| content |
HEADER HYDROLASE 08-APR-09 2WFM
TITLE CRYSTAL STRUCTURE OF POLYNEURIDINE ALDEHYDE ESTERASE
TITLE 2 MUTANT (H244A)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POLYNEURIDINE ALDEHYDE ESTERASE;
COMPND 3 CHAIN: A, B, C, D, E;
COMPND 4 EC: 3.1.1.78;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RAUVOLFIA SERPENTINA;
SOURCE 3 ORGANISM_COMMON: SERPENTWOOD;
SOURCE 4 ORGANISM_TAXID: 4060;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: M15PREP4;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PQE-2
KEYWDS ALKALOID METABOLISM, MONOTERPENOID INDOLE ALKALOIDS, PNAE,
KEYWDS 2 HYDROLASE, SERINE ESTERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR L.YANG,M.HILL,S.PANJIKAR,M.WANG,J.STOECKIGT
REVDAT 1 21-APR-10 2WFM 0
JRNL AUTH L.YANG,M.HILL,M.WANG,S.PANJIKAR,J.STOCKIGT
JRNL TITL STRUCTURAL BASIS AND ENZYMATIC MECHANISM OF THE
JRNL TITL 2 BIOSYNTHESIS OF C9- FROM C10-MONOTERPENOID INDOLE
JRNL TITL 3 ALKALOIDS.
JRNL REF ANGEW.CHEM.INT.ED.ENGL. V. 48 5211 2009
JRNL REFN ISSN 1433-7851
JRNL PMID 19496101
JRNL DOI 10.1002/ANIE.200900150
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.4.0069
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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.94
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.83
REMARK 3 NUMBER OF REFLECTIONS : 69184
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) : 0.19827
REMARK 3 R VALUE (WORKING SET) : 0.19795
REMARK 3 FREE R VALUE : 0.23579
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 0.9
REMARK 3 FREE R VALUE TEST SET COUNT : 613
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) : 2.200
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.256
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5116
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.70
REMARK 3 BIN R VALUE (WORKING SET) : 0.265
REMARK 3 BIN FREE R VALUE SET COUNT : 48
REMARK 3 BIN FREE R VALUE : 0.337
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 10033
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 188
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 45
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.009
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.08
REMARK 3 B22 (A**2) : -0.16
REMARK 3 B33 (A**2) : 0.09
REMARK 3 B12 (A**2) : 0.00
REMARK 3 B13 (A**2) : 0.01
REMARK 3 B23 (A**2) : 0.00
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.265
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.202
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.165
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.437
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.954
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.934
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 10284 ; 0.017 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 13867 ; 1.701 ; 1.975
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1272 ; 6.420 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 435 ;33.303 ;24.713
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1856 ;16.861 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 35 ;16.854 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1476 ; 0.112 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7714 ; 0.009 ; 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): 6373 ; 0.731 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 10261 ; 1.386 ; 2.500
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3911 ; 4.024 ; 5.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3605 ; 6.196 ;10.000
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
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 4
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 10 A 75 2
REMARK 3 1 B 10 B 75 2
REMARK 3 1 C 10 C 75 2
REMARK 3 1 D 10 D 75 2
REMARK 3 2 A 90 A 122 2
REMARK 3 2 B 90 B 122 2
REMARK 3 2 C 90 C 122 2
REMARK 3 2 D 90 D 122 2
REMARK 3 3 A 151 A 230 2
REMARK 3 3 B 151 B 230 2
REMARK 3 3 C 151 C 230 2
REMARK 3 3 D 151 D 230 2
REMARK 3 4 A 237 A 261 2
REMARK 3 4 B 237 B 261 2
REMARK 3 4 C 237 C 261 2
REMARK 3 4 D 237 D 261 2
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 815 ; 0.07 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 B (A): 815 ; 0.07 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 C (A): 815 ; 0.07 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 D (A): 815 ; 0.07 ; 0.05
REMARK 3 MEDIUM POSITIONAL 1 A (A): 789 ; 0.11 ; 0.50
REMARK 3 MEDIUM POSITIONAL 1 B (A): 789 ; 0.14 ; 0.50
REMARK 3 MEDIUM POSITIONAL 1 C (A): 789 ; 0.11 ; 0.50
REMARK 3 MEDIUM POSITIONAL 1 D (A): 789 ; 0.13 ; 0.50
REMARK 3 TIGHT THERMAL 1 A (A**2): 815 ; 0.70 ; 1.50
REMARK 3 TIGHT THERMAL 1 B (A**2): 815 ; 0.73 ; 1.50
REMARK 3 TIGHT THERMAL 1 C (A**2): 815 ; 0.73 ; 1.50
REMARK 3 TIGHT THERMAL 1 D (A**2): 815 ; 0.69 ; 1.50
REMARK 3 MEDIUM THERMAL 1 A (A**2): 789 ; 1.04 ; 2.50
REMARK 3 MEDIUM THERMAL 1 B (A**2): 789 ; 1.10 ; 2.50
REMARK 3 MEDIUM THERMAL 1 C (A**2): 789 ; 1.10 ; 2.50
REMARK 3 MEDIUM THERMAL 1 D (A**2): 789 ; 1.02 ; 2.50
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 45
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 9 A 52
REMARK 3 ORIGIN FOR THE GROUP (A): -39.7125 27.8308 41.2191
REMARK 3 T TENSOR
REMARK 3 T11: 0.1006 T22: 0.1377
REMARK 3 T33: 0.1142 T12: -0.0260
REMARK 3 T13: -0.0020 T23: 0.0096
REMARK 3 L TENSOR
REMARK 3 L11: 2.4047 L22: 2.8967
REMARK 3 L33: 1.2248 L12: 0.2748
REMARK 3 L13: -1.2169 L23: -0.8665
REMARK 3 S TENSOR
REMARK 3 S11: 0.0686 S12: 0.4342 S13: 0.1419
REMARK 3 S21: -0.2607 S22: 0.0401 S23: 0.2292
REMARK 3 S31: -0.1008 S32: -0.0881 S33: -0.1087
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 53 A 58
REMARK 3 ORIGIN FOR THE GROUP (A): -42.0365 9.3093 52.7494
REMARK 3 T TENSOR
REMARK 3 T11: 0.1836 T22: 0.1865
REMARK 3 T33: 0.1891 T12: -0.0261
REMARK 3 T13: 0.0092 T23: 0.0010
REMARK 3 L TENSOR
REMARK 3 L11: 20.3545 L22: 21.8777
REMARK 3 L33: 0.7006 L12: -5.0968
REMARK 3 L13: 0.1073 L23: -3.8245
REMARK 3 S TENSOR
REMARK 3 S11: 0.0511 S12: -0.1979 S13: -0.6274
REMARK 3 S21: 0.0379 S22: 0.0496 S23: 0.6991
REMARK 3 S31: 0.6273 S32: -0.7142 S33: -0.1008
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 59 A 78
REMARK 3 ORIGIN FOR THE GROUP (A): -38.3125 13.8274 37.4359
REMARK 3 T TENSOR
REMARK 3 T11: 0.1454 T22: 0.1695
REMARK 3 T33: 0.1928 T12: -0.0262
REMARK 3 T13: 0.0187 T23: -0.0384
REMARK 3 L TENSOR
REMARK 3 L11: 3.0939 L22: 2.8316
REMARK 3 L33: 8.6206 L12: -1.2080
REMARK 3 L13: 2.8384 L23: -2.8094
REMARK 3 S TENSOR
REMARK 3 S11: 0.1141 S12: 0.2675 S13: -0.0528
REMARK 3 S21: -0.4680 S22: -0.0262 S23: 0.2013
REMARK 3 S31: 0.4665 S32: -0.0747 S33: -0.0879
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 79 A 115
REMARK 3 ORIGIN FOR THE GROUP (A): -29.9045 20.5125 36.0638
REMARK 3 T TENSOR
REMARK 3 T11: 0.0493 T22: 0.1560
REMARK 3 T33: 0.0948 T12: -0.0102
REMARK 3 T13: 0.0322 T23: 0.0311
REMARK 3 L TENSOR
REMARK 3 L11: 2.2048 L22: 6.0440
REMARK 3 L33: 5.6208 L12: -0.5074
REMARK 3 L13: -0.2682 L23: 0.6113
REMARK 3 S TENSOR
REMARK 3 S11: 0.0159 S12: 0.4216 S13: -0.0225
REMARK 3 S21: -0.1157 S22: -0.0719 S23: 0.0238
REMARK 3 S31: 0.0139 S32: -0.1759 S33: 0.0560
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 116 A 145
REMARK 3 ORIGIN FOR THE GROUP (A): -21.2604 15.7036 53.0368
REMARK 3 T TENSOR
REMARK 3 T11: 0.1332 T22: 0.1100
REMARK 3 T33: 0.1667 T12: -0.0205
REMARK 3 T13: -0.0132 T23: 0.0320
REMARK 3 L TENSOR
REMARK 3 L11: 1.7742 L22: 0.2237
REMARK 3 L33: 3.7348 L12: -0.1461
REMARK 3 L13: -1.9520 L23: 0.7403
REMARK 3 S TENSOR
REMARK 3 S11: 0.0320 S12: -0.1323 S13: 0.0438
REMARK 3 S21: -0.1450 S22: 0.0311 S23: -0.1552
REMARK 3 S31: -0.1818 S32: 0.3677 S33: -0.0631
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 146 A 176
REMARK 3 ORIGIN FOR THE GROUP (A): -31.9477 23.1897 58.6601
REMARK 3 T TENSOR
REMARK 3 T11: 0.0863 T22: 0.1103
REMARK 3 T33: 0.1097 T12: -0.0396
REMARK 3 T13: -0.0103 T23: -0.0098
REMARK 3 L TENSOR
REMARK 3 L11: 2.0920 L22: 8.3895
REMARK 3 L33: 1.2602 L12: 0.5434
REMARK 3 L13: -0.0511 L23: -1.8824
REMARK 3 S TENSOR
REMARK 3 S11: 0.0171 S12: 0.1134 S13: -0.0897
REMARK 3 S21: -0.1898 S22: -0.0653 S23: -0.0419
REMARK 3 S31: 0.1593 S32: -0.1329 S33: 0.0481
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 177 A 206
REMARK 3 ORIGIN FOR THE GROUP (A): -29.4928 14.0623 44.8974
REMARK 3 T TENSOR
REMARK 3 T11: 0.0271 T22: 0.0426
REMARK 3 T33: 0.1540 T12: -0.0904
REMARK 3 T13: -0.0196 T23: -0.0282
REMARK 3 L TENSOR
REMARK 3 L11: 2.5076 L22: 1.3950
REMARK 3 L33: 3.6370 L12: -0.7850
REMARK 3 L13: -0.7797 L23: -0.3356
REMARK 3 S TENSOR
REMARK 3 S11: -0.0886 S12: 0.1635 S13: -0.1832
REMARK 3 S21: 0.0269 S22: 0.0205 S23: -0.1050
REMARK 3 S31: 0.5290 S32: 0.2162 S33: 0.0681
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 207 A 248
REMARK 3 ORIGIN FOR THE GROUP (A): -20.9682 29.6933 43.9422
REMARK 3 T TENSOR
REMARK 3 T11: 0.1048 T22: 0.0777
REMARK 3 T33: 0.1894 T12: -0.0630
REMARK 3 T13: 0.0214 T23: 0.0544
REMARK 3 L TENSOR
REMARK 3 L11: 3.2956 L22: 2.5027
REMARK 3 L33: 3.5220 L12: -1.9542
REMARK 3 L13: -1.8153 L23: 2.4631
REMARK 3 S TENSOR
REMARK 3 S11: 0.0146 S12: 0.0972 S13: 0.2506
REMARK 3 S21: -0.0984 S22: 0.0681 S23: -0.2485
REMARK 3 S31: -0.3133 S32: 0.4057 S33: -0.0827
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 249 A 263
REMARK 3 ORIGIN FOR THE GROUP (A): -30.4946 37.4079 37.8250
REMARK 3 T TENSOR
REMARK 3 T11: 0.1908 T22: 0.1908
REMARK 3 T33: 0.2614 T12: 0.0001
REMARK 3 T13: -0.0006 T23: 0.0356
REMARK 3 L TENSOR
REMARK 3 L11: 2.0714 L22: 2.9686
REMARK 3 L33: 17.9498 L12: 0.3576
REMARK 3 L13: -3.0978 L23: 3.2581
REMARK 3 S TENSOR
REMARK 3 S11: 0.0544 S12: 0.2970 S13: 0.2096
REMARK 3 S21: -0.4014 S22: 0.0103 S23: -0.0361
REMARK 3 S31: -0.5495 S32: 0.1233 S33: -0.0647
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 9 B 49
REMARK 3 ORIGIN FOR THE GROUP (A): -10.5120 8.8719 88.9323
REMARK 3 T TENSOR
REMARK 3 T11: 0.0300 T22: 0.0594
REMARK 3 T33: 0.0798 T12: -0.0238
REMARK 3 T13: 0.0298 T23: -0.0257
REMARK 3 L TENSOR
REMARK 3 L11: 1.9707 L22: 4.3960
REMARK 3 L33: 3.0498 L12: -0.8845
REMARK 3 L13: -0.4106 L23: -0.5150
REMARK 3 S TENSOR
REMARK 3 S11: -0.0743 S12: -0.2921 S13: -0.0782
REMARK 3 S21: 0.3996 S22: 0.0676 S23: -0.1248
REMARK 3 S31: 0.0683 S32: 0.4153 S33: 0.0067
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 50 B 58
REMARK 3 ORIGIN FOR THE GROUP (A): -19.5839 27.0991 85.2419
REMARK 3 T TENSOR
REMARK 3 T11: 0.1812 T22: 0.1652
REMARK 3 T33: 0.2095 T12: 0.0138
REMARK 3 T13: 0.0065 T23: -0.0301
REMARK 3 L TENSOR
REMARK 3 L11: 1.1599 L22: 7.0789
REMARK 3 L33: 13.2127 L12: 0.4884
REMARK 3 L13: -0.8773 L23: -9.4471
REMARK 3 S TENSOR
REMARK 3 S11: -0.0418 S12: 0.0809 S13: 0.5519
REMARK 3 S21: 0.3010 S22: 0.0028 S23: 0.0596
REMARK 3 S31: -0.8889 S32: -0.2377 S33: 0.0390
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 59 B 79
REMARK 3 ORIGIN FOR THE GROUP (A): -4.3459 22.2166 87.0283
REMARK 3 T TENSOR
REMARK 3 T11: 0.1349 T22: 0.1078
REMARK 3 T33: 0.1743 T12: -0.0361
REMARK 3 T13: 0.0195 T23: -0.0410
REMARK 3 L TENSOR
REMARK 3 L11: 8.6845 L22: 1.7033
REMARK 3 L33: 6.0855 L12: -2.3430
REMARK 3 L13: 4.2998 L23: -1.1561
REMARK 3 S TENSOR
REMARK 3 S11: -0.1198 S12: -0.1986 S13: 0.2766
REMARK 3 S21: 0.2711 S22: 0.0092 S23: -0.3384
REMARK 3 S31: -0.2218 S32: 0.1355 S33: 0.1106
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 : B 80 B 124
REMARK 3 ORIGIN FOR THE GROUP (A): -1.6156 15.4726 77.3589
REMARK 3 T TENSOR
REMARK 3 T11: 0.0404 T22: 0.0692
REMARK 3 T33: 0.1101 T12: -0.0012
REMARK 3 T13: 0.0232 T23: -0.0339
REMARK 3 L TENSOR
REMARK 3 L11: 1.8714 L22: 3.0614
REMARK 3 L33: 3.3508 L12: 0.3179
REMARK 3 L13: 0.3810 L23: -0.8929
REMARK 3 S TENSOR
REMARK 3 S11: -0.0763 S12: 0.0967 S13: 0.1529
REMARK 3 S21: -0.0648 S22: 0.0760 S23: -0.1769
REMARK 3 S31: -0.0947 S32: 0.1924 S33: 0.0004
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 : B 125 B 134
REMARK 3 ORIGIN FOR THE GROUP (A): -12.7030 15.0594 61.0310
REMARK 3 T TENSOR
REMARK 3 T11: 0.1826 T22: 0.1731
REMARK 3 T33: 0.1566 T12: -0.0078
REMARK 3 T13: 0.0300 T23: 0.0178
REMARK 3 L TENSOR
REMARK 3 L11: 6.2257 L22: 8.2817
REMARK 3 L33: 7.7101 L12: 1.6327
REMARK 3 L13: 4.3312 L23: 1.9166
REMARK 3 S TENSOR
REMARK 3 S11: 0.1428 S12: 0.4525 S13: -0.0988
REMARK 3 S21: -0.2802 S22: -0.0700 S23: -0.3474
REMARK 3 S31: 0.2306 S32: 0.3424 S33: -0.0728
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 : B 135 B 176
REMARK 3 ORIGIN FOR THE GROUP (A): -23.9911 15.2030 72.5409
REMARK 3 T TENSOR
REMARK 3 T11: 0.0760 T22: 0.1245
REMARK 3 T33: 0.1263 T12: -0.0372
REMARK 3 T13: -0.0106 T23: -0.0055
REMARK 3 L TENSOR
REMARK 3 L11: 1.0793 L22: 4.1117
REMARK 3 L33: 2.7978 L12: -1.1287
REMARK 3 L13: 0.4288 L23: -0.6599
REMARK 3 S TENSOR
REMARK 3 S11: -0.0226 S12: 0.0415 S13: 0.2066
REMARK 3 S21: -0.1344 S22: -0.0519 S23: -0.1626
REMARK 3 S31: -0.2160 S32: 0.0877 S33: 0.0744
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 : B 177 B 206
REMARK 3 ORIGIN FOR THE GROUP (A): -8.4893 20.9755 75.8098
REMARK 3 T TENSOR
REMARK 3 T11: 0.0970 T22: 0.0233
REMARK 3 T33: 0.0657 T12: -0.0259
REMARK 3 T13: -0.0231 T23: -0.0693
REMARK 3 L TENSOR
REMARK 3 L11: 4.5165 L22: 1.3927
REMARK 3 L33: 2.4520 L12: -0.9019
REMARK 3 L13: -0.8550 L23: -0.7537
REMARK 3 S TENSOR
REMARK 3 S11: -0.0063 S12: 0.4336 S13: 0.7380
REMARK 3 S21: -0.1644 S22: 0.0455 S23: -0.1341
REMARK 3 S31: -0.2196 S32: 0.0302 S33: -0.0393
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 : B 207 B 250
REMARK 3 ORIGIN FOR THE GROUP (A): -7.5204 3.6450 71.5793
REMARK 3 T TENSOR
REMARK 3 T11: 0.1449 T22: -0.0073
REMARK 3 T33: 0.1122 T12: 0.0172
REMARK 3 T13: 0.0378 T23: -0.0438
REMARK 3 L TENSOR
REMARK 3 L11: 7.1999 L22: 1.1020
REMARK 3 L33: 2.5050 L12: 1.8469
REMARK 3 L13: -1.3620 L23: -1.3123
REMARK 3 S TENSOR
REMARK 3 S11: -0.0456 S12: 0.2666 S13: -0.3551
REMARK 3 S21: -0.2931 S22: 0.0525 S23: -0.1315
REMARK 3 S31: 0.4089 S32: 0.1485 S33: -0.0069
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 : B 251 B 263
REMARK 3 ORIGIN FOR THE GROUP (A): -4.7609 -1.7294 84.4072
REMARK 3 T TENSOR
REMARK 3 T11: 0.2369 T22: 0.1761
REMARK 3 T33: 0.1674 T12: 0.0196
REMARK 3 T13: 0.0135 T23: 0.0091
REMARK 3 L TENSOR
REMARK 3 L11: 19.8953 L22: 4.8454
REMARK 3 L33: 3.4237 L12: 1.8499
REMARK 3 L13: 0.0344 L23: 0.7592
REMARK 3 S TENSOR
REMARK 3 S11: 0.2144 S12: -0.2672 S13: -0.6564
REMARK 3 S21: 0.2175 S22: -0.0986 S23: -0.4769
REMARK 3 S31: 0.2254 S32: 0.3672 S33: -0.1158
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 9 C 52
REMARK 3 ORIGIN FOR THE GROUP (A): 0.5808 1.1852 18.4753
REMARK 3 T TENSOR
REMARK 3 T11: 0.2103 T22: 0.1074
REMARK 3 T33: 0.0735 T12: -0.0443
REMARK 3 T13: 0.0089 T23: -0.0110
REMARK 3 L TENSOR
REMARK 3 L11: 1.7131 L22: 2.0154
REMARK 3 L33: 1.2509 L12: 0.5833
REMARK 3 L13: -0.4023 L23: -0.1609
REMARK 3 S TENSOR
REMARK 3 S11: 0.0562 S12: 0.2328 S13: -0.0426
REMARK 3 S21: -0.2110 S22: -0.1186 S23: 0.0705
REMARK 3 S31: 0.0892 S32: -0.2811 S33: 0.0625
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 53 C 67
REMARK 3 ORIGIN FOR THE GROUP (A): 12.3553 15.6131 23.0817
REMARK 3 T TENSOR
REMARK 3 T11: 0.2569 T22: 0.1289
REMARK 3 T33: 0.1614 T12: -0.0418
REMARK 3 T13: -0.0197 T23: 0.0707
REMARK 3 L TENSOR
REMARK 3 L11: 4.5187 L22: 5.4542
REMARK 3 L33: 8.0041 L12: 1.6685
REMARK 3 L13: 0.6983 L23: 3.4326
REMARK 3 S TENSOR
REMARK 3 S11: 0.0043 S12: 0.5193 S13: 0.6227
REMARK 3 S21: -0.2224 S22: -0.0126 S23: -0.4476
REMARK 3 S31: -0.3028 S32: 0.3749 S33: 0.0083
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 : C 68 C 101
REMARK 3 ORIGIN FOR THE GROUP (A): -3.8322 12.7992 20.8592
REMARK 3 T TENSOR
REMARK 3 T11: 0.1868 T22: 0.0736
REMARK 3 T33: 0.1191 T12: -0.0387
REMARK 3 T13: -0.0103 T23: 0.0149
REMARK 3 L TENSOR
REMARK 3 L11: 4.0939 L22: 4.5882
REMARK 3 L33: 2.9192 L12: -0.8040
REMARK 3 L13: -0.2173 L23: -0.2221
REMARK 3 S TENSOR
REMARK 3 S11: -0.0507 S12: 0.4118 S13: 0.2451
REMARK 3 S21: -0.4190 S22: -0.0295 S23: 0.1211
REMARK 3 S31: -0.0882 S32: -0.2788 S33: 0.0802
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 : C 102 C 124
REMARK 3 ORIGIN FOR THE GROUP (A): -4.9062 13.0512 32.2556
REMARK 3 T TENSOR
REMARK 3 T11: 0.2056 T22: 0.1092
REMARK 3 T33: 0.1461 T12: -0.0147
REMARK 3 T13: -0.0112 T23: 0.0029
REMARK 3 L TENSOR
REMARK 3 L11: 2.1645 L22: 1.6961
REMARK 3 L33: 2.3607 L12: 0.3945
REMARK 3 L13: 0.3751 L23: 1.9994
REMARK 3 S TENSOR
REMARK 3 S11: -0.1112 S12: -0.0853 S13: 0.2103
REMARK 3 S21: 0.1760 S22: -0.0112 S23: 0.1589
REMARK 3 S31: -0.3395 S32: -0.0425 S33: 0.1224
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 : C 125 C 134
REMARK 3 ORIGIN FOR THE GROUP (A): 5.9416 8.5638 45.2545
REMARK 3 T TENSOR
REMARK 3 T11: 0.2163 T22: 0.1978
REMARK 3 T33: 0.1967 T12: -0.0256
REMARK 3 T13: 0.0117 T23: -0.0139
REMARK 3 L TENSOR
REMARK 3 L11: 8.6789 L22: 6.1448
REMARK 3 L33: 6.4788 L12: -2.3221
REMARK 3 L13: 3.2432 L23: -2.0877
REMARK 3 S TENSOR
REMARK 3 S11: -0.0976 S12: -0.1590 S13: 0.0706
REMARK 3 S21: 0.1798 S22: 0.0895 S23: 0.2821
REMARK 3 S31: -0.0955 S32: -0.2956 S33: 0.0081
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 : C 135 C 176
REMARK 3 ORIGIN FOR THE GROUP (A): 14.9635 1.4750 34.5892
REMARK 3 T TENSOR
REMARK 3 T11: 0.1968 T22: 0.1298
REMARK 3 T33: 0.1054 T12: -0.0379
REMARK 3 T13: -0.0287 T23: 0.0201
REMARK 3 L TENSOR
REMARK 3 L11: 2.2116 L22: 2.6792
REMARK 3 L33: 1.7023 L12: 1.1477
REMARK 3 L13: -0.0253 L23: -0.2557
REMARK 3 S TENSOR
REMARK 3 S11: -0.0048 S12: -0.1105 S13: 0.1742
REMARK 3 S21: -0.0185 S22: -0.0698 S23: 0.0403
REMARK 3 S31: -0.0098 S32: 0.1468 S33: 0.0745
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 : C 177 C 201
REMARK 3 ORIGIN FOR THE GROUP (A): 7.6300 12.9636 30.3011
REMARK 3 T TENSOR
REMARK 3 T11: 0.1994 T22: 0.1293
REMARK 3 T33: 0.0517 T12: -0.0536
REMARK 3 T13: -0.0121 T23: 0.0678
REMARK 3 L TENSOR
REMARK 3 L11: 3.5198 L22: 0.6899
REMARK 3 L33: 2.0931 L12: 0.2645
REMARK 3 L13: 0.0635 L23: 0.9634
REMARK 3 S TENSOR
REMARK 3 S11: -0.1185 S12: -0.0578 S13: 0.7439
REMARK 3 S21: 0.2242 S22: 0.0926 S23: -0.3732
REMARK 3 S31: -0.0579 S32: -0.1092 S33: 0.0259
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 : C 202 C 251
REMARK 3 ORIGIN FOR THE GROUP (A): -5.4276 1.9030 35.3704
REMARK 3 T TENSOR
REMARK 3 T11: 0.1753 T22: 0.1140
REMARK 3 T33: 0.1021 T12: -0.0695
REMARK 3 T13: 0.0106 T23: 0.0053
REMARK 3 L TENSOR
REMARK 3 L11: 2.5260 L22: 3.4195
REMARK 3 L33: 0.7561 L12: -1.9638
REMARK 3 L13: -0.1905 L23: 0.6950
REMARK 3 S TENSOR
REMARK 3 S11: -0.0709 S12: -0.2118 S13: -0.1080
REMARK 3 S21: 0.2281 S22: -0.0181 S23: 0.2017
REMARK 3 S31: 0.1569 S32: -0.2910 S33: 0.0890
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 : C 252 C 263
REMARK 3 ORIGIN FOR THE GROUP (A): -11.1545 -4.2268 24.3931
REMARK 3 T TENSOR
REMARK 3 T11: 0.2315 T22: 0.2315
REMARK 3 T33: 0.1767 T12: -0.0531
REMARK 3 T13: -0.0055 T23: -0.0117
REMARK 3 L TENSOR
REMARK 3 L11: 12.2362 L22: 10.7630
REMARK 3 L33: 6.5291 L12: -4.8370
REMARK 3 L13: 0.5346 L23: -0.8044
REMARK 3 S TENSOR
REMARK 3 S11: 0.1316 S12: 0.1673 S13: -0.2582
REMARK 3 S21: -0.2764 S22: -0.0649 S23: 0.6225
REMARK 3 S31: 0.0405 S32: -0.2731 S33: -0.0667
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 9 D 49
REMARK 3 ORIGIN FOR THE GROUP (A): -48.8429 32.9523 64.6989
REMARK 3 T TENSOR
REMARK 3 T11: 0.0427 T22: 0.0951
REMARK 3 T33: 0.1160 T12: 0.0254
REMARK 3 T13: 0.0168 T23: 0.0354
REMARK 3 L TENSOR
REMARK 3 L11: 3.3221 L22: 4.0282
REMARK 3 L33: 1.8899 L12: 1.2782
REMARK 3 L13: 0.2614 L23: 1.0747
REMARK 3 S TENSOR
REMARK 3 S11: -0.0342 S12: -0.3670 S13: 0.0730
REMARK 3 S21: 0.1549 S22: 0.0045 S23: -0.2993
REMARK 3 S31: -0.1259 S32: 0.0959 S33: 0.0297
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 : D 50 D 54
REMARK 3 ORIGIN FOR THE GROUP (A): -50.9055 15.8407 56.7934
REMARK 3 T TENSOR
REMARK 3 T11: 0.1122 T22: 0.0930
REMARK 3 T33: 0.1103 T12: 0.0350
REMARK 3 T13: 0.0234 T23: 0.0104
REMARK 3 L TENSOR
REMARK 3 L11: 25.3556 L22: 14.5809
REMARK 3 L33: 11.4934 L12: 10.3340
REMARK 3 L13: 8.6521 L23: 6.1528
REMARK 3 S TENSOR
REMARK 3 S11: 0.1501 S12: 0.1289 S13: -1.1194
REMARK 3 S21: -0.1535 S22: 0.1152 S23: -0.0206
REMARK 3 S31: 1.0052 S32: -0.2973 S33: -0.2654
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 : D 55 D 86
REMARK 3 ORIGIN FOR THE GROUP (A): -56.8860 23.2388 68.3691
REMARK 3 T TENSOR
REMARK 3 T11: 0.0800 T22: 0.1203
REMARK 3 T33: 0.1651 T12: 0.0456
REMARK 3 T13: 0.0358 T23: 0.0605
REMARK 3 L TENSOR
REMARK 3 L11: 2.2848 L22: 3.2797
REMARK 3 L33: 5.6396 L12: 0.6074
REMARK 3 L13: 0.8742 L23: 1.3366
REMARK 3 S TENSOR
REMARK 3 S11: -0.0126 S12: -0.2496 S13: -0.1932
REMARK 3 S21: 0.4663 S22: 0.1302 S23: -0.0978
REMARK 3 S31: 0.5346 S32: 0.0897 S33: -0.1176
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 : D 87 D 117
REMARK 3 ORIGIN FOR THE GROUP (A): -63.2722 30.8653 69.5589
REMARK 3 T TENSOR
REMARK 3 T11: 0.0513 T22: 0.0720
REMARK 3 T33: 0.1099 T12: 0.0179
REMARK 3 T13: 0.0057 T23: -0.0147
REMARK 3 L TENSOR
REMARK 3 L11: 4.6314 L22: 3.0432
REMARK 3 L33: 2.7075 L12: 0.7993
REMARK 3 L13: -2.0412 L23: 0.1123
REMARK 3 S TENSOR
REMARK 3 S11: -0.1365 S12: -0.1532 S13: -0.0526
REMARK 3 S21: 0.0426 S22: 0.0587 S23: 0.0759
REMARK 3 S31: 0.0613 S32: -0.2392 S33: 0.0779
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 : D 118 D 135
REMARK 3 ORIGIN FOR THE GROUP (A): -74.6018 31.7798 56.6223
REMARK 3 T TENSOR
REMARK 3 T11: 0.1152 T22: 0.1442
REMARK 3 T33: 0.1647 T12: -0.0045
REMARK 3 T13: -0.0023 T23: -0.0112
REMARK 3 L TENSOR
REMARK 3 L11: 0.8660 L22: 1.4231
REMARK 3 L33: 10.2951 L12: 0.1408
REMARK 3 L13: -0.9645 L23: -1.4833
REMARK 3 S TENSOR
REMARK 3 S11: 0.0545 S12: 0.1334 S13: 0.1535
REMARK 3 S21: -0.0767 S22: 0.0008 S23: 0.0396
REMARK 3 S31: -0.2452 S32: -0.0178 S33: -0.0553
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 : D 136 D 156
REMARK 3 ORIGIN FOR THE GROUP (A): -66.1904 19.9533 47.5942
REMARK 3 T TENSOR
REMARK 3 T11: 0.1392 T22: 0.1694
REMARK 3 T33: 0.1854 T12: -0.0127
REMARK 3 T13: 0.0256 T23: -0.0013
REMARK 3 L TENSOR
REMARK 3 L11: 2.8689 L22: 8.3948
REMARK 3 L33: 5.2133 L12: 0.3573
REMARK 3 L13: 1.2421 L23: -1.6168
REMARK 3 S TENSOR
REMARK 3 S11: 0.1313 S12: -0.2652 S13: -0.1542
REMARK 3 S21: 0.3195 S22: -0.0479 S23: 0.6776
REMARK 3 S31: 0.3257 S32: -0.3564 S33: -0.0834
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 : D 157 D 201
REMARK 3 ORIGIN FOR THE GROUP (A): -59.7664 29.5849 53.2994
REMARK 3 T TENSOR
REMARK 3 T11: 0.0510 T22: 0.0320
REMARK 3 T33: 0.1114 T12: -0.0003
REMARK 3 T13: -0.0457 T23: 0.0117
REMARK 3 L TENSOR
REMARK 3 L11: 1.8199 L22: 1.6002
REMARK 3 L33: 2.4987 L12: -0.4478
REMARK 3 L13: -0.0245 L23: 0.4160
REMARK 3 S TENSOR
REMARK 3 S11: -0.1695 S12: 0.1072 S13: 0.0628
REMARK 3 S21: -0.1695 S22: 0.1009 S23: 0.0492
REMARK 3 S31: 0.2193 S32: -0.0141 S33: 0.0686
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 : D 202 D 239
REMARK 3 ORIGIN FOR THE GROUP (A): -66.4066 41.0368 63.7883
REMARK 3 T TENSOR
REMARK 3 T11: 0.0934 T22: 0.0392
REMARK 3 T33: 0.2107 T12: 0.0206
REMARK 3 T13: -0.0024 T23: -0.0290
REMARK 3 L TENSOR
REMARK 3 L11: 3.2598 L22: 1.4648
REMARK 3 L33: 4.1663 L12: 0.5291
REMARK 3 L13: -1.9184 L23: -1.8658
REMARK 3 S TENSOR
REMARK 3 S11: -0.0728 S12: -0.0404 S13: 0.4201
REMARK 3 S21: -0.0207 S22: 0.0330 S23: 0.1171
REMARK 3 S31: -0.2663 S32: -0.3071 S33: 0.0398
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 : D 240 D 263
REMARK 3 ORIGIN FOR THE GROUP (A): -53.0743 44.4725 62.0623
REMARK 3 T TENSOR
REMARK 3 T11: 0.1256 T22: 0.0583
REMARK 3 T33: 0.2470 T12: -0.0192
REMARK 3 T13: -0.0071 T23: 0.0255
REMARK 3 L TENSOR
REMARK 3 L11: 3.9223 L22: 1.7752
REMARK 3 L33: 8.4206 L12: -0.3137
REMARK 3 L13: -0.6159 L23: -0.0720
REMARK 3 S TENSOR
REMARK 3 S11: -0.0852 S12: -0.3374 S13: 0.4411
REMARK 3 S21: 0.1549 S22: 0.0651 S23: -0.0996
REMARK 3 S31: -0.6970 S32: 0.4009 S33: 0.0201
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 : E 9 E 46
REMARK 3 ORIGIN FOR THE GROUP (A): 22.1223 -13.6266 19.8014
REMARK 3 T TENSOR
REMARK 3 T11: 0.3632 T22: 0.0913
REMARK 3 T33: 0.1746 T12: 0.0280
REMARK 3 T13: -0.0418 T23: -0.0198
REMARK 3 L TENSOR
REMARK 3 L11: 4.7116 L22: 2.6785
REMARK 3 L33: 3.5943 L12: -0.5425
REMARK 3 L13: -0.1140 L23: -0.9388
REMARK 3 S TENSOR
REMARK 3 S11: 0.1805 S12: -0.2141 S13: -0.3828
REMARK 3 S21: 0.2659 S22: -0.0993 S23: -0.1814
REMARK 3 S31: 0.5903 S32: 0.2872 S33: -0.0812
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 : E 47 E 63
REMARK 3 ORIGIN FOR THE GROUP (A): 26.5021 4.2258 10.9713
REMARK 3 T TENSOR
REMARK 3 T11: 0.3241 T22: 0.2432
REMARK 3 T33: 0.3758 T12: 0.0098
REMARK 3 T13: 0.0203 T23: 0.0689
REMARK 3 L TENSOR
REMARK 3 L11: 3.6930 L22: 0.6594
REMARK 3 L33: 8.0092 L12: 1.2548
REMARK 3 L13: -2.3554 L23: 0.4075
REMARK 3 S TENSOR
REMARK 3 S11: 0.0420 S12: 0.4509 S13: 0.4300
REMARK 3 S21: -0.3496 S22: -0.0023 S23: -0.6159
REMARK 3 S31: -0.4046 S32: 0.5829 S33: -0.0398
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 : E 64 E 109
REMARK 3 ORIGIN FOR THE GROUP (A): 33.6872 -11.8442 14.6293
REMARK 3 T TENSOR
REMARK 3 T11: 0.3863 T22: 0.3296
REMARK 3 T33: 0.3125 T12: 0.1185
REMARK 3 T13: -0.0046 T23: 0.0178
REMARK 3 L TENSOR
REMARK 3 L11: 3.1996 L22: 4.0428
REMARK 3 L33: 0.9247 L12: -0.7093
REMARK 3 L13: -1.0189 L23: -1.2063
REMARK 3 S TENSOR
REMARK 3 S11: 0.1621 S12: -0.1284 S13: -0.2297
REMARK 3 S21: 0.2770 S22: -0.1083 S23: -0.4733
REMARK 3 S31: 0.1131 S32: 0.6536 S33: -0.0538
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 : E 110 E 134
REMARK 3 ORIGIN FOR THE GROUP (A): 27.9737 -12.5676 -4.4067
REMARK 3 T TENSOR
REMARK 3 T11: 0.6635 T22: 0.7755
REMARK 3 T33: 0.5086 T12: 0.1827
REMARK 3 T13: 0.0106 T23: 0.0018
REMARK 3 L TENSOR
REMARK 3 L11: 0.0000 L22: 0.0294
REMARK 3 L33: 0.0067 L12: 0.0011
REMARK 3 L13: 0.0005 L23: 0.0140
REMARK 3 S TENSOR
REMARK 3 S11: 0.2221 S12: 0.4423 S13: -0.1879
REMARK 3 S21: -0.5554 S22: 0.0585 S23: -0.3191
REMARK 3 S31: 0.7250 S32: 0.4070 S33: -0.2805
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 : E 135 E 172
REMARK 3 ORIGIN FOR THE GROUP (A): 14.3103 -2.3588 0.4755
REMARK 3 T TENSOR
REMARK 3 T11: 0.4020 T22: 0.3102
REMARK 3 T33: 0.2520 T12: 0.0482
REMARK 3 T13: 0.0022 T23: 0.0579
REMARK 3 L TENSOR
REMARK 3 L11: 2.9337 L22: 3.9180
REMARK 3 L33: 3.4639 L12: 1.7315
REMARK 3 L13: -1.1182 L23: -0.6498
REMARK 3 S TENSOR
REMARK 3 S11: 0.2157 S12: 0.4311 S13: 0.2423
REMARK 3 S21: -0.1858 S22: -0.1547 S23: -0.3379
REMARK 3 S31: -0.2316 S32: 0.2540 S33: -0.0610
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 : E 173 E 184
REMARK 3 ORIGIN FOR THE GROUP (A): 9.0459 -4.0460 12.4311
REMARK 3 T TENSOR
REMARK 3 T11: 0.2120 T22: 0.1533
REMARK 3 T33: 0.1343 T12: 0.0022
REMARK 3 T13: -0.0002 T23: 0.0000
REMARK 3 L TENSOR
REMARK 3 L11: 8.2334 L22: 3.2706
REMARK 3 L33: 2.3031 L12: 1.8788
REMARK 3 L13: 1.3588 L23: 0.8594
REMARK 3 S TENSOR
REMARK 3 S11: -0.0070 S12: -0.0409 S13: 0.0356
REMARK 3 S21: -0.0927 S22: 0.0452 S23: 0.3360
REMARK 3 S31: 0.2983 S32: -0.3337 S33: -0.0382
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 : E 185 E 216
REMARK 3 ORIGIN FOR THE GROUP (A): 31.7936 -12.2944 3.1416
REMARK 3 T TENSOR
REMARK 3 T11: 0.4392 T22: 0.4045
REMARK 3 T33: 0.3884 T12: 0.1513
REMARK 3 T13: 0.0464 T23: -0.0544
REMARK 3 L TENSOR
REMARK 3 L11: 2.5859 L22: 1.7129
REMARK 3 L33: 1.6257 L12: -0.9326
REMARK 3 L13: 0.5326 L23: 0.0486
REMARK 3 S TENSOR
REMARK 3 S11: 0.1635 S12: 0.5555 S13: -0.1137
REMARK 3 S21: -0.3152 S22: -0.1033 S23: -0.4585
REMARK 3 S31: 0.1599 S32: 0.5419 S33: -0.0602
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 : E 217 E 241
REMARK 3 ORIGIN FOR THE GROUP (A): 22.6429 -22.9305 0.5451
REMARK 3 T TENSOR
REMARK 3 T11: 0.7264 T22: 0.2873
REMARK 3 T33: 0.5191 T12: 0.0749
REMARK 3 T13: -0.0415 T23: -0.1382
REMARK 3 L TENSOR
REMARK 3 L11: 6.6151 L22: 2.8158
REMARK 3 L33: 5.8261 L12: -1.8273
REMARK 3 L13: 0.3349 L23: -1.2502
REMARK 3 S TENSOR
REMARK 3 S11: -0.1194 S12: 1.0320 S13: -0.4680
REMARK 3 S21: -0.5061 S22: -0.1784 S23: -0.5344
REMARK 3 S31: 0.8321 S32: 0.0838 S33: 0.2978
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 : E 242 E 263
REMARK 3 ORIGIN FOR THE GROUP (A): 17.8940 -22.3696 14.4420
REMARK 3 T TENSOR
REMARK 3 T11: 0.5748 T22: 0.1297
REMARK 3 T33: 0.3763 T12: 0.0496
REMARK 3 T13: -0.0566 T23: -0.0076
REMARK 3 L TENSOR
REMARK 3 L11: 7.3878 L22: 5.7310
REMARK 3 L33: 3.0415 L12: -4.4904
REMARK 3 L13: 2.3248 L23: -2.7928
REMARK 3 S TENSOR
REMARK 3 S11: -0.0033 S12: -0.1019 S13: -0.9823
REMARK 3 S21: 0.4252 S22: 0.0421 S23: -0.2354
REMARK 3 S31: 0.6549 S32: 0.2605 S33: -0.0388
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 RESIDUAL B FACTORS
REMARK 3 ONLY.
REMARK 4
REMARK 4 2WFM COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 08-APR-09.
REMARK 100 THE PDBE ID CODE IS EBI-39434.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : SILICON 111
REMARK 200 OPTICS : DOUBLE CRYSTAL SI 111
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL (PILATUS 6M)
REMARK 200 DETECTOR MANUFACTURER : PSI
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 91937
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.00
REMARK 200 RESOLUTION RANGE LOW (A) : 20.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.8
REMARK 200 DATA REDUNDANCY : 2.7
REMARK 200 R MERGE (I) : 0.06
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 11.50
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.12
REMARK 200 COMPLETENESS FOR SHELL (%) : 88.3
REMARK 200 DATA REDUNDANCY IN SHELL : 2.5
REMARK 200 R MERGE FOR SHELL (I) : 0.34
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.70
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AUTO-RICKSHAW,MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 2WFL
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): 2.35
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M BIS-TRIS, 0.25 M LI2SO4,
REMARK 280 25% POLYETHYLENE GLYCOL 3350, PH 6.30
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 85.12500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 23.40500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 85.12500
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 23.40500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
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: 5
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E
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 400
REMARK 400 COMPOUND
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, HIS 244 TO ALA
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, HIS 244 TO ALA
REMARK 400 ENGINEERED RESIDUE IN CHAIN C, HIS 244 TO ALA
REMARK 400 ENGINEERED RESIDUE IN CHAIN D, HIS 244 TO ALA
REMARK 400 ENGINEERED RESIDUE IN CHAIN E, HIS 244 TO ALA
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 HIS A 2
REMARK 465 SER A 3
REMARK 465 ALA A 4
REMARK 465 ALA A 5
REMARK 465 ASN A 6
REMARK 465 ALA A 7
REMARK 465 LYS A 8
REMARK 465 SER A 264
REMARK 465 MET B 1
REMARK 465 HIS B 2
REMARK 465 SER B 3
REMARK 465 ALA B 4
REMARK 465 ALA B 5
REMARK 465 ASN B 6
REMARK 465 ALA B 7
REMARK 465 LYS B 8
REMARK 465 SER B 264
REMARK 465 MET C 1
REMARK 465 HIS C 2
REMARK 465 SER C 3
REMARK 465 ALA C 4
REMARK 465 ALA C 5
REMARK 465 ASN C 6
REMARK 465 ALA C 7
REMARK 465 LYS C 8
REMARK 465 SER C 264
REMARK 465 MET D 1
REMARK 465 HIS D 2
REMARK 465 SER D 3
REMARK 465 ALA D 4
REMARK 465 ALA D 5
REMARK 465 ASN D 6
REMARK 465 ALA D 7
REMARK 465 LYS D 8
REMARK 465 SER D 264
REMARK 465 MET E 1
REMARK 465 HIS E 2
REMARK 465 SER E 3
REMARK 465 ALA E 4
REMARK 465 ALA E 5
REMARK 465 ASN E 6
REMARK 465 ALA E 7
REMARK 465 LYS E 8
REMARK 465 SER E 264
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 OE1 GLN D 160 O HOH D 2025 1.99
REMARK 500 CE MET A 136 O HOH A 2020 2.01
REMARK 500 NZ LYS D 197 O HOH D 2039 2.02
REMARK 500 O HOH A 2010 O HOH A 2033 2.05
REMARK 500 OH TYR A 128 O SER A 218 2.07
REMARK 500 NE2 GLN C 190 O HOH C 2032 2.14
REMARK 500 O HOH B 2039 O HOH B 2040 2.14
REMARK 500 OD1 ASN E 150 NZ LYS E 194 2.18
REMARK 500 CB SER A 230 ND2 ASN C 118 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 222 CB GLU A 222 CG -0.178
REMARK 500 PHE A 223 CB PHE A 223 CG -0.179
REMARK 500 PHE A 223 CE2 PHE A 223 CD2 -0.135
REMARK 500 CYS A 257 CB CYS A 257 SG -0.101
REMARK 500 PHE B 223 CB PHE B 223 CG -0.187
REMARK 500 PHE B 223 CZ PHE B 223 CE2 -0.129
REMARK 500 PHE B 223 CE2 PHE B 223 CD2 -0.159
REMARK 500 PHE C 223 CB PHE C 223 CG -0.210
REMARK 500 PHE C 223 CZ PHE C 223 CE2 -0.115
REMARK 500 PHE C 223 CE2 PHE C 223 CD2 -0.147
REMARK 500 GLN D 168 CD GLN D 168 OE1 -0.138
REMARK 500 PHE D 223 CB PHE D 223 CG -0.192
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 54 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 VAL A 221 CB - CA - C ANGL. DEV. = -11.8 DEGREES
REMARK 500 PHE A 223 CB - CG - CD2 ANGL. DEV. = -7.5 DEGREES
REMARK 500 LYS A 237 CD - CE - NZ ANGL. DEV. = 14.7 DEGREES
REMARK 500 ARG B 54 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG C 54 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 PRO C 151 C - N - CA ANGL. DEV. = 11.1 DEGREES
REMARK 500 ARG D 54 CD - NE - CZ ANGL. DEV. = 11.4 DEGREES
REMARK 500 ARG D 54 NE - CZ - NH1 ANGL. DEV. = -9.1 DEGREES
REMARK 500 ARG D 54 NE - CZ - NH2 ANGL. DEV. = 8.5 DEGREES
REMARK 500 VAL D 221 CB - CA - C ANGL. DEV. = -12.3 DEGREES
REMARK 500 PHE D 223 CB - CG - CD2 ANGL. DEV. = -6.3 DEGREES
REMARK 500 LYS D 237 CD - CE - NZ ANGL. DEV. = 15.8 DEGREES
REMARK 500 ARG D 252 CD - NE - CZ ANGL. DEV. = 11.1 DEGREES
REMARK 500 ARG D 252 NE - CZ - NH1 ANGL. DEV. = -7.7 DEGREES
REMARK 500 ARG D 252 NE - CZ - NH2 ANGL. DEV. = 7.6 DEGREES
REMARK 500 PRO E 148 C - N - CA ANGL. DEV. = 10.9 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 LEU A 21 -156.07 -110.75
REMARK 500 SER A 87 -139.14 60.87
REMARK 500 SER A 111 57.26 37.94
REMARK 500 LEU A 138 -122.70 49.22
REMARK 500 ARG A 202 -78.33 -97.59
REMARK 500 ASP A 243 -160.00 -86.13
REMARK 500 MET A 245 67.12 -104.93
REMARK 500 GLN A 250 51.34 -142.57
REMARK 500 LEU B 21 -160.33 -110.88
REMARK 500 SER B 87 -129.89 56.68
REMARK 500 SER B 111 59.98 24.31
REMARK 500 LEU B 138 -120.13 56.63
REMARK 500 ARG B 202 -75.84 -100.12
REMARK 500 MET B 245 68.99 -116.11
REMARK 500 LEU C 21 -161.21 -114.58
REMARK 500 ASP C 78 31.78 -93.36
REMARK 500 SER C 87 -124.02 63.31
REMARK 500 LEU C 138 -114.83 57.62
REMARK 500 ASN C 150 55.24 -149.46
REMARK 500 ARG C 202 -79.74 -97.07
REMARK 500 ASP C 243 -159.05 -85.87
REMARK 500 MET C 245 62.87 -109.42
REMARK 500 GLN C 250 50.37 -142.05
REMARK 500 LEU D 21 -160.17 -110.03
REMARK 500 SER D 87 -133.80 50.29
REMARK 500 SER D 111 53.28 37.01
REMARK 500 LEU D 138 -123.45 48.25
REMARK 500 ARG D 202 -80.15 -94.69
REMARK 500 MET D 245 68.47 -105.40
REMARK 500 GLN D 250 52.67 -144.94
REMARK 500 LEU E 21 -163.49 -123.41
REMARK 500 SER E 87 -124.98 49.39
REMARK 500 SER E 111 52.09 34.69
REMARK 500 HIS E 119 -165.58 -100.02
REMARK 500 GLU E 130 -18.10 -48.57
REMARK 500 LEU E 138 -120.66 44.82
REMARK 500 PRO E 148 -84.25 -46.12
REMARK 500 LYS E 194 38.16 -96.69
REMARK 500 ARG E 202 -63.99 -98.73
REMARK 500 LYS E 217 12.14 -69.09
REMARK 500 PHE E 219 81.38 -156.66
REMARK 500 VAL E 231 -55.70 -129.48
REMARK 500 ASP E 243 -160.43 -74.82
REMARK 500 MET E 245 66.06 -106.54
REMARK 500 GLN E 250 49.62 -140.37
REMARK 500 ARG E 252 -8.15 -59.88
REMARK 500 SER E 262 52.73 -91.92
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2WFL RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF POLYNEURIDINE ALDEHYDE
REMARK 900 ESTERASE
DBREF 2WFM A 1 264 UNP Q9SE93 PNAE_RAUSE 1 264
DBREF 2WFM B 1 264 UNP Q9SE93 PNAE_RAUSE 1 264
DBREF 2WFM C 1 264 UNP Q9SE93 PNAE_RAUSE 1 264
DBREF 2WFM D 1 264 UNP Q9SE93 PNAE_RAUSE 1 264
DBREF 2WFM E 1 264 UNP Q9SE93 PNAE_RAUSE 1 264
SEQADV 2WFM ALA A 244 UNP Q9SE93 HIS 244 ENGINEERED MUTATION
SEQADV 2WFM ALA B 244 UNP Q9SE93 HIS 244 ENGINEERED MUTATION
SEQADV 2WFM ALA C 244 UNP Q9SE93 HIS 244 ENGINEERED MUTATION
SEQADV 2WFM ALA D 244 UNP Q9SE93 HIS 244 ENGINEERED MUTATION
SEQADV 2WFM ALA E 244 UNP Q9SE93 HIS 244 ENGINEERED MUTATION
SEQRES 1 A 264 MET HIS SER ALA ALA ASN ALA LYS GLN GLN LYS HIS PHE
SEQRES 2 A 264 VAL LEU VAL HIS GLY GLY CYS LEU GLY ALA TRP ILE TRP
SEQRES 3 A 264 TYR LYS LEU LYS PRO LEU LEU GLU SER ALA GLY HIS LYS
SEQRES 4 A 264 VAL THR ALA VAL ASP LEU SER ALA ALA GLY ILE ASN PRO
SEQRES 5 A 264 ARG ARG LEU ASP GLU ILE HIS THR PHE ARG ASP TYR SER
SEQRES 6 A 264 GLU PRO LEU MET GLU VAL MET ALA SER ILE PRO PRO ASP
SEQRES 7 A 264 GLU LYS VAL VAL LEU LEU GLY HIS SER PHE GLY GLY MET
SEQRES 8 A 264 SER LEU GLY LEU ALA MET GLU THR TYR PRO GLU LYS ILE
SEQRES 9 A 264 SER VAL ALA VAL PHE MET SER ALA MET MET PRO ASP PRO
SEQRES 10 A 264 ASN HIS SER LEU THR TYR PRO PHE GLU LYS TYR ASN GLU
SEQRES 11 A 264 LYS CYS PRO ALA ASP MET MET LEU ASP SER GLN PHE SER
SEQRES 12 A 264 THR TYR GLY ASN PRO GLU ASN PRO GLY MET SER MET ILE
SEQRES 13 A 264 LEU GLY PRO GLN PHE MET ALA LEU LYS MET PHE GLN ASN
SEQRES 14 A 264 CYS SER VAL GLU ASP LEU GLU LEU ALA LYS MET LEU THR
SEQRES 15 A 264 ARG PRO GLY SER LEU PHE PHE GLN ASP LEU ALA LYS ALA
SEQRES 16 A 264 LYS LYS PHE SER THR GLU ARG TYR GLY SER VAL LYS ARG
SEQRES 17 A 264 ALA TYR ILE PHE CYS ASN GLU ASP LYS SER PHE PRO VAL
SEQRES 18 A 264 GLU PHE GLN LYS TRP PHE VAL GLU SER VAL GLY ALA ASP
SEQRES 19 A 264 LYS VAL LYS GLU ILE LYS GLU ALA ASP ALA MET GLY MET
SEQRES 20 A 264 LEU SER GLN PRO ARG GLU VAL CYS LYS CYS LEU LEU ASP
SEQRES 21 A 264 ILE SER ASP SER
SEQRES 1 B 264 MET HIS SER ALA ALA ASN ALA LYS GLN GLN LYS HIS PHE
SEQRES 2 B 264 VAL LEU VAL HIS GLY GLY CYS LEU GLY ALA TRP ILE TRP
SEQRES 3 B 264 TYR LYS LEU LYS PRO LEU LEU GLU SER ALA GLY HIS LYS
SEQRES 4 B 264 VAL THR ALA VAL ASP LEU SER ALA ALA GLY ILE ASN PRO
SEQRES 5 B 264 ARG ARG LEU ASP GLU ILE HIS THR PHE ARG ASP TYR SER
SEQRES 6 B 264 GLU PRO LEU MET GLU VAL MET ALA SER ILE PRO PRO ASP
SEQRES 7 B 264 GLU LYS VAL VAL LEU LEU GLY HIS SER PHE GLY GLY MET
SEQRES 8 B 264 SER LEU GLY LEU ALA MET GLU THR TYR PRO GLU LYS ILE
SEQRES 9 B 264 SER VAL ALA VAL PHE MET SER ALA MET MET PRO ASP PRO
SEQRES 10 B 264 ASN HIS SER LEU THR TYR PRO PHE GLU LYS TYR ASN GLU
SEQRES 11 B 264 LYS CYS PRO ALA ASP MET MET LEU ASP SER GLN PHE SER
SEQRES 12 B 264 THR TYR GLY ASN PRO GLU ASN PRO GLY MET SER MET ILE
SEQRES 13 B 264 LEU GLY PRO GLN PHE MET ALA LEU LYS MET PHE GLN ASN
SEQRES 14 B 264 CYS SER VAL GLU ASP LEU GLU LEU ALA LYS MET LEU THR
SEQRES 15 B 264 ARG PRO GLY SER LEU PHE PHE GLN ASP LEU ALA LYS ALA
SEQRES 16 B 264 LYS LYS PHE SER THR GLU ARG TYR GLY SER VAL LYS ARG
SEQRES 17 B 264 ALA TYR ILE PHE CYS ASN GLU ASP LYS SER PHE PRO VAL
SEQRES 18 B 264 GLU PHE GLN LYS TRP PHE VAL GLU SER VAL GLY ALA ASP
SEQRES 19 B 264 LYS VAL LYS GLU ILE LYS GLU ALA ASP ALA MET GLY MET
SEQRES 20 B 264 LEU SER GLN PRO ARG GLU VAL CYS LYS CYS LEU LEU ASP
SEQRES 21 B 264 ILE SER ASP SER
SEQRES 1 C 264 MET HIS SER ALA ALA ASN ALA LYS GLN GLN LYS HIS PHE
SEQRES 2 C 264 VAL LEU VAL HIS GLY GLY CYS LEU GLY ALA TRP ILE TRP
SEQRES 3 C 264 TYR LYS LEU LYS PRO LEU LEU GLU SER ALA GLY HIS LYS
SEQRES 4 C 264 VAL THR ALA VAL ASP LEU SER ALA ALA GLY ILE ASN PRO
SEQRES 5 C 264 ARG ARG LEU ASP GLU ILE HIS THR PHE ARG ASP TYR SER
SEQRES 6 C 264 GLU PRO LEU MET GLU VAL MET ALA SER ILE PRO PRO ASP
SEQRES 7 C 264 GLU LYS VAL VAL LEU LEU GLY HIS SER PHE GLY GLY MET
SEQRES 8 C 264 SER LEU GLY LEU ALA MET GLU THR TYR PRO GLU LYS ILE
SEQRES 9 C 264 SER VAL ALA VAL PHE MET SER ALA MET MET PRO ASP PRO
SEQRES 10 C 264 ASN HIS SER LEU THR TYR PRO PHE GLU LYS TYR ASN GLU
SEQRES 11 C 264 LYS CYS PRO ALA ASP MET MET LEU ASP SER GLN PHE SER
SEQRES 12 C 264 THR TYR GLY ASN PRO GLU ASN PRO GLY MET SER MET ILE
SEQRES 13 C 264 LEU GLY PRO GLN PHE MET ALA LEU LYS MET PHE GLN ASN
SEQRES 14 C 264 CYS SER VAL GLU ASP LEU GLU LEU ALA LYS MET LEU THR
SEQRES 15 C 264 ARG PRO GLY SER LEU PHE PHE GLN ASP LEU ALA LYS ALA
SEQRES 16 C 264 LYS LYS PHE SER THR GLU ARG TYR GLY SER VAL LYS ARG
SEQRES 17 C 264 ALA TYR ILE PHE CYS ASN GLU ASP LYS SER PHE PRO VAL
SEQRES 18 C 264 GLU PHE GLN LYS TRP PHE VAL GLU SER VAL GLY ALA ASP
SEQRES 19 C 264 LYS VAL LYS GLU ILE LYS GLU ALA ASP ALA MET GLY MET
SEQRES 20 C 264 LEU SER GLN PRO ARG GLU VAL CYS LYS CYS LEU LEU ASP
SEQRES 21 C 264 ILE SER ASP SER
SEQRES 1 D 264 MET HIS SER ALA ALA ASN ALA LYS GLN GLN LYS HIS PHE
SEQRES 2 D 264 VAL LEU VAL HIS GLY GLY CYS LEU GLY ALA TRP ILE TRP
SEQRES 3 D 264 TYR LYS LEU LYS PRO LEU LEU GLU SER ALA GLY HIS LYS
SEQRES 4 D 264 VAL THR ALA VAL ASP LEU SER ALA ALA GLY ILE ASN PRO
SEQRES 5 D 264 ARG ARG LEU ASP GLU ILE HIS THR PHE ARG ASP TYR SER
SEQRES 6 D 264 GLU PRO LEU MET GLU VAL MET ALA SER ILE PRO PRO ASP
SEQRES 7 D 264 GLU LYS VAL VAL LEU LEU GLY HIS SER PHE GLY GLY MET
SEQRES 8 D 264 SER LEU GLY LEU ALA MET GLU THR TYR PRO GLU LYS ILE
SEQRES 9 D 264 SER VAL ALA VAL PHE MET SER ALA MET MET PRO ASP PRO
SEQRES 10 D 264 ASN HIS SER LEU THR TYR PRO PHE GLU LYS TYR ASN GLU
SEQRES 11 D 264 LYS CYS PRO ALA ASP MET MET LEU ASP SER GLN PHE SER
SEQRES 12 D 264 THR TYR GLY ASN PRO GLU ASN PRO GLY MET SER MET ILE
SEQRES 13 D 264 LEU GLY PRO GLN PHE MET ALA LEU LYS MET PHE GLN ASN
SEQRES 14 D 264 CYS SER VAL GLU ASP LEU GLU LEU ALA LYS MET LEU THR
SEQRES 15 D 264 ARG PRO GLY SER LEU PHE PHE GLN ASP LEU ALA LYS ALA
SEQRES 16 D 264 LYS LYS PHE SER THR GLU ARG TYR GLY SER VAL LYS ARG
SEQRES 17 D 264 ALA TYR ILE PHE CYS ASN GLU ASP LYS SER PHE PRO VAL
SEQRES 18 D 264 GLU PHE GLN LYS TRP PHE VAL GLU SER VAL GLY ALA ASP
SEQRES 19 D 264 LYS VAL LYS GLU ILE LYS GLU ALA ASP ALA MET GLY MET
SEQRES 20 D 264 LEU SER GLN PRO ARG GLU VAL CYS LYS CYS LEU LEU ASP
SEQRES 21 D 264 ILE SER ASP SER
SEQRES 1 E 264 MET HIS SER ALA ALA ASN ALA LYS GLN GLN LYS HIS PHE
SEQRES 2 E 264 VAL LEU VAL HIS GLY GLY CYS LEU GLY ALA TRP ILE TRP
SEQRES 3 E 264 TYR LYS LEU LYS PRO LEU LEU GLU SER ALA GLY HIS LYS
SEQRES 4 E 264 VAL THR ALA VAL ASP LEU SER ALA ALA GLY ILE ASN PRO
SEQRES 5 E 264 ARG ARG LEU ASP GLU ILE HIS THR PHE ARG ASP TYR SER
SEQRES 6 E 264 GLU PRO LEU MET GLU VAL MET ALA SER ILE PRO PRO ASP
SEQRES 7 E 264 GLU LYS VAL VAL LEU LEU GLY HIS SER PHE GLY GLY MET
SEQRES 8 E 264 SER LEU GLY LEU ALA MET GLU THR TYR PRO GLU LYS ILE
SEQRES 9 E 264 SER VAL ALA VAL PHE MET SER ALA MET MET PRO ASP PRO
SEQRES 10 E 264 ASN HIS SER LEU THR TYR PRO PHE GLU LYS TYR ASN GLU
SEQRES 11 E 264 LYS CYS PRO ALA ASP MET MET LEU ASP SER GLN PHE SER
SEQRES 12 E 264 THR TYR GLY ASN PRO GLU ASN PRO GLY MET SER MET ILE
SEQRES 13 E 264 LEU GLY PRO GLN PHE MET ALA LEU LYS MET PHE GLN ASN
SEQRES 14 E 264 CYS SER VAL GLU ASP LEU GLU LEU ALA LYS MET LEU THR
SEQRES 15 E 264 ARG PRO GLY SER LEU PHE PHE GLN ASP LEU ALA LYS ALA
SEQRES 16 E 264 LYS LYS PHE SER THR GLU ARG TYR GLY SER VAL LYS ARG
SEQRES 17 E 264 ALA TYR ILE PHE CYS ASN GLU ASP LYS SER PHE PRO VAL
SEQRES 18 E 264 GLU PHE GLN LYS TRP PHE VAL GLU SER VAL GLY ALA ASP
SEQRES 19 E 264 LYS VAL LYS GLU ILE LYS GLU ALA ASP ALA MET GLY MET
SEQRES 20 E 264 LEU SER GLN PRO ARG GLU VAL CYS LYS CYS LEU LEU ASP
SEQRES 21 E 264 ILE SER ASP SER
FORMUL 6 HOH *188(H2 O)
HELIX 1 1 GLY A 22 TYR A 27 5 6
HELIX 2 2 LYS A 28 ALA A 36 1 9
HELIX 3 3 ARG A 54 ILE A 58 5 5
HELIX 4 4 THR A 60 SER A 74 1 15
HELIX 5 5 PHE A 88 TYR A 100 1 13
HELIX 6 6 THR A 122 CYS A 132 1 11
HELIX 7 7 GLY A 158 MET A 166 1 9
HELIX 8 8 SER A 171 THR A 182 1 12
HELIX 9 9 PHE A 188 ALA A 193 1 6
HELIX 10 10 ARG A 202 VAL A 206 5 5
HELIX 11 11 PRO A 220 VAL A 231 1 12
HELIX 12 12 MET A 245 GLN A 250 1 6
HELIX 13 13 GLN A 250 ASP A 263 1 14
HELIX 14 14 GLY B 22 TYR B 27 5 6
HELIX 15 15 LYS B 28 ALA B 36 1 9
HELIX 16 16 ARG B 54 ILE B 58 5 5
HELIX 17 17 THR B 60 SER B 74 1 15
HELIX 18 18 PHE B 88 TYR B 100 1 13
HELIX 19 19 THR B 122 PRO B 124 5 3
HELIX 20 20 PHE B 125 CYS B 132 1 8
HELIX 21 21 PRO B 133 LEU B 138 5 6
HELIX 22 22 GLY B 158 MET B 166 1 9
HELIX 23 23 SER B 171 THR B 182 1 12
HELIX 24 24 PHE B 188 ALA B 195 1 8
HELIX 25 25 ARG B 202 VAL B 206 5 5
HELIX 26 26 PRO B 220 VAL B 231 1 12
HELIX 27 27 MET B 245 GLN B 250 1 6
HELIX 28 28 GLN B 250 ASP B 263 1 14
HELIX 29 29 GLY C 22 TYR C 27 5 6
HELIX 30 30 LYS C 28 ALA C 36 1 9
HELIX 31 31 ARG C 54 ILE C 58 5 5
HELIX 32 32 THR C 60 SER C 74 1 15
HELIX 33 33 PHE C 88 TYR C 100 1 13
HELIX 34 34 THR C 122 PRO C 124 5 3
HELIX 35 35 PHE C 125 CYS C 132 1 8
HELIX 36 36 PRO C 133 LEU C 138 5 6
HELIX 37 37 GLY C 158 MET C 166 1 9
HELIX 38 38 SER C 171 THR C 182 1 12
HELIX 39 39 PHE C 188 ALA C 195 1 8
HELIX 40 40 ARG C 202 VAL C 206 5 5
HELIX 41 41 PRO C 220 VAL C 231 1 12
HELIX 42 42 MET C 245 GLN C 250 1 6
HELIX 43 43 GLN C 250 ASP C 263 1 14
HELIX 44 44 GLY D 22 TYR D 27 5 6
HELIX 45 45 LYS D 28 ALA D 36 1 9
HELIX 46 46 ARG D 54 ILE D 58 5 5
HELIX 47 47 THR D 60 SER D 65 1 6
HELIX 48 48 SER D 65 SER D 74 1 10
HELIX 49 49 PHE D 88 TYR D 100 1 13
HELIX 50 50 THR D 122 CYS D 132 1 11
HELIX 51 51 GLY D 158 MET D 166 1 9
HELIX 52 52 SER D 171 THR D 182 1 12
HELIX 53 53 PHE D 188 ALA D 195 1 8
HELIX 54 54 ARG D 202 VAL D 206 5 5
HELIX 55 55 PRO D 220 VAL D 231 1 12
HELIX 56 56 MET D 245 GLN D 250 1 6
HELIX 57 57 GLN D 250 ASP D 263 1 14
HELIX 58 58 GLY E 22 TYR E 27 5 6
HELIX 59 59 LYS E 28 ALA E 36 1 9
HELIX 60 60 ARG E 54 ILE E 58 5 5
HELIX 61 61 THR E 60 SER E 65 1 6
HELIX 62 62 SER E 65 ALA E 73 1 9
HELIX 63 63 GLY E 89 TYR E 100 1 12
HELIX 64 64 THR E 122 CYS E 132 1 11
HELIX 65 65 GLY E 158 MET E 166 1 9
HELIX 66 66 SER E 171 THR E 182 1 12
HELIX 67 67 PHE E 188 ALA E 193 1 6
HELIX 68 68 ARG E 202 VAL E 206 5 5
HELIX 69 69 PRO E 220 GLY E 232 1 13
HELIX 70 70 MET E 245 GLN E 250 1 6
HELIX 71 71 GLN E 250 SER E 262 1 13
SHEET 1 AA 6 LYS A 39 VAL A 43 0
SHEET 2 AA 6 HIS A 12 VAL A 16 1 O PHE A 13 N THR A 41
SHEET 3 AA 6 VAL A 81 SER A 87 1 O VAL A 82 N VAL A 14
SHEET 4 AA 6 ILE A 104 ALA A 112 1 N SER A 105 O VAL A 81
SHEET 5 AA 6 ARG A 208 CYS A 213 1 O ALA A 209 N PHE A 109
SHEET 6 AA 6 LYS A 235 ILE A 239 1 O LYS A 235 N TYR A 210
SHEET 1 AB 2 GLN A 141 TYR A 145 0
SHEET 2 AB 2 GLY A 152 ILE A 156 -1 O GLY A 152 N TYR A 145
SHEET 1 BA 6 LYS B 39 VAL B 43 0
SHEET 2 BA 6 HIS B 12 VAL B 16 1 O PHE B 13 N THR B 41
SHEET 3 BA 6 VAL B 81 SER B 87 1 O VAL B 82 N VAL B 14
SHEET 4 BA 6 ILE B 104 ALA B 112 1 N SER B 105 O VAL B 81
SHEET 5 BA 6 ARG B 208 CYS B 213 1 O ALA B 209 N PHE B 109
SHEET 6 BA 6 LYS B 235 ILE B 239 1 O LYS B 235 N TYR B 210
SHEET 1 BB 2 GLN B 141 TYR B 145 0
SHEET 2 BB 2 GLY B 152 ILE B 156 -1 O GLY B 152 N TYR B 145
SHEET 1 CA 6 LYS C 39 VAL C 43 0
SHEET 2 CA 6 HIS C 12 VAL C 16 1 O PHE C 13 N THR C 41
SHEET 3 CA 6 VAL C 81 HIS C 86 1 O VAL C 82 N VAL C 14
SHEET 4 CA 6 ILE C 104 MET C 110 1 N SER C 105 O VAL C 81
SHEET 5 CA 6 ARG C 208 CYS C 213 1 O ALA C 209 N PHE C 109
SHEET 6 CA 6 LYS C 235 ILE C 239 1 O LYS C 235 N TYR C 210
SHEET 1 CB 2 GLN C 141 TYR C 145 0
SHEET 2 CB 2 GLY C 152 ILE C 156 -1 O GLY C 152 N TYR C 145
SHEET 1 DA 6 LYS D 39 VAL D 43 0
SHEET 2 DA 6 HIS D 12 VAL D 16 1 O PHE D 13 N THR D 41
SHEET 3 DA 6 VAL D 81 SER D 87 1 O VAL D 82 N VAL D 14
SHEET 4 DA 6 ILE D 104 ALA D 112 1 N SER D 105 O VAL D 81
SHEET 5 DA 6 ARG D 208 CYS D 213 1 O ALA D 209 N PHE D 109
SHEET 6 DA 6 LYS D 235 ILE D 239 1 O LYS D 235 N TYR D 210
SHEET 1 DB 2 GLN D 141 TYR D 145 0
SHEET 2 DB 2 GLY D 152 ILE D 156 -1 O GLY D 152 N TYR D 145
SHEET 1 EA 6 LYS E 39 VAL E 43 0
SHEET 2 EA 6 HIS E 12 VAL E 16 1 O PHE E 13 N THR E 41
SHEET 3 EA 6 VAL E 81 HIS E 86 1 O VAL E 82 N VAL E 14
SHEET 4 EA 6 ILE E 104 MET E 110 1 N SER E 105 O VAL E 81
SHEET 5 EA 6 LYS E 207 CYS E 213 1 O LYS E 207 N ALA E 107
SHEET 6 EA 6 VAL E 236 ILE E 239 1 O LYS E 237 N PHE E 212
SHEET 1 EB 2 GLN E 141 GLY E 146 0
SHEET 2 EB 2 PRO E 151 ILE E 156 -1 O GLY E 152 N TYR E 145
CRYST1 170.250 46.810 184.170 90.00 104.89 90.00 C 1 2 1 20
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 0.005874 0.000000 0.001562 0.00000
SCALE2 0.000000 0.021363 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005618 0.00000
TER 2007 ASP A 263
TER 4017 ASP B 263
TER 6024 ASP C 263
TER 8031 ASP D 263
TER 10038 ASP E 263
MASTER 1326 0 0 71 40 0 0 610221 5 0 105
END |