C 1
REMARK 465 GLU C 2
REMARK 465 GLU C 3
REMARK 465 ARG C 4
REMARK 465 GLU C 5
REMARK 465 GLY A 0
REMARK 465 SER A 1
REMARK 465 GLU A 2
REMARK 465 ALA A 3
REMARK 465 ALA A 4
REMARK 465 SER A 103
REMARK 465 ASN A 104
REMARK 465 MSE A 105
REMARK 465 GLU A 106
REMARK 465 GLY D 0
REMARK 465 TYR D 1
REMARK 465 GLU D 2
REMARK 465 GLU D 3
REMARK 465 ARG D 4
REMARK 465 GLU D 5
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 N GLN B 8 OE2 GLU B 10 1.92
REMARK 500 O ALA D 52 OE1 GLN D 56 1.99
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 LEU A 100 -71.46 -93.54
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3B0C RELATED DB: PDB
REMARK 900 RELATED ID: 3B0D RELATED DB: PDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 SEQUENCE DATABASE REFERENCES FOR THESE PROTEINS DO NOT CURRENTLY
REMARK 999 EXIST.
DBREF 3B0B B 0 106 PDB 3B0B 3B0B 0 106
DBREF 3B0B A 0 106 PDB 3B0B 3B0B 0 106
DBREF 3B0B C 0 80 PDB 3B0B 3B0B 0 80
DBREF 3B0B D 0 80 PDB 3B0B 3B0B 0 80
SEQRES 1 B 107 GLY SER GLU ALA ALA GLY GLY GLU GLN ARG GLU LEU LEU
SEQRES 2 B 107 ILE GLN ARG LEU ARG ALA ALA VAL HIS TYR THR THR GLY
SEQRES 3 B 107 CYS LEU CYS GLN ASP VAL ALA GLU ASP LYS GLY VAL LEU
SEQRES 4 B 107 PHE SER LYS GLN THR VAL ALA ALA ILE SER GLU ILE THR
SEQRES 5 B 107 PHE ARG GLN CYS GLU ASN PHE ALA ARG ASP LEU GLU MSE
SEQRES 6 B 107 PHE ALA ARG HIS ALA LYS ARG SER THR ILE THR SER GLU
SEQRES 7 B 107 ASP VAL LYS LEU LEU ALA ARG ARG SER ASN SER LEU LEU
SEQRES 8 B 107 LYS TYR ILE THR GLN LYS SER ASP GLU LEU ALA SER SER
SEQRES 9 B 107 ASN MSE GLU
SEQRES 1 C 81 GLY TYR GLU GLU ARG GLU GLY GLY PHE ARG LYS GLU THR
SEQRES 2 C 81 VAL GLU ARG LEU LEU ARG LEU HIS PHE ARG ASP GLY ARG
SEQRES 3 C 81 THR ARG VAL ASN GLY ASP ALA LEU LEU LEU MSE ALA GLU
SEQRES 4 C 81 LEU LEU LYS VAL PHE VAL ARG GLU ALA ALA ALA ARG ALA
SEQRES 5 C 81 ALA ARG GLN ALA GLN ALA GLU ASP LEU GLU LYS VAL ASP
SEQRES 6 C 81 ILE GLU HIS VAL GLU LYS VAL LEU PRO GLN LEU LEU LEU
SEQRES 7 C 81 ASP PHE VAL
SEQRES 1 A 107 GLY SER GLU ALA ALA GLY GLY GLU GLN ARG GLU LEU LEU
SEQRES 2 A 107 ILE GLN ARG LEU ARG ALA ALA VAL HIS TYR THR THR GLY
SEQRES 3 A 107 CYS LEU CYS GLN ASP VAL ALA GLU ASP LYS GLY VAL LEU
SEQRES 4 A 107 PHE SER LYS GLN THR VAL ALA ALA ILE SER GLU ILE THR
SEQRES 5 A 107 PHE ARG GLN CYS GLU ASN PHE ALA ARG ASP LEU GLU MSE
SEQRES 6 A 107 PHE ALA ARG HIS ALA LYS ARG SER THR ILE THR SER GLU
SEQRES 7 A 107 ASP VAL LYS LEU LEU ALA ARG ARG SER ASN SER LEU LEU
SEQRES 8 A 107 LYS TYR ILE THR GLN LYS SER ASP GLU LEU ALA SER SER
SEQRES 9 A 107 ASN MSE GLU
SEQRES 1 D 81 GLY TYR GLU GLU ARG GLU GLY GLY PHE ARG LYS GLU THR
SEQRES 2 D 81 VAL GLU ARG LEU LEU ARG LEU HIS PHE ARG ASP GLY ARG
SEQRES 3 D 81 THR ARG VAL ASN GLY ASP ALA LEU LEU LEU MSE ALA GLU
SEQRES 4 D 81 LEU LEU LYS VAL PHE VAL ARG GLU ALA ALA ALA ARG ALA
SEQRES 5 D 81 ALA ARG GLN ALA GLN ALA GLU ASP LEU GLU LYS VAL ASP
SEQRES 6 D 81 ILE GLU HIS VAL GLU LYS VAL LEU PRO GLN LEU LEU LEU
SEQRES 7 D 81 ASP PHE VAL
MODRES 3B0B MSE B 64 MET SELENOMETHIONINE
MODRES 3B0B MSE C 36 MET SELENOMETHIONINE
MODRES 3B0B MSE A 64 MET SELENOMETHIONINE
MODRES 3B0B MSE D 36 MET SELENOMETHIONINE
HET MSE B 64 8
HET MSE C 36 8
HET MSE A 64 8
HET MSE D 36 8
HETNAM MSE SELENOMETHIONINE
FORMUL 1 MSE 4(C5 H11 N O2 SE)
FORMUL 5 HOH *119(H2 O)
HELIX 1 1 GLN B 8 GLY B 36 1 29
HELIX 2 2 SER B 40 ALA B 69 1 30
HELIX 3 3 THR B 75 ALA B 83 1 9
HELIX 4 4 SER B 86 SER B 102 1 17
HELIX 5 5 ARG C 9 PHE C 21 1 13
HELIX 6 6 ASN C 29 GLU C 58 1 30
HELIX 7 7 ASP C 64 PHE C 79 1 16
HELIX 8 8 GLY A 6 LYS A 35 1 30
HELIX 9 9 SER A 40 ALA A 69 1 30
HELIX 10 10 THR A 75 ALA A 83 1 9
HELIX 11 11 SER A 86 ALA A 101 1 16
HELIX 12 12 ARG D 9 PHE D 21 1 13
HELIX 13 13 ASN D 29 GLU D 58 1 30
HELIX 14 14 ASP D 64 VAL D 80 1 17
SHEET 1 A 2 LEU B 38 PHE B 39 0
SHEET 2 A 2 LYS C 62 VAL C 63 1 O VAL C 63 N LEU B 38
SHEET 1 B 2 THR B 73 ILE B 74 0
SHEET 2 B 2 ARG C 27 VAL C 28 1 O ARG C 27 N ILE B 74
SHEET 1 C 2 LEU A 38 PHE A 39 0
SHEET 2 C 2 LYS D 62 VAL D 63 1 O VAL D 63 N LEU A 38
SHEET 1 D 2 THR A 73 ILE A 74 0
SHEET 2 D 2 ARG D 27 VAL D 28 1 O ARG D 27 N ILE A 74
LINK C GLU B 63 N MSE B 64 1555 1555 1.32
LINK C MSE B 64 N PHE B 65 1555 1555 1.33
LINK C LEU C 35 N MSE C 36 1555 1555 1.33
LINK C MSE C 36 N ALA C 37 1555 1555 1.33
LINK C GLU A 63 N MSE A 64 1555 1555 1.32
LINK C MSE A 64 N PHE A 65 1555 1555 1.33
LINK C LEU D 35 N MSE D 36 1555 1555 1.33
LINK C MSE D 36 N ALA D 37 1555 1555 1.33
CRYST1 48.741 48.741 345.633 90.00 90.00 120.00 P 61 12
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 0.020517 0.011845 0.000000 0.00000
SCALE2 0.000000 0.023691 0.000000 0.00000
SCALE3 0.000000 0.000000 0.002893 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
