HEADER LYASE 31-AUG-10 3OOW
TITLE OCTAMERIC STRUCTURE OF THE PHOSPHORIBOSYLAMINOIMIDAZOLE CARBOXYLASE
TITLE 2 CATALYTIC SUBUNIT FROM FRANCISELLA TULARENSIS SUBSP. TULARENSIS SCHU
TITLE 3 S4.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHOSPHORIBOSYLAMINOIMIDAZOLE CARBOXYLASE,CATALYTIC SUBUNIT;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H;
COMPND 4 EC: 4.1.1.21;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: FRANCISELLA TULARENSIS SUBSP. TULARENSIS;
SOURCE 3 ORGANISM_TAXID: 119856;
SOURCE 4 GENE: FTT_0896, PURE;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21-CODONPLUS(DE3)-RIPL;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PMCSG7
KEYWDS STRUCTURAL GENOMICS, CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS
KEYWDS 2 DISEASES, CSGID, PHOSPHORIBOSYLAMINOIMIDAZOLE CARBOXYLASE, CATALYTIC
KEYWDS 3 SUBUNIT, PURE, FRANCISELLA TULARENSIS SUBSP. TULARENSIS SCHU S4,
KEYWDS 4 CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS DISEASES (CSGID), LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR E.V.FILIPPOVA,Z.WAWRZAK,M.KUDRITSKA,A.EDWARDS,A.SAVCHENKO,
AUTHOR 2 F.W.ANDERSON,CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS DISEASES
AUTHOR 3 (CSGID)
REVDAT 4 06-DEC-23 3OOW 1 REMARK
REVDAT 3 06-SEP-23 3OOW 1 REMARK SEQADV LINK
REVDAT 2 08-NOV-17 3OOW 1 REMARK
REVDAT 1 15-SEP-10 3OOW 0
JRNL AUTH E.V.FILIPPOVA,Z.WAWRZAK,M.KUDRITSKA,A.EDWARDS,A.SAVCHENKO,
JRNL AUTH 2 F.W.ANDERSON
JRNL TITL OCTAMERIC STRUCTURE OF THE PHOSPHORIBOSYLAMINOIMIDAZOLE
JRNL TITL 2 CARBOXYLASE CATALYTIC SUBUNIT FROM FRANCISELLA TULARENSIS
JRNL TITL 3 SUBSP. TULARENSIS SCHU S4.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.75 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
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) : 1.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 77.09
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 29.4
REMARK 3 NUMBER OF REFLECTIONS : 104329
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) : 0.170
REMARK 3 R VALUE (WORKING SET) : 0.168
REMARK 3 FREE R VALUE : 0.205
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 5493
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) : 1.75
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.80
REMARK 3 REFLECTION IN BIN (WORKING SET) : 7643
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.69
REMARK 3 BIN R VALUE (WORKING SET) : 0.2180
REMARK 3 BIN FREE R VALUE SET COUNT : 404
REMARK 3 BIN FREE R VALUE : 0.2580
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 9454
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 170
REMARK 3 SOLVENT ATOMS : 545
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 31.80
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.71
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.99000
REMARK 3 B22 (A**2) : 2.69000
REMARK 3 B33 (A**2) : -1.70000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.115
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.075
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.218
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.969
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.952
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 9836 ; 0.017 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 6446 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 13334 ; 1.500 ; 1.983
REMARK 3 BOND ANGLES OTHERS (DEGREES): 15919 ; 0.962 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1303 ; 5.154 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 344 ;35.630 ;25.058
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1656 ;11.603 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 40 ;22.651 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1560 ; 0.090 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 10885 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1755 ; 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): 6477 ; 0.954 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2651 ; 0.276 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 10349 ; 1.726 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3359 ; 3.158 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2985 ; 4.625 ; 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 : 12
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 2 A 161
REMARK 3 ORIGIN FOR THE GROUP (A): 19.8180 67.3747 102.0354
REMARK 3 T TENSOR
REMARK 3 T11: 0.1285 T22: 0.1166
REMARK 3 T33: 0.1580 T12: -0.0038
REMARK 3 T13: 0.0255 T23: -0.0104
REMARK 3 L TENSOR
REMARK 3 L11: 0.2231 L22: -0.0140
REMARK 3 L33: 1.1609 L12: -0.0959
REMARK 3 L13: -0.0161 L23: 0.0281
REMARK 3 S TENSOR
REMARK 3 S11: 0.0268 S12: 0.0056 S13: 0.0801
REMARK 3 S21: 0.0372 S22: -0.0273 S23: -0.0082
REMARK 3 S31: -0.0883 S32: -0.0785 S33: 0.0005
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 : B 1 B 162
REMARK 3 ORIGIN FOR THE GROUP (A): 68.0973 67.9025 92.4300
REMARK 3 T TENSOR
REMARK 3 T11: 0.1258 T22: 0.1318
REMARK 3 T33: 0.1455 T12: -0.0310
REMARK 3 T13: 0.0114 T23: -0.0143
REMARK 3 L TENSOR
REMARK 3 L11: 0.0467 L22: 0.0775
REMARK 3 L33: 0.8662 L12: 0.0686
REMARK 3 L13: 0.0518 L23: 0.0887
REMARK 3 S TENSOR
REMARK 3 S11: 0.0123 S12: 0.0123 S13: 0.0148
REMARK 3 S21: -0.0339 S22: 0.0117 S23: 0.0104
REMARK 3 S31: -0.1123 S32: 0.0802 S33: -0.0241
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 : C 2 C 162
REMARK 3 ORIGIN FOR THE GROUP (A): 39.2051 67.2198 72.8249
REMARK 3 T TENSOR
REMARK 3 T11: 0.1461 T22: 0.1257
REMARK 3 T33: 0.1220 T12: 0.0169
REMARK 3 T13: 0.0025 T23: 0.0104
REMARK 3 L TENSOR
REMARK 3 L11: 1.0356 L22: 0.0315
REMARK 3 L33: 0.1732 L12: 0.0234
REMARK 3 L13: -0.0836 L23: -0.0762
REMARK 3 S TENSOR
REMARK 3 S11: 0.0472 S12: 0.1000 S13: 0.1066
REMARK 3 S21: 0.0071 S22: -0.0052 S23: 0.0342
REMARK 3 S31: -0.0523 S32: -0.0334 S33: -0.0421
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 : D 2 D 163
REMARK 3 ORIGIN FOR THE GROUP (A): 45.8222 48.9194 72.6786
REMARK 3 T TENSOR
REMARK 3 T11: 0.1304 T22: 0.1277
REMARK 3 T33: 0.1327 T12: 0.0124
REMARK 3 T13: -0.0177 T23: -0.0214
REMARK 3 L TENSOR
REMARK 3 L11: 1.1396 L22: 0.0268
REMARK 3 L33: 0.2230 L12: 0.1519
REMARK 3 L13: -0.1202 L23: 0.0967
REMARK 3 S TENSOR
REMARK 3 S11: 0.0531 S12: 0.1195 S13: -0.1368
REMARK 3 S21: 0.0386 S22: 0.0052 S23: -0.0493
REMARK 3 S31: 0.0251 S32: 0.0045 S33: -0.0584
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 : E 2 E 161
REMARK 3 ORIGIN FOR THE GROUP (A): 68.8543 49.8451 99.5753
REMARK 3 T TENSOR
REMARK 3 T11: 0.1103 T22: 0.1286
REMARK 3 T33: 0.1572 T12: -0.0071
REMARK 3 T13: -0.0176 T23: -0.0021
REMARK 3 L TENSOR
REMARK 3 L11: 0.2121 L22: 0.0606
REMARK 3 L33: 0.9181 L12: -0.1397
REMARK 3 L13: -0.0192 L23: 0.0815
REMARK 3 S TENSOR
REMARK 3 S11: -0.0115 S12: -0.0298 S13: -0.0646
REMARK 3 S21: 0.0315 S22: 0.0215 S23: 0.0031
REMARK 3 S31: 0.0533 S32: 0.0926 S33: -0.0100
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 : F 2 F 163
REMARK 3 ORIGIN FOR THE GROUP (A): 48.3863 67.7868 121.2406
REMARK 3 T TENSOR
REMARK 3 T11: 0.1685 T22: 0.1317
REMARK 3 T33: 0.1004 T12: -0.0154
REMARK 3 T13: -0.0151 T23: -0.0076
REMARK 3 L TENSOR
REMARK 3 L11: 0.9043 L22: 0.1703
REMARK 3 L33: 0.0579 L12: 0.1469
REMARK 3 L13: 0.2361 L23: 0.1449
REMARK 3 S TENSOR
REMARK 3 S11: 0.0235 S12: -0.0605 S13: 0.1185
REMARK 3 S21: 0.0520 S22: -0.0411 S23: -0.0374
REMARK 3 S31: 0.0180 S32: -0.0136 S33: 0.0175
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 : G 2 G 160
REMARK 3 ORIGIN FOR THE GROUP (A): 41.4489 49.6643 122.1379
REMARK 3 T TENSOR
REMARK 3 T11: 0.1682 T22: 0.1331
REMARK 3 T33: 0.0997 T12: -0.0247
REMARK 3 T13: -0.0082 T23: 0.0154
REMARK 3 L TENSOR
REMARK 3 L11: 0.9297 L22: 0.0292
REMARK 3 L33: 0.1178 L12: -0.0013
REMARK 3 L13: -0.0860 L23: -0.0854
REMARK 3 S TENSOR
REMARK 3 S11: 0.0505 S12: -0.0919 S13: -0.0878
REMARK 3 S21: -0.0118 S22: -0.0348 S23: 0.0308
REMARK 3 S31: 0.0559 S32: 0.0186 S33: -0.0156
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 : H 2 H 162
REMARK 3 ORIGIN FOR THE GROUP (A): 19.3740 49.3318 95.1729
REMARK 3 T TENSOR
REMARK 3 T11: 0.1231 T22: 0.1217
REMARK 3 T33: 0.1472 T12: -0.0099
REMARK 3 T13: -0.0016 T23: -0.0090
REMARK 3 L TENSOR
REMARK 3 L11: 0.1727 L22: 0.1053
REMARK 3 L33: 1.1257 L12: 0.1394
REMARK 3 L13: 0.0562 L23: -0.0480
REMARK 3 S TENSOR
REMARK 3 S11: 0.0255 S12: 0.0346 S13: -0.0257
REMARK 3 S21: -0.0050 S22: -0.0034 S23: 0.0077
REMARK 3 S31: 0.1048 S32: -0.0966 S33: -0.0220
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 : E 1 H 169
REMARK 3 ORIGIN FOR THE GROUP (A): 44.3921 58.7684 94.3914
REMARK 3 T TENSOR
REMARK 3 T11: 0.2186 T22: 0.0081
REMARK 3 T33: 0.2004 T12: 0.0097
REMARK 3 T13: 0.0112 T23: 0.0118
REMARK 3 L TENSOR
REMARK 3 L11: -0.2046 L22: 0.4308
REMARK 3 L33: 0.6921 L12: 0.0053
REMARK 3 L13: 0.0717 L23: 0.0067
REMARK 3 S TENSOR
REMARK 3 S11: -0.0420 S12: -0.0301 S13: 0.0001
REMARK 3 S21: -0.0651 S22: 0.0167 S23: 0.1771
REMARK 3 S31: -0.0567 S32: -0.0764 S33: 0.0253
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 1 F 165
REMARK 3 ORIGIN FOR THE GROUP (A): 44.7349 58.7208 96.5202
REMARK 3 T TENSOR
REMARK 3 T11: 0.1363 T22: 0.1610
REMARK 3 T33: 0.0786 T12: 0.0134
REMARK 3 T13: -0.0060 T23: 0.0158
REMARK 3 L TENSOR
REMARK 3 L11: 0.2947 L22: 0.2075
REMARK 3 L33: -0.0848 L12: 0.0908
REMARK 3 L13: -0.0568 L23: 0.0487
REMARK 3 S TENSOR
REMARK 3 S11: 0.0774 S12: 0.0111 S13: -0.0190
REMARK 3 S21: 0.0117 S22: -0.0755 S23: -0.0019
REMARK 3 S31: -0.0101 S32: -0.0106 S33: -0.0019
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 : F 1 G 165
REMARK 3 ORIGIN FOR THE GROUP (A): 44.0519 58.5491 97.1588
REMARK 3 T TENSOR
REMARK 3 T11: 0.0779 T22: 0.3043
REMARK 3 T33: 0.0999 T12: -0.0422
REMARK 3 T13: 0.0493 T23: -0.0236
REMARK 3 L TENSOR
REMARK 3 L11: 4.2785 L22: -1.7090
REMARK 3 L33: 0.6737 L12: -0.5786
REMARK 3 L13: 9.7357 L23: -0.6550
REMARK 3 S TENSOR
REMARK 3 S11: -0.0556 S12: 0.0094 S13: 0.0852
REMARK 3 S21: 0.0190 S22: 0.0710 S23: -0.0008
REMARK 3 S31: 0.2690 S32: 0.0017 S33: -0.0154
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 1 C 168
REMARK 3 ORIGIN FOR THE GROUP (A): 43.8778 58.5894 99.1206
REMARK 3 T TENSOR
REMARK 3 T11: 0.1150 T22: 0.1456
REMARK 3 T33: 0.0648 T12: 0.0064
REMARK 3 T13: -0.0223 T23: 0.0077
REMARK 3 L TENSOR
REMARK 3 L11: 0.8968 L22: 0.2999
REMARK 3 L33: 0.1016 L12: 0.2641
REMARK 3 L13: -0.0841 L23: -0.0267
REMARK 3 S TENSOR
REMARK 3 S11: 0.0553 S12: -0.0190 S13: 0.0086
REMARK 3 S21: 0.0087 S22: 0.0034 S23: 0.0001
REMARK 3 S31: -0.0112 S32: -0.0168 S33: -0.0586
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 3OOW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-SEP-10.
REMARK 100 THE DEPOSITION ID IS D_1000061388.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-AUG-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-D
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.75145
REMARK 200 MONOCHROMATOR : SI-111 CHANNEL
REMARK 200 OPTICS : MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XSCALE
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 110138
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.750
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 7.400
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.5400
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.78
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.8
REMARK 200 DATA REDUNDANCY IN SHELL : 7.70
REMARK 200 R MERGE FOR SHELL (I) : 0.46000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.380
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MOLECULAR REPLACEMENT
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: MRBUMP, CCP4, PHENIX
REMARK 200 STARTING MODEL: PDB ENTRY 3OPQ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 36.08
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.92
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M NH4 DIHYDROGEN PO4, 0.1 M TRIS,
REMARK 280 6% MPD, PH 8.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
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
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 44.28000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 64.31000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 48.15000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 64.31000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 44.28000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 48.15000
REMARK 290 SMTRY3 4 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: OCTAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 42260 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 36840 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -584.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H
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 465 ALA A 0
REMARK 465 MSE A 1
REMARK 465 GLU A 162
REMARK 465 HIS A 163
REMARK 465 SER B -2
REMARK 465 ASN B -1
REMARK 465 ALA B 0
REMARK 465 HIS B 163
REMARK 465 SER C -2
REMARK 465 ASN C -1
REMARK 465 ALA C 0
REMARK 465 MSE C 1
REMARK 465 HIS C 163
REMARK 465 SER D -2
REMARK 465 ASN D -1
REMARK 465 ALA D 0
REMARK 465 MSE D 1
REMARK 465 SER E -2
REMARK 465 ASN E -1
REMARK 465 ALA E 0
REMARK 465 MSE E 1
REMARK 465 GLU E 162
REMARK 465 HIS E 163
REMARK 465 SER F -2
REMARK 465 ASN F -1
REMARK 465 ALA F 0
REMARK 465 MSE F 1
REMARK 465 SER G -2
REMARK 465 ASN G -1
REMARK 465 ALA G 0
REMARK 465 MSE G 1
REMARK 465 ARG G 161
REMARK 465 GLU G 162
REMARK 465 HIS G 163
REMARK 465 SER H -2
REMARK 465 ASN H -1
REMARK 465 ALA H 0
REMARK 465 MSE H 1
REMARK 465 HIS H 163
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 GLN A 104 39.00 -87.14
REMARK 500 GLN B 104 36.49 -84.35
REMARK 500 GLN C 104 41.45 -85.46
REMARK 500 GLN D 104 37.97 -83.26
REMARK 500 GLN E 104 37.17 -85.97
REMARK 500 GLN F 104 38.95 -85.90
REMARK 500 GLN G 104 35.73 -85.00
REMARK 500 GLN H 104 32.86 -82.50
REMARK 500 HIS H 134 44.47 -77.44
REMARK 500 THR H 135 -33.96 -166.26
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 CL A 164
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 165
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 166
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 167
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 168
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 169
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 170
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 164
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 165
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 166
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 167
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 168
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 169
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 164
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 165
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD C 166
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 167
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 168
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT C 169
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 164
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 165
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD D 166
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 167
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 168
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT D 169
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL E 164
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL E 165
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 E 166
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 E 167
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT E 168
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT E 169
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL F 164
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL F 165
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD F 166
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 F 167
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 F 168
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT F 169
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL G 164
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD G 165
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 G 166
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 G 167
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT G 168
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL H 164
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL H 165
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 H 166
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 H 167
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT H 168
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT H 169
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: IDP04072 RELATED DB: TARGETDB
REMARK 900 RELATED ID: 3OPQ RELATED DB: PDB
DBREF 3OOW A 1 163 UNP Q5NGE9 Q5NGE9_FRATT 1 163
DBREF 3OOW B 1 163 UNP Q5NGE9 Q5NGE9_FRATT 1 163
DBREF 3OOW C 1 163 UNP Q5NGE9 Q5NGE9_FRATT 1 163
DBREF 3OOW D 1 163 UNP Q5NGE9 Q5NGE9_FRATT 1 163
DBREF 3OOW E 1 163 UNP Q5NGE9 Q5NGE9_FRATT 1 163
DBREF 3OOW F 1 163 UNP Q5NGE9 Q5NGE9_FRATT 1 163
DBREF 3OOW G 1 163 UNP Q5NGE9 Q5NGE9_FRATT 1 163
DBREF 3OOW H 1 163 UNP Q5NGE9 Q5NGE9_FRATT 1 163
SEQADV 3OOW SER A -2 UNP Q5NGE9 EXPRESSION TAG
SEQADV 3OOW ASN A -1 UNP Q5NGE9 EXPRESSION TAG
SEQADV 3OOW ALA A 0 UNP Q5NGE9 EXPRESSION TAG
SEQADV 3OOW SER B -2 UNP Q5NGE9 EXPRESSION TAG
SEQADV 3OOW ASN B -1 UNP Q5NGE9 EXPRESSION TAG
SEQADV 3OOW ALA B 0 UNP Q5NGE9 EXPRESSION TAG
SEQADV 3OOW SER C -2 UNP Q5NGE9 EXPRESSION TAG
SEQADV 3OOW ASN C -1 UNP Q5NGE9 EXPRESSION TAG
SEQADV 3OOW ALA C 0 UNP Q5NGE9 EXPRESSION TAG
SEQADV 3OOW SER D -2 UNP Q5NGE9 EXPRESSION TAG
SEQADV 3OOW ASN D -1 UNP Q5NGE9 EXPRESSION TAG
SEQADV 3OOW ALA D 0 UNP Q5NGE9 EXPRESSION TAG
SEQADV 3OOW SER E -2 UNP Q5NGE9 EXPRESSION TAG
SEQADV 3OOW ASN E -1 UNP Q5NGE9 EXPRESSION TAG
SEQADV 3OOW ALA E 0 UNP Q5NGE9 EXPRESSION TAG
SEQADV 3OOW SER F -2 UNP Q5NGE9 EXPRESSION TAG
SEQADV 3OOW ASN F -1 UNP Q5NGE9 EXPRESSION TAG
SEQADV 3OOW ALA F 0 UNP Q5NGE9 EXPRESSION TAG
SEQADV 3OOW SER G -2 UNP Q5NGE9 EXPRESSION TAG
SEQADV 3OOW ASN G -1 UNP Q5NGE9 EXPRESSION TAG
SEQADV 3OOW ALA G 0 UNP Q5NGE9 EXPRESSION TAG
SEQADV 3OOW SER H -2 UNP Q5NGE9 EXPRESSION TAG
SEQADV 3OOW ASN H -1 UNP Q5NGE9 EXPRESSION TAG
SEQADV 3OOW ALA H 0 UNP Q5NGE9 EXPRESSION TAG
SEQRES 1 A 166 SER ASN ALA MSE SER VAL GLN VAL GLY VAL ILE MSE GLY
SEQRES 2 A 166 SER LYS SER ASP TRP SER THR MSE LYS GLU CYS CYS ASP
SEQRES 3 A 166 ILE LEU ASP ASN LEU GLY ILE GLY TYR GLU CYS GLU VAL
SEQRES 4 A 166 VAL SER ALA HIS ARG THR PRO ASP LYS MSE PHE ASP TYR
SEQRES 5 A 166 ALA GLU THR ALA LYS GLU ARG GLY LEU LYS VAL ILE ILE
SEQRES 6 A 166 ALA GLY ALA GLY GLY ALA ALA HIS LEU PRO GLY MSE VAL
SEQRES 7 A 166 ALA ALA LYS THR THR LEU PRO VAL LEU GLY VAL PRO VAL
SEQRES 8 A 166 LYS SER SER THR LEU ASN GLY GLN ASP SER LEU LEU SER
SEQRES 9 A 166 ILE VAL GLN MSE PRO ALA GLY ILE PRO VAL ALA THR PHE
SEQRES 10 A 166 ALA ILE GLY MSE ALA GLY ALA LYS ASN ALA ALA LEU PHE
SEQRES 11 A 166 ALA ALA SER ILE LEU GLN HIS THR ASP ILE ASN ILE ALA
SEQRES 12 A 166 LYS ALA LEU ALA GLU PHE ARG ALA GLU GLN THR ARG PHE
SEQRES 13 A 166 VAL LEU GLU ASN PRO ASP PRO ARG GLU HIS
SEQRES 1 B 166 SER ASN ALA MSE SER VAL GLN VAL GLY VAL ILE MSE GLY
SEQRES 2 B 166 SER LYS SER ASP TRP SER THR MSE LYS GLU CYS CYS ASP
SEQRES 3 B 166 ILE LEU ASP ASN LEU GLY ILE GLY TYR GLU CYS GLU VAL
SEQRES 4 B 166 VAL SER ALA HIS ARG THR PRO ASP LYS MSE PHE ASP TYR
SEQRES 5 B 166 ALA GLU THR ALA LYS GLU ARG GLY LEU LYS VAL ILE ILE
SEQRES 6 B 166 ALA GLY ALA GLY GLY ALA ALA HIS LEU PRO GLY MSE VAL
SEQRES 7 B 166 ALA ALA LYS THR THR LEU PRO VAL LEU GLY VAL PRO VAL
SEQRES 8 B 166 LYS SER SER THR LEU ASN GLY GLN ASP SER LEU LEU SER
SEQRES 9 B 166 ILE VAL GLN MSE PRO ALA GLY ILE PRO VAL ALA THR PHE
SEQRES 10 B 166 ALA ILE GLY MSE ALA GLY ALA LYS ASN ALA ALA LEU PHE
SEQRES 11 B 166 ALA ALA SER ILE LEU GLN HIS THR ASP ILE ASN ILE ALA
SEQRES 12 B 166 LYS ALA LEU ALA GLU PHE ARG ALA GLU GLN THR ARG PHE
SEQRES 13 B 166 VAL LEU GLU ASN PRO ASP PRO ARG GLU HIS
SEQRES 1 C 166 SER ASN ALA MSE SER VAL GLN VAL GLY VAL ILE MSE GLY
SEQRES 2 C 166 SER LYS SER ASP TRP SER THR MSE LYS GLU CYS CYS ASP
SEQRES 3 C 166 ILE LEU ASP ASN LEU GLY ILE GLY TYR GLU CYS GLU VAL
SEQRES 4 C 166 VAL SER ALA HIS ARG THR PRO ASP LYS MSE PHE ASP TYR
SEQRES 5 C 166 ALA GLU THR ALA LYS GLU ARG GLY LEU LYS VAL ILE ILE
SEQRES 6 C 166 ALA GLY ALA GLY GLY ALA ALA HIS LEU PRO GLY MSE VAL
SEQRES 7 C 166 ALA ALA LYS THR THR LEU PRO VAL LEU GLY VAL PRO VAL
SEQRES 8 C 166 LYS SER SER THR LEU ASN GLY GLN ASP SER LEU LEU SER
SEQRES 9 C 166 ILE VAL GLN MSE PRO ALA GLY ILE PRO VAL ALA THR PHE
SEQRES 10 C 166 ALA ILE GLY MSE ALA GLY ALA LYS ASN ALA ALA LEU PHE
SEQRES 11 C 166 ALA ALA SER ILE LEU GLN HIS THR ASP ILE ASN ILE ALA
SEQRES 12 C 166 LYS ALA LEU ALA GLU PHE ARG ALA GLU GLN THR ARG PHE
SEQRES 13 C 166 VAL LEU GLU ASN PRO ASP PRO ARG GLU HIS
SEQRES 1 D 166 SER ASN ALA MSE SER VAL GLN VAL GLY VAL ILE MSE GLY
SEQRES 2 D 166 SER LYS SER ASP TRP SER THR MSE LYS GLU CYS CYS ASP
SEQRES 3 D 166 ILE LEU ASP ASN LEU GLY ILE GLY TYR GLU CYS GLU VAL
SEQRES 4 D 166 VAL SER ALA HIS ARG THR PRO ASP LYS MSE PHE ASP TYR
SEQRES 5 D 166 ALA GLU THR ALA LYS GLU ARG GLY LEU LYS VAL ILE ILE
SEQRES 6 D 166 ALA GLY ALA GLY GLY ALA ALA HIS LEU PRO GLY MSE VAL
SEQRES 7 D 166 ALA ALA LYS THR THR LEU PRO VAL LEU GLY VAL PRO VAL
SEQRES 8 D 166 LYS SER SER THR LEU ASN GLY GLN ASP SER LEU LEU SER
SEQRES 9 D 166 ILE VAL GLN MSE PRO ALA GLY ILE PRO VAL ALA THR PHE
SEQRES 10 D 166 ALA ILE GLY MSE ALA GLY ALA LYS ASN ALA ALA LEU PHE
SEQRES 11 D 166 ALA ALA SER ILE LEU GLN HIS THR ASP ILE ASN ILE ALA
SEQRES 12 D 166 LYS ALA LEU ALA GLU PHE ARG ALA GLU GLN THR ARG PHE
SEQRES 13 D 166 VAL LEU GLU ASN PRO ASP PRO ARG GLU HIS
SEQRES 1 E 166 SER ASN ALA MSE SER VAL GLN VAL GLY VAL ILE MSE GLY
SEQRES 2 E 166 SER LYS SER ASP TRP SER THR MSE LYS GLU CYS CYS ASP
SEQRES 3 E 166 ILE LEU ASP ASN LEU GLY ILE GLY TYR GLU CYS GLU VAL
SEQRES 4 E 166 VAL SER ALA HIS ARG THR PRO ASP LYS MSE PHE ASP TYR
SEQRES 5 E 166 ALA GLU THR ALA LYS GLU ARG GLY LEU LYS VAL ILE ILE
SEQRES 6 E 166 ALA GLY ALA GLY GLY ALA ALA HIS LEU PRO GLY MSE VAL
SEQRES 7 E 166 ALA ALA LYS THR THR LEU PRO VAL LEU GLY VAL PRO VAL
SEQRES 8 E 166 LYS SER SER THR LEU ASN GLY GLN ASP SER LEU LEU SER
SEQRES 9 E 166 ILE VAL GLN MSE PRO ALA GLY ILE PRO VAL ALA THR PHE
SEQRES 10 E 166 ALA ILE GLY MSE ALA GLY ALA LYS ASN ALA ALA LEU PHE
SEQRES 11 E 166 ALA ALA SER ILE LEU GLN HIS THR ASP ILE ASN ILE ALA
SEQRES 12 E 166 LYS ALA LEU ALA GLU PHE ARG ALA GLU GLN THR ARG PHE
SEQRES 13 E 166 VAL LEU GLU ASN PRO ASP PRO ARG GLU HIS
SEQRES 1 F 166 SER ASN ALA MSE SER VAL GLN VAL GLY VAL ILE MSE GLY
SEQRES 2 F 166 SER LYS SER ASP TRP SER THR MSE LYS GLU CYS CYS ASP
SEQRES 3 F 166 ILE LEU ASP ASN LEU GLY ILE GLY TYR GLU CYS GLU VAL
SEQRES 4 F 166 VAL SER ALA HIS ARG THR PRO ASP LYS MSE PHE ASP TYR
SEQRES 5 F 166 ALA GLU THR ALA LYS GLU ARG GLY LEU LYS VAL ILE ILE
SEQRES 6 F 166 ALA GLY ALA GLY GLY ALA ALA HIS LEU PRO GLY MSE VAL
SEQRES 7 F 166 ALA ALA LYS THR THR LEU PRO VAL LEU GLY VAL PRO VAL
SEQRES 8 F 166 LYS SER SER THR LEU ASN GLY GLN ASP SER LEU LEU SER
SEQRES 9 F 166 ILE VAL GLN MSE PRO ALA GLY ILE PRO VAL ALA THR PHE
SEQRES 10 F 166 ALA ILE GLY MSE ALA GLY ALA LYS ASN ALA ALA LEU PHE
SEQRES 11 F 166 ALA ALA SER ILE LEU GLN HIS THR ASP ILE ASN ILE ALA
SEQRES 12 F 166 LYS ALA LEU ALA GLU PHE ARG ALA GLU GLN THR ARG PHE
SEQRES 13 F 166 VAL LEU GLU ASN PRO ASP PRO ARG GLU HIS
SEQRES 1 G 166 SER ASN ALA MSE SER VAL GLN VAL GLY VAL ILE MSE GLY
SEQRES 2 G 166 SER LYS SER ASP TRP SER THR MSE LYS GLU CYS CYS ASP
SEQRES 3 G 166 ILE LEU ASP ASN LEU GLY ILE GLY TYR GLU CYS GLU VAL
SEQRES 4 G 166 VAL SER ALA HIS ARG THR PRO ASP LYS MSE PHE ASP TYR
SEQRES 5 G 166 ALA GLU THR ALA LYS GLU ARG GLY LEU LYS VAL ILE ILE
SEQRES 6 G 166 ALA GLY ALA GLY GLY ALA ALA HIS LEU PRO GLY MSE VAL
SEQRES 7 G 166 ALA ALA LYS THR THR LEU PRO VAL LEU GLY VAL PRO VAL
SEQRES 8 G 166 LYS SER SER THR LEU ASN GLY GLN ASP SER LEU LEU SER
SEQRES 9 G 166 ILE VAL GLN MSE PRO ALA GLY ILE PRO VAL ALA THR PHE
SEQRES 10 G 166 ALA ILE GLY MSE ALA GLY ALA LYS ASN ALA ALA LEU PHE
SEQRES 11 G 166 ALA ALA SER ILE LEU GLN HIS THR ASP ILE ASN ILE ALA
SEQRES 12 G 166 LYS ALA LEU ALA GLU PHE ARG ALA GLU GLN THR ARG PHE
SEQRES 13 G 166 VAL LEU GLU ASN PRO ASP PRO ARG GLU HIS
SEQRES 1 H 166 SER ASN ALA MSE SER VAL GLN VAL GLY VAL ILE MSE GLY
SEQRES 2 H 166 SER LYS SER ASP TRP SER THR MSE LYS GLU CYS CYS ASP
SEQRES 3 H 166 ILE LEU ASP ASN LEU GLY ILE GLY TYR GLU CYS GLU VAL
SEQRES 4 H 166 VAL SER ALA HIS ARG THR PRO ASP LYS MSE PHE ASP TYR
SEQRES 5 H 166 ALA GLU THR ALA LYS GLU ARG GLY LEU LYS VAL ILE ILE
SEQRES 6 H 166 ALA GLY ALA GLY GLY ALA ALA HIS LEU PRO GLY MSE VAL
SEQRES 7 H 166 ALA ALA LYS THR THR LEU PRO VAL LEU GLY VAL PRO VAL
SEQRES 8 H 166 LYS SER SER THR LEU ASN GLY GLN ASP SER LEU LEU SER
SEQRES 9 H 166 ILE VAL GLN MSE PRO ALA GLY ILE PRO VAL ALA THR PHE
SEQRES 10 H 166 ALA ILE GLY MSE ALA GLY ALA LYS ASN ALA ALA LEU PHE
SEQRES 11 H 166 ALA ALA SER ILE LEU GLN HIS THR ASP ILE ASN ILE ALA
SEQRES 12 H 166 LYS ALA LEU ALA GLU PHE ARG ALA GLU GLN THR ARG PHE
SEQRES 13 H 166 VAL LEU GLU ASN PRO ASP PRO ARG GLU HIS
MODRES 3OOW MSE A 9 MET SELENOMETHIONINE
MODRES 3OOW MSE A 18 MET SELENOMETHIONINE
MODRES 3OOW MSE A 46 MET SELENOMETHIONINE
MODRES 3OOW MSE A 74 MET SELENOMETHIONINE
MODRES 3OOW MSE A 105 MET SELENOMETHIONINE
MODRES 3OOW MSE A 118 MET SELENOMETHIONINE
MODRES 3OOW MSE B 1 MET SELENOMETHIONINE
MODRES 3OOW MSE B 9 MET SELENOMETHIONINE
MODRES 3OOW MSE B 18 MET SELENOMETHIONINE
MODRES 3OOW MSE B 46 MET SELENOMETHIONINE
MODRES 3OOW MSE B 74 MET SELENOMETHIONINE
MODRES 3OOW MSE B 105 MET SELENOMETHIONINE
MODRES 3OOW MSE B 118 MET SELENOMETHIONINE
MODRES 3OOW MSE C 9 MET SELENOMETHIONINE
MODRES 3OOW MSE C 18 MET SELENOMETHIONINE
MODRES 3OOW MSE C 46 MET SELENOMETHIONINE
MODRES 3OOW MSE C 74 MET SELENOMETHIONINE
MODRES 3OOW MSE C 105 MET SELENOMETHIONINE
MODRES 3OOW MSE C 118 MET SELENOMETHIONINE
MODRES 3OOW MSE D 9 MET SELENOMETHIONINE
MODRES 3OOW MSE D 18 MET SELENOMETHIONINE
MODRES 3OOW MSE D 46 MET SELENOMETHIONINE
MODRES 3OOW MSE D 74 MET SELENOMETHIONINE
MODRES 3OOW MSE D 105 MET SELENOMETHIONINE
MODRES 3OOW MSE D 118 MET SELENOMETHIONINE
MODRES 3OOW MSE E 9 MET SELENOMETHIONINE
MODRES 3OOW MSE E 18 MET SELENOMETHIONINE
MODRES 3OOW MSE E 46 MET SELENOMETHIONINE
MODRES 3OOW MSE E 74 MET SELENOMETHIONINE
MODRES 3OOW MSE E 105 MET SELENOMETHIONINE
MODRES 3OOW MSE E 118 MET SELENOMETHIONINE
MODRES 3OOW MSE F 9 MET SELENOMETHIONINE
MODRES 3OOW MSE F 18 MET SELENOMETHIONINE
MODRES 3OOW MSE F 46 MET SELENOMETHIONINE
MODRES 3OOW MSE F 74 MET SELENOMETHIONINE
MODRES 3OOW MSE F 105 MET SELENOMETHIONINE
MODRES 3OOW MSE F 118 MET SELENOMETHIONINE
MODRES 3OOW MSE G 9 MET SELENOMETHIONINE
MODRES 3OOW MSE G 18 MET SELENOMETHIONINE
MODRES 3OOW MSE G 46 MET SELENOMETHIONINE
MODRES 3OOW MSE G 74 MET SELENOMETHIONINE
MODRES 3OOW MSE G 105 MET SELENOMETHIONINE
MODRES 3OOW MSE G 118 MET SELENOMETHIONINE
MODRES 3OOW MSE H 9 MET SELENOMETHIONINE
MODRES 3OOW MSE H 18 MET SELENOMETHIONINE
MODRES 3OOW MSE H 46 MET SELENOMETHIONINE
MODRES 3OOW MSE H 74 MET SELENOMETHIONINE
MODRES 3OOW MSE H 105 MET SELENOMETHIONINE
MODRES 3OOW MSE H 118 MET SELENOMETHIONINE
HET MSE A 9 8
HET MSE A 18 8
HET MSE A 46 16
HET MSE A 74 8
HET MSE A 105 8
HET MSE A 118 8
HET MSE B 1 8
HET MSE B 9 8
HET MSE B 18 8
HET MSE B 46 16
HET MSE B 74 8
HET MSE B 105 8
HET MSE B 118 8
HET MSE C 9 8
HET MSE C 18 8
HET MSE C 46 16
HET MSE C 74 8
HET MSE C 105 8
HET MSE C 118 8
HET MSE D 9 8
HET MSE D 18 8
HET MSE D 46 16
HET MSE D 74 8
HET MSE D 105 8
HET MSE D 118 8
HET MSE E 9 8
HET MSE E 18 8
HET MSE E 46 16
HET MSE E 74 8
HET MSE E 105 8
HET MSE E 118 8
HET MSE F 9 8
HET MSE F 18 8
HET MSE F 46 16
HET MSE F 74 8
HET MSE F 105 8
HET MSE F 118 8
HET MSE G 9 8
HET MSE G 18 8
HET MSE G 46 8
HET MSE G 74 8
HET MSE G 105 8
HET MSE G 118 8
HET MSE H 9 8
HET MSE H 18 8
HET MSE H 46 16
HET MSE H 74 8
HET MSE H 105 8
HET MSE H 118 8
HET CL A 164 1
HET CL A 165 1
HET PO4 A 166 5
HET PO4 A 167 5
HET PO4 A 168 5
HET FMT A 169 3
HET FMT A 170 3
HET CL B 164 1
HET PO4 B 165 5
HET PO4 B 166 5
HET FMT B 167 3
HET FMT B 168 3
HET FMT B 169 3
HET CL C 164 1
HET CL C 165 1
HET MPD C 166 8
HET PO4 C 167 5
HET PO4 C 168 5
HET FMT C 169 3
HET CL D 164 1
HET CL D 165 1
HET MPD D 166 8
HET PO4 D 167 5
HET PO4 D 168 5
HET FMT D 169 3
HET CL E 164 1
HET CL E 165 1
HET PO4 E 166 5
HET PO4 E 167 5
HET FMT E 168 3
HET FMT E 169 3
HET CL F 164 1
HET CL F 165 1
HET MPD F 166 8
HET PO4 F 167 5
HET PO4 F 168 5
HET FMT F 169 3
HET CL G 164 1
HET MPD G 165 8
HET PO4 G 166 5
HET PO4 G 167 5
HET FMT G 168 3
HET CL H 164 1
HET CL H 165 1
HET PO4 H 166 5
HET PO4 H 167 5
HET FMT H 168 3
HET FMT H 169 3
HETNAM MSE SELENOMETHIONINE
HETNAM CL CHLORIDE ION
HETNAM PO4 PHOSPHATE ION
HETNAM FMT FORMIC ACID
HETNAM MPD (4S)-2-METHYL-2,4-PENTANEDIOL
FORMUL 1 MSE 49(C5 H11 N O2 SE)
FORMUL 9 CL 14(CL 1-)
FORMUL 11 PO4 17(O4 P 3-)
FORMUL 14 FMT 13(C H2 O2)
FORMUL 24 MPD 4(C6 H14 O2)
FORMUL 57 HOH *545(H2 O)
HELIX 1 1 SER A 11 SER A 13 5 3
HELIX 2 2 ASP A 14 LEU A 28 1 15
HELIX 3 3 THR A 42 ALA A 53 1 12
HELIX 4 4 HIS A 70 LYS A 78 1 9
HELIX 5 5 GLY A 95 GLN A 104 1 10
HELIX 6 6 GLY A 117 GLN A 133 1 17
HELIX 7 7 ASP A 136 GLU A 156 1 21
HELIX 8 8 SER B 11 SER B 13 5 3
HELIX 9 9 ASP B 14 LEU B 28 1 15
HELIX 10 10 THR B 42 ALA B 53 1 12
HELIX 11 11 HIS B 70 THR B 79 1 10
HELIX 12 12 GLY B 95 GLN B 104 1 10
HELIX 13 13 GLY B 117 GLN B 133 1 17
HELIX 14 14 ASP B 136 ASN B 157 1 22
HELIX 15 15 SER C 11 SER C 13 5 3
HELIX 16 16 ASP C 14 LEU C 28 1 15
HELIX 17 17 THR C 42 ALA C 53 1 12
HELIX 18 18 HIS C 70 THR C 79 1 10
HELIX 19 19 GLY C 95 GLN C 104 1 10
HELIX 20 20 GLY C 117 GLN C 133 1 17
HELIX 21 21 ASP C 136 ASN C 157 1 22
HELIX 22 22 SER D 11 SER D 13 5 3
HELIX 23 23 ASP D 14 LEU D 28 1 15
HELIX 24 24 THR D 42 ALA D 53 1 12
HELIX 25 25 HIS D 70 THR D 79 1 10
HELIX 26 26 GLY D 95 GLN D 104 1 10
HELIX 27 27 GLY D 117 GLN D 133 1 17
HELIX 28 28 ASP D 136 ASN D 157 1 22
HELIX 29 29 SER E 11 SER E 13 5 3
HELIX 30 30 ASP E 14 LEU E 28 1 15
HELIX 31 31 THR E 42 ALA E 53 1 12
HELIX 32 32 HIS E 70 THR E 79 1 10
HELIX 33 33 GLY E 95 GLN E 104 1 10
HELIX 34 34 GLY E 117 GLN E 133 1 17
HELIX 35 35 ASP E 136 GLU E 156 1 21
HELIX 36 36 SER F 11 SER F 13 5 3
HELIX 37 37 ASP F 14 LEU F 28 1 15
HELIX 38 38 THR F 42 ALA F 53 1 12
HELIX 39 39 HIS F 70 THR F 79 1 10
HELIX 40 40 GLY F 95 GLN F 104 1 10
HELIX 41 41 GLY F 117 GLN F 133 1 17
HELIX 42 42 ASP F 136 ASN F 157 1 22
HELIX 43 43 SER G 11 SER G 13 5 3
HELIX 44 44 ASP G 14 LEU G 28 1 15
HELIX 45 45 THR G 42 ALA G 53 1 12
HELIX 46 46 HIS G 70 THR G 79 1 10
HELIX 47 47 GLY G 95 GLN G 104 1 10
HELIX 48 48 GLY G 117 GLN G 133 1 17
HELIX 49 49 ASP G 136 GLU G 156 1 21
HELIX 50 50 SER H 11 SER H 13 5 3
HELIX 51 51 ASP H 14 LEU H 28 1 15
HELIX 52 52 THR H 42 ALA H 53 1 12
HELIX 53 53 HIS H 70 THR H 79 1 10
HELIX 54 54 GLY H 95 GLN H 104 1 10
HELIX 55 55 GLY H 117 GLN H 133 1 17
HELIX 56 56 ASP H 136 GLU H 156 1 21
SHEET 1 A 5 GLY A 31 VAL A 36 0
SHEET 2 A 5 VAL A 3 MSE A 9 1 N VAL A 7 O GLU A 33
SHEET 3 A 5 VAL A 60 ALA A 65 1 O ILE A 62 N ILE A 8
SHEET 4 A 5 VAL A 83 PRO A 87 1 O LEU A 84 N ILE A 61
SHEET 5 A 5 ALA A 112 THR A 113 1 O ALA A 112 N GLY A 85
SHEET 1 B 5 GLY B 31 VAL B 36 0
SHEET 2 B 5 VAL B 3 MSE B 9 1 N VAL B 7 O GLU B 33
SHEET 3 B 5 VAL B 60 GLY B 66 1 O ILE B 62 N ILE B 8
SHEET 4 B 5 VAL B 83 VAL B 88 1 O LEU B 84 N ALA B 63
SHEET 5 B 5 ALA B 112 THR B 113 1 O ALA B 112 N GLY B 85
SHEET 1 C 5 TYR C 32 VAL C 36 0
SHEET 2 C 5 VAL C 5 MSE C 9 1 N VAL C 7 O GLU C 33
SHEET 3 C 5 VAL C 60 ALA C 65 1 O ILE C 62 N GLY C 6
SHEET 4 C 5 VAL C 83 PRO C 87 1 O LEU C 84 N ALA C 63
SHEET 5 C 5 ALA C 112 THR C 113 1 O ALA C 112 N GLY C 85
SHEET 1 D 5 GLY D 31 VAL D 36 0
SHEET 2 D 5 VAL D 3 MSE D 9 1 N VAL D 7 O GLU D 33
SHEET 3 D 5 VAL D 60 ALA D 65 1 O ILE D 62 N GLY D 6
SHEET 4 D 5 VAL D 83 PRO D 87 1 O LEU D 84 N ALA D 63
SHEET 5 D 5 ALA D 112 THR D 113 1 O ALA D 112 N GLY D 85
SHEET 1 E 5 GLY E 31 VAL E 36 0
SHEET 2 E 5 VAL E 3 MSE E 9 1 N VAL E 7 O GLU E 33
SHEET 3 E 5 VAL E 60 ALA E 65 1 O ILE E 62 N ILE E 8
SHEET 4 E 5 VAL E 83 PRO E 87 1 O LEU E 84 N ILE E 61
SHEET 5 E 5 ALA E 112 THR E 113 1 O ALA E 112 N GLY E 85
SHEET 1 F 5 TYR F 32 VAL F 36 0
SHEET 2 F 5 VAL F 5 MSE F 9 1 N VAL F 7 O GLU F 33
SHEET 3 F 5 VAL F 60 ALA F 65 1 O ILE F 62 N GLY F 6
SHEET 4 F 5 VAL F 83 PRO F 87 1 O LEU F 84 N ALA F 63
SHEET 5 F 5 ALA F 112 THR F 113 1 O ALA F 112 N GLY F 85
SHEET 1 G 5 GLY G 31 VAL G 36 0
SHEET 2 G 5 VAL G 3 MSE G 9 1 N VAL G 7 O GLU G 33
SHEET 3 G 5 VAL G 60 ALA G 65 1 O ILE G 62 N ILE G 8
SHEET 4 G 5 VAL G 83 PRO G 87 1 O LEU G 84 N ALA G 63
SHEET 5 G 5 ALA G 112 THR G 113 1 O ALA G 112 N GLY G 85
SHEET 1 H 5 GLY H 31 VAL H 36 0
SHEET 2 H 5 VAL H 3 MSE H 9 1 N VAL H 7 O GLU H 33
SHEET 3 H 5 VAL H 60 ALA H 65 1 O ILE H 62 N GLY H 6
SHEET 4 H 5 VAL H 83 PRO H 87 1 O LEU H 84 N ALA H 63
SHEET 5 H 5 ALA H 112 THR H 113 1 O ALA H 112 N GLY H 85
LINK C ILE A 8 N MSE A 9 1555 1555 1.33
LINK C MSE A 9 N GLY A 10 1555 1555 1.32
LINK C THR A 17 N MSE A 18 1555 1555 1.34
LINK C MSE A 18 N LYS A 19 1555 1555 1.35
LINK C LYS A 45 N AMSE A 46 1555 1555 1.33
LINK C LYS A 45 N BMSE A 46 1555 1555 1.32
LINK C AMSE A 46 N PHE A 47 1555 1555 1.33
LINK C BMSE A 46 N PHE A 47 1555 1555 1.34
LINK C GLY A 73 N MSE A 74 1555 1555 1.33
LINK C MSE A 74 N VAL A 75 1555 1555 1.34
LINK C GLN A 104 N MSE A 105 1555 1555 1.34
LINK C MSE A 105 N PRO A 106 1555 1555 1.34
LINK C GLY A 117 N MSE A 118 1555 1555 1.34
LINK C MSE A 118 N ALA A 119 1555 1555 1.33
LINK C MSE B 1 N SER B 2 1555 1555 1.33
LINK C ILE B 8 N MSE B 9 1555 1555 1.32
LINK C MSE B 9 N GLY B 10 1555 1555 1.33
LINK C THR B 17 N MSE B 18 1555 1555 1.32
LINK C MSE B 18 N LYS B 19 1555 1555 1.33
LINK C LYS B 45 N AMSE B 46 1555 1555 1.33
LINK C LYS B 45 N BMSE B 46 1555 1555 1.33
LINK C AMSE B 46 N PHE B 47 1555 1555 1.34
LINK C BMSE B 46 N PHE B 47 1555 1555 1.34
LINK C GLY B 73 N MSE B 74 1555 1555 1.32
LINK C MSE B 74 N VAL B 75 1555 1555 1.34
LINK C GLN B 104 N MSE B 105 1555 1555 1.34
LINK C MSE B 105 N PRO B 106 1555 1555 1.33
LINK C GLY B 117 N MSE B 118 1555 1555 1.33
LINK C MSE B 118 N ALA B 119 1555 1555 1.34
LINK C ILE C 8 N MSE C 9 1555 1555 1.32
LINK C MSE C 9 N GLY C 10 1555 1555 1.32
LINK C THR C 17 N MSE C 18 1555 1555 1.33
LINK C MSE C 18 N LYS C 19 1555 1555 1.34
LINK C LYS C 45 N AMSE C 46 1555 1555 1.32
LINK C LYS C 45 N BMSE C 46 1555 1555 1.33
LINK C AMSE C 46 N PHE C 47 1555 1555 1.34
LINK C BMSE C 46 N PHE C 47 1555 1555 1.33
LINK C GLY C 73 N MSE C 74 1555 1555 1.33
LINK C MSE C 74 N VAL C 75 1555 1555 1.33
LINK C GLN C 104 N MSE C 105 1555 1555 1.33
LINK C MSE C 105 N PRO C 106 1555 1555 1.34
LINK C GLY C 117 N MSE C 118 1555 1555 1.33
LINK C MSE C 118 N ALA C 119 1555 1555 1.34
LINK C ILE D 8 N MSE D 9 1555 1555 1.32
LINK C MSE D 9 N GLY D 10 1555 1555 1.33
LINK C THR D 17 N MSE D 18 1555 1555 1.33
LINK C MSE D 18 N LYS D 19 1555 1555 1.34
LINK C LYS D 45 N AMSE D 46 1555 1555 1.34
LINK C LYS D 45 N BMSE D 46 1555 1555 1.33
LINK C AMSE D 46 N PHE D 47 1555 1555 1.32
LINK C BMSE D 46 N PHE D 47 1555 1555 1.32
LINK C GLY D 73 N MSE D 74 1555 1555 1.33
LINK C MSE D 74 N VAL D 75 1555 1555 1.34
LINK C GLN D 104 N MSE D 105 1555 1555 1.33
LINK C MSE D 105 N PRO D 106 1555 1555 1.34
LINK C GLY D 117 N MSE D 118 1555 1555 1.34
LINK C MSE D 118 N ALA D 119 1555 1555 1.33
LINK C ILE E 8 N MSE E 9 1555 1555 1.33
LINK C MSE E 9 N GLY E 10 1555 1555 1.33
LINK C THR E 17 N MSE E 18 1555 1555 1.33
LINK C MSE E 18 N LYS E 19 1555 1555 1.33
LINK C LYS E 45 N AMSE E 46 1555 1555 1.33
LINK C LYS E 45 N BMSE E 46 1555 1555 1.32
LINK C AMSE E 46 N PHE E 47 1555 1555 1.33
LINK C BMSE E 46 N PHE E 47 1555 1555 1.33
LINK C GLY E 73 N MSE E 74 1555 1555 1.32
LINK C MSE E 74 N VAL E 75 1555 1555 1.34
LINK C GLN E 104 N MSE E 105 1555 1555 1.33
LINK C MSE E 105 N PRO E 106 1555 1555 1.32
LINK C GLY E 117 N MSE E 118 1555 1555 1.33
LINK C MSE E 118 N ALA E 119 1555 1555 1.35
LINK C ILE F 8 N MSE F 9 1555 1555 1.32
LINK C MSE F 9 N GLY F 10 1555 1555 1.33
LINK C THR F 17 N MSE F 18 1555 1555 1.33
LINK C MSE F 18 N LYS F 19 1555 1555 1.33
LINK C LYS F 45 N AMSE F 46 1555 1555 1.33
LINK C LYS F 45 N BMSE F 46 1555 1555 1.33
LINK C AMSE F 46 N PHE F 47 1555 1555 1.33
LINK C BMSE F 46 N PHE F 47 1555 1555 1.33
LINK C GLY F 73 N MSE F 74 1555 1555 1.32
LINK C MSE F 74 N VAL F 75 1555 1555 1.33
LINK C GLN F 104 N MSE F 105 1555 1555 1.32
LINK C MSE F 105 N PRO F 106 1555 1555 1.36
LINK C GLY F 117 N MSE F 118 1555 1555 1.33
LINK C MSE F 118 N ALA F 119 1555 1555 1.34
LINK C ILE G 8 N MSE G 9 1555 1555 1.33
LINK C MSE G 9 N GLY G 10 1555 1555 1.33
LINK C THR G 17 N MSE G 18 1555 1555 1.34
LINK C MSE G 18 N LYS G 19 1555 1555 1.34
LINK C LYS G 45 N MSE G 46 1555 1555 1.33
LINK C MSE G 46 N PHE G 47 1555 1555 1.33
LINK C GLY G 73 N MSE G 74 1555 1555 1.33
LINK C MSE G 74 N VAL G 75 1555 1555 1.33
LINK C GLN G 104 N MSE G 105 1555 1555 1.33
LINK C MSE G 105 N PRO G 106 1555 1555 1.35
LINK C GLY G 117 N MSE G 118 1555 1555 1.33
LINK C MSE G 118 N ALA G 119 1555 1555 1.33
LINK C ILE H 8 N MSE H 9 1555 1555 1.33
LINK C MSE H 9 N GLY H 10 1555 1555 1.33
LINK C THR H 17 N MSE H 18 1555 1555 1.33
LINK C MSE H 18 N LYS H 19 1555 1555 1.34
LINK C LYS H 45 N AMSE H 46 1555 1555 1.32
LINK C LYS H 45 N BMSE H 46 1555 1555 1.33
LINK C AMSE H 46 N PHE H 47 1555 1555 1.33
LINK C BMSE H 46 N PHE H 47 1555 1555 1.33
LINK C GLY H 73 N MSE H 74 1555 1555 1.33
LINK C MSE H 74 N VAL H 75 1555 1555 1.34
LINK C GLN H 104 N MSE H 105 1555 1555 1.33
LINK C MSE H 105 N PRO H 106 1555 1555 1.33
LINK C GLY H 117 N MSE H 118 1555 1555 1.33
LINK C MSE H 118 N ALA H 119 1555 1555 1.33
SITE 1 AC1 4 HIS A 70 LEU A 71 HOH A 182 HOH A 203
SITE 1 AC2 4 THR A 42 ASP A 44 LYS A 45 HOH A 250
SITE 1 AC3 8 SER A 38 HIS A 40 ARG A 41 PO4 A 167
SITE 2 AC3 8 HOH A 182 HOH A 311 HOH A 531 PRO G 106
SITE 1 AC4 7 GLY A 10 SER A 11 ASP A 14 ALA A 65
SITE 2 AC4 7 GLY A 66 PO4 A 166 HOH A 203
SITE 1 AC5 5 GLU A 51 LYS A 78 HOH A 465 LYS D 141
SITE 2 AC5 5 ASP G 44
SITE 1 AC6 4 ASN A 94 ASN B 94 ASN C 94 ASN F 94
SITE 1 AC7 4 GLY A 117 MSE A 118 HOH A 175 HOH A 534
SITE 1 AC8 4 THR B 42 ASP B 44 LYS B 45 HOH B 205
SITE 1 AC9 7 ASN A 138 GLY B 29 ASP B 136 ASN B 138
SITE 2 AC9 7 ILE B 139 HOH B 193 HOH B 294
SITE 1 BC1 7 SER B 38 HIS B 40 ARG B 41 FMT B 168
SITE 2 BC1 7 HOH B 183 HOH B 206 PRO D 106
SITE 1 BC2 2 THR B 52 ARG B 56
SITE 1 BC3 5 SER B 11 ASP B 14 ALA B 65 GLY B 66
SITE 2 BC3 5 PO4 B 166
SITE 1 BC4 1 MSE B 118
SITE 1 BC5 4 HIS C 70 LEU C 71 HOH C 187 HOH C 192
SITE 1 BC6 4 THR C 42 ASP C 44 LYS C 45 HOH C 301
SITE 1 BC7 4 GLN B 96 GLN C 96 HOH C 526 GLN D 96
SITE 1 BC8 9 GLY C 10 SER C 38 HIS C 40 ARG C 41
SITE 2 BC8 9 PO4 C 168 HOH C 187 HOH C 207 HOH C 335
SITE 3 BC8 9 PRO H 106
SITE 1 BC9 7 GLY C 10 SER C 11 ASP C 14 ALA C 65
SITE 2 BC9 7 GLY C 66 PO4 C 167 HOH C 192
SITE 1 CC1 2 MSE C 118 HOH C 177
SITE 1 CC2 4 HIS D 70 LEU D 71 HOH D 172 HOH D 202
SITE 1 CC3 4 THR D 42 ASP D 44 LYS D 45 HOH E 302
SITE 1 CC4 5 GLN B 96 GLN D 96 HOH D 515 HOH D 528
SITE 2 CC4 5 GLN E 96
SITE 1 CC5 8 PRO B 106 GLY D 10 SER D 38 HIS D 40
SITE 2 CC5 8 ARG D 41 PO4 D 168 HOH D 172 HOH D 399
SITE 1 CC6 8 PRO B 106 GLY D 10 SER D 11 ASP D 14
SITE 2 CC6 8 ALA D 65 GLY D 66 PO4 D 167 HOH D 202
SITE 1 CC7 3 GLY D 117 MSE D 118 HOH D 188
SITE 1 CC8 5 HIS E 40 HIS E 70 LEU E 71 HOH E 196
SITE 2 CC8 5 HOH E 383
SITE 1 CC9 5 THR E 42 ASP E 44 LYS E 45 HOH E 257
SITE 2 CC9 5 HOH E 478
SITE 1 DC1 7 GLY E 10 SER E 11 ASP E 14 ALA E 65
SITE 2 DC1 7 GLY E 66 PO4 E 167 HOH E 383
SITE 1 DC2 7 SER E 38 HIS E 40 ARG E 41 PO4 E 166
SITE 2 DC2 7 HOH E 196 HOH E 289 PRO F 106
SITE 1 DC3 3 MSE E 118 HOH E 183 HOH E 509
SITE 1 DC4 2 ASN E 94 ASN H 94
SITE 1 DC5 5 HIS F 40 HIS F 70 LEU F 71 HOH F 174
SITE 2 DC5 5 HOH F 221
SITE 1 DC6 4 THR F 42 ASP F 44 LYS F 45 HOH F 286
SITE 1 DC7 4 GLN F 96 HOH F 527 GLN G 96 LEU G 100
SITE 1 DC8 8 PRO E 106 GLY F 10 SER F 38 HIS F 40
SITE 2 DC8 8 ARG F 41 PO4 F 168 HOH F 174 HOH F 342
SITE 1 DC9 7 GLY F 10 SER F 11 ASP F 14 ALA F 65
SITE 2 DC9 7 GLY F 66 PO4 F 167 HOH F 221
SITE 1 EC1 3 GLY F 117 MSE F 118 HOH F 184
SITE 1 EC2 4 HIS G 70 LEU G 71 HOH G 178 HOH G 191
SITE 1 EC3 4 HOH C 530 GLN G 96 HOH G 529 GLN H 96
SITE 1 EC4 8 PRO A 106 GLY G 10 SER G 11 ASP G 14
SITE 2 EC4 8 ALA G 65 GLY G 66 PO4 G 167 HOH G 178
SITE 1 EC5 8 PRO A 106 SER G 38 HIS G 40 ARG G 41
SITE 2 EC5 8 PO4 G 166 HOH G 169 HOH G 191 HOH G 541
SITE 1 EC6 3 MSE G 118 HOH G 186 HOH G 188
SITE 1 EC7 4 HIS H 70 LEU H 71 HOH H 191 HOH H 262
SITE 1 EC8 5 THR H 42 ASP H 44 LYS H 45 HOH H 194
SITE 2 EC8 5 HOH H 475
SITE 1 EC9 7 GLY H 10 SER H 11 ASP H 14 ALA H 65
SITE 2 EC9 7 GLY H 66 PO4 H 167 HOH H 262
SITE 1 FC1 7 PRO C 106 SER H 38 HIS H 40 ARG H 41
SITE 2 FC1 7 PO4 H 166 HOH H 191 HOH H 351
SITE 1 FC2 3 MSE H 118 HOH H 179 HOH H 188
SITE 1 FC3 1 GLY H 29
CRYST1 88.560 96.300 128.620 90.00 90.00 90.00 P 21 21 21 32
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 0.011292 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010384 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007775 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
