| 2XLC-pdb | HEADER HYDROLASE 20-JUL-10 2XLC
TITLE ACETYL XYLAN ESTERASE FROM BACILLUS PUMILUS CECT5072 BOUND
TITLE 2 TO PARAOXON
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYL XYLAN ESTERASE;
COMPND 3 CHAIN: A, B, C, D, E, F;
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, 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 2XLC 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. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0066
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) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.62
REMARK 3 NUMBER OF REFLECTIONS : 46958
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) : 0.21731
REMARK 3 R VALUE (WORKING SET) : 0.21631
REMARK 3 FREE R VALUE : 0.23608
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.1
REMARK 3 FREE R VALUE TEST SET COUNT : 2507
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.700
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.769
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3385
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.22
REMARK 3 BIN R VALUE (WORKING SET) : 0.309
REMARK 3 BIN FREE R VALUE SET COUNT : 187
REMARK 3 BIN FREE R VALUE : 0.323
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 14506
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 48
REMARK 3 SOLVENT ATOMS : 40
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 54.137
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.763
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.90
REMARK 3 B22 (A**2) : -0.02
REMARK 3 B33 (A**2) : -3.49
REMARK 3 B12 (A**2) : 0.00
REMARK 3 B13 (A**2) : 0.73
REMARK 3 B23 (A**2) : 0.00
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.362
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.281
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 30.858
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.923
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.912
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 14969 ; 0.003 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 20437 ; 0.635 ; 1.948
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1862 ; 3.892 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 689 ;28.924 ;23.657
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2112 ;14.392 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 66 ;19.436 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2222 ; 0.047 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 11732 ; 0.003 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 9292 ; 0.162 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 14854 ; 0.314 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 5677 ; 0.424 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 5583 ; 0.697 ; 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
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 7 A 318 3
REMARK 3 1 B 7 B 318 3
REMARK 3 1 C 7 C 318 3
REMARK 3 1 D 7 D 318 3
REMARK 3 1 E 7 E 318 3
REMARK 3 1 F 7 F 318 3
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 1180 ; 0.01 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 B (A): 1180 ; 0.01 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 C (A): 1180 ; 0.01 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 D (A): 1180 ; 0.01 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 E (A): 1180 ; 0.01 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 F (A): 1180 ; 0.01 ; 0.05
REMARK 3 LOOSE POSITIONAL 1 A (A): 1123 ; 0.01 ; 5.00
REMARK 3 LOOSE POSITIONAL 1 B (A): 1123 ; 0.03 ; 5.00
REMARK 3 LOOSE POSITIONAL 1 C (A): 1123 ; 0.01 ; 5.00
REMARK 3 LOOSE POSITIONAL 1 D (A): 1123 ; 0.01 ; 5.00
REMARK 3 LOOSE POSITIONAL 1 E (A): 1123 ; 0.01 ; 5.00
REMARK 3 LOOSE POSITIONAL 1 F (A): 1123 ; 0.01 ; 5.00
REMARK 3 TIGHT THERMAL 1 A (A**2): 1180 ; 0.02 ; 0.50
REMARK 3 TIGHT THERMAL 1 B (A**2): 1180 ; 0.02 ; 0.50
REMARK 3 TIGHT THERMAL 1 C (A**2): 1180 ; 0.02 ; 0.50
REMARK 3 TIGHT THERMAL 1 D (A**2): 1180 ; 0.01 ; 0.50
REMARK 3 TIGHT THERMAL 1 E (A**2): 1180 ; 0.02 ; 0.50
REMARK 3 TIGHT THERMAL 1 F (A**2): 1180 ; 0.02 ; 0.50
REMARK 3 LOOSE THERMAL 1 A (A**2): 1123 ; 0.02 ; 10.00
REMARK 3 LOOSE THERMAL 1 B (A**2): 1123 ; 0.02 ; 10.00
REMARK 3 LOOSE THERMAL 1 C (A**2): 1123 ; 0.02 ; 10.00
REMARK 3 LOOSE THERMAL 1 D (A**2): 1123 ; 0.02 ; 10.00
REMARK 3 LOOSE THERMAL 1 E (A**2): 1123 ; 0.02 ; 10.00
REMARK 3 LOOSE THERMAL 1 F (A**2): 1123 ; 0.02 ; 10.00
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 30
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 7 A 56
REMARK 3 ORIGIN FOR THE GROUP (A): -24.4422 -4.2259 53.5746
REMARK 3 T TENSOR
REMARK 3 T11: 0.1928 T22: 0.1595
REMARK 3 T33: 0.0631 T12: -0.0621
REMARK 3 T13: 0.0698 T23: 0.0023
REMARK 3 L TENSOR
REMARK 3 L11: 0.8365 L22: 1.8246
REMARK 3 L33: 0.7656 L12: -0.6360
REMARK 3 L13: -0.1075 L23: 0.4586
REMARK 3 S TENSOR
REMARK 3 S11: 0.0025 S12: -0.1548 S13: -0.0142
REMARK 3 S21: 0.0862 S22: 0.0946 S23: -0.1218
REMARK 3 S31: 0.0354 S32: 0.0959 S33: -0.0972
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 57 A 87
REMARK 3 ORIGIN FOR THE GROUP (A): -28.2855 9.9469 56.0819
REMARK 3 T TENSOR
REMARK 3 T11: 0.2882 T22: 0.1590
REMARK 3 T33: 0.0560 T12: -0.1088
REMARK 3 T13: 0.1031 T23: -0.0083
REMARK 3 L TENSOR
REMARK 3 L11: 3.3837 L22: 2.9827
REMARK 3 L33: 3.1623 L12: -1.0480
REMARK 3 L13: 0.9977 L23: -0.2150
REMARK 3 S TENSOR
REMARK 3 S11: 0.1204 S12: 0.1610 S13: 0.2623
REMARK 3 S21: 0.1491 S22: -0.0585 S23: 0.0356
REMARK 3 S31: -0.1848 S32: 0.0313 S33: -0.0618
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 88 A 136
REMARK 3 ORIGIN FOR THE GROUP (A): -19.5763 6.1263 49.2155
REMARK 3 T TENSOR
REMARK 3 T11: 0.3136 T22: 0.1259
REMARK 3 T33: 0.1216 T12: -0.0960
REMARK 3 T13: 0.0059 T23: -0.0102
REMARK 3 L TENSOR
REMARK 3 L11: 3.3175 L22: 1.1158
REMARK 3 L33: 0.7368 L12: -1.7873
REMARK 3 L13: 0.3111 L23: -0.2307
REMARK 3 S TENSOR
REMARK 3 S11: 0.2440 S12: -0.0558 S13: 0.0230
REMARK 3 S21: 0.0636 S22: -0.0761 S23: -0.0241
REMARK 3 S31: -0.0979 S32: 0.0159 S33: -0.1680
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 137 A 222
REMARK 3 ORIGIN FOR THE GROUP (A): -22.7173 -4.4188 50.7361
REMARK 3 T TENSOR
REMARK 3 T11: 0.2716 T22: 0.1620
REMARK 3 T33: 0.1069 T12: -0.0800
REMARK 3 T13: 0.0287 T23: 0.0140
REMARK 3 L TENSOR
REMARK 3 L11: 1.5174 L22: 0.8869
REMARK 3 L33: 1.1593 L12: -0.4698
REMARK 3 L13: -0.2072 L23: 0.4317
REMARK 3 S TENSOR
REMARK 3 S11: -0.0646 S12: 0.0130 S13: -0.1245
REMARK 3 S21: 0.0452 S22: 0.0077 S23: -0.0390
REMARK 3 S31: -0.0043 S32: -0.0335 S33: 0.0569
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 223 A 317
REMARK 3 ORIGIN FOR THE GROUP (A): -23.0727 -9.3478 41.5505
REMARK 3 T TENSOR
REMARK 3 T11: 0.2353 T22: 0.1292
REMARK 3 T33: 0.1482 T12: -0.0484
REMARK 3 T13: -0.0009 T23: 0.0162
REMARK 3 L TENSOR
REMARK 3 L11: 1.0759 L22: 0.5870
REMARK 3 L33: 0.7789 L12: 0.0212
REMARK 3 L13: 0.2917 L23: 0.2054
REMARK 3 S TENSOR
REMARK 3 S11: 0.0935 S12: -0.1059 S13: -0.1110
REMARK 3 S21: -0.0145 S22: -0.0524 S23: -0.0031
REMARK 3 S31: 0.0816 S32: 0.0299 S33: -0.0411
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 7 B 56
REMARK 3 ORIGIN FOR THE GROUP (A): -27.1888 26.0924 17.7038
REMARK 3 T TENSOR
REMARK 3 T11: 0.1531 T22: 0.0567
REMARK 3 T33: 0.0999 T12: 0.0171
REMARK 3 T13: 0.0313 T23: -0.0077
REMARK 3 L TENSOR
REMARK 3 L11: 2.3378 L22: 0.7936
REMARK 3 L33: 2.2502 L12: 0.1845
REMARK 3 L13: -0.5893 L23: -0.7806
REMARK 3 S TENSOR
REMARK 3 S11: -0.0805 S12: 0.2758 S13: 0.1654
REMARK 3 S21: -0.0060 S22: 0.0280 S23: 0.0909
REMARK 3 S31: -0.1183 S32: -0.2441 S33: 0.0525
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 57 B 87
REMARK 3 ORIGIN FOR THE GROUP (A): -39.3727 20.2194 22.7392
REMARK 3 T TENSOR
REMARK 3 T11: 0.2519 T22: 0.1492
REMARK 3 T33: 0.2372 T12: 0.0464
REMARK 3 T13: 0.0755 T23: 0.0006
REMARK 3 L TENSOR
REMARK 3 L11: 1.9710 L22: 0.7133
REMARK 3 L33: 7.8947 L12: 0.8693
REMARK 3 L13: -2.5506 L23: -0.0181
REMARK 3 S TENSOR
REMARK 3 S11: 0.0186 S12: 0.2468 S13: 0.0401
REMARK 3 S21: 0.0550 S22: 0.0897 S23: -0.0081
REMARK 3 S31: -0.0130 S32: -0.7480 S33: -0.1083
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 88 B 136
REMARK 3 ORIGIN FOR THE GROUP (A): -29.3396 14.7550 20.6313
REMARK 3 T TENSOR
REMARK 3 T11: 0.2217 T22: 0.1853
REMARK 3 T33: 0.1945 T12: 0.0225
REMARK 3 T13: 0.0474 T23: 0.0183
REMARK 3 L TENSOR
REMARK 3 L11: 1.7893 L22: 0.8888
REMARK 3 L33: 1.8753 L12: 0.1959
REMARK 3 L13: -1.7864 L23: -0.4760
REMARK 3 S TENSOR
REMARK 3 S11: -0.1234 S12: -0.0602 S13: -0.1382
REMARK 3 S21: -0.0071 S22: 0.0501 S23: 0.1758
REMARK 3 S31: 0.1355 S32: 0.0428 S33: 0.0733
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 137 B 222
REMARK 3 ORIGIN FOR THE GROUP (A): -24.4114 24.4356 18.3149
REMARK 3 T TENSOR
REMARK 3 T11: 0.2275 T22: 0.0953
REMARK 3 T33: 0.1634 T12: -0.0022
REMARK 3 T13: 0.0593 T23: 0.0205
REMARK 3 L TENSOR
REMARK 3 L11: 1.1322 L22: 1.1831
REMARK 3 L33: 1.5478 L12: 0.0542
REMARK 3 L13: -0.8014 L23: 0.6766
REMARK 3 S TENSOR
REMARK 3 S11: 0.0192 S12: 0.0947 S13: 0.0130
REMARK 3 S21: 0.1255 S22: -0.0013 S23: 0.0242
REMARK 3 S31: 0.0903 S32: -0.0778 S33: -0.0179
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 223 B 317
REMARK 3 ORIGIN FOR THE GROUP (A): -15.1322 24.8861 23.0835
REMARK 3 T TENSOR
REMARK 3 T11: 0.2821 T22: 0.1122
REMARK 3 T33: 0.1701 T12: -0.0296
REMARK 3 T13: 0.0589 T23: -0.0036
REMARK 3 L TENSOR
REMARK 3 L11: 0.4859 L22: 0.4838
REMARK 3 L33: 1.1234 L12: 0.0857
REMARK 3 L13: 0.6857 L23: 0.0157
REMARK 3 S TENSOR
REMARK 3 S11: 0.0193 S12: -0.0094 S13: 0.0537
REMARK 3 S21: 0.0739 S22: -0.0108 S23: -0.0038
REMARK 3 S31: -0.0541 S32: 0.0880 S33: -0.0085
REMARK 3
REMARK 3 TLS GROUP : 11
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 7 C 56
REMARK 3 ORIGIN FOR THE GROUP (A): 23.7552 -26.0665 25.6376
REMARK 3 T TENSOR
REMARK 3 T11: 0.1683 T22: 0.2098
REMARK 3 T33: 0.1737 T12: 0.1037
REMARK 3 T13: -0.0032 T23: 0.1335
REMARK 3 L TENSOR
REMARK 3 L11: 2.4257 L22: 1.4298
REMARK 3 L33: 2.2741 L12: 0.4824
REMARK 3 L13: 0.0138 L23: 1.0077
REMARK 3 S TENSOR
REMARK 3 S11: -0.0651 S12: -0.1655 S13: -0.3046
REMARK 3 S21: 0.0498 S22: 0.0259 S23: -0.2370
REMARK 3 S31: 0.1380 S32: 0.3697 S33: 0.0392
REMARK 3
REMARK 3 TLS GROUP : 12
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 57 C 87
REMARK 3 ORIGIN FOR THE GROUP (A): 33.9996 -19.6854 32.7331
REMARK 3 T TENSOR
REMARK 3 T11: 0.1353 T22: 0.6020
REMARK 3 T33: 0.2762 T12: 0.0917
REMARK 3 T13: -0.0160 T23: 0.1182
REMARK 3 L TENSOR
REMARK 3 L11: 1.5769 L22: 3.1504
REMARK 3 L33: 4.8893 L12: 1.6658
REMARK 3 L13: -0.6504 L23: 1.8474
REMARK 3 S TENSOR
REMARK 3 S11: 0.1745 S12: -0.3859 S13: -0.2337
REMARK 3 S21: 0.1277 S22: 0.1023 S23: -0.4442
REMARK 3 S31: -0.1784 S32: 1.1238 S33: -0.2768
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 88 C 136
REMARK 3 ORIGIN FOR THE GROUP (A): 24.6425 -14.6517 28.0328
REMARK 3 T TENSOR
REMARK 3 T11: 0.1366 T22: 0.4124
REMARK 3 T33: 0.2565 T12: 0.0695
REMARK 3 T13: -0.0340 T23: 0.0828
REMARK 3 L TENSOR
REMARK 3 L11: 0.2275 L22: 1.2864
REMARK 3 L33: 1.6253 L12: 0.1816
REMARK 3 L13: 0.2265 L23: -0.0678
REMARK 3 S TENSOR
REMARK 3 S11: -0.1114 S12: -0.1631 S13: -0.0235
REMARK 3 S21: 0.1461 S22: -0.0720 S23: -0.1406
REMARK 3 S31: -0.0892 S32: 0.4000 S33: 0.1835
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 137 C 222
REMARK 3 ORIGIN FOR THE GROUP (A): 20.3846 -24.4969 25.2464
REMARK 3 T TENSOR
REMARK 3 T11: 0.1971 T22: 0.2394
REMARK 3 T33: 0.2503 T12: 0.0935
REMARK 3 T13: 0.0050 T23: 0.1221
REMARK 3 L TENSOR
REMARK 3 L11: 1.0804 L22: 0.3269
REMARK 3 L33: 2.0019 L12: 0.5801
REMARK 3 L13: 0.3397 L23: 0.0794
REMARK 3 S TENSOR
REMARK 3 S11: -0.0648 S12: -0.1394 S13: -0.0016
REMARK 3 S21: -0.0074 S22: -0.1063 S23: -0.0238
REMARK 3 S31: 0.2527 S32: 0.3882 S33: 0.1711
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 223 C 317
REMARK 3 ORIGIN FOR THE GROUP (A): 10.3407 -25.0297 27.6850
REMARK 3 T TENSOR
REMARK 3 T11: 0.1756 T22: 0.1882
REMARK 3 T33: 0.2300 T12: 0.0264
REMARK 3 T13: 0.0192 T23: 0.0555
REMARK 3 L TENSOR
REMARK 3 L11: 0.6137 L22: 0.4867
REMARK 3 L33: 0.8187 L12: -0.1356
REMARK 3 L13: -0.2381 L23: 0.1540
REMARK 3 S TENSOR
REMARK 3 S11: -0.0992 S12: -0.2083 S13: -0.0949
REMARK 3 S21: 0.0506 S22: 0.0029 S23: -0.0362
REMARK 3 S31: 0.0928 S32: 0.1219 S33: 0.0963
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 : D 7 D 56
REMARK 3 ORIGIN FOR THE GROUP (A): 12.5390 6.2477 57.8477
REMARK 3 T TENSOR
REMARK 3 T11: 0.3247 T22: 0.3259
REMARK 3 T33: 0.1175 T12: -0.1608
REMARK 3 T13: -0.1200 T23: -0.0110
REMARK 3 L TENSOR
REMARK 3 L11: 1.7244 L22: 2.2972
REMARK 3 L33: 2.3035 L12: -1.1880
REMARK 3 L13: -0.7494 L23: -1.0833
REMARK 3 S TENSOR
REMARK 3 S11: 0.0161 S12: -0.4008 S13: 0.0244
REMARK 3 S21: 0.4369 S22: 0.1351 S23: -0.0078
REMARK 3 S31: -0.3978 S32: 0.4714 S33: -0.1512
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 : D 57 D 87
REMARK 3 ORIGIN FOR THE GROUP (A): 15.6567 -7.3595 62.0563
REMARK 3 T TENSOR
REMARK 3 T11: 0.2952 T22: 0.4961
REMARK 3 T33: 0.1646 T12: -0.0789
REMARK 3 T13: -0.1221 T23: 0.0915
REMARK 3 L TENSOR
REMARK 3 L11: 1.2824 L22: 1.1538
REMARK 3 L33: 0.9082 L12: -0.4457
REMARK 3 L13: -0.1648 L23: 0.9381
REMARK 3 S TENSOR
REMARK 3 S11: 0.0443 S12: -0.0161 S13: -0.0442
REMARK 3 S21: 0.2653 S22: 0.0038 S23: -0.0639
REMARK 3 S31: 0.2375 S32: 0.2405 S33: -0.0482
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 : D 88 D 136
REMARK 3 ORIGIN FOR THE GROUP (A): 8.8608 -4.2300 53.1290
REMARK 3 T TENSOR
REMARK 3 T11: 0.3119 T22: 0.4810
REMARK 3 T33: 0.1812 T12: -0.1104
REMARK 3 T13: -0.0448 T23: 0.0131
REMARK 3 L TENSOR
REMARK 3 L11: 0.2226 L22: 1.0344
REMARK 3 L33: 0.6224 L12: -0.3675
REMARK 3 L13: -0.3642 L23: 0.5422
REMARK 3 S TENSOR
REMARK 3 S11: 0.0780 S12: -0.1593 S13: -0.0226
REMARK 3 S21: 0.0451 S22: -0.1085 S23: 0.0371
REMARK 3 S31: -0.0685 S32: 0.3350 S33: 0.0304
REMARK 3
REMARK 3 TLS GROUP : 19
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 137 D 222
REMARK 3 ORIGIN FOR THE GROUP (A): 11.6109 6.4359 54.5483
REMARK 3 T TENSOR
REMARK 3 T11: 0.3515 T22: 0.4000
REMARK 3 T33: 0.1653 T12: -0.1651
REMARK 3 T13: -0.0720 T23: -0.0023
REMARK 3 L TENSOR
REMARK 3 L11: 0.8111 L22: 0.5308
REMARK 3 L33: 0.4987 L12: -0.1438
REMARK 3 L13: -0.5868 L23: -0.0047
REMARK 3 S TENSOR
REMARK 3 S11: 0.0485 S12: -0.1947 S13: -0.0089
REMARK 3 S21: 0.2265 S22: -0.0777 S23: 0.0264
REMARK 3 S31: -0.1254 S32: 0.2913 S33: 0.0292
REMARK 3
REMARK 3 TLS GROUP : 20
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 223 D 317
REMARK 3 ORIGIN FOR THE GROUP (A): 13.8030 10.7772 45.2712
REMARK 3 T TENSOR
REMARK 3 T11: 0.3275 T22: 0.3348
REMARK 3 T33: 0.1613 T12: -0.1297
REMARK 3 T13: -0.0517 T23: 0.0020
REMARK 3 L TENSOR
REMARK 3 L11: 1.2201 L22: 0.3353
REMARK 3 L33: 0.8659 L12: 0.0423
REMARK 3 L13: -0.7091 L23: 0.2185
REMARK 3 S TENSOR
REMARK 3 S11: 0.1067 S12: -0.1675 S13: 0.1010
REMARK 3 S21: 0.0877 S22: -0.0372 S23: -0.1196
REMARK 3 S31: -0.1731 S32: 0.3276 S33: -0.0695
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 : E 7 E 56
REMARK 3 ORIGIN FOR THE GROUP (A): -22.5090 -4.2196 -6.2189
REMARK 3 T TENSOR
REMARK 3 T11: 0.2023 T22: 0.2083
REMARK 3 T33: 0.0856 T12: 0.0607
REMARK 3 T13: 0.0053 T23: 0.0022
REMARK 3 L TENSOR
REMARK 3 L11: 2.4523 L22: 1.7746
REMARK 3 L33: 1.8228 L12: 0.9567
REMARK 3 L13: -1.3536 L23: -1.2921
REMARK 3 S TENSOR
REMARK 3 S11: 0.0276 S12: 0.3563 S13: 0.0115
REMARK 3 S21: -0.0940 S22: 0.2284 S23: 0.1673
REMARK 3 S31: -0.1278 S32: -0.4383 S33: -0.2561
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 : E 57 E 87
REMARK 3 ORIGIN FOR THE GROUP (A): -15.2205 4.3044 -15.3524
REMARK 3 T TENSOR
REMARK 3 T11: 0.3633 T22: 0.1690
REMARK 3 T33: 0.0899 T12: 0.0620
REMARK 3 T13: -0.0478 T23: -0.0013
REMARK 3 L TENSOR
REMARK 3 L11: 3.5609 L22: 2.5686
REMARK 3 L33: 0.9019 L12: -1.7520
REMARK 3 L13: -1.2347 L23: -0.1995
REMARK 3 S TENSOR
REMARK 3 S11: -0.0679 S12: 0.2753 S13: 0.1518
REMARK 3 S21: -0.0793 S22: 0.1606 S23: 0.0631
REMARK 3 S31: -0.1050 S32: -0.2879 S33: -0.0926
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 : E 88 E 136
REMARK 3 ORIGIN FOR THE GROUP (A): -14.2147 4.0438 -3.7093
REMARK 3 T TENSOR
REMARK 3 T11: 0.3000 T22: 0.2064
REMARK 3 T33: 0.1094 T12: 0.0617
REMARK 3 T13: 0.0380 T23: 0.0346
REMARK 3 L TENSOR
REMARK 3 L11: 1.4586 L22: 0.5722
REMARK 3 L33: 1.9523 L12: -0.2880
REMARK 3 L13: -1.5486 L23: 0.6893
REMARK 3 S TENSOR
REMARK 3 S11: 0.0930 S12: 0.0761 S13: 0.0718
REMARK 3 S21: -0.0378 S22: -0.0530 S23: 0.0819
REMARK 3 S31: -0.2019 S32: -0.0967 S33: -0.0400
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 : E 137 E 222
REMARK 3 ORIGIN FOR THE GROUP (A): -20.8494 -4.8440 -3.1051
REMARK 3 T TENSOR
REMARK 3 T11: 0.1679 T22: 0.2310
REMARK 3 T33: 0.1519 T12: 0.0603
REMARK 3 T13: 0.0043 T23: 0.0237
REMARK 3 L TENSOR
REMARK 3 L11: 0.9210 L22: 1.1718
REMARK 3 L33: 2.5095 L12: -0.3418
REMARK 3 L13: -1.4359 L23: 0.0840
REMARK 3 S TENSOR
REMARK 3 S11: 0.0731 S12: 0.1311 S13: -0.0314
REMARK 3 S21: 0.0522 S22: -0.0067 S23: 0.1304
REMARK 3 S31: -0.2189 S32: -0.3353 S33: -0.0664
REMARK 3
REMARK 3 TLS GROUP : 25
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 223 E 318
REMARK 3 ORIGIN FOR THE GROUP (A): -16.6257 -12.0141 3.0216
REMARK 3 T TENSOR
REMARK 3 T11: 0.1390 T22: 0.1601
REMARK 3 T33: 0.1815 T12: 0.0042
REMARK 3 T13: 0.0133 T23: 0.0173
REMARK 3 L TENSOR
REMARK 3 L11: 0.9990 L22: 0.5332
REMARK 3 L33: 0.6879 L12: -0.3247
REMARK 3 L13: -0.4070 L23: 0.1354
REMARK 3 S TENSOR
REMARK 3 S11: 0.0174 S12: 0.1413 S13: -0.0324
REMARK 3 S21: 0.0366 S22: 0.0049 S23: 0.0303
REMARK 3 S31: -0.0075 S32: -0.2423 S33: -0.0223
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 : F 7 F 56
REMARK 3 ORIGIN FOR THE GROUP (A): 23.9944 2.3941 -0.7695
REMARK 3 T TENSOR
REMARK 3 T11: 0.2120 T22: 0.0930
REMARK 3 T33: 0.0814 T12: -0.0701
REMARK 3 T13: 0.0631 T23: -0.0104
REMARK 3 L TENSOR
REMARK 3 L11: 1.9694 L22: 2.8428
REMARK 3 L33: 3.4450 L12: -0.1038
REMARK 3 L13: 0.6046 L23: 2.2334
REMARK 3 S TENSOR
REMARK 3 S11: 0.1398 S12: -0.0395 S13: 0.0810
REMARK 3 S21: 0.1660 S22: 0.0826 S23: -0.2988
REMARK 3 S31: -0.0576 S32: 0.3947 S33: -0.2223
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 : F 57 F 87
REMARK 3 ORIGIN FOR THE GROUP (A): 19.2764 -7.1205 -10.7821
REMARK 3 T TENSOR
REMARK 3 T11: 0.1598 T22: 0.1345
REMARK 3 T33: 0.1029 T12: -0.0230
REMARK 3 T13: 0.0940 T23: -0.0362
REMARK 3 L TENSOR
REMARK 3 L11: 5.2116 L22: 0.3628
REMARK 3 L33: 5.5286 L12: 1.1839
REMARK 3 L13: 3.1943 L23: 0.1887
REMARK 3 S TENSOR
REMARK 3 S11: 0.0122 S12: 0.2855 S13: -0.4411
REMARK 3 S21: -0.0195 S22: 0.0521 S23: -0.1419
REMARK 3 S31: 0.0819 S32: 0.0061 S33: -0.0643
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 : F 88 F 136
REMARK 3 ORIGIN FOR THE GROUP (A): 15.5585 -5.9800 0.2351
REMARK 3 T TENSOR
REMARK 3 T11: 0.1457 T22: 0.1094
REMARK 3 T33: 0.2213 T12: -0.0141
REMARK 3 T13: 0.0021 T23: -0.0025
REMARK 3 L TENSOR
REMARK 3 L11: 1.3759 L22: 0.3716
REMARK 3 L33: 3.0095 L12: 0.6344
REMARK 3 L13: 1.4620 L23: 1.0105
REMARK 3 S TENSOR
REMARK 3 S11: -0.0561 S12: -0.0110 S13: -0.2361
REMARK 3 S21: 0.0058 S22: 0.0003 S23: -0.0484
REMARK 3 S31: 0.0387 S32: 0.0301 S33: 0.0558
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 : F 137 F 222
REMARK 3 ORIGIN FOR THE GROUP (A): 21.9563 2.9766 1.7082
REMARK 3 T TENSOR
REMARK 3 T11: 0.0834 T22: 0.1365
REMARK 3 T33: 0.1777 T12: -0.0702
REMARK 3 T13: 0.0339 T23: -0.0009
REMARK 3 L TENSOR
REMARK 3 L11: 0.9570 L22: 1.5979
REMARK 3 L33: 2.6881 L12: 0.0766
REMARK 3 L13: 0.0312 L23: 0.3638
REMARK 3 S TENSOR
REMARK 3 S11: 0.1022 S12: -0.1662 S13: 0.1208
REMARK 3 S21: -0.0078 S22: -0.0224 S23: -0.0603
REMARK 3 S31: -0.3561 S32: 0.2592 S33: -0.0799
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 : F 223 F 318
REMARK 3 ORIGIN FOR THE GROUP (A): 16.4251 10.5042 6.2823
REMARK 3 T TENSOR
REMARK 3 T11: 0.2302 T22: 0.1269
REMARK 3 T33: 0.1898 T12: -0.0571
REMARK 3 T13: 0.0258 T23: -0.0421
REMARK 3 L TENSOR
REMARK 3 L11: 1.2922 L22: 0.8631
REMARK 3 L33: 1.0507 L12: -0.5419
REMARK 3 L13: 0.5316 L23: -0.5211
REMARK 3 S TENSOR
REMARK 3 S11: 0.0215 S12: -0.1321 S13: 0.1153
REMARK 3 S21: 0.0111 S22: 0.0021 S23: -0.1223
REMARK 3 S31: -0.3328 S32: 0.1273 S33: -0.0236
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.
REMARK 4
REMARK 4 2XLC 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-44125.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-JUL-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : BM16
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9070
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
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 : 46958
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.70
REMARK 200 RESOLUTION RANGE LOW (A) : 20.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 4
REMARK 200 R MERGE (I) : 0.10
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 7.10
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.85
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6
REMARK 200 DATA REDUNDANCY IN SHELL : 3.8
REMARK 200 R MERGE FOR SHELL (I) : 0.42
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.80
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 (%): 45
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.25
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M NH4 ACETATE, 0.1 M
REMARK 280 BIS-TRIS PH 5.5, 45% 2-METHYL-2,4-PENTANEDIOL (MPD)
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 58.02600
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 17170 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 60260 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -4.2 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 MSE A 1
REMARK 465 GLN A 2
REMARK 465 LEU A 3
REMARK 465 PHE A 4
REMARK 465 ASP A 5
REMARK 465 LEU A 6
REMARK 465 LEU A 318
REMARK 465 SER A 319
REMARK 465 THR A 320
REMARK 465 MSE B 1
REMARK 465 GLN B 2
REMARK 465 LEU B 3
REMARK 465 PHE B 4
REMARK 465 ASP B 5
REMARK 465 LEU B 6
REMARK 465 LEU B 318
REMARK 465 SER B 319
REMARK 465 THR B 320
REMARK 465 MSE C 1
REMARK 465 GLN C 2
REMARK 465 LEU C 3
REMARK 465 PHE C 4
REMARK 465 ASP C 5
REMARK 465 LEU C 6
REMARK 465 LEU C 318
REMARK 465 SER C 319
REMARK 465 THR C 320
REMARK 465 MSE D 1
REMARK 465 GLN D 2
REMARK 465 LEU D 3
REMARK 465 PHE D 4
REMARK 465 ASP D 5
REMARK 465 LEU D 6
REMARK 465 LEU D 318
REMARK 465 SER D 319
REMARK 465 THR D 320
REMARK 465 MSE E 1
REMARK 465 GLN E 2
REMARK 465 LEU E 3
REMARK 465 PHE E 4
REMARK 465 ASP E 5
REMARK 465 LEU E 6
REMARK 465 SER E 319
REMARK 465 THR E 320
REMARK 465 MSE F 1
REMARK 465 GLN F 2
REMARK 465 LEU F 3
REMARK 465 PHE F 4
REMARK 465 ASP F 5
REMARK 465 LEU F 6
REMARK 465 SER F 319
REMARK 465 THR F 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 GLU A 10 CG CD OE1 OE2
REMARK 470 LYS A 12 CG CD CE NZ
REMARK 470 LYS A 13 CG CD CE NZ
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 ARG A 36 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 39 CG CD OE1 OE2
REMARK 470 ASP A 48 CG OD1 OD2
REMARK 470 LYS A 52 CG CD CE NZ
REMARK 470 LYS A 55 CG CD CE NZ
REMARK 470 LYS A 198 CG CD CE NZ
REMARK 470 GLU A 236 CG CD OE1 OE2
REMARK 470 GLU A 239 CG CD OE1 OE2
REMARK 470 LYS A 240 CG CD CE NZ
REMARK 470 GLU B 9 CG CD OE1 OE2
REMARK 470 GLU B 10 CG CD OE1 OE2
REMARK 470 LYS B 12 CG CD CE NZ
REMARK 470 LYS B 13 CG CD CE NZ
REMARK 470 LYS B 17 CG CD CE NZ
REMARK 470 LYS B 30 CG CD CE NZ
REMARK 470 GLU B 33 CG CD OE1 OE2
REMARK 470 ARG B 36 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 39 CG CD OE1 OE2
REMARK 470 GLU B 41 CG CD OE1 OE2
REMARK 470 LYS B 52 CG CD CE NZ
REMARK 470 LYS B 55 CG CD CE NZ
REMARK 470 LYS B 68 CG CD CE NZ
REMARK 470 GLN B 78 CG CD OE1 NE2
REMARK 470 LYS B 198 CG CD CE NZ
REMARK 470 GLU B 236 CG CD OE1 OE2
REMARK 470 LYS B 240 CG CD CE NZ
REMARK 470 GLU B 285 CG CD OE1 OE2
REMARK 470 LYS B 314 CG CD CE NZ
REMARK 470 GLU C 9 CG CD OE1 OE2
REMARK 470 GLU C 10 CG CD OE1 OE2
REMARK 470 LYS C 12 CG CD CE NZ
REMARK 470 LYS C 13 CG CD CE NZ
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 GLU C 33 CG CD OE1 OE2
REMARK 470 ARG C 36 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 39 CG CD OE1 OE2
REMARK 470 LYS C 52 CG CD CE NZ
REMARK 470 LYS C 68 CG CD CE NZ
REMARK 470 GLN C 78 CG CD OE1 NE2
REMARK 470 HIS C 173 CG ND1 CD2 CE1 NE2
REMARK 470 LYS C 198 CG CD CE NZ
REMARK 470 LYS C 240 CG CD CE NZ
REMARK 470 GLU C 285 CG CD OE1 OE2
REMARK 470 GLN C 305 CG CD OE1 NE2
REMARK 470 LYS C 314 CG CD CE NZ
REMARK 470 GLU D 9 CG CD OE1 OE2
REMARK 470 GLU D 10 CG CD OE1 OE2
REMARK 470 LYS D 12 CG CD CE NZ
REMARK 470 LYS D 13 CG CD CE NZ
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 GLU D 33 CG CD OE1 OE2
REMARK 470 ARG D 36 CG CD NE CZ NH1 NH2
REMARK 470 GLU D 39 CG CD OE1 OE2
REMARK 470 ASP D 48 CG OD1 OD2
REMARK 470 LYS D 52 CG CD CE NZ
REMARK 470 LYS D 55 CG CD CE NZ
REMARK 470 LYS D 68 CG CD CE NZ
REMARK 470 GLN D 78 CG CD OE1 NE2
REMARK 470 VAL D 86 CG1 CG2
REMARK 470 LYS D 198 CG CD CE NZ
REMARK 470 GLU D 236 CG CD OE1 OE2
REMARK 470 LYS D 240 CG CD CE NZ
REMARK 470 LYS D 258 CG CD CE NZ
REMARK 470 LYS D 314 CG CD CE NZ
REMARK 470 GLU E 9 CG CD OE1 OE2
REMARK 470 GLU E 10 CG CD OE1 OE2
REMARK 470 LYS E 12 CG CD CE NZ
REMARK 470 LYS E 13 CG CD CE NZ
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 ARG E 36 CG CD NE CZ NH1 NH2
REMARK 470 GLU E 39 CG CD OE1 OE2
REMARK 470 LYS E 52 CG CD CE NZ
REMARK 470 LYS E 55 CG CD CE NZ
REMARK 470 LYS E 198 CG CD CE NZ
REMARK 470 GLU E 236 CG CD OE1 OE2
REMARK 470 LYS E 240 CG CD CE NZ
REMARK 470 LYS E 314 CG CD CE NZ
REMARK 470 GLU F 9 CG CD OE1 OE2
REMARK 470 GLU F 10 CG CD OE1 OE2
REMARK 470 LYS F 13 CG CD CE NZ
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 GLU F 33 CG CD OE1 OE2
REMARK 470 ARG F 36 CG CD NE CZ NH1 NH2
REMARK 470 GLU F 39 CG CD OE1 OE2
REMARK 470 LYS F 52 CG CD CE NZ
REMARK 470 LYS F 55 CG CD CE NZ
REMARK 470 LYS F 198 CG CD CE NZ
REMARK 470 GLU F 236 CG CD OE1 OE2
REMARK 470 LYS F 240 CG CD CE NZ
REMARK 470 LYS F 258 CG CD CE NZ
REMARK 470 LYS F 314 CG CD CE NZ
REMARK 470 LEU F 318 CG CD1 CD2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 CB SER A 181 P DEP A 1318 2.16
REMARK 500 CB SER D 181 P DEP D 1318 2.17
REMARK 500 N LYS F 68 OE1 GLU F 124 2.18
REMARK 500 OG SER F 181 O1 DEP F 1319 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 PRO A 50 68.51 -63.79
REMARK 500 PHE A 64 129.59 -34.14
REMARK 500 GLN A 120 -72.67 -94.90
REMARK 500 SER A 181 -113.78 50.46
REMARK 500 TYR A 204 79.56 21.93
REMARK 500 PRO B 16 164.13 -43.88
REMARK 500 SER B 181 -114.24 50.66
REMARK 500 TYR B 204 85.95 20.17
REMARK 500 PHE C 64 135.09 -37.21
REMARK 500 GLN C 120 -64.05 -92.93
REMARK 500 SER C 181 -114.02 51.15
REMARK 500 TYR C 204 79.29 19.11
REMARK 500 PHE D 64 141.95 -21.57
REMARK 500 HIS D 66 39.54 75.28
REMARK 500 SER D 181 -113.86 50.37
REMARK 500 TYR D 204 81.46 23.64
REMARK 500 PHE E 64 137.69 -29.44
REMARK 500 SER E 181 -113.99 50.55
REMARK 500 TYR E 204 81.38 17.49
REMARK 500 HIS F 66 34.20 70.15
REMARK 500 GLN F 120 -79.59 -92.14
REMARK 500 SER F 181 -113.64 50.49
REMARK 500 TYR F 204 66.78 20.80
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600 DIETHYL PHOSPHATE (DEP): COVALENTLY LINKED TO RESIDUE
REMARK 600 SER181
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DEP A1318
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DEP B1318
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DEP C1318
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DEP D1318
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DEP E1319
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DEP F1319
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 2XLC)
DBREF 2XLC A 1 320 UNP Q9K5F2 Q9K5F2_BACPU 1 320
DBREF 2XLC B 1 320 UNP Q9K5F2 Q9K5F2_BACPU 1 320
DBREF 2XLC C 1 320 UNP Q9K5F2 Q9K5F2_BACPU 1 320
DBREF 2XLC D 1 320 UNP Q9K5F2 Q9K5F2_BACPU 1 320
DBREF 2XLC E 1 320 UNP Q9K5F2 Q9K5F2_BACPU 1 320
DBREF 2XLC F 1 320 UNP Q9K5F2 Q9K5F2_BACPU 1 320
SEQADV 2XLC ASP A 97 UNP Q9K5F2 GLY 97 SEE REMARK 999
SEQADV 2XLC GLU A 236 UNP Q9K5F2 LYS 236 SEE REMARK 999
SEQADV 2XLC GLN A 270 UNP Q9K5F2 LYS 270 SEE REMARK 999
SEQADV 2XLC GLU A 289 UNP Q9K5F2 ASP 289 SEE REMARK 999
SEQADV 2XLC ASP B 97 UNP Q9K5F2 GLY 97 SEE REMARK 999
SEQADV 2XLC GLU B 236 UNP Q9K5F2 LYS 236 SEE REMARK 999
SEQADV 2XLC GLN B 270 UNP Q9K5F2 LYS 270 SEE REMARK 999
SEQADV 2XLC GLU B 289 UNP Q9K5F2 ASP 289 SEE REMARK 999
SEQADV 2XLC ASP C 97 UNP Q9K5F2 GLY 97 SEE REMARK 999
SEQADV 2XLC GLU C 236 UNP Q9K5F2 LYS 236 SEE REMARK 999
SEQADV 2XLC GLN C 270 UNP Q9K5F2 LYS 270 SEE REMARK 999
SEQADV 2XLC GLU C 289 UNP Q9K5F2 ASP 289 SEE REMARK 999
SEQADV 2XLC ASP D 97 UNP Q9K5F2 GLY 97 SEE REMARK 999
SEQADV 2XLC GLU D 236 UNP Q9K5F2 LYS 236 SEE REMARK 999
SEQADV 2XLC GLN D 270 UNP Q9K5F2 LYS 270 SEE REMARK 999
SEQADV 2XLC GLU D 289 UNP Q9K5F2 ASP 289 SEE REMARK 999
SEQADV 2XLC ASP E 97 UNP Q9K5F2 GLY 97 SEE REMARK 999
SEQADV 2XLC GLU E 236 UNP Q9K5F2 LYS 236 SEE REMARK 999
SEQADV 2XLC GLN E 270 UNP Q9K5F2 LYS 270 SEE REMARK 999
SEQADV 2XLC GLU E 289 UNP Q9K5F2 ASP 289 SEE REMARK 999
SEQADV 2XLC ASP F 97 UNP Q9K5F2 GLY 97 SEE REMARK 999
SEQADV 2XLC GLU F 236 UNP Q9K5F2 LYS 236 SEE REMARK 999
SEQADV 2XLC GLN F 270 UNP Q9K5F2 LYS 270 SEE REMARK 999
SEQADV 2XLC GLU F 289 UNP Q9K5F2 ASP 289 SEE REMARK 999
SEQRES 1 A 320 MSE 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 MSE 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 MSE 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 MSE 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 MSE 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 MSE 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 MSE 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 MSE 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 MSE 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 MSE 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 MSE 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 MSE 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 MSE 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 MSE 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 MSE 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 MSE 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 MSE 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 MSE 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 MSE 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 MSE 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 MSE 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 MSE 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 MSE 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 MSE 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
MODRES 2XLC MSE A 115 MET SELENOMETHIONINE
MODRES 2XLC MSE A 138 MET SELENOMETHIONINE
MODRES 2XLC MSE A 263 MET SELENOMETHIONINE
MODRES 2XLC MSE B 115 MET SELENOMETHIONINE
MODRES 2XLC MSE B 138 MET SELENOMETHIONINE
MODRES 2XLC MSE B 263 MET SELENOMETHIONINE
MODRES 2XLC MSE C 115 MET SELENOMETHIONINE
MODRES 2XLC MSE C 138 MET SELENOMETHIONINE
MODRES 2XLC MSE C 263 MET SELENOMETHIONINE
MODRES 2XLC MSE D 115 MET SELENOMETHIONINE
MODRES 2XLC MSE D 138 MET SELENOMETHIONINE
MODRES 2XLC MSE D 263 MET SELENOMETHIONINE
MODRES 2XLC MSE E 115 MET SELENOMETHIONINE
MODRES 2XLC MSE E 138 MET SELENOMETHIONINE
MODRES 2XLC MSE E 263 MET SELENOMETHIONINE
MODRES 2XLC MSE F 115 MET SELENOMETHIONINE
MODRES 2XLC MSE F 138 MET SELENOMETHIONINE
MODRES 2XLC MSE F 263 MET SELENOMETHIONINE
HET MSE A 115 8
HET MSE A 138 8
HET MSE A 263 8
HET MSE B 115 8
HET MSE B 138 8
HET MSE B 263 8
HET MSE C 115 8
HET MSE C 138 8
HET MSE C 263 8
HET MSE D 115 8
HET MSE D 138 8
HET MSE D 263 8
HET MSE E 115 8
HET MSE E 138 8
HET MSE E 263 8
HET MSE F 115 8
HET MSE F 138 8
HET MSE F 263 8
HET DEP A1318 8
HET DEP B1318 8
HET DEP C1318 8
HET DEP D1318 8
HET DEP E1319 8
HET DEP F1319 8
HETNAM MSE SELENOMETHIONINE
HETNAM DEP DIETHYL PHOSPHONATE
FORMUL 6 MSE 18(C5 H11 N O2 SE)
FORMUL 7 DEP 6(C4 H11 O3 P)
FORMUL 8 HOH *40(H2 O)
HELIX 1 1 SER A 7 LYS A 13 1 7
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 GLN A 165 1 18
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 SER A 246 1 13
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 HIS A 283 1 11
HELIX 14 14 ILE A 301 LEU A 317 1 17
HELIX 15 15 LEU B 8 LYS B 13 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 SER B 166 1 19
HELIX 21 21 GLN B 182 SER B 194 1 13
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 SER B 246 1 13
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 13 1 7
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 LEU C 107 1 10
HELIX 34 34 TYR C 148 SER C 166 1 19
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 ASN C 282 1 10
HELIX 42 42 ILE C 301 LEU C 317 1 17
HELIX 43 43 SER D 7 LYS D 13 1 7
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 SER D 166 1 19
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 SER D 246 1 13
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 HIS D 283 1 11
HELIX 56 56 ILE D 301 LEU D 317 1 17
HELIX 57 57 SER E 7 LYS E 13 1 7
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 SER E 166 1 19
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 SER E 246 1 13
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 HIS E 283 1 11
HELIX 70 70 ILE E 301 LEU E 317 1 17
HELIX 71 71 SER F 7 LYS F 13 1 7
HELIX 72 72 ASP F 23 GLN F 37 1 15
HELIX 73 73 TYR F 95 ASP F 97 5 3
HELIX 74 74 GLY F 98 HIS F 108 1 11
HELIX 75 75 TYR F 148 SER F 166 1 19
HELIX 76 76 SER F 181 SER F 194 1 14
HELIX 77 77 ASN F 209 ALA F 217 1 9
HELIX 78 78 TYR F 222 ASN F 232 1 11
HELIX 79 79 ASP F 234 SER F 246 1 13
HELIX 80 80 ASP F 249 ALA F 254 1 6
HELIX 81 81 GLY F 255 VAL F 257 5 3
HELIX 82 82 PRO F 273 HIS F 283 1 11
HELIX 83 83 ILE F 301 LEU F 317 1 17
SHEET 1 AA 9 THR A 43 TYR A 47 0
SHEET 2 AA 9 VAL A 54 SER A 63 -1 O VAL A 56 N TYR A 47
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 MSE 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 MSE A 263
SHEET 1 BA 9 THR B 43 TYR B 47 0
SHEET 2 BA 9 VAL B 54 GLN B 62 -1 O VAL B 56 N TYR B 47
SHEET 3 BA 9 LYS B 68 PRO B 76 -1 O ILE B 69 N TYR B 61
SHEET 4 BA 9 ALA B 111 MSE 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 SER B 181 1 N ASP B 171 O HIS B 82
SHEET 7 BA 9 VAL B 199 PRO B 205 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 MSE B 263
SHEET 1 CA 9 THR C 43 SER C 46 0
SHEET 2 CA 9 VAL C 54 SER C 63 -1 O ARG C 58 N GLU C 45
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 MSE 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 MSE C 263
SHEET 1 DA 9 THR D 43 SER D 46 0
SHEET 2 DA 9 VAL D 54 SER D 63 -1 O ARG D 58 N GLU D 45
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 MSE 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 MSE D 263
SHEET 1 EA 9 THR E 43 TYR E 47 0
SHEET 2 EA 9 VAL E 54 SER E 63 -1 O VAL E 56 N TYR E 47
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 MSE 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 MSE E 263
SHEET 1 FA 9 THR F 43 TYR F 47 0
SHEET 2 FA 9 VAL F 54 SER F 63 -1 O VAL F 56 N TYR F 47
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 MSE 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 MSE F 263
LINK C GLY A 114 N MSE A 115 1555 1555 1.33
LINK C MSE A 115 N LEU A 116 1555 1555 1.32
LINK C TRP A 137 N MSE A 138 1555 1555 1.33
LINK C MSE A 138 N THR A 139 1555 1555 1.33
LINK OG SER A 181 P DEP A1318 1555 1555 1.55
LINK C LEU A 262 N MSE A 263 1555 1555 1.33
LINK C MSE A 263 N ALA A 264 1555 1555 1.33
LINK C GLY B 114 N MSE B 115 1555 1555 1.33
LINK C MSE B 115 N LEU B 116 1555 1555 1.33
LINK C TRP B 137 N MSE B 138 1555 1555 1.33
LINK C MSE B 138 N THR B 139 1555 1555 1.33
LINK OG SER B 181 P DEP B1318 1555 1555 1.71
LINK C LEU B 262 N MSE B 263 1555 1555 1.33
LINK C MSE B 263 N ALA B 264 1555 1555 1.33
LINK C GLY C 114 N MSE C 115 1555 1555 1.33
LINK C MSE C 115 N LEU C 116 1555 1555 1.33
LINK C TRP C 137 N MSE C 138 1555 1555 1.33
LINK C MSE C 138 N THR C 139 1555 1555 1.33
LINK OG SER C 181 P DEP C1318 1555 1555 1.59
LINK C LEU C 262 N MSE C 263 1555 1555 1.33
LINK C MSE C 263 N ALA C 264 1555 1555 1.33
LINK C GLY D 114 N MSE D 115 1555 1555 1.33
LINK C MSE D 115 N LEU D 116 1555 1555 1.33
LINK C TRP D 137 N MSE D 138 1555 1555 1.33
LINK C MSE D 138 N THR D 139 1555 1555 1.33
LINK OG SER D 181 P DEP D1318 1555 1555 1.72
LINK C LEU D 262 N MSE D 263 1555 1555 1.33
LINK C MSE D 263 N ALA D 264 1555 1555 1.33
LINK C GLY E 114 N MSE E 115 1555 1555 1.33
LINK C MSE E 115 N LEU E 116 1555 1555 1.33
LINK C TRP E 137 N MSE E 138 1555 1555 1.33
LINK C MSE E 138 N THR E 139 1555 1555 1.33
LINK OG SER E 181 P DEP E1319 1555 1555 1.82
LINK C LEU E 262 N MSE E 263 1555 1555 1.33
LINK C MSE E 263 N ALA E 264 1555 1555 1.33
LINK C GLY F 114 N MSE F 115 1555 1555 1.33
LINK C MSE F 115 N LEU F 116 1555 1555 1.33
LINK C TRP F 137 N MSE F 138 1555 1555 1.33
LINK C MSE F 138 N THR F 139 1555 1555 1.33
LINK OG SER F 181 P DEP F1319 1555 1555 1.53
LINK C LEU F 262 N MSE F 263 1555 1555 1.33
LINK C MSE F 263 N ALA F 264 1555 1555 1.33
CISPEP 1 GLY A 80 PRO A 81 0 -4.14
CISPEP 2 GLN A 220 PRO A 221 0 0.52
CISPEP 3 GLY B 80 PRO B 81 0 -1.76
CISPEP 4 GLN B 220 PRO B 221 0 2.02
CISPEP 5 GLY C 80 PRO C 81 0 -1.82
CISPEP 6 GLN C 220 PRO C 221 0 1.61
CISPEP 7 GLY D 80 PRO D 81 0 -0.18
CISPEP 8 GLN D 220 PRO D 221 0 1.14
CISPEP 9 GLY E 80 PRO E 81 0 -2.26
CISPEP 10 GLN E 220 PRO E 221 0 0.94
CISPEP 11 GLY F 80 PRO F 81 0 -2.14
CISPEP 12 GLN F 220 PRO F 221 0 1.93
SITE 1 AC1 7 GLY A 90 TYR A 91 SER A 181 GLN A 182
SITE 2 AC1 7 TYR A 206 PRO A 221 HIS A 298
SITE 1 AC2 8 GLY B 90 TYR B 91 SER B 181 GLN B 182
SITE 2 AC2 8 TYR B 206 PRO B 221 VAL B 271 HIS B 298
SITE 1 AC3 7 GLY C 90 TYR C 91 SER C 181 GLN C 182
SITE 2 AC3 7 TYR C 206 PRO C 221 HIS C 298
SITE 1 AC4 7 GLY D 90 TYR D 91 SER D 181 GLN D 182
SITE 2 AC4 7 TYR D 206 VAL D 271 HIS D 298
SITE 1 AC5 6 GLY E 90 TYR E 91 SER E 181 GLN E 182
SITE 2 AC5 6 TYR E 206 HIS E 298
SITE 1 AC6 8 GLY F 90 TYR F 91 SER F 181 GLN F 182
SITE 2 AC6 8 TYR F 206 PRO F 221 VAL F 271 HIS F 298
CRYST1 82.049 116.052 100.248 90.00 105.60 90.00 P 1 21 1 12
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 0.012188 0.000000 0.003403 0.00000
SCALE2 0.000000 0.008617 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010357 0.00000
MTRIX1 1 0.357500 -0.669200 -0.651500 13.82000 1
MTRIX2 1 -0.664400 -0.672500 0.326100 -10.17000 1
MTRIX3 1 -0.656300 0.316200 -0.685000 39.55000 1
MTRIX1 2 -0.973900 0.012260 -0.226700 0.55860 1
MTRIX2 2 -0.027900 -0.997400 0.065910 -2.11400 1
MTRIX3 2 -0.225300 0.070510 0.971700 0.31720 1
MTRIX1 3 0.020550 -0.516100 0.856300 -23.20000 1
MTRIX2 3 -0.509200 -0.742500 -0.435300 9.63000 1
MTRIX3 3 0.860400 -0.427000 -0.278000 33.47000 1
MTRIX1 4 0.402600 -0.639000 -0.655400 14.33000 1
MTRIX2 4 -0.654000 -0.701800 0.282500 -8.13400 1
MTRIX3 4 -0.640400 0.314900 -0.700500 40.52000 1
MTRIX1 5 -0.971900 -0.009972 -0.235200 0.90260 1
MTRIX2 5 -0.008179 -0.997100 0.076080 -1.77400 1
MTRIX3 5 -0.235200 0.075870 0.969000 0.18000 1
TER 2427 LEU A 317
TER 4837 LEU B 317
TER 7246 LEU C 317
TER 9651 LEU D 317
TER 12085 LEU E 318
TER 14512 LEU F 318
MASTER 1060 0 24 83 54 0 12 2114594 6 234 150
END
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