HEADER ISOMERASE 19-JUL-13 4LR9
TITLE PHOSPHOPENTOMUTASE S154A VARIANT SOAKED WITH 2,3-DIDEOXYRIBOSE 5-
TITLE 2 PHOSPHATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHOSPHOPENTOMUTASE;
COMPND 3 CHAIN: A, B, C;
COMPND 4 SYNONYM: PHOSPHODEOXYRIBOMUTASE;
COMPND 5 EC: 5.4.2.7;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS CEREUS;
SOURCE 3 ORGANISM_TAXID: 1396;
SOURCE 4 GENE: BC_4087, DEOB;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET
KEYWDS ALKALINE PHOSPHATASE FAMILY, ISOMERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR W.A.BIRMINGHAM,C.A.STARBIRD,T.D.PANOSIAN,D.P.NANNEMANN,T.M.IVERSON,
AUTHOR 2 B.O.BACHMANN
REVDAT 7 20-SEP-23 4LR9 1 REMARK HETSYN
REVDAT 6 29-JUL-20 4LR9 1 COMPND REMARK SEQADV HETNAM
REVDAT 6 2 1 LINK SITE ATOM
REVDAT 5 17-JUL-19 4LR9 1 REMARK LINK
REVDAT 4 30-APR-14 4LR9 1 JRNL
REVDAT 3 09-APR-14 4LR9 1 JRNL
REVDAT 2 26-MAR-14 4LR9 1 JRNL
REVDAT 1 31-JUL-13 4LR9 0
JRNL AUTH W.R.BIRMINGHAM,C.A.STARBIRD,T.D.PANOSIAN,D.P.NANNEMANN,
JRNL AUTH 2 T.M.IVERSON,B.O.BACHMANN
JRNL TITL BIORETROSYNTHETIC CONSTRUCTION OF A DIDANOSINE BIOSYNTHETIC
JRNL TITL 2 PATHWAY.
JRNL REF NAT.CHEM.BIOL. V. 10 392 2014
JRNL REFN ISSN 1552-4450
JRNL PMID 24657930
JRNL DOI 10.1038/NCHEMBIO.1494
REMARK 2
REMARK 2 RESOLUTION. 2.10 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) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 3 NUMBER OF REFLECTIONS : 77794
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) : 0.171
REMARK 3 R VALUE (WORKING SET) : 0.169
REMARK 3 FREE R VALUE : 0.213
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 4042
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) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.15
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5361
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.31
REMARK 3 BIN R VALUE (WORKING SET) : 0.2240
REMARK 3 BIN FREE R VALUE SET COUNT : 276
REMARK 3 BIN FREE R VALUE : 0.3010
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 9193
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 34
REMARK 3 SOLVENT ATOMS : 691
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.65
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.08000
REMARK 3 B22 (A**2) : -1.19000
REMARK 3 B33 (A**2) : 0.19000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.37000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.184
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.162
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.110
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.928
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.960
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.936
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 9363 ; 0.008 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 12665 ; 1.200 ; 1.988
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1173 ; 5.626 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 434 ;37.584 ;25.023
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1630 ;14.199 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 46 ;16.121 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1387 ; 0.080 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7120 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 4692 ; 0.446 ; 1.296
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5862 ; 0.755 ; 1.941
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4671 ; 0.707 ; 1.384
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 79
REMARK 3 ORIGIN FOR THE GROUP (A): 1.9215 5.6663 -14.3491
REMARK 3 T TENSOR
REMARK 3 T11: 0.0973 T22: 0.0588
REMARK 3 T33: 0.0474 T12: 0.0009
REMARK 3 T13: -0.0018 T23: 0.0169
REMARK 3 L TENSOR
REMARK 3 L11: 1.7071 L22: 1.7112
REMARK 3 L33: 1.2011 L12: -0.4724
REMARK 3 L13: -0.4221 L23: 0.6123
REMARK 3 S TENSOR
REMARK 3 S11: -0.0187 S12: 0.2836 S13: -0.0103
REMARK 3 S21: -0.2393 S22: -0.0046 S23: 0.1020
REMARK 3 S31: -0.0166 S32: -0.0055 S33: 0.0232
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 80 A 158
REMARK 3 ORIGIN FOR THE GROUP (A): 21.1367 18.2040 7.0375
REMARK 3 T TENSOR
REMARK 3 T11: 0.1421 T22: 0.1857
REMARK 3 T33: 0.1602 T12: 0.0107
REMARK 3 T13: -0.0008 T23: -0.0324
REMARK 3 L TENSOR
REMARK 3 L11: 3.3234 L22: 0.2365
REMARK 3 L33: 2.0415 L12: -0.2343
REMARK 3 L13: 1.9614 L23: -0.3720
REMARK 3 S TENSOR
REMARK 3 S11: 0.1066 S12: -0.0078 S13: -0.0348
REMARK 3 S21: -0.0103 S22: -0.0757 S23: -0.1530
REMARK 3 S31: 0.0996 S32: 0.3926 S33: -0.0310
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 159 A 215
REMARK 3 ORIGIN FOR THE GROUP (A): 19.0428 15.6195 16.3500
REMARK 3 T TENSOR
REMARK 3 T11: 0.0485 T22: 0.1541
REMARK 3 T33: 0.0806 T12: -0.0150
REMARK 3 T13: -0.0248 T23: -0.0448
REMARK 3 L TENSOR
REMARK 3 L11: 3.5359 L22: 6.4424
REMARK 3 L33: 5.2606 L12: -1.4038
REMARK 3 L13: 1.4611 L23: -3.3405
REMARK 3 S TENSOR
REMARK 3 S11: 0.1289 S12: -0.2483 S13: -0.0945
REMARK 3 S21: -0.0534 S22: -0.0477 S23: 0.1412
REMARK 3 S31: 0.1551 S32: -0.1260 S33: -0.0812
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 216 A 392
REMARK 3 ORIGIN FOR THE GROUP (A): -2.0765 8.9253 -2.8546
REMARK 3 T TENSOR
REMARK 3 T11: 0.0615 T22: 0.0047
REMARK 3 T33: 0.0317 T12: -0.0040
REMARK 3 T13: -0.0175 T23: 0.0040
REMARK 3 L TENSOR
REMARK 3 L11: 1.0663 L22: 1.6559
REMARK 3 L33: 0.8785 L12: -0.2598
REMARK 3 L13: -0.4073 L23: 0.1529
REMARK 3 S TENSOR
REMARK 3 S11: -0.0223 S12: -0.0179 S13: 0.0310
REMARK 3 S21: -0.0158 S22: 0.0227 S23: 0.1324
REMARK 3 S31: 0.0321 S32: -0.0430 S33: -0.0004
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 : B 2 B 31
REMARK 3 ORIGIN FOR THE GROUP (A): -26.9469 -0.7776 47.2320
REMARK 3 T TENSOR
REMARK 3 T11: 0.0306 T22: 0.0300
REMARK 3 T33: 0.1286 T12: 0.0226
REMARK 3 T13: -0.0110 T23: -0.0076
REMARK 3 L TENSOR
REMARK 3 L11: 4.0056 L22: 2.2004
REMARK 3 L33: 8.8793 L12: -1.1849
REMARK 3 L13: 4.9786 L23: -2.2302
REMARK 3 S TENSOR
REMARK 3 S11: -0.1862 S12: 0.0260 S13: 0.1544
REMARK 3 S21: -0.0041 S22: -0.0086 S23: 0.1755
REMARK 3 S31: -0.4177 S32: -0.2337 S33: 0.1948
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 : B 32 B 100
REMARK 3 ORIGIN FOR THE GROUP (A): -30.2188 -4.9898 46.0997
REMARK 3 T TENSOR
REMARK 3 T11: 0.0336 T22: 0.0880
REMARK 3 T33: 0.1646 T12: 0.0005
REMARK 3 T13: -0.0378 T23: 0.0194
REMARK 3 L TENSOR
REMARK 3 L11: 0.9284 L22: 2.6763
REMARK 3 L33: 1.6981 L12: 0.6353
REMARK 3 L13: -0.1032 L23: 0.2058
REMARK 3 S TENSOR
REMARK 3 S11: -0.0451 S12: 0.1343 S13: -0.0870
REMARK 3 S21: -0.0627 S22: 0.1023 S23: 0.2152
REMARK 3 S31: 0.1096 S32: -0.2131 S33: -0.0572
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 : B 101 B 216
REMARK 3 ORIGIN FOR THE GROUP (A): -1.3309 4.2584 29.1818
REMARK 3 T TENSOR
REMARK 3 T11: 0.1003 T22: 0.0980
REMARK 3 T33: 0.0747 T12: -0.0270
REMARK 3 T13: 0.0017 T23: 0.0234
REMARK 3 L TENSOR
REMARK 3 L11: 4.8876 L22: 3.0245
REMARK 3 L33: 3.3817 L12: -1.5512
REMARK 3 L13: -0.1476 L23: 0.9462
REMARK 3 S TENSOR
REMARK 3 S11: 0.0581 S12: 0.3199 S13: 0.1334
REMARK 3 S21: 0.0561 S22: -0.1030 S23: 0.1176
REMARK 3 S31: 0.1022 S32: -0.0065 S33: 0.0449
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 : B 217 B 392
REMARK 3 ORIGIN FOR THE GROUP (A): -20.7384 -3.7966 52.3487
REMARK 3 T TENSOR
REMARK 3 T11: 0.0226 T22: 0.0014
REMARK 3 T33: 0.0817 T12: -0.0003
REMARK 3 T13: 0.0100 T23: -0.0031
REMARK 3 L TENSOR
REMARK 3 L11: 1.0261 L22: 1.4937
REMARK 3 L33: 1.4479 L12: 0.1115
REMARK 3 L13: 0.4188 L23: 0.0198
REMARK 3 S TENSOR
REMARK 3 S11: -0.0263 S12: -0.0173 S13: -0.0006
REMARK 3 S21: 0.0231 S22: 0.0315 S23: 0.0696
REMARK 3 S31: -0.0032 S32: -0.0186 S33: -0.0051
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 : C 3 C 98
REMARK 3 ORIGIN FOR THE GROUP (A): 25.3375 -7.8131 62.0766
REMARK 3 T TENSOR
REMARK 3 T11: 0.0877 T22: 0.5339
REMARK 3 T33: 0.1433 T12: 0.1485
REMARK 3 T13: 0.0018 T23: 0.0576
REMARK 3 L TENSOR
REMARK 3 L11: 1.0200 L22: 1.6979
REMARK 3 L33: 4.6108 L12: -0.1698
REMARK 3 L13: 1.2956 L23: -1.7839
REMARK 3 S TENSOR
REMARK 3 S11: 0.0801 S12: 0.1929 S13: 0.0161
REMARK 3 S21: -0.1195 S22: -0.3201 S23: -0.2383
REMARK 3 S31: 0.4560 S32: 1.2835 S33: 0.2400
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 : C 99 C 140
REMARK 3 ORIGIN FOR THE GROUP (A): 1.9745 -1.3972 84.8970
REMARK 3 T TENSOR
REMARK 3 T11: 0.1919 T22: 0.3770
REMARK 3 T33: 0.1283 T12: -0.0052
REMARK 3 T13: 0.0039 T23: -0.0308
REMARK 3 L TENSOR
REMARK 3 L11: 5.3499 L22: 4.1236
REMARK 3 L33: 2.3185 L12: 1.4843
REMARK 3 L13: -1.8467 L23: -0.8098
REMARK 3 S TENSOR
REMARK 3 S11: 0.1226 S12: -0.7030 S13: 0.0709
REMARK 3 S21: 0.0446 S22: -0.2162 S23: -0.5761
REMARK 3 S31: -0.1395 S32: 0.7177 S33: 0.0936
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 : C 141 C 215
REMARK 3 ORIGIN FOR THE GROUP (A): -4.3751 -3.5711 78.2451
REMARK 3 T TENSOR
REMARK 3 T11: 0.0669 T22: 0.0963
REMARK 3 T33: 0.0768 T12: 0.0527
REMARK 3 T13: 0.0224 T23: -0.0258
REMARK 3 L TENSOR
REMARK 3 L11: 4.0152 L22: 5.7113
REMARK 3 L33: 5.2042 L12: 1.0435
REMARK 3 L13: -0.2422 L23: 0.2580
REMARK 3 S TENSOR
REMARK 3 S11: -0.0788 S12: -0.0767 S13: -0.0617
REMARK 3 S21: -0.1345 S22: 0.1749 S23: -0.2916
REMARK 3 S31: -0.0319 S32: 0.3714 S33: -0.0962
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 : C 216 C 392
REMARK 3 ORIGIN FOR THE GROUP (A): 16.8367 -5.3264 56.2418
REMARK 3 T TENSOR
REMARK 3 T11: 0.0768 T22: 0.2516
REMARK 3 T33: 0.0884 T12: 0.0809
REMARK 3 T13: 0.0078 T23: 0.0204
REMARK 3 L TENSOR
REMARK 3 L11: 1.0272 L22: 1.4388
REMARK 3 L33: 4.7939 L12: -0.5268
REMARK 3 L13: 1.1224 L23: -1.2914
REMARK 3 S TENSOR
REMARK 3 S11: 0.0789 S12: 0.1376 S13: 0.0122
REMARK 3 S21: -0.1566 S22: -0.1471 S23: -0.0268
REMARK 3 S31: 0.3803 S32: 0.7520 S33: 0.0682
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: NULL
REMARK 4
REMARK 4 4LR9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-JUL-13.
REMARK 100 THE DEPOSITION ID IS D_1000080985.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
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-G
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : DIAMOND(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 81866
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.08700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.18
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.6
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.37000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 3M8W
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.20
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.57
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 17% PEG3350, 50 MM MANGANESE CHLORIDE,
REMARK 280 50 MM AMMONIUM ACETATE, 100 MM BIS-TRIS, PH 5.5, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 38.30750
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A -21
REMARK 465 GLY A -20
REMARK 465 SER A -19
REMARK 465 SER A -18
REMARK 465 HIS A -17
REMARK 465 HIS A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 SER A -11
REMARK 465 SER A -10
REMARK 465 GLY A -9
REMARK 465 LEU A -8
REMARK 465 VAL A -7
REMARK 465 PRO A -6
REMARK 465 ARG A -5
REMARK 465 GLY A -4
REMARK 465 SER A -3
REMARK 465 HIS A -2
REMARK 465 MET A -1
REMARK 465 ALA A 0
REMARK 465 SER A 1
REMARK 465 LYS A 393
REMARK 465 LYS A 394
REMARK 465 MET B -21
REMARK 465 GLY B -20
REMARK 465 SER B -19
REMARK 465 SER B -18
REMARK 465 HIS B -17
REMARK 465 HIS B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 SER B -11
REMARK 465 SER B -10
REMARK 465 GLY B -9
REMARK 465 LEU B -8
REMARK 465 VAL B -7
REMARK 465 PRO B -6
REMARK 465 ARG B -5
REMARK 465 GLY B -4
REMARK 465 SER B -3
REMARK 465 HIS B -2
REMARK 465 MET B -1
REMARK 465 ALA B 0
REMARK 465 SER B 1
REMARK 465 LYS B 393
REMARK 465 LYS B 394
REMARK 465 MET C -21
REMARK 465 GLY C -20
REMARK 465 SER C -19
REMARK 465 SER C -18
REMARK 465 HIS C -17
REMARK 465 HIS C -16
REMARK 465 HIS C -15
REMARK 465 HIS C -14
REMARK 465 HIS C -13
REMARK 465 HIS C -12
REMARK 465 SER C -11
REMARK 465 SER C -10
REMARK 465 GLY C -9
REMARK 465 LEU C -8
REMARK 465 VAL C -7
REMARK 465 PRO C -6
REMARK 465 ARG C -5
REMARK 465 GLY C -4
REMARK 465 SER C -3
REMARK 465 HIS C -2
REMARK 465 MET C -1
REMARK 465 ALA C 0
REMARK 465 SER C 1
REMARK 465 ASN C 2
REMARK 465 LYS C 393
REMARK 465 LYS C 394
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 GLU A 67 CG CD OE1 OE2
REMARK 480 LYS A 257 CG CD CE NZ
REMARK 480 GLU A 355 CD OE1 OE2
REMARK 480 LYS B 110 CG CD CE NZ
REMARK 480 LYS B 257 CD CE NZ
REMARK 480 LYS C 65 CE NZ
REMARK 480 GLU C 67 CB CG CD OE1 OE2
REMARK 480 LYS C 68 CG CD CE NZ
REMARK 480 GLU C 106 CG CD OE1 OE2
REMARK 480 LYS C 110 CG CD CE NZ
REMARK 480 GLU C 111 CD OE1 OE2
REMARK 480 GLU C 118 CG CD OE1 OE2
REMARK 480 GLU C 182 CD OE1 OE2
REMARK 480 GLU C 187 CB CG CD OE1 OE2
REMARK 480 LYS C 188 CG CD CE NZ
REMARK 480 LYS C 257 CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 LYS C 65 CD LYS C 65 CE -0.202
REMARK 500 LYS C 68 CB LYS C 68 CG -0.350
REMARK 500 GLU C 118 CB GLU C 118 CG 0.145
REMARK 500 GLU C 187 CA GLU C 187 CB -0.210
REMARK 500 LYS C 257 CG LYS C 257 CD -0.215
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 LYS C 68 CA - CB - CG ANGL. DEV. = 25.0 DEGREES
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 ASP A 32 88.88 -171.69
REMARK 500 THR A 74 -169.09 -173.98
REMARK 500 THR A 153 -168.36 -128.00
REMARK 500 TYR A 189 53.46 -140.02
REMARK 500 ASN A 205 54.62 -160.05
REMARK 500 PRO A 210 3.57 -63.82
REMARK 500 HIS A 328 -171.69 174.62
REMARK 500 ASN A 330 76.76 -156.42
REMARK 500 HIS A 339 170.02 -59.02
REMARK 500 SER B 14 6.71 80.57
REMARK 500 ASP B 32 95.33 -166.09
REMARK 500 THR B 74 -169.31 -170.76
REMARK 500 TYR B 189 56.43 -144.05
REMARK 500 ASN B 205 57.25 -153.31
REMARK 500 HIS B 328 -178.22 176.32
REMARK 500 ASN B 330 75.15 -161.29
REMARK 500 LYS B 380 125.78 -39.19
REMARK 500 SER C 14 5.53 81.30
REMARK 500 ASP C 32 90.25 -168.61
REMARK 500 THR C 74 -167.22 -172.26
REMARK 500 ALA C 154 -154.72 -140.84
REMARK 500 ASN C 205 46.12 -154.58
REMARK 500 HIS C 328 -177.07 169.92
REMARK 500 ASN C 330 72.35 -161.22
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 402 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 13 OD1
REMARK 620 2 ASP A 13 OD2 54.3
REMARK 620 3 TPO A 85 OG1 121.3 102.9
REMARK 620 4 ASP A 327 OD2 117.7 87.0 112.9
REMARK 620 5 HIS A 328 NE2 107.2 156.4 99.8 90.6
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN A 403 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 27 O
REMARK 620 2 ASP A 28 OD1 77.7
REMARK 620 3 HIS A 334 NE2 83.5 97.4
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN A 401 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TPO A 85 O1P
REMARK 620 2 ASP A 156 OD2 72.4
REMARK 620 3 ASP A 156 OD1 90.8 49.9
REMARK 620 4 ASP A 286 OD1 85.9 132.1 89.6
REMARK 620 5 ASP A 286 OD2 101.6 171.4 137.7 51.8
REMARK 620 6 HIS A 291 NE2 167.6 95.4 79.3 101.4 90.8
REMARK 620 7 HIS A 339 NE2 87.1 94.7 142.9 127.0 78.7 96.2
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN B 402 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 13 OD1
REMARK 620 2 ASP B 13 OD2 54.9
REMARK 620 3 TPO B 85 OG1 126.3 103.9
REMARK 620 4 ASP B 327 OD2 112.8 85.8 113.7
REMARK 620 5 HIS B 328 NE2 99.3 150.9 102.8 93.9
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN B 404 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 36 NE2
REMARK 620 2 HOH B 720 O 70.8
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN B 401 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TPO B 85 O1P
REMARK 620 2 ASP B 156 OD2 84.2
REMARK 620 3 ASP B 286 OD1 80.9 127.1
REMARK 620 4 HIS B 291 NE2 178.5 94.3 99.5
REMARK 620 5 HIS B 339 NE2 87.7 107.4 122.3 93.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN C 402 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 13 OD1
REMARK 620 2 ASP C 13 OD2 54.8
REMARK 620 3 TPO C 85 OG1 121.4 100.7
REMARK 620 4 ASP C 327 OD2 115.0 86.1 114.8
REMARK 620 5 HIS C 328 NE2 103.5 153.9 103.6 92.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN C 403 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY C 27 O
REMARK 620 2 ASP C 28 OD1 85.5
REMARK 620 3 HIS C 334 NE2 98.2 102.8
REMARK 620 4 HOH C 572 O 92.9 175.8 81.3
REMARK 620 5 HOH C 632 O 93.9 93.9 160.0 82.3
REMARK 620 6 HOH C 659 O 166.4 81.5 88.6 99.7 83.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN C 401 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TPO C 85 O3P
REMARK 620 2 ASP C 156 OD2 85.3
REMARK 620 3 ASP C 286 OD1 77.6 125.4
REMARK 620 4 HIS C 291 NE2 169.6 89.5 98.3
REMARK 620 5 HIS C 339 NE2 89.2 102.3 128.4 100.7
REMARK 620 N 1 2 3 4
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3UN3 RELATED DB: PDB
REMARK 900 RELATED ID: 3TX0 RELATED DB: PDB
REMARK 900 RELATED ID: 3TWZ RELATED DB: PDB
REMARK 900 RELATED ID: 3M8Z RELATED DB: PDB
REMARK 900 RELATED ID: 4LR7 RELATED DB: PDB
REMARK 900 RELATED ID: 4LR8 RELATED DB: PDB
REMARK 900 RELATED ID: 4LRA RELATED DB: PDB
REMARK 900 RELATED ID: 4LRB RELATED DB: PDB
REMARK 900 RELATED ID: 4LRC RELATED DB: PDB
REMARK 900 RELATED ID: 4LRD RELATED DB: PDB
REMARK 900 RELATED ID: 4LRE RELATED DB: PDB
REMARK 900 RELATED ID: 4LRF RELATED DB: PDB
DBREF 4LR9 A 2 394 UNP Q818Z9 DEOB_BACCR 2 394
DBREF 4LR9 B 2 394 UNP Q818Z9 DEOB_BACCR 2 394
DBREF 4LR9 C 2 394 UNP Q818Z9 DEOB_BACCR 2 394
SEQADV 4LR9 MET A -21 UNP Q818Z9 EXPRESSION TAG
SEQADV 4LR9 GLY A -20 UNP Q818Z9 EXPRESSION TAG
SEQADV 4LR9 SER A -19 UNP Q818Z9 EXPRESSION TAG
SEQADV 4LR9 SER A -18 UNP Q818Z9 EXPRESSION TAG
SEQADV 4LR9 HIS A -17 UNP Q818Z9 EXPRESSION TAG
SEQADV 4LR9 HIS A -16 UNP Q818Z9 EXPRESSION TAG
SEQADV 4LR9 HIS A -15 UNP Q818Z9 EXPRESSION TAG
SEQADV 4LR9 HIS A -14 UNP Q818Z9 EXPRESSION TAG
SEQADV 4LR9 HIS A -13 UNP Q818Z9 EXPRESSION TAG
SEQADV 4LR9 HIS A -12 UNP Q818Z9 EXPRESSION TAG
SEQADV 4LR9 SER A -11 UNP Q818Z9 EXPRESSION TAG
SEQADV 4LR9 SER A -10 UNP Q818Z9 EXPRESSION TAG
SEQADV 4LR9 GLY A -9 UNP Q818Z9 EXPRESSION TAG
SEQADV 4LR9 LEU A -8 UNP Q818Z9 EXPRESSION TAG
SEQADV 4LR9 VAL A -7 UNP Q818Z9 EXPRESSION TAG
SEQADV 4LR9 PRO A -6 UNP Q818Z9 EXPRESSION TAG
SEQADV 4LR9 ARG A -5 UNP Q818Z9 EXPRESSION TAG
SEQADV 4LR9 GLY A -4 UNP Q818Z9 EXPRESSION TAG
SEQADV 4LR9 SER A -3 UNP Q818Z9 EXPRESSION TAG
SEQADV 4LR9 HIS A -2 UNP Q818Z9 EXPRESSION TAG
SEQADV 4LR9 MET A -1 UNP Q818Z9 EXPRESSION TAG
SEQADV 4LR9 ALA A 0 UNP Q818Z9 EXPRESSION TAG
SEQADV 4LR9 SER A 1 UNP Q818Z9 EXPRESSION TAG
SEQADV 4LR9 ALA A 154 UNP Q818Z9 SER 154 ENGINEERED MUTATION
SEQADV 4LR9 MET B -21 UNP Q818Z9 EXPRESSION TAG
SEQADV 4LR9 GLY B -20 UNP Q818Z9 EXPRESSION TAG
SEQADV 4LR9 SER B -19 UNP Q818Z9 EXPRESSION TAG
SEQADV 4LR9 SER B -18 UNP Q818Z9 EXPRESSION TAG
SEQADV 4LR9 HIS B -17 UNP Q818Z9 EXPRESSION TAG
SEQADV 4LR9 HIS B -16 UNP Q818Z9 EXPRESSION TAG
SEQADV 4LR9 HIS B -15 UNP Q818Z9 EXPRESSION TAG
SEQADV 4LR9 HIS B -14 UNP Q818Z9 EXPRESSION TAG
SEQADV 4LR9 HIS B -13 UNP Q818Z9 EXPRESSION TAG
SEQADV 4LR9 HIS B -12 UNP Q818Z9 EXPRESSION TAG
SEQADV 4LR9 SER B -11 UNP Q818Z9 EXPRESSION TAG
SEQADV 4LR9 SER B -10 UNP Q818Z9 EXPRESSION TAG
SEQADV 4LR9 GLY B -9 UNP Q818Z9 EXPRESSION TAG
SEQADV 4LR9 LEU B -8 UNP Q818Z9 EXPRESSION TAG
SEQADV 4LR9 VAL B -7 UNP Q818Z9 EXPRESSION TAG
SEQADV 4LR9 PRO B -6 UNP Q818Z9 EXPRESSION TAG
SEQADV 4LR9 ARG B -5 UNP Q818Z9 EXPRESSION TAG
SEQADV 4LR9 GLY B -4 UNP Q818Z9 EXPRESSION TAG
SEQADV 4LR9 SER B -3 UNP Q818Z9 EXPRESSION TAG
SEQADV 4LR9 HIS B -2 UNP Q818Z9 EXPRESSION TAG
SEQADV 4LR9 MET B -1 UNP Q818Z9 EXPRESSION TAG
SEQADV 4LR9 ALA B 0 UNP Q818Z9 EXPRESSION TAG
SEQADV 4LR9 SER B 1 UNP Q818Z9 EXPRESSION TAG
SEQADV 4LR9 ALA B 154 UNP Q818Z9 SER 154 ENGINEERED MUTATION
SEQADV 4LR9 MET C -21 UNP Q818Z9 EXPRESSION TAG
SEQADV 4LR9 GLY C -20 UNP Q818Z9 EXPRESSION TAG
SEQADV 4LR9 SER C -19 UNP Q818Z9 EXPRESSION TAG
SEQADV 4LR9 SER C -18 UNP Q818Z9 EXPRESSION TAG
SEQADV 4LR9 HIS C -17 UNP Q818Z9 EXPRESSION TAG
SEQADV 4LR9 HIS C -16 UNP Q818Z9 EXPRESSION TAG
SEQADV 4LR9 HIS C -15 UNP Q818Z9 EXPRESSION TAG
SEQADV 4LR9 HIS C -14 UNP Q818Z9 EXPRESSION TAG
SEQADV 4LR9 HIS C -13 UNP Q818Z9 EXPRESSION TAG
SEQADV 4LR9 HIS C -12 UNP Q818Z9 EXPRESSION TAG
SEQADV 4LR9 SER C -11 UNP Q818Z9 EXPRESSION TAG
SEQADV 4LR9 SER C -10 UNP Q818Z9 EXPRESSION TAG
SEQADV 4LR9 GLY C -9 UNP Q818Z9 EXPRESSION TAG
SEQADV 4LR9 LEU C -8 UNP Q818Z9 EXPRESSION TAG
SEQADV 4LR9 VAL C -7 UNP Q818Z9 EXPRESSION TAG
SEQADV 4LR9 PRO C -6 UNP Q818Z9 EXPRESSION TAG
SEQADV 4LR9 ARG C -5 UNP Q818Z9 EXPRESSION TAG
SEQADV 4LR9 GLY C -4 UNP Q818Z9 EXPRESSION TAG
SEQADV 4LR9 SER C -3 UNP Q818Z9 EXPRESSION TAG
SEQADV 4LR9 HIS C -2 UNP Q818Z9 EXPRESSION TAG
SEQADV 4LR9 MET C -1 UNP Q818Z9 EXPRESSION TAG
SEQADV 4LR9 ALA C 0 UNP Q818Z9 EXPRESSION TAG
SEQADV 4LR9 SER C 1 UNP Q818Z9 EXPRESSION TAG
SEQADV 4LR9 ALA C 154 UNP Q818Z9 SER 154 ENGINEERED MUTATION
SEQRES 1 A 416 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 416 LEU VAL PRO ARG GLY SER HIS MET ALA SER ASN LYS TYR
SEQRES 3 A 416 LYS ARG ILE PHE LEU VAL VAL MET ASP SER VAL GLY ILE
SEQRES 4 A 416 GLY GLU ALA PRO ASP ALA GLU GLN PHE GLY ASP LEU GLY
SEQRES 5 A 416 SER ASP THR ILE GLY HIS ILE ALA GLU HIS MET ASN GLY
SEQRES 6 A 416 LEU GLN MET PRO ASN MET VAL LYS LEU GLY LEU GLY ASN
SEQRES 7 A 416 ILE ARG GLU MET LYS GLY ILE SER LYS VAL GLU LYS PRO
SEQRES 8 A 416 LEU GLY TYR TYR THR LYS MET GLN GLU LYS SER THR GLY
SEQRES 9 A 416 LYS ASP TPO MET THR GLY HIS TRP GLU ILE MET GLY LEU
SEQRES 10 A 416 TYR ILE ASP THR PRO PHE GLN VAL PHE PRO GLU GLY PHE
SEQRES 11 A 416 PRO LYS GLU LEU LEU ASP GLU LEU GLU GLU LYS THR GLY
SEQRES 12 A 416 ARG LYS ILE ILE GLY ASN LYS PRO ALA SER GLY THR GLU
SEQRES 13 A 416 ILE LEU ASP GLU LEU GLY GLN GLU GLN MET GLU THR GLY
SEQRES 14 A 416 SER LEU ILE VAL TYR THR ALA ALA ASP SER VAL LEU GLN
SEQRES 15 A 416 ILE ALA ALA HIS GLU GLU VAL VAL PRO LEU ASP GLU LEU
SEQRES 16 A 416 TYR LYS ILE CYS LYS ILE ALA ARG GLU LEU THR LEU ASP
SEQRES 17 A 416 GLU LYS TYR MET VAL GLY ARG VAL ILE ALA ARG PRO PHE
SEQRES 18 A 416 VAL GLY GLU PRO GLY ASN PHE THR ARG THR PRO ASN ARG
SEQRES 19 A 416 HIS ASP TYR ALA LEU LYS PRO PHE GLY ARG THR VAL MET
SEQRES 20 A 416 ASN GLU LEU LYS ASP SER ASP TYR ASP VAL ILE ALA ILE
SEQRES 21 A 416 GLY LYS ILE SER ASP ILE TYR ASP GLY GLU GLY VAL THR
SEQRES 22 A 416 GLU SER LEU ARG THR LYS SER ASN MET ASP GLY MET ASP
SEQRES 23 A 416 LYS LEU VAL ASP THR LEU ASN MET ASP PHE THR GLY LEU
SEQRES 24 A 416 SER PHE LEU ASN LEU VAL ASP PHE ASP ALA LEU PHE GLY
SEQRES 25 A 416 HIS ARG ARG ASP PRO GLN GLY TYR GLY GLU ALA LEU GLN
SEQRES 26 A 416 GLU TYR ASP ALA ARG LEU PRO GLU VAL PHE ALA LYS LEU
SEQRES 27 A 416 LYS GLU ASP ASP LEU LEU LEU ILE THR ALA ASP HIS GLY
SEQRES 28 A 416 ASN ASP PRO ILE HIS PRO GLY THR ASP HIS THR ARG GLU
SEQRES 29 A 416 TYR VAL PRO LEU LEU ALA TYR SER PRO SER MET LYS GLU
SEQRES 30 A 416 GLY GLY GLN GLU LEU PRO LEU ARG GLN THR PHE ALA ASP
SEQRES 31 A 416 ILE GLY ALA THR VAL ALA GLU ASN PHE GLY VAL LYS MET
SEQRES 32 A 416 PRO GLU TYR GLY THR SER PHE LEU ASN GLU LEU LYS LYS
SEQRES 1 B 416 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 416 LEU VAL PRO ARG GLY SER HIS MET ALA SER ASN LYS TYR
SEQRES 3 B 416 LYS ARG ILE PHE LEU VAL VAL MET ASP SER VAL GLY ILE
SEQRES 4 B 416 GLY GLU ALA PRO ASP ALA GLU GLN PHE GLY ASP LEU GLY
SEQRES 5 B 416 SER ASP THR ILE GLY HIS ILE ALA GLU HIS MET ASN GLY
SEQRES 6 B 416 LEU GLN MET PRO ASN MET VAL LYS LEU GLY LEU GLY ASN
SEQRES 7 B 416 ILE ARG GLU MET LYS GLY ILE SER LYS VAL GLU LYS PRO
SEQRES 8 B 416 LEU GLY TYR TYR THR LYS MET GLN GLU LYS SER THR GLY
SEQRES 9 B 416 LYS ASP TPO MET THR GLY HIS TRP GLU ILE MET GLY LEU
SEQRES 10 B 416 TYR ILE ASP THR PRO PHE GLN VAL PHE PRO GLU GLY PHE
SEQRES 11 B 416 PRO LYS GLU LEU LEU ASP GLU LEU GLU GLU LYS THR GLY
SEQRES 12 B 416 ARG LYS ILE ILE GLY ASN LYS PRO ALA SER GLY THR GLU
SEQRES 13 B 416 ILE LEU ASP GLU LEU GLY GLN GLU GLN MET GLU THR GLY
SEQRES 14 B 416 SER LEU ILE VAL TYR THR ALA ALA ASP SER VAL LEU GLN
SEQRES 15 B 416 ILE ALA ALA HIS GLU GLU VAL VAL PRO LEU ASP GLU LEU
SEQRES 16 B 416 TYR LYS ILE CYS LYS ILE ALA ARG GLU LEU THR LEU ASP
SEQRES 17 B 416 GLU LYS TYR MET VAL GLY ARG VAL ILE ALA ARG PRO PHE
SEQRES 18 B 416 VAL GLY GLU PRO GLY ASN PHE THR ARG THR PRO ASN ARG
SEQRES 19 B 416 HIS ASP TYR ALA LEU LYS PRO PHE GLY ARG THR VAL MET
SEQRES 20 B 416 ASN GLU LEU LYS ASP SER ASP TYR ASP VAL ILE ALA ILE
SEQRES 21 B 416 GLY LYS ILE SER ASP ILE TYR ASP GLY GLU GLY VAL THR
SEQRES 22 B 416 GLU SER LEU ARG THR LYS SER ASN MET ASP GLY MET ASP
SEQRES 23 B 416 LYS LEU VAL ASP THR LEU ASN MET ASP PHE THR GLY LEU
SEQRES 24 B 416 SER PHE LEU ASN LEU VAL ASP PHE ASP ALA LEU PHE GLY
SEQRES 25 B 416 HIS ARG ARG ASP PRO GLN GLY TYR GLY GLU ALA LEU GLN
SEQRES 26 B 416 GLU TYR ASP ALA ARG LEU PRO GLU VAL PHE ALA LYS LEU
SEQRES 27 B 416 LYS GLU ASP ASP LEU LEU LEU ILE THR ALA ASP HIS GLY
SEQRES 28 B 416 ASN ASP PRO ILE HIS PRO GLY THR ASP HIS THR ARG GLU
SEQRES 29 B 416 TYR VAL PRO LEU LEU ALA TYR SER PRO SER MET LYS GLU
SEQRES 30 B 416 GLY GLY GLN GLU LEU PRO LEU ARG GLN THR PHE ALA ASP
SEQRES 31 B 416 ILE GLY ALA THR VAL ALA GLU ASN PHE GLY VAL LYS MET
SEQRES 32 B 416 PRO GLU TYR GLY THR SER PHE LEU ASN GLU LEU LYS LYS
SEQRES 1 C 416 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 C 416 LEU VAL PRO ARG GLY SER HIS MET ALA SER ASN LYS TYR
SEQRES 3 C 416 LYS ARG ILE PHE LEU VAL VAL MET ASP SER VAL GLY ILE
SEQRES 4 C 416 GLY GLU ALA PRO ASP ALA GLU GLN PHE GLY ASP LEU GLY
SEQRES 5 C 416 SER ASP THR ILE GLY HIS ILE ALA GLU HIS MET ASN GLY
SEQRES 6 C 416 LEU GLN MET PRO ASN MET VAL LYS LEU GLY LEU GLY ASN
SEQRES 7 C 416 ILE ARG GLU MET LYS GLY ILE SER LYS VAL GLU LYS PRO
SEQRES 8 C 416 LEU GLY TYR TYR THR LYS MET GLN GLU LYS SER THR GLY
SEQRES 9 C 416 LYS ASP TPO MET THR GLY HIS TRP GLU ILE MET GLY LEU
SEQRES 10 C 416 TYR ILE ASP THR PRO PHE GLN VAL PHE PRO GLU GLY PHE
SEQRES 11 C 416 PRO LYS GLU LEU LEU ASP GLU LEU GLU GLU LYS THR GLY
SEQRES 12 C 416 ARG LYS ILE ILE GLY ASN LYS PRO ALA SER GLY THR GLU
SEQRES 13 C 416 ILE LEU ASP GLU LEU GLY GLN GLU GLN MET GLU THR GLY
SEQRES 14 C 416 SER LEU ILE VAL TYR THR ALA ALA ASP SER VAL LEU GLN
SEQRES 15 C 416 ILE ALA ALA HIS GLU GLU VAL VAL PRO LEU ASP GLU LEU
SEQRES 16 C 416 TYR LYS ILE CYS LYS ILE ALA ARG GLU LEU THR LEU ASP
SEQRES 17 C 416 GLU LYS TYR MET VAL GLY ARG VAL ILE ALA ARG PRO PHE
SEQRES 18 C 416 VAL GLY GLU PRO GLY ASN PHE THR ARG THR PRO ASN ARG
SEQRES 19 C 416 HIS ASP TYR ALA LEU LYS PRO PHE GLY ARG THR VAL MET
SEQRES 20 C 416 ASN GLU LEU LYS ASP SER ASP TYR ASP VAL ILE ALA ILE
SEQRES 21 C 416 GLY LYS ILE SER ASP ILE TYR ASP GLY GLU GLY VAL THR
SEQRES 22 C 416 GLU SER LEU ARG THR LYS SER ASN MET ASP GLY MET ASP
SEQRES 23 C 416 LYS LEU VAL ASP THR LEU ASN MET ASP PHE THR GLY LEU
SEQRES 24 C 416 SER PHE LEU ASN LEU VAL ASP PHE ASP ALA LEU PHE GLY
SEQRES 25 C 416 HIS ARG ARG ASP PRO GLN GLY TYR GLY GLU ALA LEU GLN
SEQRES 26 C 416 GLU TYR ASP ALA ARG LEU PRO GLU VAL PHE ALA LYS LEU
SEQRES 27 C 416 LYS GLU ASP ASP LEU LEU LEU ILE THR ALA ASP HIS GLY
SEQRES 28 C 416 ASN ASP PRO ILE HIS PRO GLY THR ASP HIS THR ARG GLU
SEQRES 29 C 416 TYR VAL PRO LEU LEU ALA TYR SER PRO SER MET LYS GLU
SEQRES 30 C 416 GLY GLY GLN GLU LEU PRO LEU ARG GLN THR PHE ALA ASP
SEQRES 31 C 416 ILE GLY ALA THR VAL ALA GLU ASN PHE GLY VAL LYS MET
SEQRES 32 C 416 PRO GLU TYR GLY THR SER PHE LEU ASN GLU LEU LYS LYS
MODRES 4LR9 TPO A 85 THR PHOSPHOTHREONINE
MODRES 4LR9 TPO B 85 THR PHOSPHOTHREONINE
MODRES 4LR9 TPO C 85 THR PHOSPHOTHREONINE
HET TPO A 85 11
HET TPO B 85 11
HET TPO C 85 11
HET MN A 401 1
HET MN A 402 1
HET MN A 403 1
HET GOL A 404 6
HET 1X4 A 405 12
HET MN B 401 1
HET MN B 402 1
HET MN B 403 1
HET MN B 404 1
HET GOL B 405 6
HET MN C 401 1
HET MN C 402 1
HET MN C 403 1
HETNAM TPO PHOSPHOTHREONINE
HETNAM MN MANGANESE (II) ION
HETNAM GOL GLYCEROL
HETNAM 1X4 2,3-DIDEOXY-5-O-PHOSPHONO-ALPHA-D-RIBOFURANOSE
HETSYN TPO PHOSPHONOTHREONINE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
HETSYN 1X4 2,3-DIDEOXYRIBOSE-5-PHOSPHATE; 2,3-DIDEOXY-5-O-
HETSYN 2 1X4 PHOSPHONO-ALPHA-D-RIBOSE; 2,3-DIDEOXY-5-O-PHOSPHONO-D-
HETSYN 3 1X4 RIBOSE; 2,3-DIDEOXY-5-O-PHOSPHONO-RIBOSE
FORMUL 1 TPO 3(C4 H10 N O6 P)
FORMUL 4 MN 10(MN 2+)
FORMUL 7 GOL 2(C3 H8 O3)
FORMUL 8 1X4 C5 H11 O6 P
FORMUL 17 HOH *691(H2 O)
HELIX 1 1 ASP A 22 GLY A 27 5 6
HELIX 2 2 ASP A 32 MET A 41 1 10
HELIX 3 3 MET A 46 GLY A 53 1 8
HELIX 4 4 GLY A 53 ARG A 58 1 6
HELIX 5 5 ASP A 84 MET A 93 1 10
HELIX 6 6 PRO A 109 GLY A 121 1 13
HELIX 7 7 SER A 131 GLY A 147 1 17
HELIX 8 8 PRO A 169 THR A 184 1 16
HELIX 9 9 ASP A 186 MET A 190 5 5
HELIX 10 10 THR A 223 SER A 231 1 9
HELIX 11 11 LYS A 240 TYR A 245 1 6
HELIX 12 12 SER A 258 ASN A 271 1 14
HELIX 13 13 VAL A 283 LEU A 288 1 6
HELIX 14 14 ASP A 294 LEU A 316 1 23
HELIX 15 15 PHE A 366 GLY A 378 1 13
HELIX 16 16 PHE A 388 LEU A 392 5 5
HELIX 17 17 ASP B 22 GLY B 27 5 6
HELIX 18 18 ASP B 32 ASN B 42 1 11
HELIX 19 19 MET B 46 GLY B 53 1 8
HELIX 20 20 GLY B 53 ARG B 58 1 6
HELIX 21 21 ASP B 84 MET B 93 1 10
HELIX 22 22 PRO B 109 GLY B 121 1 13
HELIX 23 23 SER B 131 GLY B 147 1 17
HELIX 24 24 PRO B 169 THR B 184 1 16
HELIX 25 25 ASP B 186 MET B 190 5 5
HELIX 26 26 THR B 223 SER B 231 1 9
HELIX 27 27 LYS B 240 TYR B 245 1 6
HELIX 28 28 SER B 258 MET B 272 1 15
HELIX 29 29 VAL B 283 LEU B 288 1 6
HELIX 30 30 ASP B 294 ARG B 308 1 15
HELIX 31 31 ARG B 308 LEU B 316 1 9
HELIX 32 32 PHE B 366 GLY B 378 1 13
HELIX 33 33 PHE B 388 LEU B 392 5 5
HELIX 34 34 ASP C 22 GLY C 27 5 6
HELIX 35 35 ASP C 32 ASN C 42 1 11
HELIX 36 36 MET C 46 GLY C 53 1 8
HELIX 37 37 GLY C 53 ARG C 58 1 6
HELIX 38 38 ASP C 84 MET C 93 1 10
HELIX 39 39 PRO C 109 GLY C 121 1 13
HELIX 40 40 SER C 131 GLY C 147 1 17
HELIX 41 41 PRO C 169 THR C 184 1 16
HELIX 42 42 THR C 223 SER C 231 1 9
HELIX 43 43 LYS C 240 TYR C 245 1 6
HELIX 44 44 SER C 258 ASN C 271 1 14
HELIX 45 45 VAL C 283 LEU C 288 1 6
HELIX 46 46 ASP C 294 ALA C 307 1 14
HELIX 47 47 ARG C 308 LEU C 316 1 9
HELIX 48 48 PHE C 366 GLY C 378 1 13
SHEET 1 A 7 TYR A 72 MET A 76 0
SHEET 2 A 7 VAL A 344 TYR A 349 -1 O ALA A 348 N TYR A 72
SHEET 3 A 7 ASP A 320 THR A 325 -1 N LEU A 322 O TYR A 349
SHEET 4 A 7 ARG A 6 MET A 12 1 N VAL A 10 O LEU A 323
SHEET 5 A 7 GLY A 276 LEU A 282 1 O SER A 278 N LEU A 9
SHEET 6 A 7 ASP A 234 ILE A 238 1 N ILE A 238 O PHE A 279
SHEET 7 A 7 GLU A 252 LEU A 254 1 O LEU A 254 N ALA A 237
SHEET 1 B 5 ILE A 124 PRO A 129 0
SHEET 2 B 5 LEU A 149 THR A 153 1 O VAL A 151 N ASN A 127
SHEET 3 B 5 VAL A 158 HIS A 164 -1 O GLN A 160 N TYR A 152
SHEET 4 B 5 ARG A 193 GLU A 202 1 O ARG A 197 N ILE A 161
SHEET 5 B 5 ASN A 205 ARG A 208 -1 O THR A 207 N VAL A 200
SHEET 1 C 5 ILE A 124 PRO A 129 0
SHEET 2 C 5 LEU A 149 THR A 153 1 O VAL A 151 N ASN A 127
SHEET 3 C 5 VAL A 158 HIS A 164 -1 O GLN A 160 N TYR A 152
SHEET 4 C 5 ARG A 193 GLU A 202 1 O ARG A 197 N ILE A 161
SHEET 5 C 5 HIS A 213 ALA A 216 -1 O TYR A 215 N VAL A 194
SHEET 1 D 7 TYR B 72 MET B 76 0
SHEET 2 D 7 VAL B 344 TYR B 349 -1 O ALA B 348 N TYR B 72
SHEET 3 D 7 ASP B 320 THR B 325 -1 N LEU B 322 O TYR B 349
SHEET 4 D 7 ARG B 6 MET B 12 1 N PHE B 8 O LEU B 323
SHEET 5 D 7 GLY B 276 LEU B 282 1 O LEU B 280 N VAL B 11
SHEET 6 D 7 ASP B 234 ILE B 238 1 N ILE B 236 O PHE B 279
SHEET 7 D 7 GLU B 252 LEU B 254 1 O LEU B 254 N ALA B 237
SHEET 1 E 5 ILE B 124 PRO B 129 0
SHEET 2 E 5 LEU B 149 THR B 153 1 O LEU B 149 N ILE B 125
SHEET 3 E 5 VAL B 158 HIS B 164 -1 O GLN B 160 N TYR B 152
SHEET 4 E 5 ARG B 193 GLU B 202 1 O ARG B 197 N ILE B 161
SHEET 5 E 5 ASN B 205 ARG B 208 -1 O ASN B 205 N GLU B 202
SHEET 1 F 5 ILE B 124 PRO B 129 0
SHEET 2 F 5 LEU B 149 THR B 153 1 O LEU B 149 N ILE B 125
SHEET 3 F 5 VAL B 158 HIS B 164 -1 O GLN B 160 N TYR B 152
SHEET 4 F 5 ARG B 193 GLU B 202 1 O ARG B 197 N ILE B 161
SHEET 5 F 5 ASP B 214 ALA B 216 -1 O TYR B 215 N VAL B 194
SHEET 1 G 7 TYR C 72 MET C 76 0
SHEET 2 G 7 VAL C 344 TYR C 349 -1 O VAL C 344 N MET C 76
SHEET 3 G 7 ASP C 320 THR C 325 -1 N LEU C 322 O TYR C 349
SHEET 4 G 7 ARG C 6 MET C 12 1 N PHE C 8 O LEU C 321
SHEET 5 G 7 GLY C 276 LEU C 282 1 O LEU C 280 N LEU C 9
SHEET 6 G 7 ASP C 234 ILE C 238 1 N ILE C 236 O PHE C 279
SHEET 7 G 7 GLU C 252 LEU C 254 1 O LEU C 254 N ALA C 237
SHEET 1 H 5 ILE C 124 PRO C 129 0
SHEET 2 H 5 LEU C 149 THR C 153 1 O LEU C 149 N ILE C 125
SHEET 3 H 5 VAL C 158 HIS C 164 -1 O GLN C 160 N TYR C 152
SHEET 4 H 5 ARG C 193 GLU C 202 1 O ARG C 197 N ILE C 161
SHEET 5 H 5 ASN C 205 ARG C 208 -1 O THR C 207 N VAL C 200
SHEET 1 I 5 ILE C 124 PRO C 129 0
SHEET 2 I 5 LEU C 149 THR C 153 1 O LEU C 149 N ILE C 125
SHEET 3 I 5 VAL C 158 HIS C 164 -1 O GLN C 160 N TYR C 152
SHEET 4 I 5 ARG C 193 GLU C 202 1 O ARG C 197 N ILE C 161
SHEET 5 I 5 ASP C 214 ALA C 216 -1 O TYR C 215 N VAL C 194
LINK C ASP A 84 N TPO A 85 1555 1555 1.34
LINK C TPO A 85 N MET A 86 1555 1555 1.33
LINK C ASP B 84 N TPO B 85 1555 1555 1.33
LINK C TPO B 85 N MET B 86 1555 1555 1.33
LINK C ASP C 84 N TPO C 85 1555 1555 1.33
LINK C TPO C 85 N MET C 86 1555 1555 1.33
LINK OD1 ASP A 13 MN MN A 402 1555 1555 2.07
LINK OD2 ASP A 13 MN MN A 402 1555 1555 2.63
LINK O GLY A 27 MN MN A 403 1555 1555 2.75
LINK OD1 ASP A 28 MN MN A 403 1555 1555 2.34
LINK O1P TPO A 85 MN MN A 401 1555 1555 1.77
LINK OG1 TPO A 85 MN MN A 402 1555 1555 2.21
LINK OD2 ASP A 156 MN MN A 401 1555 1555 2.21
LINK OD1 ASP A 156 MN MN A 401 1555 1555 2.80
LINK OD1 ASP A 286 MN MN A 401 1555 1555 2.12
LINK OD2 ASP A 286 MN MN A 401 1555 1555 2.73
LINK NE2 HIS A 291 MN MN A 401 1555 1555 2.10
LINK OD2 ASP A 327 MN MN A 402 1555 1555 2.06
LINK NE2 HIS A 328 MN MN A 402 1555 1555 2.15
LINK NE2 HIS A 334 MN MN A 403 1555 1555 2.29
LINK NE2 HIS A 339 MN MN A 401 1555 1555 2.09
LINK OD1 ASP B 13 MN MN B 402 1555 1555 2.08
LINK OD2 ASP B 13 MN MN B 402 1555 1555 2.59
LINK NE2 HIS B 36 MN MN B 404 1555 1555 2.61
LINK O1P TPO B 85 MN MN B 401 1555 1555 1.81
LINK OG1 TPO B 85 MN MN B 402 1555 1555 2.11
LINK OD2 ASP B 156 MN MN B 401 1555 1555 2.20
LINK OD1 ASP B 286 MN MN B 401 1555 1555 2.11
LINK NE2 HIS B 291 MN MN B 401 1555 1555 2.12
LINK OD2 ASP B 327 MN MN B 402 1555 1555 2.12
LINK NE2 HIS B 328 MN MN B 402 1555 1555 2.12
LINK NE2 HIS B 339 MN MN B 401 1555 1555 2.07
LINK MN MN B 404 O HOH B 720 1555 1555 2.51
LINK OD1 ASP C 13 MN MN C 402 1555 1555 1.95
LINK OD2 ASP C 13 MN MN C 402 1555 1555 2.67
LINK O GLY C 27 MN MN C 403 1555 1555 2.45
LINK OD1 ASP C 28 MN MN C 403 1555 1555 2.20
LINK O3P TPO C 85 MN MN C 401 1555 1555 1.80
LINK OG1 TPO C 85 MN MN C 402 1555 1555 2.35
LINK OD2 ASP C 156 MN MN C 401 1555 1555 2.37
LINK OD1 ASP C 286 MN MN C 401 1555 1555 2.04
LINK NE2 HIS C 291 MN MN C 401 1555 1555 2.05
LINK OD2 ASP C 327 MN MN C 402 1555 1555 2.10
LINK NE2 HIS C 328 MN MN C 402 1555 1555 2.13
LINK NE2 HIS C 334 MN MN C 403 1555 1555 2.22
LINK NE2 HIS C 339 MN MN C 401 1555 1555 2.02
LINK MN MN C 403 O HOH C 572 1555 1555 2.32
LINK MN MN C 403 O HOH C 632 1555 1555 2.15
LINK MN MN C 403 O HOH C 659 1555 1555 2.46
CRYST1 92.329 76.615 107.236 90.00 108.96 90.00 P 1 21 1 6
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 0.010831 0.000000 0.003721 0.00000
SCALE2 0.000000 0.013052 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009860 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
