HEADER TRANSFERASE 30-JAN-12 4DI6
TITLE CRYSTAL STRUCTURE OF NUCLEOSIDE-DIPHOSPHATE KINASE FROM BORRELIA
TITLE 2 BURGDORFERI
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NUCLEOSIDE DIPHOSPHATE KINASE;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 FRAGMENT: NUCLEOSIDE-DIPHOSPHATE KINASE;
COMPND 5 SYNONYM: NDK, NDP KINASE, NUCLEOSIDE-2-P KINASE;
COMPND 6 EC: 2.7.4.6;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BORRELIA BURGDORFERI;
SOURCE 3 ORGANISM_COMMON: LYME DISEASE SPIROCHETE;
SOURCE 4 ORGANISM_TAXID: 139;
SOURCE 5 GENE: NDK, BB_0463;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: AVA0421
KEYWDS SSGCID, NUCLEOSIDE DIPHOSPHATE KINASE, KINASE, STRUCTURAL GENOMICS,
KEYWDS 2 SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE, NIAID,
KEYWDS 3 NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE (SSGCID)
REVDAT 2 13-JUN-18 4DI6 1 JRNL
REVDAT 1 08-FEB-12 4DI6 0
JRNL AUTH M.DUMAIS,D.R.DAVIES,T.LIN,B.L.STAKER,P.J.MYLER,
JRNL AUTH 2 W.C.VAN VOORHIS
JRNL TITL STRUCTURE AND ANALYSIS OF NUCLEOSIDE DIPHOSPHATE KINASE FROM
JRNL TITL 2 BORRELIA BURGDORFERI PREPARED IN A TRANSITION-STATE COMPLEX
JRNL TITL 3 WITH ADP AND VANADATE MOIETIES.
JRNL REF ACTA CRYSTALLOGR F STRUCT V. 74 373 2018
JRNL REF 2 BIOL COMMUN
JRNL REFN ESSN 2053-230X
JRNL PMID 29870023
JRNL DOI 10.1107/S2053230X18007392
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
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) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.22
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 50334
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) : 0.177
REMARK 3 R VALUE (WORKING SET) : 0.175
REMARK 3 FREE R VALUE : 0.228
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2557
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) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.46
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3513
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.20
REMARK 3 BIN R VALUE (WORKING SET) : 0.2130
REMARK 3 BIN FREE R VALUE SET COUNT : 197
REMARK 3 BIN FREE R VALUE : 0.2930
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8048
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 431
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 32.59
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.80
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.39000
REMARK 3 B22 (A**2) : -0.39000
REMARK 3 B33 (A**2) : 0.59000
REMARK 3 B12 (A**2) : -0.20000
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): 0.339
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.237
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.155
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.634
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.943
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.902
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8293 ; 0.009 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 11225 ; 1.259 ; 1.950
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1023 ; 5.801 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 384 ;35.531 ;23.594
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1452 ;14.016 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 52 ;14.922 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1238 ; 0.092 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6244 ; 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): 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 : 36
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 29
REMARK 3 ORIGIN FOR THE GROUP (A): 49.4600 6.7938 108.6116
REMARK 3 T TENSOR
REMARK 3 T11: 0.1333 T22: 0.1449
REMARK 3 T33: 0.1514 T12: -0.0327
REMARK 3 T13: 0.0227 T23: -0.0276
REMARK 3 L TENSOR
REMARK 3 L11: 0.2718 L22: 3.1348
REMARK 3 L33: 0.8246 L12: 0.0877
REMARK 3 L13: -0.2281 L23: -1.2351
REMARK 3 S TENSOR
REMARK 3 S11: -0.0753 S12: 0.0153 S13: -0.0453
REMARK 3 S21: -0.0291 S22: 0.0544 S23: -0.0159
REMARK 3 S31: 0.0017 S32: 0.0091 S33: 0.0208
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 30 A 47
REMARK 3 ORIGIN FOR THE GROUP (A): 46.9440 4.0612 105.2148
REMARK 3 T TENSOR
REMARK 3 T11: 0.1558 T22: 0.1765
REMARK 3 T33: 0.1512 T12: -0.0466
REMARK 3 T13: 0.0554 T23: -0.0106
REMARK 3 L TENSOR
REMARK 3 L11: 0.4120 L22: 2.7329
REMARK 3 L33: 0.4895 L12: -0.6158
REMARK 3 L13: 0.3592 L23: -0.0168
REMARK 3 S TENSOR
REMARK 3 S11: -0.0539 S12: -0.0065 S13: 0.0164
REMARK 3 S21: -0.1089 S22: 0.0636 S23: -0.1290
REMARK 3 S31: -0.0364 S32: -0.0075 S33: -0.0097
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 48 A 75
REMARK 3 ORIGIN FOR THE GROUP (A): 66.9654 -1.4514 104.1500
REMARK 3 T TENSOR
REMARK 3 T11: 0.1309 T22: 0.1522
REMARK 3 T33: 0.1781 T12: 0.0224
REMARK 3 T13: 0.0743 T23: -0.0645
REMARK 3 L TENSOR
REMARK 3 L11: 3.5674 L22: 2.3976
REMARK 3 L33: 1.8763 L12: 1.6817
REMARK 3 L13: 1.0303 L23: -1.1015
REMARK 3 S TENSOR
REMARK 3 S11: -0.0992 S12: 0.1405 S13: -0.0867
REMARK 3 S21: -0.1223 S22: 0.0068 S23: -0.1093
REMARK 3 S31: 0.0519 S32: 0.0970 S33: 0.0924
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 76 A 122
REMARK 3 ORIGIN FOR THE GROUP (A): 55.6358 8.5592 113.6801
REMARK 3 T TENSOR
REMARK 3 T11: 0.1384 T22: 0.1717
REMARK 3 T33: 0.1800 T12: -0.0065
REMARK 3 T13: 0.0439 T23: -0.0086
REMARK 3 L TENSOR
REMARK 3 L11: 0.6628 L22: 0.7682
REMARK 3 L33: 0.2062 L12: -0.4760
REMARK 3 L13: 0.3112 L23: -0.1879
REMARK 3 S TENSOR
REMARK 3 S11: -0.0889 S12: -0.0542 S13: 0.0524
REMARK 3 S21: -0.0883 S22: 0.0076 S23: -0.1166
REMARK 3 S31: -0.0354 S32: 0.0340 S33: 0.0812
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 123 A 157
REMARK 3 ORIGIN FOR THE GROUP (A): 56.9301 3.4977 104.1171
REMARK 3 T TENSOR
REMARK 3 T11: 0.1313 T22: 0.1569
REMARK 3 T33: 0.1361 T12: -0.0150
REMARK 3 T13: 0.0606 T23: -0.0269
REMARK 3 L TENSOR
REMARK 3 L11: 1.2913 L22: 0.9379
REMARK 3 L33: 0.8196 L12: -0.5726
REMARK 3 L13: 0.8955 L23: -0.4091
REMARK 3 S TENSOR
REMARK 3 S11: -0.0940 S12: 0.0490 S13: -0.0525
REMARK 3 S21: -0.0600 S22: 0.0191 S23: -0.0901
REMARK 3 S31: 0.0118 S32: -0.0013 S33: 0.0749
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 158 A 170
REMARK 3 ORIGIN FOR THE GROUP (A): 37.4797 19.4918 100.7026
REMARK 3 T TENSOR
REMARK 3 T11: 0.1972 T22: 0.1706
REMARK 3 T33: 0.1236 T12: -0.0545
REMARK 3 T13: -0.0180 T23: 0.0562
REMARK 3 L TENSOR
REMARK 3 L11: 1.5694 L22: 7.7622
REMARK 3 L33: 0.7034 L12: 1.2278
REMARK 3 L13: 0.1524 L23: 2.2803
REMARK 3 S TENSOR
REMARK 3 S11: 0.1041 S12: 0.1619 S13: 0.1780
REMARK 3 S21: -0.3574 S22: -0.1258 S23: 0.1561
REMARK 3 S31: -0.1173 S32: -0.0824 S33: 0.0217
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 2 B 35
REMARK 3 ORIGIN FOR THE GROUP (A): 34.4537 -1.7448 112.1645
REMARK 3 T TENSOR
REMARK 3 T11: 0.1641 T22: 0.1456
REMARK 3 T33: 0.1516 T12: -0.0382
REMARK 3 T13: 0.0449 T23: -0.0366
REMARK 3 L TENSOR
REMARK 3 L11: 0.1373 L22: 2.2507
REMARK 3 L33: 1.1353 L12: -0.2404
REMARK 3 L13: 0.3370 L23: -0.8974
REMARK 3 S TENSOR
REMARK 3 S11: -0.0653 S12: 0.0249 S13: -0.0034
REMARK 3 S21: 0.0056 S22: -0.0174 S23: 0.0202
REMARK 3 S31: 0.0347 S32: -0.0313 S33: 0.0827
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 36 B 55
REMARK 3 ORIGIN FOR THE GROUP (A): 32.3284 -3.7317 98.4266
REMARK 3 T TENSOR
REMARK 3 T11: 0.2066 T22: 0.1359
REMARK 3 T33: 0.1871 T12: -0.0642
REMARK 3 T13: 0.0001 T23: -0.0649
REMARK 3 L TENSOR
REMARK 3 L11: 0.3096 L22: 0.8859
REMARK 3 L33: 0.2983 L12: -0.3080
REMARK 3 L13: -0.2861 L23: 0.2103
REMARK 3 S TENSOR
REMARK 3 S11: -0.0860 S12: 0.0574 S13: -0.0709
REMARK 3 S21: -0.0980 S22: -0.0560 S23: -0.0668
REMARK 3 S31: 0.0656 S32: -0.0571 S33: 0.1421
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 : B 56 B 77
REMARK 3 ORIGIN FOR THE GROUP (A): 18.5025 -2.1375 96.8912
REMARK 3 T TENSOR
REMARK 3 T11: 0.1315 T22: 0.2010
REMARK 3 T33: 0.0973 T12: -0.0588
REMARK 3 T13: 0.0234 T23: -0.0834
REMARK 3 L TENSOR
REMARK 3 L11: 9.3672 L22: 7.3623
REMARK 3 L33: 1.9607 L12: 4.7678
REMARK 3 L13: 1.2133 L23: 2.1084
REMARK 3 S TENSOR
REMARK 3 S11: -0.1950 S12: -0.1349 S13: 0.1535
REMARK 3 S21: 0.1115 S22: -0.2154 S23: 0.2899
REMARK 3 S31: 0.0685 S32: -0.2239 S33: 0.4104
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 : B 78 B 95
REMARK 3 ORIGIN FOR THE GROUP (A): 32.9047 -6.3538 111.1900
REMARK 3 T TENSOR
REMARK 3 T11: 0.2411 T22: 0.1027
REMARK 3 T33: 0.1477 T12: -0.0804
REMARK 3 T13: 0.0513 T23: -0.0791
REMARK 3 L TENSOR
REMARK 3 L11: 0.8927 L22: 1.8587
REMARK 3 L33: 5.2996 L12: 0.3848
REMARK 3 L13: -0.4694 L23: -3.1152
REMARK 3 S TENSOR
REMARK 3 S11: -0.0790 S12: 0.1016 S13: -0.0631
REMARK 3 S21: -0.1520 S22: 0.0162 S23: -0.0022
REMARK 3 S31: 0.2663 S32: -0.0548 S33: 0.0628
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 : B 96 B 131
REMARK 3 ORIGIN FOR THE GROUP (A): 20.1974 6.4176 111.6830
REMARK 3 T TENSOR
REMARK 3 T11: 0.1390 T22: 0.1616
REMARK 3 T33: 0.1724 T12: -0.0745
REMARK 3 T13: -0.0114 T23: -0.0150
REMARK 3 L TENSOR
REMARK 3 L11: 0.9451 L22: 2.4880
REMARK 3 L33: 2.2038 L12: -0.5410
REMARK 3 L13: 0.1506 L23: -1.1547
REMARK 3 S TENSOR
REMARK 3 S11: -0.0567 S12: 0.0424 S13: 0.0049
REMARK 3 S21: -0.1595 S22: 0.1456 S23: 0.1556
REMARK 3 S31: 0.1203 S32: -0.2402 S33: -0.0889
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 : B 132 B 170
REMARK 3 ORIGIN FOR THE GROUP (A): 37.2031 -10.6444 110.0829
REMARK 3 T TENSOR
REMARK 3 T11: 0.1774 T22: 0.0671
REMARK 3 T33: 0.1354 T12: -0.0483
REMARK 3 T13: 0.0618 T23: -0.0266
REMARK 3 L TENSOR
REMARK 3 L11: 0.8740 L22: 1.1345
REMARK 3 L33: 1.9578 L12: 0.0614
REMARK 3 L13: 0.7032 L23: 0.2946
REMARK 3 S TENSOR
REMARK 3 S11: -0.0432 S12: 0.0361 S13: -0.1876
REMARK 3 S21: -0.0987 S22: 0.0089 S23: 0.0111
REMARK 3 S31: 0.2167 S32: 0.0372 S33: 0.0342
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 : C 5 C 35
REMARK 3 ORIGIN FOR THE GROUP (A): 24.4591 20.2511 125.2221
REMARK 3 T TENSOR
REMARK 3 T11: 0.1536 T22: 0.1327
REMARK 3 T33: 0.1656 T12: -0.0239
REMARK 3 T13: 0.0092 T23: 0.0061
REMARK 3 L TENSOR
REMARK 3 L11: 0.5992 L22: 0.7270
REMARK 3 L33: 1.4631 L12: 0.2385
REMARK 3 L13: 0.1658 L23: 0.3661
REMARK 3 S TENSOR
REMARK 3 S11: 0.0159 S12: -0.0470 S13: 0.0289
REMARK 3 S21: -0.0629 S22: 0.0881 S23: -0.0191
REMARK 3 S31: 0.0347 S32: -0.0415 S33: -0.1040
REMARK 3
REMARK 3 TLS GROUP : 14
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 36 C 55
REMARK 3 ORIGIN FOR THE GROUP (A): 17.2251 30.9870 130.7367
REMARK 3 T TENSOR
REMARK 3 T11: 0.1138 T22: 0.1127
REMARK 3 T33: 0.1999 T12: 0.0392
REMARK 3 T13: 0.0362 T23: 0.0494
REMARK 3 L TENSOR
REMARK 3 L11: 2.9027 L22: 0.9239
REMARK 3 L33: 3.4885 L12: 0.5656
REMARK 3 L13: -0.6731 L23: 0.5251
REMARK 3 S TENSOR
REMARK 3 S11: 0.1545 S12: -0.1487 S13: 0.3509
REMARK 3 S21: -0.0307 S22: 0.1703 S23: 0.0913
REMARK 3 S31: -0.2296 S32: -0.0505 S33: -0.3248
REMARK 3
REMARK 3 TLS GROUP : 15
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 56 C 66
REMARK 3 ORIGIN FOR THE GROUP (A): 3.8446 22.1933 140.3991
REMARK 3 T TENSOR
REMARK 3 T11: 0.1129 T22: 0.1743
REMARK 3 T33: 0.1675 T12: 0.0006
REMARK 3 T13: -0.0195 T23: 0.0574
REMARK 3 L TENSOR
REMARK 3 L11: 13.9181 L22: 8.7187
REMARK 3 L33: 0.3543 L12: -1.1312
REMARK 3 L13: -1.5051 L23: 1.4061
REMARK 3 S TENSOR
REMARK 3 S11: 0.2361 S12: 0.2276 S13: -0.4529
REMARK 3 S21: -0.1564 S22: -0.3122 S23: 0.4778
REMARK 3 S31: -0.0494 S32: -0.0709 S33: 0.0761
REMARK 3
REMARK 3 TLS GROUP : 16
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 67 C 95
REMARK 3 ORIGIN FOR THE GROUP (A): 17.2274 23.1155 129.9743
REMARK 3 T TENSOR
REMARK 3 T11: 0.1079 T22: 0.1419
REMARK 3 T33: 0.1826 T12: 0.0063
REMARK 3 T13: -0.0010 T23: 0.0141
REMARK 3 L TENSOR
REMARK 3 L11: 1.0352 L22: 0.6895
REMARK 3 L33: 1.2279 L12: -0.1134
REMARK 3 L13: -1.0636 L23: 0.1489
REMARK 3 S TENSOR
REMARK 3 S11: 0.0029 S12: 0.0423 S13: 0.0785
REMARK 3 S21: -0.0307 S22: 0.0373 S23: 0.0802
REMARK 3 S31: -0.0779 S32: -0.1464 S33: -0.0401
REMARK 3
REMARK 3 TLS GROUP : 17
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 96 C 157
REMARK 3 ORIGIN FOR THE GROUP (A): 18.0965 18.5267 132.2571
REMARK 3 T TENSOR
REMARK 3 T11: 0.0991 T22: 0.1734
REMARK 3 T33: 0.1770 T12: -0.0086
REMARK 3 T13: 0.0166 T23: 0.0016
REMARK 3 L TENSOR
REMARK 3 L11: 0.1666 L22: 0.6688
REMARK 3 L33: 1.5637 L12: 0.0937
REMARK 3 L13: -0.0623 L23: -0.6544
REMARK 3 S TENSOR
REMARK 3 S11: -0.0303 S12: -0.0068 S13: 0.0359
REMARK 3 S21: 0.0676 S22: 0.0873 S23: 0.0765
REMARK 3 S31: 0.0356 S32: -0.1577 S33: -0.0571
REMARK 3
REMARK 3 TLS GROUP : 18
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 158 C 170
REMARK 3 ORIGIN FOR THE GROUP (A): 23.7071 19.7113 106.4774
REMARK 3 T TENSOR
REMARK 3 T11: 0.1024 T22: 0.2454
REMARK 3 T33: 0.1296 T12: -0.0199
REMARK 3 T13: -0.0572 T23: 0.0127
REMARK 3 L TENSOR
REMARK 3 L11: 0.8735 L22: 14.4893
REMARK 3 L33: 1.3337 L12: 3.2591
REMARK 3 L13: 0.4558 L23: 3.2859
REMARK 3 S TENSOR
REMARK 3 S11: -0.1096 S12: 0.1448 S13: 0.0792
REMARK 3 S21: -0.5796 S22: -0.0904 S23: 0.4823
REMARK 3 S31: -0.2092 S32: -0.3228 S33: 0.2000
REMARK 3
REMARK 3 TLS GROUP : 19
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 2 D 30
REMARK 3 ORIGIN FOR THE GROUP (A): 52.1722 9.6547 137.3319
REMARK 3 T TENSOR
REMARK 3 T11: 0.1376 T22: 0.1671
REMARK 3 T33: 0.1469 T12: -0.0144
REMARK 3 T13: -0.0140 T23: 0.0267
REMARK 3 L TENSOR
REMARK 3 L11: 2.9501 L22: 0.4064
REMARK 3 L33: 1.4529 L12: -0.8296
REMARK 3 L13: -1.7675 L23: 0.7570
REMARK 3 S TENSOR
REMARK 3 S11: 0.0199 S12: -0.1397 S13: 0.0337
REMARK 3 S21: -0.0114 S22: 0.0090 S23: -0.0104
REMARK 3 S31: -0.0217 S32: 0.0620 S33: -0.0288
REMARK 3
REMARK 3 TLS GROUP : 20
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 31 D 56
REMARK 3 ORIGIN FOR THE GROUP (A): 54.5778 9.7793 145.9725
REMARK 3 T TENSOR
REMARK 3 T11: 0.1055 T22: 0.2130
REMARK 3 T33: 0.1566 T12: -0.0077
REMARK 3 T13: -0.0343 T23: 0.0134
REMARK 3 L TENSOR
REMARK 3 L11: 1.0158 L22: 0.9393
REMARK 3 L33: 0.6354 L12: 0.5407
REMARK 3 L13: -0.7641 L23: -0.2324
REMARK 3 S TENSOR
REMARK 3 S11: 0.0285 S12: -0.1821 S13: -0.1004
REMARK 3 S21: 0.1252 S22: -0.1211 S23: -0.0737
REMARK 3 S31: 0.0452 S32: 0.1027 S33: 0.0926
REMARK 3
REMARK 3 TLS GROUP : 21
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 57 D 66
REMARK 3 ORIGIN FOR THE GROUP (A): 65.4046 25.0843 149.3892
REMARK 3 T TENSOR
REMARK 3 T11: 0.1408 T22: 0.5129
REMARK 3 T33: 0.5648 T12: -0.1807
REMARK 3 T13: -0.1591 T23: 0.1556
REMARK 3 L TENSOR
REMARK 3 L11: 7.5161 L22: 9.5809
REMARK 3 L33: 15.3722 L12: -5.0265
REMARK 3 L13: 10.2015 L23: -5.4799
REMARK 3 S TENSOR
REMARK 3 S11: -0.2783 S12: 1.2917 S13: 1.2086
REMARK 3 S21: 0.7383 S22: -0.8190 S23: -2.0175
REMARK 3 S31: 0.0605 S32: 1.3665 S33: 1.0973
REMARK 3
REMARK 3 TLS GROUP : 22
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 67 D 96
REMARK 3 ORIGIN FOR THE GROUP (A): 55.8938 13.7255 142.3456
REMARK 3 T TENSOR
REMARK 3 T11: 0.0819 T22: 0.2139
REMARK 3 T33: 0.1629 T12: -0.0001
REMARK 3 T13: -0.0326 T23: 0.0014
REMARK 3 L TENSOR
REMARK 3 L11: 0.4147 L22: 1.3572
REMARK 3 L33: 1.9242 L12: 0.3744
REMARK 3 L13: -0.3306 L23: 0.9832
REMARK 3 S TENSOR
REMARK 3 S11: -0.0138 S12: -0.1495 S13: -0.0033
REMARK 3 S21: 0.0762 S22: -0.0390 S23: -0.0358
REMARK 3 S31: 0.1182 S32: 0.2439 S33: 0.0528
REMARK 3
REMARK 3 TLS GROUP : 23
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 97 D 154
REMARK 3 ORIGIN FOR THE GROUP (A): 55.0046 18.9929 139.5978
REMARK 3 T TENSOR
REMARK 3 T11: 0.1023 T22: 0.2054
REMARK 3 T33: 0.1621 T12: -0.0215
REMARK 3 T13: -0.0109 T23: -0.0316
REMARK 3 L TENSOR
REMARK 3 L11: 0.2893 L22: 1.1660
REMARK 3 L33: 0.4322 L12: -0.2022
REMARK 3 L13: 0.0083 L23: 0.0461
REMARK 3 S TENSOR
REMARK 3 S11: -0.0130 S12: -0.1194 S13: 0.0819
REMARK 3 S21: 0.0035 S22: 0.0480 S23: -0.0465
REMARK 3 S31: -0.0729 S32: 0.1783 S33: -0.0350
REMARK 3
REMARK 3 TLS GROUP : 24
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 155 D 170
REMARK 3 ORIGIN FOR THE GROUP (A): 56.3370 -5.4538 130.3993
REMARK 3 T TENSOR
REMARK 3 T11: 0.1262 T22: 0.0973
REMARK 3 T33: 0.2047 T12: 0.0675
REMARK 3 T13: 0.0535 T23: 0.0286
REMARK 3 L TENSOR
REMARK 3 L11: 1.4138 L22: 0.8779
REMARK 3 L33: 4.1574 L12: 1.0199
REMARK 3 L13: -0.1755 L23: -0.3560
REMARK 3 S TENSOR
REMARK 3 S11: -0.1934 S12: -0.0296 S13: -0.1963
REMARK 3 S21: -0.0587 S22: 0.0299 S23: -0.0638
REMARK 3 S31: 0.2600 S32: 0.0620 S33: 0.1635
REMARK 3
REMARK 3 TLS GROUP : 25
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 3 E 29
REMARK 3 ORIGIN FOR THE GROUP (A): 37.4804 -0.2243 139.1279
REMARK 3 T TENSOR
REMARK 3 T11: 0.1406 T22: 0.1369
REMARK 3 T33: 0.1593 T12: -0.0131
REMARK 3 T13: 0.0029 T23: -0.0059
REMARK 3 L TENSOR
REMARK 3 L11: 1.9929 L22: 1.0142
REMARK 3 L33: 0.8305 L12: -0.9176
REMARK 3 L13: -1.1426 L23: 0.2427
REMARK 3 S TENSOR
REMARK 3 S11: -0.0471 S12: -0.0840 S13: -0.0811
REMARK 3 S21: -0.0165 S22: -0.0299 S23: -0.0302
REMARK 3 S31: 0.0911 S32: 0.0202 S33: 0.0770
REMARK 3
REMARK 3 TLS GROUP : 26
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 30 E 55
REMARK 3 ORIGIN FOR THE GROUP (A): 40.3174 -4.2633 144.4917
REMARK 3 T TENSOR
REMARK 3 T11: 0.1742 T22: 0.1588
REMARK 3 T33: 0.1538 T12: -0.0186
REMARK 3 T13: 0.0345 T23: 0.0438
REMARK 3 L TENSOR
REMARK 3 L11: 0.9769 L22: 0.9344
REMARK 3 L33: 0.2591 L12: 0.4973
REMARK 3 L13: 0.3610 L23: 0.4549
REMARK 3 S TENSOR
REMARK 3 S11: 0.0131 S12: -0.1533 S13: -0.0228
REMARK 3 S21: 0.1290 S22: -0.0251 S23: -0.0841
REMARK 3 S31: 0.0404 S32: -0.0085 S33: 0.0120
REMARK 3
REMARK 3 TLS GROUP : 27
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 56 E 75
REMARK 3 ORIGIN FOR THE GROUP (A): 34.2037 -20.7657 142.4226
REMARK 3 T TENSOR
REMARK 3 T11: 0.1817 T22: 0.0954
REMARK 3 T33: 0.1951 T12: 0.0202
REMARK 3 T13: 0.0231 T23: 0.0244
REMARK 3 L TENSOR
REMARK 3 L11: 5.1803 L22: 1.5525
REMARK 3 L33: 2.5429 L12: 2.8234
REMARK 3 L13: -0.7704 L23: -0.5866
REMARK 3 S TENSOR
REMARK 3 S11: -0.0314 S12: -0.1822 S13: -0.1020
REMARK 3 S21: -0.0248 S22: -0.0869 S23: -0.0828
REMARK 3 S31: 0.0884 S32: -0.1308 S33: 0.1183
REMARK 3
REMARK 3 TLS GROUP : 28
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 76 E 96
REMARK 3 ORIGIN FOR THE GROUP (A): 34.5130 -0.7849 142.5046
REMARK 3 T TENSOR
REMARK 3 T11: 0.1580 T22: 0.1455
REMARK 3 T33: 0.1185 T12: -0.0101
REMARK 3 T13: 0.0339 T23: 0.0359
REMARK 3 L TENSOR
REMARK 3 L11: 3.0851 L22: 2.0153
REMARK 3 L33: 0.3178 L12: -1.1720
REMARK 3 L13: -0.0810 L23: 0.1566
REMARK 3 S TENSOR
REMARK 3 S11: -0.1245 S12: -0.1685 S13: -0.0360
REMARK 3 S21: 0.1380 S22: 0.0453 S23: 0.0270
REMARK 3 S31: 0.1049 S32: -0.0512 S33: 0.0791
REMARK 3
REMARK 3 TLS GROUP : 29
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 97 E 152
REMARK 3 ORIGIN FOR THE GROUP (A): 33.5284 -8.9897 135.6639
REMARK 3 T TENSOR
REMARK 3 T11: 0.1850 T22: 0.1238
REMARK 3 T33: 0.1611 T12: -0.0093
REMARK 3 T13: 0.0596 T23: -0.0012
REMARK 3 L TENSOR
REMARK 3 L11: 0.3865 L22: 0.5974
REMARK 3 L33: 0.7926 L12: 0.3652
REMARK 3 L13: 0.2896 L23: 0.0087
REMARK 3 S TENSOR
REMARK 3 S11: -0.0839 S12: -0.0398 S13: -0.0239
REMARK 3 S21: -0.0482 S22: 0.0158 S23: 0.0167
REMARK 3 S31: 0.1016 S32: -0.0629 S33: 0.0681
REMARK 3
REMARK 3 TLS GROUP : 30
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 153 E 170
REMARK 3 ORIGIN FOR THE GROUP (A): 34.4866 13.3310 149.0672
REMARK 3 T TENSOR
REMARK 3 T11: 0.1344 T22: 0.1993
REMARK 3 T33: 0.1148 T12: -0.0248
REMARK 3 T13: 0.0364 T23: -0.0326
REMARK 3 L TENSOR
REMARK 3 L11: 3.3678 L22: 1.3979
REMARK 3 L33: 1.8420 L12: -1.8892
REMARK 3 L13: 1.7316 L23: -0.9546
REMARK 3 S TENSOR
REMARK 3 S11: -0.0349 S12: -0.3069 S13: -0.0105
REMARK 3 S21: 0.1405 S22: 0.1179 S23: 0.1475
REMARK 3 S31: -0.0998 S32: 0.0871 S33: -0.0830
REMARK 3
REMARK 3 TLS GROUP : 31
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : F 3 F 28
REMARK 3 ORIGIN FOR THE GROUP (A): 37.3933 30.1009 121.2617
REMARK 3 T TENSOR
REMARK 3 T11: 0.1560 T22: 0.1220
REMARK 3 T33: 0.1765 T12: -0.0316
REMARK 3 T13: 0.0248 T23: 0.0010
REMARK 3 L TENSOR
REMARK 3 L11: 0.5588 L22: 0.1716
REMARK 3 L33: 2.4501 L12: -0.1092
REMARK 3 L13: 0.6397 L23: 0.3220
REMARK 3 S TENSOR
REMARK 3 S11: 0.0225 S12: 0.0157 S13: -0.0163
REMARK 3 S21: -0.0994 S22: 0.0133 S23: -0.0396
REMARK 3 S31: -0.0851 S32: 0.0157 S33: -0.0358
REMARK 3
REMARK 3 TLS GROUP : 32
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : F 29 F 56
REMARK 3 ORIGIN FOR THE GROUP (A): 34.8520 35.9820 119.2698
REMARK 3 T TENSOR
REMARK 3 T11: 0.1709 T22: 0.1254
REMARK 3 T33: 0.1787 T12: -0.0130
REMARK 3 T13: 0.0281 T23: -0.0252
REMARK 3 L TENSOR
REMARK 3 L11: 0.7831 L22: 0.2111
REMARK 3 L33: 0.1861 L12: 0.3969
REMARK 3 L13: -0.2178 L23: -0.0794
REMARK 3 S TENSOR
REMARK 3 S11: 0.0180 S12: 0.0193 S13: 0.1162
REMARK 3 S21: 0.0026 S22: 0.0377 S23: 0.0574
REMARK 3 S31: -0.0284 S32: 0.0295 S33: -0.0557
REMARK 3
REMARK 3 TLS GROUP : 33
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : F 57 F 66
REMARK 3 ORIGIN FOR THE GROUP (A): 47.1359 46.2504 107.5037
REMARK 3 T TENSOR
REMARK 3 T11: 0.1236 T22: 0.0949
REMARK 3 T33: 0.1875 T12: -0.0654
REMARK 3 T13: 0.0393 T23: -0.0165
REMARK 3 L TENSOR
REMARK 3 L11: 4.6654 L22: 9.7978
REMARK 3 L33: 6.7679 L12: 0.3549
REMARK 3 L13: 0.3203 L23: -1.9348
REMARK 3 S TENSOR
REMARK 3 S11: 0.1003 S12: -0.3696 S13: 0.0329
REMARK 3 S21: 0.1583 S22: -0.1667 S23: -0.2917
REMARK 3 S31: -0.3052 S32: 0.1288 S33: 0.0664
REMARK 3
REMARK 3 TLS GROUP : 34
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : F 67 F 96
REMARK 3 ORIGIN FOR THE GROUP (A): 39.3870 35.4005 117.8289
REMARK 3 T TENSOR
REMARK 3 T11: 0.1843 T22: 0.0911
REMARK 3 T33: 0.1992 T12: -0.0191
REMARK 3 T13: 0.0250 T23: -0.0116
REMARK 3 L TENSOR
REMARK 3 L11: 0.4519 L22: 0.3842
REMARK 3 L33: 1.6344 L12: -0.0239
REMARK 3 L13: -0.1165 L23: -0.7591
REMARK 3 S TENSOR
REMARK 3 S11: -0.0656 S12: -0.0364 S13: 0.1171
REMARK 3 S21: 0.0236 S22: 0.0553 S23: -0.0690
REMARK 3 S31: -0.1185 S32: -0.0916 S33: 0.0103
REMARK 3
REMARK 3 TLS GROUP : 35
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : F 97 F 146
REMARK 3 ORIGIN FOR THE GROUP (A): 45.5413 30.4934 112.3245
REMARK 3 T TENSOR
REMARK 3 T11: 0.1484 T22: 0.1296
REMARK 3 T33: 0.1737 T12: -0.0486
REMARK 3 T13: 0.0253 T23: -0.0161
REMARK 3 L TENSOR
REMARK 3 L11: 0.5135 L22: 1.3938
REMARK 3 L33: 0.4390 L12: -0.2977
REMARK 3 L13: -0.1288 L23: 0.1793
REMARK 3 S TENSOR
REMARK 3 S11: 0.0251 S12: 0.0130 S13: 0.0458
REMARK 3 S21: 0.0288 S22: -0.0151 S23: -0.0931
REMARK 3 S31: -0.0132 S32: 0.0986 S33: -0.0099
REMARK 3
REMARK 3 TLS GROUP : 36
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : F 147 F 170
REMARK 3 ORIGIN FOR THE GROUP (A): 34.7955 34.6465 134.3555
REMARK 3 T TENSOR
REMARK 3 T11: 0.1613 T22: 0.1304
REMARK 3 T33: 0.1830 T12: -0.0373
REMARK 3 T13: 0.0139 T23: -0.0582
REMARK 3 L TENSOR
REMARK 3 L11: 1.3038 L22: 1.1803
REMARK 3 L33: 1.2408 L12: -0.7168
REMARK 3 L13: -0.2432 L23: -0.7997
REMARK 3 S TENSOR
REMARK 3 S11: -0.0602 S12: -0.1695 S13: 0.1088
REMARK 3 S21: 0.1762 S22: 0.1564 S23: 0.0128
REMARK 3 S31: -0.1732 S32: -0.1234 S33: -0.0962
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 USED IF
REMARK 4
REMARK 4 4DI6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-JAN-12.
REMARK 100 THE DEPOSITION ID IS D_1000070359.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-OCT-11
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 8.50
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) : 0.978560
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 50359
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.10900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.3300
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.46
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.2
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.54000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.86
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.61
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: EBS INTERNAL TRACKING NUMBER 8.5, 20%
REMARK 280 PEG 3500. BOBUA.00664.A.A1 PS00257 AT 17 MG/ML, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 289K, PH 8.50
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/2
REMARK 290 6555 X-Y,X,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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 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 63.32500
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 63.32500
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 63.32500
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: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 19440 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 37300 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -97.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F
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 -20
REMARK 465 ALA A -19
REMARK 465 HIS 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 MET A -12
REMARK 465 GLY A -11
REMARK 465 THR A -10
REMARK 465 LEU A -9
REMARK 465 GLU A -8
REMARK 465 ALA A -7
REMARK 465 GLN A -6
REMARK 465 THR A -5
REMARK 465 GLN A -4
REMARK 465 GLY A -3
REMARK 465 PRO A -2
REMARK 465 GLY A -1
REMARK 465 SER A 0
REMARK 465 MET B -20
REMARK 465 ALA B -19
REMARK 465 HIS 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 MET B -12
REMARK 465 GLY B -11
REMARK 465 THR B -10
REMARK 465 LEU B -9
REMARK 465 GLU B -8
REMARK 465 ALA B -7
REMARK 465 GLN B -6
REMARK 465 THR B -5
REMARK 465 GLN B -4
REMARK 465 GLY B -3
REMARK 465 PRO B -2
REMARK 465 GLY B -1
REMARK 465 SER B 0
REMARK 465 MET C -20
REMARK 465 ALA C -19
REMARK 465 HIS 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 MET C -12
REMARK 465 GLY C -11
REMARK 465 THR C -10
REMARK 465 LEU C -9
REMARK 465 GLU C -8
REMARK 465 ALA C -7
REMARK 465 GLN C -6
REMARK 465 THR C -5
REMARK 465 GLN C -4
REMARK 465 GLY C -3
REMARK 465 PRO C -2
REMARK 465 GLY C -1
REMARK 465 SER C 0
REMARK 465 MET C 1
REMARK 465 SER C 2
REMARK 465 MET C 3
REMARK 465 MET D -20
REMARK 465 ALA D -19
REMARK 465 HIS D -18
REMARK 465 HIS D -17
REMARK 465 HIS D -16
REMARK 465 HIS D -15
REMARK 465 HIS D -14
REMARK 465 HIS D -13
REMARK 465 MET D -12
REMARK 465 GLY D -11
REMARK 465 THR D -10
REMARK 465 LEU D -9
REMARK 465 GLU D -8
REMARK 465 ALA D -7
REMARK 465 GLN D -6
REMARK 465 THR D -5
REMARK 465 GLN D -4
REMARK 465 GLY D -3
REMARK 465 PRO D -2
REMARK 465 GLY D -1
REMARK 465 SER D 0
REMARK 465 MET E -20
REMARK 465 ALA E -19
REMARK 465 HIS E -18
REMARK 465 HIS E -17
REMARK 465 HIS E -16
REMARK 465 HIS E -15
REMARK 465 HIS E -14
REMARK 465 HIS E -13
REMARK 465 MET E -12
REMARK 465 GLY E -11
REMARK 465 THR E -10
REMARK 465 LEU E -9
REMARK 465 GLU E -8
REMARK 465 ALA E -7
REMARK 465 GLN E -6
REMARK 465 THR E -5
REMARK 465 GLN E -4
REMARK 465 GLY E -3
REMARK 465 PRO E -2
REMARK 465 GLY E -1
REMARK 465 SER E 0
REMARK 465 MET E 1
REMARK 465 MET F -20
REMARK 465 ALA F -19
REMARK 465 HIS F -18
REMARK 465 HIS F -17
REMARK 465 HIS F -16
REMARK 465 HIS F -15
REMARK 465 HIS F -14
REMARK 465 HIS F -13
REMARK 465 MET F -12
REMARK 465 GLY F -11
REMARK 465 THR F -10
REMARK 465 LEU F -9
REMARK 465 GLU F -8
REMARK 465 ALA F -7
REMARK 465 GLN F -6
REMARK 465 THR F -5
REMARK 465 GLN F -4
REMARK 465 GLY F -3
REMARK 465 PRO F -2
REMARK 465 GLY F -1
REMARK 465 SER F 0
REMARK 465 MET F 1
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 MET A 1 CB CG SD CE
REMARK 470 LYS A 72 CG CD CE NZ
REMARK 470 MET B 1 CB CG SD CE
REMARK 470 PHE B 60 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG B 61 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 64 CG CD OE1 OE2
REMARK 470 LYS B 72 CG CD CE NZ
REMARK 470 LYS B 120 CG CD CE NZ
REMARK 470 SER B 122 OG
REMARK 470 GLU B 139 CG CD OE1 OE2
REMARK 470 LYS C 72 CG CD CE NZ
REMARK 470 LYS C 120 CG CD CE NZ
REMARK 470 GLU C 139 CG CD OE1 OE2
REMARK 470 MET D 1 CB CG SD CE
REMARK 470 VAL D 59 CG1 CG2
REMARK 470 PHE D 60 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG D 61 CG CD NE CZ NH1 NH2
REMARK 470 GLU D 139 CG CD OE1 OE2
REMARK 470 LYS E 72 CG CD CE NZ
REMARK 470 MET F 3 CG SD CE
REMARK 470 LYS F 72 CG 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 TRP F 149 CE2 TRP F 149 CD2 0.075
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 ALA A 38 146.52 -171.55
REMARK 500 HIS A 62 -99.26 -131.54
REMARK 500 TYR A 116 -17.04 -149.25
REMARK 500 VAL A 132 -46.62 71.73
REMARK 500 TYR A 168 149.72 71.12
REMARK 500 ALA B 38 147.33 -170.22
REMARK 500 HIS B 62 -101.90 -135.30
REMARK 500 TYR B 116 -8.62 -148.39
REMARK 500 VAL B 132 -49.82 76.03
REMARK 500 TYR B 168 154.68 69.72
REMARK 500 HIS C 62 -91.20 -135.23
REMARK 500 TYR C 116 -16.73 -157.41
REMARK 500 VAL C 132 -49.83 71.15
REMARK 500 TYR C 168 -24.30 94.80
REMARK 500 ALA D 38 144.77 -171.28
REMARK 500 HIS D 62 -103.23 -134.32
REMARK 500 TYR D 116 -15.71 -149.20
REMARK 500 VAL D 132 -44.09 73.41
REMARK 500 TYR D 168 161.02 69.59
REMARK 500 HIS E 62 -89.71 -120.40
REMARK 500 TYR E 116 -13.80 -154.97
REMARK 500 VAL E 132 -48.74 70.68
REMARK 500 TYR E 168 166.20 72.40
REMARK 500 ALA F 38 143.64 -172.91
REMARK 500 HIS F 62 -95.47 -132.47
REMARK 500 TYR F 116 -20.76 -150.73
REMARK 500 VAL F 132 -49.57 75.55
REMARK 500 TYR F 168 159.44 73.34
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: BOBUA.00664.A RELATED DB: TARGETTRACK
DBREF 4DI6 A 3 169 UNP O51419 NDK_BORBU 1 167
DBREF 4DI6 B 3 169 UNP O51419 NDK_BORBU 1 167
DBREF 4DI6 C 3 169 UNP O51419 NDK_BORBU 1 167
DBREF 4DI6 D 3 169 UNP O51419 NDK_BORBU 1 167
DBREF 4DI6 E 3 169 UNP O51419 NDK_BORBU 1 167
DBREF 4DI6 F 3 169 UNP O51419 NDK_BORBU 1 167
SEQADV 4DI6 MET A -20 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 ALA A -19 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 HIS A -18 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 HIS A -17 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 HIS A -16 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 HIS A -15 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 HIS A -14 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 HIS A -13 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 MET A -12 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 GLY A -11 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 THR A -10 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 LEU A -9 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 GLU A -8 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 ALA A -7 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 GLN A -6 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 THR A -5 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 GLN A -4 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 GLY A -3 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 PRO A -2 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 GLY A -1 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 SER A 0 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 MET A 1 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 SER A 2 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 MET B -20 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 ALA B -19 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 HIS B -18 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 HIS B -17 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 HIS B -16 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 HIS B -15 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 HIS B -14 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 HIS B -13 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 MET B -12 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 GLY B -11 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 THR B -10 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 LEU B -9 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 GLU B -8 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 ALA B -7 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 GLN B -6 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 THR B -5 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 GLN B -4 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 GLY B -3 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 PRO B -2 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 GLY B -1 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 SER B 0 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 MET B 1 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 SER B 2 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 MET C -20 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 ALA C -19 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 HIS C -18 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 HIS C -17 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 HIS C -16 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 HIS C -15 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 HIS C -14 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 HIS C -13 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 MET C -12 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 GLY C -11 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 THR C -10 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 LEU C -9 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 GLU C -8 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 ALA C -7 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 GLN C -6 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 THR C -5 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 GLN C -4 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 GLY C -3 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 PRO C -2 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 GLY C -1 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 SER C 0 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 MET C 1 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 SER C 2 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 MET D -20 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 ALA D -19 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 HIS D -18 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 HIS D -17 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 HIS D -16 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 HIS D -15 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 HIS D -14 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 HIS D -13 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 MET D -12 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 GLY D -11 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 THR D -10 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 LEU D -9 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 GLU D -8 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 ALA D -7 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 GLN D -6 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 THR D -5 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 GLN D -4 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 GLY D -3 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 PRO D -2 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 GLY D -1 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 SER D 0 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 MET D 1 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 SER D 2 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 MET E -20 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 ALA E -19 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 HIS E -18 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 HIS E -17 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 HIS E -16 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 HIS E -15 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 HIS E -14 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 HIS E -13 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 MET E -12 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 GLY E -11 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 THR E -10 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 LEU E -9 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 GLU E -8 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 ALA E -7 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 GLN E -6 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 THR E -5 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 GLN E -4 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 GLY E -3 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 PRO E -2 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 GLY E -1 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 SER E 0 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 MET E 1 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 SER E 2 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 MET F -20 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 ALA F -19 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 HIS F -18 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 HIS F -17 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 HIS F -16 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 HIS F -15 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 HIS F -14 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 HIS F -13 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 MET F -12 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 GLY F -11 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 THR F -10 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 LEU F -9 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 GLU F -8 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 ALA F -7 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 GLN F -6 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 THR F -5 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 GLN F -4 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 GLY F -3 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 PRO F -2 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 GLY F -1 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 SER F 0 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 MET F 1 UNP O51419 EXPRESSION TAG
SEQADV 4DI6 SER F 2 UNP O51419 EXPRESSION TAG
SEQRES 1 A 190 MET ALA HIS HIS HIS HIS HIS HIS MET GLY THR LEU GLU
SEQRES 2 A 190 ALA GLN THR GLN GLY PRO GLY SER MET SER MET LEU LEU
SEQRES 3 A 190 GLN LYS THR LEU CYS ILE VAL LYS PRO ASP GLY VAL ARG
SEQRES 4 A 190 ARG GLY LEU ILE GLY ASP VAL VAL SER ARG PHE GLU ARG
SEQRES 5 A 190 VAL GLY LEU LYS MET VAL ALA ALA LYS MET LEU ILE VAL
SEQRES 6 A 190 ASP GLU SER LEU ALA LYS LYS HIS TYR LEU TYR ASP ASP
SEQRES 7 A 190 ILE VAL PHE ARG HIS SER GLU ALA VAL TRP ASN SER LEU
SEQRES 8 A 190 ILE LYS PHE ILE SER ASN SER PRO VAL PHE THR PHE VAL
SEQRES 9 A 190 VAL GLU GLY VAL GLU SER ILE GLU VAL VAL ARG LYS LEU
SEQRES 10 A 190 CYS GLY ALA THR GLU PRO LYS LEU ALA ILE PRO GLY THR
SEQRES 11 A 190 ILE ARG GLY ASP PHE SER TYR HIS SER PHE LYS TYR SER
SEQRES 12 A 190 ASN GLU LYS GLY PHE SER ILE TYR ASN VAL ILE HIS ALA
SEQRES 13 A 190 SER ALA ASN GLU ALA ASP ALA MET ARG GLU ILE PRO ILE
SEQRES 14 A 190 TRP PHE LYS ASP ASN GLU ILE LEU ASN TYR LYS ARG ASP
SEQRES 15 A 190 ASP GLU CYS GLU HIS TYR TYR CYS
SEQRES 1 B 190 MET ALA HIS HIS HIS HIS HIS HIS MET GLY THR LEU GLU
SEQRES 2 B 190 ALA GLN THR GLN GLY PRO GLY SER MET SER MET LEU LEU
SEQRES 3 B 190 GLN LYS THR LEU CYS ILE VAL LYS PRO ASP GLY VAL ARG
SEQRES 4 B 190 ARG GLY LEU ILE GLY ASP VAL VAL SER ARG PHE GLU ARG
SEQRES 5 B 190 VAL GLY LEU LYS MET VAL ALA ALA LYS MET LEU ILE VAL
SEQRES 6 B 190 ASP GLU SER LEU ALA LYS LYS HIS TYR LEU TYR ASP ASP
SEQRES 7 B 190 ILE VAL PHE ARG HIS SER GLU ALA VAL TRP ASN SER LEU
SEQRES 8 B 190 ILE LYS PHE ILE SER ASN SER PRO VAL PHE THR PHE VAL
SEQRES 9 B 190 VAL GLU GLY VAL GLU SER ILE GLU VAL VAL ARG LYS LEU
SEQRES 10 B 190 CYS GLY ALA THR GLU PRO LYS LEU ALA ILE PRO GLY THR
SEQRES 11 B 190 ILE ARG GLY ASP PHE SER TYR HIS SER PHE LYS TYR SER
SEQRES 12 B 190 ASN GLU LYS GLY PHE SER ILE TYR ASN VAL ILE HIS ALA
SEQRES 13 B 190 SER ALA ASN GLU ALA ASP ALA MET ARG GLU ILE PRO ILE
SEQRES 14 B 190 TRP PHE LYS ASP ASN GLU ILE LEU ASN TYR LYS ARG ASP
SEQRES 15 B 190 ASP GLU CYS GLU HIS TYR TYR CYS
SEQRES 1 C 190 MET ALA HIS HIS HIS HIS HIS HIS MET GLY THR LEU GLU
SEQRES 2 C 190 ALA GLN THR GLN GLY PRO GLY SER MET SER MET LEU LEU
SEQRES 3 C 190 GLN LYS THR LEU CYS ILE VAL LYS PRO ASP GLY VAL ARG
SEQRES 4 C 190 ARG GLY LEU ILE GLY ASP VAL VAL SER ARG PHE GLU ARG
SEQRES 5 C 190 VAL GLY LEU LYS MET VAL ALA ALA LYS MET LEU ILE VAL
SEQRES 6 C 190 ASP GLU SER LEU ALA LYS LYS HIS TYR LEU TYR ASP ASP
SEQRES 7 C 190 ILE VAL PHE ARG HIS SER GLU ALA VAL TRP ASN SER LEU
SEQRES 8 C 190 ILE LYS PHE ILE SER ASN SER PRO VAL PHE THR PHE VAL
SEQRES 9 C 190 VAL GLU GLY VAL GLU SER ILE GLU VAL VAL ARG LYS LEU
SEQRES 10 C 190 CYS GLY ALA THR GLU PRO LYS LEU ALA ILE PRO GLY THR
SEQRES 11 C 190 ILE ARG GLY ASP PHE SER TYR HIS SER PHE LYS TYR SER
SEQRES 12 C 190 ASN GLU LYS GLY PHE SER ILE TYR ASN VAL ILE HIS ALA
SEQRES 13 C 190 SER ALA ASN GLU ALA ASP ALA MET ARG GLU ILE PRO ILE
SEQRES 14 C 190 TRP PHE LYS ASP ASN GLU ILE LEU ASN TYR LYS ARG ASP
SEQRES 15 C 190 ASP GLU CYS GLU HIS TYR TYR CYS
SEQRES 1 D 190 MET ALA HIS HIS HIS HIS HIS HIS MET GLY THR LEU GLU
SEQRES 2 D 190 ALA GLN THR GLN GLY PRO GLY SER MET SER MET LEU LEU
SEQRES 3 D 190 GLN LYS THR LEU CYS ILE VAL LYS PRO ASP GLY VAL ARG
SEQRES 4 D 190 ARG GLY LEU ILE GLY ASP VAL VAL SER ARG PHE GLU ARG
SEQRES 5 D 190 VAL GLY LEU LYS MET VAL ALA ALA LYS MET LEU ILE VAL
SEQRES 6 D 190 ASP GLU SER LEU ALA LYS LYS HIS TYR LEU TYR ASP ASP
SEQRES 7 D 190 ILE VAL PHE ARG HIS SER GLU ALA VAL TRP ASN SER LEU
SEQRES 8 D 190 ILE LYS PHE ILE SER ASN SER PRO VAL PHE THR PHE VAL
SEQRES 9 D 190 VAL GLU GLY VAL GLU SER ILE GLU VAL VAL ARG LYS LEU
SEQRES 10 D 190 CYS GLY ALA THR GLU PRO LYS LEU ALA ILE PRO GLY THR
SEQRES 11 D 190 ILE ARG GLY ASP PHE SER TYR HIS SER PHE LYS TYR SER
SEQRES 12 D 190 ASN GLU LYS GLY PHE SER ILE TYR ASN VAL ILE HIS ALA
SEQRES 13 D 190 SER ALA ASN GLU ALA ASP ALA MET ARG GLU ILE PRO ILE
SEQRES 14 D 190 TRP PHE LYS ASP ASN GLU ILE LEU ASN TYR LYS ARG ASP
SEQRES 15 D 190 ASP GLU CYS GLU HIS TYR TYR CYS
SEQRES 1 E 190 MET ALA HIS HIS HIS HIS HIS HIS MET GLY THR LEU GLU
SEQRES 2 E 190 ALA GLN THR GLN GLY PRO GLY SER MET SER MET LEU LEU
SEQRES 3 E 190 GLN LYS THR LEU CYS ILE VAL LYS PRO ASP GLY VAL ARG
SEQRES 4 E 190 ARG GLY LEU ILE GLY ASP VAL VAL SER ARG PHE GLU ARG
SEQRES 5 E 190 VAL GLY LEU LYS MET VAL ALA ALA LYS MET LEU ILE VAL
SEQRES 6 E 190 ASP GLU SER LEU ALA LYS LYS HIS TYR LEU TYR ASP ASP
SEQRES 7 E 190 ILE VAL PHE ARG HIS SER GLU ALA VAL TRP ASN SER LEU
SEQRES 8 E 190 ILE LYS PHE ILE SER ASN SER PRO VAL PHE THR PHE VAL
SEQRES 9 E 190 VAL GLU GLY VAL GLU SER ILE GLU VAL VAL ARG LYS LEU
SEQRES 10 E 190 CYS GLY ALA THR GLU PRO LYS LEU ALA ILE PRO GLY THR
SEQRES 11 E 190 ILE ARG GLY ASP PHE SER TYR HIS SER PHE LYS TYR SER
SEQRES 12 E 190 ASN GLU LYS GLY PHE SER ILE TYR ASN VAL ILE HIS ALA
SEQRES 13 E 190 SER ALA ASN GLU ALA ASP ALA MET ARG GLU ILE PRO ILE
SEQRES 14 E 190 TRP PHE LYS ASP ASN GLU ILE LEU ASN TYR LYS ARG ASP
SEQRES 15 E 190 ASP GLU CYS GLU HIS TYR TYR CYS
SEQRES 1 F 190 MET ALA HIS HIS HIS HIS HIS HIS MET GLY THR LEU GLU
SEQRES 2 F 190 ALA GLN THR GLN GLY PRO GLY SER MET SER MET LEU LEU
SEQRES 3 F 190 GLN LYS THR LEU CYS ILE VAL LYS PRO ASP GLY VAL ARG
SEQRES 4 F 190 ARG GLY LEU ILE GLY ASP VAL VAL SER ARG PHE GLU ARG
SEQRES 5 F 190 VAL GLY LEU LYS MET VAL ALA ALA LYS MET LEU ILE VAL
SEQRES 6 F 190 ASP GLU SER LEU ALA LYS LYS HIS TYR LEU TYR ASP ASP
SEQRES 7 F 190 ILE VAL PHE ARG HIS SER GLU ALA VAL TRP ASN SER LEU
SEQRES 8 F 190 ILE LYS PHE ILE SER ASN SER PRO VAL PHE THR PHE VAL
SEQRES 9 F 190 VAL GLU GLY VAL GLU SER ILE GLU VAL VAL ARG LYS LEU
SEQRES 10 F 190 CYS GLY ALA THR GLU PRO LYS LEU ALA ILE PRO GLY THR
SEQRES 11 F 190 ILE ARG GLY ASP PHE SER TYR HIS SER PHE LYS TYR SER
SEQRES 12 F 190 ASN GLU LYS GLY PHE SER ILE TYR ASN VAL ILE HIS ALA
SEQRES 13 F 190 SER ALA ASN GLU ALA ASP ALA MET ARG GLU ILE PRO ILE
SEQRES 14 F 190 TRP PHE LYS ASP ASN GLU ILE LEU ASN TYR LYS ARG ASP
SEQRES 15 F 190 ASP GLU CYS GLU HIS TYR TYR CYS
FORMUL 7 HOH *431(H2 O)
HELIX 1 1 LYS A 13 ARG A 19 1 7
HELIX 2 2 LEU A 21 GLY A 33 1 13
HELIX 3 3 ASP A 45 TYR A 53 1 9
HELIX 4 4 LEU A 54 HIS A 62 1 9
HELIX 5 5 SER A 63 SER A 75 1 13
HELIX 6 6 GLU A 88 GLY A 98 1 11
HELIX 7 7 THR A 109 SER A 115 1 7
HELIX 8 8 SER A 118 GLY A 126 1 9
HELIX 9 9 ASN A 138 PHE A 150 1 13
HELIX 10 10 LYS A 151 ILE A 155 5 5
HELIX 11 11 ASP A 162 TYR A 167 1 6
HELIX 12 12 LYS B 13 ARG B 19 1 7
HELIX 13 13 LEU B 21 GLY B 33 1 13
HELIX 14 14 ASP B 45 TYR B 53 1 9
HELIX 15 15 LEU B 54 HIS B 62 1 9
HELIX 16 16 SER B 63 SER B 75 1 13
HELIX 17 17 GLU B 88 GLY B 98 1 11
HELIX 18 18 THR B 109 SER B 115 1 7
HELIX 19 19 SER B 118 GLY B 126 1 9
HELIX 20 20 ASN B 138 PHE B 150 1 13
HELIX 21 21 LYS B 151 ILE B 155 5 5
HELIX 22 22 ASP B 162 TYR B 167 1 6
HELIX 23 23 LYS C 13 ARG C 19 1 7
HELIX 24 24 LEU C 21 GLY C 33 1 13
HELIX 25 25 ASP C 45 TYR C 53 1 9
HELIX 26 26 LEU C 54 HIS C 62 1 9
HELIX 27 27 SER C 63 SER C 75 1 13
HELIX 28 28 GLU C 88 GLY C 98 1 11
HELIX 29 29 THR C 109 SER C 115 1 7
HELIX 30 30 SER C 118 GLY C 126 1 9
HELIX 31 31 ASN C 138 PHE C 150 1 13
HELIX 32 32 LYS C 151 ILE C 155 5 5
HELIX 33 33 ASP C 162 TYR C 167 1 6
HELIX 34 34 LYS D 13 ARG D 19 1 7
HELIX 35 35 LEU D 21 GLY D 33 1 13
HELIX 36 36 ASP D 45 TYR D 53 1 9
HELIX 37 37 LEU D 54 HIS D 62 1 9
HELIX 38 38 SER D 63 SER D 75 1 13
HELIX 39 39 GLU D 88 GLY D 98 1 11
HELIX 40 40 THR D 109 SER D 115 1 7
HELIX 41 41 SER D 118 GLY D 126 1 9
HELIX 42 42 ASN D 138 PHE D 150 1 13
HELIX 43 43 LYS D 151 ILE D 155 5 5
HELIX 44 44 ASP D 162 TYR D 167 1 6
HELIX 45 45 LYS E 13 ARG E 19 1 7
HELIX 46 46 LEU E 21 GLY E 33 1 13
HELIX 47 47 ASP E 45 TYR E 53 1 9
HELIX 48 48 LEU E 54 HIS E 62 1 9
HELIX 49 49 SER E 63 SER E 75 1 13
HELIX 50 50 GLU E 88 GLY E 98 1 11
HELIX 51 51 THR E 109 SER E 115 1 7
HELIX 52 52 SER E 118 GLY E 126 1 9
HELIX 53 53 ASN E 138 PHE E 150 1 13
HELIX 54 54 LYS E 151 ILE E 155 5 5
HELIX 55 55 ASP E 162 TYR E 167 1 6
HELIX 56 56 LYS F 13 ARG F 19 1 7
HELIX 57 57 LEU F 21 GLY F 33 1 13
HELIX 58 58 ASP F 45 TYR F 53 1 9
HELIX 59 59 LEU F 54 HIS F 62 1 9
HELIX 60 60 SER F 63 SER F 75 1 13
HELIX 61 61 GLU F 88 GLY F 98 1 11
HELIX 62 62 THR F 109 SER F 115 1 7
HELIX 63 63 SER F 118 GLY F 126 1 9
HELIX 64 64 ASN F 138 PHE F 150 1 13
HELIX 65 65 LYS F 151 ILE F 155 5 5
HELIX 66 66 ASP F 162 TYR F 167 1 6
SHEET 1 A 4 LYS A 35 VAL A 44 0
SHEET 2 A 4 SER A 77 VAL A 87 -1 O GLU A 85 N LYS A 35
SHEET 3 A 4 LEU A 5 VAL A 12 -1 N VAL A 12 O PHE A 80
SHEET 4 A 4 ILE A 133 ALA A 135 -1 O HIS A 134 N ILE A 11
SHEET 1 B 4 LYS B 35 VAL B 44 0
SHEET 2 B 4 SER B 77 VAL B 87 -1 O THR B 81 N LYS B 40
SHEET 3 B 4 LEU B 5 VAL B 12 -1 N CYS B 10 O PHE B 82
SHEET 4 B 4 ILE B 133 ALA B 135 -1 O HIS B 134 N ILE B 11
SHEET 1 C 4 LYS C 35 VAL C 44 0
SHEET 2 C 4 SER C 77 VAL C 87 -1 O THR C 81 N LYS C 40
SHEET 3 C 4 LEU C 5 VAL C 12 -1 N VAL C 12 O PHE C 80
SHEET 4 C 4 ILE C 133 ALA C 135 -1 O HIS C 134 N ILE C 11
SHEET 1 D 4 LYS D 35 VAL D 44 0
SHEET 2 D 4 SER D 77 VAL D 87 -1 O VAL D 83 N VAL D 37
SHEET 3 D 4 LEU D 5 VAL D 12 -1 N CYS D 10 O PHE D 82
SHEET 4 D 4 ILE D 133 ALA D 135 -1 O HIS D 134 N ILE D 11
SHEET 1 E 4 LYS E 35 VAL E 44 0
SHEET 2 E 4 SER E 77 VAL E 87 -1 O SER E 77 N VAL E 44
SHEET 3 E 4 LEU E 5 VAL E 12 -1 N VAL E 12 O PHE E 80
SHEET 4 E 4 ILE E 133 ALA E 135 -1 O HIS E 134 N ILE E 11
SHEET 1 F 4 LYS F 35 VAL F 44 0
SHEET 2 F 4 SER F 77 VAL F 87 -1 O VAL F 83 N VAL F 37
SHEET 3 F 4 LEU F 5 VAL F 12 -1 N VAL F 12 O PHE F 80
SHEET 4 F 4 ILE F 133 ALA F 135 -1 O HIS F 134 N ILE F 11
SSBOND 1 CYS A 164 CYS A 169 1555 1555 2.06
SSBOND 2 CYS B 164 CYS B 169 1555 1555 2.07
SSBOND 3 CYS C 164 CYS C 169 1555 1555 2.06
SSBOND 4 CYS D 164 CYS D 169 1555 1555 2.05
SSBOND 5 CYS E 164 CYS E 169 1555 1555 2.06
SSBOND 6 CYS F 164 CYS F 169 1555 1555 2.06
CRYST1 135.260 135.260 126.650 90.00 90.00 120.00 P 63 36
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 0.007393 0.004268 0.000000 0.00000
SCALE2 0.000000 0.008537 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007896 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
