HEADER HYDROLASE 14-MAR-08 3CK2
TITLE CRYSTAL STRUCTURE OF CONSERVED UNCHARACTERIZED PROTEIN (PREDICTED
TITLE 2 PHOSPHOESTERASE COG0622) FROM STREPTOCOCCUS PNEUMONIAE TIGR4
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CONSERVED UNCHARACTERIZED PROTEIN (PREDICTED
COMPND 3 PHOSPHOESTERASE COG0622);
COMPND 4 CHAIN: A;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOCOCCUS PNEUMONIAE;
SOURCE 3 ORGANISM_TAXID: 170187;
SOURCE 4 STRAIN: TIGR4;
SOURCE 5 ATCC: BAA-334;
SOURCE 6 GENE: SP_1879;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PMCSG7
KEYWDS STRUCTURAL GENOMICS, PREDICTED PHOSPHODIESTERASE, PSI-2, PROTEIN
KEYWDS 2 STRUCTURE INITIATIVE, MIDWEST CENTER FOR STRUCTURAL GENOMICS, MCSG,
KEYWDS 3 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR B.NOCEK,M.ZHOU,J.ABDULLAH,A.JOACHIMIAK,MIDWEST CENTER FOR STRUCTURAL
AUTHOR 2 GENOMICS (MCSG)
REVDAT 4 25-OCT-17 3CK2 1 REMARK
REVDAT 3 13-JUL-11 3CK2 1 VERSN
REVDAT 2 24-FEB-09 3CK2 1 VERSN
REVDAT 1 01-APR-08 3CK2 0
JRNL AUTH B.NOCEK,M.ZHOU,J.ABDULLAH,A.JOACHIMIAK
JRNL TITL CRYSTAL STRUCTURE OF CONSERVED UNCHARACTERIZED PROTEIN
JRNL TITL 2 (PREDICTED PHOSPHOESTERASE COG0622) FROM STREPTOCOCCUS
JRNL TITL 3 PNEUMONIAE TIGR4.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.30 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) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.88
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 10609
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) : 0.150
REMARK 3 R VALUE (WORKING SET) : 0.148
REMARK 3 FREE R VALUE : 0.203
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 507
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) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.36
REMARK 3 REFLECTION IN BIN (WORKING SET) : 698
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.34
REMARK 3 BIN R VALUE (WORKING SET) : 0.1890
REMARK 3 BIN FREE R VALUE SET COUNT : 55
REMARK 3 BIN FREE R VALUE : 0.2550
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1407
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 14
REMARK 3 SOLVENT ATOMS : 132
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) : 18.80
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.218
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.187
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.124
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.201
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.969
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.937
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1452 ; 0.016 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 989 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1963 ; 1.546 ; 1.949
REMARK 3 BOND ANGLES OTHERS (DEGREES): 2392 ; 0.970 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 173 ; 7.666 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 74 ;32.951 ;23.649
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 240 ;13.686 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 10 ;17.068 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 208 ; 0.089 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1623 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 316 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 197 ; 0.180 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 1047 ; 0.205 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 665 ; 0.177 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 753 ; 0.083 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 84 ; 0.158 ; 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): 3 ; 0.112 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 13 ; 0.212 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 14 ; 0.190 ; 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): 1057 ; 0.756 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 353 ; 0.162 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1393 ; 0.991 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 679 ; 1.788 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 570 ; 2.473 ; 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 : 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 5
REMARK 3 ORIGIN FOR THE GROUP (A): 24.3701 -3.3813 -22.0288
REMARK 3 T TENSOR
REMARK 3 T11: 0.3073 T22: 0.6382
REMARK 3 T33: 0.4304 T12: -0.2266
REMARK 3 T13: 0.0296 T23: 0.1773
REMARK 3 L TENSOR
REMARK 3 L11: 30.5766 L22: 6.0518
REMARK 3 L33: 3.3974 L12: 9.0623
REMARK 3 L13: 7.6131 L23: 4.5047
REMARK 3 S TENSOR
REMARK 3 S11: -2.0480 S12: 1.4301 S13: 1.4116
REMARK 3 S21: -1.3668 S22: 1.8899 S23: -0.2669
REMARK 3 S31: -1.2809 S32: 1.0589 S33: 0.1581
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 6 A 28
REMARK 3 ORIGIN FOR THE GROUP (A): 9.5960 -19.2160 -20.3404
REMARK 3 T TENSOR
REMARK 3 T11: 0.0582 T22: 0.0932
REMARK 3 T33: 0.0343 T12: 0.0688
REMARK 3 T13: -0.0110 T23: 0.0231
REMARK 3 L TENSOR
REMARK 3 L11: 3.5250 L22: 4.3997
REMARK 3 L33: 4.9234 L12: 0.1290
REMARK 3 L13: -1.0269 L23: -0.1571
REMARK 3 S TENSOR
REMARK 3 S11: -0.0163 S12: 0.4362 S13: -0.1613
REMARK 3 S21: -0.3939 S22: -0.0662 S23: -0.1837
REMARK 3 S31: 0.3497 S32: 0.0506 S33: 0.0825
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 29 A 42
REMARK 3 ORIGIN FOR THE GROUP (A): 12.4728 -18.9603 -14.8445
REMARK 3 T TENSOR
REMARK 3 T11: -0.0006 T22: 0.0805
REMARK 3 T33: 0.0249 T12: 0.0837
REMARK 3 T13: -0.0501 T23: 0.0588
REMARK 3 L TENSOR
REMARK 3 L11: 6.7737 L22: 5.6684
REMARK 3 L33: 3.7492 L12: 1.5300
REMARK 3 L13: -2.5420 L23: -2.0431
REMARK 3 S TENSOR
REMARK 3 S11: -0.1218 S12: 0.0175 S13: -0.0552
REMARK 3 S21: -0.1301 S22: -0.1289 S23: -0.1774
REMARK 3 S31: 0.3291 S32: 0.3946 S33: 0.2507
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 43 A 57
REMARK 3 ORIGIN FOR THE GROUP (A): 14.0116 -23.4990 -11.9402
REMARK 3 T TENSOR
REMARK 3 T11: 0.0408 T22: 0.1026
REMARK 3 T33: 0.0732 T12: 0.1286
REMARK 3 T13: -0.0323 T23: 0.0561
REMARK 3 L TENSOR
REMARK 3 L11: 3.8460 L22: 4.9010
REMARK 3 L33: 2.5736 L12: 1.6162
REMARK 3 L13: -1.8106 L23: -1.6632
REMARK 3 S TENSOR
REMARK 3 S11: -0.0608 S12: -0.0279 S13: -0.2318
REMARK 3 S21: -0.3097 S22: -0.1713 S23: -0.4682
REMARK 3 S31: 0.1612 S32: 0.4097 S33: 0.2321
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 58 A 69
REMARK 3 ORIGIN FOR THE GROUP (A): 12.3210 -21.8939 -3.9937
REMARK 3 T TENSOR
REMARK 3 T11: 0.1548 T22: 0.1738
REMARK 3 T33: 0.1105 T12: 0.0511
REMARK 3 T13: -0.0051 T23: 0.0247
REMARK 3 L TENSOR
REMARK 3 L11: 3.6485 L22: 4.3139
REMARK 3 L33: 3.5689 L12: 2.2108
REMARK 3 L13: -0.6597 L23: -3.6029
REMARK 3 S TENSOR
REMARK 3 S11: 0.0556 S12: -0.2118 S13: -0.0410
REMARK 3 S21: 0.0789 S22: -0.2770 S23: -0.2602
REMARK 3 S31: 0.0377 S32: 0.1510 S33: 0.2214
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 70 A 87
REMARK 3 ORIGIN FOR THE GROUP (A): 15.8492 -10.3134 -5.6834
REMARK 3 T TENSOR
REMARK 3 T11: 0.0730 T22: 0.0539
REMARK 3 T33: 0.1215 T12: -0.0265
REMARK 3 T13: -0.1313 T23: 0.0746
REMARK 3 L TENSOR
REMARK 3 L11: 3.6249 L22: 3.9831
REMARK 3 L33: 6.2913 L12: 1.1299
REMARK 3 L13: -1.8733 L23: -1.7809
REMARK 3 S TENSOR
REMARK 3 S11: -0.0810 S12: -0.2274 S13: 0.1998
REMARK 3 S21: 0.3435 S22: -0.2141 S23: -0.6079
REMARK 3 S31: -0.2189 S32: 0.7068 S33: 0.2951
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 88 A 100
REMARK 3 ORIGIN FOR THE GROUP (A): 11.6181 -3.9499 1.6439
REMARK 3 T TENSOR
REMARK 3 T11: 0.3079 T22: 0.0599
REMARK 3 T33: 0.0589 T12: -0.0913
REMARK 3 T13: -0.1142 T23: -0.0394
REMARK 3 L TENSOR
REMARK 3 L11: 26.4466 L22: 6.8555
REMARK 3 L33: 8.3199 L12: 8.1564
REMARK 3 L13: -5.1214 L23: -1.7039
REMARK 3 S TENSOR
REMARK 3 S11: 0.2235 S12: -1.5144 S13: 1.1770
REMARK 3 S21: 0.6726 S22: -0.3120 S23: 0.0307
REMARK 3 S31: -1.0479 S32: 0.5294 S33: 0.0885
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 101 A 114
REMARK 3 ORIGIN FOR THE GROUP (A): 10.6588 -7.5744 -7.6153
REMARK 3 T TENSOR
REMARK 3 T11: 0.1145 T22: 0.1125
REMARK 3 T33: 0.0892 T12: -0.0076
REMARK 3 T13: -0.0800 T23: 0.0361
REMARK 3 L TENSOR
REMARK 3 L11: 2.2189 L22: 2.1682
REMARK 3 L33: 3.7383 L12: -0.6395
REMARK 3 L13: -1.8579 L23: -1.5454
REMARK 3 S TENSOR
REMARK 3 S11: 0.0634 S12: -0.1979 S13: 0.4420
REMARK 3 S21: 0.4081 S22: -0.1849 S23: -0.1303
REMARK 3 S31: -0.2962 S32: 0.3230 S33: 0.1215
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 115 A 120
REMARK 3 ORIGIN FOR THE GROUP (A): 10.0348 1.5226 -8.8281
REMARK 3 T TENSOR
REMARK 3 T11: 0.3752 T22: 0.2657
REMARK 3 T33: 0.3548 T12: -0.0185
REMARK 3 T13: -0.0293 T23: 0.0062
REMARK 3 L TENSOR
REMARK 3 L11: 22.1306 L22: 2.9297
REMARK 3 L33: 27.1334 L12: 8.0521
REMARK 3 L13: 24.5046 L23: 8.9159
REMARK 3 S TENSOR
REMARK 3 S11: -0.0640 S12: -1.5436 S13: 0.9348
REMARK 3 S21: 1.6842 S22: -0.9655 S23: 0.2119
REMARK 3 S31: -1.0305 S32: -0.9696 S33: 1.0295
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 121 A 133
REMARK 3 ORIGIN FOR THE GROUP (A): 7.4327 -7.9934 -11.9964
REMARK 3 T TENSOR
REMARK 3 T11: 0.0354 T22: 0.0724
REMARK 3 T33: 0.1166 T12: 0.0378
REMARK 3 T13: -0.0404 T23: 0.0727
REMARK 3 L TENSOR
REMARK 3 L11: 2.4456 L22: 3.5062
REMARK 3 L33: 5.1158 L12: 0.4586
REMARK 3 L13: -0.0475 L23: -0.1167
REMARK 3 S TENSOR
REMARK 3 S11: -0.0639 S12: 0.4418 S13: 0.5463
REMARK 3 S21: 0.0846 S22: 0.0170 S23: 0.0407
REMARK 3 S31: -0.3021 S32: 0.4641 S33: 0.0469
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 134 A 140
REMARK 3 ORIGIN FOR THE GROUP (A): -4.7682 -9.1891 -16.0884
REMARK 3 T TENSOR
REMARK 3 T11: 0.0618 T22: 0.1368
REMARK 3 T33: 0.0791 T12: 0.0221
REMARK 3 T13: 0.0194 T23: 0.0615
REMARK 3 L TENSOR
REMARK 3 L11: 16.2388 L22: 6.8399
REMARK 3 L33: 7.0107 L12: -8.8361
REMARK 3 L13: -8.7541 L23: 6.0753
REMARK 3 S TENSOR
REMARK 3 S11: -0.1533 S12: -0.6103 S13: 0.2661
REMARK 3 S21: 0.4248 S22: 0.2689 S23: 0.3790
REMARK 3 S31: 0.1302 S32: -0.1900 S33: -0.1156
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 141 A 158
REMARK 3 ORIGIN FOR THE GROUP (A): 13.0458 -3.4648 -20.6266
REMARK 3 T TENSOR
REMARK 3 T11: 0.0376 T22: 0.1462
REMARK 3 T33: 0.1268 T12: -0.0105
REMARK 3 T13: -0.0145 T23: 0.1437
REMARK 3 L TENSOR
REMARK 3 L11: 9.3360 L22: 3.5820
REMARK 3 L33: 2.3096 L12: 2.6797
REMARK 3 L13: 1.5913 L23: 1.3310
REMARK 3 S TENSOR
REMARK 3 S11: -0.1258 S12: 0.6060 S13: 0.4646
REMARK 3 S21: -0.1914 S22: 0.0146 S23: -0.2879
REMARK 3 S31: -0.1793 S32: 0.3462 S33: 0.1112
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 159 A 165
REMARK 3 ORIGIN FOR THE GROUP (A): 2.7275 -9.9766 -26.2967
REMARK 3 T TENSOR
REMARK 3 T11: 0.0637 T22: 0.1855
REMARK 3 T33: 0.0655 T12: 0.0305
REMARK 3 T13: -0.0110 T23: 0.0497
REMARK 3 L TENSOR
REMARK 3 L11: 1.6960 L22: 22.3367
REMARK 3 L33: 1.5867 L12: 2.1661
REMARK 3 L13: 1.5736 L23: 1.9759
REMARK 3 S TENSOR
REMARK 3 S11: 0.0659 S12: 0.2037 S13: -0.1200
REMARK 3 S21: -0.8986 S22: -0.1920 S23: 0.4796
REMARK 3 S31: -0.0054 S32: 0.1068 S33: 0.1262
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 166 A 173
REMARK 3 ORIGIN FOR THE GROUP (A): 11.2540 3.0067 -17.9051
REMARK 3 T TENSOR
REMARK 3 T11: 0.1176 T22: 0.0682
REMARK 3 T33: 0.1861 T12: -0.0756
REMARK 3 T13: -0.0476 T23: 0.0565
REMARK 3 L TENSOR
REMARK 3 L11: 22.0308 L22: 2.7599
REMARK 3 L33: 2.9891 L12: 3.0354
REMARK 3 L13: 4.8459 L23: 2.1899
REMARK 3 S TENSOR
REMARK 3 S11: 0.7257 S12: -0.0706 S13: 0.6045
REMARK 3 S21: 0.2662 S22: -0.5869 S23: -0.6738
REMARK 3 S31: -0.3752 S32: 0.3088 S33: -0.1388
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 3CK2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-MAR-08.
REMARK 100 THE DEPOSITION ID IS D_1000046870.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-FEB-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
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) : 0.97920
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 : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 10635
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 21.10
REMARK 200 R MERGE (I) : 0.14300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.34
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.5
REMARK 200 DATA REDUNDANCY IN SHELL : 12.30
REMARK 200 R MERGE FOR SHELL (I) : 0.71900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHELXD, HKL2MAP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.89
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.92
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.0M K/NA TARTRATE, TRIS-HCL PH 7.0,
REMARK 280 0.1M LITHIUM SULFATE, 2MM MNCL2, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 294K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 21 3
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290 5555 Z,X,Y
REMARK 290 6555 Z+1/2,-X+1/2,-Y
REMARK 290 7555 -Z+1/2,-X,Y+1/2
REMARK 290 8555 -Z,X+1/2,-Y+1/2
REMARK 290 9555 Y,Z,X
REMARK 290 10555 -Y,Z+1/2,-X+1/2
REMARK 290 11555 Y+1/2,-Z+1/2,-X
REMARK 290 12555 -Y+1/2,-Z,X+1/2
REMARK 290 13555 X+1/2,Y+1/2,Z+1/2
REMARK 290 14555 -X,-Y+1/2,Z
REMARK 290 15555 -X+1/2,Y,-Z
REMARK 290 16555 X,-Y,-Z+1/2
REMARK 290 17555 Z+1/2,X+1/2,Y+1/2
REMARK 290 18555 Z,-X,-Y+1/2
REMARK 290 19555 -Z,-X+1/2,Y
REMARK 290 20555 -Z+1/2,X,-Y
REMARK 290 21555 Y+1/2,Z+1/2,X+1/2
REMARK 290 22555 -Y+1/2,Z,-X
REMARK 290 23555 Y,-Z,-X+1/2
REMARK 290 24555 -Y,-Z+1/2,X
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 56.23350
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 56.23350
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 56.23350
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 56.23350
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 56.23350
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 56.23350
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 6 0.000000 0.000000 1.000000 56.23350
REMARK 290 SMTRY2 6 -1.000000 0.000000 0.000000 56.23350
REMARK 290 SMTRY3 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 0.000000 -1.000000 56.23350
REMARK 290 SMTRY2 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 1.000000 0.000000 56.23350
REMARK 290 SMTRY1 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 8 1.000000 0.000000 0.000000 56.23350
REMARK 290 SMTRY3 8 0.000000 -1.000000 0.000000 56.23350
REMARK 290 SMTRY1 9 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 9 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 9 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 10 0.000000 0.000000 1.000000 56.23350
REMARK 290 SMTRY3 10 -1.000000 0.000000 0.000000 56.23350
REMARK 290 SMTRY1 11 0.000000 1.000000 0.000000 56.23350
REMARK 290 SMTRY2 11 0.000000 0.000000 -1.000000 56.23350
REMARK 290 SMTRY3 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 12 0.000000 -1.000000 0.000000 56.23350
REMARK 290 SMTRY2 12 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 12 1.000000 0.000000 0.000000 56.23350
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 56.23350
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 56.23350
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 56.23350
REMARK 290 SMTRY1 14 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 56.23350
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 15 -1.000000 0.000000 0.000000 56.23350
REMARK 290 SMTRY2 15 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 16 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 16 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 56.23350
REMARK 290 SMTRY1 17 0.000000 0.000000 1.000000 56.23350
REMARK 290 SMTRY2 17 1.000000 0.000000 0.000000 56.23350
REMARK 290 SMTRY3 17 0.000000 1.000000 0.000000 56.23350
REMARK 290 SMTRY1 18 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 18 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 18 0.000000 -1.000000 0.000000 56.23350
REMARK 290 SMTRY1 19 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 19 -1.000000 0.000000 0.000000 56.23350
REMARK 290 SMTRY3 19 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 20 0.000000 0.000000 -1.000000 56.23350
REMARK 290 SMTRY2 20 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 20 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 21 0.000000 1.000000 0.000000 56.23350
REMARK 290 SMTRY2 21 0.000000 0.000000 1.000000 56.23350
REMARK 290 SMTRY3 21 1.000000 0.000000 0.000000 56.23350
REMARK 290 SMTRY1 22 0.000000 -1.000000 0.000000 56.23350
REMARK 290 SMTRY2 22 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 22 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 23 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 23 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 23 -1.000000 0.000000 0.000000 56.23350
REMARK 290 SMTRY1 24 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 24 0.000000 0.000000 -1.000000 56.23350
REMARK 290 SMTRY3 24 1.000000 0.000000 0.000000 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 300 REMARK: AUTHORS STATE THAT THE BIOLOGICAL UNIT OF THIS PROTEIN IS
REMARK 300 UNKNOWN.
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 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 -2
REMARK 465 ASN 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 OD1 ASP A 155 O2 SRT A 301 2.19
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 HIS A 110 -47.70 78.57
REMARK 500 HIS A 161 33.53 74.09
REMARK 500
REMARK 500 REMARK: NULL
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 MN A 201 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 11 OD1
REMARK 620 2 ASP A 38 OD2 91.1
REMARK 620 3 HOH A 386 O 173.2 91.0
REMARK 620 4 HOH A 403 O 94.5 85.7 79.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN A 202 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 57 OD1
REMARK 620 2 HOH A 403 O 136.4
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 204
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SRT A 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: APC80634 RELATED DB: TARGETDB
DBREF 3CK2 A 1 173 UNP Q97NX4 Q97NX4_STRPN 1 173
SEQADV 3CK2 SER A -2 UNP Q97NX4 EXPRESSION TAG
SEQADV 3CK2 ASN A -1 UNP Q97NX4 EXPRESSION TAG
SEQADV 3CK2 ALA A 0 UNP Q97NX4 EXPRESSION TAG
SEQRES 1 A 176 SER ASN ALA MSE ALA LYS GLN THR ILE ILE VAL MSE SER
SEQRES 2 A 176 ASP SER HIS GLY ASP SER LEU ILE VAL GLU GLU VAL ARG
SEQRES 3 A 176 ASP ARG TYR VAL GLY LYS VAL ASP ALA VAL PHE HIS ASN
SEQRES 4 A 176 GLY ASP SER GLU LEU ARG PRO ASP SER PRO LEU TRP GLU
SEQRES 5 A 176 GLY ILE ARG VAL VAL LYS GLY ASN MSE ASP PHE TYR ALA
SEQRES 6 A 176 GLY TYR PRO GLU ARG LEU VAL THR GLU LEU GLY SER THR
SEQRES 7 A 176 LYS ILE ILE GLN THR HIS GLY HIS LEU PHE ASP ILE ASN
SEQRES 8 A 176 PHE ASN PHE GLN LYS LEU ASP TYR TRP ALA GLN GLU GLU
SEQRES 9 A 176 GLU ALA ALA ILE CYS LEU TYR GLY HIS LEU HIS VAL PRO
SEQRES 10 A 176 SER ALA TRP LEU GLU GLY LYS ILE LEU PHE LEU ASN PRO
SEQRES 11 A 176 GLY SER ILE SER GLN PRO ARG GLY THR ILE ARG GLU CYS
SEQRES 12 A 176 LEU TYR ALA ARG VAL GLU ILE ASP ASP SER TYR PHE LYS
SEQRES 13 A 176 VAL ASP PHE LEU THR ARG ASP HIS GLU VAL TYR PRO GLY
SEQRES 14 A 176 LEU SER LYS GLU PHE SER ARG
MODRES 3CK2 MSE A 1 MET SELENOMETHIONINE
MODRES 3CK2 MSE A 9 MET SELENOMETHIONINE
MODRES 3CK2 MSE A 58 MET SELENOMETHIONINE
HET MSE A 1 8
HET MSE A 9 8
HET MSE A 58 8
HET MN A 201 1
HET MN A 202 1
HET CL A 203 1
HET CL A 204 1
HET SRT A 301 10
HETNAM MSE SELENOMETHIONINE
HETNAM MN MANGANESE (II) ION
HETNAM CL CHLORIDE ION
HETNAM SRT S,R MESO-TARTARIC ACID
FORMUL 1 MSE 3(C5 H11 N O2 SE)
FORMUL 2 MN 2(MN 2+)
FORMUL 4 CL 2(CL 1-)
FORMUL 6 SRT C4 H6 O6
FORMUL 7 HOH *132(H2 O)
HELIX 1 1 ASP A 15 VAL A 27 1 13
HELIX 2 2 SER A 45 GLU A 49 5 5
HELIX 3 3 GLY A 82 ASP A 86 5 5
HELIX 4 4 PHE A 91 GLU A 101 1 11
SHEET 1 A 6 ILE A 51 VAL A 53 0
SHEET 2 A 6 ALA A 32 HIS A 35 1 N VAL A 33 O ARG A 52
SHEET 3 A 6 GLN A 4 MSE A 9 1 N ILE A 7 O PHE A 34
SHEET 4 A 6 TYR A 142 ILE A 147 -1 O ALA A 143 N VAL A 8
SHEET 5 A 6 TYR A 151 LEU A 157 -1 O LEU A 157 N TYR A 142
SHEET 6 A 6 LYS A 169 SER A 172 -1 O LYS A 169 N VAL A 154
SHEET 1 B 5 ARG A 67 LEU A 72 0
SHEET 2 B 5 THR A 75 THR A 80 -1 O THR A 75 N LEU A 72
SHEET 3 B 5 ILE A 105 LEU A 107 1 O LEU A 107 N ILE A 78
SHEET 4 B 5 ILE A 122 PRO A 127 1 O LEU A 123 N CYS A 106
SHEET 5 B 5 PRO A 114 GLU A 119 -1 N TRP A 117 O PHE A 124
LINK C ALA A 0 N MSE A 1 1555 1555 1.34
LINK C MSE A 1 N ALA A 2 1555 1555 1.33
LINK C VAL A 8 N MSE A 9 1555 1555 1.34
LINK C MSE A 9 N SER A 10 1555 1555 1.33
LINK C ASN A 57 N MSE A 58 1555 1555 1.34
LINK C MSE A 58 N ASP A 59 1555 1555 1.33
LINK OD1 ASP A 11 MN MN A 201 1555 1555 2.10
LINK OD2 ASP A 38 MN MN A 201 1555 1555 2.22
LINK OD1 ASN A 57 MN MN A 202 1555 1555 2.14
LINK MN MN A 201 O HOH A 386 1555 1555 2.21
LINK MN MN A 201 O HOH A 403 1555 1555 2.20
LINK MN MN A 202 O HOH A 403 1555 1555 2.32
SITE 1 AC1 6 ASP A 11 HIS A 13 ASP A 38 HIS A 112
SITE 2 AC1 6 HOH A 386 HOH A 403
SITE 1 AC2 5 ASP A 38 ASN A 57 HIS A 81 HIS A 110
SITE 2 AC2 5 HOH A 403
SITE 1 AC3 3 ASN A 57 THR A 136 HOH A 403
SITE 1 AC4 5 ASP A 86 ILE A 87 ASN A 88 HIS A 110
SITE 2 AC4 5 HOH A 334
SITE 1 AC5 4 LYS A 153 ASP A 155 SER A 168 HOH A 316
CRYST1 112.467 112.467 112.467 90.00 90.00 90.00 I 21 3 24
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 0.008891 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008891 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008891 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
