HEADER TRANSCRIPTION 10-FEB-14 4OQP
TITLE STRUCTURE OF THE EFFECTOR-BINDING DOMAIN OF DEOXYRIBONUCLEOSIDE
TITLE 2 REGULATOR DEOR FROM BACILLUS SUBTILIS IN COMPLEX WITH DEOXYRIBOSE-5-
TITLE 3 PHOSPHATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DEOXYRIBONUCLEOSIDE REGULATOR;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: C-TERMINAL DOMAIN;
COMPND 5 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: DEOR, YXXC, BSU39430;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
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: PET151
KEYWDS ROSSMANN FOLD, SUGAR-BINDING TRANSCRIPTIONAL REGULATOR, SCHIFF BASE,
KEYWDS 2 TRANSCRIPTION
EXPDTA X-RAY DIFFRACTION
AUTHOR P.REZACOVA,J.SKERLOVA
REVDAT 5 20-SEP-23 4OQP 1 REMARK LINK
REVDAT 4 20-NOV-19 4OQP 1 SEQADV LINK
REVDAT 3 01-OCT-14 4OQP 1 JRNL
REVDAT 2 18-JUN-14 4OQP 1 JRNL
REVDAT 1 04-JUN-14 4OQP 0
JRNL AUTH J.SKERLOVA,M.FABRY,M.HUBALEK,Z.OTWINOWSKI,P.REZACOVA
JRNL TITL STRUCTURE OF THE EFFECTOR-BINDING DOMAIN OF
JRNL TITL 2 DEOXYRIBONUCLEOSIDE REGULATOR DEOR FROM BACILLUS SUBTILIS.
JRNL REF FEBS J. V. 281 4280 2014
JRNL REFN ISSN 1742-464X
JRNL PMID 24863636
JRNL DOI 10.1111/FEBS.12856
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH P.REZACOVA,M.KOZISEK,S.F.MOY,I.SIEGLOVA,A.JOACHIMIAK,
REMARK 1 AUTH 2 M.MACHIUS,Z.OTWINOWSKI
REMARK 1 TITL CRYSTAL STRUCTURES OF THE EFFECTOR-BINDING DOMAIN OF
REMARK 1 TITL 2 REPRESSOR CENTRAL GLYCOLYTIC GENE REGULATOR FROM BACILLUS
REMARK 1 TITL 3 SUBTILIS REVEAL LIGAND-INDUCED STRUCTURAL CHANGES UPON
REMARK 1 TITL 4 BINDING OF SEVERAL GLYCOLYTIC INTERMEDIATES.
REMARK 1 REF MOL.MICROBIOL. V. 69 895 2008
REMARK 1 REFN ISSN 0950-382X
REMARK 1 PMID 18554327
REMARK 1 DOI 10.1111/J.1365-2958.2008.06318.X
REMARK 1 REFERENCE 2
REMARK 1 AUTH J.PISACKOVA,K.PROCHAZKOVA,M.FABRY,P.REZACOVA
REMARK 1 TITL CRYSTALLIZATION OF THE EFFECTOR-BINDING DOMAIN OF REPRESSOR
REMARK 1 TITL 2 DEOR FROM BACILLUS SUBTILIS
REMARK 1 REF CRYST.GROWTHDES. V. 13 844 2013
REMARK 1 REFN ISSN 1528-7483
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0032
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) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.77
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.4
REMARK 3 NUMBER OF REFLECTIONS : 32880
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) : 0.156
REMARK 3 R VALUE (WORKING SET) : 0.154
REMARK 3 FREE R VALUE : 0.191
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1750
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) : 1.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.64
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1548
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 59.99
REMARK 3 BIN R VALUE (WORKING SET) : 0.2370
REMARK 3 BIN FREE R VALUE SET COUNT : 74
REMARK 3 BIN FREE R VALUE : 0.2860
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1988
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 18
REMARK 3 SOLVENT ATOMS : 264
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.60
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
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): 0.082
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.085
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.055
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.784
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.972
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.958
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2163 ; 0.012 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2117 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2949 ; 1.488 ; 1.967
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4894 ; 0.847 ; 3.001
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 294 ; 5.701 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 102 ;34.758 ;24.118
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 403 ;12.846 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 16 ;17.438 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 337 ; 0.130 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2480 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 498 ; 0.001 ; 0.020
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): 1057 ; 0.838 ; 1.041
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1056 ; 0.831 ; 1.039
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1330 ; 1.435 ; 1.553
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1331 ; 1.437 ; 1.555
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1105 ; 1.097 ; 1.225
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1106 ; 1.097 ; 1.225
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 1599 ; 1.782 ; 1.782
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 2678 ; 6.715 ;10.354
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 2679 ; 6.714 ;10.356
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 : 20
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 58 A 76
REMARK 3 ORIGIN FOR THE GROUP (A): 15.4240 19.3420 34.0000
REMARK 3 T TENSOR
REMARK 3 T11: 0.1767 T22: 0.1317
REMARK 3 T33: 0.1167 T12: -0.0095
REMARK 3 T13: 0.0193 T23: -0.0888
REMARK 3 L TENSOR
REMARK 3 L11: 9.3332 L22: 3.0322
REMARK 3 L33: 4.2366 L12: 2.6912
REMARK 3 L13: 1.6052 L23: -1.2655
REMARK 3 S TENSOR
REMARK 3 S11: 0.2016 S12: -1.0242 S13: 0.6422
REMARK 3 S21: 0.4598 S22: -0.2896 S23: 0.0124
REMARK 3 S31: -0.5676 S32: -0.0778 S33: 0.0879
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 77 A 88
REMARK 3 ORIGIN FOR THE GROUP (A): 6.8930 7.9230 29.7890
REMARK 3 T TENSOR
REMARK 3 T11: 0.1150 T22: 0.1606
REMARK 3 T33: 0.2186 T12: -0.0212
REMARK 3 T13: 0.1550 T23: -0.0349
REMARK 3 L TENSOR
REMARK 3 L11: 5.8180 L22: 1.2432
REMARK 3 L33: 3.1620 L12: 0.5126
REMARK 3 L13: -1.3257 L23: -1.6813
REMARK 3 S TENSOR
REMARK 3 S11: -0.0139 S12: -0.3067 S13: -0.0737
REMARK 3 S21: 0.2420 S22: 0.1691 S23: 0.3579
REMARK 3 S31: -0.0924 S32: -0.4433 S33: -0.1551
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 89 A 99
REMARK 3 ORIGIN FOR THE GROUP (A): 5.8730 9.3520 22.5330
REMARK 3 T TENSOR
REMARK 3 T11: 0.0138 T22: 0.1488
REMARK 3 T33: 0.1426 T12: -0.0080
REMARK 3 T13: 0.0225 T23: 0.0018
REMARK 3 L TENSOR
REMARK 3 L11: 2.4996 L22: 8.5177
REMARK 3 L33: 5.9872 L12: -1.4391
REMARK 3 L13: 1.1980 L23: -6.1066
REMARK 3 S TENSOR
REMARK 3 S11: 0.0380 S12: -0.0811 S13: 0.0951
REMARK 3 S21: -0.0225 S22: 0.1088 S23: 0.2741
REMARK 3 S31: -0.0202 S32: -0.2763 S33: -0.1468
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 100 A 107
REMARK 3 ORIGIN FOR THE GROUP (A): 8.8080 21.1670 15.3780
REMARK 3 T TENSOR
REMARK 3 T11: 0.1061 T22: 0.0401
REMARK 3 T33: 0.1963 T12: 0.0578
REMARK 3 T13: 0.0190 T23: 0.0192
REMARK 3 L TENSOR
REMARK 3 L11: 8.2453 L22: 8.3889
REMARK 3 L33: 6.0533 L12: 6.7441
REMARK 3 L13: -0.4611 L23: 0.3321
REMARK 3 S TENSOR
REMARK 3 S11: 0.1825 S12: -0.0425 S13: 0.6197
REMARK 3 S21: -0.1206 S22: -0.1239 S23: 0.7225
REMARK 3 S31: -0.2501 S32: -0.2619 S33: -0.0586
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 108 A 121
REMARK 3 ORIGIN FOR THE GROUP (A): 15.3020 11.5570 11.4320
REMARK 3 T TENSOR
REMARK 3 T11: 0.0720 T22: 0.1400
REMARK 3 T33: 0.1331 T12: 0.0418
REMARK 3 T13: 0.0286 T23: 0.0187
REMARK 3 L TENSOR
REMARK 3 L11: 0.5515 L22: 2.3130
REMARK 3 L33: 1.6284 L12: -0.4256
REMARK 3 L13: 0.2977 L23: -0.1846
REMARK 3 S TENSOR
REMARK 3 S11: 0.1020 S12: 0.1697 S13: 0.0017
REMARK 3 S21: -0.0870 S22: -0.0113 S23: 0.0424
REMARK 3 S31: -0.0624 S32: -0.2398 S33: -0.0907
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 122 A 129
REMARK 3 ORIGIN FOR THE GROUP (A): 5.0330 10.4570 12.8530
REMARK 3 T TENSOR
REMARK 3 T11: 0.0217 T22: 0.1791
REMARK 3 T33: 0.1521 T12: 0.0213
REMARK 3 T13: 0.0053 T23: 0.0235
REMARK 3 L TENSOR
REMARK 3 L11: 2.2110 L22: 7.3330
REMARK 3 L33: 8.2237 L12: 1.3459
REMARK 3 L13: 1.0905 L23: -4.8161
REMARK 3 S TENSOR
REMARK 3 S11: -0.0228 S12: 0.0919 S13: 0.0710
REMARK 3 S21: 0.0751 S22: 0.2217 S23: 0.3907
REMARK 3 S31: 0.0378 S32: -0.5607 S33: -0.1989
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 130 A 151
REMARK 3 ORIGIN FOR THE GROUP (A): 16.8300 7.8700 6.3530
REMARK 3 T TENSOR
REMARK 3 T11: 0.0807 T22: 0.0946
REMARK 3 T33: 0.1414 T12: 0.0146
REMARK 3 T13: 0.0059 T23: 0.0202
REMARK 3 L TENSOR
REMARK 3 L11: 0.8227 L22: 2.4463
REMARK 3 L33: 1.2711 L12: -1.1601
REMARK 3 L13: -0.2627 L23: -0.0152
REMARK 3 S TENSOR
REMARK 3 S11: 0.0644 S12: 0.1545 S13: -0.0930
REMARK 3 S21: -0.0499 S22: -0.0198 S23: 0.1217
REMARK 3 S31: -0.1429 S32: -0.0965 S33: -0.0445
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 152 A 167
REMARK 3 ORIGIN FOR THE GROUP (A): 10.7650 10.1970 5.2000
REMARK 3 T TENSOR
REMARK 3 T11: 0.0841 T22: 0.1964
REMARK 3 T33: 0.0999 T12: 0.0236
REMARK 3 T13: -0.0404 T23: 0.0128
REMARK 3 L TENSOR
REMARK 3 L11: 2.8579 L22: 6.0102
REMARK 3 L33: 2.2159 L12: -1.9254
REMARK 3 L13: -1.0287 L23: -2.1989
REMARK 3 S TENSOR
REMARK 3 S11: 0.1493 S12: 0.3641 S13: -0.1422
REMARK 3 S21: -0.2941 S22: -0.0876 S23: 0.2875
REMARK 3 S31: 0.0005 S32: -0.2903 S33: -0.0617
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 168 A 177
REMARK 3 ORIGIN FOR THE GROUP (A): 23.9840 5.3670 3.8830
REMARK 3 T TENSOR
REMARK 3 T11: 0.1177 T22: 0.0992
REMARK 3 T33: 0.1083 T12: -0.0110
REMARK 3 T13: -0.0210 T23: -0.0139
REMARK 3 L TENSOR
REMARK 3 L11: 1.3832 L22: 1.1364
REMARK 3 L33: 2.2080 L12: -0.8222
REMARK 3 L13: -1.0344 L23: -0.2674
REMARK 3 S TENSOR
REMARK 3 S11: 0.0992 S12: 0.1773 S13: -0.0920
REMARK 3 S21: -0.1216 S22: -0.0900 S23: 0.0276
REMARK 3 S31: -0.0604 S32: -0.0862 S33: -0.0092
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 178 A 190
REMARK 3 ORIGIN FOR THE GROUP (A): 36.5620 4.2770 2.8120
REMARK 3 T TENSOR
REMARK 3 T11: 0.0395 T22: 0.1452
REMARK 3 T33: 0.1061 T12: -0.0195
REMARK 3 T13: -0.0082 T23: 0.0019
REMARK 3 L TENSOR
REMARK 3 L11: 1.8983 L22: 8.8816
REMARK 3 L33: 7.1742 L12: -3.1512
REMARK 3 L13: 2.3794 L23: -3.7862
REMARK 3 S TENSOR
REMARK 3 S11: 0.0125 S12: 0.0805 S13: 0.1955
REMARK 3 S21: -0.0965 S22: -0.1199 S23: -0.2435
REMARK 3 S31: -0.0670 S32: 0.4146 S33: 0.1073
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 191 A 203
REMARK 3 ORIGIN FOR THE GROUP (A): 27.2100 16.0160 3.8350
REMARK 3 T TENSOR
REMARK 3 T11: 0.1382 T22: 0.0915
REMARK 3 T33: 0.1583 T12: -0.0343
REMARK 3 T13: 0.0532 T23: 0.0367
REMARK 3 L TENSOR
REMARK 3 L11: 2.5122 L22: 6.8087
REMARK 3 L33: 9.2414 L12: -4.0158
REMARK 3 L13: -2.8996 L23: 5.2859
REMARK 3 S TENSOR
REMARK 3 S11: 0.1395 S12: 0.1162 S13: 0.0917
REMARK 3 S21: -0.1277 S22: -0.0448 S23: 0.0437
REMARK 3 S31: -0.3767 S32: 0.1331 S33: -0.0948
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 204 A 211
REMARK 3 ORIGIN FOR THE GROUP (A): 19.0930 10.0400 18.8620
REMARK 3 T TENSOR
REMARK 3 T11: 0.1551 T22: 0.0532
REMARK 3 T33: 0.1719 T12: -0.0000
REMARK 3 T13: 0.0536 T23: 0.0012
REMARK 3 L TENSOR
REMARK 3 L11: 1.0866 L22: 0.7709
REMARK 3 L33: 1.3988 L12: -0.2245
REMARK 3 L13: -1.0532 L23: 0.5689
REMARK 3 S TENSOR
REMARK 3 S11: 0.0772 S12: 0.0168 S13: 0.0312
REMARK 3 S21: 0.1609 S22: 0.0302 S23: 0.1352
REMARK 3 S31: -0.1194 S32: 0.0262 S33: -0.1074
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 212 A 226
REMARK 3 ORIGIN FOR THE GROUP (A): 23.9920 -6.6620 17.8490
REMARK 3 T TENSOR
REMARK 3 T11: 0.1126 T22: 0.0800
REMARK 3 T33: 0.1391 T12: -0.0462
REMARK 3 T13: 0.0278 T23: -0.0126
REMARK 3 L TENSOR
REMARK 3 L11: 3.3412 L22: 0.2938
REMARK 3 L33: 1.8424 L12: 0.1538
REMARK 3 L13: 1.4188 L23: 0.4321
REMARK 3 S TENSOR
REMARK 3 S11: -0.0521 S12: 0.0604 S13: -0.2734
REMARK 3 S21: 0.0152 S22: -0.0773 S23: 0.0412
REMARK 3 S31: 0.1521 S32: -0.2298 S33: 0.1293
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 227 A 233
REMARK 3 ORIGIN FOR THE GROUP (A): 31.4740 -7.5940 21.8100
REMARK 3 T TENSOR
REMARK 3 T11: 0.0792 T22: 0.0458
REMARK 3 T33: 0.1376 T12: 0.0018
REMARK 3 T13: -0.0035 T23: 0.0039
REMARK 3 L TENSOR
REMARK 3 L11: 6.1033 L22: 5.3110
REMARK 3 L33: 11.0406 L12: -3.7654
REMARK 3 L13: -5.6150 L23: 1.7462
REMARK 3 S TENSOR
REMARK 3 S11: -0.1944 S12: 0.0256 S13: -0.1436
REMARK 3 S21: 0.0262 S22: -0.1115 S23: 0.1629
REMARK 3 S31: 0.1871 S32: 0.2738 S33: 0.3059
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 234 A 247
REMARK 3 ORIGIN FOR THE GROUP (A): 28.5360 3.0810 23.1080
REMARK 3 T TENSOR
REMARK 3 T11: 0.0848 T22: 0.1105
REMARK 3 T33: 0.0985 T12: 0.0010
REMARK 3 T13: 0.0048 T23: -0.0039
REMARK 3 L TENSOR
REMARK 3 L11: 3.4115 L22: 1.7549
REMARK 3 L33: 1.8004 L12: -1.2960
REMARK 3 L13: 2.1645 L23: -0.5335
REMARK 3 S TENSOR
REMARK 3 S11: 0.0132 S12: -0.1669 S13: -0.0005
REMARK 3 S21: 0.0788 S22: 0.1217 S23: 0.0323
REMARK 3 S31: -0.0366 S32: -0.0127 S33: -0.1350
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 248 A 264
REMARK 3 ORIGIN FOR THE GROUP (A): 33.8510 5.3060 17.3820
REMARK 3 T TENSOR
REMARK 3 T11: 0.0759 T22: 0.1317
REMARK 3 T33: 0.1000 T12: -0.0215
REMARK 3 T13: 0.0026 T23: 0.0054
REMARK 3 L TENSOR
REMARK 3 L11: 1.7066 L22: 1.6350
REMARK 3 L33: 1.4785 L12: -1.4870
REMARK 3 L13: 0.1624 L23: 0.1905
REMARK 3 S TENSOR
REMARK 3 S11: -0.0406 S12: -0.0388 S13: 0.0371
REMARK 3 S21: 0.0359 S22: -0.0011 S23: 0.0078
REMARK 3 S31: -0.0510 S32: 0.2425 S33: 0.0418
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 : A 265 A 270
REMARK 3 ORIGIN FOR THE GROUP (A): 29.5270 16.6730 18.0950
REMARK 3 T TENSOR
REMARK 3 T11: 0.1111 T22: 0.1080
REMARK 3 T33: 0.1288 T12: -0.0954
REMARK 3 T13: 0.0255 T23: -0.0225
REMARK 3 L TENSOR
REMARK 3 L11: 4.3763 L22: 3.4976
REMARK 3 L33: 7.9806 L12: -0.3477
REMARK 3 L13: -1.8758 L23: 3.3939
REMARK 3 S TENSOR
REMARK 3 S11: 0.0100 S12: -0.3246 S13: 0.0561
REMARK 3 S21: 0.0782 S22: 0.0593 S23: 0.0170
REMARK 3 S31: -0.3943 S32: 0.5602 S33: -0.0692
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 : A 271 A 277
REMARK 3 ORIGIN FOR THE GROUP (A): 18.9190 18.4200 18.9270
REMARK 3 T TENSOR
REMARK 3 T11: 0.1729 T22: 0.0123
REMARK 3 T33: 0.1884 T12: 0.0270
REMARK 3 T13: -0.0004 T23: 0.0149
REMARK 3 L TENSOR
REMARK 3 L11: 2.3439 L22: 5.0689
REMARK 3 L33: 6.0385 L12: 3.2851
REMARK 3 L13: -0.9256 L23: -0.4465
REMARK 3 S TENSOR
REMARK 3 S11: 0.1716 S12: -0.0253 S13: 0.1912
REMARK 3 S21: 0.0378 S22: -0.0183 S23: 0.4740
REMARK 3 S31: -0.5423 S32: -0.0155 S33: -0.1532
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 : A 278 A 295
REMARK 3 ORIGIN FOR THE GROUP (A): 21.7670 8.0720 28.5260
REMARK 3 T TENSOR
REMARK 3 T11: 0.0842 T22: 0.0833
REMARK 3 T33: 0.0944 T12: 0.0152
REMARK 3 T13: 0.0104 T23: -0.0265
REMARK 3 L TENSOR
REMARK 3 L11: 5.1499 L22: 3.1878
REMARK 3 L33: 2.3882 L12: 2.2535
REMARK 3 L13: -0.7613 L23: -1.2635
REMARK 3 S TENSOR
REMARK 3 S11: -0.0637 S12: -0.3654 S13: 0.1545
REMARK 3 S21: 0.1970 S22: -0.0041 S23: 0.0909
REMARK 3 S31: -0.0478 S32: 0.0009 S33: 0.0678
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 : A 296 A 311
REMARK 3 ORIGIN FOR THE GROUP (A): 14.5260 11.9650 32.3950
REMARK 3 T TENSOR
REMARK 3 T11: 0.1016 T22: 0.2069
REMARK 3 T33: 0.1093 T12: 0.0513
REMARK 3 T13: 0.0321 T23: -0.0639
REMARK 3 L TENSOR
REMARK 3 L11: 2.7222 L22: 0.8234
REMARK 3 L33: 4.8894 L12: 1.2300
REMARK 3 L13: -1.4767 L23: -1.1656
REMARK 3 S TENSOR
REMARK 3 S11: -0.0187 S12: -0.4940 S13: 0.2897
REMARK 3 S21: 0.0772 S22: -0.0424 S23: 0.1187
REMARK 3 S31: -0.2192 S32: -0.1596 S33: 0.0611
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH 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 4OQP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-FEB-14.
REMARK 100 THE DEPOSITION ID IS D_1000084830.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-JUL-12
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 : BESSY
REMARK 200 BEAMLINE : 14.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.91841
REMARK 200 MONOCHROMATOR : SI(111) CRYSTAL
REMARK 200 OPTICS : DOUBLE CRYSTAL MONOCHROMATOR
REMARK 200 WITH 2 SETS OF RH-SOATED
REMARK 200 SILLICON AND GLASS MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 34660
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.5
REMARK 200 DATA REDUNDANCY : 5.600
REMARK 200 R MERGE (I) : 0.04000
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) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.66
REMARK 200 COMPLETENESS FOR SHELL (%) : 62.3
REMARK 200 DATA REDUNDANCY IN SHELL : 3.30
REMARK 200 R MERGE FOR SHELL (I) : 0.25500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.800
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: PDB ENTRY 3NZE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.97
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.36
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.08 M HEPES, 9.6% (W/V) PEG 3350, 4
REMARK 280 MM COCL2, 4 MM CDCL2, 4 MM MGCL2, AND 4 MM NICL2; 16.5 MG/ML
REMARK 280 PROTEIN IN 20 MM TRISODIUM CITRATE PH 7.0, 150 MM NACL, 0.02% (V/
REMARK 280 V) 2-MERCAPTOETHANOL, 50 MM DEOXYRIBOSE-5-PHOSPHATE; PROTEIN:
REMARK 280 RESERVOIR 2:1, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K,
REMARK 280 PH 7.5
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
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 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 45.66900
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 45.66900
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 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 38.49750
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 39.49150
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 38.49750
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 39.49150
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 45.66900
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 38.49750
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 39.49150
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 45.66900
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 38.49750
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 39.49150
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2960 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21540 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -75.0 KCAL/MOL
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 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 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 503 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 607 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 612 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 632 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 GLY A 50
REMARK 465 ILE A 51
REMARK 465 ASP A 52
REMARK 465 PRO A 53
REMARK 465 PHE A 54
REMARK 465 THR A 55
REMARK 465 ASP A 56
REMARK 465 PRO A 57
REMARK 465 ASP A 312
REMARK 465 LEU A 313
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 SER A 115 -156.16 -93.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 THE ORGINAL SUGAR D 2-DEOXYRIBOSE-5-PHOSPHATE WAS COVALENTLY BOUND
REMARK 600 TO LYS141 BY SCHIFF BASE. THE PRODUCT 3,4-DIHYDROXY-5-(PHOSPHONOOXY)
REMARK 600 PENTANE-LYS ADDUCT WAS OBTAINED. NZ LYS A 141 - C1' PED A 401 BOND
REMARK 600 REPRESENTS A DOUBLE BOND
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CO A 406 CO
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 78 ND1
REMARK 620 2 TYR A 97 OH 91.6
REMARK 620 3 GLU A 226 OE1 47.7 73.3
REMARK 620 4 GLU A 226 OE2 45.9 74.4 1.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CO A 406 CO
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 78 ND1
REMARK 620 2 TYR A 97 OH 93.6
REMARK 620 3 GLU A 226 OE1 46.5 70.5
REMARK 620 4 GLU A 226 OE2 45.5 72.4 1.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 407 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 93 OD1
REMARK 620 2 ASP A 93 OD2 54.6
REMARK 620 3 HOH A 704 O 86.9 87.8
REMARK 620 4 HOH A 705 O 157.4 110.3 74.9
REMARK 620 5 HOH A 715 O 94.0 91.8 178.5 103.9
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD A 402 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 146 ND1
REMARK 620 2 ASP A 189 OD1 51.1
REMARK 620 3 ASP A 189 OD2 52.7 5.8
REMARK 620 4 HIS A 191 ND1 44.9 6.9 8.2
REMARK 620 5 HOH A 540 O 46.3 13.6 9.9 9.3
REMARK 620 6 HOH A 700 O 52.1 7.8 2.3 8.4 7.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NI A 403 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 304 ND1
REMARK 620 2 HOH A 742 O 88.9
REMARK 620 3 HOH A 743 O 106.1 164.4
REMARK 620 4 HOH A 756 O 96.4 75.2 98.6
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PED A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 407
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4OQQ RELATED DB: PDB
DBREF 4OQP A 56 313 UNP P39140 DEOR_BACSU 56 313
SEQADV 4OQP GLY A 50 UNP P39140 EXPRESSION TAG
SEQADV 4OQP ILE A 51 UNP P39140 EXPRESSION TAG
SEQADV 4OQP ASP A 52 UNP P39140 EXPRESSION TAG
SEQADV 4OQP PRO A 53 UNP P39140 EXPRESSION TAG
SEQADV 4OQP PHE A 54 UNP P39140 EXPRESSION TAG
SEQADV 4OQP THR A 55 UNP P39140 EXPRESSION TAG
SEQRES 1 A 264 GLY ILE ASP PRO PHE THR ASP PRO PHE GLU ASP LEU ASP
SEQRES 2 A 264 ALA LEU GLY SER ILE LEU GLU GLU LYS TYR GLY LEU LEU
SEQRES 3 A 264 GLU ALA HIS VAL VAL PHE SER PRO THR PRO ASP TYR ALA
SEQRES 4 A 264 GLY ILE THR HIS ASP LEU SER ARG TYR GLY ALA GLU TYR
SEQRES 5 A 264 MET HIS GLU THR VAL LYS ASP GLY ASP ILE VAL GLY VAL
SEQRES 6 A 264 SER TRP GLY THR THR MET TYR GLN ILE ALA GLN ASN MET
SEQRES 7 A 264 GLN PRO LYS GLN VAL LYS GLY VAL GLU VAL VAL GLN LEU
SEQRES 8 A 264 LYS GLY GLY ILE SER HIS SER ARG VAL ASN THR TYR SER
SEQRES 9 A 264 ALA GLU THR ILE GLN LEU PHE ALA GLU ALA PHE GLN THR
SEQRES 10 A 264 MET PRO ARG TYR LEU PRO LEU PRO VAL VAL PHE ASP ASN
SEQRES 11 A 264 ALA ASP VAL LYS ARG MET VAL GLU LYS ASP ARG HIS ILE
SEQRES 12 A 264 GLU ARG ILE ILE GLU MET GLY LYS GLN ALA ASN ILE ALA
SEQRES 13 A 264 LEU PHE THR VAL GLY THR VAL ARG ASP GLU ALA LEU LEU
SEQRES 14 A 264 PHE ARG LEU GLY TYR PHE ASN GLU GLU GLU LYS ALA LEU
SEQRES 15 A 264 LEU LYS LYS GLN ALA VAL GLY ASP ILE CYS SER ARG PHE
SEQRES 16 A 264 PHE ASP ALA LYS GLY ASN ILE CYS SER SER ALA ILE ASN
SEQRES 17 A 264 ASP ARG THR ILE GLY VAL GLU LEU GLN ASP LEU ARG LEU
SEQRES 18 A 264 LYS GLU ARG SER ILE LEU VAL ALA GLY GLY SER ARG LYS
SEQRES 19 A 264 VAL SER SER ILE HIS GLY ALA LEU THR GLY LYS TYR ALA
SEQRES 20 A 264 ASN VAL LEU ILE ILE ASP GLN HIS THR ALA ARG ALA LEU
SEQRES 21 A 264 VAL ASN ASP LEU
HET PED A 401 12
HET CD A 402 1
HET NI A 403 1
HET NI A 404 1
HET NI A 405 1
HET CO A 406 2
HET MG A 407 1
HETNAM PED PENTANE-3,4-DIOL-5-PHOSPHATE
HETNAM CD CADMIUM ION
HETNAM NI NICKEL (II) ION
HETNAM CO COBALT (II) ION
HETNAM MG MAGNESIUM ION
HETSYN PED OPEN FORM OF 1'-2'-DIDEOXYRIBOFURANOSE-5'-PHOSPHATE
FORMUL 2 PED C5 H13 O6 P
FORMUL 3 CD CD 2+
FORMUL 4 NI 3(NI 2+)
FORMUL 7 CO CO 2+
FORMUL 8 MG MG 2+
FORMUL 9 HOH *264(H2 O)
HELIX 1 1 ASP A 60 GLY A 73 1 14
HELIX 2 2 ASP A 86 VAL A 106 1 21
HELIX 3 3 GLY A 117 MET A 127 1 11
HELIX 4 4 TYR A 152 PHE A 164 1 13
HELIX 5 5 ASN A 179 LYS A 188 1 10
HELIX 6 6 ASP A 189 ALA A 202 1 14
HELIX 7 7 ALA A 216 ARG A 220 5 5
HELIX 8 8 ASN A 225 ALA A 236 1 12
HELIX 9 9 SER A 253 ASP A 258 1 6
HELIX 10 10 GLU A 264 ARG A 269 1 6
HELIX 11 11 GLY A 280 ARG A 282 5 3
HELIX 12 12 LYS A 283 GLY A 293 1 11
HELIX 13 13 GLN A 303 ASN A 311 1 9
SHEET 1 A 7 GLU A 76 VAL A 80 0
SHEET 2 A 7 VAL A 298 ASP A 302 1 O ILE A 301 N VAL A 80
SHEET 3 A 7 ARG A 273 VAL A 277 1 N LEU A 276 O VAL A 298
SHEET 4 A 7 ILE A 204 PHE A 207 1 N ALA A 205 O ILE A 275
SHEET 5 A 7 ILE A 111 VAL A 114 1 N GLY A 113 O ILE A 204
SHEET 6 A 7 GLU A 136 GLN A 139 1 O GLU A 136 N VAL A 112
SHEET 7 A 7 PRO A 168 ARG A 169 1 O ARG A 169 N GLN A 139
SHEET 1 B 2 GLY A 238 ILE A 240 0
SHEET 2 B 2 ARG A 243 PHE A 245 -1 O PHE A 245 N GLY A 238
LINK NZ LYS A 141 C1' PED A 401 1555 1555 1.29
LINK ND1 HIS A 78 CO A CO A 406 1555 7555 2.26
LINK ND1 HIS A 78 CO B CO A 406 1555 7555 2.45
LINK OD1 ASP A 93 MG MG A 407 1555 1555 2.37
LINK OD2 ASP A 93 MG MG A 407 1555 1555 2.44
LINK OH ATYR A 97 CO A CO A 406 1555 7555 2.67
LINK OH BTYR A 97 CO B CO A 406 1555 7555 2.69
LINK NE2 HIS A 103 NI NI A 404 1555 1555 2.53
LINK ND1 HIS A 146 CD CD A 402 1555 4555 2.32
LINK OD1 ASP A 189 CD CD A 402 1555 1555 2.39
LINK OD2 ASP A 189 CD CD A 402 1555 1555 2.38
LINK ND1 HIS A 191 CD CD A 402 1555 1555 2.25
LINK OE1 GLU A 226 CO A CO A 406 1555 1555 2.63
LINK OE1 GLU A 226 CO B CO A 406 1555 1555 2.39
LINK OE2 GLU A 226 CO A CO A 406 1555 1555 2.29
LINK OE2 GLU A 226 CO B CO A 406 1555 1555 2.41
LINK NE2 HIS A 288 NI NI A 405 1555 1555 2.61
LINK ND1 HIS A 304 NI NI A 403 1555 1555 2.41
LINK CD CD A 402 O HOH A 540 1555 1555 2.39
LINK CD CD A 402 O HOH A 700 1555 1555 2.34
LINK NI NI A 403 O HOH A 742 1555 1555 2.19
LINK NI NI A 403 O HOH A 743 1555 1555 2.24
LINK NI NI A 403 O HOH A 756 1555 1555 2.58
LINK MG MG A 407 O HOH A 704 1555 1555 2.20
LINK MG MG A 407 O HOH A 705 1555 3555 2.32
LINK MG MG A 407 O HOH A 715 1555 3555 2.06
SITE 1 AC1 15 SER A 115 TRP A 116 THR A 118 THR A 119
SITE 2 AC1 15 LYS A 141 THR A 208 GLY A 210 LEU A 218
SITE 3 AC1 15 ASP A 239 LYS A 283 HOH A 501 HOH A 505
SITE 4 AC1 15 HOH A 614 HOH A 640 HOH A 701
SITE 1 AC2 5 HIS A 146 ASP A 189 HIS A 191 HOH A 540
SITE 2 AC2 5 HOH A 700
SITE 1 AC3 4 HIS A 304 HOH A 742 HOH A 743 HOH A 756
SITE 1 AC4 1 HIS A 103
SITE 1 AC5 1 HIS A 288
SITE 1 AC6 3 HIS A 78 TYR A 97 GLU A 226
SITE 1 AC7 5 HIS A 92 ASP A 93 HOH A 704 HOH A 705
SITE 2 AC7 5 HOH A 715
CRYST1 76.995 78.983 91.338 90.00 90.00 90.00 C 2 2 21 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 0.012988 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012661 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010948 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
