HEADER PROTEIN BINDING 11-DEC-10 3ASF
TITLE MAMA MSR-1 C2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MAGNETOSOME PROTEIN MAMA;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 41-217;
COMPND 5 SYNONYM: MAGNETOSOME PROTEIN MAMA, TPR-LIKE;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MAGNETOSPIRILLUM GRYPHISWALDENSE;
SOURCE 3 ORGANISM_TAXID: 431944;
SOURCE 4 STRAIN: MSR-1;
SOURCE 5 GENE: MAMA, MGI495, MGR_4099;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET52B
KEYWDS TETRATRICOPEPTIDE REPEATS (TPR) CONTAINING PROTEIN, TPR PROTEIN,
KEYWDS 2 PROTEIN-PROTEIN INTERACTIONS, MAMA, CYTOSOL, PROTEIN BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR N.ZEYTUNI,G.DAVIDOV,R.ZARIVACH
REVDAT 3 01-NOV-23 3ASF 1 REMARK SEQADV
REVDAT 2 26-JUN-13 3ASF 1 JRNL
REVDAT 1 20-JUL-11 3ASF 0
JRNL AUTH N.ZEYTUNI,E.OZYAMAK,K.BEN-HARUSH,G.DAVIDOV,M.LEVIN,Y.GAT,
JRNL AUTH 2 T.MOYAL,A.BRIK,A.KOMEILI,R.ZARIVACH
JRNL TITL SELF-RECOGNITION MECHANISM OF MAMA, A MAGNETOSOME-ASSOCIATED
JRNL TITL 2 TPR-CONTAINING PROTEIN, PROMOTES COMPLEX ASSEMBLY
JRNL REF PROC.NATL.ACAD.SCI.USA V. 108 E480 2011
JRNL REFN ISSN 0027-8424
JRNL PMID 21784982
JRNL DOI 10.1073/PNAS.1103367108
REMARK 2
REMARK 2 RESOLUTION. 2.39 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.39
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.20
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.2
REMARK 3 NUMBER OF REFLECTIONS : 22001
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) : 0.248
REMARK 3 R VALUE (WORKING SET) : 0.247
REMARK 3 FREE R VALUE : 0.270
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1132
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) : 2.39
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.45
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1432
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 90.76
REMARK 3 BIN R VALUE (WORKING SET) : 0.3710
REMARK 3 BIN FREE R VALUE SET COUNT : 61
REMARK 3 BIN FREE R VALUE : 0.4690
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2693
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 65
REMARK 3 SOLVENT ATOMS : 82
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 73.86
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.11000
REMARK 3 B22 (A**2) : 1.80000
REMARK 3 B33 (A**2) : -5.11000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -1.38000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.338
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.198
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 19.448
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.935
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.922
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2852 ; 0.011 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3881 ; 1.374 ; 1.977
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 356 ; 5.479 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 141 ;40.529 ;23.759
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 471 ;20.941 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 22 ;12.459 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 425 ; 0.097 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2160 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): 1727 ; 1.136 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2769 ; 2.074 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1125 ; 1.980 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1105 ; 3.407 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
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 : 32
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 43 A 49
REMARK 3 ORIGIN FOR THE GROUP (A): -28.0315 -30.2605 -24.0604
REMARK 3 T TENSOR
REMARK 3 T11: 0.9320 T22: 0.1523
REMARK 3 T33: 0.4384 T12: -0.0591
REMARK 3 T13: 0.0472 T23: -0.1340
REMARK 3 L TENSOR
REMARK 3 L11: 19.6903 L22: 18.7597
REMARK 3 L33: 12.8697 L12: -0.2037
REMARK 3 L13: -15.9167 L23: 0.0421
REMARK 3 S TENSOR
REMARK 3 S11: -1.9080 S12: -0.1654 S13: -1.9184
REMARK 3 S21: -1.9319 S22: 0.3465 S23: -0.5409
REMARK 3 S31: 1.5130 S32: 0.1217 S33: 1.5616
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 50 A 55
REMARK 3 ORIGIN FOR THE GROUP (A): -31.0680 -23.8987 -17.6530
REMARK 3 T TENSOR
REMARK 3 T11: 0.3620 T22: 0.1628
REMARK 3 T33: 0.6904 T12: 0.1796
REMARK 3 T13: -0.0797 T23: -0.2040
REMARK 3 L TENSOR
REMARK 3 L11: 4.8761 L22: 14.1432
REMARK 3 L33: 49.3862 L12: 7.2734
REMARK 3 L13: 1.7206 L23: -10.1074
REMARK 3 S TENSOR
REMARK 3 S11: -1.1849 S12: -0.6149 S13: -0.1991
REMARK 3 S21: -2.0507 S22: -0.5788 S23: -0.7438
REMARK 3 S31: 0.4672 S32: -1.4291 S33: 1.7637
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 56 A 68
REMARK 3 ORIGIN FOR THE GROUP (A): -25.0672 -21.0317 -12.1896
REMARK 3 T TENSOR
REMARK 3 T11: 0.3339 T22: 0.3655
REMARK 3 T33: 0.2113 T12: -0.0150
REMARK 3 T13: -0.0317 T23: -0.0564
REMARK 3 L TENSOR
REMARK 3 L11: 1.1015 L22: 3.9470
REMARK 3 L33: 4.0044 L12: -1.6597
REMARK 3 L13: -0.8002 L23: -0.9858
REMARK 3 S TENSOR
REMARK 3 S11: 0.0801 S12: -0.0102 S13: -0.0858
REMARK 3 S21: -0.3030 S22: -0.0891 S23: 0.1833
REMARK 3 S31: 0.3419 S32: 0.0175 S33: 0.0090
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 69 A 79
REMARK 3 ORIGIN FOR THE GROUP (A): -25.0161 -18.2814 -27.2572
REMARK 3 T TENSOR
REMARK 3 T11: 0.5002 T22: 0.3329
REMARK 3 T33: 0.1652 T12: 0.1177
REMARK 3 T13: -0.0486 T23: -0.1242
REMARK 3 L TENSOR
REMARK 3 L11: 8.2486 L22: 1.6905
REMARK 3 L33: 1.7061 L12: 2.6743
REMARK 3 L13: -1.6192 L23: -1.5902
REMARK 3 S TENSOR
REMARK 3 S11: 0.2233 S12: 0.1467 S13: -0.1915
REMARK 3 S21: -0.1193 S22: 0.1017 S23: 0.2117
REMARK 3 S31: 0.1425 S32: -0.0816 S33: -0.3249
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 80 A 88
REMARK 3 ORIGIN FOR THE GROUP (A): -28.9832 -14.5046 -19.7116
REMARK 3 T TENSOR
REMARK 3 T11: 0.3362 T22: 0.3044
REMARK 3 T33: 0.2517 T12: 0.1302
REMARK 3 T13: -0.0471 T23: -0.0632
REMARK 3 L TENSOR
REMARK 3 L11: 3.8630 L22: 5.2805
REMARK 3 L33: 6.8230 L12: 4.2913
REMARK 3 L13: -1.3369 L23: 0.3102
REMARK 3 S TENSOR
REMARK 3 S11: -0.0144 S12: 0.0343 S13: 0.1041
REMARK 3 S21: 0.0025 S22: -0.0390 S23: 0.1639
REMARK 3 S31: 0.2245 S32: -0.2471 S33: 0.0535
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 89 A 106
REMARK 3 ORIGIN FOR THE GROUP (A): -21.2262 -9.2639 -19.3129
REMARK 3 T TENSOR
REMARK 3 T11: 0.3020 T22: 0.3326
REMARK 3 T33: 0.1718 T12: 0.0681
REMARK 3 T13: 0.0062 T23: -0.0326
REMARK 3 L TENSOR
REMARK 3 L11: 5.6921 L22: 6.9281
REMARK 3 L33: 1.3783 L12: -2.0776
REMARK 3 L13: 1.5045 L23: -2.0767
REMARK 3 S TENSOR
REMARK 3 S11: 0.3141 S12: 0.2685 S13: 0.0878
REMARK 3 S21: -0.1997 S22: -0.4076 S23: -0.3537
REMARK 3 S31: -0.1280 S32: 0.2615 S33: 0.0935
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 107 A 122
REMARK 3 ORIGIN FOR THE GROUP (A): -33.1723 -4.8502 -20.0659
REMARK 3 T TENSOR
REMARK 3 T11: 0.3291 T22: 0.1939
REMARK 3 T33: 0.2512 T12: 0.1191
REMARK 3 T13: 0.0065 T23: -0.0303
REMARK 3 L TENSOR
REMARK 3 L11: 3.5002 L22: 2.3676
REMARK 3 L33: 17.2919 L12: 0.1607
REMARK 3 L13: 1.2036 L23: 4.3750
REMARK 3 S TENSOR
REMARK 3 S11: 0.0766 S12: 0.3700 S13: 0.2742
REMARK 3 S21: 0.3128 S22: -0.1650 S23: 0.3694
REMARK 3 S31: 0.2567 S32: -0.0240 S33: 0.0883
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 123 A 127
REMARK 3 ORIGIN FOR THE GROUP (A): -23.0615 -1.2052 -13.0309
REMARK 3 T TENSOR
REMARK 3 T11: 0.3355 T22: 0.3117
REMARK 3 T33: 0.2700 T12: 0.1039
REMARK 3 T13: 0.0094 T23: -0.0131
REMARK 3 L TENSOR
REMARK 3 L11: 11.9622 L22: 4.3835
REMARK 3 L33: 3.9749 L12: 3.1912
REMARK 3 L13: -0.5279 L23: -2.1884
REMARK 3 S TENSOR
REMARK 3 S11: -0.0336 S12: -0.2811 S13: -0.5371
REMARK 3 S21: 0.0680 S22: -0.3213 S23: -0.1297
REMARK 3 S31: 0.0600 S32: 0.3151 S33: 0.3550
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 128 A 138
REMARK 3 ORIGIN FOR THE GROUP (A): -26.8592 4.7261 -15.5693
REMARK 3 T TENSOR
REMARK 3 T11: 0.3357 T22: 0.3237
REMARK 3 T33: 0.2136 T12: 0.0389
REMARK 3 T13: 0.0169 T23: -0.0041
REMARK 3 L TENSOR
REMARK 3 L11: 11.7734 L22: 1.2164
REMARK 3 L33: 5.3719 L12: 2.6104
REMARK 3 L13: 1.0425 L23: -0.6356
REMARK 3 S TENSOR
REMARK 3 S11: 0.0913 S12: 0.2520 S13: -0.1040
REMARK 3 S21: -0.1870 S22: -0.0595 S23: 0.0193
REMARK 3 S31: 0.1375 S32: 0.2834 S33: -0.0319
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 139 A 144
REMARK 3 ORIGIN FOR THE GROUP (A): -39.8488 1.8372 -14.3913
REMARK 3 T TENSOR
REMARK 3 T11: 0.3441 T22: 0.3198
REMARK 3 T33: 0.2741 T12: 0.0046
REMARK 3 T13: 0.0120 T23: -0.0354
REMARK 3 L TENSOR
REMARK 3 L11: 8.5525 L22: 8.5074
REMARK 3 L33: 12.5898 L12: 3.3143
REMARK 3 L13: -7.2959 L23: -3.1655
REMARK 3 S TENSOR
REMARK 3 S11: -0.1055 S12: 0.0667 S13: 0.2519
REMARK 3 S21: -0.0844 S22: 0.0676 S23: 0.1871
REMARK 3 S31: 0.1997 S32: -0.4772 S33: 0.0379
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 145 A 159
REMARK 3 ORIGIN FOR THE GROUP (A): -32.7142 3.4329 -6.3991
REMARK 3 T TENSOR
REMARK 3 T11: 0.3247 T22: 0.2615
REMARK 3 T33: 0.2177 T12: 0.0545
REMARK 3 T13: 0.0338 T23: -0.0073
REMARK 3 L TENSOR
REMARK 3 L11: 6.4545 L22: 3.4463
REMARK 3 L33: 4.7211 L12: 3.9836
REMARK 3 L13: -0.1553 L23: -0.0151
REMARK 3 S TENSOR
REMARK 3 S11: 0.0464 S12: -0.0492 S13: -0.0812
REMARK 3 S21: 0.1045 S22: -0.1045 S23: -0.0034
REMARK 3 S31: 0.1372 S32: 0.1425 S33: 0.0580
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 160 A 176
REMARK 3 ORIGIN FOR THE GROUP (A): -32.1974 11.9866 -4.8836
REMARK 3 T TENSOR
REMARK 3 T11: 0.3642 T22: 0.2964
REMARK 3 T33: 0.2333 T12: -0.0009
REMARK 3 T13: -0.0164 T23: -0.0006
REMARK 3 L TENSOR
REMARK 3 L11: 3.9401 L22: 2.2718
REMARK 3 L33: 1.6691 L12: 1.1207
REMARK 3 L13: -1.0444 L23: -0.1752
REMARK 3 S TENSOR
REMARK 3 S11: 0.0515 S12: 0.1601 S13: 0.1818
REMARK 3 S21: -0.0745 S22: 0.0017 S23: 0.1188
REMARK 3 S31: -0.3063 S32: -0.1004 S33: -0.0532
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 177 A 192
REMARK 3 ORIGIN FOR THE GROUP (A): -31.7654 6.8872 3.6337
REMARK 3 T TENSOR
REMARK 3 T11: 0.3060 T22: 0.3029
REMARK 3 T33: 0.1881 T12: 0.0083
REMARK 3 T13: -0.0206 T23: 0.0427
REMARK 3 L TENSOR
REMARK 3 L11: 1.8791 L22: 2.3811
REMARK 3 L33: 2.8167 L12: 0.1184
REMARK 3 L13: 0.0886 L23: 2.1334
REMARK 3 S TENSOR
REMARK 3 S11: -0.0948 S12: -0.4878 S13: -0.0597
REMARK 3 S21: -0.0202 S22: 0.0858 S23: 0.0430
REMARK 3 S31: 0.0994 S32: 0.1303 S33: 0.0090
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 193 A 204
REMARK 3 ORIGIN FOR THE GROUP (A): -27.3899 18.4133 5.5927
REMARK 3 T TENSOR
REMARK 3 T11: 0.3397 T22: 0.3288
REMARK 3 T33: 0.2792 T12: 0.0030
REMARK 3 T13: -0.0698 T23: -0.0022
REMARK 3 L TENSOR
REMARK 3 L11: 1.3099 L22: 4.4719
REMARK 3 L33: 8.0118 L12: 2.0333
REMARK 3 L13: -0.4773 L23: 2.3641
REMARK 3 S TENSOR
REMARK 3 S11: 0.0159 S12: -0.1088 S13: 0.0215
REMARK 3 S21: -0.0122 S22: -0.1117 S23: -0.0536
REMARK 3 S31: -0.3921 S32: 0.1049 S33: 0.0958
REMARK 3
REMARK 3 TLS GROUP : 15
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 205 A 210
REMARK 3 ORIGIN FOR THE GROUP (A): -30.4888 9.2146 12.5817
REMARK 3 T TENSOR
REMARK 3 T11: 0.3684 T22: 0.3402
REMARK 3 T33: 0.1483 T12: -0.0884
REMARK 3 T13: -0.0628 T23: 0.0391
REMARK 3 L TENSOR
REMARK 3 L11: 2.3470 L22: 10.0034
REMARK 3 L33: 8.8600 L12: 0.4568
REMARK 3 L13: -3.2227 L23: 5.9716
REMARK 3 S TENSOR
REMARK 3 S11: 0.3869 S12: -0.3065 S13: -0.1402
REMARK 3 S21: 0.7134 S22: -0.7638 S23: 0.2074
REMARK 3 S31: -0.0399 S32: 0.0278 S33: 0.3769
REMARK 3
REMARK 3 TLS GROUP : 16
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 211 A 216
REMARK 3 ORIGIN FOR THE GROUP (A): -32.6541 0.3163 14.7730
REMARK 3 T TENSOR
REMARK 3 T11: 1.3691 T22: 0.2338
REMARK 3 T33: 0.4949 T12: -0.1841
REMARK 3 T13: -0.0762 T23: 0.2503
REMARK 3 L TENSOR
REMARK 3 L11: 6.7085 L22: 87.4940
REMARK 3 L33: 4.5760 L12: 24.1887
REMARK 3 L13: -5.5348 L23: -20.0020
REMARK 3 S TENSOR
REMARK 3 S11: -0.1221 S12: -0.0236 S13: -1.2023
REMARK 3 S21: 1.4352 S22: -0.4926 S23: -4.3216
REMARK 3 S31: -0.2829 S32: 0.0069 S33: 0.6147
REMARK 3
REMARK 3 TLS GROUP : 17
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 44 B 55
REMARK 3 ORIGIN FOR THE GROUP (A): -23.6205 33.2078 -24.6024
REMARK 3 T TENSOR
REMARK 3 T11: 0.8072 T22: 0.4627
REMARK 3 T33: 0.8807 T12: 0.0309
REMARK 3 T13: 0.0556 T23: 0.4343
REMARK 3 L TENSOR
REMARK 3 L11: 11.3492 L22: 1.4973
REMARK 3 L33: 1.5972 L12: -3.3325
REMARK 3 L13: -4.1479 L23: 1.0165
REMARK 3 S TENSOR
REMARK 3 S11: -0.7197 S12: -1.6234 S13: -0.0886
REMARK 3 S21: 0.3755 S22: 0.8611 S23: 0.6897
REMARK 3 S31: 0.1895 S32: 0.4827 S33: -0.1414
REMARK 3
REMARK 3 TLS GROUP : 18
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 56 B 68
REMARK 3 ORIGIN FOR THE GROUP (A): -19.6073 26.0059 -33.4976
REMARK 3 T TENSOR
REMARK 3 T11: 0.5856 T22: 0.3768
REMARK 3 T33: 0.2112 T12: -0.2576
REMARK 3 T13: -0.0374 T23: 0.1486
REMARK 3 L TENSOR
REMARK 3 L11: 8.7991 L22: 0.2540
REMARK 3 L33: 0.7217 L12: 1.4930
REMARK 3 L13: -0.7492 L23: -0.1117
REMARK 3 S TENSOR
REMARK 3 S11: 0.1459 S12: -0.5008 S13: 0.2605
REMARK 3 S21: 0.0094 S22: -0.0962 S23: 0.0415
REMARK 3 S31: -0.3129 S32: -0.1168 S33: -0.0496
REMARK 3
REMARK 3 TLS GROUP : 19
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 69 B 86
REMARK 3 ORIGIN FOR THE GROUP (A): -22.3082 22.4246 -21.2025
REMARK 3 T TENSOR
REMARK 3 T11: 0.5981 T22: 0.3053
REMARK 3 T33: 0.4488 T12: -0.2222
REMARK 3 T13: 0.1996 T23: 0.1125
REMARK 3 L TENSOR
REMARK 3 L11: 8.6670 L22: 0.9489
REMARK 3 L33: 4.7674 L12: 0.0346
REMARK 3 L13: 1.1871 L23: 0.6298
REMARK 3 S TENSOR
REMARK 3 S11: 0.0221 S12: 0.4875 S13: 0.4172
REMARK 3 S21: 0.4216 S22: 0.1886 S23: 0.5176
REMARK 3 S31: -0.4279 S32: 0.8902 S33: -0.2107
REMARK 3
REMARK 3 TLS GROUP : 20
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 87 B 97
REMARK 3 ORIGIN FOR THE GROUP (A): -16.7835 14.9817 -31.1063
REMARK 3 T TENSOR
REMARK 3 T11: 0.2314 T22: 0.7141
REMARK 3 T33: 0.1871 T12: -0.2723
REMARK 3 T13: 0.0699 T23: -0.0867
REMARK 3 L TENSOR
REMARK 3 L11: 12.7544 L22: 2.3621
REMARK 3 L33: 12.5842 L12: -4.7200
REMARK 3 L13: -3.5398 L23: -1.1542
REMARK 3 S TENSOR
REMARK 3 S11: 0.3363 S12: -0.3919 S13: 0.0436
REMARK 3 S21: -0.3218 S22: 0.2859 S23: 0.0883
REMARK 3 S31: 0.3202 S32: 0.6740 S33: -0.6223
REMARK 3
REMARK 3 TLS GROUP : 21
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 98 B 109
REMARK 3 ORIGIN FOR THE GROUP (A): -22.7182 12.2945 -22.5559
REMARK 3 T TENSOR
REMARK 3 T11: 0.3453 T22: 0.4402
REMARK 3 T33: 0.1021 T12: -0.0167
REMARK 3 T13: -0.0560 T23: 0.0599
REMARK 3 L TENSOR
REMARK 3 L11: 7.9079 L22: 5.9176
REMARK 3 L33: 1.7324 L12: -1.4918
REMARK 3 L13: -3.6753 L23: 0.5785
REMARK 3 S TENSOR
REMARK 3 S11: -0.1363 S12: -0.0444 S13: -0.3174
REMARK 3 S21: 0.1128 S22: -0.0235 S23: 0.0846
REMARK 3 S31: 0.0509 S32: 0.1191 S33: 0.1599
REMARK 3
REMARK 3 TLS GROUP : 22
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 110 B 124
REMARK 3 ORIGIN FOR THE GROUP (A): -29.0599 10.7351 -29.1072
REMARK 3 T TENSOR
REMARK 3 T11: 0.2863 T22: 0.3691
REMARK 3 T33: 0.3445 T12: 0.0096
REMARK 3 T13: -0.0846 T23: -0.0704
REMARK 3 L TENSOR
REMARK 3 L11: 3.7015 L22: 1.4883
REMARK 3 L33: 7.8599 L12: -0.8702
REMARK 3 L13: -1.9352 L23: 3.2604
REMARK 3 S TENSOR
REMARK 3 S11: -0.1026 S12: -0.0819 S13: -0.1360
REMARK 3 S21: -0.1431 S22: -0.0008 S23: 0.2429
REMARK 3 S31: -0.1652 S32: 0.3060 S33: 0.1034
REMARK 3
REMARK 3 TLS GROUP : 23
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 125 B 131
REMARK 3 ORIGIN FOR THE GROUP (A): -20.5403 1.1705 -33.4689
REMARK 3 T TENSOR
REMARK 3 T11: 0.2616 T22: 0.4485
REMARK 3 T33: 0.1796 T12: 0.1946
REMARK 3 T13: 0.0897 T23: -0.0488
REMARK 3 L TENSOR
REMARK 3 L11: 21.1364 L22: 2.7690
REMARK 3 L33: 4.2306 L12: 7.5525
REMARK 3 L13: 7.5188 L23: 3.0136
REMARK 3 S TENSOR
REMARK 3 S11: 0.0545 S12: 0.5776 S13: -1.0268
REMARK 3 S21: 0.0181 S22: 0.2278 S23: -0.3516
REMARK 3 S31: 0.0784 S32: 0.4472 S33: -0.2823
REMARK 3
REMARK 3 TLS GROUP : 24
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 132 B 142
REMARK 3 ORIGIN FOR THE GROUP (A): -32.9408 4.1018 -31.2506
REMARK 3 T TENSOR
REMARK 3 T11: 0.3867 T22: 0.3975
REMARK 3 T33: 0.2719 T12: 0.0716
REMARK 3 T13: -0.0151 T23: -0.0401
REMARK 3 L TENSOR
REMARK 3 L11: 3.3498 L22: 5.5533
REMARK 3 L33: 0.2918 L12: -0.4857
REMARK 3 L13: -0.7123 L23: -0.7648
REMARK 3 S TENSOR
REMARK 3 S11: 0.0984 S12: -0.2678 S13: 0.1015
REMARK 3 S21: 0.0374 S22: -0.0580 S23: 0.1217
REMARK 3 S31: 0.0021 S32: 0.0667 S33: -0.0404
REMARK 3
REMARK 3 TLS GROUP : 25
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 143 B 156
REMARK 3 ORIGIN FOR THE GROUP (A): -32.2003 6.3569 -40.7443
REMARK 3 T TENSOR
REMARK 3 T11: 0.3110 T22: 0.3235
REMARK 3 T33: 0.3363 T12: 0.0498
REMARK 3 T13: -0.0079 T23: 0.0540
REMARK 3 L TENSOR
REMARK 3 L11: 1.9166 L22: 3.1937
REMARK 3 L33: 7.1100 L12: -0.2706
REMARK 3 L13: -1.8350 L23: 1.7259
REMARK 3 S TENSOR
REMARK 3 S11: 0.1346 S12: 0.2464 S13: 0.6513
REMARK 3 S21: -0.1539 S22: -0.0337 S23: -0.0660
REMARK 3 S31: 0.1156 S32: 0.2839 S33: -0.1009
REMARK 3
REMARK 3 TLS GROUP : 26
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 157 B 164
REMARK 3 ORIGIN FOR THE GROUP (A): -27.9704 -7.3333 -37.5304
REMARK 3 T TENSOR
REMARK 3 T11: 0.6090 T22: 0.4885
REMARK 3 T33: 0.2600 T12: 0.2356
REMARK 3 T13: -0.0585 T23: -0.0256
REMARK 3 L TENSOR
REMARK 3 L11: 0.5002 L22: 8.4972
REMARK 3 L33: 4.6092 L12: 2.0056
REMARK 3 L13: 1.4849 L23: 6.2558
REMARK 3 S TENSOR
REMARK 3 S11: 0.1122 S12: 0.1256 S13: -0.0621
REMARK 3 S21: 0.3184 S22: 0.2263 S23: -0.5072
REMARK 3 S31: 0.2404 S32: 0.1690 S33: -0.3385
REMARK 3
REMARK 3 TLS GROUP : 27
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 165 B 171
REMARK 3 ORIGIN FOR THE GROUP (A): -34.5847 -5.0144 -42.1538
REMARK 3 T TENSOR
REMARK 3 T11: 0.4989 T22: 0.2876
REMARK 3 T33: 0.1855 T12: 0.0801
REMARK 3 T13: -0.0911 T23: -0.2043
REMARK 3 L TENSOR
REMARK 3 L11: 12.1820 L22: 13.0198
REMARK 3 L33: 22.4117 L12: -11.5415
REMARK 3 L13: 15.5986 L23: -12.5252
REMARK 3 S TENSOR
REMARK 3 S11: 1.0968 S12: 0.0989 S13: -0.6445
REMARK 3 S21: -0.8532 S22: -0.3814 S23: 0.6935
REMARK 3 S31: 1.5187 S32: -0.2102 S33: -0.7154
REMARK 3
REMARK 3 TLS GROUP : 28
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 172 B 184
REMARK 3 ORIGIN FOR THE GROUP (A): -33.5150 3.8968 -50.0976
REMARK 3 T TENSOR
REMARK 3 T11: 0.3328 T22: 0.3600
REMARK 3 T33: 0.3074 T12: 0.0732
REMARK 3 T13: -0.0359 T23: 0.0115
REMARK 3 L TENSOR
REMARK 3 L11: 3.8119 L22: 2.9765
REMARK 3 L33: 5.5960 L12: -0.8749
REMARK 3 L13: 2.6592 L23: 1.5876
REMARK 3 S TENSOR
REMARK 3 S11: 0.1678 S12: 0.4634 S13: 0.4302
REMARK 3 S21: -0.2936 S22: -0.1208 S23: 0.2780
REMARK 3 S31: -0.0173 S32: 0.4162 S33: -0.0470
REMARK 3
REMARK 3 TLS GROUP : 29
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 185 B 193
REMARK 3 ORIGIN FOR THE GROUP (A): -28.6164 -7.4816 -49.4507
REMARK 3 T TENSOR
REMARK 3 T11: 0.4756 T22: 0.3456
REMARK 3 T33: 0.2491 T12: 0.1597
REMARK 3 T13: -0.1475 T23: -0.2647
REMARK 3 L TENSOR
REMARK 3 L11: 3.0640 L22: 15.5019
REMARK 3 L33: 10.7781 L12: 5.1641
REMARK 3 L13: -4.8270 L23: -12.7797
REMARK 3 S TENSOR
REMARK 3 S11: 0.3220 S12: 0.3900 S13: -0.6473
REMARK 3 S21: -0.2579 S22: -0.7478 S23: -0.2231
REMARK 3 S31: 0.0580 S32: 0.3412 S33: 0.4258
REMARK 3
REMARK 3 TLS GROUP : 30
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 194 B 202
REMARK 3 ORIGIN FOR THE GROUP (A): -32.1920 -14.3200 -50.7759
REMARK 3 T TENSOR
REMARK 3 T11: 2.0971 T22: 0.3746
REMARK 3 T33: 0.6083 T12: -0.4903
REMARK 3 T13: -0.4499 T23: -0.2590
REMARK 3 L TENSOR
REMARK 3 L11: 13.4059 L22: 31.8679
REMARK 3 L33: 5.2269 L12: 20.6516
REMARK 3 L13: 7.7666 L23: 12.1320
REMARK 3 S TENSOR
REMARK 3 S11: -0.0545 S12: 0.6097 S13: -0.9748
REMARK 3 S21: 0.1805 S22: 0.7956 S23: -1.4514
REMARK 3 S31: 1.1910 S32: -0.0003 S33: -0.7411
REMARK 3
REMARK 3 TLS GROUP : 31
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 203 B 207
REMARK 3 ORIGIN FOR THE GROUP (A): -30.4281 -6.6435 -56.8996
REMARK 3 T TENSOR
REMARK 3 T11: 0.8686 T22: 1.0575
REMARK 3 T33: 0.3277 T12: -0.1945
REMARK 3 T13: -0.3074 T23: 0.2515
REMARK 3 L TENSOR
REMARK 3 L11: 0.4384 L22: 0.2565
REMARK 3 L33: 27.0174 L12: 0.2912
REMARK 3 L13: -2.9465 L23: -1.3057
REMARK 3 S TENSOR
REMARK 3 S11: -0.4461 S12: 0.4656 S13: 0.1672
REMARK 3 S21: -0.2508 S22: 0.5402 S23: 0.1753
REMARK 3 S31: 3.8633 S32: -1.4585 S33: -0.0941
REMARK 3
REMARK 3 TLS GROUP : 32
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 208 B 213
REMARK 3 ORIGIN FOR THE GROUP (A): -26.2739 0.5700 -60.4202
REMARK 3 T TENSOR
REMARK 3 T11: 0.3743 T22: 0.8651
REMARK 3 T33: 0.7017 T12: -0.0283
REMARK 3 T13: 0.1069 T23: 0.1102
REMARK 3 L TENSOR
REMARK 3 L11: 15.0294 L22: 4.7778
REMARK 3 L33: 31.0533 L12: -8.4616
REMARK 3 L13: -21.6024 L23: 12.1600
REMARK 3 S TENSOR
REMARK 3 S11: 0.1251 S12: 0.6612 S13: -0.1936
REMARK 3 S21: -0.0909 S22: -0.4057 S23: 0.0104
REMARK 3 S31: -0.2121 S32: -0.9054 S33: 0.2806
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
REMARK 3 U VALUES: WITH TLS ADDED
REMARK 4
REMARK 4 3ASF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 21-DEC-10.
REMARK 100 THE DEPOSITION ID IS D_1000029638.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-JUL-09
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 : ESRF
REMARK 200 BEAMLINE : ID14-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.933
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22523
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.390
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 7.300
REMARK 200 R MERGE (I) : 0.07900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.44
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.30
REMARK 200 R MERGE FOR SHELL (I) : 0.55800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: COOT
REMARK 200 STARTING MODEL: PDB ENTRY 3AS5
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 64.69
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.48
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFAT, HEPES, NACL, PH 7.5,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 286K
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 43.56450
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 36.68850
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 43.56450
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 36.68850
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 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 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 MET A 39
REMARK 465 GLY A 40
REMARK 465 ASN A 41
REMARK 465 ASP A 42
REMARK 465 VAL A 217
REMARK 465 GLU A 218
REMARK 465 LEU A 219
REMARK 465 ALA A 220
REMARK 465 LEU A 221
REMARK 465 VAL A 222
REMARK 465 PRO A 223
REMARK 465 ARG A 224
REMARK 465 MET B 39
REMARK 465 GLY B 40
REMARK 465 ASN B 41
REMARK 465 ASP B 42
REMARK 465 ASP B 43
REMARK 465 ARG B 214
REMARK 465 SER B 215
REMARK 465 ALA B 216
REMARK 465 VAL B 217
REMARK 465 GLU B 218
REMARK 465 LEU B 219
REMARK 465 ALA B 220
REMARK 465 LEU B 221
REMARK 465 VAL B 222
REMARK 465 PRO B 223
REMARK 465 ARG B 224
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 ASP B 212 CG OD1 OD2
REMARK 470 GLU B 213 CG CD OE1 OE2
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 O2 SO4 B 12 O HOH B 239 2.00
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 ALA A 110 76.86 -154.07
REMARK 500 ALA B 77 42.83 -142.82
REMARK 500 THR B 93 51.01 -92.23
REMARK 500 ASN B 144 71.44 -118.32
REMARK 500 PHE B 164 -60.78 17.12
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 SO4 A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 4
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 10
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 24
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 31
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 32
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 33
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 9
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 12
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 28
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 29
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 34
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3AS4 RELATED DB: PDB
REMARK 900 HOMOLOGOUS STRUCTURE
REMARK 900 RELATED ID: 3AS5 RELATED DB: PDB
REMARK 900 HOMOLOGOUS STRUCTURE
REMARK 900 RELATED ID: 3AS8 RELATED DB: PDB
REMARK 900 DIFFERENT PACKING
REMARK 900 RELATED ID: 3ASD RELATED DB: PDB
REMARK 900 R50E MUTANT OF HOMOLOGOUS STRUCTURE
REMARK 900 RELATED ID: 3ASG RELATED DB: PDB
REMARK 900 D159K MUTANT OF HOMOLOGOUS STRUCTURE
REMARK 900 RELATED ID: 3ASH RELATED DB: PDB
REMARK 900 D159K MUTANT OF HOMOLOGOUS STRUCTURE
DBREF 3ASF A 41 217 UNP Q93DY9 Q93DY9_9PROT 41 217
DBREF 3ASF B 41 217 UNP Q93DY9 Q93DY9_9PROT 41 217
SEQADV 3ASF MET A 39 UNP Q93DY9 EXPRESSION TAG
SEQADV 3ASF GLY A 40 UNP Q93DY9 EXPRESSION TAG
SEQADV 3ASF GLU A 218 UNP Q93DY9 EXPRESSION TAG
SEQADV 3ASF LEU A 219 UNP Q93DY9 EXPRESSION TAG
SEQADV 3ASF ALA A 220 UNP Q93DY9 EXPRESSION TAG
SEQADV 3ASF LEU A 221 UNP Q93DY9 EXPRESSION TAG
SEQADV 3ASF VAL A 222 UNP Q93DY9 EXPRESSION TAG
SEQADV 3ASF PRO A 223 UNP Q93DY9 EXPRESSION TAG
SEQADV 3ASF ARG A 224 UNP Q93DY9 EXPRESSION TAG
SEQADV 3ASF MET B 39 UNP Q93DY9 EXPRESSION TAG
SEQADV 3ASF GLY B 40 UNP Q93DY9 EXPRESSION TAG
SEQADV 3ASF GLU B 218 UNP Q93DY9 EXPRESSION TAG
SEQADV 3ASF LEU B 219 UNP Q93DY9 EXPRESSION TAG
SEQADV 3ASF ALA B 220 UNP Q93DY9 EXPRESSION TAG
SEQADV 3ASF LEU B 221 UNP Q93DY9 EXPRESSION TAG
SEQADV 3ASF VAL B 222 UNP Q93DY9 EXPRESSION TAG
SEQADV 3ASF PRO B 223 UNP Q93DY9 EXPRESSION TAG
SEQADV 3ASF ARG B 224 UNP Q93DY9 EXPRESSION TAG
SEQRES 1 A 186 MET GLY ASN ASP ASP ILE ARG GLN VAL TYR TYR ARG ASP
SEQRES 2 A 186 LYS GLY ILE SER HIS ALA LYS ALA GLY ARG TYR SER GLU
SEQRES 3 A 186 ALA VAL VAL MET LEU GLU GLN VAL TYR ASP ALA ASP ALA
SEQRES 4 A 186 PHE ASP VAL GLU VAL ALA LEU HIS LEU GLY ILE ALA TYR
SEQRES 5 A 186 VAL LYS THR GLY ALA VAL ASP ARG GLY THR GLU LEU LEU
SEQRES 6 A 186 GLU ARG SER ILE ALA ASP ALA PRO ASP ASN ILE LYS VAL
SEQRES 7 A 186 ALA THR VAL LEU GLY LEU THR TYR VAL GLN VAL GLN LYS
SEQRES 8 A 186 TYR ASP LEU ALA VAL PRO LEU LEU VAL LYS VAL ALA GLU
SEQRES 9 A 186 ALA ASN PRO VAL ASN PHE ASN VAL ARG PHE ARG LEU GLY
SEQRES 10 A 186 VAL ALA LEU ASP ASN LEU GLY ARG PHE ASP GLU ALA ILE
SEQRES 11 A 186 ASP SER PHE LYS ILE ALA LEU GLY LEU ARG PRO ASN GLU
SEQRES 12 A 186 GLY LYS VAL HIS ARG ALA ILE ALA TYR SER TYR GLU GLN
SEQRES 13 A 186 MET GLY SER HIS GLU GLU ALA LEU PRO HIS PHE LYS LYS
SEQRES 14 A 186 ALA ASN GLU LEU ASP GLU ARG SER ALA VAL GLU LEU ALA
SEQRES 15 A 186 LEU VAL PRO ARG
SEQRES 1 B 186 MET GLY ASN ASP ASP ILE ARG GLN VAL TYR TYR ARG ASP
SEQRES 2 B 186 LYS GLY ILE SER HIS ALA LYS ALA GLY ARG TYR SER GLU
SEQRES 3 B 186 ALA VAL VAL MET LEU GLU GLN VAL TYR ASP ALA ASP ALA
SEQRES 4 B 186 PHE ASP VAL GLU VAL ALA LEU HIS LEU GLY ILE ALA TYR
SEQRES 5 B 186 VAL LYS THR GLY ALA VAL ASP ARG GLY THR GLU LEU LEU
SEQRES 6 B 186 GLU ARG SER ILE ALA ASP ALA PRO ASP ASN ILE LYS VAL
SEQRES 7 B 186 ALA THR VAL LEU GLY LEU THR TYR VAL GLN VAL GLN LYS
SEQRES 8 B 186 TYR ASP LEU ALA VAL PRO LEU LEU VAL LYS VAL ALA GLU
SEQRES 9 B 186 ALA ASN PRO VAL ASN PHE ASN VAL ARG PHE ARG LEU GLY
SEQRES 10 B 186 VAL ALA LEU ASP ASN LEU GLY ARG PHE ASP GLU ALA ILE
SEQRES 11 B 186 ASP SER PHE LYS ILE ALA LEU GLY LEU ARG PRO ASN GLU
SEQRES 12 B 186 GLY LYS VAL HIS ARG ALA ILE ALA TYR SER TYR GLU GLN
SEQRES 13 B 186 MET GLY SER HIS GLU GLU ALA LEU PRO HIS PHE LYS LYS
SEQRES 14 B 186 ALA ASN GLU LEU ASP GLU ARG SER ALA VAL GLU LEU ALA
SEQRES 15 B 186 LEU VAL PRO ARG
HET SO4 A 1 5
HET SO4 A 2 5
HET SO4 A 4 5
HET SO4 A 10 5
HET SO4 A 24 5
HET SO4 A 31 5
HET SO4 A 32 5
HET SO4 A 33 5
HET SO4 B 9 5
HET SO4 B 12 5
HET SO4 B 28 5
HET SO4 B 29 5
HET SO4 B 34 5
HETNAM SO4 SULFATE ION
FORMUL 3 SO4 13(O4 S 2-)
FORMUL 16 HOH *82(H2 O)
HELIX 1 1 ASP A 43 ALA A 59 1 17
HELIX 2 2 ARG A 61 GLU A 70 1 10
HELIX 3 3 ASP A 79 THR A 93 1 15
HELIX 4 4 ALA A 95 ALA A 110 1 16
HELIX 5 5 ASN A 113 VAL A 127 1 15
HELIX 6 6 LYS A 129 ASN A 144 1 16
HELIX 7 7 ASN A 147 LEU A 161 1 15
HELIX 8 8 ARG A 163 ARG A 178 1 16
HELIX 9 9 GLU A 181 MET A 195 1 15
HELIX 10 10 SER A 197 ARG A 214 1 18
HELIX 11 11 ILE B 44 ILE B 54 1 11
HELIX 12 12 ILE B 54 ALA B 59 1 6
HELIX 13 13 ARG B 61 GLU B 70 1 10
HELIX 14 14 ASP B 79 THR B 93 1 15
HELIX 15 15 ALA B 95 ALA B 110 1 16
HELIX 16 16 ASN B 113 VAL B 127 1 15
HELIX 17 17 LYS B 129 ASN B 144 1 16
HELIX 18 18 ASN B 147 LEU B 161 1 15
HELIX 19 19 PHE B 164 ARG B 178 1 15
HELIX 20 20 GLU B 181 GLY B 196 1 16
HELIX 21 21 SER B 197 ASP B 212 1 16
SITE 1 AC1 4 ALA A 95 VAL A 96 ASP A 97 ARG A 98
SITE 1 AC2 3 ARG A 178 HOH A 239 HOH A 261
SITE 1 AC3 2 TYR A 62 HIS A 198
SITE 1 AC4 2 ARG A 153 HOH A 250
SITE 1 AC5 4 ARG A 163 PHE A 164 ASP A 165 GLU A 166
SITE 1 AC6 4 GLN A 126 ASN A 149 ARG A 153 HOH A 255
SITE 1 AC7 4 LYS A 172 HOH A 227 HOH A 254 HOH A 259
SITE 1 AC8 3 LYS A 52 HIS A 56 ARG A 61
SITE 1 AC9 3 ASN B 149 ARG B 178 HOH B 237
SITE 1 BC1 5 LYS B 52 SER B 55 ALA B 59 ARG B 61
SITE 2 BC1 5 HOH B 239
SITE 1 BC2 2 ARG B 153 HOH B 228
SITE 1 BC3 3 LEU B 122 ASN B 149 ARG B 153
SITE 1 BC4 4 VAL B 146 PHE B 148 ARG B 178 HOH B 237
CRYST1 87.129 73.377 90.224 90.00 93.70 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 0.011477 0.000000 0.000743 0.00000
SCALE2 0.000000 0.013628 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011107 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
