HEADER OXIDOREDUCTASE 30-MAR-10 3MDT
TITLE VORICONAZOLE COMPLEX OF CYTOCHROME P450 46A1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CHOLESTEROL 24-HYDROXYLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 51-500;
COMPND 5 SYNONYM: CH24H, CYTOCHROME P450 46A1;
COMPND 6 EC: 1.14.13.98;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: CYP46A1, CYP46;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: DH5ALPHA;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PUC18
KEYWDS CYP46A1, P450 46A1, P450, VORICONAZOLE, MONOOXYGENASE, METABOLIC
KEYWDS 2 ENZYME, OXIDOREDUCTASE, HEME, CHOLESTEROL METABOLISM, ENDOPLASMIC
KEYWDS 3 RETICULUM, IRON, LIPID METABOLISM, MEMBRANE, METAL-BINDING,
KEYWDS 4 MICROSOME, NADP, STEROID METABOLISM, TRANSMEMBRANE
EXPDTA X-RAY DIFFRACTION
AUTHOR N.MAST,C.CHARVET,I.PIKULEVA,C.D.STOUT
REVDAT 6 06-SEP-23 3MDT 1 REMARK SEQADV LINK
REVDAT 5 10-SEP-14 3MDT 1 HETNAM HETSYN
REVDAT 4 13-JUL-11 3MDT 1 VERSN
REVDAT 3 20-OCT-10 3MDT 1 JRNL
REVDAT 2 13-OCT-10 3MDT 1 JRNL
REVDAT 1 28-JUL-10 3MDT 0
JRNL AUTH N.MAST,C.CHARVET,I.A.PIKULEVA,C.D.STOUT
JRNL TITL STRUCTURAL BASIS OF DRUG BINDING TO CYP46A1, AN ENZYME THAT
JRNL TITL 2 CONTROLS CHOLESTEROL TURNOVER IN THE BRAIN.
JRNL REF J.BIOL.CHEM. V. 285 31783 2010
JRNL REFN ISSN 0021-9258
JRNL PMID 20667828
JRNL DOI 10.1074/JBC.M110.143313
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH N.MAST,M.A.WHITE,I.BJORKHEM,E.F.JOHNSON,C.D.STOUT,
REMARK 1 AUTH 2 I.A.PIKULEVA
REMARK 1 TITL CRYSTAL STRUCTURES OF SUBSTRATE-BOUND AND SUBSTRATE-FREE
REMARK 1 TITL 2 CYTOCHROME P450 46A1, THE PRINCIPAL CHOLESTEROL HYDROXYLASE
REMARK 1 TITL 3 IN THE BRAIN.
REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 105 9546 2008
REMARK 1 REFN ISSN 0027-8424
REMARK 1 PMID 18621681
REMARK 1 DOI 10.1073/PNAS.0803717105
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0072
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 92.86
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 3 NUMBER OF REFLECTIONS : 43462
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) : 0.232
REMARK 3 R VALUE (WORKING SET) : 0.229
REMARK 3 FREE R VALUE : 0.287
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2325
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) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.36
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3251
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.88
REMARK 3 BIN R VALUE (WORKING SET) : 0.2280
REMARK 3 BIN FREE R VALUE SET COUNT : 150
REMARK 3 BIN FREE R VALUE : 0.3310
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6836
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 136
REMARK 3 SOLVENT ATOMS : 378
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : 48.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.10
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.05000
REMARK 3 B22 (A**2) : -1.05000
REMARK 3 B33 (A**2) : 2.10000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.082
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.059
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.197
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 16.563
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.889
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.840
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7966 ; 0.006 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 12204 ; 0.854 ; 1.961
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1688 ; 4.306 ; 7.500
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 332 ;37.032 ;23.193
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1284 ;15.494 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 68 ;10.488 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1060 ; 0.068 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 8836 ; 0.002 ; 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): 4226 ; 0.207 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6830 ; 0.380 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2896 ; 0.418 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2802 ; 0.716 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TWIN DETAILS
REMARK 3 NUMBER OF TWIN DOMAINS : 2
REMARK 3 TWIN DOMAIN : 1
REMARK 3 TWIN OPERATOR : H, K, L
REMARK 3 TWIN FRACTION : 0.500
REMARK 3 TWIN DOMAIN : 2
REMARK 3 TWIN OPERATOR : -H, K, -L
REMARK 3 TWIN FRACTION : 0.500
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 40
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 59 A 68
REMARK 3 ORIGIN FOR THE GROUP (A): 14.2047 -39.4256 -25.9672
REMARK 3 T TENSOR
REMARK 3 T11: 0.1615 T22: 0.1621
REMARK 3 T33: 0.1605 T12: -0.0008
REMARK 3 T13: -0.0010 T23: -0.0008
REMARK 3 L TENSOR
REMARK 3 L11: 0.9772 L22: 0.3763
REMARK 3 L33: 0.8636 L12: 0.2916
REMARK 3 L13: 0.0000 L23: -0.4998
REMARK 3 S TENSOR
REMARK 3 S11: -0.0062 S12: -0.0432 S13: 0.0147
REMARK 3 S21: 0.0462 S22: 0.0047 S23: 0.0071
REMARK 3 S31: -0.0080 S32: -0.0003 S33: 0.0016
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 69 A 82
REMARK 3 ORIGIN FOR THE GROUP (A): 9.7138 -45.5715 -26.2428
REMARK 3 T TENSOR
REMARK 3 T11: 0.2024 T22: 0.2017
REMARK 3 T33: 0.2025 T12: -0.0004
REMARK 3 T13: -0.0003 T23: 0.0000
REMARK 3 L TENSOR
REMARK 3 L11: 0.0475 L22: 0.0261
REMARK 3 L33: 0.0895 L12: -0.0302
REMARK 3 L13: -0.0516 L23: 0.0176
REMARK 3 S TENSOR
REMARK 3 S11: -0.0050 S12: -0.0664 S13: 0.0452
REMARK 3 S21: 0.0730 S22: 0.0033 S23: 0.0842
REMARK 3 S31: -0.0458 S32: -0.0773 S33: 0.0016
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 83 A 107
REMARK 3 ORIGIN FOR THE GROUP (A): 3.2369 -45.6458 -39.2289
REMARK 3 T TENSOR
REMARK 3 T11: 0.1919 T22: 0.1867
REMARK 3 T33: 0.1915 T12: -0.0008
REMARK 3 T13: 0.0001 T23: -0.0007
REMARK 3 L TENSOR
REMARK 3 L11: 0.4019 L22: 0.2484
REMARK 3 L33: 0.1734 L12: -0.0346
REMARK 3 L13: 0.2586 L23: -0.0638
REMARK 3 S TENSOR
REMARK 3 S11: 0.0012 S12: 0.0374 S13: -0.0090
REMARK 3 S21: -0.0103 S22: -0.0012 S23: 0.0912
REMARK 3 S31: -0.0015 S32: -0.1086 S33: 0.0001
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 108 A 120
REMARK 3 ORIGIN FOR THE GROUP (A): -9.7989 -34.0485 -25.4377
REMARK 3 T TENSOR
REMARK 3 T11: 0.2364 T22: 0.2347
REMARK 3 T33: 0.2352 T12: -0.0017
REMARK 3 T13: 0.0001 T23: 0.0013
REMARK 3 L TENSOR
REMARK 3 L11: 0.5552 L22: 0.2945
REMARK 3 L33: 0.0680 L12: -0.4044
REMARK 3 L13: -0.1943 L23: 0.1415
REMARK 3 S TENSOR
REMARK 3 S11: 0.0023 S12: -0.0220 S13: 0.0232
REMARK 3 S21: 0.0349 S22: -0.0125 S23: 0.0670
REMARK 3 S31: -0.0298 S32: -0.0675 S33: 0.0103
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 121 A 153
REMARK 3 ORIGIN FOR THE GROUP (A): -9.7652 -30.8804 -44.4868
REMARK 3 T TENSOR
REMARK 3 T11: 0.1948 T22: 0.2034
REMARK 3 T33: 0.2004 T12: 0.0036
REMARK 3 T13: 0.0005 T23: -0.0039
REMARK 3 L TENSOR
REMARK 3 L11: 0.3149 L22: 0.9259
REMARK 3 L33: 0.2636 L12: 0.1498
REMARK 3 L13: 0.0476 L23: -0.2155
REMARK 3 S TENSOR
REMARK 3 S11: -0.0080 S12: 0.0393 S13: 0.0333
REMARK 3 S21: -0.0593 S22: 0.0148 S23: 0.0021
REMARK 3 S31: -0.0154 S32: 0.0025 S33: -0.0069
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 154 A 194
REMARK 3 ORIGIN FOR THE GROUP (A): 4.3294 -7.9059 -35.0538
REMARK 3 T TENSOR
REMARK 3 T11: 0.1715 T22: 0.1698
REMARK 3 T33: 0.1735 T12: 0.0063
REMARK 3 T13: 0.0069 T23: -0.0007
REMARK 3 L TENSOR
REMARK 3 L11: 0.5085 L22: 0.6779
REMARK 3 L33: 0.5417 L12: 0.0155
REMARK 3 L13: -0.1214 L23: -0.1786
REMARK 3 S TENSOR
REMARK 3 S11: -0.0267 S12: 0.0373 S13: 0.0767
REMARK 3 S21: -0.0152 S22: 0.0116 S23: -0.0141
REMARK 3 S31: -0.0827 S32: 0.0601 S33: 0.0152
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 195 A 224
REMARK 3 ORIGIN FOR THE GROUP (A): -5.4977 -15.5029 -27.6747
REMARK 3 T TENSOR
REMARK 3 T11: 0.2104 T22: 0.2157
REMARK 3 T33: 0.2156 T12: 0.0012
REMARK 3 T13: 0.0009 T23: -0.0046
REMARK 3 L TENSOR
REMARK 3 L11: 0.3630 L22: 0.2804
REMARK 3 L33: 0.5099 L12: 0.2753
REMARK 3 L13: -0.1563 L23: 0.0596
REMARK 3 S TENSOR
REMARK 3 S11: 0.0126 S12: -0.0713 S13: -0.0791
REMARK 3 S21: 0.0447 S22: -0.0100 S23: -0.0116
REMARK 3 S31: 0.0825 S32: 0.0170 S33: -0.0025
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 225 A 251
REMARK 3 ORIGIN FOR THE GROUP (A): -8.9056 -25.2837 -17.4568
REMARK 3 T TENSOR
REMARK 3 T11: 0.2741 T22: 0.2746
REMARK 3 T33: 0.2767 T12: -0.0042
REMARK 3 T13: 0.0012 T23: 0.0003
REMARK 3 L TENSOR
REMARK 3 L11: 0.3595 L22: 0.3473
REMARK 3 L33: 0.0719 L12: -0.3534
REMARK 3 L13: 0.1608 L23: -0.1580
REMARK 3 S TENSOR
REMARK 3 S11: -0.0284 S12: -0.1502 S13: -0.0045
REMARK 3 S21: 0.1585 S22: 0.0251 S23: -0.0903
REMARK 3 S31: 0.0303 S32: 0.0583 S33: 0.0034
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 252 A 290
REMARK 3 ORIGIN FOR THE GROUP (A): -20.6260 -19.1225 -39.9573
REMARK 3 T TENSOR
REMARK 3 T11: 0.2572 T22: 0.2579
REMARK 3 T33: 0.2616 T12: 0.0006
REMARK 3 T13: 0.0004 T23: -0.0003
REMARK 3 L TENSOR
REMARK 3 L11: 0.4064 L22: 0.0172
REMARK 3 L33: 0.6644 L12: 0.0245
REMARK 3 L13: 0.0229 L23: 0.1033
REMARK 3 S TENSOR
REMARK 3 S11: -0.0042 S12: 0.0654 S13: -0.0047
REMARK 3 S21: -0.0677 S22: 0.0081 S23: 0.0615
REMARK 3 S31: 0.0101 S32: -0.0716 S33: -0.0040
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 291 A 315
REMARK 3 ORIGIN FOR THE GROUP (A): -2.3689 -22.4587 -34.3394
REMARK 3 T TENSOR
REMARK 3 T11: 0.1589 T22: 0.1251
REMARK 3 T33: 0.1259 T12: 0.0084
REMARK 3 T13: 0.0004 T23: 0.0001
REMARK 3 L TENSOR
REMARK 3 L11: 0.0958 L22: 1.0514
REMARK 3 L33: 1.2216 L12: -0.3175
REMARK 3 L13: 0.0005 L23: -0.0005
REMARK 3 S TENSOR
REMARK 3 S11: 0.0014 S12: 0.0038 S13: -0.0536
REMARK 3 S21: -0.0026 S22: -0.0019 S23: 0.1567
REMARK 3 S31: 0.0894 S32: -0.1619 S33: 0.0005
REMARK 3
REMARK 3 TLS GROUP : 11
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 316 A 335
REMARK 3 ORIGIN FOR THE GROUP (A): 21.0125 -14.1815 -42.2830
REMARK 3 T TENSOR
REMARK 3 T11: 0.1730 T22: 0.1704
REMARK 3 T33: 0.1775 T12: 0.0004
REMARK 3 T13: 0.0008 T23: -0.0050
REMARK 3 L TENSOR
REMARK 3 L11: 0.5515 L22: 0.5187
REMARK 3 L33: 0.4166 L12: 0.1864
REMARK 3 L13: -0.3271 L23: -0.0628
REMARK 3 S TENSOR
REMARK 3 S11: 0.0070 S12: 0.1011 S13: 0.0661
REMARK 3 S21: -0.1034 S22: -0.0209 S23: 0.0027
REMARK 3 S31: -0.0227 S32: 0.0373 S33: 0.0138
REMARK 3
REMARK 3 TLS GROUP : 12
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 336 A 349
REMARK 3 ORIGIN FOR THE GROUP (A): 7.6527 -9.3986 -52.6472
REMARK 3 T TENSOR
REMARK 3 T11: 0.2204 T22: 0.2205
REMARK 3 T33: 0.2184 T12: -0.0003
REMARK 3 T13: -0.0003 T23: 0.0014
REMARK 3 L TENSOR
REMARK 3 L11: 0.1065 L22: 0.4193
REMARK 3 L33: 0.1156 L12: -0.2113
REMARK 3 L13: -0.1110 L23: 0.2202
REMARK 3 S TENSOR
REMARK 3 S11: 0.0034 S12: -0.0817 S13: 0.1284
REMARK 3 S21: 0.0368 S22: -0.0340 S23: 0.1387
REMARK 3 S31: -0.1185 S32: -0.1026 S33: 0.0305
REMARK 3
REMARK 3 TLS GROUP : 13
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 350 A 372
REMARK 3 ORIGIN FOR THE GROUP (A): 11.8252 -27.7510 -39.8725
REMARK 3 T TENSOR
REMARK 3 T11: 0.1150 T22: 0.1191
REMARK 3 T33: 0.1146 T12: 0.0107
REMARK 3 T13: -0.0067 T23: -0.0101
REMARK 3 L TENSOR
REMARK 3 L11: 1.0224 L22: 0.6876
REMARK 3 L33: 0.8822 L12: -0.1008
REMARK 3 L13: 0.0577 L23: 0.1793
REMARK 3 S TENSOR
REMARK 3 S11: -0.0280 S12: 0.0762 S13: 0.0451
REMARK 3 S21: -0.0708 S22: 0.0476 S23: 0.0163
REMARK 3 S31: 0.0131 S32: -0.0460 S33: -0.0195
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 : A 373 A 390
REMARK 3 ORIGIN FOR THE GROUP (A): 2.8756 -54.6271 -34.9258
REMARK 3 T TENSOR
REMARK 3 T11: 0.2139 T22: 0.2142
REMARK 3 T33: 0.2107 T12: -0.0007
REMARK 3 T13: -0.0007 T23: 0.0017
REMARK 3 L TENSOR
REMARK 3 L11: 0.2358 L22: 0.5417
REMARK 3 L33: 0.1144 L12: -0.3574
REMARK 3 L13: -0.1643 L23: 0.2490
REMARK 3 S TENSOR
REMARK 3 S11: -0.0076 S12: 0.0867 S13: -0.1773
REMARK 3 S21: -0.0623 S22: -0.0062 S23: -0.0566
REMARK 3 S31: 0.1431 S32: 0.0855 S33: 0.0139
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 : A 391 A 402
REMARK 3 ORIGIN FOR THE GROUP (A): 13.0389 -38.6233 -34.6194
REMARK 3 T TENSOR
REMARK 3 T11: 0.1292 T22: 0.1210
REMARK 3 T33: 0.1174 T12: 0.0063
REMARK 3 T13: 0.0001 T23: 0.0048
REMARK 3 L TENSOR
REMARK 3 L11: 0.2720 L22: 1.8385
REMARK 3 L33: 1.6053 L12: -0.0068
REMARK 3 L13: 0.5259 L23: 0.5821
REMARK 3 S TENSOR
REMARK 3 S11: 0.0146 S12: -0.0159 S13: -0.0798
REMARK 3 S21: -0.0104 S22: -0.0229 S23: 0.0295
REMARK 3 S31: 0.0911 S32: -0.0418 S33: 0.0084
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 : A 403 A 425
REMARK 3 ORIGIN FOR THE GROUP (A): 20.5588 -32.4377 -43.8404
REMARK 3 T TENSOR
REMARK 3 T11: 0.1639 T22: 0.1665
REMARK 3 T33: 0.1659 T12: 0.0021
REMARK 3 T13: 0.0013 T23: -0.0006
REMARK 3 L TENSOR
REMARK 3 L11: 0.1190 L22: 0.3475
REMARK 3 L33: 0.0020 L12: 0.2034
REMARK 3 L13: 0.0152 L23: 0.0260
REMARK 3 S TENSOR
REMARK 3 S11: -0.0121 S12: 0.0500 S13: 0.0545
REMARK 3 S21: -0.0384 S22: 0.0060 S23: -0.0315
REMARK 3 S31: -0.0625 S32: 0.0664 S33: 0.0062
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 : A 426 A 435
REMARK 3 ORIGIN FOR THE GROUP (A): 5.0681 -35.1530 -42.5668
REMARK 3 T TENSOR
REMARK 3 T11: 0.1274 T22: 0.1234
REMARK 3 T33: 0.1232 T12: 0.0020
REMARK 3 T13: 0.0012 T23: -0.0021
REMARK 3 L TENSOR
REMARK 3 L11: 0.4402 L22: 0.6646
REMARK 3 L33: 0.5802 L12: 0.4563
REMARK 3 L13: 0.1216 L23: -0.1405
REMARK 3 S TENSOR
REMARK 3 S11: 0.0000 S12: 0.0936 S13: -0.1012
REMARK 3 S21: -0.0461 S22: 0.0019 S23: 0.1230
REMARK 3 S31: 0.1002 S32: -0.1126 S33: -0.0019
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 : A 436 A 454
REMARK 3 ORIGIN FOR THE GROUP (A): 4.5368 -19.0958 -44.1017
REMARK 3 T TENSOR
REMARK 3 T11: 0.1559 T22: 0.1590
REMARK 3 T33: 0.1559 T12: 0.0028
REMARK 3 T13: 0.0002 T23: -0.0003
REMARK 3 L TENSOR
REMARK 3 L11: 0.3174 L22: 0.3361
REMARK 3 L33: 0.2410 L12: 0.1028
REMARK 3 L13: -0.1363 L23: -0.2792
REMARK 3 S TENSOR
REMARK 3 S11: -0.0195 S12: 0.0213 S13: 0.0282
REMARK 3 S21: -0.0445 S22: 0.0182 S23: 0.0114
REMARK 3 S31: -0.0225 S32: 0.0095 S33: 0.0014
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 : A 455 A 474
REMARK 3 ORIGIN FOR THE GROUP (A): 15.4238 -15.1513 -29.5148
REMARK 3 T TENSOR
REMARK 3 T11: 0.2096 T22: 0.2096
REMARK 3 T33: 0.2096 T12: 0.0000
REMARK 3 T13: 0.0000 T23: 0.0000
REMARK 3 L TENSOR
REMARK 3 L11: 0.0000 L22: 0.0000
REMARK 3 L33: 0.0000 L12: 0.0000
REMARK 3 L13: 0.0000 L23: 0.0000
REMARK 3 S TENSOR
REMARK 3 S11: 0.0147 S12: -0.0438 S13: 0.0112
REMARK 3 S21: 0.1007 S22: -0.0463 S23: -0.1093
REMARK 3 S31: -0.0836 S32: 0.1028 S33: 0.0315
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 : A 475 A 489
REMARK 3 ORIGIN FOR THE GROUP (A): 13.8135 -13.3429 -29.0952
REMARK 3 T TENSOR
REMARK 3 T11: 0.1966 T22: 0.2012
REMARK 3 T33: 0.2005 T12: 0.0019
REMARK 3 T13: 0.0000 T23: -0.0004
REMARK 3 L TENSOR
REMARK 3 L11: 0.0969 L22: 0.8114
REMARK 3 L33: 0.0765 L12: 0.2804
REMARK 3 L13: -0.0861 L23: -0.2492
REMARK 3 S TENSOR
REMARK 3 S11: 0.0193 S12: 0.0722 S13: 0.1506
REMARK 3 S21: -0.0229 S22: -0.0183 S23: -0.0536
REMARK 3 S31: -0.1581 S32: 0.1246 S33: -0.0011
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 : B 59 B 71
REMARK 3 ORIGIN FOR THE GROUP (A): 19.3274 -45.3723 -68.4227
REMARK 3 T TENSOR
REMARK 3 T11: 0.1532 T22: 0.1496
REMARK 3 T33: 0.1454 T12: -0.0032
REMARK 3 T13: -0.0003 T23: 0.0024
REMARK 3 L TENSOR
REMARK 3 L11: 0.9972 L22: 1.3940
REMARK 3 L33: 1.4845 L12: 0.6275
REMARK 3 L13: 0.3933 L23: -0.0551
REMARK 3 S TENSOR
REMARK 3 S11: 0.0176 S12: 0.0421 S13: 0.0364
REMARK 3 S21: -0.0499 S22: -0.0177 S23: 0.0280
REMARK 3 S31: -0.0452 S32: -0.0428 S33: 0.0000
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 : B 72 B 107
REMARK 3 ORIGIN FOR THE GROUP (A): 15.0881 -56.6799 -59.3049
REMARK 3 T TENSOR
REMARK 3 T11: 0.2030 T22: 0.2101
REMARK 3 T33: 0.2123 T12: -0.0002
REMARK 3 T13: 0.0008 T23: 0.0008
REMARK 3 L TENSOR
REMARK 3 L11: 0.2384 L22: 0.4116
REMARK 3 L33: 0.3641 L12: 0.0282
REMARK 3 L13: 0.0827 L23: 0.0937
REMARK 3 S TENSOR
REMARK 3 S11: -0.0005 S12: 0.0612 S13: -0.1017
REMARK 3 S21: -0.0659 S22: -0.0021 S23: -0.0078
REMARK 3 S31: 0.1277 S32: 0.0271 S33: 0.0026
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 : B 108 B 117
REMARK 3 ORIGIN FOR THE GROUP (A): 24.7335 -69.4840 -68.5373
REMARK 3 T TENSOR
REMARK 3 T11: 0.2563 T22: 0.2575
REMARK 3 T33: 0.2567 T12: -0.0008
REMARK 3 T13: -0.0016 T23: 0.0009
REMARK 3 L TENSOR
REMARK 3 L11: 0.3459 L22: 0.5070
REMARK 3 L33: 0.4279 L12: -0.4188
REMARK 3 L13: -0.3847 L23: 0.4658
REMARK 3 S TENSOR
REMARK 3 S11: -0.0124 S12: -0.0386 S13: -0.0027
REMARK 3 S21: 0.0603 S22: 0.0128 S23: 0.0308
REMARK 3 S31: 0.0217 S32: -0.0162 S33: -0.0004
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 : B 118 B 164
REMARK 3 ORIGIN FOR THE GROUP (A): 35.3966 -68.1355 -51.3004
REMARK 3 T TENSOR
REMARK 3 T11: 0.2211 T22: 0.2149
REMARK 3 T33: 0.2220 T12: 0.0048
REMARK 3 T13: -0.0005 T23: 0.0004
REMARK 3 L TENSOR
REMARK 3 L11: 0.4105 L22: 0.1150
REMARK 3 L33: 0.0124 L12: 0.2172
REMARK 3 L13: -0.0713 L23: -0.0377
REMARK 3 S TENSOR
REMARK 3 S11: 0.0356 S12: -0.0798 S13: -0.0244
REMARK 3 S21: 0.0523 S22: -0.0276 S23: 0.0199
REMARK 3 S31: 0.0372 S32: -0.0329 S33: -0.0081
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 : B 165 B 182
REMARK 3 ORIGIN FOR THE GROUP (A): 56.4319 -50.5270 -65.0289
REMARK 3 T TENSOR
REMARK 3 T11: 0.2079 T22: 0.2075
REMARK 3 T33: 0.2081 T12: 0.0016
REMARK 3 T13: 0.0009 T23: -0.0003
REMARK 3 L TENSOR
REMARK 3 L11: 0.3192 L22: 0.2011
REMARK 3 L33: 0.0840 L12: 0.1976
REMARK 3 L13: 0.0620 L23: 0.1137
REMARK 3 S TENSOR
REMARK 3 S11: -0.0162 S12: 0.0809 S13: 0.1053
REMARK 3 S21: -0.0367 S22: 0.0062 S23: -0.0682
REMARK 3 S31: -0.0998 S32: 0.1029 S33: 0.0100
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 : B 183 B 198
REMARK 3 ORIGIN FOR THE GROUP (A): 47.1706 -64.1038 -58.5885
REMARK 3 T TENSOR
REMARK 3 T11: 0.1735 T22: 0.1799
REMARK 3 T33: 0.1764 T12: 0.0018
REMARK 3 T13: -0.0004 T23: -0.0059
REMARK 3 L TENSOR
REMARK 3 L11: 0.9389 L22: 0.5474
REMARK 3 L33: 0.9844 L12: -0.3198
REMARK 3 L13: 0.2421 L23: 0.1650
REMARK 3 S TENSOR
REMARK 3 S11: -0.0076 S12: -0.0858 S13: -0.1105
REMARK 3 S21: 0.0361 S22: -0.0039 S23: -0.0014
REMARK 3 S31: 0.1088 S32: -0.0293 S33: 0.0116
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 : B 199 B 228
REMARK 3 ORIGIN FOR THE GROUP (A): 42.2969 -65.6605 -69.2047
REMARK 3 T TENSOR
REMARK 3 T11: 0.2264 T22: 0.2202
REMARK 3 T33: 0.2226 T12: -0.0012
REMARK 3 T13: 0.0035 T23: 0.0018
REMARK 3 L TENSOR
REMARK 3 L11: 0.4550 L22: 0.1266
REMARK 3 L33: 0.3828 L12: 0.1097
REMARK 3 L13: 0.3022 L23: 0.0886
REMARK 3 S TENSOR
REMARK 3 S11: 0.0127 S12: 0.0571 S13: -0.0167
REMARK 3 S21: -0.0793 S22: 0.0058 S23: 0.0975
REMARK 3 S31: -0.0099 S32: -0.0822 S33: -0.0185
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 : B 236 B 246
REMARK 3 ORIGIN FOR THE GROUP (A): 36.2659 -70.8493 -80.7462
REMARK 3 T TENSOR
REMARK 3 T11: 0.3156 T22: 0.3156
REMARK 3 T33: 0.3156 T12: 0.0000
REMARK 3 T13: 0.0000 T23: 0.0000
REMARK 3 L TENSOR
REMARK 3 L11: 0.0000 L22: 0.0000
REMARK 3 L33: 0.0000 L12: 0.0000
REMARK 3 L13: 0.0000 L23: 0.0000
REMARK 3 S TENSOR
REMARK 3 S11: 0.0042 S12: 0.1594 S13: 0.0807
REMARK 3 S21: -0.1516 S22: -0.0101 S23: 0.0543
REMARK 3 S31: -0.0602 S32: -0.0302 S33: 0.0058
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 : B 247 B 290
REMARK 3 ORIGIN FOR THE GROUP (A): 41.3051 -80.5146 -55.7170
REMARK 3 T TENSOR
REMARK 3 T11: 0.2928 T22: 0.2923
REMARK 3 T33: 0.2951 T12: 0.0015
REMARK 3 T13: 0.0010 T23: -0.0010
REMARK 3 L TENSOR
REMARK 3 L11: 0.1557 L22: 0.2319
REMARK 3 L33: 0.2848 L12: 0.0769
REMARK 3 L13: -0.0211 L23: -0.0229
REMARK 3 S TENSOR
REMARK 3 S11: 0.0033 S12: -0.0935 S13: -0.0266
REMARK 3 S21: 0.0911 S22: -0.0011 S23: -0.0320
REMARK 3 S31: 0.0241 S32: 0.0226 S33: -0.0022
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 : B 291 B 299
REMARK 3 ORIGIN FOR THE GROUP (A): 35.0519 -74.2797 -59.1359
REMARK 3 T TENSOR
REMARK 3 T11: 0.2067 T22: 0.2079
REMARK 3 T33: 0.2087 T12: 0.0004
REMARK 3 T13: -0.0005 T23: 0.0007
REMARK 3 L TENSOR
REMARK 3 L11: 0.0093 L22: 0.1450
REMARK 3 L33: 0.5339 L12: -0.0367
REMARK 3 L13: -0.0704 L23: 0.2782
REMARK 3 S TENSOR
REMARK 3 S11: -0.0035 S12: 0.0385 S13: -0.3141
REMARK 3 S21: 0.0107 S22: -0.0092 S23: 0.1061
REMARK 3 S31: 0.3193 S32: -0.1344 S33: 0.0126
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 : B 300 B 315
REMARK 3 ORIGIN FOR THE GROUP (A): 40.1255 -56.7006 -60.6023
REMARK 3 T TENSOR
REMARK 3 T11: 0.1034 T22: 0.1273
REMARK 3 T33: 0.1039 T12: 0.0024
REMARK 3 T13: 0.0010 T23: 0.0015
REMARK 3 L TENSOR
REMARK 3 L11: 1.6817 L22: 0.2804
REMARK 3 L33: 1.8843 L12: -0.6821
REMARK 3 L13: 0.0319 L23: 0.0704
REMARK 3 S TENSOR
REMARK 3 S11: -0.0099 S12: 0.0266 S13: -0.0615
REMARK 3 S21: -0.0294 S22: 0.0116 S23: -0.0222
REMARK 3 S31: 0.0504 S32: 0.0143 S33: -0.0018
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 : B 316 B 341
REMARK 3 ORIGIN FOR THE GROUP (A): 49.0706 -42.2701 -51.0304
REMARK 3 T TENSOR
REMARK 3 T11: 0.1936 T22: 0.1973
REMARK 3 T33: 0.1988 T12: -0.0040
REMARK 3 T13: 0.0051 T23: -0.0023
REMARK 3 L TENSOR
REMARK 3 L11: 0.3012 L22: 0.5199
REMARK 3 L33: 0.3960 L12: 0.1000
REMARK 3 L13: -0.1533 L23: 0.1755
REMARK 3 S TENSOR
REMARK 3 S11: -0.0117 S12: -0.1289 S13: -0.0782
REMARK 3 S21: 0.1579 S22: -0.0058 S23: -0.1582
REMARK 3 S31: 0.0919 S32: 0.1428 S33: 0.0175
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 : B 342 B 349
REMARK 3 ORIGIN FOR THE GROUP (A): 47.4148 -52.9312 -40.3970
REMARK 3 T TENSOR
REMARK 3 T11: 0.2152 T22: 0.2178
REMARK 3 T33: 0.2155 T12: 0.0000
REMARK 3 T13: 0.0006 T23: 0.0025
REMARK 3 L TENSOR
REMARK 3 L11: 0.1014 L22: 1.4135
REMARK 3 L33: 0.6443 L12: 0.1069
REMARK 3 L13: 0.1848 L23: 0.8273
REMARK 3 S TENSOR
REMARK 3 S11: 0.0095 S12: 0.0654 S13: -0.2747
REMARK 3 S21: -0.0480 S22: -0.0027 S23: -0.1332
REMARK 3 S31: 0.2899 S32: 0.1621 S33: -0.0069
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 : B 350 B 372
REMARK 3 ORIGIN FOR THE GROUP (A): 33.1220 -48.8452 -54.9127
REMARK 3 T TENSOR
REMARK 3 T11: 0.1189 T22: 0.1147
REMARK 3 T33: 0.1119 T12: 0.0097
REMARK 3 T13: 0.0107 T23: 0.0067
REMARK 3 L TENSOR
REMARK 3 L11: 0.8233 L22: 0.8988
REMARK 3 L33: 0.9695 L12: -0.1451
REMARK 3 L13: 0.0247 L23: -0.0032
REMARK 3 S TENSOR
REMARK 3 S11: 0.0467 S12: -0.0740 S13: -0.0061
REMARK 3 S21: 0.0861 S22: -0.0308 S23: -0.0639
REMARK 3 S31: 0.0271 S32: 0.0070 S33: -0.0160
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 : B 373 B 389
REMARK 3 ORIGIN FOR THE GROUP (A): 5.7661 -57.7306 -58.5830
REMARK 3 T TENSOR
REMARK 3 T11: 0.2177 T22: 0.2186
REMARK 3 T33: 0.2145 T12: -0.0016
REMARK 3 T13: -0.0023 T23: 0.0009
REMARK 3 L TENSOR
REMARK 3 L11: 0.6200 L22: 0.6499
REMARK 3 L33: 0.1685 L12: -0.6348
REMARK 3 L13: -0.3232 L23: 0.3309
REMARK 3 S TENSOR
REMARK 3 S11: -0.0262 S12: -0.1299 S13: 0.0487
REMARK 3 S21: 0.1894 S22: 0.0221 S23: 0.1473
REMARK 3 S31: -0.0745 S32: -0.1116 S33: 0.0041
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 : B 390 B 402
REMARK 3 ORIGIN FOR THE GROUP (A): 21.5900 -48.6445 -60.3327
REMARK 3 T TENSOR
REMARK 3 T11: 0.1141 T22: 0.1247
REMARK 3 T33: 0.1109 T12: 0.0096
REMARK 3 T13: -0.0036 T23: 0.0019
REMARK 3 L TENSOR
REMARK 3 L11: 1.4285 L22: 0.5430
REMARK 3 L33: 1.6191 L12: -0.2965
REMARK 3 L13: -0.3443 L23: -0.1959
REMARK 3 S TENSOR
REMARK 3 S11: -0.0088 S12: -0.0045 S13: 0.0227
REMARK 3 S21: -0.0264 S22: 0.0069 S23: 0.0977
REMARK 3 S31: 0.0169 S32: -0.0727 S33: 0.0018
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 : B 403 B 424
REMARK 3 ORIGIN FOR THE GROUP (A): 28.9604 -39.5836 -51.1876
REMARK 3 T TENSOR
REMARK 3 T11: 0.1792 T22: 0.1735
REMARK 3 T33: 0.1779 T12: 0.0022
REMARK 3 T13: 0.0005 T23: -0.0018
REMARK 3 L TENSOR
REMARK 3 L11: 0.7499 L22: 0.2294
REMARK 3 L33: 0.0385 L12: 0.1922
REMARK 3 L13: -0.0096 L23: 0.0807
REMARK 3 S TENSOR
REMARK 3 S11: 0.0006 S12: -0.0288 S13: 0.0042
REMARK 3 S21: 0.0344 S22: -0.0047 S23: -0.0227
REMARK 3 S31: -0.0223 S32: 0.0179 S33: 0.0040
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 : B 425 B 454
REMARK 3 ORIGIN FOR THE GROUP (A): 34.9563 -55.7367 -51.0367
REMARK 3 T TENSOR
REMARK 3 T11: 0.1612 T22: 0.1546
REMARK 3 T33: 0.1488 T12: 0.0012
REMARK 3 T13: 0.0008 T23: -0.0006
REMARK 3 L TENSOR
REMARK 3 L11: 0.2682 L22: 0.4176
REMARK 3 L33: 0.2997 L12: -0.0435
REMARK 3 L13: 0.1265 L23: 0.0070
REMARK 3 S TENSOR
REMARK 3 S11: 0.0011 S12: -0.0264 S13: -0.0331
REMARK 3 S21: 0.0130 S22: -0.0008 S23: -0.0219
REMARK 3 S31: 0.0079 S32: 0.0191 S33: -0.0002
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 : B 455 B 473
REMARK 3 ORIGIN FOR THE GROUP (A): 46.0629 -45.3401 -65.4450
REMARK 3 T TENSOR
REMARK 3 T11: 0.2068 T22: 0.2058
REMARK 3 T33: 0.2079 T12: 0.0013
REMARK 3 T13: 0.0007 T23: -0.0003
REMARK 3 L TENSOR
REMARK 3 L11: 0.0607 L22: 0.0153
REMARK 3 L33: 0.1742 L12: 0.0258
REMARK 3 L13: 0.0964 L23: 0.0314
REMARK 3 S TENSOR
REMARK 3 S11: -0.0177 S12: 0.0530 S13: 0.0376
REMARK 3 S21: -0.0220 S22: 0.0062 S23: -0.0086
REMARK 3 S31: -0.0419 S32: 0.0480 S33: 0.0116
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 : B 474 B 489
REMARK 3 ORIGIN FOR THE GROUP (A): 46.7335 -47.8859 -65.9465
REMARK 3 T TENSOR
REMARK 3 T11: 0.1993 T22: 0.1903
REMARK 3 T33: 0.1968 T12: 0.0041
REMARK 3 T13: 0.0013 T23: 0.0002
REMARK 3 L TENSOR
REMARK 3 L11: 0.4669 L22: 0.0665
REMARK 3 L33: 0.2330 L12: 0.0083
REMARK 3 L13: -0.0362 L23: -0.0713
REMARK 3 S TENSOR
REMARK 3 S11: -0.0149 S12: -0.0012 S13: 0.0321
REMARK 3 S21: 0.0438 S22: 0.0178 S23: -0.1102
REMARK 3 S31: -0.0881 S32: 0.1108 S33: -0.0029
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH 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:
REMARK 3 HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
REMARK 3 U VALUES: RESIDUAL ONLY
REMARK 3 TWO TWIN DOMAINS:
REMARK 3 H,K,L TWIN FRACTION 0.500
REMARK 3 -H,K,-L TWIN FRACTION 0.500
REMARK 3 20 TLS GROUPS REFINED PER CHAIN
REMARK 4
REMARK 4 3MDT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-APR-10.
REMARK 100 THE DEPOSITION ID IS D_1000058420.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 31-JUL-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL7-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : SIDE SCATTERING I-BEAM BENT
REMARK 200 SINGLE CRYSTAL, ASYMMETRIC CUT
REMARK 200 4.9650 DEG
REMARK 200 OPTICS : RH COATED FLAT MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.15
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 45803
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 92.860
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : 0.06500
REMARK 200 R SYM (I) : 0.06500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.42
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.50
REMARK 200 R MERGE FOR SHELL (I) : 0.39200
REMARK 200 R SYM FOR SHELL (I) : 0.39200
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.900
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 2Q9F
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.46
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.59
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 8% PEG 8000, 20% GLYCEROL, 50 MM KPI,
REMARK 280 0.03% UNDECYLMALTOSIDE, PH 5.8, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 41
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 3555 -Y,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X,Z+3/4
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X,-Y,Z
REMARK 290 7555 -Y+1/2,X,Z+3/4
REMARK 290 8555 Y,-X+1/2,Z+1/4
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 60.80000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 60.80000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 71.91500
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 60.80000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 35.95750
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 60.80000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 107.87250
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 60.80000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 60.80000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 71.91500
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 -1.000000 0.000000 60.80000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 107.87250
REMARK 290 SMTRY1 8 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 60.80000
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 35.95750
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 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 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 49
REMARK 465 ALA A 50
REMARK 465 LYS A 51
REMARK 465 LYS A 52
REMARK 465 ASP A 53
REMARK 465 GLU A 54
REMARK 465 VAL A 55
REMARK 465 GLY A 56
REMARK 465 GLY A 57
REMARK 465 ARG A 58
REMARK 465 LEU A 229
REMARK 465 ALA A 230
REMARK 465 LYS A 231
REMARK 465 PHE A 232
REMARK 465 LEU A 233
REMARK 465 PRO A 234
REMARK 465 GLY A 235
REMARK 465 GLY A 490
REMARK 465 TRP A 491
REMARK 465 GLN A 492
REMARK 465 PRO A 493
REMARK 465 ALA A 494
REMARK 465 PRO A 495
REMARK 465 PRO A 496
REMARK 465 PRO A 497
REMARK 465 PRO A 498
REMARK 465 PRO A 499
REMARK 465 CYS A 500
REMARK 465 HIS A 501
REMARK 465 HIS A 502
REMARK 465 HIS A 503
REMARK 465 HIS A 504
REMARK 465 MET B 49
REMARK 465 ALA B 50
REMARK 465 LYS B 51
REMARK 465 LYS B 52
REMARK 465 ASP B 53
REMARK 465 GLU B 54
REMARK 465 VAL B 55
REMARK 465 GLY B 56
REMARK 465 GLY B 57
REMARK 465 ARG B 58
REMARK 465 LEU B 229
REMARK 465 ALA B 230
REMARK 465 LYS B 231
REMARK 465 PHE B 232
REMARK 465 LEU B 233
REMARK 465 PRO B 234
REMARK 465 GLY B 235
REMARK 465 GLY B 490
REMARK 465 TRP B 491
REMARK 465 GLN B 492
REMARK 465 PRO B 493
REMARK 465 ALA B 494
REMARK 465 PRO B 495
REMARK 465 PRO B 496
REMARK 465 PRO B 497
REMARK 465 PRO B 498
REMARK 465 PRO B 499
REMARK 465 CYS B 500
REMARK 465 HIS B 501
REMARK 465 HIS B 502
REMARK 465 HIS B 503
REMARK 465 HIS B 504
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 NH2 ARG A 119 OD2 ASP A 294 1.47
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 119 CD - NE - CZ ANGL. DEV. = 28.2 DEGREES
REMARK 500 ARG A 119 NE - CZ - NH1 ANGL. DEV. = 5.2 DEGREES
REMARK 500 ARG A 119 O - C - N ANGL. DEV. = -13.3 DEGREES
REMARK 500 LEU A 120 O - C - N ANGL. DEV. = -15.2 DEGREES
REMARK 500 PHE A 121 O - C - N ANGL. DEV. = -13.2 DEGREES
REMARK 500 ASN B 103 O - C - N ANGL. DEV. = 9.9 DEGREES
REMARK 500 ASP B 105 CB - CG - OD1 ANGL. DEV. = 7.0 DEGREES
REMARK 500 PHE B 121 C - N - CA ANGL. DEV. = 15.6 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 120 -87.82 -122.08
REMARK 500 GLN A 175 -16.68 -153.12
REMARK 500 ASN A 227 67.74 -107.57
REMARK 500 HIS A 304 -40.81 -135.49
REMARK 500 SER A 431 -171.85 63.92
REMARK 500 GLN A 473 -138.09 -98.84
REMARK 500 PRO A 481 23.77 -71.73
REMARK 500 LEU B 120 -100.01 -115.69
REMARK 500 GLN B 123 40.89 -105.35
REMARK 500 ASP B 274 -162.49 -116.16
REMARK 500 HIS B 304 -39.98 -136.59
REMARK 500 GLU B 334 -63.86 -94.75
REMARK 500 SER B 431 179.55 62.51
REMARK 500 GLN B 473 -128.27 -101.43
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 PHE A 121 10.67
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM A 505 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 437 SG
REMARK 620 2 HEM A 505 NA 99.2
REMARK 620 3 HEM A 505 NB 84.5 84.1
REMARK 620 4 HEM A 505 NC 91.9 163.4 84.7
REMARK 620 5 HEM A 505 ND 99.0 96.7 176.1 93.6
REMARK 620 6 VOR A 506 N8 162.4 71.8 79.5 94.1 97.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM B 505 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 437 SG
REMARK 620 2 HEM B 505 NA 98.4
REMARK 620 3 HEM B 505 NB 86.0 85.5
REMARK 620 4 HEM B 505 NC 93.6 164.3 85.2
REMARK 620 5 HEM B 505 ND 96.3 95.2 177.5 93.6
REMARK 620 6 VOR B 506 N8 167.5 77.1 82.0 89.0 95.8
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE VOR A 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE VOR B 506
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2Q9F RELATED DB: PDB
REMARK 900 CHOLESTEROL 3-SULFATE COMPLEX OF CYTOCHROME P450 46A1
REMARK 900 RELATED ID: 2Q9G RELATED DB: PDB
REMARK 900 APO FORM OF CYTOCHROME P450 46A1
REMARK 900 RELATED ID: 3MDM RELATED DB: PDB
REMARK 900 RELATED ID: 3MDR RELATED DB: PDB
REMARK 900 RELATED ID: 3MDV RELATED DB: PDB
DBREF 3MDT A 51 500 UNP Q9Y6A2 CP46A_HUMAN 51 500
DBREF 3MDT B 51 500 UNP Q9Y6A2 CP46A_HUMAN 51 500
SEQADV 3MDT MET A 49 UNP Q9Y6A2 EXPRESSION TAG
SEQADV 3MDT ALA A 50 UNP Q9Y6A2 EXPRESSION TAG
SEQADV 3MDT HIS A 501 UNP Q9Y6A2 EXPRESSION TAG
SEQADV 3MDT HIS A 502 UNP Q9Y6A2 EXPRESSION TAG
SEQADV 3MDT HIS A 503 UNP Q9Y6A2 EXPRESSION TAG
SEQADV 3MDT HIS A 504 UNP Q9Y6A2 EXPRESSION TAG
SEQADV 3MDT MET B 49 UNP Q9Y6A2 EXPRESSION TAG
SEQADV 3MDT ALA B 50 UNP Q9Y6A2 EXPRESSION TAG
SEQADV 3MDT HIS B 501 UNP Q9Y6A2 EXPRESSION TAG
SEQADV 3MDT HIS B 502 UNP Q9Y6A2 EXPRESSION TAG
SEQADV 3MDT HIS B 503 UNP Q9Y6A2 EXPRESSION TAG
SEQADV 3MDT HIS B 504 UNP Q9Y6A2 EXPRESSION TAG
SEQRES 1 A 456 MET ALA LYS LYS ASP GLU VAL GLY GLY ARG VAL LEU GLN
SEQRES 2 A 456 ASP VAL PHE LEU ASP TRP ALA LYS LYS TYR GLY PRO VAL
SEQRES 3 A 456 VAL ARG VAL ASN VAL PHE HIS LYS THR SER VAL ILE VAL
SEQRES 4 A 456 THR SER PRO GLU SER VAL LYS LYS PHE LEU MET SER THR
SEQRES 5 A 456 LYS TYR ASN LYS ASP SER LYS MET TYR ARG ALA LEU GLN
SEQRES 6 A 456 THR VAL PHE GLY GLU ARG LEU PHE GLY GLN GLY LEU VAL
SEQRES 7 A 456 SER GLU CYS ASN TYR GLU ARG TRP HIS LYS GLN ARG ARG
SEQRES 8 A 456 VAL ILE ASP LEU ALA PHE SER ARG SER SER LEU VAL SER
SEQRES 9 A 456 LEU MET GLU THR PHE ASN GLU LYS ALA GLU GLN LEU VAL
SEQRES 10 A 456 GLU ILE LEU GLU ALA LYS ALA ASP GLY GLN THR PRO VAL
SEQRES 11 A 456 SER MET GLN ASP MET LEU THR TYR THR ALA MET ASP ILE
SEQRES 12 A 456 LEU ALA LYS ALA ALA PHE GLY MET GLU THR SER MET LEU
SEQRES 13 A 456 LEU GLY ALA GLN LYS PRO LEU SER GLN ALA VAL LYS LEU
SEQRES 14 A 456 MET LEU GLU GLY ILE THR ALA SER ARG ASN THR LEU ALA
SEQRES 15 A 456 LYS PHE LEU PRO GLY LYS ARG LYS GLN LEU ARG GLU VAL
SEQRES 16 A 456 ARG GLU SER ILE ARG PHE LEU ARG GLN VAL GLY ARG ASP
SEQRES 17 A 456 TRP VAL GLN ARG ARG ARG GLU ALA LEU LYS ARG GLY GLU
SEQRES 18 A 456 GLU VAL PRO ALA ASP ILE LEU THR GLN ILE LEU LYS ALA
SEQRES 19 A 456 GLU GLU GLY ALA GLN ASP ASP GLU GLY LEU LEU ASP ASN
SEQRES 20 A 456 PHE VAL THR PHE PHE ILE ALA GLY HIS GLU THR SER ALA
SEQRES 21 A 456 ASN HIS LEU ALA PHE THR VAL MET GLU LEU SER ARG GLN
SEQRES 22 A 456 PRO GLU ILE VAL ALA ARG LEU GLN ALA GLU VAL ASP GLU
SEQRES 23 A 456 VAL ILE GLY SER LYS ARG TYR LEU ASP PHE GLU ASP LEU
SEQRES 24 A 456 GLY ARG LEU GLN TYR LEU SER GLN VAL LEU LYS GLU SER
SEQRES 25 A 456 LEU ARG LEU TYR PRO PRO ALA TRP GLY THR PHE ARG LEU
SEQRES 26 A 456 LEU GLU GLU GLU THR LEU ILE ASP GLY VAL ARG VAL PRO
SEQRES 27 A 456 GLY ASN THR PRO LEU LEU PHE SER THR TYR VAL MET GLY
SEQRES 28 A 456 ARG MET ASP THR TYR PHE GLU ASP PRO LEU THR PHE ASN
SEQRES 29 A 456 PRO ASP ARG PHE GLY PRO GLY ALA PRO LYS PRO ARG PHE
SEQRES 30 A 456 THR TYR PHE PRO PHE SER LEU GLY HIS ARG SER CYS ILE
SEQRES 31 A 456 GLY GLN GLN PHE ALA GLN MET GLU VAL LYS VAL VAL MET
SEQRES 32 A 456 ALA LYS LEU LEU GLN ARG LEU GLU PHE ARG LEU VAL PRO
SEQRES 33 A 456 GLY GLN ARG PHE GLY LEU GLN GLU GLN ALA THR LEU LYS
SEQRES 34 A 456 PRO LEU ASP PRO VAL LEU CYS THR LEU ARG PRO ARG GLY
SEQRES 35 A 456 TRP GLN PRO ALA PRO PRO PRO PRO PRO CYS HIS HIS HIS
SEQRES 36 A 456 HIS
SEQRES 1 B 456 MET ALA LYS LYS ASP GLU VAL GLY GLY ARG VAL LEU GLN
SEQRES 2 B 456 ASP VAL PHE LEU ASP TRP ALA LYS LYS TYR GLY PRO VAL
SEQRES 3 B 456 VAL ARG VAL ASN VAL PHE HIS LYS THR SER VAL ILE VAL
SEQRES 4 B 456 THR SER PRO GLU SER VAL LYS LYS PHE LEU MET SER THR
SEQRES 5 B 456 LYS TYR ASN LYS ASP SER LYS MET TYR ARG ALA LEU GLN
SEQRES 6 B 456 THR VAL PHE GLY GLU ARG LEU PHE GLY GLN GLY LEU VAL
SEQRES 7 B 456 SER GLU CYS ASN TYR GLU ARG TRP HIS LYS GLN ARG ARG
SEQRES 8 B 456 VAL ILE ASP LEU ALA PHE SER ARG SER SER LEU VAL SER
SEQRES 9 B 456 LEU MET GLU THR PHE ASN GLU LYS ALA GLU GLN LEU VAL
SEQRES 10 B 456 GLU ILE LEU GLU ALA LYS ALA ASP GLY GLN THR PRO VAL
SEQRES 11 B 456 SER MET GLN ASP MET LEU THR TYR THR ALA MET ASP ILE
SEQRES 12 B 456 LEU ALA LYS ALA ALA PHE GLY MET GLU THR SER MET LEU
SEQRES 13 B 456 LEU GLY ALA GLN LYS PRO LEU SER GLN ALA VAL LYS LEU
SEQRES 14 B 456 MET LEU GLU GLY ILE THR ALA SER ARG ASN THR LEU ALA
SEQRES 15 B 456 LYS PHE LEU PRO GLY LYS ARG LYS GLN LEU ARG GLU VAL
SEQRES 16 B 456 ARG GLU SER ILE ARG PHE LEU ARG GLN VAL GLY ARG ASP
SEQRES 17 B 456 TRP VAL GLN ARG ARG ARG GLU ALA LEU LYS ARG GLY GLU
SEQRES 18 B 456 GLU VAL PRO ALA ASP ILE LEU THR GLN ILE LEU LYS ALA
SEQRES 19 B 456 GLU GLU GLY ALA GLN ASP ASP GLU GLY LEU LEU ASP ASN
SEQRES 20 B 456 PHE VAL THR PHE PHE ILE ALA GLY HIS GLU THR SER ALA
SEQRES 21 B 456 ASN HIS LEU ALA PHE THR VAL MET GLU LEU SER ARG GLN
SEQRES 22 B 456 PRO GLU ILE VAL ALA ARG LEU GLN ALA GLU VAL ASP GLU
SEQRES 23 B 456 VAL ILE GLY SER LYS ARG TYR LEU ASP PHE GLU ASP LEU
SEQRES 24 B 456 GLY ARG LEU GLN TYR LEU SER GLN VAL LEU LYS GLU SER
SEQRES 25 B 456 LEU ARG LEU TYR PRO PRO ALA TRP GLY THR PHE ARG LEU
SEQRES 26 B 456 LEU GLU GLU GLU THR LEU ILE ASP GLY VAL ARG VAL PRO
SEQRES 27 B 456 GLY ASN THR PRO LEU LEU PHE SER THR TYR VAL MET GLY
SEQRES 28 B 456 ARG MET ASP THR TYR PHE GLU ASP PRO LEU THR PHE ASN
SEQRES 29 B 456 PRO ASP ARG PHE GLY PRO GLY ALA PRO LYS PRO ARG PHE
SEQRES 30 B 456 THR TYR PHE PRO PHE SER LEU GLY HIS ARG SER CYS ILE
SEQRES 31 B 456 GLY GLN GLN PHE ALA GLN MET GLU VAL LYS VAL VAL MET
SEQRES 32 B 456 ALA LYS LEU LEU GLN ARG LEU GLU PHE ARG LEU VAL PRO
SEQRES 33 B 456 GLY GLN ARG PHE GLY LEU GLN GLU GLN ALA THR LEU LYS
SEQRES 34 B 456 PRO LEU ASP PRO VAL LEU CYS THR LEU ARG PRO ARG GLY
SEQRES 35 B 456 TRP GLN PRO ALA PRO PRO PRO PRO PRO CYS HIS HIS HIS
SEQRES 36 B 456 HIS
HET HEM A 505 43
HET VOR A 506 25
HET HEM B 505 43
HET VOR B 506 25
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM VOR VORICONAZOLE
HETSYN HEM HEME
HETSYN VOR (2R,3S)-2-(2,4-DIFLUOROPHENYL)-3-(5-FLUOROPYRIMIDIN-4-
HETSYN 2 VOR YL)-1-(1H-1,2,4-TRIAZOL-1-YL)BUTAN-2-OL
FORMUL 3 HEM 2(C34 H32 FE N4 O4)
FORMUL 4 VOR 2(C16 H14 F3 N5 O)
FORMUL 7 HOH *378(H2 O)
HELIX 1 1 VAL A 59 GLY A 72 1 14
HELIX 2 2 SER A 89 MET A 98 1 10
HELIX 3 3 ASP A 105 GLN A 113 1 9
HELIX 4 4 ASN A 130 ASP A 142 1 13
HELIX 5 5 LEU A 143 PHE A 145 5 3
HELIX 6 6 SER A 146 SER A 152 1 7
HELIX 7 7 LEU A 153 ALA A 170 1 18
HELIX 8 8 MET A 180 GLY A 198 1 19
HELIX 9 9 SER A 202 GLY A 206 5 5
HELIX 10 10 GLN A 208 ASN A 227 1 20
HELIX 11 11 ARG A 237 ARG A 267 1 31
HELIX 12 12 ASP A 274 ALA A 282 1 9
HELIX 13 13 ASP A 289 GLY A 303 1 15
HELIX 14 14 HIS A 304 LEU A 318 1 15
HELIX 15 15 GLN A 321 ILE A 336 1 16
HELIX 16 16 ASP A 343 GLY A 348 1 6
HELIX 17 17 LEU A 350 TYR A 364 1 15
HELIX 18 18 THR A 395 ARG A 400 1 6
HELIX 19 19 ASN A 412 GLY A 417 5 6
HELIX 20 20 LEU A 432 SER A 436 5 5
HELIX 21 21 GLY A 439 ARG A 457 1 19
HELIX 22 22 VAL B 59 GLY B 72 1 14
HELIX 23 23 SER B 89 MET B 98 1 10
HELIX 24 24 TYR B 109 GLN B 113 1 5
HELIX 25 25 ASN B 130 ASP B 142 1 13
HELIX 26 26 LEU B 143 PHE B 145 5 3
HELIX 27 27 SER B 146 SER B 152 1 7
HELIX 28 28 LEU B 153 LYS B 171 1 19
HELIX 29 29 MET B 180 GLY B 198 1 19
HELIX 30 30 GLN B 208 ARG B 226 1 19
HELIX 31 31 LYS B 236 ARG B 267 1 32
HELIX 32 32 ASP B 274 GLU B 283 1 10
HELIX 33 33 ASP B 289 GLY B 303 1 15
HELIX 34 34 HIS B 304 SER B 319 1 16
HELIX 35 35 GLN B 321 ILE B 336 1 16
HELIX 36 36 ASP B 343 ARG B 349 1 7
HELIX 37 37 LEU B 350 TYR B 364 1 15
HELIX 38 38 THR B 395 ARG B 400 1 6
HELIX 39 39 ASN B 412 GLY B 417 5 6
HELIX 40 40 GLY B 439 ARG B 457 1 19
SHEET 1 A 4 VAL A 74 VAL A 79 0
SHEET 2 A 4 LYS A 82 VAL A 87 -1 O SER A 84 N VAL A 77
SHEET 3 A 4 THR A 389 SER A 394 1 O LEU A 392 N VAL A 85
SHEET 4 A 4 GLY A 369 LEU A 374 -1 N ARG A 372 O LEU A 391
SHEET 1 B 2 THR A 114 VAL A 115 0
SHEET 2 B 2 GLU A 118 ARG A 119 -1 O GLU A 118 N VAL A 115
SHEET 1 C 3 VAL A 178 SER A 179 0
SHEET 2 C 3 LEU A 483 PRO A 488 -1 O CYS A 484 N VAL A 178
SHEET 3 C 3 LEU A 458 LEU A 462 -1 N GLU A 459 O ARG A 487
SHEET 1 D 2 THR A 378 ILE A 380 0
SHEET 2 D 2 VAL A 383 VAL A 385 -1 O VAL A 383 N ILE A 380
SHEET 1 E 2 LEU A 470 GLU A 472 0
SHEET 2 E 2 LEU A 476 PRO A 478 -1 O LYS A 477 N GLN A 471
SHEET 1 F 4 VAL B 74 VAL B 79 0
SHEET 2 F 4 LYS B 82 VAL B 87 -1 O SER B 84 N VAL B 77
SHEET 3 F 4 THR B 389 SER B 394 1 O LEU B 392 N VAL B 85
SHEET 4 F 4 GLY B 369 LEU B 374 -1 N LEU B 374 O THR B 389
SHEET 1 G 2 THR B 114 VAL B 115 0
SHEET 2 G 2 GLU B 118 ARG B 119 -1 O GLU B 118 N VAL B 115
SHEET 1 H 3 VAL B 178 SER B 179 0
SHEET 2 H 3 LEU B 483 PRO B 488 -1 O CYS B 484 N VAL B 178
SHEET 3 H 3 LEU B 458 LEU B 462 -1 N GLU B 459 O ARG B 487
SHEET 1 I 2 THR B 378 ILE B 380 0
SHEET 2 I 2 VAL B 383 VAL B 385 -1 O VAL B 383 N ILE B 380
SHEET 1 J 2 LEU B 470 GLU B 472 0
SHEET 2 J 2 LEU B 476 PRO B 478 -1 O LYS B 477 N GLN B 471
LINK SG CYS A 437 FE HEM A 505 1555 1555 2.36
LINK FE HEM A 505 N8 VOR A 506 1555 1555 1.95
LINK SG CYS B 437 FE HEM B 505 1555 1555 2.23
LINK FE HEM B 505 N8 VOR B 506 1555 1555 2.16
SITE 1 AC1 21 LYS A 104 TYR A 109 LEU A 125 VAL A 126
SITE 2 AC1 21 TRP A 134 ARG A 138 PHE A 145 ALA A 302
SITE 3 AC1 21 GLY A 303 THR A 306 ALA A 367 THR A 370
SITE 4 AC1 21 PRO A 429 PHE A 430 SER A 431 ARG A 435
SITE 5 AC1 21 CYS A 437 ALA A 443 VOR A 506 HOH A 618
SITE 6 AC1 21 HOH A 970
SITE 1 AC2 9 LEU A 112 PHE A 121 VAL A 126 SER A 127
SITE 2 AC2 9 ILE A 301 ALA A 302 THR A 306 THR A 475
SITE 3 AC2 9 HEM A 505
SITE 1 AC3 24 LYS B 104 TYR B 109 LEU B 125 VAL B 126
SITE 2 AC3 24 TRP B 134 ARG B 138 ALA B 302 GLY B 303
SITE 3 AC3 24 THR B 306 SER B 307 THR B 370 PRO B 429
SITE 4 AC3 24 PHE B 430 SER B 431 ARG B 435 SER B 436
SITE 5 AC3 24 CYS B 437 ILE B 438 GLY B 439 ALA B 443
SITE 6 AC3 24 VOR B 506 HOH B 616 HOH B 617 HOH B 960
SITE 1 AC4 11 LEU B 112 PHE B 121 SER B 127 ILE B 222
SITE 2 AC4 11 ALA B 302 THR B 306 ALA B 474 THR B 475
SITE 3 AC4 11 HEM B 505 HOH B 605 HOH B 617
CRYST1 121.600 121.600 143.830 90.00 90.00 90.00 I 41 16
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 0.008224 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008224 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006953 0.00000
(ATOM LINES ARE NOT SHOWN.)
END