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HEADER HYDROLASE 20-JUL-10 2XLB
TITLE ACETYL XYLAN ESTERASE FROM BACILLUS PUMILUS WITHOUT LIGANDS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYL XYLAN ESTERASE;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H, I, J, K, L;
COMPND 4 SYNONYM: CEPHALOSPORIN C DEACETYLASE;
COMPND 5 EC: 3.1.1.72;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS PUMILUS;
SOURCE 3 ORGANISM_TAXID: 1408;
SOURCE 4 STRAIN: CECT5072;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: ROSETTA (DE3) PLYS;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR: PET28A;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET28A6HIS-AXE
KEYWDS HYDROLASE, PARAOXON, CE-7 FAMILY, IRREVERSIBLE INHIBITION
EXPDTA X-RAY DIFFRACTION
AUTHOR F.GIL-ORTIZ,S.MONTORO-GARCIA,L.M.POLO,V.RUBIO,A.SANCHEZ-FERRER
REVDAT 1 25-MAY-11 2XLB 0
JRNL AUTH S.MONTORO-GARCIA,F.GIL-ORTIZ,F.GARCIA-CARMONA,L.M.POLO,
JRNL AUTH 2 V.RUBIO,A.SANCHEZ-FERRER
JRNL TITL THE CRYSTAL STRUCTURE OF THE CEPHALOSPORIN DEACETYLATING
JRNL TITL 2 ENZYME ACETYL XYLAN ESTERASE BOUND TO PARAOXON EXPLAINS THE
JRNL TITL 3 LOW SENSITIVITY OF THIS SERINE HYDROLASE TO ORGANOPHOSPHATE
JRNL TITL 4 INACTIVATION.
JRNL REF BIOCHEM.J. V. 436 321 2011
JRNL REFN ISSN 0264-6021
JRNL PMID 21382014
JRNL DOI 10.1042/BJ20101859
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0088
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.08
REMARK 3 NUMBER OF REFLECTIONS : 288931
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) : 0.13719
REMARK 3 R VALUE (WORKING SET) : 0.13649
REMARK 3 FREE R VALUE : 0.15033
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.0
REMARK 3 FREE R VALUE TEST SET COUNT : 15312
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.899
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.948
REMARK 3 REFLECTION IN BIN (WORKING SET) : 19111
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 83.13
REMARK 3 BIN R VALUE (WORKING SET) : 0.179
REMARK 3 BIN FREE R VALUE SET COUNT : 1039
REMARK 3 BIN FREE R VALUE : 0.210
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 30050
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 1504
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 13.661
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 13.162
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.77
REMARK 3 B22 (A**2) : -0.86
REMARK 3 B33 (A**2) : 2.63
REMARK 3 B12 (A**2) : 0.00
REMARK 3 B13 (A**2) : -2.19
REMARK 3 B23 (A**2) : 0.00
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.025
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.021
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.055
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.257
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.954
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): 30914 ; 0.015 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 20476 ; 0.005 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 42107 ; 1.338 ; 1.951
REMARK 3 BOND ANGLES OTHERS (DEGREES): 49732 ; 1.394 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 3792 ; 5.452 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 1461 ;32.850 ;23.758
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 4688 ;15.491 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 144 ;17.827 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 34884 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 6672 ; 0.002 ; 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): 18924 ; 0.380 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 7680 ; 0.146 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 30359 ; 0.741 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 11990 ; 1.221 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 11748 ; 1.828 ; 4.500
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 : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B C D E F G H I J K L
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 1 A 400 3
REMARK 3 1 B 1 B 400 3
REMARK 3 1 C 1 C 400 3
REMARK 3 1 D 1 D 400 3
REMARK 3 1 E 1 E 400 3
REMARK 3 1 F 1 F 400 3
REMARK 3 1 G 1 G 400 3
REMARK 3 1 H 1 H 400 3
REMARK 3 1 I 1 I 400 3
REMARK 3 1 J 1 J 400 3
REMARK 3 1 K 1 K 400 3
REMARK 3 1 L 1 L 400 3
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 1830 ; 0.03 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 B (A): 1830 ; 0.03 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 C (A): 1830 ; 0.02 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 D (A): 1830 ; 0.03 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 E (A): 1830 ; 0.03 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 F (A): 1830 ; 0.03 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 G (A): 1830 ; 0.02 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 H (A): 1830 ; 0.02 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 I (A): 1830 ; 0.02 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 J (A): 1830 ; 0.02 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 K (A): 1830 ; 0.03 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 L (A): 1830 ; 0.03 ; 0.05
REMARK 3 LOOSE POSITIONAL 1 A (A): 2339 ; 0.11 ; 5.00
REMARK 3 LOOSE POSITIONAL 1 B (A): 2339 ; 0.09 ; 5.00
REMARK 3 LOOSE POSITIONAL 1 C (A): 2339 ; 0.09 ; 5.00
REMARK 3 LOOSE POSITIONAL 1 D (A): 2339 ; 0.05 ; 5.00
REMARK 3 LOOSE POSITIONAL 1 E (A): 2339 ; 0.07 ; 5.00
REMARK 3 LOOSE POSITIONAL 1 F (A): 2339 ; 0.05 ; 5.00
REMARK 3 LOOSE POSITIONAL 1 G (A): 2339 ; 0.06 ; 5.00
REMARK 3 LOOSE POSITIONAL 1 H (A): 2339 ; 0.06 ; 5.00
REMARK 3 LOOSE POSITIONAL 1 I (A): 2339 ; 0.05 ; 5.00
REMARK 3 LOOSE POSITIONAL 1 J (A): 2339 ; 0.06 ; 5.00
REMARK 3 LOOSE POSITIONAL 1 K (A): 2339 ; 0.05 ; 5.00
REMARK 3 LOOSE POSITIONAL 1 L (A): 2339 ; 0.05 ; 5.00
REMARK 3 TIGHT THERMAL 1 A (A**2): 1830 ; 0.09 ; 0.50
REMARK 3 TIGHT THERMAL 1 B (A**2): 1830 ; 0.09 ; 0.50
REMARK 3 TIGHT THERMAL 1 C (A**2): 1830 ; 0.10 ; 0.50
REMARK 3 TIGHT THERMAL 1 D (A**2): 1830 ; 0.09 ; 0.50
REMARK 3 TIGHT THERMAL 1 E (A**2): 1830 ; 0.08 ; 0.50
REMARK 3 TIGHT THERMAL 1 F (A**2): 1830 ; 0.08 ; 0.50
REMARK 3 TIGHT THERMAL 1 G (A**2): 1830 ; 0.07 ; 0.50
REMARK 3 TIGHT THERMAL 1 H (A**2): 1830 ; 0.08 ; 0.50
REMARK 3 TIGHT THERMAL 1 I (A**2): 1830 ; 0.09 ; 0.50
REMARK 3 TIGHT THERMAL 1 H (A**2): 1830 ; 0.08 ; 0.50
REMARK 3 TIGHT THERMAL 1 K (A**2): 1830 ; 0.09 ; 0.50
REMARK 3 TIGHT THERMAL 1 L (A**2): 1830 ; 0.08 ; 0.50
REMARK 3 LOOSE THERMAL 1 A (A**2): 2339 ; 0.09 ; 10.00
REMARK 3 LOOSE THERMAL 1 B (A**2): 2339 ; 0.08 ; 10.00
REMARK 3 LOOSE THERMAL 1 C (A**2): 2339 ; 0.09 ; 10.00
REMARK 3 LOOSE THERMAL 1 D (A**2): 2339 ; 0.08 ; 10.00
REMARK 3 LOOSE THERMAL 1 E (A**2): 2339 ; 0.08 ; 10.00
REMARK 3 LOOSE THERMAL 1 F (A**2): 2339 ; 0.08 ; 10.00
REMARK 3 LOOSE THERMAL 1 G (A**2): 2339 ; 0.07 ; 10.00
REMARK 3 LOOSE THERMAL 1 H (A**2): 2339 ; 0.07 ; 10.00
REMARK 3 LOOSE THERMAL 1 I (A**2): 2339 ; 0.08 ; 10.00
REMARK 3 LOOSE THERMAL 1 J (A**2): 2339 ; 0.07 ; 10.00
REMARK 3 LOOSE THERMAL 1 K (A**2): 2339 ; 0.08 ; 10.00
REMARK 3 LOOSE THERMAL 1 L (A**2): 2339 ; 0.07 ; 10.00
REMARK 3
REMARK 3 TWIN DETAILS
REMARK 3 NUMBER OF TWIN DOMAINS : 2
REMARK 3 TWIN DOMAIN : 1
REMARK 3 TWIN OPERATOR : 1.000H, 1.000K, L
REMARK 3 TWIN FRACTION : 0.540
REMARK 3 TWIN DOMAIN : 2
REMARK 3 TWIN OPERATOR : -1.000H, -1.000K, 1.000H+L
REMARK 3 TWIN FRACTION : 0.460
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 93
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 1 A 78
REMARK 3 ORIGIN FOR THE GROUP (A): -4.0590 -2.0140 115.4050
REMARK 3 T TENSOR
REMARK 3 T11: 0.0848 T22: 0.0333
REMARK 3 T33: 0.0454 T12: -0.0067
REMARK 3 T13: -0.0117 T23: 0.0260
REMARK 3 L TENSOR
REMARK 3 L11: 1.7615 L22: 0.9032
REMARK 3 L33: 1.0694 L12: 0.3714
REMARK 3 L13: 0.0972 L23: 0.3647
REMARK 3 S TENSOR
REMARK 3 S11: 0.0930 S12: -0.1624 S13: 0.0111
REMARK 3 S21: 0.1024 S22: -0.0769 S23: -0.0372
REMARK 3 S31: 0.0023 S32: -0.0379 S33: -0.0161
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 79 A 116
REMARK 3 ORIGIN FOR THE GROUP (A): -13.2860 -7.1570 109.6330
REMARK 3 T TENSOR
REMARK 3 T11: 0.0586 T22: 0.0654
REMARK 3 T33: 0.0464 T12: -0.0200
REMARK 3 T13: -0.0044 T23: 0.0212
REMARK 3 L TENSOR
REMARK 3 L11: 1.2896 L22: 2.1574
REMARK 3 L33: 0.2534 L12: 0.8692
REMARK 3 L13: 0.2841 L23: 0.7381
REMARK 3 S TENSOR
REMARK 3 S11: 0.0029 S12: 0.0104 S13: -0.0383
REMARK 3 S21: -0.0012 S22: -0.0263 S23: 0.0770
REMARK 3 S31: 0.0035 S32: -0.0111 S33: 0.0235
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 117 A 218
REMARK 3 ORIGIN FOR THE GROUP (A): -1.1630 0.7670 114.3920
REMARK 3 T TENSOR
REMARK 3 T11: 0.0455 T22: 0.0442
REMARK 3 T33: 0.0325 T12: -0.0113
REMARK 3 T13: -0.0147 T23: 0.0180
REMARK 3 L TENSOR
REMARK 3 L11: 0.7840 L22: 1.3361
REMARK 3 L33: 0.7425 L12: 0.3286
REMARK 3 L13: -0.1890 L23: -0.2043
REMARK 3 S TENSOR
REMARK 3 S11: 0.0056 S12: -0.0665 S13: -0.0182
REMARK 3 S21: 0.1128 S22: -0.0059 S23: 0.0227
REMARK 3 S31: 0.0233 S32: -0.0329 S33: 0.0004
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 219 A 243
REMARK 3 ORIGIN FOR THE GROUP (A): 10.1880 14.8350 106.1060
REMARK 3 T TENSOR
REMARK 3 T11: 0.0663 T22: 0.0690
REMARK 3 T33: 0.0542 T12: -0.0201
REMARK 3 T13: 0.0122 T23: -0.0028
REMARK 3 L TENSOR
REMARK 3 L11: 1.9045 L22: 5.4106
REMARK 3 L33: 1.2791 L12: 0.7285
REMARK 3 L13: -0.5133 L23: -1.2895
REMARK 3 S TENSOR
REMARK 3 S11: -0.0172 S12: -0.0628 S13: 0.1396
REMARK 3 S21: 0.0719 S22: 0.0210 S23: -0.1406
REMARK 3 S31: -0.2220 S32: 0.1861 S33: -0.0038
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 244 A 317
REMARK 3 ORIGIN FOR THE GROUP (A): 4.5570 -9.7710 105.4330
REMARK 3 T TENSOR
REMARK 3 T11: 0.0535 T22: 0.0499
REMARK 3 T33: 0.0847 T12: 0.0013
REMARK 3 T13: -0.0084 T23: 0.0146
REMARK 3 L TENSOR
REMARK 3 L11: 0.4966 L22: 0.7472
REMARK 3 L33: 0.9022 L12: 0.3842
REMARK 3 L13: 0.0764 L23: 0.5600
REMARK 3 S TENSOR
REMARK 3 S11: 0.0007 S12: -0.0452 S13: -0.1138
REMARK 3 S21: 0.0465 S22: -0.0282 S23: -0.0872
REMARK 3 S31: 0.0965 S32: 0.0245 S33: 0.0275
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 1 B 19
REMARK 3 ORIGIN FOR THE GROUP (A): -28.0360 10.2720 79.9170
REMARK 3 T TENSOR
REMARK 3 T11: 0.1093 T22: 0.0332
REMARK 3 T33: 0.1594 T12: 0.0319
REMARK 3 T13: 0.0239 T23: 0.0330
REMARK 3 L TENSOR
REMARK 3 L11: 2.2118 L22: 1.8438
REMARK 3 L33: 4.6367 L12: 0.7962
REMARK 3 L13: 0.7404 L23: 1.3770
REMARK 3 S TENSOR
REMARK 3 S11: 0.0947 S12: -0.0885 S13: 0.2125
REMARK 3 S21: 0.0579 S22: -0.0340 S23: 0.0955
REMARK 3 S31: -0.3409 S32: -0.0609 S33: -0.0606
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 20 B 38
REMARK 3 ORIGIN FOR THE GROUP (A): -31.3400 -17.3870 67.4640
REMARK 3 T TENSOR
REMARK 3 T11: 0.0714 T22: 0.1044
REMARK 3 T33: 0.1081 T12: -0.0317
REMARK 3 T13: -0.0142 T23: -0.0156
REMARK 3 L TENSOR
REMARK 3 L11: 1.5727 L22: 10.1066
REMARK 3 L33: 3.5661 L12: -3.4896
REMARK 3 L13: 1.4650 L23: -3.0871
REMARK 3 S TENSOR
REMARK 3 S11: 0.1113 S12: 0.1093 S13: -0.1088
REMARK 3 S21: -0.5332 S22: -0.0633 S23: 0.0298
REMARK 3 S31: 0.2423 S32: -0.0838 S33: -0.0479
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 39 B 75
REMARK 3 ORIGIN FOR THE GROUP (A): -17.5230 -26.8860 87.1870
REMARK 3 T TENSOR
REMARK 3 T11: 0.0542 T22: 0.0082
REMARK 3 T33: 0.1258 T12: -0.0035
REMARK 3 T13: 0.0053 T23: -0.0010
REMARK 3 L TENSOR
REMARK 3 L11: 1.5281 L22: 0.8820
REMARK 3 L33: 8.0739 L12: 0.1868
REMARK 3 L13: 1.4656 L23: 0.1593
REMARK 3 S TENSOR
REMARK 3 S11: 0.0978 S12: 0.0557 S13: -0.2548
REMARK 3 S21: 0.0160 S22: 0.0449 S23: -0.0393
REMARK 3 S31: 0.3994 S32: 0.0824 S33: -0.1427
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 76 B 97
REMARK 3 ORIGIN FOR THE GROUP (A): -19.8440 -17.6140 91.3150
REMARK 3 T TENSOR
REMARK 3 T11: 0.0705 T22: 0.0650
REMARK 3 T33: 0.0913 T12: -0.0242
REMARK 3 T13: -0.0128 T23: 0.0056
REMARK 3 L TENSOR
REMARK 3 L11: 2.0801 L22: 1.2315
REMARK 3 L33: 1.6726 L12: 0.4795
REMARK 3 L13: -0.5986 L23: -0.5262
REMARK 3 S TENSOR
REMARK 3 S11: 0.1221 S12: -0.3253 S13: -0.1488
REMARK 3 S21: 0.2342 S22: -0.1584 S23: -0.0403
REMARK 3 S31: 0.0222 S32: 0.1868 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 : B 98 B 119
REMARK 3 ORIGIN FOR THE GROUP (A): -18.8930 -17.4760 92.5120
REMARK 3 T TENSOR
REMARK 3 T11: 0.0140 T22: 0.0228
REMARK 3 T33: 0.0721 T12: -0.0088
REMARK 3 T13: -0.0229 T23: 0.0109
REMARK 3 L TENSOR
REMARK 3 L11: 0.9335 L22: 1.2917
REMARK 3 L33: 2.1913 L12: -0.2963
REMARK 3 L13: 0.3817 L23: -0.5878
REMARK 3 S TENSOR
REMARK 3 S11: -0.0017 S12: -0.0892 S13: 0.0529
REMARK 3 S21: 0.0519 S22: -0.0128 S23: -0.0745
REMARK 3 S31: 0.0452 S32: 0.0458 S33: 0.0145
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 120 B 243
REMARK 3 ORIGIN FOR THE GROUP (A): -21.4630 -9.8980 74.9500
REMARK 3 T TENSOR
REMARK 3 T11: 0.0151 T22: 0.0211
REMARK 3 T33: 0.0721 T12: -0.0024
REMARK 3 T13: -0.0256 T23: -0.0113
REMARK 3 L TENSOR
REMARK 3 L11: 1.0099 L22: 1.0406
REMARK 3 L33: 1.0136 L12: 0.3531
REMARK 3 L13: -0.4568 L23: -0.4005
REMARK 3 S TENSOR
REMARK 3 S11: 0.0052 S12: 0.0465 S13: -0.0369
REMARK 3 S21: -0.0650 S22: 0.0093 S23: 0.0399
REMARK 3 S31: 0.0121 S32: -0.0695 S33: -0.0145
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 244 B 317
REMARK 3 ORIGIN FOR THE GROUP (A): -28.2230 -1.6740 86.3870
REMARK 3 T TENSOR
REMARK 3 T11: 0.0161 T22: 0.0240
REMARK 3 T33: 0.0949 T12: 0.0020
REMARK 3 T13: -0.0017 T23: 0.0006
REMARK 3 L TENSOR
REMARK 3 L11: 0.2851 L22: 0.8030
REMARK 3 L33: 1.6493 L12: 0.1642
REMARK 3 L13: 0.1108 L23: 0.1893
REMARK 3 S TENSOR
REMARK 3 S11: 0.0475 S12: -0.0493 S13: -0.0202
REMARK 3 S21: 0.0701 S22: -0.0044 S23: 0.0973
REMARK 3 S31: -0.0052 S32: -0.1001 S33: -0.0432
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 1 C 19
REMARK 3 ORIGIN FOR THE GROUP (A): 27.2870 12.6260 90.0290
REMARK 3 T TENSOR
REMARK 3 T11: 0.1085 T22: 0.0372
REMARK 3 T33: 0.1180 T12: 0.0190
REMARK 3 T13: -0.0365 T23: 0.0193
REMARK 3 L TENSOR
REMARK 3 L11: 4.4330 L22: 2.2786
REMARK 3 L33: 4.4084 L12: 2.0735
REMARK 3 L13: -3.1905 L23: -1.1226
REMARK 3 S TENSOR
REMARK 3 S11: 0.0324 S12: -0.1892 S13: -0.2104
REMARK 3 S21: 0.1791 S22: -0.0672 S23: -0.0922
REMARK 3 S31: 0.2753 S32: 0.0224 S33: 0.0349
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 20 C 38
REMARK 3 ORIGIN FOR THE GROUP (A): 36.8920 34.6940 71.2620
REMARK 3 T TENSOR
REMARK 3 T11: 0.1288 T22: 0.0881
REMARK 3 T33: 0.1075 T12: -0.0447
REMARK 3 T13: 0.0221 T23: -0.0153
REMARK 3 L TENSOR
REMARK 3 L11: 2.7745 L22: 10.0869
REMARK 3 L33: 1.6759 L12: -4.7084
REMARK 3 L13: -0.8707 L23: -0.1538
REMARK 3 S TENSOR
REMARK 3 S11: 0.2243 S12: 0.0549 S13: 0.1687
REMARK 3 S21: -0.5668 S22: -0.1377 S23: -0.3007
REMARK 3 S31: -0.0320 S32: 0.0793 S33: -0.0866
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 39 C 75
REMARK 3 ORIGIN FOR THE GROUP (A): 17.7370 49.5170 80.4260
REMARK 3 T TENSOR
REMARK 3 T11: 0.0470 T22: 0.0202
REMARK 3 T33: 0.1062 T12: -0.0061
REMARK 3 T13: -0.0107 T23: 0.0210
REMARK 3 L TENSOR
REMARK 3 L11: 2.3771 L22: 1.1877
REMARK 3 L33: 4.4214 L12: -0.8039
REMARK 3 L13: -2.2446 L23: 1.1108
REMARK 3 S TENSOR
REMARK 3 S11: 0.1687 S12: 0.1363 S13: 0.2785
REMARK 3 S21: -0.1113 S22: 0.0065 S23: -0.0150
REMARK 3 S31: -0.2720 S32: -0.1337 S33: -0.1751
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 76 C 97
REMARK 3 ORIGIN FOR THE GROUP (A): 17.7350 42.2750 87.8970
REMARK 3 T TENSOR
REMARK 3 T11: 0.1032 T22: 0.0500
REMARK 3 T33: 0.1933 T12: -0.0404
REMARK 3 T13: 0.0400 T23: -0.0382
REMARK 3 L TENSOR
REMARK 3 L11: 1.9858 L22: 0.4943
REMARK 3 L33: 1.4414 L12: 0.1333
REMARK 3 L13: -0.0695 L23: 0.3964
REMARK 3 S TENSOR
REMARK 3 S11: -0.0443 S12: -0.1635 S13: 0.3170
REMARK 3 S21: 0.1737 S22: -0.0992 S23: 0.2389
REMARK 3 S31: 0.0404 S32: -0.1473 S33: 0.1435
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 98 C 119
REMARK 3 ORIGIN FOR THE GROUP (A): 16.4130 42.4940 88.6550
REMARK 3 T TENSOR
REMARK 3 T11: 0.0452 T22: 0.0173
REMARK 3 T33: 0.1135 T12: -0.0024
REMARK 3 T13: -0.0429 T23: 0.0052
REMARK 3 L TENSOR
REMARK 3 L11: 0.6309 L22: 1.8791
REMARK 3 L33: 2.4769 L12: -0.1966
REMARK 3 L13: -1.1480 L23: 0.7912
REMARK 3 S TENSOR
REMARK 3 S11: 0.0103 S12: 0.0385 S13: -0.0943
REMARK 3 S21: 0.1456 S22: -0.0508 S23: 0.1333
REMARK 3 S31: 0.1124 S32: -0.0900 S33: 0.0406
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 120 C 243
REMARK 3 ORIGIN FOR THE GROUP (A): 24.4660 29.6490 76.7070
REMARK 3 T TENSOR
REMARK 3 T11: 0.0044 T22: 0.0320
REMARK 3 T33: 0.0610 T12: 0.0003
REMARK 3 T13: 0.0019 T23: 0.0269
REMARK 3 L TENSOR
REMARK 3 L11: 0.6053 L22: 1.5667
REMARK 3 L33: 1.0213 L12: 0.3361
REMARK 3 L13: 0.2000 L23: 0.5659
REMARK 3 S TENSOR
REMARK 3 S11: 0.0014 S12: 0.0298 S13: 0.0100
REMARK 3 S21: -0.0690 S22: -0.0021 S23: -0.0580
REMARK 3 S31: 0.0032 S32: 0.0234 S33: 0.0006
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 : C 244 C 286
REMARK 3 ORIGIN FOR THE GROUP (A): 29.5420 23.6530 86.3550
REMARK 3 T TENSOR
REMARK 3 T11: 0.0405 T22: 0.0213
REMARK 3 T33: 0.0807 T12: 0.0145
REMARK 3 T13: -0.0173 T23: -0.0007
REMARK 3 L TENSOR
REMARK 3 L11: 0.1983 L22: 0.7048
REMARK 3 L33: 1.6610 L12: -0.0227
REMARK 3 L13: -0.5192 L23: -0.3735
REMARK 3 S TENSOR
REMARK 3 S11: -0.0398 S12: -0.0481 S13: 0.0346
REMARK 3 S21: 0.0771 S22: 0.0638 S23: -0.1129
REMARK 3 S31: 0.0899 S32: 0.0880 S33: -0.0239
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 : C 287 C 317
REMARK 3 ORIGIN FOR THE GROUP (A): 21.8200 28.9830 98.5620
REMARK 3 T TENSOR
REMARK 3 T11: 0.0744 T22: 0.0616
REMARK 3 T33: 0.0762 T12: 0.0089
REMARK 3 T13: -0.0111 T23: -0.0091
REMARK 3 L TENSOR
REMARK 3 L11: 1.0829 L22: 3.1325
REMARK 3 L33: 0.5918 L12: 1.2992
REMARK 3 L13: -0.5034 L23: -0.2081
REMARK 3 S TENSOR
REMARK 3 S11: 0.1050 S12: -0.1364 S13: 0.0825
REMARK 3 S21: 0.2220 S22: -0.1172 S23: -0.0462
REMARK 3 S31: -0.0834 S32: 0.0114 S33: 0.0122
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 1 D 20
REMARK 3 ORIGIN FOR THE GROUP (A): -19.4200 31.4610 86.4880
REMARK 3 T TENSOR
REMARK 3 T11: 0.0639 T22: 0.1012
REMARK 3 T33: 0.1129 T12: -0.0123
REMARK 3 T13: -0.0425 T23: -0.0105
REMARK 3 L TENSOR
REMARK 3 L11: 2.8262 L22: 1.9164
REMARK 3 L33: 6.0363 L12: 0.2683
REMARK 3 L13: -2.9295 L23: -1.2695
REMARK 3 S TENSOR
REMARK 3 S11: -0.0014 S12: 0.3880 S13: -0.0106
REMARK 3 S21: -0.2507 S22: -0.0476 S23: 0.0806
REMARK 3 S31: -0.0932 S32: -0.2166 S33: 0.0489
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 21 D 39
REMARK 3 ORIGIN FOR THE GROUP (A): -19.2230 33.0440 117.3260
REMARK 3 T TENSOR
REMARK 3 T11: 0.0785 T22: 0.1026
REMARK 3 T33: 0.1121 T12: -0.0253
REMARK 3 T13: 0.0592 T23: -0.0225
REMARK 3 L TENSOR
REMARK 3 L11: 6.9720 L22: 1.6511
REMARK 3 L33: 4.6711 L12: 0.5174
REMARK 3 L13: 4.2199 L23: 0.2702
REMARK 3 S TENSOR
REMARK 3 S11: 0.1604 S12: -0.6056 S13: 0.0853
REMARK 3 S21: 0.1921 S22: -0.1553 S23: 0.0604
REMARK 3 S31: 0.2491 S32: -0.4295 S33: -0.0051
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 40 D 75
REMARK 3 ORIGIN FOR THE GROUP (A): 5.8070 36.0240 115.8280
REMARK 3 T TENSOR
REMARK 3 T11: 0.1018 T22: 0.0562
REMARK 3 T33: 0.0572 T12: -0.0056
REMARK 3 T13: -0.0169 T23: -0.0233
REMARK 3 L TENSOR
REMARK 3 L11: 4.1109 L22: 1.5035
REMARK 3 L33: 1.4539 L12: 1.8708
REMARK 3 L13: -1.6103 L23: -1.0648
REMARK 3 S TENSOR
REMARK 3 S11: 0.0883 S12: -0.3335 S13: -0.0603
REMARK 3 S21: 0.1884 S22: -0.1078 S23: -0.0395
REMARK 3 S31: -0.0366 S32: 0.1660 S33: 0.0194
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 76 D 97
REMARK 3 ORIGIN FOR THE GROUP (A): 3.5810 38.2440 106.1760
REMARK 3 T TENSOR
REMARK 3 T11: 0.1070 T22: 0.0702
REMARK 3 T33: 0.1268 T12: -0.0404
REMARK 3 T13: 0.0120 T23: -0.0425
REMARK 3 L TENSOR
REMARK 3 L11: 1.0012 L22: 1.7692
REMARK 3 L33: 0.4111 L12: 0.1665
REMARK 3 L13: -0.1836 L23: -0.2812
REMARK 3 S TENSOR
REMARK 3 S11: -0.0349 S12: -0.0442 S13: 0.0935
REMARK 3 S21: -0.1314 S22: 0.0813 S23: -0.3164
REMARK 3 S31: -0.1014 S32: 0.1179 S33: -0.0464
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 : D 98 D 119
REMARK 3 ORIGIN FOR THE GROUP (A): 4.9720 38.1970 105.5050
REMARK 3 T TENSOR
REMARK 3 T11: 0.0277 T22: 0.0644
REMARK 3 T33: 0.0569 T12: 0.0036
REMARK 3 T13: 0.0085 T23: -0.0127
REMARK 3 L TENSOR
REMARK 3 L11: 2.2677 L22: 0.6056
REMARK 3 L33: 0.4088 L12: 0.8932
REMARK 3 L13: 0.3843 L23: 0.3066
REMARK 3 S TENSOR
REMARK 3 S11: 0.0097 S12: 0.1407 S13: -0.0567
REMARK 3 S21: 0.0352 S22: 0.0048 S23: -0.0640
REMARK 3 S31: 0.0184 S32: 0.0627 S33: -0.0145
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 : D 120 D 243
REMARK 3 ORIGIN FOR THE GROUP (A): -11.3990 27.9590 105.9460
REMARK 3 T TENSOR
REMARK 3 T11: 0.0090 T22: 0.0386
REMARK 3 T33: 0.0502 T12: 0.0073
REMARK 3 T13: 0.0138 T23: -0.0026
REMARK 3 L TENSOR
REMARK 3 L11: 0.7181 L22: 1.8759
REMARK 3 L33: 0.8183 L12: 0.4607
REMARK 3 L13: 0.1085 L23: 0.1651
REMARK 3 S TENSOR
REMARK 3 S11: 0.0318 S12: -0.0487 S13: 0.0336
REMARK 3 S21: 0.0772 S22: -0.0310 S23: 0.0443
REMARK 3 S31: 0.0120 S32: -0.0389 S33: -0.0007
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 : D 244 D 286
REMARK 3 ORIGIN FOR THE GROUP (A): -16.1560 34.9350 96.8190
REMARK 3 T TENSOR
REMARK 3 T11: 0.0367 T22: 0.0451
REMARK 3 T33: 0.0949 T12: -0.0052
REMARK 3 T13: -0.0080 T23: 0.0044
REMARK 3 L TENSOR
REMARK 3 L11: 0.9956 L22: 0.4462
REMARK 3 L33: 1.1913 L12: 0.5956
REMARK 3 L13: -0.2378 L23: -0.4389
REMARK 3 S TENSOR
REMARK 3 S11: -0.0033 S12: -0.0227 S13: 0.1477
REMARK 3 S21: -0.0060 S22: 0.0201 S23: 0.1056
REMARK 3 S31: -0.0338 S32: -0.0691 S33: -0.0169
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 : D 287 D 317
REMARK 3 ORIGIN FOR THE GROUP (A): -3.9300 42.1580 90.8450
REMARK 3 T TENSOR
REMARK 3 T11: 0.0592 T22: 0.0476
REMARK 3 T33: 0.0678 T12: -0.0171
REMARK 3 T13: -0.0079 T23: 0.0191
REMARK 3 L TENSOR
REMARK 3 L11: 1.2519 L22: 1.2592
REMARK 3 L33: 2.1126 L12: 0.2629
REMARK 3 L13: -0.2325 L23: 1.4362
REMARK 3 S TENSOR
REMARK 3 S11: 0.0414 S12: -0.0323 S13: 0.0847
REMARK 3 S21: -0.1417 S22: -0.0054 S23: -0.0433
REMARK 3 S31: -0.2876 S32: 0.0657 S33: -0.0360
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 1 E 20
REMARK 3 ORIGIN FOR THE GROUP (A): 21.8030 -6.2120 76.2150
REMARK 3 T TENSOR
REMARK 3 T11: 0.0293 T22: 0.0827
REMARK 3 T33: 0.1017 T12: 0.0009
REMARK 3 T13: -0.0218 T23: 0.0228
REMARK 3 L TENSOR
REMARK 3 L11: 1.1867 L22: 6.1051
REMARK 3 L33: 1.3972 L12: 1.1826
REMARK 3 L13: -0.0829 L23: -0.1066
REMARK 3 S TENSOR
REMARK 3 S11: 0.0456 S12: -0.0813 S13: 0.0136
REMARK 3 S21: 0.0701 S22: -0.0597 S23: -0.3114
REMARK 3 S31: -0.0590 S32: 0.2101 S33: 0.0141
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 21 E 38
REMARK 3 ORIGIN FOR THE GROUP (A): 6.9710 -29.1610 63.0970
REMARK 3 T TENSOR
REMARK 3 T11: 0.1082 T22: 0.0326
REMARK 3 T33: 0.1986 T12: 0.0222
REMARK 3 T13: 0.0266 T23: -0.0231
REMARK 3 L TENSOR
REMARK 3 L11: 4.9273 L22: 1.6931
REMARK 3 L33: 10.2748 L12: 0.6554
REMARK 3 L13: 6.4837 L23: -0.6435
REMARK 3 S TENSOR
REMARK 3 S11: 0.1681 S12: -0.1631 S13: -0.2728
REMARK 3 S21: -0.1077 S22: 0.0233 S23: 0.0431
REMARK 3 S31: 0.3804 S32: -0.3120 S33: -0.1915
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 : E 39 E 75
REMARK 3 ORIGIN FOR THE GROUP (A): -3.8290 -11.9800 47.4060
REMARK 3 T TENSOR
REMARK 3 T11: 0.1136 T22: 0.0957
REMARK 3 T33: 0.0620 T12: -0.0069
REMARK 3 T13: -0.0263 T23: -0.0414
REMARK 3 L TENSOR
REMARK 3 L11: 1.0583 L22: 4.7718
REMARK 3 L33: 2.0025 L12: 0.2370
REMARK 3 L13: -0.2696 L23: -2.8077
REMARK 3 S TENSOR
REMARK 3 S11: -0.0328 S12: 0.1420 S13: -0.0660
REMARK 3 S21: -0.2717 S22: 0.0907 S23: 0.2451
REMARK 3 S31: 0.1578 S32: -0.0441 S33: -0.0580
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 : E 76 E 97
REMARK 3 ORIGIN FOR THE GROUP (A): 3.9040 -5.9610 50.8790
REMARK 3 T TENSOR
REMARK 3 T11: 0.0771 T22: 0.0648
REMARK 3 T33: 0.0749 T12: -0.0130
REMARK 3 T13: -0.0048 T23: -0.0267
REMARK 3 L TENSOR
REMARK 3 L11: 1.6492 L22: 1.3495
REMARK 3 L33: 3.2607 L12: -0.2651
REMARK 3 L13: -1.1134 L23: 0.0323
REMARK 3 S TENSOR
REMARK 3 S11: 0.0846 S12: 0.1641 S13: 0.0616
REMARK 3 S21: -0.2273 S22: -0.0082 S23: -0.0249
REMARK 3 S31: -0.1547 S32: 0.0581 S33: -0.0763
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 : E 98 E 119
REMARK 3 ORIGIN FOR THE GROUP (A): 3.5150 -4.5290 50.4550
REMARK 3 T TENSOR
REMARK 3 T11: 0.1010 T22: 0.0521
REMARK 3 T33: 0.0589 T12: 0.0072
REMARK 3 T13: -0.0030 T23: -0.0248
REMARK 3 L TENSOR
REMARK 3 L11: 0.6523 L22: 1.5823
REMARK 3 L33: 1.0701 L12: -0.1669
REMARK 3 L13: 0.2547 L23: -1.1933
REMARK 3 S TENSOR
REMARK 3 S11: -0.0220 S12: 0.0230 S13: 0.0371
REMARK 3 S21: 0.0695 S22: 0.0053 S23: 0.0155
REMARK 3 S31: -0.0005 S32: 0.0059 S33: 0.0168
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 : E 120 E 243
REMARK 3 ORIGIN FOR THE GROUP (A): 4.9690 -15.0770 66.5490
REMARK 3 T TENSOR
REMARK 3 T11: 0.0512 T22: 0.0110
REMARK 3 T33: 0.0853 T12: 0.0192
REMARK 3 T13: -0.0105 T23: -0.0085
REMARK 3 L TENSOR
REMARK 3 L11: 0.9132 L22: 0.4746
REMARK 3 L33: 1.8414 L12: 0.1888
REMARK 3 L13: -0.4683 L23: 0.1524
REMARK 3 S TENSOR
REMARK 3 S11: -0.0047 S12: 0.0422 S13: -0.0726
REMARK 3 S21: -0.0684 S22: -0.0384 S23: -0.0128
REMARK 3 S31: 0.0778 S32: 0.0029 S33: 0.0432
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 : E 244 E 286
REMARK 3 ORIGIN FOR THE GROUP (A): 16.9540 -11.9540 67.6690
REMARK 3 T TENSOR
REMARK 3 T11: 0.0393 T22: 0.0423
REMARK 3 T33: 0.0958 T12: 0.0163
REMARK 3 T13: 0.0065 T23: 0.0129
REMARK 3 L TENSOR
REMARK 3 L11: 0.5794 L22: 1.1539
REMARK 3 L33: 0.7266 L12: 0.6318
REMARK 3 L13: -0.0423 L23: -0.6234
REMARK 3 S TENSOR
REMARK 3 S11: 0.0060 S12: 0.0463 S13: -0.0475
REMARK 3 S21: -0.0735 S22: -0.0772 S23: -0.0932
REMARK 3 S31: 0.0929 S32: 0.1598 S33: 0.0712
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 : E 287 E 317
REMARK 3 ORIGIN FOR THE GROUP (A): 18.5860 0.1300 58.2700
REMARK 3 T TENSOR
REMARK 3 T11: 0.0536 T22: 0.1088
REMARK 3 T33: 0.1005 T12: -0.0137
REMARK 3 T13: 0.0027 T23: -0.0060
REMARK 3 L TENSOR
REMARK 3 L11: 0.1636 L22: 1.5329
REMARK 3 L33: 2.9784 L12: 0.3005
REMARK 3 L13: 0.3618 L23: 1.2072
REMARK 3 S TENSOR
REMARK 3 S11: -0.0466 S12: 0.1180 S13: -0.0391
REMARK 3 S21: -0.2158 S22: 0.0921 S23: -0.0636
REMARK 3 S31: -0.1072 S32: 0.2496 S33: -0.0456
REMARK 3
REMARK 3 TLS GROUP : 37
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : F 1 F 20
REMARK 3 ORIGIN FOR THE GROUP (A): -16.5930 24.3590 63.6030
REMARK 3 T TENSOR
REMARK 3 T11: 0.0736 T22: 0.1790
REMARK 3 T33: 0.1834 T12: 0.0018
REMARK 3 T13: 0.0125 T23: -0.0377
REMARK 3 L TENSOR
REMARK 3 L11: 1.6574 L22: 3.9764
REMARK 3 L33: 1.5408 L12: 0.9063
REMARK 3 L13: 0.5895 L23: 0.2042
REMARK 3 S TENSOR
REMARK 3 S11: -0.0334 S12: -0.1597 S13: -0.0670
REMARK 3 S21: 0.0420 S22: -0.0371 S23: 0.4321
REMARK 3 S31: 0.1372 S32: -0.3532 S33: 0.0704
REMARK 3
REMARK 3 TLS GROUP : 38
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : F 21 F 39
REMARK 3 ORIGIN FOR THE GROUP (A): 4.3470 42.1230 49.4390
REMARK 3 T TENSOR
REMARK 3 T11: 0.1546 T22: 0.0754
REMARK 3 T33: 0.1013 T12: -0.0245
REMARK 3 T13: -0.0331 T23: 0.0206
REMARK 3 L TENSOR
REMARK 3 L11: 10.0621 L22: 3.7415
REMARK 3 L33: 3.6081 L12: -3.3568
REMARK 3 L13: -4.2571 L23: 2.1819
REMARK 3 S TENSOR
REMARK 3 S11: 0.2868 S12: -0.1661 S13: 0.5233
REMARK 3 S21: -0.3630 S22: 0.0289 S23: -0.1373
REMARK 3 S31: -0.4250 S32: 0.2140 S33: -0.3158
REMARK 3
REMARK 3 TLS GROUP : 39
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : F 40 F 78
REMARK 3 ORIGIN FOR THE GROUP (A): 17.6110 20.1320 44.9910
REMARK 3 T TENSOR
REMARK 3 T11: 0.0782 T22: 0.1242
REMARK 3 T33: 0.0582 T12: -0.0180
REMARK 3 T13: 0.0126 T23: 0.0274
REMARK 3 L TENSOR
REMARK 3 L11: 1.0261 L22: 6.9510
REMARK 3 L33: 0.7917 L12: -0.8367
REMARK 3 L13: -0.3377 L23: 0.9240
REMARK 3 S TENSOR
REMARK 3 S11: -0.0293 S12: 0.1282 S13: -0.0105
REMARK 3 S21: -0.2687 S22: 0.0030 S23: -0.3785
REMARK 3 S31: -0.0504 S32: 0.1323 S33: 0.0264
REMARK 3
REMARK 3 TLS GROUP : 40
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : F 79 F 116
REMARK 3 ORIGIN FOR THE GROUP (A): 8.8040 15.5950 48.4470
REMARK 3 T TENSOR
REMARK 3 T11: 0.0620 T22: 0.0932
REMARK 3 T33: 0.0637 T12: 0.0004
REMARK 3 T13: -0.0100 T23: 0.0287
REMARK 3 L TENSOR
REMARK 3 L11: 0.5489 L22: 2.5030
REMARK 3 L33: 1.7395 L12: -0.1148
REMARK 3 L13: 0.1689 L23: 2.0083
REMARK 3 S TENSOR
REMARK 3 S11: 0.0109 S12: 0.0910 S13: -0.0161
REMARK 3 S21: 0.0347 S22: -0.0138 S23: 0.0118
REMARK 3 S31: 0.0459 S32: 0.0379 S33: 0.0029
REMARK 3
REMARK 3 TLS GROUP : 41
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : F 117 F 243
REMARK 3 ORIGIN FOR THE GROUP (A): 3.3930 30.3720 58.2660
REMARK 3 T TENSOR
REMARK 3 T11: 0.0457 T22: 0.0265
REMARK 3 T33: 0.0739 T12: 0.0063
REMARK 3 T13: -0.0289 T23: 0.0314
REMARK 3 L TENSOR
REMARK 3 L11: 0.6691 L22: 0.6442
REMARK 3 L33: 1.7916 L12: 0.2408
REMARK 3 L13: 0.1511 L23: 0.4958
REMARK 3 S TENSOR
REMARK 3 S11: 0.0018 S12: 0.0433 S13: 0.0544
REMARK 3 S21: -0.0768 S22: -0.0214 S23: 0.0383
REMARK 3 S31: -0.0568 S32: 0.0273 S33: 0.0195
REMARK 3
REMARK 3 TLS GROUP : 42
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : F 244 F 317
REMARK 3 ORIGIN FOR THE GROUP (A): -8.1780 20.6520 53.8340
REMARK 3 T TENSOR
REMARK 3 T11: 0.0620 T22: 0.0683
REMARK 3 T33: 0.0885 T12: -0.0021
REMARK 3 T13: -0.0364 T23: 0.0195
REMARK 3 L TENSOR
REMARK 3 L11: 0.3755 L22: 1.1514
REMARK 3 L33: 0.4675 L12: 0.2833
REMARK 3 L13: -0.0622 L23: 0.2501
REMARK 3 S TENSOR
REMARK 3 S11: -0.0072 S12: 0.0660 S13: 0.0057
REMARK 3 S21: -0.1196 S22: -0.0481 S23: 0.0793
REMARK 3 S31: 0.0143 S32: -0.0903 S33: 0.0552
REMARK 3
REMARK 3 TLS GROUP : 43
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : G 1 G 20
REMARK 3 ORIGIN FOR THE GROUP (A): 20.4830 -24.2710 19.7590
REMARK 3 T TENSOR
REMARK 3 T11: 0.1229 T22: 0.2473
REMARK 3 T33: 0.1892 T12: 0.0102
REMARK 3 T13: -0.0295 T23: -0.0115
REMARK 3 L TENSOR
REMARK 3 L11: 1.2898 L22: 5.8017
REMARK 3 L33: 0.4577 L12: -0.9829
REMARK 3 L13: -0.1300 L23: -0.8638
REMARK 3 S TENSOR
REMARK 3 S11: 0.0504 S12: -0.0752 S13: 0.0361
REMARK 3 S21: 0.0547 S22: 0.0075 S23: 0.5627
REMARK 3 S31: -0.1050 S32: -0.2096 S33: -0.0579
REMARK 3
REMARK 3 TLS GROUP : 44
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : G 21 G 38
REMARK 3 ORIGIN FOR THE GROUP (A): 41.4720 -42.3130 32.1040
REMARK 3 T TENSOR
REMARK 3 T11: 0.2232 T22: 0.1661
REMARK 3 T33: 0.1330 T12: 0.0176
REMARK 3 T13: -0.0080 T23: 0.0715
REMARK 3 L TENSOR
REMARK 3 L11: 8.3632 L22: 1.8628
REMARK 3 L33: 1.6479 L12: 1.9811
REMARK 3 L13: 3.0445 L23: 1.3643
REMARK 3 S TENSOR
REMARK 3 S11: 0.0858 S12: 0.0538 S13: -0.4274
REMARK 3 S21: 0.1000 S22: 0.0540 S23: -0.0996
REMARK 3 S31: 0.2320 S32: 0.1768 S33: -0.1398
REMARK 3
REMARK 3 TLS GROUP : 45
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : G 39 G 75
REMARK 3 ORIGIN FOR THE GROUP (A): 56.1330 -21.5090 35.3200
REMARK 3 T TENSOR
REMARK 3 T11: 0.0971 T22: 0.1714
REMARK 3 T33: 0.0914 T12: 0.0277
REMARK 3 T13: -0.0438 T23: 0.0446
REMARK 3 L TENSOR
REMARK 3 L11: 0.7364 L22: 7.5966
REMARK 3 L33: 1.0631 L12: 0.3904
REMARK 3 L13: 0.0538 L23: 1.8962
REMARK 3 S TENSOR
REMARK 3 S11: 0.0325 S12: -0.1917 S13: -0.0416
REMARK 3 S21: 0.2115 S22: -0.0460 S23: -0.3920
REMARK 3 S31: 0.0979 S32: 0.0825 S33: 0.0136
REMARK 3
REMARK 3 TLS GROUP : 46
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : G 76 G 97
REMARK 3 ORIGIN FOR THE GROUP (A): 47.1330 -16.5630 33.6560
REMARK 3 T TENSOR
REMARK 3 T11: 0.2817 T22: 0.1375
REMARK 3 T33: 0.1020 T12: 0.0259
REMARK 3 T13: -0.0431 T23: 0.0270
REMARK 3 L TENSOR
REMARK 3 L11: 1.0270 L22: 0.8590
REMARK 3 L33: 0.9203 L12: 0.2489
REMARK 3 L13: -0.4997 L23: 0.5289
REMARK 3 S TENSOR
REMARK 3 S11: 0.0972 S12: -0.2336 S13: 0.0377
REMARK 3 S21: -0.0374 S22: -0.0390 S23: -0.0756
REMARK 3 S31: -0.2944 S32: 0.0956 S33: -0.0582
REMARK 3
REMARK 3 TLS GROUP : 47
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : G 98 G 119
REMARK 3 ORIGIN FOR THE GROUP (A): 47.5340 -15.1050 33.3880
REMARK 3 T TENSOR
REMARK 3 T11: 0.1228 T22: 0.1351
REMARK 3 T33: 0.0542 T12: 0.0134
REMARK 3 T13: -0.0285 T23: 0.0444
REMARK 3 L TENSOR
REMARK 3 L11: 1.0266 L22: 2.9231
REMARK 3 L33: 0.7100 L12: 0.3556
REMARK 3 L13: -0.1509 L23: 1.3270
REMARK 3 S TENSOR
REMARK 3 S11: 0.0075 S12: -0.0274 S13: 0.0430
REMARK 3 S21: -0.0209 S22: -0.0081 S23: 0.0656
REMARK 3 S31: 0.0042 S32: -0.0202 S33: 0.0005
REMARK 3
REMARK 3 TLS GROUP : 48
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : G 120 G 226
REMARK 3 ORIGIN FOR THE GROUP (A): 41.2630 -28.6790 26.4760
REMARK 3 T TENSOR
REMARK 3 T11: 0.0809 T22: 0.0924
REMARK 3 T33: 0.0937 T12: -0.0019
REMARK 3 T13: -0.0030 T23: 0.0590
REMARK 3 L TENSOR
REMARK 3 L11: 0.6615 L22: 0.6055
REMARK 3 L33: 1.5218 L12: -0.2226
REMARK 3 L13: 0.0693 L23: 0.3970
REMARK 3 S TENSOR
REMARK 3 S11: 0.0000 S12: -0.0846 S13: -0.0452
REMARK 3 S21: 0.0958 S22: 0.0049 S23: -0.0247
REMARK 3 S31: 0.0253 S32: -0.0021 S33: -0.0049
REMARK 3
REMARK 3 TLS GROUP : 49
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : G 227 G 243
REMARK 3 ORIGIN FOR THE GROUP (A): 36.6240 -39.4320 8.6650
REMARK 3 T TENSOR
REMARK 3 T11: 0.1377 T22: 0.0836
REMARK 3 T33: 0.1718 T12: -0.0051
REMARK 3 T13: -0.0338 T23: 0.0318
REMARK 3 L TENSOR
REMARK 3 L11: 0.6888 L22: 2.0116
REMARK 3 L33: 9.7811 L12: 0.2759
REMARK 3 L13: -2.2401 L23: 1.2272
REMARK 3 S TENSOR
REMARK 3 S11: -0.2438 S12: 0.0630 S13: -0.0703
REMARK 3 S21: -0.1707 S22: 0.1343 S23: -0.0317
REMARK 3 S31: 0.7801 S32: -0.0931 S33: 0.1096
REMARK 3
REMARK 3 TLS GROUP : 50
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : G 244 G 286
REMARK 3 ORIGIN FOR THE GROUP (A): 28.9390 -27.0850 26.8300
REMARK 3 T TENSOR
REMARK 3 T11: 0.0796 T22: 0.1532
REMARK 3 T33: 0.1126 T12: -0.0040
REMARK 3 T13: 0.0078 T23: 0.0452
REMARK 3 L TENSOR
REMARK 3 L11: 0.6899 L22: 1.5545
REMARK 3 L33: 0.3274 L12: -0.5603
REMARK 3 L13: 0.1515 L23: 0.4380
REMARK 3 S TENSOR
REMARK 3 S11: -0.0123 S12: -0.1037 S13: -0.0350
REMARK 3 S21: 0.1675 S22: -0.0651 S23: 0.1510
REMARK 3 S31: 0.0689 S32: -0.1009 S33: 0.0774
REMARK 3
REMARK 3 TLS GROUP : 51
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : G 287 G 317
REMARK 3 ORIGIN FOR THE GROUP (A): 30.2210 -12.4790 31.5610
REMARK 3 T TENSOR
REMARK 3 T11: 0.1001 T22: 0.1834
REMARK 3 T33: 0.0971 T12: 0.0290
REMARK 3 T13: -0.0082 T23: 0.0196
REMARK 3 L TENSOR
REMARK 3 L11: 0.6395 L22: 1.1937
REMARK 3 L33: 2.0908 L12: -0.2957
REMARK 3 L13: 1.1113 L23: -0.6246
REMARK 3 S TENSOR
REMARK 3 S11: -0.0677 S12: -0.1823 S13: 0.0391
REMARK 3 S21: 0.1866 S22: 0.0195 S23: -0.0337
REMARK 3 S31: -0.1019 S32: -0.1875 S33: 0.0481
REMARK 3
REMARK 3 TLS GROUP : 52
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : H 1 H 20
REMARK 3 ORIGIN FOR THE GROUP (A): 57.9910 6.3200 4.4730
REMARK 3 T TENSOR
REMARK 3 T11: 0.0552 T22: 0.1565
REMARK 3 T33: 0.1454 T12: 0.0220
REMARK 3 T13: -0.0010 T23: 0.0116
REMARK 3 L TENSOR
REMARK 3 L11: 1.1612 L22: 4.5840
REMARK 3 L33: 1.5981 L12: -0.5441
REMARK 3 L13: -0.1362 L23: -0.0203
REMARK 3 S TENSOR
REMARK 3 S11: 0.0270 S12: 0.0608 S13: -0.1019
REMARK 3 S21: -0.2321 S22: -0.0064 S23: -0.2730
REMARK 3 S31: 0.1303 S32: 0.2063 S33: -0.0206
REMARK 3
REMARK 3 TLS GROUP : 53
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : H 21 H 37
REMARK 3 ORIGIN FOR THE GROUP (A): 44.4240 29.3200 18.0390
REMARK 3 T TENSOR
REMARK 3 T11: 0.1539 T22: 0.0935
REMARK 3 T33: 0.1415 T12: -0.0123
REMARK 3 T13: -0.0381 T23: -0.0121
REMARK 3 L TENSOR
REMARK 3 L11: 2.4928 L22: 1.8478
REMARK 3 L33: 6.7733 L12: 0.6702
REMARK 3 L13: -3.3024 L23: -2.0580
REMARK 3 S TENSOR
REMARK 3 S11: 0.2998 S12: 0.0487 S13: 0.3794
REMARK 3 S21: 0.1665 S22: 0.0177 S23: -0.0324
REMARK 3 S31: -0.5621 S32: -0.3281 S33: -0.3176
REMARK 3
REMARK 3 TLS GROUP : 54
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : H 38 H 75
REMARK 3 ORIGIN FOR THE GROUP (A): 34.3400 12.4290 34.8150
REMARK 3 T TENSOR
REMARK 3 T11: 0.1351 T22: 0.1600
REMARK 3 T33: 0.1105 T12: 0.0184
REMARK 3 T13: 0.0051 T23: -0.0449
REMARK 3 L TENSOR
REMARK 3 L11: 0.4801 L22: 5.3126
REMARK 3 L33: 2.6267 L12: -0.6051
REMARK 3 L13: 0.3010 L23: -3.4991
REMARK 3 S TENSOR
REMARK 3 S11: -0.0653 S12: -0.1677 S13: 0.0615
REMARK 3 S21: 0.3636 S22: 0.0663 S23: 0.1969
REMARK 3 S31: -0.1765 S32: -0.0524 S33: -0.0010
REMARK 3
REMARK 3 TLS GROUP : 55
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : H 76 H 97
REMARK 3 ORIGIN FOR THE GROUP (A): 41.8280 6.0550 30.9790
REMARK 3 T TENSOR
REMARK 3 T11: 0.2008 T22: 0.1499
REMARK 3 T33: 0.0935 T12: 0.0230
REMARK 3 T13: -0.0215 T23: -0.0258
REMARK 3 L TENSOR
REMARK 3 L11: 1.7245 L22: 1.0116
REMARK 3 L33: 3.6599 L12: 0.5544
REMARK 3 L13: 1.8007 L23: -0.0829
REMARK 3 S TENSOR
REMARK 3 S11: 0.1351 S12: -0.2207 S13: -0.0188
REMARK 3 S21: 0.3020 S22: -0.0668 S23: 0.0119
REMARK 3 S31: 0.3016 S32: -0.0876 S33: -0.0683
REMARK 3
REMARK 3 TLS GROUP : 56
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : H 98 H 119
REMARK 3 ORIGIN FOR THE GROUP (A): 41.4630 4.6300 31.4310
REMARK 3 T TENSOR
REMARK 3 T11: 0.0894 T22: 0.1258
REMARK 3 T33: 0.0821 T12: -0.0037
REMARK 3 T13: -0.0246 T23: -0.0344
REMARK 3 L TENSOR
REMARK 3 L11: 0.8295 L22: 1.0263
REMARK 3 L33: 2.7680 L12: -0.0768
REMARK 3 L13: 0.2733 L23: -0.8892
REMARK 3 S TENSOR
REMARK 3 S11: -0.0095 S12: 0.0423 S13: -0.1052
REMARK 3 S21: 0.0893 S22: 0.0401 S23: 0.0422
REMARK 3 S31: 0.0273 S32: -0.0415 S33: -0.0307
REMARK 3
REMARK 3 TLS GROUP : 57
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : H 120 H 243
REMARK 3 ORIGIN FOR THE GROUP (A): 41.8100 15.1430 15.2500
REMARK 3 T TENSOR
REMARK 3 T11: 0.0548 T22: 0.0417
REMARK 3 T33: 0.1007 T12: -0.0201
REMARK 3 T13: -0.0042 T23: -0.0145
REMARK 3 L TENSOR
REMARK 3 L11: 1.0252 L22: 0.7040
REMARK 3 L33: 1.4136 L12: -0.1698
REMARK 3 L13: 0.4547 L23: 0.0859
REMARK 3 S TENSOR
REMARK 3 S11: 0.0026 S12: -0.0589 S13: 0.0778
REMARK 3 S21: 0.0563 S22: -0.0191 S23: -0.0311
REMARK 3 S31: -0.0783 S32: -0.0012 S33: 0.0166
REMARK 3
REMARK 3 TLS GROUP : 58
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : H 244 H 286
REMARK 3 ORIGIN FOR THE GROUP (A): 53.7090 12.0580 13.3270
REMARK 3 T TENSOR
REMARK 3 T11: 0.0629 T22: 0.0840
REMARK 3 T33: 0.1121 T12: -0.0092
REMARK 3 T13: -0.0223 T23: -0.0115
REMARK 3 L TENSOR
REMARK 3 L11: 0.5652 L22: 0.7573
REMARK 3 L33: 0.6842 L12: -0.5089
REMARK 3 L13: 0.0151 L23: -0.4622
REMARK 3 S TENSOR
REMARK 3 S11: 0.0134 S12: -0.0219 S13: 0.0692
REMARK 3 S21: 0.0510 S22: -0.0730 S23: -0.1012
REMARK 3 S31: -0.0804 S32: 0.1594 S33: 0.0596
REMARK 3
REMARK 3 TLS GROUP : 59
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : H 287 H 317
REMARK 3 ORIGIN FOR THE GROUP (A): 56.0000 -0.0030 22.6160
REMARK 3 T TENSOR
REMARK 3 T11: 0.0831 T22: 0.1545
REMARK 3 T33: 0.1206 T12: 0.0339
REMARK 3 T13: -0.0341 T23: -0.0252
REMARK 3 L TENSOR
REMARK 3 L11: 0.2725 L22: 1.9311
REMARK 3 L33: 2.7524 L12: 0.3968
REMARK 3 L13: 0.1144 L23: 1.0196
REMARK 3 S TENSOR
REMARK 3 S11: -0.0148 S12: -0.1517 S13: 0.0389
REMARK 3 S21: 0.2050 S22: 0.0485 S23: -0.1081
REMARK 3 S31: 0.0789 S32: 0.1635 S33: -0.0336
REMARK 3
REMARK 3 TLS GROUP : 60
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : I 1 I 19
REMARK 3 ORIGIN FOR THE GROUP (A): 16.6020 -31.6630 -2.1530
REMARK 3 T TENSOR
REMARK 3 T11: 0.0668 T22: 0.1262
REMARK 3 T33: 0.0815 T12: 0.0145
REMARK 3 T13: 0.0394 T23: 0.0190
REMARK 3 L TENSOR
REMARK 3 L11: 3.0888 L22: 2.4293
REMARK 3 L33: 4.1095 L12: 0.3525
REMARK 3 L13: 1.1729 L23: -0.3410
REMARK 3 S TENSOR
REMARK 3 S11: 0.0018 S12: -0.5153 S13: -0.1290
REMARK 3 S21: 0.3362 S22: 0.0363 S23: 0.0027
REMARK 3 S31: 0.0107 S32: -0.1882 S33: -0.0382
REMARK 3
REMARK 3 TLS GROUP : 61
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : I 20 I 38
REMARK 3 ORIGIN FOR THE GROUP (A): 13.3880 -33.1120 -32.4570
REMARK 3 T TENSOR
REMARK 3 T11: 0.1093 T22: 0.0998
REMARK 3 T33: 0.0974 T12: 0.0011
REMARK 3 T13: -0.0304 T23: -0.0183
REMARK 3 L TENSOR
REMARK 3 L11: 6.5653 L22: 1.3737
REMARK 3 L33: 4.5036 L12: -1.5113
REMARK 3 L13: -3.9984 L23: 0.9010
REMARK 3 S TENSOR
REMARK 3 S11: 0.0758 S12: 0.6101 S13: -0.2064
REMARK 3 S21: -0.2415 S22: -0.1806 S23: 0.1154
REMARK 3 S31: -0.2632 S32: -0.5285 S33: 0.1049
REMARK 3
REMARK 3 TLS GROUP : 62
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : I 39 I 75
REMARK 3 ORIGIN FOR THE GROUP (A): 39.0470 -36.2270 -34.0910
REMARK 3 T TENSOR
REMARK 3 T11: 0.1149 T22: 0.0774
REMARK 3 T33: 0.0947 T12: -0.0237
REMARK 3 T13: 0.0411 T23: -0.0238
REMARK 3 L TENSOR
REMARK 3 L11: 4.3301 L22: 1.3604
REMARK 3 L33: 1.3142 L12: -1.8768
REMARK 3 L13: 1.6752 L23: -0.8164
REMARK 3 S TENSOR
REMARK 3 S11: 0.1045 S12: 0.3615 S13: 0.0003
REMARK 3 S21: -0.2269 S22: -0.1160 S23: -0.1245
REMARK 3 S31: 0.1118 S32: 0.1555 S33: 0.0116
REMARK 3
REMARK 3 TLS GROUP : 63
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : I 76 I 97
REMARK 3 ORIGIN FOR THE GROUP (A): 37.9110 -38.3670 -23.9730
REMARK 3 T TENSOR
REMARK 3 T11: 0.0879 T22: 0.0807
REMARK 3 T33: 0.1173 T12: 0.0053
REMARK 3 T13: 0.0110 T23: -0.0072
REMARK 3 L TENSOR
REMARK 3 L11: 1.3529 L22: 1.9989
REMARK 3 L33: 0.7353 L12: -0.5951
REMARK 3 L13: 0.1984 L23: 0.2860
REMARK 3 S TENSOR
REMARK 3 S11: -0.0350 S12: 0.0525 S13: -0.0924
REMARK 3 S21: 0.1276 S22: 0.1029 S23: -0.3001
REMARK 3 S31: 0.1743 S32: 0.1267 S33: -0.0680
REMARK 3
REMARK 3 TLS GROUP : 64
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : I 98 I 119
REMARK 3 ORIGIN FOR THE GROUP (A): 39.3400 -38.3080 -23.4020
REMARK 3 T TENSOR
REMARK 3 T11: 0.0375 T22: 0.0526
REMARK 3 T33: 0.0768 T12: -0.0231
REMARK 3 T13: 0.0124 T23: -0.0134
REMARK 3 L TENSOR
REMARK 3 L11: 1.8429 L22: 1.9748
REMARK 3 L33: 0.5218 L12: -0.4018
REMARK 3 L13: 0.0017 L23: -0.3357
REMARK 3 S TENSOR
REMARK 3 S11: 0.0430 S12: -0.0880 S13: -0.0235
REMARK 3 S21: -0.0247 S22: -0.0089 S23: -0.1283
REMARK 3 S31: -0.0176 S32: 0.1209 S33: -0.0342
REMARK 3
REMARK 3 TLS GROUP : 65
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : I 120 I 243
REMARK 3 ORIGIN FOR THE GROUP (A): 22.9010 -28.1970 -22.7260
REMARK 3 T TENSOR
REMARK 3 T11: 0.0162 T22: 0.0447
REMARK 3 T33: 0.0472 T12: -0.0246
REMARK 3 T13: -0.0057 T23: 0.0061
REMARK 3 L TENSOR
REMARK 3 L11: 0.6975 L22: 1.7600
REMARK 3 L33: 0.8336 L12: -0.3610
REMARK 3 L13: -0.1264 L23: 0.1803
REMARK 3 S TENSOR
REMARK 3 S11: 0.0091 S12: 0.0339 S13: -0.0466
REMARK 3 S21: -0.0698 S22: 0.0164 S23: 0.0160
REMARK 3 S31: 0.0178 S32: -0.0235 S33: -0.0255
REMARK 3
REMARK 3 TLS GROUP : 66
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : I 244 I 286
REMARK 3 ORIGIN FOR THE GROUP (A): 18.8580 -35.1530 -13.2410
REMARK 3 T TENSOR
REMARK 3 T11: 0.0265 T22: 0.0479
REMARK 3 T33: 0.0688 T12: -0.0106
REMARK 3 T13: 0.0041 T23: 0.0175
REMARK 3 L TENSOR
REMARK 3 L11: 0.8340 L22: 1.2008
REMARK 3 L33: 1.0726 L12: -0.6407
REMARK 3 L13: 0.2519 L23: -0.6383
REMARK 3 S TENSOR
REMARK 3 S11: -0.0105 S12: 0.0135 S13: -0.1354
REMARK 3 S21: 0.0736 S22: 0.0148 S23: 0.1072
REMARK 3 S31: 0.0751 S32: -0.0683 S33: -0.0043
REMARK 3
REMARK 3 TLS GROUP : 67
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : I 287 I 317
REMARK 3 ORIGIN FOR THE GROUP (A): 31.5190 -42.2490 -8.1270
REMARK 3 T TENSOR
REMARK 3 T11: 0.0665 T22: 0.0557
REMARK 3 T33: 0.1138 T12: 0.0141
REMARK 3 T13: -0.0043 T23: 0.0264
REMARK 3 L TENSOR
REMARK 3 L11: 1.2556 L22: 1.3083
REMARK 3 L33: 2.7049 L12: -0.1266
REMARK 3 L13: 0.0530 L23: 1.7946
REMARK 3 S TENSOR
REMARK 3 S11: 0.0523 S12: 0.0492 S13: -0.1305
REMARK 3 S21: 0.1324 S22: 0.0199 S23: -0.1204
REMARK 3 S31: 0.2495 S32: 0.0700 S33: -0.0721
REMARK 3
REMARK 3 TLS GROUP : 68
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : J 1 J 19
REMARK 3 ORIGIN FOR THE GROUP (A): 62.6810 -12.6850 -9.6360
REMARK 3 T TENSOR
REMARK 3 T11: 0.1685 T22: 0.0729
REMARK 3 T33: 0.2010 T12: -0.0359
REMARK 3 T13: 0.0081 T23: 0.0399
REMARK 3 L TENSOR
REMARK 3 L11: 4.0101 L22: 2.1881
REMARK 3 L33: 3.8927 L12: -1.8532
REMARK 3 L13: 1.7452 L23: -1.0017
REMARK 3 S TENSOR
REMARK 3 S11: 0.0015 S12: 0.2730 S13: 0.3354
REMARK 3 S21: -0.2897 S22: -0.0511 S23: -0.0823
REMARK 3 S31: -0.3361 S32: 0.0153 S33: 0.0495
REMARK 3
REMARK 3 TLS GROUP : 69
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : J 20 J 38
REMARK 3 ORIGIN FOR THE GROUP (A): 73.4050 -34.7110 8.5670
REMARK 3 T TENSOR
REMARK 3 T11: 0.0818 T22: 0.1087
REMARK 3 T33: 0.1506 T12: 0.0353
REMARK 3 T13: -0.0144 T23: -0.0146
REMARK 3 L TENSOR
REMARK 3 L11: 2.3819 L22: 9.7819
REMARK 3 L33: 1.7911 L12: 3.0260
REMARK 3 L13: 0.2677 L23: -1.8136
REMARK 3 S TENSOR
REMARK 3 S11: 0.0603 S12: -0.1579 S13: -0.1620
REMARK 3 S21: 0.4971 S22: -0.0664 S23: -0.3941
REMARK 3 S31: 0.0731 S32: 0.0940 S33: 0.0061
REMARK 3
REMARK 3 TLS GROUP : 70
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : J 39 J 75
REMARK 3 ORIGIN FOR THE GROUP (A): 53.6700 -49.5120 0.7080
REMARK 3 T TENSOR
REMARK 3 T11: 0.0588 T22: 0.0433
REMARK 3 T33: 0.1510 T12: 0.0116
REMARK 3 T13: 0.0141 T23: 0.0226
REMARK 3 L TENSOR
REMARK 3 L11: 2.7243 L22: 1.4133
REMARK 3 L33: 3.5383 L12: 0.9087
REMARK 3 L13: 2.7356 L23: 0.9815
REMARK 3 S TENSOR
REMARK 3 S11: 0.1289 S12: -0.0754 S13: -0.3020
REMARK 3 S21: 0.1259 S22: 0.0215 S23: -0.0727
REMARK 3 S31: 0.2577 S32: -0.0124 S33: -0.1504
REMARK 3
REMARK 3 TLS GROUP : 71
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : J 76 J 97
REMARK 3 ORIGIN FOR THE GROUP (A): 53.2200 -42.3080 -6.7800
REMARK 3 T TENSOR
REMARK 3 T11: 0.1147 T22: 0.0589
REMARK 3 T33: 0.1695 T12: 0.0312
REMARK 3 T13: -0.0176 T23: -0.0198
REMARK 3 L TENSOR
REMARK 3 L11: 1.2304 L22: 1.0263
REMARK 3 L33: 1.4897 L12: 0.0787
REMARK 3 L13: 0.2027 L23: 0.4671
REMARK 3 S TENSOR
REMARK 3 S11: 0.0382 S12: 0.1136 S13: -0.2925
REMARK 3 S21: -0.2986 S22: -0.1192 S23: 0.1135
REMARK 3 S31: -0.0190 S32: -0.1600 S33: 0.0810
REMARK 3
REMARK 3 TLS GROUP : 72
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : J 98 J 119
REMARK 3 ORIGIN FOR THE GROUP (A): 51.8480 -42.5220 -7.4460
REMARK 3 T TENSOR
REMARK 3 T11: 0.0459 T22: 0.0503
REMARK 3 T33: 0.1451 T12: -0.0008
REMARK 3 T13: 0.0104 T23: 0.0108
REMARK 3 L TENSOR
REMARK 3 L11: 0.8979 L22: 0.6909
REMARK 3 L33: 2.5936 L12: 0.1505
REMARK 3 L13: 0.0264 L23: 0.8402
REMARK 3 S TENSOR
REMARK 3 S11: -0.0072 S12: 0.0105 S13: 0.0563
REMARK 3 S21: -0.0628 S22: -0.0442 S23: 0.0894
REMARK 3 S31: -0.1446 S32: 0.0211 S33: 0.0514
REMARK 3
REMARK 3 TLS GROUP : 73
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : J 120 J 243
REMARK 3 ORIGIN FOR THE GROUP (A): 60.6700 -29.6490 3.9060
REMARK 3 T TENSOR
REMARK 3 T11: 0.0053 T22: 0.0658
REMARK 3 T33: 0.1148 T12: 0.0041
REMARK 3 T13: -0.0172 T23: 0.0277
REMARK 3 L TENSOR
REMARK 3 L11: 0.6427 L22: 1.4488
REMARK 3 L33: 1.2702 L12: -0.2923
REMARK 3 L13: -0.1665 L23: 0.5441
REMARK 3 S TENSOR
REMARK 3 S11: -0.0180 S12: -0.0285 S13: -0.0590
REMARK 3 S21: 0.0265 S22: 0.0207 S23: -0.0735
REMARK 3 S31: -0.0111 S32: 0.0448 S33: -0.0026
REMARK 3
REMARK 3 TLS GROUP : 74
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : J 244 J 284
REMARK 3 ORIGIN FOR THE GROUP (A): 64.6720 -23.5360 -5.7690
REMARK 3 T TENSOR
REMARK 3 T11: 0.0571 T22: 0.0606
REMARK 3 T33: 0.1366 T12: -0.0077
REMARK 3 T13: 0.0164 T23: 0.0060
REMARK 3 L TENSOR
REMARK 3 L11: 0.6553 L22: 0.4018
REMARK 3 L33: 1.7865 L12: 0.1137
REMARK 3 L13: 0.4759 L23: -0.5826
REMARK 3 S TENSOR
REMARK 3 S11: -0.0646 S12: 0.0375 S13: -0.0163
REMARK 3 S21: -0.0317 S22: 0.0230 S23: -0.1056
REMARK 3 S31: -0.0742 S32: 0.0574 S33: 0.0416
REMARK 3
REMARK 3 TLS GROUP : 75
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : J 285 J 299
REMARK 3 ORIGIN FOR THE GROUP (A): 58.3510 -22.6890 -15.5810
REMARK 3 T TENSOR
REMARK 3 T11: 0.0552 T22: 0.0367
REMARK 3 T33: 0.1046 T12: -0.0056
REMARK 3 T13: 0.0214 T23: 0.0143
REMARK 3 L TENSOR
REMARK 3 L11: 4.5771 L22: 2.5459
REMARK 3 L33: 1.6935 L12: -1.9367
REMARK 3 L13: 1.8314 L23: -0.7346
REMARK 3 S TENSOR
REMARK 3 S11: 0.0402 S12: 0.3287 S13: 0.0163
REMARK 3 S21: -0.1396 S22: -0.1067 S23: -0.2842
REMARK 3 S31: 0.0799 S32: 0.0742 S33: 0.0666
REMARK 3
REMARK 3 TLS GROUP : 76
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : J 300 J 317
REMARK 3 ORIGIN FOR THE GROUP (A): 56.9840 -34.4940 -19.0660
REMARK 3 T TENSOR
REMARK 3 T11: 0.1356 T22: 0.0233
REMARK 3 T33: 0.1402 T12: -0.0179
REMARK 3 T13: 0.0378 T23: 0.0174
REMARK 3 L TENSOR
REMARK 3 L11: 7.9714 L22: 8.1315
REMARK 3 L33: 3.2216 L12: -7.9055
REMARK 3 L13: -0.1175 L23: 0.9685
REMARK 3 S TENSOR
REMARK 3 S11: 0.1415 S12: 0.1096 S13: -0.1087
REMARK 3 S21: -0.1903 S22: -0.0975 S23: 0.0313
REMARK 3 S31: 0.1123 S32: 0.0519 S33: -0.0440
REMARK 3
REMARK 3 TLS GROUP : 77
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : K 1 K 19
REMARK 3 ORIGIN FOR THE GROUP (A): 8.0520 -10.4030 4.4370
REMARK 3 T TENSOR
REMARK 3 T11: 0.1274 T22: 0.0750
REMARK 3 T33: 0.1436 T12: -0.0214
REMARK 3 T13: -0.0272 T23: 0.0435
REMARK 3 L TENSOR
REMARK 3 L11: 1.8865 L22: 2.6223
REMARK 3 L33: 4.4721 L12: -0.4436
REMARK 3 L13: -0.9186 L23: 1.8413
REMARK 3 S TENSOR
REMARK 3 S11: -0.0470 S12: 0.0360 S13: -0.3150
REMARK 3 S21: -0.0282 S22: -0.0406 S23: 0.1953
REMARK 3 S31: 0.4145 S32: 0.0051 S33: 0.0877
REMARK 3
REMARK 3 TLS GROUP : 78
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : K 20 K 38
REMARK 3 ORIGIN FOR THE GROUP (A): 5.5530 17.3350 16.9090
REMARK 3 T TENSOR
REMARK 3 T11: 0.0689 T22: 0.1458
REMARK 3 T33: 0.1164 T12: 0.0358
REMARK 3 T13: 0.0089 T23: -0.0195
REMARK 3 L TENSOR
REMARK 3 L11: 1.5402 L22: 8.8356
REMARK 3 L33: 4.7529 L12: 2.8726
REMARK 3 L13: -2.0841 L23: -3.7670
REMARK 3 S TENSOR
REMARK 3 S11: 0.1079 S12: -0.1205 S13: 0.1157
REMARK 3 S21: 0.5545 S22: 0.0408 S23: 0.0811
REMARK 3 S31: -0.3422 S32: -0.0484 S33: -0.1487
REMARK 3
REMARK 3 TLS GROUP : 79
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : K 39 K 75
REMARK 3 ORIGIN FOR THE GROUP (A): 17.9030 26.7270 -3.8070
REMARK 3 T TENSOR
REMARK 3 T11: 0.0648 T22: 0.0288
REMARK 3 T33: 0.1563 T12: 0.0118
REMARK 3 T13: 0.0073 T23: -0.0054
REMARK 3 L TENSOR
REMARK 3 L11: 0.9767 L22: 0.6042
REMARK 3 L33: 8.7294 L12: 0.1892
REMARK 3 L13: -1.9268 L23: 0.2756
REMARK 3 S TENSOR
REMARK 3 S11: 0.1193 S12: -0.0654 S13: 0.1755
REMARK 3 S21: -0.0238 S22: 0.0418 S23: -0.0379
REMARK 3 S31: -0.5259 S32: 0.0464 S33: -0.1610
REMARK 3
REMARK 3 TLS GROUP : 80
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : K 76 K 97
REMARK 3 ORIGIN FOR THE GROUP (A): 15.3150 17.4250 -7.6980
REMARK 3 T TENSOR
REMARK 3 T11: 0.2103 T22: 0.1004
REMARK 3 T33: 0.1204 T12: 0.0913
REMARK 3 T13: -0.0194 T23: 0.0011
REMARK 3 L TENSOR
REMARK 3 L11: 2.1209 L22: 0.0714
REMARK 3 L33: 2.1284 L12: 0.1191
REMARK 3 L13: 0.2206 L23: 0.2156
REMARK 3 S TENSOR
REMARK 3 S11: 0.1401 S12: 0.2608 S13: 0.2352
REMARK 3 S21: -0.0719 S22: -0.0282 S23: 0.0223
REMARK 3 S31: 0.0626 S32: 0.1052 S33: -0.1119
REMARK 3
REMARK 3 TLS GROUP : 81
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : K 98 K 119
REMARK 3 ORIGIN FOR THE GROUP (A): 16.1810 17.2800 -8.9570
REMARK 3 T TENSOR
REMARK 3 T11: 0.0440 T22: 0.0531
REMARK 3 T33: 0.0732 T12: 0.0154
REMARK 3 T13: 0.0033 T23: -0.0013
REMARK 3 L TENSOR
REMARK 3 L11: 1.1455 L22: 0.8775
REMARK 3 L33: 2.0042 L12: 0.3808
REMARK 3 L13: 0.4742 L23: -1.0038
REMARK 3 S TENSOR
REMARK 3 S11: 0.0284 S12: -0.0161 S13: -0.0769
REMARK 3 S21: -0.0346 S22: 0.0094 S23: -0.0244
REMARK 3 S31: 0.0908 S32: -0.0440 S33: -0.0378
REMARK 3
REMARK 3 TLS GROUP : 82
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : K 120 K 243
REMARK 3 ORIGIN FOR THE GROUP (A): 14.8980 9.8190 8.7880
REMARK 3 T TENSOR
REMARK 3 T11: 0.0253 T22: 0.0646
REMARK 3 T33: 0.0761 T12: 0.0077
REMARK 3 T13: 0.0242 T23: -0.0104
REMARK 3 L TENSOR
REMARK 3 L11: 0.9686 L22: 1.0746
REMARK 3 L33: 1.0076 L12: -0.3128
REMARK 3 L13: 0.4248 L23: -0.3567
REMARK 3 S TENSOR
REMARK 3 S11: 0.0293 S12: -0.1028 S13: 0.0378
REMARK 3 S21: 0.0556 S22: 0.0208 S23: 0.0269
REMARK 3 S31: -0.0311 S32: -0.0653 S33: -0.0500
REMARK 3
REMARK 3 TLS GROUP : 83
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : K 244 K 284
REMARK 3 ORIGIN FOR THE GROUP (A): 7.2820 1.2430 4.8760
REMARK 3 T TENSOR
REMARK 3 T11: 0.0193 T22: 0.0417
REMARK 3 T33: 0.0876 T12: 0.0014
REMARK 3 T13: 0.0118 T23: 0.0097
REMARK 3 L TENSOR
REMARK 3 L11: 0.5144 L22: 0.9634
REMARK 3 L33: 1.3078 L12: 0.0364
REMARK 3 L13: 0.1289 L23: 0.2360
REMARK 3 S TENSOR
REMARK 3 S11: 0.0466 S12: -0.0300 S13: -0.0531
REMARK 3 S21: -0.0054 S22: 0.0221 S23: 0.0740
REMARK 3 S31: 0.0101 S32: -0.1189 S33: -0.0686
REMARK 3
REMARK 3 TLS GROUP : 84
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : K 285 K 299
REMARK 3 ORIGIN FOR THE GROUP (A): 8.1920 -3.4230 -5.8190
REMARK 3 T TENSOR
REMARK 3 T11: 0.0419 T22: 0.0953
REMARK 3 T33: 0.0764 T12: -0.0303
REMARK 3 T13: -0.0130 T23: 0.0378
REMARK 3 L TENSOR
REMARK 3 L11: 3.4113 L22: 3.7884
REMARK 3 L33: 4.1001 L12: -3.1911
REMARK 3 L13: -2.1528 L23: 2.4618
REMARK 3 S TENSOR
REMARK 3 S11: -0.0074 S12: 0.2801 S13: -0.2396
REMARK 3 S21: -0.1140 S22: -0.0437 S23: 0.3793
REMARK 3 S31: -0.0497 S32: -0.2299 S33: 0.0511
REMARK 3
REMARK 3 TLS GROUP : 85
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : K 300 K 317
REMARK 3 ORIGIN FOR THE GROUP (A): 6.7840 6.3640 -13.2710
REMARK 3 T TENSOR
REMARK 3 T11: 0.0660 T22: 0.0550
REMARK 3 T33: 0.0959 T12: -0.0184
REMARK 3 T13: 0.0013 T23: 0.0116
REMARK 3 L TENSOR
REMARK 3 L11: 6.1434 L22: 6.7703
REMARK 3 L33: 2.4223 L12: -5.5415
REMARK 3 L13: 0.0391 L23: 0.5651
REMARK 3 S TENSOR
REMARK 3 S11: 0.0352 S12: 0.0638 S13: 0.0328
REMARK 3 S21: -0.2344 S22: -0.0398 S23: 0.2364
REMARK 3 S31: -0.1922 S32: -0.0821 S33: 0.0047
REMARK 3
REMARK 3 TLS GROUP : 86
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : L 1 L 20
REMARK 3 ORIGIN FOR THE GROUP (A): 50.2940 5.2900 -18.6960
REMARK 3 T TENSOR
REMARK 3 T11: 0.0698 T22: 0.1267
REMARK 3 T33: 0.1886 T12: -0.0191
REMARK 3 T13: -0.0388 T23: -0.0179
REMARK 3 L TENSOR
REMARK 3 L11: 0.6075 L22: 2.8536
REMARK 3 L33: 6.5805 L12: -0.3005
REMARK 3 L13: -0.4355 L23: 2.1783
REMARK 3 S TENSOR
REMARK 3 S11: -0.0736 S12: -0.2142 S13: 0.1318
REMARK 3 S21: 0.1934 S22: 0.0907 S23: -0.1711
REMARK 3 S31: -0.2276 S32: 0.3309 S33: -0.0172
REMARK 3
REMARK 3 TLS GROUP : 87
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : L 21 L 39
REMARK 3 ORIGIN FOR THE GROUP (A): 36.8140 -3.5140 -45.0480
REMARK 3 T TENSOR
REMARK 3 T11: 0.1241 T22: 0.0826
REMARK 3 T33: 0.0508 T12: -0.0013
REMARK 3 T13: 0.0173 T23: 0.0087
REMARK 3 L TENSOR
REMARK 3 L11: 10.2399 L22: 1.4239
REMARK 3 L33: 1.4398 L12: -0.2478
REMARK 3 L13: 0.9652 L23: 0.6696
REMARK 3 S TENSOR
REMARK 3 S11: 0.1343 S12: 0.5139 S13: -0.2813
REMARK 3 S21: -0.1203 S22: -0.0477 S23: 0.0910
REMARK 3 S31: 0.0276 S32: 0.0426 S33: -0.0865
REMARK 3
REMARK 3 TLS GROUP : 88
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : L 40 L 75
REMARK 3 ORIGIN FOR THE GROUP (A): 14.6560 1.4260 -34.0370
REMARK 3 T TENSOR
REMARK 3 T11: 0.0710 T22: 0.1087
REMARK 3 T33: 0.0638 T12: -0.0170
REMARK 3 T13: -0.0441 T23: 0.0251
REMARK 3 L TENSOR
REMARK 3 L11: 3.3520 L22: 2.7274
REMARK 3 L33: 3.1235 L12: -1.9691
REMARK 3 L13: -2.4475 L23: 2.1417
REMARK 3 S TENSOR
REMARK 3 S11: -0.0324 S12: 0.2732 S13: -0.0557
REMARK 3 S21: -0.0676 S22: -0.1209 S23: 0.2370
REMARK 3 S31: 0.1044 S32: -0.3012 S33: 0.1534
REMARK 3
REMARK 3 TLS GROUP : 89
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : L 76 L 97
REMARK 3 ORIGIN FOR THE GROUP (A): 20.5790 6.5860 -27.6060
REMARK 3 T TENSOR
REMARK 3 T11: 0.1089 T22: 0.1028
REMARK 3 T33: 0.0890 T12: 0.0327
REMARK 3 T13: -0.0011 T23: 0.0210
REMARK 3 L TENSOR
REMARK 3 L11: 1.0021 L22: 1.7538
REMARK 3 L33: 1.0484 L12: -0.2447
REMARK 3 L13: -0.1396 L23: -0.5885
REMARK 3 S TENSOR
REMARK 3 S11: -0.1011 S12: 0.0301 S13: 0.0594
REMARK 3 S21: 0.2614 S22: 0.1605 S23: 0.2044
REMARK 3 S31: -0.2592 S32: -0.2412 S33: -0.0593
REMARK 3
REMARK 3 TLS GROUP : 90
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : L 98 L 119
REMARK 3 ORIGIN FOR THE GROUP (A): 19.6270 6.8590 -26.4310
REMARK 3 T TENSOR
REMARK 3 T11: 0.0371 T22: 0.0723
REMARK 3 T33: 0.0639 T12: -0.0096
REMARK 3 T13: 0.0022 T23: 0.0184
REMARK 3 L TENSOR
REMARK 3 L11: 2.0283 L22: 1.5935
REMARK 3 L33: 0.8594 L12: -1.0716
REMARK 3 L13: -0.2057 L23: 0.8359
REMARK 3 S TENSOR
REMARK 3 S11: -0.0677 S12: -0.1232 S13: -0.0655
REMARK 3 S21: 0.0014 S22: 0.0514 S23: 0.1308
REMARK 3 S31: 0.0083 S32: 0.0403 S33: 0.0163
REMARK 3
REMARK 3 TLS GROUP : 91
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : L 120 L 243
REMARK 3 ORIGIN FOR THE GROUP (A): 35.0800 -3.9770 -30.4510
REMARK 3 T TENSOR
REMARK 3 T11: 0.0401 T22: 0.0381
REMARK 3 T33: 0.0277 T12: -0.0181
REMARK 3 T13: 0.0204 T23: 0.0071
REMARK 3 L TENSOR
REMARK 3 L11: 0.9564 L22: 1.7237
REMARK 3 L33: 0.9022 L12: -0.3898
REMARK 3 L13: 0.3776 L23: -0.3983
REMARK 3 S TENSOR
REMARK 3 S11: 0.0173 S12: 0.0525 S13: -0.0033
REMARK 3 S21: -0.0772 S22: 0.0079 S23: -0.0101
REMARK 3 S31: -0.0019 S32: -0.0076 S33: -0.0251
REMARK 3
REMARK 3 TLS GROUP : 92
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : L 244 L 286
REMARK 3 ORIGIN FOR THE GROUP (A): 42.6440 5.3200 -27.1150
REMARK 3 T TENSOR
REMARK 3 T11: 0.0479 T22: 0.0589
REMARK 3 T33: 0.0958 T12: -0.0138
REMARK 3 T13: -0.0056 T23: 0.0320
REMARK 3 L TENSOR
REMARK 3 L11: 0.7039 L22: 1.7772
REMARK 3 L33: 0.8641 L12: -0.1052
REMARK 3 L13: -0.3993 L23: 0.9473
REMARK 3 S TENSOR
REMARK 3 S11: 0.0125 S12: 0.0549 S13: 0.1194
REMARK 3 S21: -0.0799 S22: 0.0094 S23: -0.1265
REMARK 3 S31: -0.0887 S32: 0.0543 S33: -0.0220
REMARK 3
REMARK 3 TLS GROUP : 93
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : L 287 L 317
REMARK 3 ORIGIN FOR THE GROUP (A): 33.5510 14.9070 -19.2250
REMARK 3 T TENSOR
REMARK 3 T11: 0.1073 T22: 0.0552
REMARK 3 T33: 0.0953 T12: -0.0180
REMARK 3 T13: -0.0038 T23: -0.0079
REMARK 3 L TENSOR
REMARK 3 L11: 1.9260 L22: 0.2601
REMARK 3 L33: 1.8946 L12: -0.5775
REMARK 3 L13: 1.0336 L23: -0.6179
REMARK 3 S TENSOR
REMARK 3 S11: -0.0625 S12: 0.0023 S13: 0.2061
REMARK 3 S21: 0.0223 S22: 0.0257 S23: -0.0448
REMARK 3 S31: -0.1911 S32: -0.0192 S33: 0.0368
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
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
REMARK 3 RIDING POSITIONS. ATOM RECORD CONTAINS SUM OF TLS AND
REMARK 3 RESIDUAL B FACTORS ANISOU RECORD CONTAINS SUM OF TLS AND
REMARK 3 RESIDUAL U FACTORS.
REMARK 4
REMARK 4 2XLB COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 21-JUL-10.
REMARK 100 THE PDBE ID CODE IS EBI-44079.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-APR-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9789
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 304261
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.90
REMARK 200 RESOLUTION RANGE LOW (A) : 30.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.1
REMARK 200 DATA REDUNDANCY : 4.6
REMARK 200 R MERGE (I) : 0.09
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 6.00
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 85.2
REMARK 200 DATA REDUNDANCY IN SHELL : 4.8
REMARK 200 R MERGE FOR SHELL (I) : 0.25
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.00
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: PDB ENTRY 1ODS
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M MGCL2, 0.1 M NA HEPES PH
REMARK 280 7.5 AND 30 % PEG 400
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 43.65050
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
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: 16680 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 62010 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -41.4 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, J, H, K, I, L
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: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 16670 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 62290 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -41.2 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D, B, E, C, 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 LEU A 318
REMARK 465 SER A 319
REMARK 465 THR A 320
REMARK 465 LEU B 318
REMARK 465 SER B 319
REMARK 465 THR B 320
REMARK 465 LEU C 318
REMARK 465 SER C 319
REMARK 465 THR C 320
REMARK 465 LEU D 318
REMARK 465 SER D 319
REMARK 465 THR D 320
REMARK 465 LEU E 318
REMARK 465 SER E 319
REMARK 465 THR E 320
REMARK 465 LEU F 318
REMARK 465 SER F 319
REMARK 465 THR F 320
REMARK 465 LEU G 318
REMARK 465 SER G 319
REMARK 465 THR G 320
REMARK 465 LEU H 318
REMARK 465 SER H 319
REMARK 465 THR H 320
REMARK 465 LEU I 318
REMARK 465 SER I 319
REMARK 465 THR I 320
REMARK 465 LEU J 318
REMARK 465 SER J 319
REMARK 465 THR J 320
REMARK 465 LEU K 318
REMARK 465 SER K 319
REMARK 465 THR K 320
REMARK 465 LEU L 318
REMARK 465 SER L 319
REMARK 465 THR L 320
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 CG SD CE
REMARK 470 GLU A 9 CG CD OE1 OE2
REMARK 470 LYS A 17 CG CD CE NZ
REMARK 470 LYS A 29 CG CD CE NZ
REMARK 470 LYS A 30 CG CD CE NZ
REMARK 470 LYS A 52 CG CD CE NZ
REMARK 470 LYS A 55 CG CD CE NZ
REMARK 470 MET B 1 CG SD CE
REMARK 470 GLU B 9 CG CD OE1 OE2
REMARK 470 LYS B 29 CG CD CE NZ
REMARK 470 LYS B 30 CG CD CE NZ
REMARK 470 LYS B 52 CG CD CE NZ
REMARK 470 GLU B 219 CG CD OE1 OE2
REMARK 470 GLU B 236 CG CD OE1 OE2
REMARK 470 MET C 1 CG SD CE
REMARK 470 GLU C 9 CG CD OE1 OE2
REMARK 470 LYS C 17 CG CD CE NZ
REMARK 470 LYS C 29 CG CD CE NZ
REMARK 470 LYS C 30 CG CD CE NZ
REMARK 470 LYS C 52 CG CD CE NZ
REMARK 470 LYS C 55 CG CD CE NZ
REMARK 470 GLU C 219 CG CD OE1 OE2
REMARK 470 GLU C 236 CG CD OE1 OE2
REMARK 470 MET D 1 CG SD CE
REMARK 470 GLU D 9 CG CD OE1 OE2
REMARK 470 LYS D 17 CG CD CE NZ
REMARK 470 LYS D 29 CG CD CE NZ
REMARK 470 LYS D 30 CG CD CE NZ
REMARK 470 LYS D 52 CG CD CE NZ
REMARK 470 LYS D 55 CG CD CE NZ
REMARK 470 GLU D 219 CG CD OE1 OE2
REMARK 470 GLU D 236 CG CD OE1 OE2
REMARK 470 MET E 1 CG SD CE
REMARK 470 GLU E 9 CG CD OE1 OE2
REMARK 470 LYS E 17 CG CD CE NZ
REMARK 470 LYS E 29 CG CD CE NZ
REMARK 470 LYS E 30 CG CD CE NZ
REMARK 470 ASP E 48 CG OD1 OD2
REMARK 470 LYS E 52 CG CD CE NZ
REMARK 470 LYS E 55 CG CD CE NZ
REMARK 470 GLU E 219 CG CD OE1 OE2
REMARK 470 GLU E 236 CG CD OE1 OE2
REMARK 470 MET F 1 CG SD CE
REMARK 470 GLU F 9 CG CD OE1 OE2
REMARK 470 LYS F 17 CG CD CE NZ
REMARK 470 LYS F 29 CG CD CE NZ
REMARK 470 LYS F 30 CG CD CE NZ
REMARK 470 LYS F 52 CG CD CE NZ
REMARK 470 LYS F 55 CG CD CE NZ
REMARK 470 GLU F 219 CG CD OE1 OE2
REMARK 470 GLU F 236 CG CD OE1 OE2
REMARK 470 MET G 1 CG SD CE
REMARK 470 GLU G 9 CG CD OE1 OE2
REMARK 470 LYS G 17 CG CD CE NZ
REMARK 470 LYS G 29 CG CD CE NZ
REMARK 470 LYS G 30 CG CD CE NZ
REMARK 470 LYS G 52 CG CD CE NZ
REMARK 470 LYS G 55 CG CD CE NZ
REMARK 470 GLU G 219 CG CD OE1 OE2
REMARK 470 GLU G 236 CG CD OE1 OE2
REMARK 470 MET H 1 CG SD CE
REMARK 470 GLU H 9 CG CD OE1 OE2
REMARK 470 LYS H 17 CG CD CE NZ
REMARK 470 LYS H 29 CG CD CE NZ
REMARK 470 LYS H 30 CG CD CE NZ
REMARK 470 ASP H 48 CG OD1 OD2
REMARK 470 LYS H 52 CG CD CE NZ
REMARK 470 LYS H 55 CG CD CE NZ
REMARK 470 GLU H 219 CG CD OE1 OE2
REMARK 470 GLU H 236 CG CD OE1 OE2
REMARK 470 MET I 1 CG SD CE
REMARK 470 GLU I 9 CG CD OE1 OE2
REMARK 470 LYS I 17 CG CD CE NZ
REMARK 470 LYS I 29 CG CD CE NZ
REMARK 470 LYS I 30 CG CD CE NZ
REMARK 470 ASP I 48 CG OD1 OD2
REMARK 470 LYS I 52 CG CD CE NZ
REMARK 470 LYS I 55 CG CD CE NZ
REMARK 470 GLU I 219 CG CD OE1 OE2
REMARK 470 GLU I 236 CG CD OE1 OE2
REMARK 470 MET J 1 CG SD CE
REMARK 470 GLU J 9 CG CD OE1 OE2
REMARK 470 LYS J 17 CG CD CE NZ
REMARK 470 LYS J 29 CG CD CE NZ
REMARK 470 LYS J 30 CG CD CE NZ
REMARK 470 ASP J 48 CG OD1 OD2
REMARK 470 LYS J 52 CG CD CE NZ
REMARK 470 LYS J 55 CG CD CE NZ
REMARK 470 GLU J 219 CG CD OE1 OE2
REMARK 470 GLU J 236 CG CD OE1 OE2
REMARK 470 MET K 1 CG SD CE
REMARK 470 GLU K 9 CG CD OE1 OE2
REMARK 470 LYS K 17 CG CD CE NZ
REMARK 470 LYS K 29 CG CD CE NZ
REMARK 470 LYS K 30 CG CD CE NZ
REMARK 470 ASP K 48 CG OD1 OD2
REMARK 470 LYS K 52 CG CD CE NZ
REMARK 470 LYS K 55 CG CD CE NZ
REMARK 470 GLU K 219 CG CD OE1 OE2
REMARK 470 GLU K 236 CG CD OE1 OE2
REMARK 470 MET L 1 CG SD CE
REMARK 470 GLU L 9 CG CD OE1 OE2
REMARK 470 LYS L 17 CG CD CE NZ
REMARK 470 LYS L 29 CG CD CE NZ
REMARK 470 LYS L 30 CG CD CE NZ
REMARK 470 ASP L 48 CG OD1 OD2
REMARK 470 LYS L 52 CG CD CE NZ
REMARK 470 LYS L 55 CG CD CE NZ
REMARK 470 GLU L 236 CG CD OE1 OE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 GLN A 120 -80.54 -85.23
REMARK 500 SER A 181 -123.66 64.94
REMARK 500 TYR A 204 69.13 28.94
REMARK 500 GLN B 120 -80.68 -88.24
REMARK 500 SER B 181 -121.50 62.34
REMARK 500 TYR B 204 74.14 23.20
REMARK 500 GLN C 120 -80.30 -89.44
REMARK 500 SER C 181 -120.41 63.34
REMARK 500 TYR C 204 68.32 26.55
REMARK 500 PHE D 64 135.84 -39.60
REMARK 500 GLN D 120 -81.60 -88.53
REMARK 500 SER D 181 -121.66 65.32
REMARK 500 TYR D 204 71.05 25.75
REMARK 500 GLN E 120 -82.30 -85.99
REMARK 500 SER E 181 -121.18 65.35
REMARK 500 TYR E 204 71.44 25.98
REMARK 500 GLN F 120 -78.59 -86.59
REMARK 500 SER F 181 -122.63 62.83
REMARK 500 TYR F 204 69.59 27.05
REMARK 500 GLN G 120 -78.42 -92.55
REMARK 500 SER G 181 -122.04 64.18
REMARK 500 TYR G 204 71.24 26.06
REMARK 500 PHE H 64 132.92 -36.60
REMARK 500 GLN H 120 -77.68 -85.65
REMARK 500 SER H 181 -121.75 64.36
REMARK 500 TYR H 204 72.21 24.72
REMARK 500 PHE I 64 132.24 -37.39
REMARK 500 GLN I 120 -81.97 -89.04
REMARK 500 SER I 181 -121.35 64.71
REMARK 500 TYR I 204 69.59 26.97
REMARK 500 PHE J 64 129.38 -35.38
REMARK 500 GLN J 120 -78.48 -88.34
REMARK 500 SER J 181 -122.39 63.95
REMARK 500 TYR J 204 72.30 23.28
REMARK 500 GLN K 120 -82.93 -86.45
REMARK 500 SER K 181 -121.48 64.48
REMARK 500 TYR K 204 72.15 25.46
REMARK 500 GLN L 120 -78.20 -88.14
REMARK 500 SER L 181 -121.47 63.49
REMARK 500 TYR L 204 75.84 25.51
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2XLC RELATED DB: PDB
REMARK 900 ACETYL XYLAN ESTERASE FROM BACILLUS PUMILUS
REMARK 900 CECT5072 BOUND TO PARAOXON
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 SEQUENCE CONFLICTS ARE DUE TO SEQUENCES COMING FROM DIFFERENT
REMARK 999 BACILLUS PUMILUS STRAINS, PS213 (UNIPROT SEQUENCE) AND CECT 5072
REMARK 999 (PDB ENTRY 2XLB)
DBREF 2XLB A 1 320 UNP Q9K5F2 Q9K5F2_BACPU 1 320
DBREF 2XLB B 1 320 UNP Q9K5F2 Q9K5F2_BACPU 1 320
DBREF 2XLB C 1 320 UNP Q9K5F2 Q9K5F2_BACPU 1 320
DBREF 2XLB D 1 320 UNP Q9K5F2 Q9K5F2_BACPU 1 320
DBREF 2XLB E 1 320 UNP Q9K5F2 Q9K5F2_BACPU 1 320
DBREF 2XLB F 1 320 UNP Q9K5F2 Q9K5F2_BACPU 1 320
DBREF 2XLB G 1 320 UNP Q9K5F2 Q9K5F2_BACPU 1 320
DBREF 2XLB H 1 320 UNP Q9K5F2 Q9K5F2_BACPU 1 320
DBREF 2XLB I 1 320 UNP Q9K5F2 Q9K5F2_BACPU 1 320
DBREF 2XLB J 1 320 UNP Q9K5F2 Q9K5F2_BACPU 1 320
DBREF 2XLB K 1 320 UNP Q9K5F2 Q9K5F2_BACPU 1 320
DBREF 2XLB L 1 320 UNP Q9K5F2 Q9K5F2_BACPU 1 320
SEQADV 2XLB ASP A 97 UNP Q9K5F2 GLY 97 CONFLICT
SEQADV 2XLB GLU A 236 UNP Q9K5F2 LYS 236 CONFLICT
SEQADV 2XLB GLN A 270 UNP Q9K5F2 LYS 270 CONFLICT
SEQADV 2XLB GLU A 289 UNP Q9K5F2 ASP 289 CONFLICT
SEQADV 2XLB ASP B 97 UNP Q9K5F2 GLY 97 CONFLICT
SEQADV 2XLB GLU B 236 UNP Q9K5F2 LYS 236 CONFLICT
SEQADV 2XLB GLN B 270 UNP Q9K5F2 LYS 270 CONFLICT
SEQADV 2XLB GLU B 289 UNP Q9K5F2 ASP 289 CONFLICT
SEQADV 2XLB ASP C 97 UNP Q9K5F2 GLY 97 CONFLICT
SEQADV 2XLB GLU C 236 UNP Q9K5F2 LYS 236 CONFLICT
SEQADV 2XLB GLN C 270 UNP Q9K5F2 LYS 270 CONFLICT
SEQADV 2XLB GLU C 289 UNP Q9K5F2 ASP 289 CONFLICT
SEQADV 2XLB ASP D 97 UNP Q9K5F2 GLY 97 CONFLICT
SEQADV 2XLB GLU D 236 UNP Q9K5F2 LYS 236 CONFLICT
SEQADV 2XLB GLN D 270 UNP Q9K5F2 LYS 270 CONFLICT
SEQADV 2XLB GLU D 289 UNP Q9K5F2 ASP 289 CONFLICT
SEQADV 2XLB ASP E 97 UNP Q9K5F2 GLY 97 CONFLICT
SEQADV 2XLB GLU E 236 UNP Q9K5F2 LYS 236 CONFLICT
SEQADV 2XLB GLN E 270 UNP Q9K5F2 LYS 270 CONFLICT
SEQADV 2XLB GLU E 289 UNP Q9K5F2 ASP 289 CONFLICT
SEQADV 2XLB ASP F 97 UNP Q9K5F2 GLY 97 CONFLICT
SEQADV 2XLB GLU F 236 UNP Q9K5F2 LYS 236 CONFLICT
SEQADV 2XLB GLN F 270 UNP Q9K5F2 LYS 270 CONFLICT
SEQADV 2XLB GLU F 289 UNP Q9K5F2 ASP 289 CONFLICT
SEQADV 2XLB ASP G 97 UNP Q9K5F2 GLY 97 CONFLICT
SEQADV 2XLB GLU G 236 UNP Q9K5F2 LYS 236 CONFLICT
SEQADV 2XLB GLN G 270 UNP Q9K5F2 LYS 270 CONFLICT
SEQADV 2XLB GLU G 289 UNP Q9K5F2 ASP 289 CONFLICT
SEQADV 2XLB ASP H 97 UNP Q9K5F2 GLY 97 CONFLICT
SEQADV 2XLB GLU H 236 UNP Q9K5F2 LYS 236 CONFLICT
SEQADV 2XLB GLN H 270 UNP Q9K5F2 LYS 270 CONFLICT
SEQADV 2XLB GLU H 289 UNP Q9K5F2 ASP 289 CONFLICT
SEQADV 2XLB ASP I 97 UNP Q9K5F2 GLY 97 CONFLICT
SEQADV 2XLB GLU I 236 UNP Q9K5F2 LYS 236 CONFLICT
SEQADV 2XLB GLN I 270 UNP Q9K5F2 LYS 270 CONFLICT
SEQADV 2XLB GLU I 289 UNP Q9K5F2 ASP 289 CONFLICT
SEQADV 2XLB ASP J 97 UNP Q9K5F2 GLY 97 CONFLICT
SEQADV 2XLB GLU J 236 UNP Q9K5F2 LYS 236 CONFLICT
SEQADV 2XLB GLN J 270 UNP Q9K5F2 LYS 270 CONFLICT
SEQADV 2XLB GLU J 289 UNP Q9K5F2 ASP 289 CONFLICT
SEQADV 2XLB ASP K 97 UNP Q9K5F2 GLY 97 CONFLICT
SEQADV 2XLB GLU K 236 UNP Q9K5F2 LYS 236 CONFLICT
SEQADV 2XLB GLN K 270 UNP Q9K5F2 LYS 270 CONFLICT
SEQADV 2XLB GLU K 289 UNP Q9K5F2 ASP 289 CONFLICT
SEQADV 2XLB ASP L 97 UNP Q9K5F2 GLY 97 CONFLICT
SEQADV 2XLB GLU L 236 UNP Q9K5F2 LYS 236 CONFLICT
SEQADV 2XLB GLN L 270 UNP Q9K5F2 LYS 270 CONFLICT
SEQADV 2XLB GLU L 289 UNP Q9K5F2 ASP 289 CONFLICT
SEQRES 1 A 320 MET GLN LEU PHE ASP LEU SER LEU GLU GLU LEU LYS LYS
SEQRES 2 A 320 TYR LYS PRO LYS LYS THR ALA ARG PRO ASP PHE ALA ASP
SEQRES 3 A 320 PHE TRP LYS LYS SER LEU GLU GLU LEU ARG GLN VAL GLU
SEQRES 4 A 320 ALA GLU PRO THR LEU GLU SER TYR ASP TYR PRO VAL LYS
SEQRES 5 A 320 GLY VAL LYS VAL TYR ARG LEU THR TYR GLN SER PHE GLY
SEQRES 6 A 320 HIS SER LYS ILE GLU GLY PHE TYR ALA VAL PRO ASP GLN
SEQRES 7 A 320 THR GLY PRO HIS PRO ALA LEU VAL ARG PHE HIS GLY TYR
SEQRES 8 A 320 ASN ALA SER TYR ASP ASP GLY ILE HIS ASP ILE VAL ASN
SEQRES 9 A 320 TRP ALA LEU HIS GLY TYR ALA THR PHE GLY MET LEU VAL
SEQRES 10 A 320 ARG GLY GLN GLY GLY SER GLU ASP THR SER VAL THR PRO
SEQRES 11 A 320 GLY GLY HIS ALA LEU GLY TRP MET THR LYS GLY ILE LEU
SEQRES 12 A 320 SER LYS ASP THR TYR TYR TYR ARG GLY VAL TYR LEU ASP
SEQRES 13 A 320 ALA VAL ARG ALA LEU GLU VAL ILE GLN SER PHE PRO GLU
SEQRES 14 A 320 VAL ASP GLU HIS ARG ILE GLY VAL ILE GLY GLY SER GLN
SEQRES 15 A 320 GLY GLY ALA LEU ALA ILE ALA ALA ALA ALA LEU SER ASP
SEQRES 16 A 320 ILE PRO LYS VAL VAL VAL ALA ASP TYR PRO TYR LEU SER
SEQRES 17 A 320 ASN PHE GLU ARG ALA VAL ASP VAL ALA LEU GLU GLN PRO
SEQRES 18 A 320 TYR LEU GLU ILE ASN SER TYR PHE ARG ARG ASN SER ASP
SEQRES 19 A 320 PRO GLU VAL GLU GLU LYS ALA PHE GLU THR LEU SER TYR
SEQRES 20 A 320 PHE ASP LEU ILE ASN LEU ALA GLY TRP VAL LYS GLN PRO
SEQRES 21 A 320 THR LEU MET ALA ILE GLY LEU ILE ASP GLN VAL THR PRO
SEQRES 22 A 320 PRO SER THR VAL PHE ALA ALA TYR ASN HIS LEU GLU THR
SEQRES 23 A 320 ASP LYS GLU LEU LYS VAL TYR ARG TYR PHE GLY HIS GLU
SEQRES 24 A 320 PHE ILE PRO ALA PHE GLN THR GLU LYS LEU SER PHE LEU
SEQRES 25 A 320 GLN LYS HIS LEU LEU LEU SER THR
SEQRES 1 B 320 MET GLN LEU PHE ASP LEU SER LEU GLU GLU LEU LYS LYS
SEQRES 2 B 320 TYR LYS PRO LYS LYS THR ALA ARG PRO ASP PHE ALA ASP
SEQRES 3 B 320 PHE TRP LYS LYS SER LEU GLU GLU LEU ARG GLN VAL GLU
SEQRES 4 B 320 ALA GLU PRO THR LEU GLU SER TYR ASP TYR PRO VAL LYS
SEQRES 5 B 320 GLY VAL LYS VAL TYR ARG LEU THR TYR GLN SER PHE GLY
SEQRES 6 B 320 HIS SER LYS ILE GLU GLY PHE TYR ALA VAL PRO ASP GLN
SEQRES 7 B 320 THR GLY PRO HIS PRO ALA LEU VAL ARG PHE HIS GLY TYR
SEQRES 8 B 320 ASN ALA SER TYR ASP ASP GLY ILE HIS ASP ILE VAL ASN
SEQRES 9 B 320 TRP ALA LEU HIS GLY TYR ALA THR PHE GLY MET LEU VAL
SEQRES 10 B 320 ARG GLY GLN GLY GLY SER GLU ASP THR SER VAL THR PRO
SEQRES 11 B 320 GLY GLY HIS ALA LEU GLY TRP MET THR LYS GLY ILE LEU
SEQRES 12 B 320 SER LYS ASP THR TYR TYR TYR ARG GLY VAL TYR LEU ASP
SEQRES 13 B 320 ALA VAL ARG ALA LEU GLU VAL ILE GLN SER PHE PRO GLU
SEQRES 14 B 320 VAL ASP GLU HIS ARG ILE GLY VAL ILE GLY GLY SER GLN
SEQRES 15 B 320 GLY GLY ALA LEU ALA ILE ALA ALA ALA ALA LEU SER ASP
SEQRES 16 B 320 ILE PRO LYS VAL VAL VAL ALA ASP TYR PRO TYR LEU SER
SEQRES 17 B 320 ASN PHE GLU ARG ALA VAL ASP VAL ALA LEU GLU GLN PRO
SEQRES 18 B 320 TYR LEU GLU ILE ASN SER TYR PHE ARG ARG ASN SER ASP
SEQRES 19 B 320 PRO GLU VAL GLU GLU LYS ALA PHE GLU THR LEU SER TYR
SEQRES 20 B 320 PHE ASP LEU ILE ASN LEU ALA GLY TRP VAL LYS GLN PRO
SEQRES 21 B 320 THR LEU MET ALA ILE GLY LEU ILE ASP GLN VAL THR PRO
SEQRES 22 B 320 PRO SER THR VAL PHE ALA ALA TYR ASN HIS LEU GLU THR
SEQRES 23 B 320 ASP LYS GLU LEU LYS VAL TYR ARG TYR PHE GLY HIS GLU
SEQRES 24 B 320 PHE ILE PRO ALA PHE GLN THR GLU LYS LEU SER PHE LEU
SEQRES 25 B 320 GLN LYS HIS LEU LEU LEU SER THR
SEQRES 1 C 320 MET GLN LEU PHE ASP LEU SER LEU GLU GLU LEU LYS LYS
SEQRES 2 C 320 TYR LYS PRO LYS LYS THR ALA ARG PRO ASP PHE ALA ASP
SEQRES 3 C 320 PHE TRP LYS LYS SER LEU GLU GLU LEU ARG GLN VAL GLU
SEQRES 4 C 320 ALA GLU PRO THR LEU GLU SER TYR ASP TYR PRO VAL LYS
SEQRES 5 C 320 GLY VAL LYS VAL TYR ARG LEU THR TYR GLN SER PHE GLY
SEQRES 6 C 320 HIS SER LYS ILE GLU GLY PHE TYR ALA VAL PRO ASP GLN
SEQRES 7 C 320 THR GLY PRO HIS PRO ALA LEU VAL ARG PHE HIS GLY TYR
SEQRES 8 C 320 ASN ALA SER TYR ASP ASP GLY ILE HIS ASP ILE VAL ASN
SEQRES 9 C 320 TRP ALA LEU HIS GLY TYR ALA THR PHE GLY MET LEU VAL
SEQRES 10 C 320 ARG GLY GLN GLY GLY SER GLU ASP THR SER VAL THR PRO
SEQRES 11 C 320 GLY GLY HIS ALA LEU GLY TRP MET THR LYS GLY ILE LEU
SEQRES 12 C 320 SER LYS ASP THR TYR TYR TYR ARG GLY VAL TYR LEU ASP
SEQRES 13 C 320 ALA VAL ARG ALA LEU GLU VAL ILE GLN SER PHE PRO GLU
SEQRES 14 C 320 VAL ASP GLU HIS ARG ILE GLY VAL ILE GLY GLY SER GLN
SEQRES 15 C 320 GLY GLY ALA LEU ALA ILE ALA ALA ALA ALA LEU SER ASP
SEQRES 16 C 320 ILE PRO LYS VAL VAL VAL ALA ASP TYR PRO TYR LEU SER
SEQRES 17 C 320 ASN PHE GLU ARG ALA VAL ASP VAL ALA LEU GLU GLN PRO
SEQRES 18 C 320 TYR LEU GLU ILE ASN SER TYR PHE ARG ARG ASN SER ASP
SEQRES 19 C 320 PRO GLU VAL GLU GLU LYS ALA PHE GLU THR LEU SER TYR
SEQRES 20 C 320 PHE ASP LEU ILE ASN LEU ALA GLY TRP VAL LYS GLN PRO
SEQRES 21 C 320 THR LEU MET ALA ILE GLY LEU ILE ASP GLN VAL THR PRO
SEQRES 22 C 320 PRO SER THR VAL PHE ALA ALA TYR ASN HIS LEU GLU THR
SEQRES 23 C 320 ASP LYS GLU LEU LYS VAL TYR ARG TYR PHE GLY HIS GLU
SEQRES 24 C 320 PHE ILE PRO ALA PHE GLN THR GLU LYS LEU SER PHE LEU
SEQRES 25 C 320 GLN LYS HIS LEU LEU LEU SER THR
SEQRES 1 D 320 MET GLN LEU PHE ASP LEU SER LEU GLU GLU LEU LYS LYS
SEQRES 2 D 320 TYR LYS PRO LYS LYS THR ALA ARG PRO ASP PHE ALA ASP
SEQRES 3 D 320 PHE TRP LYS LYS SER LEU GLU GLU LEU ARG GLN VAL GLU
SEQRES 4 D 320 ALA GLU PRO THR LEU GLU SER TYR ASP TYR PRO VAL LYS
SEQRES 5 D 320 GLY VAL LYS VAL TYR ARG LEU THR TYR GLN SER PHE GLY
SEQRES 6 D 320 HIS SER LYS ILE GLU GLY PHE TYR ALA VAL PRO ASP GLN
SEQRES 7 D 320 THR GLY PRO HIS PRO ALA LEU VAL ARG PHE HIS GLY TYR
SEQRES 8 D 320 ASN ALA SER TYR ASP ASP GLY ILE HIS ASP ILE VAL ASN
SEQRES 9 D 320 TRP ALA LEU HIS GLY TYR ALA THR PHE GLY MET LEU VAL
SEQRES 10 D 320 ARG GLY GLN GLY GLY SER GLU ASP THR SER VAL THR PRO
SEQRES 11 D 320 GLY GLY HIS ALA LEU GLY TRP MET THR LYS GLY ILE LEU
SEQRES 12 D 320 SER LYS ASP THR TYR TYR TYR ARG GLY VAL TYR LEU ASP
SEQRES 13 D 320 ALA VAL ARG ALA LEU GLU VAL ILE GLN SER PHE PRO GLU
SEQRES 14 D 320 VAL ASP GLU HIS ARG ILE GLY VAL ILE GLY GLY SER GLN
SEQRES 15 D 320 GLY GLY ALA LEU ALA ILE ALA ALA ALA ALA LEU SER ASP
SEQRES 16 D 320 ILE PRO LYS VAL VAL VAL ALA ASP TYR PRO TYR LEU SER
SEQRES 17 D 320 ASN PHE GLU ARG ALA VAL ASP VAL ALA LEU GLU GLN PRO
SEQRES 18 D 320 TYR LEU GLU ILE ASN SER TYR PHE ARG ARG ASN SER ASP
SEQRES 19 D 320 PRO GLU VAL GLU GLU LYS ALA PHE GLU THR LEU SER TYR
SEQRES 20 D 320 PHE ASP LEU ILE ASN LEU ALA GLY TRP VAL LYS GLN PRO
SEQRES 21 D 320 THR LEU MET ALA ILE GLY LEU ILE ASP GLN VAL THR PRO
SEQRES 22 D 320 PRO SER THR VAL PHE ALA ALA TYR ASN HIS LEU GLU THR
SEQRES 23 D 320 ASP LYS GLU LEU LYS VAL TYR ARG TYR PHE GLY HIS GLU
SEQRES 24 D 320 PHE ILE PRO ALA PHE GLN THR GLU LYS LEU SER PHE LEU
SEQRES 25 D 320 GLN LYS HIS LEU LEU LEU SER THR
SEQRES 1 E 320 MET GLN LEU PHE ASP LEU SER LEU GLU GLU LEU LYS LYS
SEQRES 2 E 320 TYR LYS PRO LYS LYS THR ALA ARG PRO ASP PHE ALA ASP
SEQRES 3 E 320 PHE TRP LYS LYS SER LEU GLU GLU LEU ARG GLN VAL GLU
SEQRES 4 E 320 ALA GLU PRO THR LEU GLU SER TYR ASP TYR PRO VAL LYS
SEQRES 5 E 320 GLY VAL LYS VAL TYR ARG LEU THR TYR GLN SER PHE GLY
SEQRES 6 E 320 HIS SER LYS ILE GLU GLY PHE TYR ALA VAL PRO ASP GLN
SEQRES 7 E 320 THR GLY PRO HIS PRO ALA LEU VAL ARG PHE HIS GLY TYR
SEQRES 8 E 320 ASN ALA SER TYR ASP ASP GLY ILE HIS ASP ILE VAL ASN
SEQRES 9 E 320 TRP ALA LEU HIS GLY TYR ALA THR PHE GLY MET LEU VAL
SEQRES 10 E 320 ARG GLY GLN GLY GLY SER GLU ASP THR SER VAL THR PRO
SEQRES 11 E 320 GLY GLY HIS ALA LEU GLY TRP MET THR LYS GLY ILE LEU
SEQRES 12 E 320 SER LYS ASP THR TYR TYR TYR ARG GLY VAL TYR LEU ASP
SEQRES 13 E 320 ALA VAL ARG ALA LEU GLU VAL ILE GLN SER PHE PRO GLU
SEQRES 14 E 320 VAL ASP GLU HIS ARG ILE GLY VAL ILE GLY GLY SER GLN
SEQRES 15 E 320 GLY GLY ALA LEU ALA ILE ALA ALA ALA ALA LEU SER ASP
SEQRES 16 E 320 ILE PRO LYS VAL VAL VAL ALA ASP TYR PRO TYR LEU SER
SEQRES 17 E 320 ASN PHE GLU ARG ALA VAL ASP VAL ALA LEU GLU GLN PRO
SEQRES 18 E 320 TYR LEU GLU ILE ASN SER TYR PHE ARG ARG ASN SER ASP
SEQRES 19 E 320 PRO GLU VAL GLU GLU LYS ALA PHE GLU THR LEU SER TYR
SEQRES 20 E 320 PHE ASP LEU ILE ASN LEU ALA GLY TRP VAL LYS GLN PRO
SEQRES 21 E 320 THR LEU MET ALA ILE GLY LEU ILE ASP GLN VAL THR PRO
SEQRES 22 E 320 PRO SER THR VAL PHE ALA ALA TYR ASN HIS LEU GLU THR
SEQRES 23 E 320 ASP LYS GLU LEU LYS VAL TYR ARG TYR PHE GLY HIS GLU
SEQRES 24 E 320 PHE ILE PRO ALA PHE GLN THR GLU LYS LEU SER PHE LEU
SEQRES 25 E 320 GLN LYS HIS LEU LEU LEU SER THR
SEQRES 1 F 320 MET GLN LEU PHE ASP LEU SER LEU GLU GLU LEU LYS LYS
SEQRES 2 F 320 TYR LYS PRO LYS LYS THR ALA ARG PRO ASP PHE ALA ASP
SEQRES 3 F 320 PHE TRP LYS LYS SER LEU GLU GLU LEU ARG GLN VAL GLU
SEQRES 4 F 320 ALA GLU PRO THR LEU GLU SER TYR ASP TYR PRO VAL LYS
SEQRES 5 F 320 GLY VAL LYS VAL TYR ARG LEU THR TYR GLN SER PHE GLY
SEQRES 6 F 320 HIS SER LYS ILE GLU GLY PHE TYR ALA VAL PRO ASP GLN
SEQRES 7 F 320 THR GLY PRO HIS PRO ALA LEU VAL ARG PHE HIS GLY TYR
SEQRES 8 F 320 ASN ALA SER TYR ASP ASP GLY ILE HIS ASP ILE VAL ASN
SEQRES 9 F 320 TRP ALA LEU HIS GLY TYR ALA THR PHE GLY MET LEU VAL
SEQRES 10 F 320 ARG GLY GLN GLY GLY SER GLU ASP THR SER VAL THR PRO
SEQRES 11 F 320 GLY GLY HIS ALA LEU GLY TRP MET THR LYS GLY ILE LEU
SEQRES 12 F 320 SER LYS ASP THR TYR TYR TYR ARG GLY VAL TYR LEU ASP
SEQRES 13 F 320 ALA VAL ARG ALA LEU GLU VAL ILE GLN SER PHE PRO GLU
SEQRES 14 F 320 VAL ASP GLU HIS ARG ILE GLY VAL ILE GLY GLY SER GLN
SEQRES 15 F 320 GLY GLY ALA LEU ALA ILE ALA ALA ALA ALA LEU SER ASP
SEQRES 16 F 320 ILE PRO LYS VAL VAL VAL ALA ASP TYR PRO TYR LEU SER
SEQRES 17 F 320 ASN PHE GLU ARG ALA VAL ASP VAL ALA LEU GLU GLN PRO
SEQRES 18 F 320 TYR LEU GLU ILE ASN SER TYR PHE ARG ARG ASN SER ASP
SEQRES 19 F 320 PRO GLU VAL GLU GLU LYS ALA PHE GLU THR LEU SER TYR
SEQRES 20 F 320 PHE ASP LEU ILE ASN LEU ALA GLY TRP VAL LYS GLN PRO
SEQRES 21 F 320 THR LEU MET ALA ILE GLY LEU ILE ASP GLN VAL THR PRO
SEQRES 22 F 320 PRO SER THR VAL PHE ALA ALA TYR ASN HIS LEU GLU THR
SEQRES 23 F 320 ASP LYS GLU LEU LYS VAL TYR ARG TYR PHE GLY HIS GLU
SEQRES 24 F 320 PHE ILE PRO ALA PHE GLN THR GLU LYS LEU SER PHE LEU
SEQRES 25 F 320 GLN LYS HIS LEU LEU LEU SER THR
SEQRES 1 G 320 MET GLN LEU PHE ASP LEU SER LEU GLU GLU LEU LYS LYS
SEQRES 2 G 320 TYR LYS PRO LYS LYS THR ALA ARG PRO ASP PHE ALA ASP
SEQRES 3 G 320 PHE TRP LYS LYS SER LEU GLU GLU LEU ARG GLN VAL GLU
SEQRES 4 G 320 ALA GLU PRO THR LEU GLU SER TYR ASP TYR PRO VAL LYS
SEQRES 5 G 320 GLY VAL LYS VAL TYR ARG LEU THR TYR GLN SER PHE GLY
SEQRES 6 G 320 HIS SER LYS ILE GLU GLY PHE TYR ALA VAL PRO ASP GLN
SEQRES 7 G 320 THR GLY PRO HIS PRO ALA LEU VAL ARG PHE HIS GLY TYR
SEQRES 8 G 320 ASN ALA SER TYR ASP ASP GLY ILE HIS ASP ILE VAL ASN
SEQRES 9 G 320 TRP ALA LEU HIS GLY TYR ALA THR PHE GLY MET LEU VAL
SEQRES 10 G 320 ARG GLY GLN GLY GLY SER GLU ASP THR SER VAL THR PRO
SEQRES 11 G 320 GLY GLY HIS ALA LEU GLY TRP MET THR LYS GLY ILE LEU
SEQRES 12 G 320 SER LYS ASP THR TYR TYR TYR ARG GLY VAL TYR LEU ASP
SEQRES 13 G 320 ALA VAL ARG ALA LEU GLU VAL ILE GLN SER PHE PRO GLU
SEQRES 14 G 320 VAL ASP GLU HIS ARG ILE GLY VAL ILE GLY GLY SER GLN
SEQRES 15 G 320 GLY GLY ALA LEU ALA ILE ALA ALA ALA ALA LEU SER ASP
SEQRES 16 G 320 ILE PRO LYS VAL VAL VAL ALA ASP TYR PRO TYR LEU SER
SEQRES 17 G 320 ASN PHE GLU ARG ALA VAL ASP VAL ALA LEU GLU GLN PRO
SEQRES 18 G 320 TYR LEU GLU ILE ASN SER TYR PHE ARG ARG ASN SER ASP
SEQRES 19 G 320 PRO GLU VAL GLU GLU LYS ALA PHE GLU THR LEU SER TYR
SEQRES 20 G 320 PHE ASP LEU ILE ASN LEU ALA GLY TRP VAL LYS GLN PRO
SEQRES 21 G 320 THR LEU MET ALA ILE GLY LEU ILE ASP GLN VAL THR PRO
SEQRES 22 G 320 PRO SER THR VAL PHE ALA ALA TYR ASN HIS LEU GLU THR
SEQRES 23 G 320 ASP LYS GLU LEU LYS VAL TYR ARG TYR PHE GLY HIS GLU
SEQRES 24 G 320 PHE ILE PRO ALA PHE GLN THR GLU LYS LEU SER PHE LEU
SEQRES 25 G 320 GLN LYS HIS LEU LEU LEU SER THR
SEQRES 1 H 320 MET GLN LEU PHE ASP LEU SER LEU GLU GLU LEU LYS LYS
SEQRES 2 H 320 TYR LYS PRO LYS LYS THR ALA ARG PRO ASP PHE ALA ASP
SEQRES 3 H 320 PHE TRP LYS LYS SER LEU GLU GLU LEU ARG GLN VAL GLU
SEQRES 4 H 320 ALA GLU PRO THR LEU GLU SER TYR ASP TYR PRO VAL LYS
SEQRES 5 H 320 GLY VAL LYS VAL TYR ARG LEU THR TYR GLN SER PHE GLY
SEQRES 6 H 320 HIS SER LYS ILE GLU GLY PHE TYR ALA VAL PRO ASP GLN
SEQRES 7 H 320 THR GLY PRO HIS PRO ALA LEU VAL ARG PHE HIS GLY TYR
SEQRES 8 H 320 ASN ALA SER TYR ASP ASP GLY ILE HIS ASP ILE VAL ASN
SEQRES 9 H 320 TRP ALA LEU HIS GLY TYR ALA THR PHE GLY MET LEU VAL
SEQRES 10 H 320 ARG GLY GLN GLY GLY SER GLU ASP THR SER VAL THR PRO
SEQRES 11 H 320 GLY GLY HIS ALA LEU GLY TRP MET THR LYS GLY ILE LEU
SEQRES 12 H 320 SER LYS ASP THR TYR TYR TYR ARG GLY VAL TYR LEU ASP
SEQRES 13 H 320 ALA VAL ARG ALA LEU GLU VAL ILE GLN SER PHE PRO GLU
SEQRES 14 H 320 VAL ASP GLU HIS ARG ILE GLY VAL ILE GLY GLY SER GLN
SEQRES 15 H 320 GLY GLY ALA LEU ALA ILE ALA ALA ALA ALA LEU SER ASP
SEQRES 16 H 320 ILE PRO LYS VAL VAL VAL ALA ASP TYR PRO TYR LEU SER
SEQRES 17 H 320 ASN PHE GLU ARG ALA VAL ASP VAL ALA LEU GLU GLN PRO
SEQRES 18 H 320 TYR LEU GLU ILE ASN SER TYR PHE ARG ARG ASN SER ASP
SEQRES 19 H 320 PRO GLU VAL GLU GLU LYS ALA PHE GLU THR LEU SER TYR
SEQRES 20 H 320 PHE ASP LEU ILE ASN LEU ALA GLY TRP VAL LYS GLN PRO
SEQRES 21 H 320 THR LEU MET ALA ILE GLY LEU ILE ASP GLN VAL THR PRO
SEQRES 22 H 320 PRO SER THR VAL PHE ALA ALA TYR ASN HIS LEU GLU THR
SEQRES 23 H 320 ASP LYS GLU LEU LYS VAL TYR ARG TYR PHE GLY HIS GLU
SEQRES 24 H 320 PHE ILE PRO ALA PHE GLN THR GLU LYS LEU SER PHE LEU
SEQRES 25 H 320 GLN LYS HIS LEU LEU LEU SER THR
SEQRES 1 I 320 MET GLN LEU PHE ASP LEU SER LEU GLU GLU LEU LYS LYS
SEQRES 2 I 320 TYR LYS PRO LYS LYS THR ALA ARG PRO ASP PHE ALA ASP
SEQRES 3 I 320 PHE TRP LYS LYS SER LEU GLU GLU LEU ARG GLN VAL GLU
SEQRES 4 I 320 ALA GLU PRO THR LEU GLU SER TYR ASP TYR PRO VAL LYS
SEQRES 5 I 320 GLY VAL LYS VAL TYR ARG LEU THR TYR GLN SER PHE GLY
SEQRES 6 I 320 HIS SER LYS ILE GLU GLY PHE TYR ALA VAL PRO ASP GLN
SEQRES 7 I 320 THR GLY PRO HIS PRO ALA LEU VAL ARG PHE HIS GLY TYR
SEQRES 8 I 320 ASN ALA SER TYR ASP ASP GLY ILE HIS ASP ILE VAL ASN
SEQRES 9 I 320 TRP ALA LEU HIS GLY TYR ALA THR PHE GLY MET LEU VAL
SEQRES 10 I 320 ARG GLY GLN GLY GLY SER GLU ASP THR SER VAL THR PRO
SEQRES 11 I 320 GLY GLY HIS ALA LEU GLY TRP MET THR LYS GLY ILE LEU
SEQRES 12 I 320 SER LYS ASP THR TYR TYR TYR ARG GLY VAL TYR LEU ASP
SEQRES 13 I 320 ALA VAL ARG ALA LEU GLU VAL ILE GLN SER PHE PRO GLU
SEQRES 14 I 320 VAL ASP GLU HIS ARG ILE GLY VAL ILE GLY GLY SER GLN
SEQRES 15 I 320 GLY GLY ALA LEU ALA ILE ALA ALA ALA ALA LEU SER ASP
SEQRES 16 I 320 ILE PRO LYS VAL VAL VAL ALA ASP TYR PRO TYR LEU SER
SEQRES 17 I 320 ASN PHE GLU ARG ALA VAL ASP VAL ALA LEU GLU GLN PRO
SEQRES 18 I 320 TYR LEU GLU ILE ASN SER TYR PHE ARG ARG ASN SER ASP
SEQRES 19 I 320 PRO GLU VAL GLU GLU LYS ALA PHE GLU THR LEU SER TYR
SEQRES 20 I 320 PHE ASP LEU ILE ASN LEU ALA GLY TRP VAL LYS GLN PRO
SEQRES 21 I 320 THR LEU MET ALA ILE GLY LEU ILE ASP GLN VAL THR PRO
SEQRES 22 I 320 PRO SER THR VAL PHE ALA ALA TYR ASN HIS LEU GLU THR
SEQRES 23 I 320 ASP LYS GLU LEU LYS VAL TYR ARG TYR PHE GLY HIS GLU
SEQRES 24 I 320 PHE ILE PRO ALA PHE GLN THR GLU LYS LEU SER PHE LEU
SEQRES 25 I 320 GLN LYS HIS LEU LEU LEU SER THR
SEQRES 1 J 320 MET GLN LEU PHE ASP LEU SER LEU GLU GLU LEU LYS LYS
SEQRES 2 J 320 TYR LYS PRO LYS LYS THR ALA ARG PRO ASP PHE ALA ASP
SEQRES 3 J 320 PHE TRP LYS LYS SER LEU GLU GLU LEU ARG GLN VAL GLU
SEQRES 4 J 320 ALA GLU PRO THR LEU GLU SER TYR ASP TYR PRO VAL LYS
SEQRES 5 J 320 GLY VAL LYS VAL TYR ARG LEU THR TYR GLN SER PHE GLY
SEQRES 6 J 320 HIS SER LYS ILE GLU GLY PHE TYR ALA VAL PRO ASP GLN
SEQRES 7 J 320 THR GLY PRO HIS PRO ALA LEU VAL ARG PHE HIS GLY TYR
SEQRES 8 J 320 ASN ALA SER TYR ASP ASP GLY ILE HIS ASP ILE VAL ASN
SEQRES 9 J 320 TRP ALA LEU HIS GLY TYR ALA THR PHE GLY MET LEU VAL
SEQRES 10 J 320 ARG GLY GLN GLY GLY SER GLU ASP THR SER VAL THR PRO
SEQRES 11 J 320 GLY GLY HIS ALA LEU GLY TRP MET THR LYS GLY ILE LEU
SEQRES 12 J 320 SER LYS ASP THR TYR TYR TYR ARG GLY VAL TYR LEU ASP
SEQRES 13 J 320 ALA VAL ARG ALA LEU GLU VAL ILE GLN SER PHE PRO GLU
SEQRES 14 J 320 VAL ASP GLU HIS ARG ILE GLY VAL ILE GLY GLY SER GLN
SEQRES 15 J 320 GLY GLY ALA LEU ALA ILE ALA ALA ALA ALA LEU SER ASP
SEQRES 16 J 320 ILE PRO LYS VAL VAL VAL ALA ASP TYR PRO TYR LEU SER
SEQRES 17 J 320 ASN PHE GLU ARG ALA VAL ASP VAL ALA LEU GLU GLN PRO
SEQRES 18 J 320 TYR LEU GLU ILE ASN SER TYR PHE ARG ARG ASN SER ASP
SEQRES 19 J 320 PRO GLU VAL GLU GLU LYS ALA PHE GLU THR LEU SER TYR
SEQRES 20 J 320 PHE ASP LEU ILE ASN LEU ALA GLY TRP VAL LYS GLN PRO
SEQRES 21 J 320 THR LEU MET ALA ILE GLY LEU ILE ASP GLN VAL THR PRO
SEQRES 22 J 320 PRO SER THR VAL PHE ALA ALA TYR ASN HIS LEU GLU THR
SEQRES 23 J 320 ASP LYS GLU LEU LYS VAL TYR ARG TYR PHE GLY HIS GLU
SEQRES 24 J 320 PHE ILE PRO ALA PHE GLN THR GLU LYS LEU SER PHE LEU
SEQRES 25 J 320 GLN LYS HIS LEU LEU LEU SER THR
SEQRES 1 K 320 MET GLN LEU PHE ASP LEU SER LEU GLU GLU LEU LYS LYS
SEQRES 2 K 320 TYR LYS PRO LYS LYS THR ALA ARG PRO ASP PHE ALA ASP
SEQRES 3 K 320 PHE TRP LYS LYS SER LEU GLU GLU LEU ARG GLN VAL GLU
SEQRES 4 K 320 ALA GLU PRO THR LEU GLU SER TYR ASP TYR PRO VAL LYS
SEQRES 5 K 320 GLY VAL LYS VAL TYR ARG LEU THR TYR GLN SER PHE GLY
SEQRES 6 K 320 HIS SER LYS ILE GLU GLY PHE TYR ALA VAL PRO ASP GLN
SEQRES 7 K 320 THR GLY PRO HIS PRO ALA LEU VAL ARG PHE HIS GLY TYR
SEQRES 8 K 320 ASN ALA SER TYR ASP ASP GLY ILE HIS ASP ILE VAL ASN
SEQRES 9 K 320 TRP ALA LEU HIS GLY TYR ALA THR PHE GLY MET LEU VAL
SEQRES 10 K 320 ARG GLY GLN GLY GLY SER GLU ASP THR SER VAL THR PRO
SEQRES 11 K 320 GLY GLY HIS ALA LEU GLY TRP MET THR LYS GLY ILE LEU
SEQRES 12 K 320 SER LYS ASP THR TYR TYR TYR ARG GLY VAL TYR LEU ASP
SEQRES 13 K 320 ALA VAL ARG ALA LEU GLU VAL ILE GLN SER PHE PRO GLU
SEQRES 14 K 320 VAL ASP GLU HIS ARG ILE GLY VAL ILE GLY GLY SER GLN
SEQRES 15 K 320 GLY GLY ALA LEU ALA ILE ALA ALA ALA ALA LEU SER ASP
SEQRES 16 K 320 ILE PRO LYS VAL VAL VAL ALA ASP TYR PRO TYR LEU SER
SEQRES 17 K 320 ASN PHE GLU ARG ALA VAL ASP VAL ALA LEU GLU GLN PRO
SEQRES 18 K 320 TYR LEU GLU ILE ASN SER TYR PHE ARG ARG ASN SER ASP
SEQRES 19 K 320 PRO GLU VAL GLU GLU LYS ALA PHE GLU THR LEU SER TYR
SEQRES 20 K 320 PHE ASP LEU ILE ASN LEU ALA GLY TRP VAL LYS GLN PRO
SEQRES 21 K 320 THR LEU MET ALA ILE GLY LEU ILE ASP GLN VAL THR PRO
SEQRES 22 K 320 PRO SER THR VAL PHE ALA ALA TYR ASN HIS LEU GLU THR
SEQRES 23 K 320 ASP LYS GLU LEU LYS VAL TYR ARG TYR PHE GLY HIS GLU
SEQRES 24 K 320 PHE ILE PRO ALA PHE GLN THR GLU LYS LEU SER PHE LEU
SEQRES 25 K 320 GLN LYS HIS LEU LEU LEU SER THR
SEQRES 1 L 320 MET GLN LEU PHE ASP LEU SER LEU GLU GLU LEU LYS LYS
SEQRES 2 L 320 TYR LYS PRO LYS LYS THR ALA ARG PRO ASP PHE ALA ASP
SEQRES 3 L 320 PHE TRP LYS LYS SER LEU GLU GLU LEU ARG GLN VAL GLU
SEQRES 4 L 320 ALA GLU PRO THR LEU GLU SER TYR ASP TYR PRO VAL LYS
SEQRES 5 L 320 GLY VAL LYS VAL TYR ARG LEU THR TYR GLN SER PHE GLY
SEQRES 6 L 320 HIS SER LYS ILE GLU GLY PHE TYR ALA VAL PRO ASP GLN
SEQRES 7 L 320 THR GLY PRO HIS PRO ALA LEU VAL ARG PHE HIS GLY TYR
SEQRES 8 L 320 ASN ALA SER TYR ASP ASP GLY ILE HIS ASP ILE VAL ASN
SEQRES 9 L 320 TRP ALA LEU HIS GLY TYR ALA THR PHE GLY MET LEU VAL
SEQRES 10 L 320 ARG GLY GLN GLY GLY SER GLU ASP THR SER VAL THR PRO
SEQRES 11 L 320 GLY GLY HIS ALA LEU GLY TRP MET THR LYS GLY ILE LEU
SEQRES 12 L 320 SER LYS ASP THR TYR TYR TYR ARG GLY VAL TYR LEU ASP
SEQRES 13 L 320 ALA VAL ARG ALA LEU GLU VAL ILE GLN SER PHE PRO GLU
SEQRES 14 L 320 VAL ASP GLU HIS ARG ILE GLY VAL ILE GLY GLY SER GLN
SEQRES 15 L 320 GLY GLY ALA LEU ALA ILE ALA ALA ALA ALA LEU SER ASP
SEQRES 16 L 320 ILE PRO LYS VAL VAL VAL ALA ASP TYR PRO TYR LEU SER
SEQRES 17 L 320 ASN PHE GLU ARG ALA VAL ASP VAL ALA LEU GLU GLN PRO
SEQRES 18 L 320 TYR LEU GLU ILE ASN SER TYR PHE ARG ARG ASN SER ASP
SEQRES 19 L 320 PRO GLU VAL GLU GLU LYS ALA PHE GLU THR LEU SER TYR
SEQRES 20 L 320 PHE ASP LEU ILE ASN LEU ALA GLY TRP VAL LYS GLN PRO
SEQRES 21 L 320 THR LEU MET ALA ILE GLY LEU ILE ASP GLN VAL THR PRO
SEQRES 22 L 320 PRO SER THR VAL PHE ALA ALA TYR ASN HIS LEU GLU THR
SEQRES 23 L 320 ASP LYS GLU LEU LYS VAL TYR ARG TYR PHE GLY HIS GLU
SEQRES 24 L 320 PHE ILE PRO ALA PHE GLN THR GLU LYS LEU SER PHE LEU
SEQRES 25 L 320 GLN LYS HIS LEU LEU LEU SER THR
FORMUL 13 HOH *1504(H2 O)
HELIX 1 1 SER A 7 TYR A 14 1 8
HELIX 2 2 ASP A 23 GLN A 37 1 15
HELIX 3 3 PHE A 64 HIS A 66 5 3
HELIX 4 4 TYR A 95 ASP A 97 5 3
HELIX 5 5 GLY A 98 HIS A 108 1 11
HELIX 6 6 TYR A 148 PHE A 167 1 20
HELIX 7 7 SER A 181 SER A 194 1 14
HELIX 8 8 ASN A 209 ALA A 217 1 9
HELIX 9 9 TYR A 222 ASN A 232 1 11
HELIX 10 10 ASP A 234 TYR A 247 1 14
HELIX 11 11 ASP A 249 ALA A 254 1 6
HELIX 12 12 GLY A 255 VAL A 257 5 3
HELIX 13 13 PRO A 273 LEU A 284 1 12
HELIX 14 14 ILE A 301 LEU A 317 1 17
HELIX 15 15 SER B 7 LYS B 12 1 6
HELIX 16 16 ASP B 23 GLN B 37 1 15
HELIX 17 17 PHE B 64 HIS B 66 5 3
HELIX 18 18 TYR B 95 ASP B 97 5 3
HELIX 19 19 GLY B 98 HIS B 108 1 11
HELIX 20 20 TYR B 148 PHE B 167 1 20
HELIX 21 21 SER B 181 SER B 194 1 14
HELIX 22 22 ASN B 209 ALA B 217 1 9
HELIX 23 23 TYR B 222 ASN B 232 1 11
HELIX 24 24 ASP B 234 TYR B 247 1 14
HELIX 25 25 ASP B 249 ALA B 254 1 6
HELIX 26 26 GLY B 255 VAL B 257 5 3
HELIX 27 27 PRO B 273 HIS B 283 1 11
HELIX 28 28 ILE B 301 LEU B 317 1 17
HELIX 29 29 SER C 7 LYS C 12 1 6
HELIX 30 30 ASP C 23 GLN C 37 1 15
HELIX 31 31 PHE C 64 HIS C 66 5 3
HELIX 32 32 TYR C 95 ASP C 97 5 3
HELIX 33 33 GLY C 98 HIS C 108 1 11
HELIX 34 34 TYR C 148 PHE C 167 1 20
HELIX 35 35 SER C 181 SER C 194 1 14
HELIX 36 36 ASN C 209 ALA C 217 1 9
HELIX 37 37 TYR C 222 ASN C 232 1 11
HELIX 38 38 ASP C 234 TYR C 247 1 14
HELIX 39 39 ASP C 249 ALA C 254 1 6
HELIX 40 40 GLY C 255 VAL C 257 5 3
HELIX 41 41 PRO C 273 HIS C 283 1 11
HELIX 42 42 ILE C 301 LEU C 317 1 17
HELIX 43 43 SER D 7 TYR D 14 1 8
HELIX 44 44 ASP D 23 GLN D 37 1 15
HELIX 45 45 PHE D 64 HIS D 66 5 3
HELIX 46 46 TYR D 95 ASP D 97 5 3
HELIX 47 47 GLY D 98 HIS D 108 1 11
HELIX 48 48 TYR D 148 PHE D 167 1 20
HELIX 49 49 SER D 181 SER D 194 1 14
HELIX 50 50 ASN D 209 ALA D 217 1 9
HELIX 51 51 TYR D 222 ASN D 232 1 11
HELIX 52 52 ASP D 234 TYR D 247 1 14
HELIX 53 53 ASP D 249 ALA D 254 1 6
HELIX 54 54 GLY D 255 VAL D 257 5 3
HELIX 55 55 PRO D 273 LEU D 284 1 12
HELIX 56 56 ILE D 301 LEU D 317 1 17
HELIX 57 57 SER E 7 TYR E 14 1 8
HELIX 58 58 ASP E 23 GLN E 37 1 15
HELIX 59 59 PHE E 64 HIS E 66 5 3
HELIX 60 60 TYR E 95 ASP E 97 5 3
HELIX 61 61 GLY E 98 HIS E 108 1 11
HELIX 62 62 TYR E 148 PHE E 167 1 20
HELIX 63 63 SER E 181 SER E 194 1 14
HELIX 64 64 ASN E 209 ALA E 217 1 9
HELIX 65 65 TYR E 222 ASN E 232 1 11
HELIX 66 66 ASP E 234 TYR E 247 1 14
HELIX 67 67 ASP E 249 ALA E 254 1 6
HELIX 68 68 GLY E 255 VAL E 257 5 3
HELIX 69 69 PRO E 273 LEU E 284 1 12
HELIX 70 70 ILE E 301 LEU E 317 1 17
HELIX 71 71 SER F 7 TYR F 14 1 8
HELIX 72 72 ASP F 23 GLN F 37 1 15
HELIX 73 73 PHE F 64 HIS F 66 5 3
HELIX 74 74 TYR F 95 ASP F 97 5 3
HELIX 75 75 GLY F 98 HIS F 108 1 11
HELIX 76 76 TYR F 148 SER F 166 1 19
HELIX 77 77 SER F 181 SER F 194 1 14
HELIX 78 78 ASN F 209 ALA F 217 1 9
HELIX 79 79 TYR F 222 ASN F 232 1 11
HELIX 80 80 ASP F 234 TYR F 247 1 14
HELIX 81 81 ASP F 249 ALA F 254 1 6
HELIX 82 82 GLY F 255 VAL F 257 5 3
HELIX 83 83 PRO F 273 LEU F 284 1 12
HELIX 84 84 ILE F 301 LEU F 316 1 16
HELIX 85 85 SER G 7 LYS G 12 1 6
HELIX 86 86 ASP G 23 GLN G 37 1 15
HELIX 87 87 PHE G 64 HIS G 66 5 3
HELIX 88 88 TYR G 95 ASP G 97 5 3
HELIX 89 89 GLY G 98 HIS G 108 1 11
HELIX 90 90 TYR G 148 SER G 166 1 19
HELIX 91 91 SER G 181 SER G 194 1 14
HELIX 92 92 ASN G 209 ALA G 217 1 9
HELIX 93 93 TYR G 222 ASN G 232 1 11
HELIX 94 94 ASP G 234 TYR G 247 1 14
HELIX 95 95 ASP G 249 ALA G 254 1 6
HELIX 96 96 GLY G 255 VAL G 257 5 3
HELIX 97 97 PRO G 273 LEU G 284 1 12
HELIX 98 98 ILE G 301 LEU G 317 1 17
HELIX 99 99 SER H 7 TYR H 14 1 8
HELIX 100 100 ASP H 23 GLN H 37 1 15
HELIX 101 101 PHE H 64 HIS H 66 5 3
HELIX 102 102 TYR H 95 ASP H 97 5 3
HELIX 103 103 GLY H 98 HIS H 108 1 11
HELIX 104 104 TYR H 148 SER H 166 1 19
HELIX 105 105 SER H 181 SER H 194 1 14
HELIX 106 106 ASN H 209 ALA H 217 1 9
HELIX 107 107 TYR H 222 ASN H 232 1 11
HELIX 108 108 ASP H 234 TYR H 247 1 14
HELIX 109 109 ASP H 249 ALA H 254 1 6
HELIX 110 110 GLY H 255 VAL H 257 5 3
HELIX 111 111 PRO H 273 LEU H 284 1 12
HELIX 112 112 ILE H 301 LEU H 317 1 17
HELIX 113 113 SER I 7 LYS I 12 1 6
HELIX 114 114 ASP I 23 GLN I 37 1 15
HELIX 115 115 PHE I 64 HIS I 66 5 3
HELIX 116 116 TYR I 95 ASP I 97 5 3
HELIX 117 117 GLY I 98 HIS I 108 1 11
HELIX 118 118 TYR I 148 PHE I 167 1 20
HELIX 119 119 SER I 181 SER I 194 1 14
HELIX 120 120 ASN I 209 ALA I 217 1 9
HELIX 121 121 TYR I 222 ASN I 232 1 11
HELIX 122 122 ASP I 234 TYR I 247 1 14
HELIX 123 123 ASP I 249 ALA I 254 1 6
HELIX 124 124 GLY I 255 VAL I 257 5 3
HELIX 125 125 PRO I 273 LEU I 284 1 12
HELIX 126 126 ILE I 301 LEU I 317 1 17
HELIX 127 127 SER J 7 LYS J 12 1 6
HELIX 128 128 ASP J 23 GLN J 37 1 15
HELIX 129 129 PHE J 64 HIS J 66 5 3
HELIX 130 130 TYR J 95 ASP J 97 5 3
HELIX 131 131 GLY J 98 HIS J 108 1 11
HELIX 132 132 TYR J 148 PHE J 167 1 20
HELIX 133 133 SER J 181 SER J 194 1 14
HELIX 134 134 ASN J 209 ALA J 217 1 9
HELIX 135 135 TYR J 222 ASN J 232 1 11
HELIX 136 136 ASP J 234 TYR J 247 1 14
HELIX 137 137 ASP J 249 ALA J 254 1 6
HELIX 138 138 GLY J 255 VAL J 257 5 3
HELIX 139 139 PRO J 273 LEU J 284 1 12
HELIX 140 140 ILE J 301 LEU J 317 1 17
HELIX 141 141 SER K 7 LYS K 12 1 6
HELIX 142 142 ASP K 23 GLN K 37 1 15
HELIX 143 143 PHE K 64 HIS K 66 5 3
HELIX 144 144 TYR K 95 ASP K 97 5 3
HELIX 145 145 GLY K 98 HIS K 108 1 11
HELIX 146 146 TYR K 148 PHE K 167 1 20
HELIX 147 147 SER K 181 SER K 194 1 14
HELIX 148 148 ASN K 209 ALA K 217 1 9
HELIX 149 149 TYR K 222 ASN K 232 1 11
HELIX 150 150 ASP K 234 TYR K 247 1 14
HELIX 151 151 ASP K 249 ALA K 254 1 6
HELIX 152 152 GLY K 255 VAL K 257 5 3
HELIX 153 153 PRO K 273 LEU K 284 1 12
HELIX 154 154 ILE K 301 LEU K 317 1 17
HELIX 155 155 SER L 7 LYS L 12 1 6
HELIX 156 156 ASP L 23 GLN L 37 1 15
HELIX 157 157 PHE L 64 HIS L 66 5 3
HELIX 158 158 TYR L 95 ASP L 97 5 3
HELIX 159 159 GLY L 98 HIS L 108 1 11
HELIX 160 160 TYR L 148 PHE L 167 1 20
HELIX 161 161 SER L 181 SER L 194 1 14
HELIX 162 162 ASN L 209 ALA L 217 1 9
HELIX 163 163 TYR L 222 ASN L 232 1 11
HELIX 164 164 ASP L 234 TYR L 247 1 14
HELIX 165 165 ASP L 249 ALA L 254 1 6
HELIX 166 166 GLY L 255 VAL L 257 5 3
HELIX 167 167 PRO L 273 LEU L 284 1 12
HELIX 168 168 ILE L 301 LEU L 317 1 17
SHEET 1 AA 9 THR A 43 SER A 46 0
SHEET 2 AA 9 VAL A 54 SER A 63 -1 O ARG A 58 N GLU A 45
SHEET 3 AA 9 SER A 67 PRO A 76 -1 O SER A 67 N SER A 63
SHEET 4 AA 9 ALA A 111 MET A 115 -1 O THR A 112 N ALA A 74
SHEET 5 AA 9 HIS A 82 PHE A 88 1 O PRO A 83 N ALA A 111
SHEET 6 AA 9 VAL A 170 GLY A 180 1 N ASP A 171 O HIS A 82
SHEET 7 AA 9 VAL A 199 ASP A 203 1 O VAL A 199 N VAL A 177
SHEET 8 AA 9 THR A 261 GLY A 266 1 O LEU A 262 N ALA A 202
SHEET 9 AA 9 LYS A 288 TYR A 293 1 O GLU A 289 N MET A 263
SHEET 1 BA 9 THR B 43 TYR B 47 0
SHEET 2 BA 9 VAL B 54 SER B 63 -1 O VAL B 56 N TYR B 47
SHEET 3 BA 9 SER B 67 PRO B 76 -1 O SER B 67 N SER B 63
SHEET 4 BA 9 ALA B 111 MET B 115 -1 O THR B 112 N ALA B 74
SHEET 5 BA 9 HIS B 82 PHE B 88 1 O PRO B 83 N ALA B 111
SHEET 6 BA 9 VAL B 170 GLY B 180 1 N ASP B 171 O HIS B 82
SHEET 7 BA 9 VAL B 199 ASP B 203 1 O VAL B 199 N VAL B 177
SHEET 8 BA 9 THR B 261 GLY B 266 1 O LEU B 262 N ALA B 202
SHEET 9 BA 9 LYS B 288 TYR B 293 1 O GLU B 289 N MET B 263
SHEET 1 CA 9 THR C 43 TYR C 47 0
SHEET 2 CA 9 VAL C 54 SER C 63 -1 O VAL C 56 N TYR C 47
SHEET 3 CA 9 SER C 67 PRO C 76 -1 O SER C 67 N SER C 63
SHEET 4 CA 9 ALA C 111 MET C 115 -1 O THR C 112 N ALA C 74
SHEET 5 CA 9 HIS C 82 PHE C 88 1 O PRO C 83 N ALA C 111
SHEET 6 CA 9 VAL C 170 GLY C 180 1 N ASP C 171 O HIS C 82
SHEET 7 CA 9 VAL C 199 ASP C 203 1 O VAL C 199 N VAL C 177
SHEET 8 CA 9 THR C 261 GLY C 266 1 O LEU C 262 N ALA C 202
SHEET 9 CA 9 LYS C 288 TYR C 293 1 O GLU C 289 N MET C 263
SHEET 1 DA 9 THR D 43 TYR D 47 0
SHEET 2 DA 9 VAL D 54 SER D 63 -1 O VAL D 56 N TYR D 47
SHEET 3 DA 9 SER D 67 PRO D 76 -1 O SER D 67 N SER D 63
SHEET 4 DA 9 ALA D 111 MET D 115 -1 O THR D 112 N ALA D 74
SHEET 5 DA 9 HIS D 82 PHE D 88 1 O PRO D 83 N ALA D 111
SHEET 6 DA 9 VAL D 170 GLY D 180 1 N ASP D 171 O HIS D 82
SHEET 7 DA 9 VAL D 199 ASP D 203 1 O VAL D 199 N VAL D 177
SHEET 8 DA 9 THR D 261 GLY D 266 1 O LEU D 262 N ALA D 202
SHEET 9 DA 9 LYS D 288 TYR D 293 1 O GLU D 289 N MET D 263
SHEET 1 EA 9 THR E 43 SER E 46 0
SHEET 2 EA 9 VAL E 54 SER E 63 -1 O ARG E 58 N GLU E 45
SHEET 3 EA 9 SER E 67 PRO E 76 -1 O SER E 67 N SER E 63
SHEET 4 EA 9 ALA E 111 MET E 115 -1 O THR E 112 N ALA E 74
SHEET 5 EA 9 HIS E 82 PHE E 88 1 O PRO E 83 N ALA E 111
SHEET 6 EA 9 VAL E 170 GLY E 180 1 N ASP E 171 O HIS E 82
SHEET 7 EA 9 VAL E 199 ASP E 203 1 O VAL E 199 N VAL E 177
SHEET 8 EA 9 THR E 261 GLY E 266 1 O LEU E 262 N ALA E 202
SHEET 9 EA 9 LYS E 288 TYR E 293 1 O GLU E 289 N MET E 263
SHEET 1 FA 9 THR F 43 SER F 46 0
SHEET 2 FA 9 VAL F 54 SER F 63 -1 O ARG F 58 N GLU F 45
SHEET 3 FA 9 SER F 67 PRO F 76 -1 O SER F 67 N SER F 63
SHEET 4 FA 9 ALA F 111 MET F 115 -1 O THR F 112 N ALA F 74
SHEET 5 FA 9 HIS F 82 PHE F 88 1 O PRO F 83 N ALA F 111
SHEET 6 FA 9 VAL F 170 GLY F 180 1 N ASP F 171 O HIS F 82
SHEET 7 FA 9 VAL F 199 ASP F 203 1 O VAL F 199 N VAL F 177
SHEET 8 FA 9 THR F 261 GLY F 266 1 O LEU F 262 N ALA F 202
SHEET 9 FA 9 LYS F 288 TYR F 293 1 O GLU F 289 N MET F 263
SHEET 1 GA 9 THR G 43 SER G 46 0
SHEET 2 GA 9 VAL G 54 SER G 63 -1 O ARG G 58 N GLU G 45
SHEET 3 GA 9 SER G 67 PRO G 76 -1 O SER G 67 N SER G 63
SHEET 4 GA 9 ALA G 111 MET G 115 -1 O THR G 112 N ALA G 74
SHEET 5 GA 9 HIS G 82 PHE G 88 1 O PRO G 83 N ALA G 111
SHEET 6 GA 9 VAL G 170 GLY G 180 1 N ASP G 171 O HIS G 82
SHEET 7 GA 9 VAL G 199 ASP G 203 1 O VAL G 199 N VAL G 177
SHEET 8 GA 9 THR G 261 GLY G 266 1 O LEU G 262 N ALA G 202
SHEET 9 GA 9 LYS G 288 TYR G 293 1 O GLU G 289 N MET G 263
SHEET 1 HA 9 THR H 43 SER H 46 0
SHEET 2 HA 9 VAL H 54 SER H 63 -1 O ARG H 58 N GLU H 45
SHEET 3 HA 9 SER H 67 PRO H 76 -1 O SER H 67 N SER H 63
SHEET 4 HA 9 ALA H 111 MET H 115 -1 O THR H 112 N ALA H 74
SHEET 5 HA 9 HIS H 82 PHE H 88 1 O PRO H 83 N ALA H 111
SHEET 6 HA 9 VAL H 170 GLY H 180 1 N ASP H 171 O HIS H 82
SHEET 7 HA 9 VAL H 199 ASP H 203 1 O VAL H 199 N VAL H 177
SHEET 8 HA 9 THR H 261 GLY H 266 1 O LEU H 262 N ALA H 202
SHEET 9 HA 9 LYS H 288 TYR H 293 1 O GLU H 289 N MET H 263
SHEET 1 IA 9 THR I 43 SER I 46 0
SHEET 2 IA 9 VAL I 54 SER I 63 -1 O ARG I 58 N GLU I 45
SHEET 3 IA 9 SER I 67 PRO I 76 -1 O SER I 67 N SER I 63
SHEET 4 IA 9 ALA I 111 MET I 115 -1 O THR I 112 N ALA I 74
SHEET 5 IA 9 HIS I 82 PHE I 88 1 O PRO I 83 N ALA I 111
SHEET 6 IA 9 VAL I 170 GLY I 180 1 N ASP I 171 O HIS I 82
SHEET 7 IA 9 VAL I 199 ASP I 203 1 O VAL I 199 N VAL I 177
SHEET 8 IA 9 THR I 261 GLY I 266 1 O LEU I 262 N ALA I 202
SHEET 9 IA 9 LYS I 288 TYR I 293 1 O GLU I 289 N MET I 263
SHEET 1 JA 9 THR J 43 SER J 46 0
SHEET 2 JA 9 VAL J 54 SER J 63 -1 O ARG J 58 N GLU J 45
SHEET 3 JA 9 SER J 67 PRO J 76 -1 O SER J 67 N SER J 63
SHEET 4 JA 9 ALA J 111 MET J 115 -1 O THR J 112 N ALA J 74
SHEET 5 JA 9 HIS J 82 PHE J 88 1 O PRO J 83 N ALA J 111
SHEET 6 JA 9 VAL J 170 GLY J 180 1 N ASP J 171 O HIS J 82
SHEET 7 JA 9 VAL J 199 ASP J 203 1 O VAL J 199 N VAL J 177
SHEET 8 JA 9 THR J 261 GLY J 266 1 O LEU J 262 N ALA J 202
SHEET 9 JA 9 LYS J 288 TYR J 293 1 O GLU J 289 N MET J 263
SHEET 1 KA 9 THR K 43 SER K 46 0
SHEET 2 KA 9 VAL K 54 SER K 63 -1 O ARG K 58 N GLU K 45
SHEET 3 KA 9 SER K 67 PRO K 76 -1 O SER K 67 N SER K 63
SHEET 4 KA 9 ALA K 111 MET K 115 -1 O THR K 112 N ALA K 74
SHEET 5 KA 9 HIS K 82 PHE K 88 1 O PRO K 83 N ALA K 111
SHEET 6 KA 9 VAL K 170 GLY K 180 1 N ASP K 171 O HIS K 82
SHEET 7 KA 9 VAL K 199 ASP K 203 1 O VAL K 199 N VAL K 177
SHEET 8 KA 9 THR K 261 GLY K 266 1 O LEU K 262 N ALA K 202
SHEET 9 KA 9 LYS K 288 TYR K 293 1 O GLU K 289 N MET K 263
SHEET 1 LA 9 THR L 43 SER L 46 0
SHEET 2 LA 9 VAL L 54 SER L 63 -1 O ARG L 58 N GLU L 45
SHEET 3 LA 9 SER L 67 PRO L 76 -1 O SER L 67 N SER L 63
SHEET 4 LA 9 ALA L 111 MET L 115 -1 O THR L 112 N ALA L 74
SHEET 5 LA 9 HIS L 82 PHE L 88 1 O PRO L 83 N ALA L 111
SHEET 6 LA 9 VAL L 170 GLY L 180 1 N ASP L 171 O HIS L 82
SHEET 7 LA 9 VAL L 199 ASP L 203 1 O VAL L 199 N VAL L 177
SHEET 8 LA 9 THR L 261 GLY L 266 1 O LEU L 262 N ALA L 202
SHEET 9 LA 9 LYS L 288 TYR L 293 1 O GLU L 289 N MET L 263
CISPEP 1 GLY A 80 PRO A 81 0 0.07
CISPEP 2 GLN A 220 PRO A 221 0 4.79
CISPEP 3 GLY B 80 PRO B 81 0 0.78
CISPEP 4 GLN B 220 PRO B 221 0 2.38
CISPEP 5 GLY C 80 PRO C 81 0 0.54
CISPEP 6 GLN C 220 PRO C 221 0 4.77
CISPEP 7 GLY D 80 PRO D 81 0 -0.16
CISPEP 8 GLN D 220 PRO D 221 0 2.72
CISPEP 9 GLY E 80 PRO E 81 0 0.46
CISPEP 10 GLN E 220 PRO E 221 0 2.28
CISPEP 11 GLY F 80 PRO F 81 0 0.92
CISPEP 12 GLN F 220 PRO F 221 0 2.77
CISPEP 13 GLY G 80 PRO G 81 0 2.31
CISPEP 14 GLN G 220 PRO G 221 0 4.31
CISPEP 15 GLY H 80 PRO H 81 0 0.12
CISPEP 16 GLN H 220 PRO H 221 0 1.60
CISPEP 17 GLY I 80 PRO I 81 0 0.85
CISPEP 18 GLN I 220 PRO I 221 0 2.02
CISPEP 19 GLY J 80 PRO J 81 0 1.78
CISPEP 20 GLN J 220 PRO J 221 0 4.10
CISPEP 21 GLY K 80 PRO K 81 0 0.09
CISPEP 22 GLN K 220 PRO K 221 0 2.02
CISPEP 23 GLY L 80 PRO L 81 0 1.14
CISPEP 24 GLN L 220 PRO L 221 0 2.47
CRYST1 143.477 87.301 184.291 90.00 112.89 90.00 P 1 21 1 24
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.006970 0.000000 0.002943 0.00000
SCALE2 0.000000 0.011455 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005890 0.00000
MTRIX1 1 -0.528400 0.662300 -0.531200 36.67000 1
MTRIX2 1 0.666200 -0.064440 -0.743000 73.00000 1
MTRIX3 1 -0.526300 -0.746500 -0.407100 124.40000 1
MTRIX1 2 -0.811100 0.524600 0.258600 -26.93000 1
MTRIX2 2 0.521300 0.448000 0.726300 -53.79000 1
MTRIX3 2 0.265200 0.723000 -0.636900 126.90000 1
MTRIX1 3 -0.931900 -0.075580 -0.354700 30.30000 1
MTRIX2 3 -0.050300 -0.941600 0.332800 -5.70000 1
MTRIX3 3 -0.359100 0.328000 0.873700 6.76300 1
MTRIX1 4 -0.521900 0.668700 -0.529600 36.44000 1
MTRIX2 4 0.666800 -0.067430 -0.742200 73.04000 1
MTRIX3 4 -0.532000 -0.740500 -0.410700 124.70000 1
MTRIX1 5 -0.931900 -0.071100 -0.355600 30.40000 1
MTRIX2 5 -0.054100 -0.942000 0.330200 -5.50500 1
MTRIX3 5 -0.358500 0.327000 0.874400 6.81200 1
MTRIX1 6 -0.829400 0.469300 0.302900 5.94700 1
MTRIX2 6 -0.521100 -0.454600 -0.722400 53.55000 1
MTRIX3 6 -0.201000 -0.757000 0.621600 -43.07000 1
TER 2513 LEU A 317
TER 5026 LEU B 317
TER 7531 LEU C 317
TER 10036 LEU D 317
TER 12538 LEU E 317
TER 15043 LEU F 317
TER 17548 LEU G 317
TER 20050 LEU H 317
TER 22552 LEU I 317
TER 25054 LEU J 317
TER 27556 LEU K 317
TER 30062 LEU L 317
MASTER 2213 0 0 168 108 0 0 2431554 12 0 300
END |