HEADER HYDROLASE 10-AUG-17 5OPO
TITLE CRYSTAL STRUCTURE OF R238G CN-II MUTANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOSOLIC PURINE 5'-NUCLEOTIDASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CYTOSOLIC 5'-NUCLEOTIDASE II;
COMPND 5 EC: 3.1.3.5;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: NT5C2, NT5B, NT5CP, PNT5;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: RIL;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLAMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28
KEYWDS NUCLEOTIDASE, RELAPSED LEUKEMIA, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.HNIZDA,P.PACHL,P.REZACOVA
REVDAT 4 17-JAN-24 5OPO 1 REMARK
REVDAT 3 16-OCT-19 5OPO 1 REMARK
REVDAT 2 20-JUN-18 5OPO 1 JRNL
REVDAT 1 13-JUN-18 5OPO 0
JRNL AUTH A.HNIZDA,M.FABRY,T.MORIYAMA,P.PACHL,M.KUGLER,V.BRINSA,
JRNL AUTH 2 D.B.ASCHER,W.L.CARROLL,P.NOVAK,M.ZALIOVA,J.TRKA,P.REZACOVA,
JRNL AUTH 3 J.J.YANG,V.VEVERKA
JRNL TITL RELAPSED ACUTE LYMPHOBLASTIC LEUKEMIA-SPECIFIC MUTATIONS IN
JRNL TITL 2 NT5C2 CLUSTER INTO HOTSPOTS DRIVING INTERSUBUNIT
JRNL TITL 3 STIMULATION.
JRNL REF LEUKEMIA V. 32 1393 2018
JRNL REFN ESSN 1476-5551
JRNL PMID 29535428
JRNL DOI 10.1038/S41375-018-0073-5
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0131
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.43
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 49530
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) : 0.172
REMARK 3 R VALUE (WORKING SET) : 0.171
REMARK 3 FREE R VALUE : 0.203
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2100
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3552
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.36
REMARK 3 BIN R VALUE (WORKING SET) : 0.2880
REMARK 3 BIN FREE R VALUE SET COUNT : 150
REMARK 3 BIN FREE R VALUE : 0.3160
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3858
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 43
REMARK 3 SOLVENT ATOMS : 460
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 30.67
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.03
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.01000
REMARK 3 B33 (A**2) : -0.01000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.130
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.123
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.961
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.946
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4082 ; 0.012 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 3849 ; 0.000 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5518 ; 1.512 ; 1.966
REMARK 3 BOND ANGLES OTHERS (DEGREES): 8883 ; 3.583 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 500 ; 6.326 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 195 ;32.268 ;23.128
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 713 ;13.022 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 27 ;16.546 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 591 ; 0.091 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4547 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 994 ; 0.011 ; 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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 : 13
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 3 A 20
REMARK 3 ORIGIN FOR THE GROUP (A): -5.2680 -38.2150 -30.9600
REMARK 3 T TENSOR
REMARK 3 T11: 0.3857 T22: 0.2601
REMARK 3 T33: 0.2625 T12: -0.0022
REMARK 3 T13: -0.0285 T23: -0.0801
REMARK 3 L TENSOR
REMARK 3 L11: 8.3193 L22: 6.2575
REMARK 3 L33: 0.2529 L12: 6.2999
REMARK 3 L13: -0.5170 L23: -0.7852
REMARK 3 S TENSOR
REMARK 3 S11: -0.0008 S12: 0.2459 S13: -0.4944
REMARK 3 S21: -0.1653 S22: 0.0962 S23: -0.0539
REMARK 3 S31: 0.2387 S32: 0.0274 S33: -0.0954
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 21 A 34
REMARK 3 ORIGIN FOR THE GROUP (A): -11.1550 -47.1990 -22.0520
REMARK 3 T TENSOR
REMARK 3 T11: 0.4770 T22: 0.3441
REMARK 3 T33: 0.7537 T12: 0.0467
REMARK 3 T13: 0.1026 T23: -0.0303
REMARK 3 L TENSOR
REMARK 3 L11: 10.7559 L22: 12.2520
REMARK 3 L33: 8.8979 L12: 11.3175
REMARK 3 L13: 5.5362 L23: 4.4383
REMARK 3 S TENSOR
REMARK 3 S11: 0.2285 S12: -0.1746 S13: -0.9798
REMARK 3 S21: 0.0185 S22: -0.1941 S23: -1.0238
REMARK 3 S31: 1.2428 S32: 0.0141 S33: -0.0343
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 35 A 127
REMARK 3 ORIGIN FOR THE GROUP (A): 6.5650 -22.4570 -20.7310
REMARK 3 T TENSOR
REMARK 3 T11: 0.0590 T22: 0.0235
REMARK 3 T33: 0.0139 T12: 0.0088
REMARK 3 T13: 0.0110 T23: -0.0079
REMARK 3 L TENSOR
REMARK 3 L11: 1.6698 L22: 0.4717
REMARK 3 L33: 0.9047 L12: 0.3768
REMARK 3 L13: 0.1605 L23: -0.0350
REMARK 3 S TENSOR
REMARK 3 S11: -0.0329 S12: 0.1064 S13: 0.0336
REMARK 3 S21: -0.0735 S22: 0.0275 S23: -0.0083
REMARK 3 S31: 0.0466 S32: 0.0471 S33: 0.0054
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 128 A 145
REMARK 3 ORIGIN FOR THE GROUP (A): 21.4700 -22.9210 -4.8820
REMARK 3 T TENSOR
REMARK 3 T11: 0.1648 T22: 0.1043
REMARK 3 T33: 0.0616 T12: 0.0154
REMARK 3 T13: -0.0012 T23: 0.0037
REMARK 3 L TENSOR
REMARK 3 L11: 5.2786 L22: 4.8092
REMARK 3 L33: 9.1392 L12: 3.3154
REMARK 3 L13: -1.7648 L23: -0.7996
REMARK 3 S TENSOR
REMARK 3 S11: -0.1236 S12: -0.0266 S13: -0.4181
REMARK 3 S21: 0.0658 S22: -0.0849 S23: -0.4704
REMARK 3 S31: 0.5454 S32: 0.7051 S33: 0.2086
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 146 A 186
REMARK 3 ORIGIN FOR THE GROUP (A): 17.7960 -14.6330 -19.4010
REMARK 3 T TENSOR
REMARK 3 T11: 0.0539 T22: 0.0318
REMARK 3 T33: 0.0453 T12: 0.0243
REMARK 3 T13: 0.0114 T23: 0.0250
REMARK 3 L TENSOR
REMARK 3 L11: 3.4576 L22: 2.6282
REMARK 3 L33: 2.0927 L12: 1.2766
REMARK 3 L13: 0.6788 L23: 0.4164
REMARK 3 S TENSOR
REMARK 3 S11: -0.1063 S12: 0.1713 S13: 0.2523
REMARK 3 S21: 0.0104 S22: 0.0939 S23: -0.0578
REMARK 3 S31: -0.0762 S32: 0.0341 S33: 0.0124
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 187 A 212
REMARK 3 ORIGIN FOR THE GROUP (A): 12.9190 -7.2110 -21.9060
REMARK 3 T TENSOR
REMARK 3 T11: 0.1116 T22: 0.0974
REMARK 3 T33: 0.1183 T12: 0.0497
REMARK 3 T13: 0.0323 T23: 0.0279
REMARK 3 L TENSOR
REMARK 3 L11: 6.5755 L22: 2.5213
REMARK 3 L33: 2.9653 L12: 0.7478
REMARK 3 L13: 3.7935 L23: 0.2102
REMARK 3 S TENSOR
REMARK 3 S11: 0.0103 S12: -0.1617 S13: 0.3476
REMARK 3 S21: -0.0350 S22: -0.0035 S23: 0.1626
REMARK 3 S31: -0.0475 S32: -0.2844 S33: -0.0069
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 213 A 248
REMARK 3 ORIGIN FOR THE GROUP (A): -11.7000 -25.0090 -30.1910
REMARK 3 T TENSOR
REMARK 3 T11: 0.1267 T22: 0.1078
REMARK 3 T33: 0.0392 T12: -0.0080
REMARK 3 T13: -0.0537 T23: 0.0031
REMARK 3 L TENSOR
REMARK 3 L11: 4.1681 L22: 1.8907
REMARK 3 L33: 2.3540 L12: 1.0193
REMARK 3 L13: -0.8156 L23: 0.2074
REMARK 3 S TENSOR
REMARK 3 S11: -0.1539 S12: 0.4715 S13: -0.0046
REMARK 3 S21: -0.1590 S22: 0.1416 S23: 0.0026
REMARK 3 S31: 0.2267 S32: -0.1514 S33: 0.0122
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 249 A 290
REMARK 3 ORIGIN FOR THE GROUP (A): -17.1000 -21.9550 -31.1540
REMARK 3 T TENSOR
REMARK 3 T11: 0.0663 T22: 0.0667
REMARK 3 T33: 0.0279 T12: -0.0122
REMARK 3 T13: -0.0378 T23: -0.0055
REMARK 3 L TENSOR
REMARK 3 L11: 2.2718 L22: 1.3401
REMARK 3 L33: 2.0698 L12: 0.9729
REMARK 3 L13: 0.6083 L23: 0.9937
REMARK 3 S TENSOR
REMARK 3 S11: -0.0486 S12: 0.1490 S13: -0.0095
REMARK 3 S21: -0.1212 S22: 0.0437 S23: 0.0112
REMARK 3 S31: -0.0425 S32: 0.0125 S33: 0.0048
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 291 A 371
REMARK 3 ORIGIN FOR THE GROUP (A): -16.0550 -15.5930 -15.8360
REMARK 3 T TENSOR
REMARK 3 T11: 0.1023 T22: 0.1008
REMARK 3 T33: 0.0691 T12: -0.0233
REMARK 3 T13: -0.0176 T23: -0.0264
REMARK 3 L TENSOR
REMARK 3 L11: 0.9061 L22: 2.8575
REMARK 3 L33: 1.6841 L12: -0.8203
REMARK 3 L13: 0.7429 L23: -1.0420
REMARK 3 S TENSOR
REMARK 3 S11: -0.0954 S12: -0.0602 S13: 0.1374
REMARK 3 S21: 0.0094 S22: 0.0589 S23: 0.1706
REMARK 3 S31: -0.2440 S32: -0.1218 S33: 0.0364
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 372 A 399
REMARK 3 ORIGIN FOR THE GROUP (A): 10.1410 -42.8250 -14.4360
REMARK 3 T TENSOR
REMARK 3 T11: 0.3238 T22: 0.1660
REMARK 3 T33: 0.4127 T12: 0.0592
REMARK 3 T13: 0.1018 T23: 0.0266
REMARK 3 L TENSOR
REMARK 3 L11: 3.8547 L22: 3.6581
REMARK 3 L33: 5.3004 L12: -2.8371
REMARK 3 L13: 3.6186 L23: -1.8879
REMARK 3 S TENSOR
REMARK 3 S11: 0.2168 S12: 0.1520 S13: -0.4258
REMARK 3 S21: 0.0292 S22: -0.1087 S23: -0.1958
REMARK 3 S31: 0.8632 S32: 0.3209 S33: -0.1080
REMARK 3
REMARK 3 TLS GROUP : 11
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 400 A 419
REMARK 3 ORIGIN FOR THE GROUP (A): 26.9660 -47.1490 -0.1970
REMARK 3 T TENSOR
REMARK 3 T11: 0.2806 T22: 0.3721
REMARK 3 T33: 0.2990 T12: 0.0616
REMARK 3 T13: -0.0924 T23: 0.0405
REMARK 3 L TENSOR
REMARK 3 L11: 29.7900 L22: 1.0264
REMARK 3 L33: 20.9235 L12: 3.1686
REMARK 3 L13: -23.9758 L23: -1.4941
REMARK 3 S TENSOR
REMARK 3 S11: -0.3757 S12: 0.7891 S13: 0.3481
REMARK 3 S21: 0.1130 S22: 0.4261 S23: 0.1735
REMARK 3 S31: 0.5148 S32: -0.1469 S33: -0.0504
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 420 A 477
REMARK 3 ORIGIN FOR THE GROUP (A): 4.1110 -35.9310 -13.5250
REMARK 3 T TENSOR
REMARK 3 T11: 0.1328 T22: 0.0263
REMARK 3 T33: 0.0453 T12: 0.0281
REMARK 3 T13: 0.0101 T23: 0.0060
REMARK 3 L TENSOR
REMARK 3 L11: 2.6368 L22: 1.7106
REMARK 3 L33: 2.3117 L12: 0.8354
REMARK 3 L13: -0.7475 L23: -0.2409
REMARK 3 S TENSOR
REMARK 3 S11: -0.0156 S12: -0.1612 S13: -0.2761
REMARK 3 S21: -0.0982 S22: -0.0169 S23: -0.1915
REMARK 3 S31: 0.2580 S32: 0.1581 S33: 0.0324
REMARK 3
REMARK 3 TLS GROUP : 13
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 478 A 488
REMARK 3 ORIGIN FOR THE GROUP (A): -5.2180 -40.9630 4.7810
REMARK 3 T TENSOR
REMARK 3 T11: 0.1863 T22: 0.1397
REMARK 3 T33: 0.1712 T12: 0.0131
REMARK 3 T13: -0.0281 T23: -0.0156
REMARK 3 L TENSOR
REMARK 3 L11: 2.4281 L22: 0.7273
REMARK 3 L33: 11.3675 L12: 1.2916
REMARK 3 L13: 4.2156 L23: 1.8661
REMARK 3 S TENSOR
REMARK 3 S11: 0.1079 S12: -0.0094 S13: -0.0717
REMARK 3 S21: 0.0313 S22: 0.0192 S23: -0.0258
REMARK 3 S31: 0.2046 S32: -0.1527 S33: -0.1271
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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 U VALUES : WITH TLS ADDED
REMARK 4
REMARK 4 5OPO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 10-AUG-17.
REMARK 100 THE DEPOSITION ID IS D_1200006173.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-MAR-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : BESSY
REMARK 200 BEAMLINE : 14.3
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.894
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX-225
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 54032
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.969
REMARK 200 RESOLUTION RANGE LOW (A) : 48.430
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 4.600
REMARK 200 R MERGE (I) : 0.09900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.97
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.09
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.3
REMARK 200 DATA REDUNDANCY IN SHELL : 4.58
REMARK 200 R MERGE FOR SHELL (I) : 0.75100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.980
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 5K7Y
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.61
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.38
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MOPS/HEPES-NA PH 7.5; 0.03 M OF
REMARK 280 EACH DIVALENT CATION ; 10% W/V PEG 4000, 20% V/V GLYCEROL A7
REMARK 280 MORPHEUS CONDITION, VAPOR DIFFUSION, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 45.80600
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 63.43100
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 65.28600
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 45.80600
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 63.43100
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 65.28600
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 45.80600
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 63.43100
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 65.28600
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 45.80600
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 63.43100
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 65.28600
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 20170 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 76780 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -73.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 3 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT1 4 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 4 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 LYS A 404
REMARK 465 HIS A 405
REMARK 465 LEU A 406
REMARK 465 ASP A 407
REMARK 465 SER A 408
REMARK 465 SER A 409
REMARK 465 SER A 410
REMARK 465 ASN A 411
REMARK 465 GLU A 412
REMARK 465 ARG A 413
REMARK 465 PRO A 414
REMARK 465 ASP A 415
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH A 720 O HOH A 832 1.59
REMARK 500 O HOH A 963 O HOH A 985 1.73
REMARK 500 O HOH A 833 O HOH A 902 1.75
REMARK 500 O HOH A 677 O HOH A 985 1.81
REMARK 500 O HOH A 957 O HOH A 1018 1.97
REMARK 500 O HOH A 609 O HOH A 737 2.08
REMARK 500 O HOH A 638 O HOH A 978 2.10
REMARK 500 O HOH A 940 O HOH A 982 2.13
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 ARG A 202 NE - CZ - NH1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 ARG A 202 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 ASP A 252 CB - CG - OD1 ANGL. DEV. = 6.4 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 MET A 53 -74.19 -93.68
REMARK 500 TYR A 55 16.95 59.44
REMARK 500 THR A 56 -77.33 -121.47
REMARK 500 LYS A 140 52.67 39.59
REMARK 500 ILE A 357 -60.00 -95.61
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 MG A 508 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 52 OD2
REMARK 620 2 ASP A 54 O 90.3
REMARK 620 3 ASP A 351 OD1 88.6 86.8
REMARK 620 4 HOH A 613 O 80.9 170.0 88.4
REMARK 620 5 HOH A 711 O 176.0 92.4 94.5 96.7
REMARK 620 6 HOH A 908 O 93.9 97.6 174.9 87.6 82.8
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 508
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5OPL RELATED DB: PDB
REMARK 900 RELATED ID: 5OPK RELATED DB: PDB
REMARK 900 RELATED ID: 5OPM RELATED DB: PDB
REMARK 900 RELATED ID: 5OPN RELATED DB: PDB
DBREF 5OPO A 3 488 UNP P49902 5NTC_HUMAN 3 488
SEQADV 5OPO GLY A 238 UNP P49902 ARG 238 ENGINEERED MUTATION
SEQRES 1 A 486 THR SER TRP SER ASP ARG LEU GLN ASN ALA ALA ASP MET
SEQRES 2 A 486 PRO ALA ASN MET ASP LYS HIS ALA LEU LYS LYS TYR ARG
SEQRES 3 A 486 ARG GLU ALA TYR HIS ARG VAL PHE VAL ASN ARG SER LEU
SEQRES 4 A 486 ALA MET GLU LYS ILE LYS CYS PHE GLY PHE ASP MET ASP
SEQRES 5 A 486 TYR THR LEU ALA VAL TYR LYS SER PRO GLU TYR GLU SER
SEQRES 6 A 486 LEU GLY PHE GLU LEU THR VAL GLU ARG LEU VAL SER ILE
SEQRES 7 A 486 GLY TYR PRO GLN GLU LEU LEU SER PHE ALA TYR ASP SER
SEQRES 8 A 486 THR PHE PRO THR ARG GLY LEU VAL PHE ASP THR LEU TYR
SEQRES 9 A 486 GLY ASN LEU LEU LYS VAL ASP ALA TYR GLY ASN LEU LEU
SEQRES 10 A 486 VAL CYS ALA HIS GLY PHE ASN PHE ILE ARG GLY PRO GLU
SEQRES 11 A 486 THR ARG GLU GLN TYR PRO ASN LYS PHE ILE GLN ARG ASP
SEQRES 12 A 486 ASP THR GLU ARG PHE TYR ILE LEU ASN THR LEU PHE ASN
SEQRES 13 A 486 LEU PRO GLU THR TYR LEU LEU ALA CYS LEU VAL ASP PHE
SEQRES 14 A 486 PHE THR ASN CYS PRO ARG TYR THR SER CYS GLU THR GLY
SEQRES 15 A 486 PHE LYS ASP GLY ASP LEU PHE MET SER TYR ARG SER MET
SEQRES 16 A 486 PHE GLN ASP VAL ARG ASP ALA VAL ASP TRP VAL HIS TYR
SEQRES 17 A 486 LYS GLY SER LEU LYS GLU LYS THR VAL GLU ASN LEU GLU
SEQRES 18 A 486 LYS TYR VAL VAL LYS ASP GLY LYS LEU PRO LEU LEU LEU
SEQRES 19 A 486 SER GLY MET LYS GLU VAL GLY LYS VAL PHE LEU ALA THR
SEQRES 20 A 486 ASN SER ASP TYR LYS TYR THR ASP LYS ILE MET THR TYR
SEQRES 21 A 486 LEU PHE ASP PHE PRO HIS GLY PRO LYS PRO GLY SER SER
SEQRES 22 A 486 HIS ARG PRO TRP GLN SER TYR PHE ASP LEU ILE LEU VAL
SEQRES 23 A 486 ASP ALA ARG LYS PRO LEU PHE PHE GLY GLU GLY THR VAL
SEQRES 24 A 486 LEU ARG GLN VAL ASP THR LYS THR GLY LYS LEU LYS ILE
SEQRES 25 A 486 GLY THR TYR THR GLY PRO LEU GLN HIS GLY ILE VAL TYR
SEQRES 26 A 486 SER GLY GLY SER SER ASP THR ILE CYS ASP LEU LEU GLY
SEQRES 27 A 486 ALA LYS GLY LYS ASP ILE LEU TYR ILE GLY ASP HIS ILE
SEQRES 28 A 486 PHE GLY ASP ILE LEU LYS SER LYS LYS ARG GLN GLY TRP
SEQRES 29 A 486 ARG THR PHE LEU VAL ILE PRO GLU LEU ALA GLN GLU LEU
SEQRES 30 A 486 HIS VAL TRP THR ASP LYS SER SER LEU PHE GLU GLU LEU
SEQRES 31 A 486 GLN SER LEU ASP ILE PHE LEU ALA GLU LEU TYR LYS HIS
SEQRES 32 A 486 LEU ASP SER SER SER ASN GLU ARG PRO ASP ILE SER SER
SEQRES 33 A 486 ILE GLN ARG ARG ILE LYS LYS VAL THR HIS ASP MET ASP
SEQRES 34 A 486 MET CYS TYR GLY MET MET GLY SER LEU PHE ARG SER GLY
SEQRES 35 A 486 SER ARG GLN THR LEU PHE ALA SER GLN VAL MET ARG TYR
SEQRES 36 A 486 ALA ASP LEU TYR ALA ALA SER PHE ILE ASN LEU LEU TYR
SEQRES 37 A 486 TYR PRO PHE SER TYR LEU PHE ARG ALA ALA HIS VAL LEU
SEQRES 38 A 486 MET PRO HIS GLU SER
HET GOL A 501 6
HET GOL A 502 6
HET GOL A 503 6
HET GOL A 504 6
HET GOL A 505 6
HET GOL A 506 6
HET GOL A 507 6
HET MG A 508 1
HETNAM GOL GLYCEROL
HETNAM MG MAGNESIUM ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 GOL 7(C3 H8 O3)
FORMUL 9 MG MG 2+
FORMUL 10 HOH *460(H2 O)
HELIX 1 AA1 SER A 4 MET A 15 1 12
HELIX 2 AA2 ASP A 20 GLU A 30 1 11
HELIX 3 AA3 ALA A 31 ARG A 34 5 4
HELIX 4 AA4 GLU A 44 ILE A 46 5 3
HELIX 5 AA5 PRO A 63 ILE A 80 1 18
HELIX 6 AA6 PRO A 83 PHE A 89 5 7
HELIX 7 AA7 ARG A 129 ARG A 134 1 6
HELIX 8 AA8 THR A 155 PHE A 157 5 3
HELIX 9 AA9 ASN A 158 CYS A 175 1 18
HELIX 10 AB1 TYR A 194 LYS A 211 1 18
HELIX 11 AB2 SER A 213 GLU A 220 1 8
HELIX 12 AB3 ASN A 221 VAL A 226 1 6
HELIX 13 AB4 GLY A 230 GLY A 243 1 14
HELIX 14 AB5 ASP A 252 PHE A 264 1 13
HELIX 15 AB6 PRO A 278 PHE A 283 5 6
HELIX 16 AB7 PRO A 293 GLY A 297 5 5
HELIX 17 AB8 SER A 331 GLY A 340 1 10
HELIX 18 AB9 LYS A 342 LYS A 344 5 3
HELIX 19 AC1 ASP A 356 GLY A 365 1 10
HELIX 20 AC2 GLU A 374 LYS A 385 1 12
HELIX 21 AC3 LYS A 385 LEU A 402 1 18
HELIX 22 AC4 GLN A 420 CYS A 433 1 14
HELIX 23 AC5 THR A 448 ALA A 458 1 11
HELIX 24 AC6 SER A 464 TYR A 471 5 8
HELIX 25 AC7 MET A 484 SER A 488 5 5
SHEET 1 AA110 PHE A 36 VAL A 37 0
SHEET 2 AA110 LEU A 460 ALA A 462 -1 O TYR A 461 N PHE A 36
SHEET 3 AA110 ARG A 367 VAL A 371 1 N LEU A 370 O LEU A 460
SHEET 4 AA110 ILE A 346 GLY A 350 1 N TYR A 348 O ARG A 367
SHEET 5 AA110 CYS A 48 PHE A 51 1 N GLY A 50 O LEU A 347
SHEET 6 AA110 LYS A 244 ALA A 248 1 O ALA A 248 N PHE A 51
SHEET 7 AA110 LEU A 285 VAL A 288 1 O LEU A 285 N LEU A 247
SHEET 8 AA110 TYR A 327 GLY A 329 1 O TYR A 327 N ILE A 286
SHEET 9 AA110 LEU A 302 ASP A 306 -1 N ARG A 303 O SER A 328
SHEET 10 AA110 LYS A 311 LEU A 312 -1 O LYS A 311 N ASP A 306
SHEET 1 AA2 2 LEU A 41 ALA A 42 0
SHEET 2 AA2 2 LEU A 476 PHE A 477 -1 O PHE A 477 N LEU A 41
SHEET 1 AA3 5 ASN A 126 PHE A 127 0
SHEET 2 AA3 5 LEU A 118 HIS A 123 -1 N HIS A 123 O ASN A 126
SHEET 3 AA3 5 ASN A 108 VAL A 112 -1 N LYS A 111 O LEU A 119
SHEET 4 AA3 5 LEU A 100 ASP A 103 -1 N ASP A 103 O ASN A 108
SHEET 5 AA3 5 PHE A 150 LEU A 153 -1 O LEU A 153 N LEU A 100
SHEET 1 AA4 3 THR A 179 CYS A 181 0
SHEET 2 AA4 3 GLY A 184 ASP A 187 -1 O GLY A 184 N CYS A 181
SHEET 3 AA4 3 LEU A 190 SER A 193 -1 O MET A 192 N PHE A 185
SHEET 1 AA5 2 ARG A 442 SER A 443 0
SHEET 2 AA5 2 ARG A 446 GLN A 447 -1 O ARG A 446 N SER A 443
LINK OD2 ASP A 52 MG MG A 508 1555 1555 2.05
LINK O ASP A 54 MG MG A 508 1555 1555 2.13
LINK OD1 ASP A 351 MG MG A 508 1555 1555 2.09
LINK MG MG A 508 O HOH A 613 1555 1555 2.13
LINK MG MG A 508 O HOH A 711 1555 1555 2.25
LINK MG MG A 508 O HOH A 908 1555 1555 2.01
CISPEP 1 SER A 62 PRO A 63 0 4.20
CISPEP 2 LYS A 292 PRO A 293 0 9.34
SITE 1 AC1 7 GLU A 374 GLU A 378 TYR A 434 GLY A 438
SITE 2 AC1 7 HOH A 623 HOH A 627 HOH A 712
SITE 1 AC2 7 ARG A 34 TYR A 471 TYR A 475 PHE A 477
SITE 2 AC2 7 ARG A 478 HOH A 674 HOH A 710
SITE 1 AC3 8 ASP A 252 TYR A 253 VAL A 288 ASP A 289
SITE 2 AC3 8 GLY A 310 LEU A 312 HOH A 865 HOH A 880
SITE 1 AC4 8 PHE A 283 ASP A 284 ILE A 286 GLN A 322
SITE 2 AC4 8 HIS A 323 GLY A 324 ILE A 325 HOH A 642
SITE 1 AC5 5 HIS A 276 MET A 432 HOH A 654 HOH A 661
SITE 2 AC5 5 HOH A 726
SITE 1 AC6 5 ARG A 144 LYS A 362 GLN A 453 ARG A 456
SITE 2 AC6 5 TYR A 457
SITE 1 AC7 9 ALA A 114 TYR A 115 ARG A 144 LYS A 362
SITE 2 AC7 9 SER A 452 ARG A 456 TYR A 457 HOH A 615
SITE 3 AC7 9 HOH A 701
SITE 1 AC8 6 ASP A 52 ASP A 54 ASP A 351 HOH A 613
SITE 2 AC8 6 HOH A 711 HOH A 908
CRYST1 91.612 126.862 130.572 90.00 90.00 90.00 I 2 2 2 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.010916 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007883 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007659 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
