HEADER TRANSFERASE, TRANSPORT PROTEIN 30-AUG-07 2R48
TITLE CRYSTAL STRUCTURE OF THE FRUCTOSE SPECIFIC IIB SUBUNIT OF PTS SYSTEM
TITLE 2 FROM BACILLUS SUBTILIS SUBSP. SUBTILIS STR. 168
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHOSPHOTRANSFERASE SYSTEM (PTS) MANNOSE-SPECIFIC ENZYME
COMPND 3 IIBCA COMPONENT;
COMPND 4 CHAIN: A;
COMPND 5 FRAGMENT: RESIDUES 2-104;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS SUBSP. SUBTILIS;
SOURCE 3 ORGANISM_TAXID: 224308;
SOURCE 4 STRAIN: 168;
SOURCE 5 GENE: MANP, BSU12010;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PMCSG7
KEYWDS PTS SYSTEM, PHOSPHOTRANSFERASE SYSTEM, FRUCTOSE SPECIFIC IIB SUBUNIT,
KEYWDS 2 PFAM02379, PSI-2, MCSG, STRUCTURAL GENOMICS, PROTEIN STRUCTURE
KEYWDS 3 INITIATIVE, MIDWEST CENTER FOR STRUCTURAL GENOMICS, MEMBRANE, SUGAR
KEYWDS 4 TRANSPORT, TRANSMEMBRANE, TRANSPORT, TRANSFERASE, TRANSPORT PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR B.NOCEK,M.CUFF,A.SATHER,S.CLANCY,A.JOACHIMIAK,MIDWEST CENTER FOR
AUTHOR 2 STRUCTURAL GENOMICS (MCSG)
REVDAT 3 13-JUL-11 2R48 1 VERSN
REVDAT 2 24-FEB-09 2R48 1 VERSN
REVDAT 1 11-SEP-07 2R48 0
JRNL AUTH B.NOCEK,M.CUFF,A.SATHER,S.CLANCY,A.JOACHIMIAK
JRNL TITL CRYSTAL STRUCTURE OF THE FRUCTOSE SPECIFIC IIB SUBUNIT OF
JRNL TITL 2 PTS SYSTEM FROM BACILLUS SUBTILIS SUBSP. SUBTILIS STR. 168.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.78
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.2
REMARK 3 NUMBER OF REFLECTIONS : 7402
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.186
REMARK 3 R VALUE (WORKING SET) : 0.183
REMARK 3 FREE R VALUE : 0.237
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.700
REMARK 3 FREE R VALUE TEST SET COUNT : 361
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.85
REMARK 3 REFLECTION IN BIN (WORKING SET) : 359
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 65.03
REMARK 3 BIN R VALUE (WORKING SET) : 0.2560
REMARK 3 BIN FREE R VALUE SET COUNT : 13
REMARK 3 BIN FREE R VALUE : 0.3310
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 795
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 57
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.63
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.57000
REMARK 3 B22 (A**2) : 1.57000
REMARK 3 B33 (A**2) : -3.13000
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 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.158
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.153
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.117
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.620
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.962
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.948
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 805 ; 0.019 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 550 ; 0.011 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1086 ; 1.712 ; 1.989
REMARK 3 BOND ANGLES OTHERS (DEGREES): 1360 ; 1.033 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 106 ; 5.461 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 34 ;37.292 ;25.882
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 155 ;13.805 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 5 ;14.832 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 129 ; 0.092 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 896 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 137 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 159 ; 0.203 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 556 ; 0.207 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 392 ; 0.171 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 443 ; 0.089 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 42 ; 0.201 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 16 ; 0.229 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 35 ; 0.248 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 7 ; 0.135 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 629 ; 1.171 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 216 ; 0.267 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 838 ; 1.417 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 300 ; 2.453 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 247 ; 3.519 ; 4.500
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 14
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 0 A 7
REMARK 3 ORIGIN FOR THE GROUP (A): 13.9321 7.1277 20.1301
REMARK 3 T TENSOR
REMARK 3 T11: 0.1251 T22: 0.1426
REMARK 3 T33: 0.1441 T12: -0.0642
REMARK 3 T13: -0.0525 T23: 0.0065
REMARK 3 L TENSOR
REMARK 3 L11: 5.6179 L22: 7.9656
REMARK 3 L33: 16.4570 L12: -3.4615
REMARK 3 L13: 4.6220 L23: -7.7610
REMARK 3 S TENSOR
REMARK 3 S11: 0.0940 S12: -0.1794 S13: -0.2212
REMARK 3 S21: 0.2578 S22: -0.1483 S23: -0.4807
REMARK 3 S31: 0.0345 S32: 0.4865 S33: 0.0543
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 8 A 14
REMARK 3 ORIGIN FOR THE GROUP (A): 5.1731 16.4606 3.1306
REMARK 3 T TENSOR
REMARK 3 T11: 0.2730 T22: 0.1979
REMARK 3 T33: 0.0971 T12: 0.0634
REMARK 3 T13: -0.0413 T23: 0.0733
REMARK 3 L TENSOR
REMARK 3 L11: 5.0906 L22: 0.5335
REMARK 3 L33: 20.2913 L12: -0.8160
REMARK 3 L13: -9.5412 L23: 2.5142
REMARK 3 S TENSOR
REMARK 3 S11: 0.4876 S12: 0.4491 S13: -0.1222
REMARK 3 S21: -0.6574 S22: -0.2086 S23: 0.2103
REMARK 3 S31: -1.4826 S32: -0.7701 S33: -0.2790
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 15 A 22
REMARK 3 ORIGIN FOR THE GROUP (A): 12.4663 11.5128 5.0293
REMARK 3 T TENSOR
REMARK 3 T11: 0.1309 T22: 0.2012
REMARK 3 T33: 0.0645 T12: -0.0495
REMARK 3 T13: 0.0027 T23: -0.0244
REMARK 3 L TENSOR
REMARK 3 L11: 3.6193 L22: 1.6498
REMARK 3 L33: 4.7648 L12: -2.3206
REMARK 3 L13: -1.3600 L23: 0.0423
REMARK 3 S TENSOR
REMARK 3 S11: -0.0280 S12: 0.2722 S13: -0.1386
REMARK 3 S21: 0.0658 S22: 0.0530 S23: 0.0328
REMARK 3 S31: -0.2252 S32: 0.3266 S33: -0.0250
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 23 A 28
REMARK 3 ORIGIN FOR THE GROUP (A): 19.2290 6.8132 12.0649
REMARK 3 T TENSOR
REMARK 3 T11: 0.1145 T22: 0.1989
REMARK 3 T33: 0.0749 T12: -0.0289
REMARK 3 T13: -0.0268 T23: -0.0395
REMARK 3 L TENSOR
REMARK 3 L11: 4.3642 L22: 10.7034
REMARK 3 L33: 9.7303 L12: -2.6329
REMARK 3 L13: -0.6913 L23: -6.5657
REMARK 3 S TENSOR
REMARK 3 S11: 0.1189 S12: 0.4724 S13: 0.1149
REMARK 3 S21: -0.5788 S22: -0.2735 S23: -0.1648
REMARK 3 S31: 0.9969 S32: -0.1877 S33: 0.1546
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 29 A 37
REMARK 3 ORIGIN FOR THE GROUP (A): 16.5147 5.9149 16.1082
REMARK 3 T TENSOR
REMARK 3 T11: 0.1191 T22: 0.1296
REMARK 3 T33: 0.1058 T12: -0.0044
REMARK 3 T13: -0.0299 T23: -0.0822
REMARK 3 L TENSOR
REMARK 3 L11: 20.1694 L22: 1.5174
REMARK 3 L33: 2.5294 L12: -0.6031
REMARK 3 L13: 1.4149 L23: -1.9511
REMARK 3 S TENSOR
REMARK 3 S11: 0.2866 S12: 0.2759 S13: -0.4066
REMARK 3 S21: -0.0574 S22: -0.1032 S23: -0.0315
REMARK 3 S31: 0.0579 S32: 0.2533 S33: -0.1834
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 38 A 44
REMARK 3 ORIGIN FOR THE GROUP (A): 0.9645 10.2465 7.3578
REMARK 3 T TENSOR
REMARK 3 T11: 0.1227 T22: 0.2006
REMARK 3 T33: 0.0950 T12: -0.0466
REMARK 3 T13: -0.0319 T23: 0.0622
REMARK 3 L TENSOR
REMARK 3 L11: 12.9077 L22: 16.8084
REMARK 3 L33: 6.7492 L12: -2.1269
REMARK 3 L13: 8.5681 L23: -5.5920
REMARK 3 S TENSOR
REMARK 3 S11: -0.0059 S12: 0.8655 S13: 0.1718
REMARK 3 S21: -0.8942 S22: 0.3388 S23: 0.5387
REMARK 3 S31: 0.3377 S32: 0.5316 S33: -0.3329
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 45 A 49
REMARK 3 ORIGIN FOR THE GROUP (A): 3.2867 4.3065 14.3260
REMARK 3 T TENSOR
REMARK 3 T11: 0.0541 T22: 0.1136
REMARK 3 T33: 0.1419 T12: -0.0497
REMARK 3 T13: -0.0268 T23: 0.0151
REMARK 3 L TENSOR
REMARK 3 L11: 1.2511 L22: 6.0429
REMARK 3 L33: 34.3763 L12: -2.2822
REMARK 3 L13: 3.1636 L23: -2.6459
REMARK 3 S TENSOR
REMARK 3 S11: -0.0066 S12: 0.1042 S13: -0.2526
REMARK 3 S21: -0.3727 S22: 0.3250 S23: 0.2075
REMARK 3 S31: 0.0422 S32: -0.8866 S33: -0.3184
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 50 A 54
REMARK 3 ORIGIN FOR THE GROUP (A): 3.9783 3.1053 25.1406
REMARK 3 T TENSOR
REMARK 3 T11: 0.1083 T22: 0.1107
REMARK 3 T33: 0.1315 T12: -0.0384
REMARK 3 T13: 0.0404 T23: 0.0670
REMARK 3 L TENSOR
REMARK 3 L11: 15.3247 L22: 15.4545
REMARK 3 L33: 13.5616 L12: 2.3432
REMARK 3 L13: 14.3456 L23: 0.7788
REMARK 3 S TENSOR
REMARK 3 S11: 0.1880 S12: -0.9389 S13: -0.4709
REMARK 3 S21: 0.6321 S22: -0.1915 S23: 0.5438
REMARK 3 S31: 0.0261 S32: -0.5540 S33: 0.0035
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 55 A 66
REMARK 3 ORIGIN FOR THE GROUP (A): 8.4543 14.1038 17.9965
REMARK 3 T TENSOR
REMARK 3 T11: 0.1551 T22: 0.0958
REMARK 3 T33: 0.0798 T12: -0.0241
REMARK 3 T13: -0.0037 T23: -0.0033
REMARK 3 L TENSOR
REMARK 3 L11: 1.2691 L22: 2.8351
REMARK 3 L33: 9.5780 L12: 0.9828
REMARK 3 L13: 0.4655 L23: -4.0567
REMARK 3 S TENSOR
REMARK 3 S11: 0.0046 S12: -0.0934 S13: 0.1234
REMARK 3 S21: 0.0317 S22: 0.1124 S23: 0.0117
REMARK 3 S31: -0.1417 S32: -0.0593 S33: -0.1171
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 67 A 74
REMARK 3 ORIGIN FOR THE GROUP (A): 1.3162 14.4677 22.1823
REMARK 3 T TENSOR
REMARK 3 T11: 0.1353 T22: 0.1111
REMARK 3 T33: 0.0953 T12: 0.0287
REMARK 3 T13: 0.0542 T23: 0.0071
REMARK 3 L TENSOR
REMARK 3 L11: 5.6148 L22: 3.3661
REMARK 3 L33: 17.7920 L12: 0.6792
REMARK 3 L13: 2.4333 L23: -6.4840
REMARK 3 S TENSOR
REMARK 3 S11: 0.0157 S12: -0.1594 S13: 0.0456
REMARK 3 S21: 0.4454 S22: 0.3323 S23: 0.4401
REMARK 3 S31: -0.9211 S32: -0.0938 S33: -0.3479
REMARK 3
REMARK 3 TLS GROUP : 11
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 75 A 82
REMARK 3 ORIGIN FOR THE GROUP (A): 10.6717 17.3855 20.1150
REMARK 3 T TENSOR
REMARK 3 T11: 0.1457 T22: 0.1230
REMARK 3 T33: 0.0818 T12: -0.0389
REMARK 3 T13: -0.0070 T23: -0.0313
REMARK 3 L TENSOR
REMARK 3 L11: 1.6040 L22: 2.7049
REMARK 3 L33: 8.4246 L12: 0.6606
REMARK 3 L13: -0.8564 L23: -3.0023
REMARK 3 S TENSOR
REMARK 3 S11: 0.1168 S12: -0.0643 S13: 0.1380
REMARK 3 S21: 0.1504 S22: 0.1602 S23: 0.0498
REMARK 3 S31: -0.2098 S32: 0.0277 S33: -0.2770
REMARK 3
REMARK 3 TLS GROUP : 12
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 83 A 87
REMARK 3 ORIGIN FOR THE GROUP (A): 16.9641 19.1970 7.7891
REMARK 3 T TENSOR
REMARK 3 T11: 0.1713 T22: 0.2219
REMARK 3 T33: 0.0706 T12: -0.1009
REMARK 3 T13: 0.0822 T23: -0.0113
REMARK 3 L TENSOR
REMARK 3 L11: 13.0902 L22: 5.5926
REMARK 3 L33: 9.1583 L12: 0.9207
REMARK 3 L13: 4.1223 L23: 2.1781
REMARK 3 S TENSOR
REMARK 3 S11: 0.2052 S12: 0.0792 S13: 0.2494
REMARK 3 S21: -0.7086 S22: 0.1443 S23: -0.0892
REMARK 3 S31: -1.0264 S32: 0.9109 S33: -0.3495
REMARK 3
REMARK 3 TLS GROUP : 13
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 88 A 97
REMARK 3 ORIGIN FOR THE GROUP (A): 20.6096 15.5253 17.9873
REMARK 3 T TENSOR
REMARK 3 T11: 0.0232 T22: 0.1651
REMARK 3 T33: 0.1110 T12: -0.0792
REMARK 3 T13: -0.0216 T23: -0.0394
REMARK 3 L TENSOR
REMARK 3 L11: 4.7936 L22: 3.4697
REMARK 3 L33: 33.1470 L12: -1.3329
REMARK 3 L13: 4.5168 L23: -2.4981
REMARK 3 S TENSOR
REMARK 3 S11: -0.1619 S12: 0.2423 S13: -0.1452
REMARK 3 S21: 0.2347 S22: 0.0903 S23: -0.5422
REMARK 3 S31: -0.7477 S32: 0.7397 S33: 0.0716
REMARK 3
REMARK 3 TLS GROUP : 14
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 98 A 104
REMARK 3 ORIGIN FOR THE GROUP (A): 12.5790 18.6175 27.5104
REMARK 3 T TENSOR
REMARK 3 T11: 0.0748 T22: 0.0670
REMARK 3 T33: 0.1409 T12: 0.0730
REMARK 3 T13: -0.0186 T23: -0.1130
REMARK 3 L TENSOR
REMARK 3 L11: 41.6031 L22: 7.1482
REMARK 3 L33: 7.4387 L12: -2.7172
REMARK 3 L13: 3.8688 L23: -3.6201
REMARK 3 S TENSOR
REMARK 3 S11: -0.6178 S12: -1.0372 S13: 1.5352
REMARK 3 S21: 0.2931 S22: 0.1069 S23: -0.8760
REMARK 3 S31: -0.0898 S32: -0.3332 S33: 0.5110
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 2R48 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-AUG-07.
REMARK 100 THE RCSB ID CODE IS RCSB044404.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-AUG-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97950, 0.97960
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 7790
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.0
REMARK 200 DATA REDUNDANCY : 7.000
REMARK 200 R MERGE (I) : 0.07000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 28.7000
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) : 1.85
REMARK 200 COMPLETENESS FOR SHELL (%) : 61.7
REMARK 200 DATA REDUNDANCY IN SHELL : 4.70
REMARK 200 R MERGE FOR SHELL (I) : 0.37800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: HKL-3000, SHELXD, SHELXE, MLPHARE, DM, SOLVE/
REMARK 200 RESOLVE, ARP/WARP, CCP4, COOT
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 30.89
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.78
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M SODIUM CITRATE TRIBASIC
REMARK 280 DIHYDRATE, 20% PEG 3350, PH 7.5, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-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 34.12500
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 24.46550
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 24.46550
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 17.06250
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 24.46550
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 24.46550
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 51.18750
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 24.46550
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 24.46550
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 17.06250
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 24.46550
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 24.46550
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 51.18750
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 34.12500
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 300 REMARK: ACCORDING TO AUTHORS, THE CRYSTAL PACKING INDICATES THAT
REMARK 300 DIMER COULD BE THE BIOLOGICALLY RELEVANT OLIGOMERIZATION STATE.
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 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 A 126 LIES ON A SPECIAL POSITION.
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 SER A -1
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 121 O HOH A 158 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: APC1979.1 RELATED DB: TARGETDB
DBREF 2R48 A 2 104 UNP O31645 O31645_BACSU 2 104
SEQADV 2R48 SER A -1 UNP O31645 EXPRESSION TAG
SEQADV 2R48 ASN A 0 UNP O31645 EXPRESSION TAG
SEQADV 2R48 ALA A 1 UNP O31645 EXPRESSION TAG
SEQRES 1 A 106 SER ASN ALA LYS LEU LEU ALA ILE THR SER CYS PRO ASN
SEQRES 2 A 106 GLY ILE ALA HIS THR TYR MSE ALA ALA GLU ASN LEU GLN
SEQRES 3 A 106 LYS ALA ALA ASP ARG LEU GLY VAL SER ILE LYS VAL GLU
SEQRES 4 A 106 THR GLN GLY GLY ILE GLY VAL GLU ASN LYS LEU THR GLU
SEQRES 5 A 106 GLU GLU ILE ARG GLU ALA ASP ALA ILE ILE ILE ALA ALA
SEQRES 6 A 106 ASP ARG SER VAL ASN LYS ASP ARG PHE ILE GLY LYS LYS
SEQRES 7 A 106 LEU LEU SER VAL GLY VAL GLN ASP GLY ILE ARG LYS PRO
SEQRES 8 A 106 GLU GLU LEU ILE GLN LYS ALA LEU ASN GLY ASP ILE PRO
SEQRES 9 A 106 VAL TYR
MODRES 2R48 MSE A 18 MET SELENOMETHIONINE
HET MSE A 18 8
HETNAM MSE SELENOMETHIONINE
FORMUL 1 MSE C5 H11 N O2 SE
FORMUL 2 HOH *57(H2 O)
HELIX 1 1 ILE A 13 GLY A 31 1 19
HELIX 2 2 THR A 49 ALA A 56 1 8
HELIX 3 3 LYS A 69 ILE A 73 5 5
HELIX 4 4 GLY A 81 LYS A 88 1 8
HELIX 5 5 LYS A 88 GLY A 99 1 12
SHEET 1 A 5 GLY A 43 GLU A 45 0
SHEET 2 A 5 SER A 33 GLY A 40 -1 N THR A 38 O GLU A 45
SHEET 3 A 5 LYS A 2 SER A 8 1 N ALA A 5 O GLU A 37
SHEET 4 A 5 ALA A 58 ALA A 63 1 O ALA A 62 N ILE A 6
SHEET 5 A 5 LEU A 77 VAL A 80 1 O VAL A 80 N ILE A 61
LINK C TYR A 17 N MSE A 18 1555 1555 1.33
LINK C MSE A 18 N ALA A 19 1555 1555 1.34
CRYST1 48.931 48.931 68.250 90.00 90.00 90.00 P 41 21 2 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 0.020437 0.000000 0.000000 0.00000
SCALE2 0.000000 0.020437 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014652 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
