HEADER OXIDOREDUCTASE 07-AUG-15 5ABM
TITLE SHEEP ALDEHYDE DEHYDROGENASE 1A1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RETINAL DEHYDROGENASE 1;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: UNP RESIDUES 2-501;
COMPND 5 SYNONYM: RALDH 1, RALDH1, ALDH-E1, ALHDII, ALDEHYDE DEHYDROGENASE
COMPND 6 FAMILY 1 MEMBER A1, ALDEHYDE DEHYDROGENASE, CYTOSOLIC, ALDEHYDE
COMPND 7 DEHYDROGENASE 1A1;
COMPND 8 EC: 1.2.1.36;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: OVIS ARIES;
SOURCE 3 ORGANISM_COMMON: SHEEP;
SOURCE 4 ORGANISM_TAXID: 9940;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS OXIDOREDUCTASE, OXIDATION-REDUCTION PROCESS, ACTIVITY
EXPDTA X-RAY DIFFRACTION
AUTHOR M.F.KOCH,S.HARTEIS,I.D.BLANK,G.PESTEL,L.F.TIETZE,C.OCHSENFELD,
AUTHOR 2 S.SCHNEIDER,S.A.SIEBER
REVDAT 5 10-JAN-24 5ABM 1 COMPND REMARK HETNAM LINK
REVDAT 4 08-MAY-19 5ABM 1 REMARK
REVDAT 3 18-NOV-15 5ABM 1 JRNL
REVDAT 2 30-SEP-15 5ABM 1 JRNL
REVDAT 1 16-SEP-15 5ABM 0
JRNL AUTH M.F.KOCH,S.HARTEIS,I.D.BLANK,G.PESTEL,L.F.TIETZE,
JRNL AUTH 2 C.OCHSENFELD,S.SCHNEIDER,S.A.SIEBER
JRNL TITL STRUCTURAL, BIOCHEMICAL, AND COMPUTATIONAL STUDIES REVEAL
JRNL TITL 2 THE MECHANISM OF SELECTIVE ALDEHYDE DEHYDROGENASE 1A1
JRNL TITL 3 INHIBITION BY CYTOTOXIC DUOCARMYCIN ANALOGUES.
JRNL REF ANGEW.CHEM.INT.ED.ENGL. V. 54 13550 2015
JRNL REFN ISSN 1433-7851
JRNL PMID 26373694
JRNL DOI 10.1002/ANIE.201505749
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0073
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) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 151.85
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 237099
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) : 0.181
REMARK 3 R VALUE (WORKING SET) : 0.180
REMARK 3 FREE R VALUE : 0.203
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 12505
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.74
REMARK 3 REFLECTION IN BIN (WORKING SET) : 16877
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.33
REMARK 3 BIN R VALUE (WORKING SET) : 0.3720
REMARK 3 BIN FREE R VALUE SET COUNT : 881
REMARK 3 BIN FREE R VALUE : 0.3770
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 15225
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 180
REMARK 3 SOLVENT ATOMS : 1340
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.18
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.10000
REMARK 3 B22 (A**2) : -0.01000
REMARK 3 B33 (A**2) : -1.05000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.52000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.099
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.094
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.072
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.268
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.959
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.948
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 16043 ; 0.018 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 15189 ; 0.007 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 21762 ; 1.810 ; 1.975
REMARK 3 BOND ANGLES OTHERS (DEGREES): 35143 ; 1.311 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2036 ; 6.557 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 682 ;33.991 ;24.853
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2750 ;13.731 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 68 ;17.276 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2361 ; 0.118 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 18295 ; 0.011 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 3601 ; 0.005 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 8036 ; 0.751 ; 0.908
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 8035 ; 0.751 ; 0.908
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 10084 ; 1.124 ; 1.359
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 8007 ; 1.507 ; 1.109
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 24
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 7 A 57
REMARK 3 ORIGIN FOR THE GROUP (A): 80.4556 15.6211 86.7508
REMARK 3 T TENSOR
REMARK 3 T11: 0.0801 T22: 0.0165
REMARK 3 T33: 0.1988 T12: 0.0146
REMARK 3 T13: -0.1073 T23: 0.0034
REMARK 3 L TENSOR
REMARK 3 L11: 1.8531 L22: 1.4923
REMARK 3 L33: 2.2079 L12: -0.2006
REMARK 3 L13: -0.2625 L23: -0.1690
REMARK 3 S TENSOR
REMARK 3 S11: -0.0244 S12: -0.1620 S13: -0.2003
REMARK 3 S21: 0.0925 S22: 0.0341 S23: -0.0793
REMARK 3 S31: 0.1760 S32: 0.0745 S33: -0.0097
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 58 A 269
REMARK 3 ORIGIN FOR THE GROUP (A): 71.2616 30.5814 79.5716
REMARK 3 T TENSOR
REMARK 3 T11: 0.0537 T22: 0.0114
REMARK 3 T33: 0.1004 T12: 0.0054
REMARK 3 T13: -0.0699 T23: -0.0060
REMARK 3 L TENSOR
REMARK 3 L11: 0.5865 L22: 0.8198
REMARK 3 L33: 0.3698 L12: -0.1888
REMARK 3 L13: 0.2809 L23: -0.3583
REMARK 3 S TENSOR
REMARK 3 S11: -0.0041 S12: -0.0219 S13: -0.0602
REMARK 3 S21: 0.0541 S22: 0.0299 S23: -0.0233
REMARK 3 S31: -0.0187 S32: -0.0161 S33: -0.0258
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 270 A 407
REMARK 3 ORIGIN FOR THE GROUP (A): 68.9381 32.5286 111.4767
REMARK 3 T TENSOR
REMARK 3 T11: 0.1494 T22: 0.3189
REMARK 3 T33: 0.0996 T12: 0.0817
REMARK 3 T13: -0.0841 T23: 0.0608
REMARK 3 L TENSOR
REMARK 3 L11: 2.2234 L22: 2.4285
REMARK 3 L33: 1.5108 L12: -1.3960
REMARK 3 L13: -0.7938 L23: 0.8963
REMARK 3 S TENSOR
REMARK 3 S11: -0.2569 S12: -0.7261 S13: -0.1461
REMARK 3 S21: 0.2884 S22: 0.3358 S23: 0.0228
REMARK 3 S31: 0.2102 S32: 0.2125 S33: -0.0789
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 408 A 478
REMARK 3 ORIGIN FOR THE GROUP (A): 61.4292 46.1744 101.0364
REMARK 3 T TENSOR
REMARK 3 T11: 0.0961 T22: 0.0817
REMARK 3 T33: 0.0956 T12: 0.0084
REMARK 3 T13: -0.0834 T23: -0.0104
REMARK 3 L TENSOR
REMARK 3 L11: 2.4815 L22: 0.8297
REMARK 3 L33: 1.0323 L12: -0.3930
REMARK 3 L13: -0.8285 L23: -0.2219
REMARK 3 S TENSOR
REMARK 3 S11: 0.0135 S12: -0.3366 S13: 0.0740
REMARK 3 S21: 0.1209 S22: 0.0668 S23: -0.0310
REMARK 3 S31: -0.0634 S32: 0.0376 S33: -0.0803
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 479 A 484
REMARK 3 ORIGIN FOR THE GROUP (A): 61.9712 41.7843 79.7503
REMARK 3 T TENSOR
REMARK 3 T11: 0.1717 T22: 0.1801
REMARK 3 T33: 0.1608 T12: 0.0224
REMARK 3 T13: 0.0065 T23: 0.0165
REMARK 3 L TENSOR
REMARK 3 L11: 7.4254 L22: 1.5073
REMARK 3 L33: 2.0853 L12: 3.3378
REMARK 3 L13: -2.4267 L23: -1.1556
REMARK 3 S TENSOR
REMARK 3 S11: -0.0157 S12: 0.1912 S13: 0.0207
REMARK 3 S21: -0.0132 S22: 0.0689 S23: 0.0004
REMARK 3 S31: -0.1177 S32: -0.1166 S33: -0.0532
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 485 A 500
REMARK 3 ORIGIN FOR THE GROUP (A): 62.6829 52.5981 60.6553
REMARK 3 T TENSOR
REMARK 3 T11: 0.0511 T22: 0.0360
REMARK 3 T33: 0.0916 T12: -0.0028
REMARK 3 T13: -0.0642 T23: 0.0082
REMARK 3 L TENSOR
REMARK 3 L11: 0.8865 L22: 1.8660
REMARK 3 L33: 0.9974 L12: -0.5682
REMARK 3 L13: 0.6805 L23: -0.6748
REMARK 3 S TENSOR
REMARK 3 S11: -0.0758 S12: 0.0605 S13: 0.0891
REMARK 3 S21: 0.0583 S22: 0.0266 S23: -0.0518
REMARK 3 S31: -0.0966 S32: -0.0055 S33: 0.0491
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 7 B 20
REMARK 3 ORIGIN FOR THE GROUP (A): 75.3922 86.1024 72.1789
REMARK 3 T TENSOR
REMARK 3 T11: 0.3183 T22: 0.1416
REMARK 3 T33: 0.2199 T12: 0.0168
REMARK 3 T13: -0.0729 T23: 0.0354
REMARK 3 L TENSOR
REMARK 3 L11: 0.9114 L22: 0.7295
REMARK 3 L33: 17.6238 L12: 0.7568
REMARK 3 L13: 2.8971 L23: 1.9155
REMARK 3 S TENSOR
REMARK 3 S11: -0.1407 S12: 0.2357 S13: 0.0665
REMARK 3 S21: -0.2708 S22: 0.2114 S23: 0.0901
REMARK 3 S31: -0.3590 S32: -0.0022 S33: -0.0708
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 21 B 86
REMARK 3 ORIGIN FOR THE GROUP (A): 76.2778 72.1566 88.8484
REMARK 3 T TENSOR
REMARK 3 T11: 0.0923 T22: 0.0185
REMARK 3 T33: 0.1449 T12: -0.0035
REMARK 3 T13: -0.1055 T23: -0.0166
REMARK 3 L TENSOR
REMARK 3 L11: 2.2139 L22: 1.0133
REMARK 3 L33: 0.9800 L12: 1.0434
REMARK 3 L13: -0.0979 L23: 0.0218
REMARK 3 S TENSOR
REMARK 3 S11: 0.0181 S12: -0.1510 S13: 0.1808
REMARK 3 S21: 0.0839 S22: -0.0505 S23: -0.0266
REMARK 3 S31: -0.0964 S32: 0.0926 S33: 0.0323
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 87 B 269
REMARK 3 ORIGIN FOR THE GROUP (A): 71.1805 64.7175 80.4811
REMARK 3 T TENSOR
REMARK 3 T11: 0.0798 T22: 0.0113
REMARK 3 T33: 0.1042 T12: 0.0003
REMARK 3 T13: -0.0787 T23: -0.0067
REMARK 3 L TENSOR
REMARK 3 L11: 0.6237 L22: 0.8745
REMARK 3 L33: 0.1447 L12: 0.4335
REMARK 3 L13: -0.0631 L23: -0.2645
REMARK 3 S TENSOR
REMARK 3 S11: -0.0725 S12: 0.0543 S13: 0.0362
REMARK 3 S21: -0.0832 S22: 0.0435 S23: -0.0542
REMARK 3 S31: 0.0230 S32: 0.0001 S33: 0.0290
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 270 B 362
REMARK 3 ORIGIN FOR THE GROUP (A): 83.9065 63.2238 54.0913
REMARK 3 T TENSOR
REMARK 3 T11: 0.0891 T22: 0.1491
REMARK 3 T33: 0.1398 T12: -0.0444
REMARK 3 T13: -0.0364 T23: 0.0304
REMARK 3 L TENSOR
REMARK 3 L11: 0.7276 L22: 1.8689
REMARK 3 L33: 1.3496 L12: 0.5762
REMARK 3 L13: 0.1183 L23: 0.5385
REMARK 3 S TENSOR
REMARK 3 S11: -0.0788 S12: 0.2153 S13: 0.0395
REMARK 3 S21: -0.1700 S22: 0.0677 S23: -0.0609
REMARK 3 S31: -0.1243 S32: 0.1853 S33: 0.0111
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 363 B 482
REMARK 3 ORIGIN FOR THE GROUP (A): 80.5845 54.3878 58.3472
REMARK 3 T TENSOR
REMARK 3 T11: 0.0729 T22: 0.0824
REMARK 3 T33: 0.1234 T12: -0.0048
REMARK 3 T13: -0.0571 T23: 0.0014
REMARK 3 L TENSOR
REMARK 3 L11: 1.3018 L22: 1.0464
REMARK 3 L33: 1.2674 L12: 0.5998
REMARK 3 L13: 0.1520 L23: -0.1325
REMARK 3 S TENSOR
REMARK 3 S11: -0.0583 S12: 0.1695 S13: -0.0060
REMARK 3 S21: -0.1102 S22: 0.0632 S23: -0.1312
REMARK 3 S31: 0.0083 S32: 0.1846 S33: -0.0049
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 483 B 500
REMARK 3 ORIGIN FOR THE GROUP (A): 53.8936 43.8836 91.6070
REMARK 3 T TENSOR
REMARK 3 T11: 0.0763 T22: 0.0511
REMARK 3 T33: 0.0868 T12: -0.0050
REMARK 3 T13: -0.0733 T23: 0.0029
REMARK 3 L TENSOR
REMARK 3 L11: 5.1384 L22: 2.9166
REMARK 3 L33: 0.0788 L12: 3.0818
REMARK 3 L13: -0.5885 L23: -0.2501
REMARK 3 S TENSOR
REMARK 3 S11: -0.1539 S12: 0.1966 S13: -0.0334
REMARK 3 S21: -0.1180 S22: 0.1572 S23: -0.0857
REMARK 3 S31: 0.0172 S32: -0.0269 S33: -0.0033
REMARK 3
REMARK 3 TLS GROUP : 13
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 7 C 56
REMARK 3 ORIGIN FOR THE GROUP (A): 87.4363 25.4282 131.0133
REMARK 3 T TENSOR
REMARK 3 T11: 0.1313 T22: 0.0177
REMARK 3 T33: 0.1912 T12: 0.0061
REMARK 3 T13: -0.1136 T23: -0.0360
REMARK 3 L TENSOR
REMARK 3 L11: 2.1818 L22: 1.2885
REMARK 3 L33: 1.9554 L12: 0.6808
REMARK 3 L13: -0.3719 L23: 0.2884
REMARK 3 S TENSOR
REMARK 3 S11: -0.0726 S12: 0.1752 S13: -0.3271
REMARK 3 S21: -0.0866 S22: 0.0000 S23: -0.0204
REMARK 3 S31: 0.1860 S32: -0.0152 S33: 0.0726
REMARK 3
REMARK 3 TLS GROUP : 14
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 57 C 270
REMARK 3 ORIGIN FOR THE GROUP (A): 92.8547 40.6310 141.1436
REMARK 3 T TENSOR
REMARK 3 T11: 0.0676 T22: 0.0169
REMARK 3 T33: 0.1074 T12: 0.0004
REMARK 3 T13: -0.0813 T23: -0.0067
REMARK 3 L TENSOR
REMARK 3 L11: 0.3014 L22: 0.7800
REMARK 3 L33: 0.6617 L12: 0.0384
REMARK 3 L13: 0.2326 L23: 0.4688
REMARK 3 S TENSOR
REMARK 3 S11: 0.0380 S12: 0.0112 S13: -0.0515
REMARK 3 S21: -0.0500 S22: -0.0010 S23: -0.0089
REMARK 3 S31: -0.0209 S32: 0.0244 S33: -0.0371
REMARK 3
REMARK 3 TLS GROUP : 15
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 271 C 327
REMARK 3 ORIGIN FOR THE GROUP (A): 114.5323 46.8089 115.4741
REMARK 3 T TENSOR
REMARK 3 T11: 0.1407 T22: 0.1652
REMARK 3 T33: 0.1110 T12: 0.0297
REMARK 3 T13: -0.0556 T23: -0.0360
REMARK 3 L TENSOR
REMARK 3 L11: 0.8794 L22: 1.6510
REMARK 3 L33: 1.1484 L12: 0.5975
REMARK 3 L13: 0.1769 L23: 0.4332
REMARK 3 S TENSOR
REMARK 3 S11: 0.0183 S12: 0.2130 S13: -0.0941
REMARK 3 S21: -0.1642 S22: 0.0167 S23: -0.2403
REMARK 3 S31: -0.0463 S32: 0.1962 S33: -0.0350
REMARK 3
REMARK 3 TLS GROUP : 16
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 328 C 372
REMARK 3 ORIGIN FOR THE GROUP (A): 101.5760 36.7142 110.6448
REMARK 3 T TENSOR
REMARK 3 T11: 0.1586 T22: 0.2190
REMARK 3 T33: 0.1061 T12: 0.0284
REMARK 3 T13: -0.0978 T23: -0.1046
REMARK 3 L TENSOR
REMARK 3 L11: 1.5195 L22: 3.0983
REMARK 3 L33: 1.5608 L12: 0.6417
REMARK 3 L13: -1.0302 L23: -1.1992
REMARK 3 S TENSOR
REMARK 3 S11: -0.0260 S12: 0.4087 S13: -0.1555
REMARK 3 S21: -0.2454 S22: -0.0338 S23: -0.0063
REMARK 3 S31: -0.0184 S32: -0.0560 S33: 0.0599
REMARK 3
REMARK 3 TLS GROUP : 17
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 373 C 482
REMARK 3 ORIGIN FOR THE GROUP (A): 107.3240 51.5326 120.7115
REMARK 3 T TENSOR
REMARK 3 T11: 0.1167 T22: 0.0883
REMARK 3 T33: 0.0898 T12: 0.0351
REMARK 3 T13: -0.0799 T23: -0.0028
REMARK 3 L TENSOR
REMARK 3 L11: 1.4035 L22: 0.8589
REMARK 3 L33: 1.1081 L12: 0.1627
REMARK 3 L13: 0.0915 L23: 0.5561
REMARK 3 S TENSOR
REMARK 3 S11: 0.0227 S12: 0.2178 S13: -0.0021
REMARK 3 S21: -0.1317 S22: -0.0004 S23: -0.0274
REMARK 3 S31: -0.0541 S32: 0.0110 S33: -0.0222
REMARK 3
REMARK 3 TLS GROUP : 18
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 483 C 500
REMARK 3 ORIGIN FOR THE GROUP (A): 94.2391 61.5548 160.0748
REMARK 3 T TENSOR
REMARK 3 T11: 0.0690 T22: 0.0725
REMARK 3 T33: 0.0969 T12: -0.0085
REMARK 3 T13: -0.0587 T23: -0.0290
REMARK 3 L TENSOR
REMARK 3 L11: 1.0997 L22: 3.2187
REMARK 3 L33: 3.4085 L12: 1.4370
REMARK 3 L13: 1.9287 L23: 2.5401
REMARK 3 S TENSOR
REMARK 3 S11: -0.0474 S12: 0.1040 S13: -0.0287
REMARK 3 S21: -0.1012 S22: 0.1212 S23: -0.0413
REMARK 3 S31: -0.0879 S32: 0.2199 S33: -0.0738
REMARK 3
REMARK 3 TLS GROUP : 19
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 7 D 57
REMARK 3 ORIGIN FOR THE GROUP (A): 83.6814 89.7805 135.1716
REMARK 3 T TENSOR
REMARK 3 T11: 0.1396 T22: 0.0186
REMARK 3 T33: 0.1776 T12: 0.0261
REMARK 3 T13: -0.1340 T23: -0.0181
REMARK 3 L TENSOR
REMARK 3 L11: 1.5736 L22: 1.5443
REMARK 3 L33: 1.9889 L12: -0.4627
REMARK 3 L13: -0.2646 L23: -0.2534
REMARK 3 S TENSOR
REMARK 3 S11: -0.0091 S12: -0.0191 S13: 0.1581
REMARK 3 S21: -0.0106 S22: -0.0108 S23: 0.1580
REMARK 3 S31: -0.1735 S32: -0.1416 S33: 0.0200
REMARK 3
REMARK 3 TLS GROUP : 20
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 58 D 269
REMARK 3 ORIGIN FOR THE GROUP (A): 94.7358 74.8434 138.9677
REMARK 3 T TENSOR
REMARK 3 T11: 0.0944 T22: 0.0203
REMARK 3 T33: 0.0938 T12: 0.0085
REMARK 3 T13: -0.0851 T23: -0.0004
REMARK 3 L TENSOR
REMARK 3 L11: 0.6335 L22: 0.9104
REMARK 3 L33: 0.2210 L12: -0.3884
REMARK 3 L13: 0.1887 L23: 0.0400
REMARK 3 S TENSOR
REMARK 3 S11: -0.0393 S12: -0.0258 S13: 0.0271
REMARK 3 S21: 0.0134 S22: -0.0095 S23: 0.0790
REMARK 3 S31: -0.0235 S32: -0.0026 S33: 0.0489
REMARK 3
REMARK 3 TLS GROUP : 21
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 270 D 375
REMARK 3 ORIGIN FOR THE GROUP (A): 70.3312 73.2696 159.7478
REMARK 3 T TENSOR
REMARK 3 T11: 0.1257 T22: 0.2189
REMARK 3 T33: 0.2128 T12: 0.0573
REMARK 3 T13: -0.0320 T23: -0.0582
REMARK 3 L TENSOR
REMARK 3 L11: 0.8793 L22: 1.8122
REMARK 3 L33: 1.4152 L12: 0.0066
REMARK 3 L13: -0.0042 L23: -0.5958
REMARK 3 S TENSOR
REMARK 3 S11: -0.0139 S12: -0.2276 S13: 0.1357
REMARK 3 S21: 0.1718 S22: 0.0251 S23: 0.2537
REMARK 3 S31: -0.1924 S32: -0.3501 S33: -0.0112
REMARK 3
REMARK 3 TLS GROUP : 22
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 376 D 479
REMARK 3 ORIGIN FOR THE GROUP (A): 77.2022 63.2424 157.3918
REMARK 3 T TENSOR
REMARK 3 T11: 0.0827 T22: 0.1119
REMARK 3 T33: 0.1491 T12: -0.0026
REMARK 3 T13: -0.0601 T23: -0.0278
REMARK 3 L TENSOR
REMARK 3 L11: 1.2425 L22: 0.9205
REMARK 3 L33: 1.5848 L12: -0.5705
REMARK 3 L13: 0.2807 L23: -0.1461
REMARK 3 S TENSOR
REMARK 3 S11: -0.0358 S12: -0.1074 S13: -0.0009
REMARK 3 S21: 0.0747 S22: 0.0286 S23: 0.1937
REMARK 3 S31: -0.0162 S32: -0.2907 S33: 0.0072
REMARK 3
REMARK 3 TLS GROUP : 23
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 480 D 485
REMARK 3 ORIGIN FOR THE GROUP (A): 98.5529 64.4312 144.6457
REMARK 3 T TENSOR
REMARK 3 T11: 0.2572 T22: 0.2367
REMARK 3 T33: 0.2653 T12: 0.0446
REMARK 3 T13: 0.0443 T23: 0.0251
REMARK 3 L TENSOR
REMARK 3 L11: 0.1218 L22: 0.3929
REMARK 3 L33: 11.7289 L12: -0.1721
REMARK 3 L13: 1.0025 L23: -2.1221
REMARK 3 S TENSOR
REMARK 3 S11: -0.0236 S12: -0.0079 S13: -0.0229
REMARK 3 S21: -0.1311 S22: -0.0986 S23: -0.0430
REMARK 3 S31: 0.6757 S32: 0.3140 S33: 0.1222
REMARK 3
REMARK 3 TLS GROUP : 24
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 486 D 500
REMARK 3 ORIGIN FOR THE GROUP (A): 116.7544 51.6460 135.3324
REMARK 3 T TENSOR
REMARK 3 T11: 0.0922 T22: 0.0269
REMARK 3 T33: 0.0735 T12: 0.0125
REMARK 3 T13: -0.0764 T23: -0.0113
REMARK 3 L TENSOR
REMARK 3 L11: 2.2740 L22: 1.9131
REMARK 3 L33: 0.9335 L12: -1.1586
REMARK 3 L13: 0.0444 L23: -0.3930
REMARK 3 S TENSOR
REMARK 3 S11: 0.0924 S12: 0.0809 S13: -0.1602
REMARK 3 S21: -0.0711 S22: -0.0358 S23: 0.0548
REMARK 3 S31: 0.0326 S32: 0.0926 S33: -0.0565
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS. U VALUES WITH TLS ADDED
REMARK 4
REMARK 4 5ABM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 07-AUG-15.
REMARK 100 THE DEPOSITION ID IS D_1290064621.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-MAY-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
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
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 249604
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 51.800
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 12.600
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 6.700
REMARK 200 R MERGE (I) : 0.11000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.76
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.3
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.86000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 4X4L
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 26.20
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.62
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM BIS-TRIS, PH 6.0, 4.5-7%
REMARK 280 PEG5000, 150=225MM MGCL2, 4DEGREE, TEMPERATURE 277K
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 93.99250
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 40.40200
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 93.99250
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 40.40200
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
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 20940 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 58700 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -112.3 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, 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 BIOMT1 2 -1.000000 0.000000 0.000000 215.18615
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 302.77279
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 21090 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 58440 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -112.1 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 BIOMT1 2 -1.000000 0.000000 0.000000 107.59307
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 151.38639
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH B2054 LIES ON A SPECIAL POSITION.
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 SER A 1
REMARK 465 SER A 2
REMARK 465 SER A 3
REMARK 465 ALA A 4
REMARK 465 MET A 5
REMARK 465 PRO A 6
REMARK 465 SER B 1
REMARK 465 SER B 2
REMARK 465 SER B 3
REMARK 465 ALA B 4
REMARK 465 MET B 5
REMARK 465 PRO B 6
REMARK 465 SER C 1
REMARK 465 SER C 2
REMARK 465 SER C 3
REMARK 465 ALA C 4
REMARK 465 MET C 5
REMARK 465 PRO C 6
REMARK 465 SER D 1
REMARK 465 SER D 2
REMARK 465 SER D 3
REMARK 465 ALA D 4
REMARK 465 MET D 5
REMARK 465 PRO D 6
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ASP D 7 CG OD1 OD2
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 GLU D 268 O HOH D 2198 2.11
REMARK 500 OH TYR B 480 O HOH A 2347 2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH B 2111 O HOH B 2111 2656 1.84
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 LEU A 15 C GLN A 16 N -0.212
REMARK 500 LEU C 12 C THR C 13 N -0.188
REMARK 500 THR C 13 C ASN C 14 N -0.172
REMARK 500 LEU C 269 C GLY C 270 N -0.164
REMARK 500 GLU C 484 C TYR C 485 N -0.189
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 LEU A 15 CA - C - N ANGL. DEV. = -17.2 DEGREES
REMARK 500 LEU A 15 O - C - N ANGL. DEV. = 15.6 DEGREES
REMARK 500 ASP A 55 CB - CG - OD1 ANGL. DEV. = 7.3 DEGREES
REMARK 500 ARG A 130 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 ARG A 130 NE - CZ - NH2 ANGL. DEV. = -5.0 DEGREES
REMARK 500 ARG A 142 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG A 142 NE - CZ - NH2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 ARG A 155 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ARG A 155 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 ARG B 130 NE - CZ - NH2 ANGL. DEV. = -5.3 DEGREES
REMARK 500 ARG B 142 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 ARG B 142 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 ARG B 155 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG B 155 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ARG B 325 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 LEU C 12 CA - C - N ANGL. DEV. = 15.3 DEGREES
REMARK 500 LEU C 12 O - C - N ANGL. DEV. = -15.4 DEGREES
REMARK 500 THR C 13 C - N - CA ANGL. DEV. = 19.4 DEGREES
REMARK 500 THR C 13 CA - C - N ANGL. DEV. = 13.7 DEGREES
REMARK 500 THR C 13 O - C - N ANGL. DEV. = -17.7 DEGREES
REMARK 500 ARG C 86 NE - CZ - NH1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 ARG C 86 NE - CZ - NH2 ANGL. DEV. = -5.1 DEGREES
REMARK 500 ARG C 130 NE - CZ - NH2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 ARG C 142 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ARG C 142 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ARG C 155 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 ARG C 155 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 LEU C 269 O - C - N ANGL. DEV. = -10.5 DEGREES
REMARK 500 ARG D 130 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG D 130 NE - CZ - NH2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 ARG D 142 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG D 142 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ARG D 155 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 ARG D 155 NE - CZ - NH2 ANGL. DEV. = -4.0 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 LYS A 18 -43.58 -131.56
REMARK 500 THR A 227 -82.27 -99.65
REMARK 500 SER A 260 -83.43 -99.34
REMARK 500 GLN A 300 55.76 -94.52
REMARK 500 LYS A 328 41.20 -98.02
REMARK 500 LYS A 469 -133.16 55.68
REMARK 500 LEU A 477 -176.77 64.32
REMARK 500 LYS B 18 -46.15 -131.01
REMARK 500 CYS B 49 -179.86 -172.59
REMARK 500 THR B 227 -82.32 -100.54
REMARK 500 SER B 260 -83.32 -100.36
REMARK 500 GLN B 300 53.76 -92.28
REMARK 500 LYS B 328 32.09 -96.79
REMARK 500 LYS B 469 -135.45 56.56
REMARK 500 LEU B 477 -177.20 66.77
REMARK 500 LYS C 18 -44.74 -130.46
REMARK 500 CYS C 49 -178.65 -173.93
REMARK 500 THR C 227 -80.24 -99.62
REMARK 500 SER C 260 -83.57 -100.55
REMARK 500 GLN C 300 53.08 -91.80
REMARK 500 LYS C 328 35.43 -95.62
REMARK 500 LYS C 469 -134.22 56.78
REMARK 500 LEU C 477 177.72 75.89
REMARK 500 LYS D 18 -41.39 -132.51
REMARK 500 THR D 227 -83.70 -98.17
REMARK 500 SER D 260 -86.00 -101.51
REMARK 500 GLN D 300 54.41 -95.60
REMARK 500 LYS D 328 57.77 -100.60
REMARK 500 LYS D 469 -134.53 54.63
REMARK 500 LEU D 477 179.52 74.37
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 THR C 13 -16.93
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 MG A 502 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TXE A 501 O1N
REMARK 620 2 TXE A 501 O1P 82.8
REMARK 620 3 HOH A2212 O 93.1 93.8
REMARK 620 4 HOH A2216 O 167.7 107.3 79.5
REMARK 620 5 HOH A2280 O 85.3 167.3 91.5 85.1
REMARK 620 6 HOH A2360 O 91.6 91.0 173.7 95.2 84.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 502 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TXE B 501 O2N
REMARK 620 2 TXE B 501 O2P 91.7
REMARK 620 3 HOH B2205 O 88.4 87.4
REMARK 620 4 HOH B2209 O 152.4 111.9 78.9
REMARK 620 5 HOH B2330 O 94.5 95.2 176.1 97.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C 502 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TXE C 501 O2P
REMARK 620 2 TXE C 501 O1N 89.9
REMARK 620 3 HOH C2205 O 89.0 96.0
REMARK 620 4 HOH C2208 O 109.0 160.0 78.3
REMARK 620 5 HOH C2278 O 167.3 80.1 84.4 80.3
REMARK 620 6 HOH C2355 O 88.8 91.9 171.8 95.0 99.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D 502 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TXE D 501 O2P
REMARK 620 2 TXE D 501 O2N 78.8
REMARK 620 3 HOH D2187 O 93.0 89.9
REMARK 620 4 HOH D2191 O 113.8 161.5 76.5
REMARK 620 5 HOH D2240 O 159.9 81.4 83.0 84.6
REMARK 620 6 HOH D2287 O 100.4 88.8 166.0 101.5 83.0
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 TXE A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TXE B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TXE C 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TXE D 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 502
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5AC0 RELATED DB: PDB
REMARK 900 OVIS ARIES ALDEHYDE DEHYDROGENASE 1A1 IN COMPLEX WITH A DUOCARMYCIN
REMARK 900 ANALOG
REMARK 900 RELATED ID: 5AC1 RELATED DB: PDB
REMARK 900 SHEEP ALDEHYDE DEHYDROGENASE 1A1 WITH DUOCARMYCIN ANALOG INHIBITOR
REMARK 900 RELATED ID: 5AC2 RELATED DB: PDB
REMARK 900 HUMAN ALDEHYDE DEHYDROGENASE 1A1 WITH DUOCARMYCIN ANALOG
DBREF 5ABM A 1 500 UNP P51977 AL1A1_SHEEP 2 501
DBREF 5ABM B 1 500 UNP P51977 AL1A1_SHEEP 2 501
DBREF 5ABM C 1 500 UNP P51977 AL1A1_SHEEP 2 501
DBREF 5ABM D 1 500 UNP P51977 AL1A1_SHEEP 2 501
SEQRES 1 A 500 SER SER SER ALA MET PRO ASP VAL PRO ALA PRO LEU THR
SEQRES 2 A 500 ASN LEU GLN PHE LYS TYR THR LYS ILE PHE ILE ASN ASN
SEQRES 3 A 500 GLU TRP HIS SER SER VAL SER GLY LYS LYS PHE PRO VAL
SEQRES 4 A 500 PHE ASN PRO ALA THR GLU GLU LYS LEU CYS GLU VAL GLU
SEQRES 5 A 500 GLU GLY ASP LYS GLU ASP VAL ASP LYS ALA VAL LYS ALA
SEQRES 6 A 500 ALA ARG GLN ALA PHE GLN ILE GLY SER PRO TRP ARG THR
SEQRES 7 A 500 MET ASP ALA SER GLU ARG GLY ARG LEU LEU ASN LYS LEU
SEQRES 8 A 500 ALA ASP LEU ILE GLU ARG ASP ARG LEU LEU LEU ALA THR
SEQRES 9 A 500 MET GLU ALA MET ASN GLY GLY LYS LEU PHE SER ASN ALA
SEQRES 10 A 500 TYR LEU MET ASP LEU GLY GLY CYS ILE LYS THR LEU ARG
SEQRES 11 A 500 TYR CYS ALA GLY TRP ALA ASP LYS ILE GLN GLY ARG THR
SEQRES 12 A 500 ILE PRO MET ASP GLY ASN PHE PHE THR TYR THR ARG SER
SEQRES 13 A 500 GLU PRO VAL GLY VAL CYS GLY GLN ILE ILE PRO TRP ASN
SEQRES 14 A 500 PHE PRO LEU LEU MET PHE LEU TRP LYS ILE GLY PRO ALA
SEQRES 15 A 500 LEU SER CYS GLY ASN THR VAL VAL VAL LYS PRO ALA GLU
SEQRES 16 A 500 GLN THR PRO LEU THR ALA LEU HIS MET GLY SER LEU ILE
SEQRES 17 A 500 LYS GLU ALA GLY PHE PRO PRO GLY VAL VAL ASN ILE VAL
SEQRES 18 A 500 PRO GLY TYR GLY PRO THR ALA GLY ALA ALA ILE SER SER
SEQRES 19 A 500 HIS MET ASP VAL ASP LYS VAL ALA PHE THR GLY SER THR
SEQRES 20 A 500 GLU VAL GLY LYS LEU ILE LYS GLU ALA ALA GLY LYS SER
SEQRES 21 A 500 ASN LEU LYS ARG VAL SER LEU GLU LEU GLY GLY LYS SER
SEQRES 22 A 500 PRO CYS ILE VAL PHE ALA ASP ALA ASP LEU ASP ASN ALA
SEQRES 23 A 500 VAL GLU PHE ALA HIS GLN GLY VAL PHE TYR HIS GLN GLY
SEQRES 24 A 500 GLN CYS CYS ILE ALA ALA SER ARG LEU PHE VAL GLU GLU
SEQRES 25 A 500 SER ILE TYR ASP GLU PHE VAL ARG ARG SER VAL GLU ARG
SEQRES 26 A 500 ALA LYS LYS TYR VAL LEU GLY ASN PRO LEU THR PRO GLY
SEQRES 27 A 500 VAL SER GLN GLY PRO GLN ILE ASP LYS GLU GLN TYR GLU
SEQRES 28 A 500 LYS ILE LEU ASP LEU ILE GLU SER GLY LYS LYS GLU GLY
SEQRES 29 A 500 ALA LYS LEU GLU CYS GLY GLY GLY PRO TRP GLY ASN LYS
SEQRES 30 A 500 GLY TYR PHE ILE GLN PRO THR VAL PHE SER ASP VAL THR
SEQRES 31 A 500 ASP ASP MET ARG ILE ALA LYS GLU GLU ILE PHE GLY PRO
SEQRES 32 A 500 VAL GLN GLN ILE MET LYS PHE LYS SER LEU ASP ASP VAL
SEQRES 33 A 500 ILE LYS ARG ALA ASN ASN THR PHE TYR GLY LEU SER ALA
SEQRES 34 A 500 GLY ILE PHE THR ASN ASP ILE ASP LYS ALA ILE THR VAL
SEQRES 35 A 500 SER SER ALA LEU GLN SER GLY THR VAL TRP VAL ASN CYS
SEQRES 36 A 500 TYR SER VAL VAL SER ALA GLN CYS PRO PHE GLY GLY PHE
SEQRES 37 A 500 LYS MET SER GLY ASN GLY ARG GLU LEU GLY GLU TYR GLY
SEQRES 38 A 500 PHE HIS GLU TYR THR GLU VAL LYS THR VAL THR ILE LYS
SEQRES 39 A 500 ILE SER GLN LYS ASN SER
SEQRES 1 B 500 SER SER SER ALA MET PRO ASP VAL PRO ALA PRO LEU THR
SEQRES 2 B 500 ASN LEU GLN PHE LYS TYR THR LYS ILE PHE ILE ASN ASN
SEQRES 3 B 500 GLU TRP HIS SER SER VAL SER GLY LYS LYS PHE PRO VAL
SEQRES 4 B 500 PHE ASN PRO ALA THR GLU GLU LYS LEU CYS GLU VAL GLU
SEQRES 5 B 500 GLU GLY ASP LYS GLU ASP VAL ASP LYS ALA VAL LYS ALA
SEQRES 6 B 500 ALA ARG GLN ALA PHE GLN ILE GLY SER PRO TRP ARG THR
SEQRES 7 B 500 MET ASP ALA SER GLU ARG GLY ARG LEU LEU ASN LYS LEU
SEQRES 8 B 500 ALA ASP LEU ILE GLU ARG ASP ARG LEU LEU LEU ALA THR
SEQRES 9 B 500 MET GLU ALA MET ASN GLY GLY LYS LEU PHE SER ASN ALA
SEQRES 10 B 500 TYR LEU MET ASP LEU GLY GLY CYS ILE LYS THR LEU ARG
SEQRES 11 B 500 TYR CYS ALA GLY TRP ALA ASP LYS ILE GLN GLY ARG THR
SEQRES 12 B 500 ILE PRO MET ASP GLY ASN PHE PHE THR TYR THR ARG SER
SEQRES 13 B 500 GLU PRO VAL GLY VAL CYS GLY GLN ILE ILE PRO TRP ASN
SEQRES 14 B 500 PHE PRO LEU LEU MET PHE LEU TRP LYS ILE GLY PRO ALA
SEQRES 15 B 500 LEU SER CYS GLY ASN THR VAL VAL VAL LYS PRO ALA GLU
SEQRES 16 B 500 GLN THR PRO LEU THR ALA LEU HIS MET GLY SER LEU ILE
SEQRES 17 B 500 LYS GLU ALA GLY PHE PRO PRO GLY VAL VAL ASN ILE VAL
SEQRES 18 B 500 PRO GLY TYR GLY PRO THR ALA GLY ALA ALA ILE SER SER
SEQRES 19 B 500 HIS MET ASP VAL ASP LYS VAL ALA PHE THR GLY SER THR
SEQRES 20 B 500 GLU VAL GLY LYS LEU ILE LYS GLU ALA ALA GLY LYS SER
SEQRES 21 B 500 ASN LEU LYS ARG VAL SER LEU GLU LEU GLY GLY LYS SER
SEQRES 22 B 500 PRO CYS ILE VAL PHE ALA ASP ALA ASP LEU ASP ASN ALA
SEQRES 23 B 500 VAL GLU PHE ALA HIS GLN GLY VAL PHE TYR HIS GLN GLY
SEQRES 24 B 500 GLN CYS CYS ILE ALA ALA SER ARG LEU PHE VAL GLU GLU
SEQRES 25 B 500 SER ILE TYR ASP GLU PHE VAL ARG ARG SER VAL GLU ARG
SEQRES 26 B 500 ALA LYS LYS TYR VAL LEU GLY ASN PRO LEU THR PRO GLY
SEQRES 27 B 500 VAL SER GLN GLY PRO GLN ILE ASP LYS GLU GLN TYR GLU
SEQRES 28 B 500 LYS ILE LEU ASP LEU ILE GLU SER GLY LYS LYS GLU GLY
SEQRES 29 B 500 ALA LYS LEU GLU CYS GLY GLY GLY PRO TRP GLY ASN LYS
SEQRES 30 B 500 GLY TYR PHE ILE GLN PRO THR VAL PHE SER ASP VAL THR
SEQRES 31 B 500 ASP ASP MET ARG ILE ALA LYS GLU GLU ILE PHE GLY PRO
SEQRES 32 B 500 VAL GLN GLN ILE MET LYS PHE LYS SER LEU ASP ASP VAL
SEQRES 33 B 500 ILE LYS ARG ALA ASN ASN THR PHE TYR GLY LEU SER ALA
SEQRES 34 B 500 GLY ILE PHE THR ASN ASP ILE ASP LYS ALA ILE THR VAL
SEQRES 35 B 500 SER SER ALA LEU GLN SER GLY THR VAL TRP VAL ASN CYS
SEQRES 36 B 500 TYR SER VAL VAL SER ALA GLN CYS PRO PHE GLY GLY PHE
SEQRES 37 B 500 LYS MET SER GLY ASN GLY ARG GLU LEU GLY GLU TYR GLY
SEQRES 38 B 500 PHE HIS GLU TYR THR GLU VAL LYS THR VAL THR ILE LYS
SEQRES 39 B 500 ILE SER GLN LYS ASN SER
SEQRES 1 C 500 SER SER SER ALA MET PRO ASP VAL PRO ALA PRO LEU THR
SEQRES 2 C 500 ASN LEU GLN PHE LYS TYR THR LYS ILE PHE ILE ASN ASN
SEQRES 3 C 500 GLU TRP HIS SER SER VAL SER GLY LYS LYS PHE PRO VAL
SEQRES 4 C 500 PHE ASN PRO ALA THR GLU GLU LYS LEU CYS GLU VAL GLU
SEQRES 5 C 500 GLU GLY ASP LYS GLU ASP VAL ASP LYS ALA VAL LYS ALA
SEQRES 6 C 500 ALA ARG GLN ALA PHE GLN ILE GLY SER PRO TRP ARG THR
SEQRES 7 C 500 MET ASP ALA SER GLU ARG GLY ARG LEU LEU ASN LYS LEU
SEQRES 8 C 500 ALA ASP LEU ILE GLU ARG ASP ARG LEU LEU LEU ALA THR
SEQRES 9 C 500 MET GLU ALA MET ASN GLY GLY LYS LEU PHE SER ASN ALA
SEQRES 10 C 500 TYR LEU MET ASP LEU GLY GLY CYS ILE LYS THR LEU ARG
SEQRES 11 C 500 TYR CYS ALA GLY TRP ALA ASP LYS ILE GLN GLY ARG THR
SEQRES 12 C 500 ILE PRO MET ASP GLY ASN PHE PHE THR TYR THR ARG SER
SEQRES 13 C 500 GLU PRO VAL GLY VAL CYS GLY GLN ILE ILE PRO TRP ASN
SEQRES 14 C 500 PHE PRO LEU LEU MET PHE LEU TRP LYS ILE GLY PRO ALA
SEQRES 15 C 500 LEU SER CYS GLY ASN THR VAL VAL VAL LYS PRO ALA GLU
SEQRES 16 C 500 GLN THR PRO LEU THR ALA LEU HIS MET GLY SER LEU ILE
SEQRES 17 C 500 LYS GLU ALA GLY PHE PRO PRO GLY VAL VAL ASN ILE VAL
SEQRES 18 C 500 PRO GLY TYR GLY PRO THR ALA GLY ALA ALA ILE SER SER
SEQRES 19 C 500 HIS MET ASP VAL ASP LYS VAL ALA PHE THR GLY SER THR
SEQRES 20 C 500 GLU VAL GLY LYS LEU ILE LYS GLU ALA ALA GLY LYS SER
SEQRES 21 C 500 ASN LEU LYS ARG VAL SER LEU GLU LEU GLY GLY LYS SER
SEQRES 22 C 500 PRO CYS ILE VAL PHE ALA ASP ALA ASP LEU ASP ASN ALA
SEQRES 23 C 500 VAL GLU PHE ALA HIS GLN GLY VAL PHE TYR HIS GLN GLY
SEQRES 24 C 500 GLN CYS CYS ILE ALA ALA SER ARG LEU PHE VAL GLU GLU
SEQRES 25 C 500 SER ILE TYR ASP GLU PHE VAL ARG ARG SER VAL GLU ARG
SEQRES 26 C 500 ALA LYS LYS TYR VAL LEU GLY ASN PRO LEU THR PRO GLY
SEQRES 27 C 500 VAL SER GLN GLY PRO GLN ILE ASP LYS GLU GLN TYR GLU
SEQRES 28 C 500 LYS ILE LEU ASP LEU ILE GLU SER GLY LYS LYS GLU GLY
SEQRES 29 C 500 ALA LYS LEU GLU CYS GLY GLY GLY PRO TRP GLY ASN LYS
SEQRES 30 C 500 GLY TYR PHE ILE GLN PRO THR VAL PHE SER ASP VAL THR
SEQRES 31 C 500 ASP ASP MET ARG ILE ALA LYS GLU GLU ILE PHE GLY PRO
SEQRES 32 C 500 VAL GLN GLN ILE MET LYS PHE LYS SER LEU ASP ASP VAL
SEQRES 33 C 500 ILE LYS ARG ALA ASN ASN THR PHE TYR GLY LEU SER ALA
SEQRES 34 C 500 GLY ILE PHE THR ASN ASP ILE ASP LYS ALA ILE THR VAL
SEQRES 35 C 500 SER SER ALA LEU GLN SER GLY THR VAL TRP VAL ASN CYS
SEQRES 36 C 500 TYR SER VAL VAL SER ALA GLN CYS PRO PHE GLY GLY PHE
SEQRES 37 C 500 LYS MET SER GLY ASN GLY ARG GLU LEU GLY GLU TYR GLY
SEQRES 38 C 500 PHE HIS GLU TYR THR GLU VAL LYS THR VAL THR ILE LYS
SEQRES 39 C 500 ILE SER GLN LYS ASN SER
SEQRES 1 D 500 SER SER SER ALA MET PRO ASP VAL PRO ALA PRO LEU THR
SEQRES 2 D 500 ASN LEU GLN PHE LYS TYR THR LYS ILE PHE ILE ASN ASN
SEQRES 3 D 500 GLU TRP HIS SER SER VAL SER GLY LYS LYS PHE PRO VAL
SEQRES 4 D 500 PHE ASN PRO ALA THR GLU GLU LYS LEU CYS GLU VAL GLU
SEQRES 5 D 500 GLU GLY ASP LYS GLU ASP VAL ASP LYS ALA VAL LYS ALA
SEQRES 6 D 500 ALA ARG GLN ALA PHE GLN ILE GLY SER PRO TRP ARG THR
SEQRES 7 D 500 MET ASP ALA SER GLU ARG GLY ARG LEU LEU ASN LYS LEU
SEQRES 8 D 500 ALA ASP LEU ILE GLU ARG ASP ARG LEU LEU LEU ALA THR
SEQRES 9 D 500 MET GLU ALA MET ASN GLY GLY LYS LEU PHE SER ASN ALA
SEQRES 10 D 500 TYR LEU MET ASP LEU GLY GLY CYS ILE LYS THR LEU ARG
SEQRES 11 D 500 TYR CYS ALA GLY TRP ALA ASP LYS ILE GLN GLY ARG THR
SEQRES 12 D 500 ILE PRO MET ASP GLY ASN PHE PHE THR TYR THR ARG SER
SEQRES 13 D 500 GLU PRO VAL GLY VAL CYS GLY GLN ILE ILE PRO TRP ASN
SEQRES 14 D 500 PHE PRO LEU LEU MET PHE LEU TRP LYS ILE GLY PRO ALA
SEQRES 15 D 500 LEU SER CYS GLY ASN THR VAL VAL VAL LYS PRO ALA GLU
SEQRES 16 D 500 GLN THR PRO LEU THR ALA LEU HIS MET GLY SER LEU ILE
SEQRES 17 D 500 LYS GLU ALA GLY PHE PRO PRO GLY VAL VAL ASN ILE VAL
SEQRES 18 D 500 PRO GLY TYR GLY PRO THR ALA GLY ALA ALA ILE SER SER
SEQRES 19 D 500 HIS MET ASP VAL ASP LYS VAL ALA PHE THR GLY SER THR
SEQRES 20 D 500 GLU VAL GLY LYS LEU ILE LYS GLU ALA ALA GLY LYS SER
SEQRES 21 D 500 ASN LEU LYS ARG VAL SER LEU GLU LEU GLY GLY LYS SER
SEQRES 22 D 500 PRO CYS ILE VAL PHE ALA ASP ALA ASP LEU ASP ASN ALA
SEQRES 23 D 500 VAL GLU PHE ALA HIS GLN GLY VAL PHE TYR HIS GLN GLY
SEQRES 24 D 500 GLN CYS CYS ILE ALA ALA SER ARG LEU PHE VAL GLU GLU
SEQRES 25 D 500 SER ILE TYR ASP GLU PHE VAL ARG ARG SER VAL GLU ARG
SEQRES 26 D 500 ALA LYS LYS TYR VAL LEU GLY ASN PRO LEU THR PRO GLY
SEQRES 27 D 500 VAL SER GLN GLY PRO GLN ILE ASP LYS GLU GLN TYR GLU
SEQRES 28 D 500 LYS ILE LEU ASP LEU ILE GLU SER GLY LYS LYS GLU GLY
SEQRES 29 D 500 ALA LYS LEU GLU CYS GLY GLY GLY PRO TRP GLY ASN LYS
SEQRES 30 D 500 GLY TYR PHE ILE GLN PRO THR VAL PHE SER ASP VAL THR
SEQRES 31 D 500 ASP ASP MET ARG ILE ALA LYS GLU GLU ILE PHE GLY PRO
SEQRES 32 D 500 VAL GLN GLN ILE MET LYS PHE LYS SER LEU ASP ASP VAL
SEQRES 33 D 500 ILE LYS ARG ALA ASN ASN THR PHE TYR GLY LEU SER ALA
SEQRES 34 D 500 GLY ILE PHE THR ASN ASP ILE ASP LYS ALA ILE THR VAL
SEQRES 35 D 500 SER SER ALA LEU GLN SER GLY THR VAL TRP VAL ASN CYS
SEQRES 36 D 500 TYR SER VAL VAL SER ALA GLN CYS PRO PHE GLY GLY PHE
SEQRES 37 D 500 LYS MET SER GLY ASN GLY ARG GLU LEU GLY GLU TYR GLY
SEQRES 38 D 500 PHE HIS GLU TYR THR GLU VAL LYS THR VAL THR ILE LYS
SEQRES 39 D 500 ILE SER GLN LYS ASN SER
HET TXE A 501 44
HET MG A 502 1
HET TXE B 501 44
HET MG B 502 1
HET TXE C 501 44
HET MG C 502 1
HET TXE D 501 44
HET MG D 502 1
HETNAM TXE [[(2R,3S,4R,5R)-5-[(3R)-3-AMINOCARBONYL-3,4-DIHYDRO-2H-
HETNAM 2 TXE PYRIDIN-1-YL]-3,4-BIS(OXIDANYL)OXOLAN-2-YL]METHOXY-
HETNAM 3 TXE OXIDANIDYL-PH OSPHORYL] [(2R,3S,4R,5R)-5-(6-
HETNAM 4 TXE AMINOPURIN-9-YL)-3,4-BIS(OXIDANYL)OXOLAN-2-YL]METHYL
HETNAM 5 TXE PHOSPHATE
HETNAM MG MAGNESIUM ION
HETSYN TXE 1,2,3,4-TETRAHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE
FORMUL 5 TXE 4(C21 H31 N7 O14 P2)
FORMUL 6 MG 4(MG 2+)
FORMUL 13 HOH *1340(H2 O)
HELIX 1 1 ASP A 55 PHE A 70 1 16
HELIX 2 2 SER A 74 MET A 79 1 6
HELIX 3 3 ASP A 80 ASP A 98 1 19
HELIX 4 4 ASP A 98 GLY A 111 1 14
HELIX 5 5 LEU A 113 MET A 120 1 8
HELIX 6 6 MET A 120 ALA A 136 1 17
HELIX 7 7 ASP A 137 ILE A 139 5 3
HELIX 8 8 PHE A 170 CYS A 185 1 16
HELIX 9 9 PRO A 198 GLY A 212 1 15
HELIX 10 10 THR A 227 SER A 234 1 8
HELIX 11 11 SER A 246 SER A 260 1 15
HELIX 12 12 ASP A 282 TYR A 296 1 15
HELIX 13 13 HIS A 297 GLN A 300 5 4
HELIX 14 14 GLU A 312 LYS A 327 1 16
HELIX 15 15 ASP A 346 GLY A 364 1 19
HELIX 16 16 MET A 393 GLU A 398 1 6
HELIX 17 17 SER A 412 ASN A 422 1 11
HELIX 18 18 ASP A 435 LEU A 446 1 12
HELIX 19 19 PHE A 468 MET A 470 5 3
HELIX 20 20 LEU A 477 GLU A 484 1 8
HELIX 21 21 ASP B 55 PHE B 70 1 16
HELIX 22 22 SER B 74 MET B 79 1 6
HELIX 23 23 ASP B 80 ASP B 98 1 19
HELIX 24 24 ASP B 98 GLY B 111 1 14
HELIX 25 25 LEU B 113 MET B 120 1 8
HELIX 26 26 MET B 120 ALA B 136 1 17
HELIX 27 27 ASP B 137 ILE B 139 5 3
HELIX 28 28 PHE B 170 CYS B 185 1 16
HELIX 29 29 PRO B 198 GLY B 212 1 15
HELIX 30 30 THR B 227 SER B 234 1 8
HELIX 31 31 SER B 246 SER B 260 1 15
HELIX 32 32 ASP B 282 TYR B 296 1 15
HELIX 33 33 HIS B 297 GLN B 300 5 4
HELIX 34 34 GLU B 312 LYS B 327 1 16
HELIX 35 35 ASP B 346 GLU B 363 1 18
HELIX 36 36 MET B 393 GLU B 398 1 6
HELIX 37 37 SER B 412 ASN B 422 1 11
HELIX 38 38 ASP B 435 LEU B 446 1 12
HELIX 39 39 PHE B 468 MET B 470 5 3
HELIX 40 40 LEU B 477 GLU B 484 1 8
HELIX 41 41 ASP C 55 PHE C 70 1 16
HELIX 42 42 SER C 74 MET C 79 1 6
HELIX 43 43 ASP C 80 ASP C 98 1 19
HELIX 44 44 ASP C 98 GLY C 111 1 14
HELIX 45 45 LEU C 113 MET C 120 1 8
HELIX 46 46 MET C 120 ALA C 136 1 17
HELIX 47 47 ASP C 137 ILE C 139 5 3
HELIX 48 48 PHE C 170 CYS C 185 1 16
HELIX 49 49 PRO C 198 GLY C 212 1 15
HELIX 50 50 THR C 227 SER C 234 1 8
HELIX 51 51 SER C 246 SER C 260 1 15
HELIX 52 52 ASP C 282 TYR C 296 1 15
HELIX 53 53 HIS C 297 GLN C 300 5 4
HELIX 54 54 GLU C 312 LYS C 327 1 16
HELIX 55 55 ASP C 346 GLU C 363 1 18
HELIX 56 56 MET C 393 GLU C 398 1 6
HELIX 57 57 SER C 412 ASN C 422 1 11
HELIX 58 58 ASP C 435 LEU C 446 1 12
HELIX 59 59 PHE C 468 MET C 470 5 3
HELIX 60 60 LEU C 477 GLU C 484 1 8
HELIX 61 61 ASP D 55 PHE D 70 1 16
HELIX 62 62 SER D 74 MET D 79 1 6
HELIX 63 63 ASP D 80 ASP D 98 1 19
HELIX 64 64 ASP D 98 GLY D 111 1 14
HELIX 65 65 LEU D 113 MET D 120 1 8
HELIX 66 66 MET D 120 ALA D 136 1 17
HELIX 67 67 ASP D 137 ILE D 139 5 3
HELIX 68 68 PHE D 170 CYS D 185 1 16
HELIX 69 69 PRO D 198 GLY D 212 1 15
HELIX 70 70 THR D 227 SER D 234 1 8
HELIX 71 71 SER D 246 SER D 260 1 15
HELIX 72 72 ASP D 282 TYR D 296 1 15
HELIX 73 73 HIS D 297 GLN D 300 5 4
HELIX 74 74 GLU D 312 LYS D 327 1 16
HELIX 75 75 ASP D 346 GLU D 363 1 18
HELIX 76 76 MET D 393 GLU D 398 1 6
HELIX 77 77 SER D 412 ASN D 422 1 11
HELIX 78 78 ASP D 435 LEU D 446 1 12
HELIX 79 79 PHE D 468 MET D 470 5 3
HELIX 80 80 LEU D 477 HIS D 483 1 7
SHEET 1 AA 2 ILE A 22 ILE A 24 0
SHEET 2 AA 2 GLU A 27 HIS A 29 -1 O GLU A 27 N ILE A 24
SHEET 1 AB 2 LYS A 36 PHE A 40 0
SHEET 2 AB 2 LYS A 47 GLU A 52 -1 N LEU A 48 O VAL A 39
SHEET 1 AC10 THR A 143 ILE A 144 0
SHEET 2 AC10 PHE A 150 PRO A 158 -1 O THR A 152 N ILE A 144
SHEET 3 AC10 THR A 486 LYS A 494 -1 O GLU A 487 N GLU A 157
SHEET 4 AC10 THR B 450 VAL B 453 1 O VAL B 451 N THR A 492
SHEET 5 AC10 SER B 428 PHE B 432 1 O ALA B 429 N TRP B 452
SHEET 6 AC10 PRO B 274 VAL B 277 1 O PRO B 274 N GLY B 430
SHEET 7 AC10 ARG B 307 GLU B 311 1 O ARG B 307 N CYS B 275
SHEET 8 AC10 VAL B 404 PHE B 410 1 O GLN B 406 N LEU B 308
SHEET 9 AC10 THR B 384 SER B 387 1 O THR B 384 N GLN B 405
SHEET 10 AC10 LYS B 366 CYS B 369 -1 O LYS B 366 N SER B 387
SHEET 1 AD 6 VAL A 218 ILE A 220 0
SHEET 2 AD 6 THR A 188 LYS A 192 1 O VAL A 189 N ASN A 219
SHEET 3 AD 6 VAL A 161 ILE A 165 1 O CYS A 162 N VAL A 190
SHEET 4 AD 6 LYS A 240 THR A 244 1 O LYS A 240 N GLY A 163
SHEET 5 AD 6 ARG A 264 GLU A 268 1 O ARG A 264 N VAL A 241
SHEET 6 AD 6 GLY A 472 ASN A 473 -1 O ASN A 473 N LEU A 267
SHEET 1 AE10 LYS A 366 CYS A 369 0
SHEET 2 AE10 THR A 384 SER A 387 -1 O VAL A 385 N GLU A 368
SHEET 3 AE10 VAL A 404 PHE A 410 1 O GLN A 405 N PHE A 386
SHEET 4 AE10 ARG A 307 GLU A 311 1 O LEU A 308 N MET A 408
SHEET 5 AE10 PRO A 274 VAL A 277 1 O CYS A 275 N PHE A 309
SHEET 6 AE10 SER A 428 PHE A 432 1 O GLY A 430 N ILE A 276
SHEET 7 AE10 THR A 450 VAL A 453 1 O THR A 450 N ALA A 429
SHEET 8 AE10 THR B 486 LYS B 494 1 O THR B 490 N VAL A 451
SHEET 9 AE10 PHE B 150 PRO B 158 -1 O PHE B 151 N ILE B 493
SHEET 10 AE10 THR B 143 ILE B 144 -1 N ILE B 144 O THR B 152
SHEET 1 AF 2 PRO A 373 TRP A 374 0
SHEET 2 AF 2 PHE A 380 ILE A 381 -1 O PHE A 380 N TRP A 374
SHEET 1 BA 2 ILE B 22 ILE B 24 0
SHEET 2 BA 2 GLU B 27 HIS B 29 -1 O GLU B 27 N ILE B 24
SHEET 1 BB 2 LYS B 36 PHE B 40 0
SHEET 2 BB 2 LYS B 47 GLU B 52 -1 N LEU B 48 O VAL B 39
SHEET 1 BC 6 VAL B 218 ILE B 220 0
SHEET 2 BC 6 THR B 188 LYS B 192 1 O VAL B 189 N ASN B 219
SHEET 3 BC 6 VAL B 161 ILE B 165 1 O CYS B 162 N VAL B 190
SHEET 4 BC 6 LYS B 240 THR B 244 1 O LYS B 240 N GLY B 163
SHEET 5 BC 6 ARG B 264 GLU B 268 1 O ARG B 264 N VAL B 241
SHEET 6 BC 6 GLY B 472 ASN B 473 -1 O ASN B 473 N LEU B 267
SHEET 1 BD 2 PRO B 373 TRP B 374 0
SHEET 2 BD 2 PHE B 380 ILE B 381 -1 O PHE B 380 N TRP B 374
SHEET 1 CA 2 ILE C 22 ILE C 24 0
SHEET 2 CA 2 GLU C 27 HIS C 29 -1 O GLU C 27 N ILE C 24
SHEET 1 CB 2 LYS C 36 PHE C 40 0
SHEET 2 CB 2 LYS C 47 GLU C 52 -1 N LEU C 48 O VAL C 39
SHEET 1 CC10 THR C 143 ILE C 144 0
SHEET 2 CC10 PHE C 150 PRO C 158 -1 O THR C 152 N ILE C 144
SHEET 3 CC10 THR C 486 LYS C 494 -1 O GLU C 487 N GLU C 157
SHEET 4 CC10 THR D 450 VAL D 453 1 O VAL D 451 N THR C 492
SHEET 5 CC10 SER D 428 PHE D 432 1 O ALA D 429 N TRP D 452
SHEET 6 CC10 PRO D 274 VAL D 277 1 O PRO D 274 N GLY D 430
SHEET 7 CC10 ARG D 307 GLU D 311 1 O ARG D 307 N CYS D 275
SHEET 8 CC10 VAL D 404 PHE D 410 1 O GLN D 406 N LEU D 308
SHEET 9 CC10 THR D 384 SER D 387 1 O THR D 384 N GLN D 405
SHEET 10 CC10 LYS D 366 CYS D 369 -1 O LYS D 366 N SER D 387
SHEET 1 CD 6 VAL C 218 ILE C 220 0
SHEET 2 CD 6 THR C 188 LYS C 192 1 O VAL C 189 N ASN C 219
SHEET 3 CD 6 VAL C 161 ILE C 165 1 O CYS C 162 N VAL C 190
SHEET 4 CD 6 LYS C 240 THR C 244 1 O LYS C 240 N GLY C 163
SHEET 5 CD 6 ARG C 264 GLU C 268 1 O ARG C 264 N VAL C 241
SHEET 6 CD 6 GLY C 472 ASN C 473 -1 O ASN C 473 N LEU C 267
SHEET 1 CE10 LYS C 366 CYS C 369 0
SHEET 2 CE10 THR C 384 SER C 387 -1 O VAL C 385 N GLU C 368
SHEET 3 CE10 VAL C 404 PHE C 410 1 O GLN C 405 N PHE C 386
SHEET 4 CE10 ARG C 307 GLU C 311 1 O LEU C 308 N MET C 408
SHEET 5 CE10 PRO C 274 VAL C 277 1 O CYS C 275 N PHE C 309
SHEET 6 CE10 SER C 428 PHE C 432 1 O GLY C 430 N ILE C 276
SHEET 7 CE10 THR C 450 VAL C 453 1 O THR C 450 N ALA C 429
SHEET 8 CE10 THR D 486 LYS D 494 1 O THR D 490 N VAL C 451
SHEET 9 CE10 PHE D 150 PRO D 158 -1 O PHE D 151 N ILE D 493
SHEET 10 CE10 THR D 143 ILE D 144 -1 N ILE D 144 O THR D 152
SHEET 1 CF 2 PRO C 373 TRP C 374 0
SHEET 2 CF 2 PHE C 380 ILE C 381 -1 O PHE C 380 N TRP C 374
SHEET 1 DA 2 ILE D 22 ILE D 24 0
SHEET 2 DA 2 GLU D 27 HIS D 29 -1 O GLU D 27 N ILE D 24
SHEET 1 DB 2 LYS D 36 PHE D 40 0
SHEET 2 DB 2 LYS D 47 GLU D 52 -1 N LEU D 48 O VAL D 39
SHEET 1 DC 6 VAL D 218 ILE D 220 0
SHEET 2 DC 6 THR D 188 LYS D 192 1 O VAL D 189 N ASN D 219
SHEET 3 DC 6 VAL D 161 ILE D 165 1 O CYS D 162 N VAL D 190
SHEET 4 DC 6 LYS D 240 THR D 244 1 O LYS D 240 N GLY D 163
SHEET 5 DC 6 ARG D 264 GLU D 268 1 O ARG D 264 N VAL D 241
SHEET 6 DC 6 GLY D 472 ASN D 473 -1 O ASN D 473 N LEU D 267
SHEET 1 DD 2 PRO D 373 TRP D 374 0
SHEET 2 DD 2 PHE D 380 ILE D 381 -1 O PHE D 380 N TRP D 374
LINK O1N TXE A 501 MG MG A 502 1555 1555 1.96
LINK O1P TXE A 501 MG MG A 502 1555 1555 2.30
LINK MG MG A 502 O HOH A2212 1555 1555 2.23
LINK MG MG A 502 O HOH A2216 1555 1555 2.07
LINK MG MG A 502 O HOH A2280 1555 1555 2.11
LINK MG MG A 502 O HOH A2360 1555 1555 2.01
LINK O2N TXE B 501 MG MG B 502 1555 1555 2.09
LINK O2P TXE B 501 MG MG B 502 1555 1555 2.10
LINK MG MG B 502 O HOH B2205 1555 1555 2.40
LINK MG MG B 502 O HOH B2209 1555 1555 1.97
LINK MG MG B 502 O HOH B2330 1555 1555 1.97
LINK O2P TXE C 501 MG MG C 502 1555 1555 2.09
LINK O1N TXE C 501 MG MG C 502 1555 1555 2.07
LINK MG MG C 502 O HOH C2205 1555 1555 2.28
LINK MG MG C 502 O HOH C2208 1555 1555 1.97
LINK MG MG C 502 O HOH C2278 1555 1555 2.26
LINK MG MG C 502 O HOH C2355 1555 1555 1.89
LINK O2P TXE D 501 MG MG D 502 1555 1555 2.19
LINK O2N TXE D 501 MG MG D 502 1555 1555 2.11
LINK MG MG D 502 O HOH D2187 1555 1555 2.42
LINK MG MG D 502 O HOH D2191 1555 1555 2.09
LINK MG MG D 502 O HOH D2240 1555 1555 2.28
LINK MG MG D 502 O HOH D2287 1555 1555 2.00
SITE 1 AC1 33 ILE A 165 ILE A 166 PRO A 167 TRP A 168
SITE 2 AC1 33 ASN A 169 LYS A 192 ALA A 194 GLU A 195
SITE 3 AC1 33 GLY A 225 GLY A 229 ALA A 230 PHE A 243
SITE 4 AC1 33 GLY A 245 SER A 246 VAL A 249 GLU A 268
SITE 5 AC1 33 GLY A 270 CYS A 302 GLU A 348 GLN A 349
SITE 6 AC1 33 LYS A 352 GLU A 399 MG A 502 HOH A2170
SITE 7 AC1 33 HOH A2182 HOH A2201 HOH A2212 HOH A2231
SITE 8 AC1 33 HOH A2280 HOH A2360 HOH A2361 HOH A2362
SITE 9 AC1 33 HOH A2363
SITE 1 AC2 5 TXE A 501 HOH A2212 HOH A2216 HOH A2280
SITE 2 AC2 5 HOH A2360
SITE 1 AC3 31 ILE B 165 ILE B 166 PRO B 167 TRP B 168
SITE 2 AC3 31 ASN B 169 LYS B 192 ALA B 194 GLU B 195
SITE 3 AC3 31 GLY B 225 GLY B 229 ALA B 230 PHE B 243
SITE 4 AC3 31 GLY B 245 SER B 246 VAL B 249 GLU B 268
SITE 5 AC3 31 GLY B 270 CYS B 302 GLU B 348 GLN B 349
SITE 6 AC3 31 LYS B 352 GLU B 399 PHE B 401 MG B 502
SITE 7 AC3 31 HOH B2168 HOH B2177 HOH B2181 HOH B2196
SITE 8 AC3 31 HOH B2217 HOH B2330 HOH B2332
SITE 1 AC4 4 TXE B 501 HOH B2205 HOH B2209 HOH B2330
SITE 1 AC5 34 HOH A2289 ILE C 165 ILE C 166 PRO C 167
SITE 2 AC5 34 TRP C 168 ASN C 169 LYS C 192 ALA C 194
SITE 3 AC5 34 GLU C 195 GLY C 225 GLY C 229 ALA C 230
SITE 4 AC5 34 PHE C 243 GLY C 245 SER C 246 VAL C 249
SITE 5 AC5 34 GLU C 268 LEU C 269 GLY C 270 CYS C 302
SITE 6 AC5 34 GLU C 348 GLN C 349 LYS C 352 GLU C 399
SITE 7 AC5 34 PHE C 401 MG C 502 HOH C2171 HOH C2179
SITE 8 AC5 34 HOH C2195 HOH C2205 HOH C2222 HOH C2278
SITE 9 AC5 34 HOH C2355 HOH C2356
SITE 1 AC6 5 TXE C 501 HOH C2205 HOH C2208 HOH C2278
SITE 2 AC6 5 HOH C2355
SITE 1 AC7 33 ILE D 165 ILE D 166 PRO D 167 TRP D 168
SITE 2 AC7 33 ASN D 169 LYS D 192 ALA D 194 GLU D 195
SITE 3 AC7 33 GLY D 225 GLY D 229 ALA D 230 PHE D 243
SITE 4 AC7 33 GLY D 245 SER D 246 VAL D 249 GLU D 268
SITE 5 AC7 33 GLY D 270 CYS D 302 GLU D 348 GLN D 349
SITE 6 AC7 33 LYS D 352 GLU D 399 PHE D 401 MG D 502
SITE 7 AC7 33 HOH D2154 HOH D2163 HOH D2177 HOH D2198
SITE 8 AC7 33 HOH D2240 HOH D2287 HOH D2288 HOH D2289
SITE 9 AC7 33 HOH D2290
SITE 1 AC8 5 TXE D 501 HOH D2187 HOH D2191 HOH D2240
SITE 2 AC8 5 HOH D2287
CRYST1 187.985 80.804 171.408 90.00 117.97 90.00 C 1 2 1 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 0.005320 0.000000 0.002825 0.00000
SCALE2 0.000000 0.012376 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006606 0.00000
MTRIX1 1 0.826400 0.000412 0.563200 -33.30000 1
MTRIX2 1 0.001694 -1.000000 -0.001755 95.41000 1
MTRIX3 1 0.563200 0.002404 -0.826000 107.80000 1
(ATOM LINES ARE NOT SHOWN.)
END
