HEADER TRANSCRIPTION/RNA 09-OCT-04 1XPU
TITLE STRUCTURAL MECHANISM OF INHIBITION OF THE RHO TRANSCRIPTION
TITLE 2 TERMINATION FACTOR BY THE ANTIBIOTIC 5A-(3-FORMYLPHENYLSULFANYL)-
TITLE 3 DIHYDROBICYCLOMYCIN (FPDB)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 5'-R(*CP*UP*CP*UP*CP*UP*CP*U)-3';
COMPND 3 CHAIN: G, M, H, J, K, L;
COMPND 4 ENGINEERED: YES;
COMPND 5 OTHER_DETAILS: SSRNA;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: RHO TRANSCRIPTION TERMINATION FACTOR;
COMPND 8 CHAIN: A, B, C, D, E, F;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 MOL_ID: 2;
SOURCE 4 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 5 ORGANISM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS RHO TRANSCRIPTION TERMINATION FACTOR; 5A-(3-FORMYLPHENYLSULFANYL)-
KEYWDS 2 DIHYDROBICYCLOMYCIN (FPDB); ATPGAMMAS, TRANSCRIPTION-RNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR E.SKORDALAKES,A.P.BROGAN,B.S.PARK,H.KOHN,J.M.BERGER
REVDAT 4 13-JUL-11 1XPU 1 VERSN
REVDAT 3 24-FEB-09 1XPU 1 VERSN
REVDAT 2 08-FEB-05 1XPU 1 JRNL AUTHOR REMARK
REVDAT 1 02-NOV-04 1XPU 0
JRNL AUTH E.SKORDALAKES,A.P.BROGAN,B.S.PARK,H.KOHN,J.M.BERGER
JRNL TITL STRUCTURAL MECHANISM OF INHIBITION OF THE RHO TRANSCRIPTION
JRNL TITL 2 TERMINATION FACTOR BY THE ANTIBIOTIC BICYCLOMYCIN
JRNL REF STRUCTURE V. 13 99 2005
JRNL REFN ISSN 0969-2126
JRNL PMID 15642265
JRNL DOI 10.1016/J.STR.2004.10.013
REMARK 2
REMARK 2 RESOLUTION. 3.05 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.05
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 86.5
REMARK 3 NUMBER OF REFLECTIONS : 54446
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) : 0.288
REMARK 3 R VALUE (WORKING SET) : 0.276
REMARK 3 FREE R VALUE : 0.295
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2885
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) : 3.05
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.13
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2505
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 83.79
REMARK 3 BIN R VALUE (WORKING SET) : 0.4710
REMARK 3 BIN FREE R VALUE SET COUNT : 133
REMARK 3 BIN FREE R VALUE : 0.4550
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 19271
REMARK 3 NUCLEIC ACID ATOMS : 240
REMARK 3 HETEROGEN ATOMS : 342
REMARK 3 SOLVENT ATOMS : 20
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 33.43
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.78000
REMARK 3 B22 (A**2) : 1.86000
REMARK 3 B33 (A**2) : 0.05000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.55000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.575
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.451
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 59.115
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.896
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.897
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 20163 ; 0.006 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 27253 ; 1.049 ; 2.004
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2423 ; 5.043 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 888 ;38.741 ;24.189
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 3731 ;17.536 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 162 ;12.791 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 3131 ; 0.061 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 14686 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 9802 ; 0.206 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 13711 ; 0.298 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 629 ; 0.174 ; 0.200
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): 51 ; 0.207 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 3 ; 0.118 ; 0.200
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): 12578 ; 0.002 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 19632 ; 0.002 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 8449 ; 0.005 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 7621 ; 0.008 ; 4.500
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 47
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 46
REMARK 3 ORIGIN FOR THE GROUP (A): -12.7176 -56.6920 -9.9670
REMARK 3 T TENSOR
REMARK 3 T11: 0.3094 T22: 0.0557
REMARK 3 T33: 0.4622 T12: -0.0844
REMARK 3 T13: 0.0028 T23: -0.1378
REMARK 3 L TENSOR
REMARK 3 L11: 4.8535 L22: 1.9041
REMARK 3 L33: 5.6001 L12: -0.7402
REMARK 3 L13: -2.0322 L23: -0.7652
REMARK 3 S TENSOR
REMARK 3 S11: -0.2990 S12: 0.2614 S13: -0.3272
REMARK 3 S21: -0.0364 S22: 0.2705 S23: 0.0407
REMARK 3 S31: 1.2126 S32: 0.5555 S33: 0.0285
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 : B 1 B 46
REMARK 3 ORIGIN FOR THE GROUP (A): -47.5334 -34.9588 19.1134
REMARK 3 T TENSOR
REMARK 3 T11: 0.1363 T22: 0.0022
REMARK 3 T33: 0.8480 T12: -0.2033
REMARK 3 T13: 0.0305 T23: 0.0028
REMARK 3 L TENSOR
REMARK 3 L11: 8.0032 L22: 0.6184
REMARK 3 L33: 1.0978 L12: -1.6509
REMARK 3 L13: 2.2781 L23: -0.1166
REMARK 3 S TENSOR
REMARK 3 S11: -0.4673 S12: -0.4593 S13: -0.5469
REMARK 3 S21: -0.2168 S22: -0.0716 S23: 1.0633
REMARK 3 S31: 0.0898 S32: -0.5782 S33: 0.5390
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 : C 1 C 46
REMARK 3 ORIGIN FOR THE GROUP (A): -52.6604 13.4007 28.1488
REMARK 3 T TENSOR
REMARK 3 T11: -0.2631 T22: 0.0143
REMARK 3 T33: 0.2851 T12: 0.1334
REMARK 3 T13: 0.0079 T23: 0.1337
REMARK 3 L TENSOR
REMARK 3 L11: 2.9470 L22: 6.9957
REMARK 3 L33: 5.6232 L12: 1.6400
REMARK 3 L13: -1.3432 L23: 0.5942
REMARK 3 S TENSOR
REMARK 3 S11: -0.1601 S12: 0.0490 S13: 0.0764
REMARK 3 S21: 0.0843 S22: 0.2226 S23: 0.8252
REMARK 3 S31: -0.2632 S32: 0.0147 S33: -0.0625
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 : D 1 D 46
REMARK 3 ORIGIN FOR THE GROUP (A): -16.8437 47.1866 21.0213
REMARK 3 T TENSOR
REMARK 3 T11: 0.2221 T22: -0.2590
REMARK 3 T33: 0.0082 T12: 0.2569
REMARK 3 T13: -0.0769 T23: 0.1321
REMARK 3 L TENSOR
REMARK 3 L11: 6.6432 L22: 5.7574
REMARK 3 L33: 5.4018 L12: 0.8199
REMARK 3 L13: -3.0012 L23: 1.2085
REMARK 3 S TENSOR
REMARK 3 S11: 0.2889 S12: 0.5592 S13: 1.1654
REMARK 3 S21: -0.3941 S22: -0.0682 S23: 0.4562
REMARK 3 S31: -0.5704 S32: -0.2285 S33: -0.2207
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 : E 1 E 46
REMARK 3 ORIGIN FOR THE GROUP (A): 29.6539 33.8078 8.3116
REMARK 3 T TENSOR
REMARK 3 T11: 0.3932 T22: -0.0701
REMARK 3 T33: 0.1824 T12: -0.0536
REMARK 3 T13: 0.3632 T23: 0.1923
REMARK 3 L TENSOR
REMARK 3 L11: 6.9151 L22: 2.8353
REMARK 3 L33: 3.4238 L12: -2.7975
REMARK 3 L13: -3.4423 L23: 2.3532
REMARK 3 S TENSOR
REMARK 3 S11: 0.2533 S12: 0.2796 S13: 0.8065
REMARK 3 S21: -0.0379 S22: -0.0904 S23: -0.5362
REMARK 3 S31: -0.4373 S32: 0.6057 S33: -0.1629
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 : F 1 F 46
REMARK 3 ORIGIN FOR THE GROUP (A): 45.2809 -12.7703 10.2366
REMARK 3 T TENSOR
REMARK 3 T11: 0.0109 T22: -0.0305
REMARK 3 T33: 0.0029 T12: 0.0500
REMARK 3 T13: 0.0937 T23: -0.1118
REMARK 3 L TENSOR
REMARK 3 L11: 3.1043 L22: 14.5750
REMARK 3 L33: 3.0721 L12: 0.3793
REMARK 3 L13: -1.1626 L23: 3.8466
REMARK 3 S TENSOR
REMARK 3 S11: -0.0554 S12: 0.1238 S13: -0.4836
REMARK 3 S21: -0.6069 S22: 0.4160 S23: -1.1841
REMARK 3 S31: 0.5314 S32: -0.1021 S33: -0.3606
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 47 A 155
REMARK 3 ORIGIN FOR THE GROUP (A): -25.1103 -44.2001 7.2309
REMARK 3 T TENSOR
REMARK 3 T11: -0.1099 T22: -0.2864
REMARK 3 T33: 0.0464 T12: -0.1505
REMARK 3 T13: 0.0099 T23: 0.0787
REMARK 3 L TENSOR
REMARK 3 L11: 1.4879 L22: 2.3476
REMARK 3 L33: 4.9496 L12: -0.6622
REMARK 3 L13: -0.1372 L23: 0.5599
REMARK 3 S TENSOR
REMARK 3 S11: -0.1093 S12: 0.1769 S13: -0.1049
REMARK 3 S21: 0.0441 S22: -0.0215 S23: 0.3527
REMARK 3 S31: 0.0096 S32: -0.4662 S33: 0.1309
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 47 B 155
REMARK 3 ORIGIN FOR THE GROUP (A): -48.1786 -13.4299 26.1169
REMARK 3 T TENSOR
REMARK 3 T11: -0.1334 T22: 0.0964
REMARK 3 T33: 0.4539 T12: 0.0197
REMARK 3 T13: 0.0339 T23: -0.0299
REMARK 3 L TENSOR
REMARK 3 L11: 1.6155 L22: 2.3240
REMARK 3 L33: 2.2877 L12: 0.5679
REMARK 3 L13: 0.1602 L23: 0.7905
REMARK 3 S TENSOR
REMARK 3 S11: 0.0057 S12: 0.2540 S13: -0.2236
REMARK 3 S21: -0.3307 S22: -0.0213 S23: 0.9059
REMARK 3 S31: 0.0402 S32: -0.1927 S33: 0.0156
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 : C 47 C 155
REMARK 3 ORIGIN FOR THE GROUP (A): -34.8933 28.0462 27.8675
REMARK 3 T TENSOR
REMARK 3 T11: -0.2354 T22: -0.0364
REMARK 3 T33: -0.0059 T12: 0.2096
REMARK 3 T13: -0.0771 T23: 0.0572
REMARK 3 L TENSOR
REMARK 3 L11: 3.2033 L22: 1.3769
REMARK 3 L33: 3.0803 L12: 1.0306
REMARK 3 L13: 1.1807 L23: 0.2399
REMARK 3 S TENSOR
REMARK 3 S11: -0.2614 S12: 0.5328 S13: 0.5282
REMARK 3 S21: -0.2500 S22: 0.3258 S23: 0.5740
REMARK 3 S31: -0.2619 S32: -0.2960 S33: -0.0644
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 : D 47 D 155
REMARK 3 ORIGIN FOR THE GROUP (A): 5.1780 41.0573 18.4421
REMARK 3 T TENSOR
REMARK 3 T11: 0.2817 T22: -0.2313
REMARK 3 T33: -0.0764 T12: 0.1683
REMARK 3 T13: 0.1899 T23: 0.1344
REMARK 3 L TENSOR
REMARK 3 L11: 3.6083 L22: 2.0795
REMARK 3 L33: 1.3304 L12: -0.6935
REMARK 3 L13: 0.6226 L23: 0.0813
REMARK 3 S TENSOR
REMARK 3 S11: 0.3357 S12: 0.8292 S13: 0.5001
REMARK 3 S21: -0.7536 S22: -0.1658 S23: -0.4609
REMARK 3 S31: -0.3884 S32: -0.0894 S33: -0.1699
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 : E 47 E 155
REMARK 3 ORIGIN FOR THE GROUP (A): 37.7100 13.0718 12.2176
REMARK 3 T TENSOR
REMARK 3 T11: -0.1937 T22: 0.0107
REMARK 3 T33: -0.0954 T12: -0.0031
REMARK 3 T13: 0.2332 T23: 0.0053
REMARK 3 L TENSOR
REMARK 3 L11: 0.5985 L22: 2.6490
REMARK 3 L33: 5.0348 L12: -0.5596
REMARK 3 L13: 1.1684 L23: -1.0495
REMARK 3 S TENSOR
REMARK 3 S11: 0.2150 S12: 0.1969 S13: 0.3977
REMARK 3 S21: -0.6652 S22: 0.0312 S23: -0.3794
REMARK 3 S31: -0.1604 S32: 0.1826 S33: -0.2462
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 : F 47 F 155
REMARK 3 ORIGIN FOR THE GROUP (A): 35.4737 -28.6162 23.7520
REMARK 3 T TENSOR
REMARK 3 T11: 0.1651 T22: -0.2382
REMARK 3 T33: -0.0411 T12: 0.0988
REMARK 3 T13: -0.1039 T23: -0.1418
REMARK 3 L TENSOR
REMARK 3 L11: 3.9138 L22: 1.6107
REMARK 3 L33: 4.2239 L12: 0.2894
REMARK 3 L13: 1.5509 L23: 0.6600
REMARK 3 S TENSOR
REMARK 3 S11: -0.0875 S12: -0.0257 S13: -0.4998
REMARK 3 S21: -0.2979 S22: 0.0211 S23: -0.1101
REMARK 3 S31: 0.4576 S32: -0.4089 S33: 0.0664
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 156 A 400
REMARK 3 ORIGIN FOR THE GROUP (A): -9.0905 -33.3686 25.4197
REMARK 3 T TENSOR
REMARK 3 T11: -0.1726 T22: -0.2035
REMARK 3 T33: 0.0007 T12: 0.1058
REMARK 3 T13: -0.0031 T23: 0.0179
REMARK 3 L TENSOR
REMARK 3 L11: 2.2773 L22: 3.0048
REMARK 3 L33: 3.7554 L12: -0.0515
REMARK 3 L13: 0.3204 L23: 0.2753
REMARK 3 S TENSOR
REMARK 3 S11: -0.0330 S12: -0.3100 S13: 0.0430
REMARK 3 S21: 0.3756 S22: 0.1360 S23: -0.3683
REMARK 3 S31: 0.2493 S32: 0.4823 S33: -0.1031
REMARK 3
REMARK 3 TLS GROUP : 14
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 156 B 400
REMARK 3 ORIGIN FOR THE GROUP (A): -27.0721 -12.3493 42.2763
REMARK 3 T TENSOR
REMARK 3 T11: -0.2334 T22: -0.2065
REMARK 3 T33: -0.0974 T12: -0.0005
REMARK 3 T13: 0.1392 T23: 0.0149
REMARK 3 L TENSOR
REMARK 3 L11: 2.1821 L22: 3.2495
REMARK 3 L33: 2.5851 L12: 0.2352
REMARK 3 L13: 0.2830 L23: 0.8476
REMARK 3 S TENSOR
REMARK 3 S11: 0.0351 S12: -0.3015 S13: -0.1884
REMARK 3 S21: 0.6754 S22: 0.0313 S23: 0.0563
REMARK 3 S31: 0.2814 S32: 0.1119 S33: -0.0664
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 156 C 400
REMARK 3 ORIGIN FOR THE GROUP (A): -19.0643 18.4395 46.8031
REMARK 3 T TENSOR
REMARK 3 T11: -0.3945 T22: -0.2686
REMARK 3 T33: -0.5014 T12: 0.1953
REMARK 3 T13: 0.0720 T23: -0.0328
REMARK 3 L TENSOR
REMARK 3 L11: 1.8061 L22: 3.5664
REMARK 3 L33: 3.1568 L12: 0.9368
REMARK 3 L13: 0.5595 L23: 0.7798
REMARK 3 S TENSOR
REMARK 3 S11: -0.0361 S12: -0.2180 S13: -0.1817
REMARK 3 S21: 0.4091 S22: 0.0611 S23: 0.2336
REMARK 3 S31: 0.1436 S32: -0.0463 S33: -0.0250
REMARK 3
REMARK 3 TLS GROUP : 16
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 156 D 400
REMARK 3 ORIGIN FOR THE GROUP (A): 10.5129 30.2112 41.7794
REMARK 3 T TENSOR
REMARK 3 T11: -0.2396 T22: -0.3508
REMARK 3 T33: -0.3191 T12: 0.0621
REMARK 3 T13: 0.0110 T23: -0.1152
REMARK 3 L TENSOR
REMARK 3 L11: 3.9845 L22: 2.1366
REMARK 3 L33: 2.6341 L12: -0.0471
REMARK 3 L13: 0.4381 L23: -0.1010
REMARK 3 S TENSOR
REMARK 3 S11: 0.0379 S12: -0.4843 S13: 0.2387
REMARK 3 S21: 0.4152 S22: 0.1840 S23: -0.6346
REMARK 3 S31: -0.2192 S32: 0.0990 S33: -0.2219
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 : E 156 E 400
REMARK 3 ORIGIN FOR THE GROUP (A): 37.1489 12.2695 38.5922
REMARK 3 T TENSOR
REMARK 3 T11: -0.4399 T22: -0.1731
REMARK 3 T33: -0.2252 T12: 0.0174
REMARK 3 T13: 0.0253 T23: -0.1942
REMARK 3 L TENSOR
REMARK 3 L11: 3.0895 L22: 2.4033
REMARK 3 L33: 3.3015 L12: -0.5296
REMARK 3 L13: 0.5078 L23: -0.8410
REMARK 3 S TENSOR
REMARK 3 S11: 0.0456 S12: -0.4339 S13: 0.3220
REMARK 3 S21: 0.4261 S22: 0.1200 S23: -0.3942
REMARK 3 S31: -0.1702 S32: 0.1220 S33: -0.1656
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 : F 156 F 400
REMARK 3 ORIGIN FOR THE GROUP (A): 39.2333 -18.4236 47.9121
REMARK 3 T TENSOR
REMARK 3 T11: -0.0510 T22: -0.0193
REMARK 3 T33: -0.2409 T12: 0.0821
REMARK 3 T13: -0.1677 T23: -0.0711
REMARK 3 L TENSOR
REMARK 3 L11: 1.8073 L22: 2.8198
REMARK 3 L33: 3.3025 L12: -0.2854
REMARK 3 L13: 0.4406 L23: -0.9375
REMARK 3 S TENSOR
REMARK 3 S11: 0.0964 S12: -0.4528 S13: -0.2779
REMARK 3 S21: 0.2503 S22: 0.0405 S23: 0.0487
REMARK 3 S31: 0.2501 S32: 0.0119 S33: -0.1369
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 401 A 417
REMARK 3 ORIGIN FOR THE GROUP (A): 0.8657 -46.4498 47.6915
REMARK 3 T TENSOR
REMARK 3 T11: 0.6019 T22: 0.5817
REMARK 3 T33: 0.7425 T12: 0.3393
REMARK 3 T13: -0.2992 T23: 0.0327
REMARK 3 L TENSOR
REMARK 3 L11: 0.8500 L22: 8.1197
REMARK 3 L33: 10.1963 L12: 2.0778
REMARK 3 L13: -2.4088 L23: -2.6869
REMARK 3 S TENSOR
REMARK 3 S11: 0.8786 S12: -0.5536 S13: -0.1083
REMARK 3 S21: 1.2787 S22: -1.4209 S23: 1.1395
REMARK 3 S31: -0.3554 S32: 1.2265 S33: 0.5423
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 : B 401 B 417
REMARK 3 ORIGIN FOR THE GROUP (A): -26.7523 -18.4131 69.0990
REMARK 3 T TENSOR
REMARK 3 T11: 0.8095 T22: 0.4081
REMARK 3 T33: 0.4261 T12: -0.1395
REMARK 3 T13: 0.1679 T23: 0.1982
REMARK 3 L TENSOR
REMARK 3 L11: 9.7262 L22: 6.5284
REMARK 3 L33: 20.4991 L12: 0.3014
REMARK 3 L13: 6.9319 L23: 10.2860
REMARK 3 S TENSOR
REMARK 3 S11: -0.7103 S12: -0.3016 S13: 1.4501
REMARK 3 S21: -0.7597 S22: 0.4886 S23: -0.3062
REMARK 3 S31: -0.9854 S32: 0.2051 S33: 0.2218
REMARK 3
REMARK 3 TLS GROUP : 21
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 401 C 417
REMARK 3 ORIGIN FOR THE GROUP (A): -19.6628 26.2637 73.0093
REMARK 3 T TENSOR
REMARK 3 T11: 0.3196 T22: 0.4394
REMARK 3 T33: -0.3221 T12: -0.0895
REMARK 3 T13: 0.1603 T23: 0.0842
REMARK 3 L TENSOR
REMARK 3 L11: 21.1904 L22: 18.4275
REMARK 3 L33: 10.1054 L12: -19.3994
REMARK 3 L13: -1.9584 L23: 4.3673
REMARK 3 S TENSOR
REMARK 3 S11: -0.4653 S12: 0.4395 S13: 0.7309
REMARK 3 S21: 0.3964 S22: 0.4454 S23: 0.3070
REMARK 3 S31: 0.3653 S32: 2.0784 S33: 0.0199
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 401 D 417
REMARK 3 ORIGIN FOR THE GROUP (A): 19.6261 43.3994 63.9475
REMARK 3 T TENSOR
REMARK 3 T11: 0.5281 T22: 0.2305
REMARK 3 T33: 0.2811 T12: 0.1482
REMARK 3 T13: -0.0804 T23: -0.3241
REMARK 3 L TENSOR
REMARK 3 L11: 26.2176 L22: 10.5398
REMARK 3 L33: 4.3082 L12: 1.1918
REMARK 3 L13: 10.4681 L23: 1.6367
REMARK 3 S TENSOR
REMARK 3 S11: 0.3928 S12: -0.0818 S13: 0.1881
REMARK 3 S21: 0.5337 S22: -1.1298 S23: -1.0121
REMARK 3 S31: -0.3639 S32: 1.1312 S33: 0.7370
REMARK 3
REMARK 3 TLS GROUP : 23
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 401 E 417
REMARK 3 ORIGIN FOR THE GROUP (A): 57.0323 20.3126 55.4088
REMARK 3 T TENSOR
REMARK 3 T11: 0.1598 T22: 0.3342
REMARK 3 T33: 0.5825 T12: -0.1434
REMARK 3 T13: -0.2097 T23: -0.3549
REMARK 3 L TENSOR
REMARK 3 L11: 8.8904 L22: 12.2862
REMARK 3 L33: 13.7598 L12: -5.8977
REMARK 3 L13: -2.4455 L23: -8.8461
REMARK 3 S TENSOR
REMARK 3 S11: -0.4171 S12: 0.2546 S13: 0.6278
REMARK 3 S21: -0.4675 S22: -0.0865 S23: -1.2065
REMARK 3 S31: -0.1162 S32: 1.0649 S33: 0.5036
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 : F 401 F 417
REMARK 3 ORIGIN FOR THE GROUP (A): 60.3563 -22.4992 63.9811
REMARK 3 T TENSOR
REMARK 3 T11: 0.2935 T22: 0.4169
REMARK 3 T33: 0.2548 T12: 0.0463
REMARK 3 T13: -0.3183 T23: 0.0364
REMARK 3 L TENSOR
REMARK 3 L11: 6.9909 L22: 2.3529
REMARK 3 L33: 5.9572 L12: -1.5215
REMARK 3 L13: -3.0036 L23: -2.4179
REMARK 3 S TENSOR
REMARK 3 S11: -0.1660 S12: -0.1732 S13: -1.6204
REMARK 3 S21: 0.2863 S22: -0.3695 S23: -0.1421
REMARK 3 S31: 0.8621 S32: -0.0646 S33: 0.5355
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 : A 1600 A 1600
REMARK 3 ORIGIN FOR THE GROUP (A): 5.6962 -36.1517 23.2751
REMARK 3 T TENSOR
REMARK 3 T11: 0.3306 T22: 0.2020
REMARK 3 T33: 0.4678 T12: -0.0855
REMARK 3 T13: 0.1227 T23: -0.1529
REMARK 3 L TENSOR
REMARK 3 L11: 78.7175 L22: 155.8946
REMARK 3 L33: 37.7651 L12: -20.9612
REMARK 3 L13: 25.2051 L23: -14.6970
REMARK 3 S TENSOR
REMARK 3 S11: 5.0919 S12: -0.5224 S13: -3.8439
REMARK 3 S21: 0.3098 S22: -2.0379 S23: 6.7354
REMARK 3 S31: 0.4746 S32: 4.0491 S33: -3.0541
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 2600 B 2600
REMARK 3 ORIGIN FOR THE GROUP (A): -20.2870 -25.6211 44.7036
REMARK 3 T TENSOR
REMARK 3 T11: 0.2201 T22: 0.1553
REMARK 3 T33: 0.2868 T12: 0.1602
REMARK 3 T13: -0.0081 T23: -0.2219
REMARK 3 L TENSOR
REMARK 3 L11: 28.6645 L22: 62.3266
REMARK 3 L33: 77.4511 L12: 25.4984
REMARK 3 L13: 23.1720 L23: -27.6357
REMARK 3 S TENSOR
REMARK 3 S11: 2.1246 S12: -2.7014 S13: 2.0955
REMARK 3 S21: 0.2562 S22: -0.0451 S23: -0.3772
REMARK 3 S31: 4.5849 S32: -3.4786 S33: -2.0795
REMARK 3
REMARK 3 TLS GROUP : 27
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 3600 C 3600
REMARK 3 ORIGIN FOR THE GROUP (A): -25.1039 7.0757 54.8640
REMARK 3 T TENSOR
REMARK 3 T11: 0.2160 T22: 0.3053
REMARK 3 T33: 0.2407 T12: -0.0358
REMARK 3 T13: -0.0422 T23: 0.0425
REMARK 3 L TENSOR
REMARK 3 L11: 147.7853 L22: 38.6946
REMARK 3 L33: 114.2259 L12: -40.7695
REMARK 3 L13: -73.2226 L23: 16.0394
REMARK 3 S TENSOR
REMARK 3 S11: -0.2609 S12: -3.2894 S13: -0.5409
REMARK 3 S21: -0.2988 S22: 1.0395 S23: 0.0134
REMARK 3 S31: 1.5102 S32: -4.8912 S33: -0.7787
REMARK 3
REMARK 3 TLS GROUP : 28
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 4600 D 4600
REMARK 3 ORIGIN FOR THE GROUP (A): -0.4985 31.6183 52.1148
REMARK 3 T TENSOR
REMARK 3 T11: 0.1341 T22: 0.0674
REMARK 3 T33: 0.1296 T12: 0.1758
REMARK 3 T13: 0.0810 T23: 0.1171
REMARK 3 L TENSOR
REMARK 3 L11: 8.5924 L22: 118.6106
REMARK 3 L33: 62.6333 L12: -20.1140
REMARK 3 L13: -5.7118 L23: 16.6287
REMARK 3 S TENSOR
REMARK 3 S11: -1.7712 S12: -0.5352 S13: -0.8078
REMARK 3 S21: 2.9117 S22: 2.5077 S23: 0.3019
REMARK 3 S31: -0.8570 S32: -0.7813 S33: -0.7364
REMARK 3
REMARK 3 TLS GROUP : 29
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 5600 E 5600
REMARK 3 ORIGIN FOR THE GROUP (A): 33.0863 25.1608 45.2385
REMARK 3 T TENSOR
REMARK 3 T11: 0.2423 T22: 0.1877
REMARK 3 T33: 0.2855 T12: -0.0019
REMARK 3 T13: 0.1540 T23: -0.0615
REMARK 3 L TENSOR
REMARK 3 L11: 134.5019 L22: 136.5481
REMARK 3 L33: 51.6405 L12: 77.3321
REMARK 3 L13: 46.3830 L23: 9.5003
REMARK 3 S TENSOR
REMARK 3 S11: 2.7385 S12: -1.7269 S13: 0.5281
REMARK 3 S21: 3.5984 S22: -2.7755 S23: -1.1398
REMARK 3 S31: -3.6632 S32: -1.8902 S33: 0.0369
REMARK 3
REMARK 3 TLS GROUP : 30
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 6600 E 6600
REMARK 3 ORIGIN FOR THE GROUP (A): 47.6932 -5.8447 48.0948
REMARK 3 T TENSOR
REMARK 3 T11: 0.2803 T22: 0.1010
REMARK 3 T33: 0.1112 T12: 0.0546
REMARK 3 T13: 0.0018 T23: -0.2144
REMARK 3 L TENSOR
REMARK 3 L11: 283.9218 L22: 1.4401
REMARK 3 L33: 23.1319 L12: 15.9043
REMARK 3 L13: 62.7635 L23: 1.2610
REMARK 3 S TENSOR
REMARK 3 S11: 0.9392 S12: -0.6312 S13: 4.8895
REMARK 3 S21: 0.7401 S22: -1.1326 S23: 1.5649
REMARK 3 S31: -0.7079 S32: 0.6203 S33: 0.1934
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 : A 1601 A 1601
REMARK 3 ORIGIN FOR THE GROUP (A): 1.0557 -33.5990 18.4731
REMARK 3 T TENSOR
REMARK 3 T11: 0.0171 T22: 0.0130
REMARK 3 T33: 0.0181 T12: 0.0309
REMARK 3 T13: -0.0056 T23: 0.0152
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: 0.0000 S12: 0.0000 S13: 0.0000
REMARK 3 S21: 0.0000 S22: 0.0000 S23: 0.0000
REMARK 3 S31: 0.0000 S32: 0.0000 S33: 0.0000
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 2601 B 2601
REMARK 3 ORIGIN FOR THE GROUP (A): -22.1731 -22.0120 37.5333
REMARK 3 T TENSOR
REMARK 3 T11: 0.0125 T22: -0.0056
REMARK 3 T33: 0.0041 T12: 0.0003
REMARK 3 T13: -0.0024 T23: 0.0204
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: 0.0000 S12: 0.0000 S13: 0.0000
REMARK 3 S21: 0.0000 S22: 0.0000 S23: 0.0000
REMARK 3 S31: 0.0000 S32: 0.0000 S33: 0.0000
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 : C 3601 C 3601
REMARK 3 ORIGIN FOR THE GROUP (A): -24.2423 9.9061 47.1923
REMARK 3 T TENSOR
REMARK 3 T11: 0.0023 T22: -0.0012
REMARK 3 T33: 0.0020 T12: -0.0077
REMARK 3 T13: 0.0094 T23: -0.0005
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: 0.0000 S12: 0.0000 S13: 0.0000
REMARK 3 S21: 0.0000 S22: 0.0000 S23: 0.0000
REMARK 3 S31: 0.0000 S32: 0.0000 S33: 0.0000
REMARK 3
REMARK 3 TLS GROUP : 34
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 4601 D 4601
REMARK 3 ORIGIN FOR THE GROUP (A): -1.7447 29.1904 45.4103
REMARK 3 T TENSOR
REMARK 3 T11: 0.0076 T22: 0.0105
REMARK 3 T33: 0.0094 T12: 0.0078
REMARK 3 T13: -0.0033 T23: -0.0062
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: 0.0000 S12: 0.0000 S13: 0.0000
REMARK 3 S21: 0.0000 S22: 0.0000 S23: 0.0000
REMARK 3 S31: 0.0000 S32: 0.0000 S33: 0.0000
REMARK 3
REMARK 3 TLS GROUP : 35
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 5601 E 5601
REMARK 3 ORIGIN FOR THE GROUP (A): 29.5851 21.9870 38.2423
REMARK 3 T TENSOR
REMARK 3 T11: 0.0003 T22: 0.0002
REMARK 3 T33: 0.0002 T12: 0.0002
REMARK 3 T13: 0.0007 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: 0.0000 S12: 0.0000 S13: 0.0000
REMARK 3 S21: 0.0000 S22: 0.0000 S23: 0.0000
REMARK 3 S31: 0.0000 S32: 0.0000 S33: 0.0000
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 : F 6601 F 6601
REMARK 3 ORIGIN FOR THE GROUP (A): 41.7393 -7.6903 44.0323
REMARK 3 T TENSOR
REMARK 3 T11: -0.0088 T22: 0.0161
REMARK 3 T33: 0.0214 T12: 0.0012
REMARK 3 T13: -0.0191 T23: 0.0086
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: 0.0000 S12: 0.0000 S13: 0.0000
REMARK 3 S21: 0.0000 S22: 0.0000 S23: 0.0000
REMARK 3 S31: 0.0000 S32: 0.0000 S33: 0.0000
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 2701 B 2701
REMARK 3 ORIGIN FOR THE GROUP (A): -17.0379 -20.5686 34.5414
REMARK 3 T TENSOR
REMARK 3 T11: -0.0028 T22: 0.1249
REMARK 3 T33: 0.0376 T12: -0.1451
REMARK 3 T13: 0.0567 T23: -0.1272
REMARK 3 L TENSOR
REMARK 3 L11: 594.8557 L22: 165.7645
REMARK 3 L33: 70.7835 L12:-132.2267
REMARK 3 L13: 92.0609 L23: 10.2200
REMARK 3 S TENSOR
REMARK 3 S11: -1.9750 S12: 1.4689 S13: 3.0710
REMARK 3 S21: -1.5265 S22: 3.4383 S23: -1.0158
REMARK 3 S31: 4.4239 S32: 4.3860 S33: -1.4633
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 : C 3701 C 3701
REMARK 3 ORIGIN FOR THE GROUP (A): -20.4122 3.2958 44.6420
REMARK 3 T TENSOR
REMARK 3 T11: 0.0636 T22: 0.2560
REMARK 3 T33: -0.0173 T12: 0.3936
REMARK 3 T13: -0.2502 T23: -0.1194
REMARK 3 L TENSOR
REMARK 3 L11: 131.6617 L22: 397.5977
REMARK 3 L33: 47.1520 L12: -73.8323
REMARK 3 L13: -28.0405 L23:-105.3877
REMARK 3 S TENSOR
REMARK 3 S11: 4.5667 S12: 2.8535 S13: 3.6357
REMARK 3 S21: 3.1241 S22: -6.1512 S23: 1.4800
REMARK 3 S31: 5.5396 S32: -1.0130 S33: 1.5845
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 : D 4701 D 4701
REMARK 3 ORIGIN FOR THE GROUP (A): -2.3328 22.7795 44.6399
REMARK 3 T TENSOR
REMARK 3 T11: 0.0677 T22: -0.0330
REMARK 3 T33: 0.0449 T12: 0.0164
REMARK 3 T13: -0.0797 T23: 0.0523
REMARK 3 L TENSOR
REMARK 3 L11: 176.0970 L22: 157.3889
REMARK 3 L33: 108.8209 L12: 114.5842
REMARK 3 L13:-110.9036 L23: -15.3452
REMARK 3 S TENSOR
REMARK 3 S11: -3.0842 S12: -5.8303 S13: -0.1858
REMARK 3 S21: -0.7516 S22: -6.0026 S23: -10.3086
REMARK 3 S31: 3.7369 S32: 1.6676 S33: 9.0868
REMARK 3
REMARK 3 TLS GROUP : 40
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 5701 E 5701
REMARK 3 ORIGIN FOR THE GROUP (A): 23.7542 18.9483 41.6600
REMARK 3 T TENSOR
REMARK 3 T11: 0.0616 T22: 0.0469
REMARK 3 T33: 0.1041 T12: -0.1023
REMARK 3 T13: 0.2235 T23: 0.2135
REMARK 3 L TENSOR
REMARK 3 L11: 195.5872 L22: 127.2709
REMARK 3 L33: 54.8086 L12: -52.8130
REMARK 3 L13: 27.0913 L23: 68.6443
REMARK 3 S TENSOR
REMARK 3 S11: -7.4401 S12: 1.6734 S13: 3.0270
REMARK 3 S21: 3.9525 S22: 2.4646 S23: -0.9836
REMARK 3 S31: 4.7222 S32: -4.1757 S33: 4.9756
REMARK 3
REMARK 3 TLS GROUP : 41
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : F 6701 F 6701
REMARK 3 ORIGIN FOR THE GROUP (A): 36.8405 -3.8759 45.2434
REMARK 3 T TENSOR
REMARK 3 T11: 0.1192 T22: 0.2172
REMARK 3 T33: -0.0053 T12: 0.2079
REMARK 3 T13: 0.2327 T23: -0.1404
REMARK 3 L TENSOR
REMARK 3 L11: 68.1408 L22: 581.0687
REMARK 3 L33: 240.0562 L12: -12.5312
REMARK 3 L13: -19.5072 L23: 214.5826
REMARK 3 S TENSOR
REMARK 3 S11: 2.5889 S12: 3.6415 S13: 0.7105
REMARK 3 S21: 5.9004 S22: -6.0321 S23: -6.0325
REMARK 3 S31: 0.5797 S32: -2.4697 S33: 3.4432
REMARK 3
REMARK 3 TLS GROUP : 42
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : G 1 G 2
REMARK 3 ORIGIN FOR THE GROUP (A): -24.2050 -36.5700 -7.5834
REMARK 3 T TENSOR
REMARK 3 T11: 0.0208 T22: -0.0602
REMARK 3 T33: -0.0037 T12: -0.1009
REMARK 3 T13: -0.1433 T23: -0.0404
REMARK 3 L TENSOR
REMARK 3 L11: 25.1336 L22: 18.9818
REMARK 3 L33: 51.3273 L12: -15.2293
REMARK 3 L13: 31.5899 L23: -29.7887
REMARK 3 S TENSOR
REMARK 3 S11: 0.3341 S12: 1.2647 S13: 1.8298
REMARK 3 S21: -0.0401 S22: -0.8308 S23: 1.9892
REMARK 3 S31: -1.2985 S32: 3.0148 S33: 0.4968
REMARK 3
REMARK 3 TLS GROUP : 43
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : M 1 M 2
REMARK 3 ORIGIN FOR THE GROUP (A): -43.1916 -13.3321 8.5606
REMARK 3 T TENSOR
REMARK 3 T11: 0.3546 T22: -0.0343
REMARK 3 T33: 0.3371 T12: 0.1566
REMARK 3 T13: 0.3099 T23: -0.1431
REMARK 3 L TENSOR
REMARK 3 L11: 298.0574 L22: 55.9636
REMARK 3 L33: 102.3434 L12: 8.0751
REMARK 3 L13: 95.1061 L23: -4.7278
REMARK 3 S TENSOR
REMARK 3 S11: -4.9850 S12: 4.5784 S13: 2.7196
REMARK 3 S21: 1.0749 S22: 0.9002 S23: -0.9330
REMARK 3 S31: -3.8975 S32: 2.6591 S33: 4.0849
REMARK 3
REMARK 3 TLS GROUP : 44
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : H 1 H 2
REMARK 3 ORIGIN FOR THE GROUP (A): -36.6628 17.3364 14.4106
REMARK 3 T TENSOR
REMARK 3 T11: 0.0208 T22: 0.3977
REMARK 3 T33: 0.2232 T12: -0.0215
REMARK 3 T13: 0.2157 T23: 0.1657
REMARK 3 L TENSOR
REMARK 3 L11: 71.2359 L22: 31.6489
REMARK 3 L33: 78.4304 L12: 6.1065
REMARK 3 L13: 20.8497 L23: 49.2345
REMARK 3 S TENSOR
REMARK 3 S11: 0.0983 S12: -0.8377 S13: -0.7907
REMARK 3 S21: -2.6331 S22: 0.5306 S23: 2.0722
REMARK 3 S31: 4.2752 S32: -0.9564 S33: -0.6289
REMARK 3
REMARK 3 TLS GROUP : 45
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : J 1 J 2
REMARK 3 ORIGIN FOR THE GROUP (A): -6.2358 32.5384 9.4617
REMARK 3 T TENSOR
REMARK 3 T11: -0.0222 T22: 0.2715
REMARK 3 T33: 0.3357 T12: -0.0019
REMARK 3 T13: 0.0279 T23: -0.1613
REMARK 3 L TENSOR
REMARK 3 L11: 17.5180 L22: 111.2439
REMARK 3 L33: 264.3293 L12: 10.6288
REMARK 3 L13: 39.9098 L23:-110.5892
REMARK 3 S TENSOR
REMARK 3 S11: 0.1542 S12: -0.0226 S13: 2.7801
REMARK 3 S21: -0.0992 S22: 3.1146 S23: 0.9128
REMARK 3 S31: 3.0970 S32: -1.4093 S33: -3.2688
REMARK 3
REMARK 3 TLS GROUP : 46
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : K 1 K 2
REMARK 3 ORIGIN FOR THE GROUP (A): 22.2621 13.6724 5.1592
REMARK 3 T TENSOR
REMARK 3 T11: 0.5418 T22: 0.5122
REMARK 3 T33: 0.3177 T12: -0.0698
REMARK 3 T13: -0.0687 T23: 0.2126
REMARK 3 L TENSOR
REMARK 3 L11: 43.3752 L22: 29.3309
REMARK 3 L33: 120.8896 L12: 6.7871
REMARK 3 L13: -54.7718 L23: -1.2389
REMARK 3 S TENSOR
REMARK 3 S11: 1.4528 S12: 2.7678 S13: -0.6994
REMARK 3 S21: -0.6988 S22: -0.4720 S23: 0.1477
REMARK 3 S31: 1.7029 S32: -7.4423 S33: -0.9808
REMARK 3
REMARK 3 TLS GROUP : 47
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : L 1 L 2
REMARK 3 ORIGIN FOR THE GROUP (A): 24.7346 -19.2476 14.2869
REMARK 3 T TENSOR
REMARK 3 T11: 0.4351 T22: 0.4382
REMARK 3 T33: 0.2466 T12: -0.0062
REMARK 3 T13: 0.0120 T23: 0.0894
REMARK 3 L TENSOR
REMARK 3 L11: 38.5773 L22: 110.8777
REMARK 3 L33: 152.1447 L12: -26.1495
REMARK 3 L13: 22.9645 L23: 93.8320
REMARK 3 S TENSOR
REMARK 3 S11: 1.5617 S12: -2.3257 S13: 1.7510
REMARK 3 S21: 1.4464 S22: -0.5709 S23: -2.6176
REMARK 3 S31: 0.7974 S32: 0.3236 S33: -0.9909
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 : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1XPU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-OCT-04.
REMARK 100 THE RCSB ID CODE IS RCSB030624.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.3.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.1000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 63215
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.97
REMARK 200 COMPLETENESS FOR SHELL (%) : 81.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.80
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.16
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, NA CACODYLATE, NACL,
REMARK 280 GLYCEROL, FOS-CHOLINE-12, PH 6.5, VAPOR DIFFUSION, TEMPERATURE
REMARK 280 293K
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 59.73850
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 103.46750
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 59.73850
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 103.46750
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, 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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: M, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: J, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 5
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: K, E
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 6
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, F
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 C G -4
REMARK 465 U G -3
REMARK 465 C G -2
REMARK 465 U G -1
REMARK 465 C G 0
REMARK 465 U G 3
REMARK 465 C M -4
REMARK 465 U M -3
REMARK 465 C M -2
REMARK 465 U M -1
REMARK 465 C M 0
REMARK 465 U M 3
REMARK 465 C H -4
REMARK 465 U H -3
REMARK 465 C H -2
REMARK 465 U H -1
REMARK 465 C H 0
REMARK 465 U H 3
REMARK 465 C J -4
REMARK 465 U J -3
REMARK 465 C J -2
REMARK 465 U J -1
REMARK 465 C J 0
REMARK 465 U J 3
REMARK 465 C K -4
REMARK 465 U K -3
REMARK 465 C K -2
REMARK 465 U K -1
REMARK 465 C K 0
REMARK 465 U K 3
REMARK 465 C L -4
REMARK 465 U L -3
REMARK 465 C L -2
REMARK 465 U L -1
REMARK 465 C L 0
REMARK 465 U L 3
REMARK 465 ALA A 127
REMARK 465 ARG A 128
REMARK 465 GLU A 148
REMARK 465 ARG A 149
REMARK 465 GLY A 150
REMARK 465 ASN A 151
REMARK 465 SER A 281
REMARK 465 GLY A 282
REMARK 465 LYS A 283
REMARK 465 ARG A 418
REMARK 465 SER A 419
REMARK 465 ALA B 127
REMARK 465 ARG B 128
REMARK 465 GLU B 148
REMARK 465 ARG B 149
REMARK 465 GLY B 150
REMARK 465 ASN B 151
REMARK 465 SER B 281
REMARK 465 GLY B 282
REMARK 465 LYS B 283
REMARK 465 ARG B 418
REMARK 465 SER B 419
REMARK 465 ALA C 127
REMARK 465 ARG C 128
REMARK 465 GLU C 148
REMARK 465 ARG C 149
REMARK 465 GLY C 150
REMARK 465 ASN C 151
REMARK 465 SER C 281
REMARK 465 GLY C 282
REMARK 465 LYS C 283
REMARK 465 ARG C 418
REMARK 465 SER C 419
REMARK 465 ALA D 127
REMARK 465 ARG D 128
REMARK 465 GLU D 148
REMARK 465 ARG D 149
REMARK 465 GLY D 150
REMARK 465 ASN D 151
REMARK 465 SER D 281
REMARK 465 GLY D 282
REMARK 465 LYS D 283
REMARK 465 ARG D 418
REMARK 465 SER D 419
REMARK 465 ALA E 127
REMARK 465 ARG E 128
REMARK 465 GLU E 148
REMARK 465 ARG E 149
REMARK 465 GLY E 150
REMARK 465 ASN E 151
REMARK 465 SER E 281
REMARK 465 GLY E 282
REMARK 465 LYS E 283
REMARK 465 VAL E 284
REMARK 465 ARG E 418
REMARK 465 SER E 419
REMARK 465 ALA F 127
REMARK 465 ARG F 128
REMARK 465 GLU F 148
REMARK 465 ARG F 149
REMARK 465 GLY F 150
REMARK 465 ASN F 151
REMARK 465 SER F 281
REMARK 465 GLY F 282
REMARK 465 LYS F 283
REMARK 465 ARG F 418
REMARK 465 SER F 419
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 NE ARG C 366 S1G AGS D 4600 2.12
REMARK 500 NE ARG A 366 S1G AGS B 2600 2.13
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 U H 1 C3' - O3' - P ANGL. DEV. = 7.9 DEGREES
REMARK 500 ASP A 77 CB - CG - OD2 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ASP B 156 CB - CG - OD2 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ASP D 77 CB - CG - OD2 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ASP E 77 CB - CG - OD2 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ASP F 233 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ASP F 290 CB - CG - OD2 ANGL. DEV. = 5.4 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 HIS A 42 29.66 -64.90
REMARK 500 ALA A 43 3.81 -68.74
REMARK 500 LYS A 44 63.94 -68.16
REMARK 500 SER A 45 121.04 -18.75
REMARK 500 LYS A 105 -168.53 -74.39
REMARK 500 LEU A 113 103.23 -58.82
REMARK 500 GLU A 125 30.27 -79.61
REMARK 500 GLU A 134 30.66 -143.81
REMARK 500 HIS A 140 -8.77 98.44
REMARK 500 SER A 153 -130.21 -159.96
REMARK 500 LYS A 181 81.47 57.38
REMARK 500 ALA A 182 6.94 -152.88
REMARK 500 MET A 341 130.95 -171.56
REMARK 500 PHE A 355 -167.85 -69.95
REMARK 500 PRO A 356 104.61 -17.84
REMARK 500 ALA A 357 38.54 -65.42
REMARK 500 ALA A 404 14.82 -66.84
REMARK 500 LYS A 407 -96.80 -87.54
REMARK 500 THR A 408 -56.75 -143.09
REMARK 500 PRO B 10 150.01 -48.98
REMARK 500 ASN B 20 5.88 -65.10
REMARK 500 GLU B 24 -123.87 -89.15
REMARK 500 ASN B 25 96.77 -68.26
REMARK 500 LEU B 26 -3.81 -143.95
REMARK 500 ALA B 43 38.63 -71.02
REMARK 500 ALA B 74 -163.86 -69.54
REMARK 500 ASP B 77 35.85 -93.44
REMARK 500 ASN B 90 82.57 46.15
REMARK 500 GLU B 106 -51.80 72.01
REMARK 500 TYR B 110 169.99 71.41
REMARK 500 LEU B 114 -95.21 -106.30
REMARK 500 GLU B 125 46.25 -84.33
REMARK 500 PHE B 133 -9.94 -54.64
REMARK 500 GLU B 134 19.30 -140.58
REMARK 500 SER B 153 -123.34 -117.28
REMARK 500 LYS B 181 78.93 54.56
REMARK 500 ALA B 182 -15.34 -144.93
REMARK 500 TYR B 197 -66.11 -103.18
REMARK 500 ILE B 209 -63.07 -100.62
REMARK 500 SER B 266 105.67 61.38
REMARK 500 ALA B 404 45.24 -74.25
REMARK 500 MET B 405 -28.24 -147.75
REMARK 500 THR B 406 -158.95 -122.33
REMARK 500 ASN C 25 79.24 64.81
REMARK 500 ARG C 28 63.50 -112.14
REMARK 500 GLN C 41 6.13 -69.08
REMARK 500 ALA C 43 50.19 -115.67
REMARK 500 LYS C 44 -85.54 -141.69
REMARK 500 SER C 45 107.54 -42.86
REMARK 500 GLU C 47 -14.06 160.88
REMARK 500
REMARK 500 THIS ENTRY HAS 127 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 PHE A 355 PRO A 356 -142.51
REMARK 500 PHE E 355 PRO E 356 -101.48
REMARK 500 PHE F 355 PRO F 356 -123.11
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 TYR B 110 25.0 L L OUTSIDE RANGE
REMARK 500 PHE E 355 20.5 L L OUTSIDE RANGE
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 A1601 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 185 OG1
REMARK 620 2 AGS A1600 O2B 80.5
REMARK 620 3 AGS A1600 O2G 132.7 76.1
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B2601 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR B 185 OG1
REMARK 620 2 AGS B2600 O2G 101.1
REMARK 620 3 HOH B2702 O 58.6 49.7
REMARK 620 4 FPD B2701 O6 152.1 78.8 128.5
REMARK 620 5 LYS B 184 NZ 100.0 85.9 116.2 52.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C3601 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR C 185 OG1
REMARK 620 2 ASP C 265 OD2 141.3
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D4601 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 AGS D4600 O2B
REMARK 620 2 THR D 185 OG1 71.9
REMARK 620 3 AGS D4600 O2G 74.4 142.5
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG F6601 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 FPD F6701 O6
REMARK 620 2 AGS E6600 O2B 101.2
REMARK 620 3 AGS E6600 O2G 58.4 68.6
REMARK 620 4 THR F 185 OG1 167.8 66.6 114.8
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 2601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 3601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 4601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG E 5601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG F 6601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AGS A 1600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AGS B 2600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FPD B 2701
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AGS C 3600
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FPD C 3701
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AGS D 4600
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FPD D 4701
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AGS E 5600
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FPD E 5701
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AGS E 6600
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FPD F 6701
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1XPO RELATED DB: PDB
REMARK 900 RELATED ID: 1XPR RELATED DB: PDB
DBREF 1XPU A 1 419 UNP P22869 MEMA_METCA 1 419
DBREF 1XPU B 1 419 UNP P22869 MEMA_METCA 1 419
DBREF 1XPU C 1 419 UNP P22869 MEMA_METCA 1 419
DBREF 1XPU D 1 419 UNP P22869 MEMA_METCA 1 419
DBREF 1XPU E 1 419 UNP P22869 MEMA_METCA 1 419
DBREF 1XPU F 1 419 UNP P22869 MEMA_METCA 1 419
DBREF 1XPU G -4 3 PDB 1XPU 1XPU -4 3
DBREF 1XPU M -4 3 PDB 1XPU 1XPU -4 3
DBREF 1XPU H -4 3 PDB 1XPU 1XPU -4 3
DBREF 1XPU J -4 3 PDB 1XPU 1XPU -4 3
DBREF 1XPU K -4 3 PDB 1XPU 1XPU -4 3
DBREF 1XPU L -4 3 PDB 1XPU 1XPU -4 3
SEQRES 1 G 8 C U C U C U C U
SEQRES 1 M 8 C U C U C U C U
SEQRES 1 H 8 C U C U C U C U
SEQRES 1 J 8 C U C U C U C U
SEQRES 1 K 8 C U C U C U C U
SEQRES 1 L 8 C U C U C U C U
SEQRES 1 A 419 MET ASN LEU THR GLU LEU LYS ASN THR PRO VAL SER GLU
SEQRES 2 A 419 LEU ILE THR LEU GLY GLU ASN MET GLY LEU GLU ASN LEU
SEQRES 3 A 419 ALA ARG MET ARG LYS GLN ASP ILE ILE PHE ALA ILE LEU
SEQRES 4 A 419 LYS GLN HIS ALA LYS SER GLY GLU ASP ILE PHE GLY ASP
SEQRES 5 A 419 GLY VAL LEU GLU ILE LEU GLN ASP GLY PHE GLY PHE LEU
SEQRES 6 A 419 ARG SER ALA ASP SER SER TYR LEU ALA GLY PRO ASP ASP
SEQRES 7 A 419 ILE TYR VAL SER PRO SER GLN ILE ARG ARG PHE ASN LEU
SEQRES 8 A 419 ARG THR GLY ASP THR ILE SER GLY LYS ILE ARG PRO PRO
SEQRES 9 A 419 LYS GLU GLY GLU ARG TYR PHE ALA LEU LEU LYS VAL ASN
SEQRES 10 A 419 GLU VAL ASN PHE ASP LYS PRO GLU ASN ALA ARG ASN LYS
SEQRES 11 A 419 ILE LEU PHE GLU ASN LEU THR PRO LEU HIS ALA ASN SER
SEQRES 12 A 419 ARG LEU ARG MET GLU ARG GLY ASN GLY SER THR GLU ASP
SEQRES 13 A 419 LEU THR ALA ARG VAL LEU ASP LEU ALA SER PRO ILE GLY
SEQRES 14 A 419 ARG GLY GLN ARG GLY LEU ILE VAL ALA PRO PRO LYS ALA
SEQRES 15 A 419 GLY LYS THR MET LEU LEU GLN ASN ILE ALA GLN SER ILE
SEQRES 16 A 419 ALA TYR ASN HIS PRO ASP CYS VAL LEU MET VAL LEU LEU
SEQRES 17 A 419 ILE ASP GLU ARG PRO GLU GLU VAL THR GLU MET GLN ARG
SEQRES 18 A 419 LEU VAL LYS GLY GLU VAL VAL ALA SER THR PHE ASP GLU
SEQRES 19 A 419 PRO ALA SER ARG HIS VAL GLN VAL ALA GLU MET VAL ILE
SEQRES 20 A 419 GLU LYS ALA LYS ARG LEU VAL GLU HIS LYS LYS ASP VAL
SEQRES 21 A 419 ILE ILE LEU LEU ASP SER ILE THR ARG LEU ALA ARG ALA
SEQRES 22 A 419 TYR ASN THR VAL VAL PRO ALA SER GLY LYS VAL LEU THR
SEQRES 23 A 419 GLY GLY VAL ASP ALA ASN ALA LEU HIS ARG PRO LYS ARG
SEQRES 24 A 419 PHE PHE GLY ALA ALA ARG ASN VAL GLU GLU GLY GLY SER
SEQRES 25 A 419 LEU THR ILE ILE ALA THR ALA LEU ILE ASP THR GLY SER
SEQRES 26 A 419 LYS MET ASP GLU VAL ILE TYR GLU GLU PHE LYS GLY THR
SEQRES 27 A 419 GLY ASN MET GLU LEU HIS LEU SER ARG LYS ILE ALA GLU
SEQRES 28 A 419 LYS ARG VAL PHE PRO ALA ILE ASP TYR ASN ARG SER GLY
SEQRES 29 A 419 THR ARG LYS GLU GLU LEU LEU THR THR GLN GLU GLU LEU
SEQRES 30 A 419 GLN LYS MET TRP ILE LEU ARG LYS ILE ILE HIS PRO MET
SEQRES 31 A 419 GLY GLU ILE ASP ALA MET GLU PHE LEU ILE ASN LYS LEU
SEQRES 32 A 419 ALA MET THR LYS THR ASN ASP ASP PHE PHE GLU MET MET
SEQRES 33 A 419 LYS ARG SER
SEQRES 1 B 419 MET ASN LEU THR GLU LEU LYS ASN THR PRO VAL SER GLU
SEQRES 2 B 419 LEU ILE THR LEU GLY GLU ASN MET GLY LEU GLU ASN LEU
SEQRES 3 B 419 ALA ARG MET ARG LYS GLN ASP ILE ILE PHE ALA ILE LEU
SEQRES 4 B 419 LYS GLN HIS ALA LYS SER GLY GLU ASP ILE PHE GLY ASP
SEQRES 5 B 419 GLY VAL LEU GLU ILE LEU GLN ASP GLY PHE GLY PHE LEU
SEQRES 6 B 419 ARG SER ALA ASP SER SER TYR LEU ALA GLY PRO ASP ASP
SEQRES 7 B 419 ILE TYR VAL SER PRO SER GLN ILE ARG ARG PHE ASN LEU
SEQRES 8 B 419 ARG THR GLY ASP THR ILE SER GLY LYS ILE ARG PRO PRO
SEQRES 9 B 419 LYS GLU GLY GLU ARG TYR PHE ALA LEU LEU LYS VAL ASN
SEQRES 10 B 419 GLU VAL ASN PHE ASP LYS PRO GLU ASN ALA ARG ASN LYS
SEQRES 11 B 419 ILE LEU PHE GLU ASN LEU THR PRO LEU HIS ALA ASN SER
SEQRES 12 B 419 ARG LEU ARG MET GLU ARG GLY ASN GLY SER THR GLU ASP
SEQRES 13 B 419 LEU THR ALA ARG VAL LEU ASP LEU ALA SER PRO ILE GLY
SEQRES 14 B 419 ARG GLY GLN ARG GLY LEU ILE VAL ALA PRO PRO LYS ALA
SEQRES 15 B 419 GLY LYS THR MET LEU LEU GLN ASN ILE ALA GLN SER ILE
SEQRES 16 B 419 ALA TYR ASN HIS PRO ASP CYS VAL LEU MET VAL LEU LEU
SEQRES 17 B 419 ILE ASP GLU ARG PRO GLU GLU VAL THR GLU MET GLN ARG
SEQRES 18 B 419 LEU VAL LYS GLY GLU VAL VAL ALA SER THR PHE ASP GLU
SEQRES 19 B 419 PRO ALA SER ARG HIS VAL GLN VAL ALA GLU MET VAL ILE
SEQRES 20 B 419 GLU LYS ALA LYS ARG LEU VAL GLU HIS LYS LYS ASP VAL
SEQRES 21 B 419 ILE ILE LEU LEU ASP SER ILE THR ARG LEU ALA ARG ALA
SEQRES 22 B 419 TYR ASN THR VAL VAL PRO ALA SER GLY LYS VAL LEU THR
SEQRES 23 B 419 GLY GLY VAL ASP ALA ASN ALA LEU HIS ARG PRO LYS ARG
SEQRES 24 B 419 PHE PHE GLY ALA ALA ARG ASN VAL GLU GLU GLY GLY SER
SEQRES 25 B 419 LEU THR ILE ILE ALA THR ALA LEU ILE ASP THR GLY SER
SEQRES 26 B 419 LYS MET ASP GLU VAL ILE TYR GLU GLU PHE LYS GLY THR
SEQRES 27 B 419 GLY ASN MET GLU LEU HIS LEU SER ARG LYS ILE ALA GLU
SEQRES 28 B 419 LYS ARG VAL PHE PRO ALA ILE ASP TYR ASN ARG SER GLY
SEQRES 29 B 419 THR ARG LYS GLU GLU LEU LEU THR THR GLN GLU GLU LEU
SEQRES 30 B 419 GLN LYS MET TRP ILE LEU ARG LYS ILE ILE HIS PRO MET
SEQRES 31 B 419 GLY GLU ILE ASP ALA MET GLU PHE LEU ILE ASN LYS LEU
SEQRES 32 B 419 ALA MET THR LYS THR ASN ASP ASP PHE PHE GLU MET MET
SEQRES 33 B 419 LYS ARG SER
SEQRES 1 C 419 MET ASN LEU THR GLU LEU LYS ASN THR PRO VAL SER GLU
SEQRES 2 C 419 LEU ILE THR LEU GLY GLU ASN MET GLY LEU GLU ASN LEU
SEQRES 3 C 419 ALA ARG MET ARG LYS GLN ASP ILE ILE PHE ALA ILE LEU
SEQRES 4 C 419 LYS GLN HIS ALA LYS SER GLY GLU ASP ILE PHE GLY ASP
SEQRES 5 C 419 GLY VAL LEU GLU ILE LEU GLN ASP GLY PHE GLY PHE LEU
SEQRES 6 C 419 ARG SER ALA ASP SER SER TYR LEU ALA GLY PRO ASP ASP
SEQRES 7 C 419 ILE TYR VAL SER PRO SER GLN ILE ARG ARG PHE ASN LEU
SEQRES 8 C 419 ARG THR GLY ASP THR ILE SER GLY LYS ILE ARG PRO PRO
SEQRES 9 C 419 LYS GLU GLY GLU ARG TYR PHE ALA LEU LEU LYS VAL ASN
SEQRES 10 C 419 GLU VAL ASN PHE ASP LYS PRO GLU ASN ALA ARG ASN LYS
SEQRES 11 C 419 ILE LEU PHE GLU ASN LEU THR PRO LEU HIS ALA ASN SER
SEQRES 12 C 419 ARG LEU ARG MET GLU ARG GLY ASN GLY SER THR GLU ASP
SEQRES 13 C 419 LEU THR ALA ARG VAL LEU ASP LEU ALA SER PRO ILE GLY
SEQRES 14 C 419 ARG GLY GLN ARG GLY LEU ILE VAL ALA PRO PRO LYS ALA
SEQRES 15 C 419 GLY LYS THR MET LEU LEU GLN ASN ILE ALA GLN SER ILE
SEQRES 16 C 419 ALA TYR ASN HIS PRO ASP CYS VAL LEU MET VAL LEU LEU
SEQRES 17 C 419 ILE ASP GLU ARG PRO GLU GLU VAL THR GLU MET GLN ARG
SEQRES 18 C 419 LEU VAL LYS GLY GLU VAL VAL ALA SER THR PHE ASP GLU
SEQRES 19 C 419 PRO ALA SER ARG HIS VAL GLN VAL ALA GLU MET VAL ILE
SEQRES 20 C 419 GLU LYS ALA LYS ARG LEU VAL GLU HIS LYS LYS ASP VAL
SEQRES 21 C 419 ILE ILE LEU LEU ASP SER ILE THR ARG LEU ALA ARG ALA
SEQRES 22 C 419 TYR ASN THR VAL VAL PRO ALA SER GLY LYS VAL LEU THR
SEQRES 23 C 419 GLY GLY VAL ASP ALA ASN ALA LEU HIS ARG PRO LYS ARG
SEQRES 24 C 419 PHE PHE GLY ALA ALA ARG ASN VAL GLU GLU GLY GLY SER
SEQRES 25 C 419 LEU THR ILE ILE ALA THR ALA LEU ILE ASP THR GLY SER
SEQRES 26 C 419 LYS MET ASP GLU VAL ILE TYR GLU GLU PHE LYS GLY THR
SEQRES 27 C 419 GLY ASN MET GLU LEU HIS LEU SER ARG LYS ILE ALA GLU
SEQRES 28 C 419 LYS ARG VAL PHE PRO ALA ILE ASP TYR ASN ARG SER GLY
SEQRES 29 C 419 THR ARG LYS GLU GLU LEU LEU THR THR GLN GLU GLU LEU
SEQRES 30 C 419 GLN LYS MET TRP ILE LEU ARG LYS ILE ILE HIS PRO MET
SEQRES 31 C 419 GLY GLU ILE ASP ALA MET GLU PHE LEU ILE ASN LYS LEU
SEQRES 32 C 419 ALA MET THR LYS THR ASN ASP ASP PHE PHE GLU MET MET
SEQRES 33 C 419 LYS ARG SER
SEQRES 1 D 419 MET ASN LEU THR GLU LEU LYS ASN THR PRO VAL SER GLU
SEQRES 2 D 419 LEU ILE THR LEU GLY GLU ASN MET GLY LEU GLU ASN LEU
SEQRES 3 D 419 ALA ARG MET ARG LYS GLN ASP ILE ILE PHE ALA ILE LEU
SEQRES 4 D 419 LYS GLN HIS ALA LYS SER GLY GLU ASP ILE PHE GLY ASP
SEQRES 5 D 419 GLY VAL LEU GLU ILE LEU GLN ASP GLY PHE GLY PHE LEU
SEQRES 6 D 419 ARG SER ALA ASP SER SER TYR LEU ALA GLY PRO ASP ASP
SEQRES 7 D 419 ILE TYR VAL SER PRO SER GLN ILE ARG ARG PHE ASN LEU
SEQRES 8 D 419 ARG THR GLY ASP THR ILE SER GLY LYS ILE ARG PRO PRO
SEQRES 9 D 419 LYS GLU GLY GLU ARG TYR PHE ALA LEU LEU LYS VAL ASN
SEQRES 10 D 419 GLU VAL ASN PHE ASP LYS PRO GLU ASN ALA ARG ASN LYS
SEQRES 11 D 419 ILE LEU PHE GLU ASN LEU THR PRO LEU HIS ALA ASN SER
SEQRES 12 D 419 ARG LEU ARG MET GLU ARG GLY ASN GLY SER THR GLU ASP
SEQRES 13 D 419 LEU THR ALA ARG VAL LEU ASP LEU ALA SER PRO ILE GLY
SEQRES 14 D 419 ARG GLY GLN ARG GLY LEU ILE VAL ALA PRO PRO LYS ALA
SEQRES 15 D 419 GLY LYS THR MET LEU LEU GLN ASN ILE ALA GLN SER ILE
SEQRES 16 D 419 ALA TYR ASN HIS PRO ASP CYS VAL LEU MET VAL LEU LEU
SEQRES 17 D 419 ILE ASP GLU ARG PRO GLU GLU VAL THR GLU MET GLN ARG
SEQRES 18 D 419 LEU VAL LYS GLY GLU VAL VAL ALA SER THR PHE ASP GLU
SEQRES 19 D 419 PRO ALA SER ARG HIS VAL GLN VAL ALA GLU MET VAL ILE
SEQRES 20 D 419 GLU LYS ALA LYS ARG LEU VAL GLU HIS LYS LYS ASP VAL
SEQRES 21 D 419 ILE ILE LEU LEU ASP SER ILE THR ARG LEU ALA ARG ALA
SEQRES 22 D 419 TYR ASN THR VAL VAL PRO ALA SER GLY LYS VAL LEU THR
SEQRES 23 D 419 GLY GLY VAL ASP ALA ASN ALA LEU HIS ARG PRO LYS ARG
SEQRES 24 D 419 PHE PHE GLY ALA ALA ARG ASN VAL GLU GLU GLY GLY SER
SEQRES 25 D 419 LEU THR ILE ILE ALA THR ALA LEU ILE ASP THR GLY SER
SEQRES 26 D 419 LYS MET ASP GLU VAL ILE TYR GLU GLU PHE LYS GLY THR
SEQRES 27 D 419 GLY ASN MET GLU LEU HIS LEU SER ARG LYS ILE ALA GLU
SEQRES 28 D 419 LYS ARG VAL PHE PRO ALA ILE ASP TYR ASN ARG SER GLY
SEQRES 29 D 419 THR ARG LYS GLU GLU LEU LEU THR THR GLN GLU GLU LEU
SEQRES 30 D 419 GLN LYS MET TRP ILE LEU ARG LYS ILE ILE HIS PRO MET
SEQRES 31 D 419 GLY GLU ILE ASP ALA MET GLU PHE LEU ILE ASN LYS LEU
SEQRES 32 D 419 ALA MET THR LYS THR ASN ASP ASP PHE PHE GLU MET MET
SEQRES 33 D 419 LYS ARG SER
SEQRES 1 E 419 MET ASN LEU THR GLU LEU LYS ASN THR PRO VAL SER GLU
SEQRES 2 E 419 LEU ILE THR LEU GLY GLU ASN MET GLY LEU GLU ASN LEU
SEQRES 3 E 419 ALA ARG MET ARG LYS GLN ASP ILE ILE PHE ALA ILE LEU
SEQRES 4 E 419 LYS GLN HIS ALA LYS SER GLY GLU ASP ILE PHE GLY ASP
SEQRES 5 E 419 GLY VAL LEU GLU ILE LEU GLN ASP GLY PHE GLY PHE LEU
SEQRES 6 E 419 ARG SER ALA ASP SER SER TYR LEU ALA GLY PRO ASP ASP
SEQRES 7 E 419 ILE TYR VAL SER PRO SER GLN ILE ARG ARG PHE ASN LEU
SEQRES 8 E 419 ARG THR GLY ASP THR ILE SER GLY LYS ILE ARG PRO PRO
SEQRES 9 E 419 LYS GLU GLY GLU ARG TYR PHE ALA LEU LEU LYS VAL ASN
SEQRES 10 E 419 GLU VAL ASN PHE ASP LYS PRO GLU ASN ALA ARG ASN LYS
SEQRES 11 E 419 ILE LEU PHE GLU ASN LEU THR PRO LEU HIS ALA ASN SER
SEQRES 12 E 419 ARG LEU ARG MET GLU ARG GLY ASN GLY SER THR GLU ASP
SEQRES 13 E 419 LEU THR ALA ARG VAL LEU ASP LEU ALA SER PRO ILE GLY
SEQRES 14 E 419 ARG GLY GLN ARG GLY LEU ILE VAL ALA PRO PRO LYS ALA
SEQRES 15 E 419 GLY LYS THR MET LEU LEU GLN ASN ILE ALA GLN SER ILE
SEQRES 16 E 419 ALA TYR ASN HIS PRO ASP CYS VAL LEU MET VAL LEU LEU
SEQRES 17 E 419 ILE ASP GLU ARG PRO GLU GLU VAL THR GLU MET GLN ARG
SEQRES 18 E 419 LEU VAL LYS GLY GLU VAL VAL ALA SER THR PHE ASP GLU
SEQRES 19 E 419 PRO ALA SER ARG HIS VAL GLN VAL ALA GLU MET VAL ILE
SEQRES 20 E 419 GLU LYS ALA LYS ARG LEU VAL GLU HIS LYS LYS ASP VAL
SEQRES 21 E 419 ILE ILE LEU LEU ASP SER ILE THR ARG LEU ALA ARG ALA
SEQRES 22 E 419 TYR ASN THR VAL VAL PRO ALA SER GLY LYS VAL LEU THR
SEQRES 23 E 419 GLY GLY VAL ASP ALA ASN ALA LEU HIS ARG PRO LYS ARG
SEQRES 24 E 419 PHE PHE GLY ALA ALA ARG ASN VAL GLU GLU GLY GLY SER
SEQRES 25 E 419 LEU THR ILE ILE ALA THR ALA LEU ILE ASP THR GLY SER
SEQRES 26 E 419 LYS MET ASP GLU VAL ILE TYR GLU GLU PHE LYS GLY THR
SEQRES 27 E 419 GLY ASN MET GLU LEU HIS LEU SER ARG LYS ILE ALA GLU
SEQRES 28 E 419 LYS ARG VAL PHE PRO ALA ILE ASP TYR ASN ARG SER GLY
SEQRES 29 E 419 THR ARG LYS GLU GLU LEU LEU THR THR GLN GLU GLU LEU
SEQRES 30 E 419 GLN LYS MET TRP ILE LEU ARG LYS ILE ILE HIS PRO MET
SEQRES 31 E 419 GLY GLU ILE ASP ALA MET GLU PHE LEU ILE ASN LYS LEU
SEQRES 32 E 419 ALA MET THR LYS THR ASN ASP ASP PHE PHE GLU MET MET
SEQRES 33 E 419 LYS ARG SER
SEQRES 1 F 419 MET ASN LEU THR GLU LEU LYS ASN THR PRO VAL SER GLU
SEQRES 2 F 419 LEU ILE THR LEU GLY GLU ASN MET GLY LEU GLU ASN LEU
SEQRES 3 F 419 ALA ARG MET ARG LYS GLN ASP ILE ILE PHE ALA ILE LEU
SEQRES 4 F 419 LYS GLN HIS ALA LYS SER GLY GLU ASP ILE PHE GLY ASP
SEQRES 5 F 419 GLY VAL LEU GLU ILE LEU GLN ASP GLY PHE GLY PHE LEU
SEQRES 6 F 419 ARG SER ALA ASP SER SER TYR LEU ALA GLY PRO ASP ASP
SEQRES 7 F 419 ILE TYR VAL SER PRO SER GLN ILE ARG ARG PHE ASN LEU
SEQRES 8 F 419 ARG THR GLY ASP THR ILE SER GLY LYS ILE ARG PRO PRO
SEQRES 9 F 419 LYS GLU GLY GLU ARG TYR PHE ALA LEU LEU LYS VAL ASN
SEQRES 10 F 419 GLU VAL ASN PHE ASP LYS PRO GLU ASN ALA ARG ASN LYS
SEQRES 11 F 419 ILE LEU PHE GLU ASN LEU THR PRO LEU HIS ALA ASN SER
SEQRES 12 F 419 ARG LEU ARG MET GLU ARG GLY ASN GLY SER THR GLU ASP
SEQRES 13 F 419 LEU THR ALA ARG VAL LEU ASP LEU ALA SER PRO ILE GLY
SEQRES 14 F 419 ARG GLY GLN ARG GLY LEU ILE VAL ALA PRO PRO LYS ALA
SEQRES 15 F 419 GLY LYS THR MET LEU LEU GLN ASN ILE ALA GLN SER ILE
SEQRES 16 F 419 ALA TYR ASN HIS PRO ASP CYS VAL LEU MET VAL LEU LEU
SEQRES 17 F 419 ILE ASP GLU ARG PRO GLU GLU VAL THR GLU MET GLN ARG
SEQRES 18 F 419 LEU VAL LYS GLY GLU VAL VAL ALA SER THR PHE ASP GLU
SEQRES 19 F 419 PRO ALA SER ARG HIS VAL GLN VAL ALA GLU MET VAL ILE
SEQRES 20 F 419 GLU LYS ALA LYS ARG LEU VAL GLU HIS LYS LYS ASP VAL
SEQRES 21 F 419 ILE ILE LEU LEU ASP SER ILE THR ARG LEU ALA ARG ALA
SEQRES 22 F 419 TYR ASN THR VAL VAL PRO ALA SER GLY LYS VAL LEU THR
SEQRES 23 F 419 GLY GLY VAL ASP ALA ASN ALA LEU HIS ARG PRO LYS ARG
SEQRES 24 F 419 PHE PHE GLY ALA ALA ARG ASN VAL GLU GLU GLY GLY SER
SEQRES 25 F 419 LEU THR ILE ILE ALA THR ALA LEU ILE ASP THR GLY SER
SEQRES 26 F 419 LYS MET ASP GLU VAL ILE TYR GLU GLU PHE LYS GLY THR
SEQRES 27 F 419 GLY ASN MET GLU LEU HIS LEU SER ARG LYS ILE ALA GLU
SEQRES 28 F 419 LYS ARG VAL PHE PRO ALA ILE ASP TYR ASN ARG SER GLY
SEQRES 29 F 419 THR ARG LYS GLU GLU LEU LEU THR THR GLN GLU GLU LEU
SEQRES 30 F 419 GLN LYS MET TRP ILE LEU ARG LYS ILE ILE HIS PRO MET
SEQRES 31 F 419 GLY GLU ILE ASP ALA MET GLU PHE LEU ILE ASN LYS LEU
SEQRES 32 F 419 ALA MET THR LYS THR ASN ASP ASP PHE PHE GLU MET MET
SEQRES 33 F 419 LYS ARG SER
HET MG A1601 1
HET MG B2601 1
HET MG C3601 1
HET MG D4601 1
HET MG E5601 1
HET MG F6601 1
HET AGS A1600 31
HET AGS B2600 31
HET FPD B2701 30
HET AGS C3600 31
HET FPD C3701 30
HET AGS D4600 31
HET FPD D4701 30
HET AGS E5600 31
HET FPD E5701 30
HET AGS E6600 31
HET FPD F6701 30
HETNAM MG MAGNESIUM ION
HETNAM AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER
HETNAM FPD 5A-(3-FORMYLPHENYLSULFANYL)-DIHYDROBICYCLOMYCIN
HETSYN AGS ATP GAMMA-S
FORMUL 13 MG 6(MG 2+)
FORMUL 19 AGS 6(C10 H16 N5 O12 P3 S)
FORMUL 21 FPD 5(C19 H24 N2 O8 S)
FORMUL 30 HOH *20(H2 O)
HELIX 1 1 ASN A 2 THR A 9 1 8
HELIX 2 2 PRO A 10 GLU A 19 1 10
HELIX 3 3 ASN A 20 GLY A 22 5 3
HELIX 4 4 ASN A 25 MET A 29 5 5
HELIX 5 5 ARG A 30 HIS A 42 1 13
HELIX 6 6 SER A 67 SER A 71 5 5
HELIX 7 7 SER A 82 ASN A 90 1 9
HELIX 8 8 ILE A 131 ASN A 135 5 5
HELIX 9 9 GLU A 155 SER A 166 1 12
HELIX 10 10 GLY A 183 HIS A 199 1 17
HELIX 11 11 ARG A 212 VAL A 223 1 12
HELIX 12 12 PRO A 235 GLU A 255 1 21
HELIX 13 13 SER A 266 VAL A 278 1 13
HELIX 14 14 LEU A 294 ALA A 303 1 10
HELIX 15 15 SER A 325 LYS A 336 1 12
HELIX 16 16 SER A 346 GLU A 351 1 6
HELIX 17 17 LYS A 367 THR A 372 5 6
HELIX 18 18 THR A 373 HIS A 388 1 16
HELIX 19 19 GLY A 391 ALA A 404 1 14
HELIX 20 20 ASN A 409 MET A 415 1 7
HELIX 21 21 ASN B 2 LYS B 7 1 6
HELIX 22 22 PRO B 10 ASN B 20 1 11
HELIX 23 23 ARG B 30 GLN B 41 1 12
HELIX 24 24 SER B 67 SER B 71 5 5
HELIX 25 25 SER B 82 ASN B 90 1 9
HELIX 26 26 ILE B 131 ASN B 135 5 5
HELIX 27 27 LEU B 139 ASN B 142 5 4
HELIX 28 28 GLU B 155 SER B 166 1 12
HELIX 29 29 GLY B 183 HIS B 199 1 17
HELIX 30 30 ARG B 212 VAL B 223 1 12
HELIX 31 31 PRO B 235 HIS B 256 1 22
HELIX 32 32 ILE B 267 VAL B 278 1 12
HELIX 33 33 ASP B 290 ALA B 293 5 4
HELIX 34 34 LEU B 294 ALA B 303 1 10
HELIX 35 35 SER B 325 GLU B 334 1 10
HELIX 36 36 SER B 346 LYS B 352 1 7
HELIX 37 37 LYS B 367 THR B 372 1 6
HELIX 38 38 THR B 373 HIS B 388 1 16
HELIX 39 39 GLY B 391 ALA B 404 1 14
HELIX 40 40 LYS B 407 ASP B 411 5 5
HELIX 41 41 PHE B 412 LYS B 417 1 6
HELIX 42 42 ASN C 2 THR C 9 1 8
HELIX 43 43 PRO C 10 ASN C 20 1 11
HELIX 44 44 ARG C 30 GLN C 41 1 12
HELIX 45 45 SER C 67 SER C 71 5 5
HELIX 46 46 SER C 82 PHE C 89 1 8
HELIX 47 47 ILE C 131 ASN C 135 5 5
HELIX 48 48 GLU C 155 SER C 166 1 12
HELIX 49 49 GLY C 183 HIS C 199 1 17
HELIX 50 50 ARG C 212 VAL C 223 1 12
HELIX 51 51 PRO C 235 GLU C 255 1 21
HELIX 52 52 SER C 266 VAL C 278 1 13
HELIX 53 53 LEU C 294 ALA C 303 1 10
HELIX 54 54 SER C 325 PHE C 335 1 11
HELIX 55 55 SER C 346 LYS C 352 1 7
HELIX 56 56 LYS C 367 LEU C 371 5 5
HELIX 57 57 THR C 373 HIS C 388 1 16
HELIX 58 58 GLY C 391 LYS C 402 1 12
HELIX 59 59 LYS C 407 MET C 416 1 10
HELIX 60 60 ASN D 2 ASN D 8 1 7
HELIX 61 61 PRO D 10 ASN D 20 1 11
HELIX 62 62 ARG D 30 GLN D 41 1 12
HELIX 63 63 SER D 67 SER D 71 5 5
HELIX 64 64 SER D 82 ASN D 90 1 9
HELIX 65 65 ILE D 131 ASN D 135 5 5
HELIX 66 66 GLU D 155 SER D 166 1 12
HELIX 67 67 GLY D 183 HIS D 199 1 17
HELIX 68 68 ARG D 212 VAL D 223 1 12
HELIX 69 69 PRO D 235 GLU D 255 1 21
HELIX 70 70 SER D 266 VAL D 278 1 13
HELIX 71 71 LEU D 294 ALA D 303 1 10
HELIX 72 72 SER D 325 LYS D 336 1 12
HELIX 73 73 SER D 346 LYS D 352 1 7
HELIX 74 74 THR D 373 HIS D 388 1 16
HELIX 75 75 GLY D 391 ALA D 404 1 14
HELIX 76 76 ASN D 409 GLU D 414 1 6
HELIX 77 77 ASN E 2 THR E 9 1 8
HELIX 78 78 PRO E 10 ASN E 20 1 11
HELIX 79 79 ASN E 25 MET E 29 5 5
HELIX 80 80 ARG E 30 HIS E 42 1 13
HELIX 81 81 SER E 67 SER E 71 5 5
HELIX 82 82 SER E 82 PHE E 89 1 8
HELIX 83 83 ILE E 131 ASN E 135 5 5
HELIX 84 84 GLU E 155 SER E 166 1 12
HELIX 85 85 LYS E 184 TYR E 197 1 14
HELIX 86 86 ARG E 212 VAL E 223 1 12
HELIX 87 87 PRO E 235 GLU E 255 1 21
HELIX 88 88 SER E 266 VAL E 278 1 13
HELIX 89 89 LEU E 294 ALA E 303 1 10
HELIX 90 90 SER E 325 LYS E 336 1 12
HELIX 91 91 SER E 346 LYS E 352 1 7
HELIX 92 92 LYS E 367 THR E 372 5 6
HELIX 93 93 THR E 373 HIS E 388 1 16
HELIX 94 94 GLY E 391 ALA E 404 1 14
HELIX 95 95 LYS E 407 LYS E 417 1 11
HELIX 96 96 ASN F 2 ASN F 8 1 7
HELIX 97 97 PRO F 10 ASN F 20 1 11
HELIX 98 98 ARG F 30 HIS F 42 1 13
HELIX 99 99 SER F 82 PHE F 89 1 8
HELIX 100 100 GLU F 155 SER F 166 1 12
HELIX 101 101 GLY F 183 HIS F 199 1 17
HELIX 102 102 ARG F 212 ARG F 221 1 10
HELIX 103 103 PRO F 235 GLU F 255 1 21
HELIX 104 104 SER F 266 VAL F 278 1 13
HELIX 105 105 LEU F 294 GLY F 302 1 9
HELIX 106 106 SER F 325 GLU F 334 1 10
HELIX 107 107 SER F 346 LYS F 352 1 7
HELIX 108 108 LYS F 367 LEU F 371 5 5
HELIX 109 109 THR F 373 HIS F 388 1 16
HELIX 110 110 GLY F 391 ALA F 404 1 14
HELIX 111 111 ASP F 410 MET F 415 1 6
SHEET 1 A 6 ILE A 49 ILE A 57 0
SHEET 2 A 6 GLY A 63 ARG A 66 -1 O ARG A 66 N VAL A 54
SHEET 3 A 6 ILE A 79 VAL A 81 -1 O VAL A 81 N GLY A 63
SHEET 4 A 6 PHE A 111 VAL A 119 1 O PHE A 111 N TYR A 80
SHEET 5 A 6 THR A 96 ARG A 102 -1 N LYS A 100 O LYS A 115
SHEET 6 A 6 ILE A 49 ILE A 57 -1 N ILE A 49 O ILE A 101
SHEET 1 B 5 GLU A 226 THR A 231 0
SHEET 2 B 5 VAL A 203 GLU A 211 1 N LEU A 208 O SER A 230
SHEET 3 B 5 ASP A 259 LEU A 264 1 O LEU A 263 N MET A 205
SHEET 4 B 5 SER A 312 LEU A 320 1 O THR A 314 N ILE A 262
SHEET 5 B 5 ARG A 305 ASN A 306 -1 N ARG A 305 O LEU A 313
SHEET 1 C 7 GLU A 226 THR A 231 0
SHEET 2 C 7 VAL A 203 GLU A 211 1 N LEU A 208 O SER A 230
SHEET 3 C 7 ASP A 259 LEU A 264 1 O LEU A 263 N MET A 205
SHEET 4 C 7 SER A 312 LEU A 320 1 O THR A 314 N ILE A 262
SHEET 5 C 7 ARG A 173 ALA A 178 1 N ILE A 176 O ALA A 319
SHEET 6 C 7 MET A 341 HIS A 344 1 O MET A 341 N LEU A 175
SHEET 7 C 7 GLY A 364 THR A 365 -1 O GLY A 364 N GLU A 342
SHEET 1 D 6 ASP B 52 ILE B 57 0
SHEET 2 D 6 GLY B 63 ARG B 66 -1 O ARG B 66 N VAL B 54
SHEET 3 D 6 ILE B 79 VAL B 81 -1 O VAL B 81 N GLY B 63
SHEET 4 D 6 ALA B 112 VAL B 116 1 O LEU B 113 N TYR B 80
SHEET 5 D 6 THR B 96 ARG B 102 -1 N LYS B 100 O LEU B 114
SHEET 6 D 6 ASP B 52 ILE B 57 -1 N GLY B 53 O ILE B 97
SHEET 1 E 2 ARG B 144 LEU B 145 0
SHEET 2 E 2 ILE B 168 GLY B 169 -1 O ILE B 168 N LEU B 145
SHEET 1 F 5 GLU B 226 THR B 231 0
SHEET 2 F 5 VAL B 203 GLU B 211 1 N VAL B 206 O GLU B 226
SHEET 3 F 5 ASP B 259 ASP B 265 1 O ASP B 265 N LEU B 207
SHEET 4 F 5 SER B 312 LEU B 320 1 O THR B 314 N ILE B 262
SHEET 5 F 5 ARG B 305 ASN B 306 -1 N ARG B 305 O LEU B 313
SHEET 1 G 7 GLU B 226 THR B 231 0
SHEET 2 G 7 VAL B 203 GLU B 211 1 N VAL B 206 O GLU B 226
SHEET 3 G 7 ASP B 259 ASP B 265 1 O ASP B 265 N LEU B 207
SHEET 4 G 7 SER B 312 LEU B 320 1 O THR B 314 N ILE B 262
SHEET 5 G 7 ARG B 173 ALA B 178 1 N ILE B 176 O ALA B 319
SHEET 6 G 7 MET B 341 HIS B 344 1 O LEU B 343 N LEU B 175
SHEET 7 G 7 GLY B 364 THR B 365 -1 O GLY B 364 N GLU B 342
SHEET 1 H 6 PHE C 50 LEU C 55 0
SHEET 2 H 6 GLY C 63 ARG C 66 -1 O ARG C 66 N VAL C 54
SHEET 3 H 6 ILE C 79 VAL C 81 -1 O VAL C 81 N GLY C 63
SHEET 4 H 6 ALA C 112 VAL C 119 1 O LEU C 113 N TYR C 80
SHEET 5 H 6 THR C 96 ARG C 102 -1 N LYS C 100 O LEU C 114
SHEET 6 H 6 PHE C 50 LEU C 55 -1 N GLY C 53 O ILE C 97
SHEET 1 I 5 GLU C 226 THR C 231 0
SHEET 2 I 5 VAL C 203 GLU C 211 1 N VAL C 206 O GLU C 226
SHEET 3 I 5 ASP C 259 ASP C 265 1 O ILE C 261 N VAL C 203
SHEET 4 I 5 SER C 312 LEU C 320 1 O THR C 314 N ILE C 262
SHEET 5 I 5 ARG C 305 ASN C 306 -1 N ARG C 305 O LEU C 313
SHEET 1 J 7 GLU C 226 THR C 231 0
SHEET 2 J 7 VAL C 203 GLU C 211 1 N VAL C 206 O GLU C 226
SHEET 3 J 7 ASP C 259 ASP C 265 1 O ILE C 261 N VAL C 203
SHEET 4 J 7 SER C 312 LEU C 320 1 O THR C 314 N ILE C 262
SHEET 5 J 7 ARG C 173 ALA C 178 1 N ILE C 176 O ALA C 319
SHEET 6 J 7 MET C 341 HIS C 344 1 O MET C 341 N LEU C 175
SHEET 7 J 7 GLY C 364 THR C 365 -1 O GLY C 364 N GLU C 342
SHEET 1 K 6 ASP D 52 ILE D 57 0
SHEET 2 K 6 GLY D 63 ARG D 66 -1 O ARG D 66 N VAL D 54
SHEET 3 K 6 ILE D 79 VAL D 81 -1 O ILE D 79 N LEU D 65
SHEET 4 K 6 ALA D 112 VAL D 116 1 O LEU D 113 N TYR D 80
SHEET 5 K 6 THR D 96 ARG D 102 -1 N ARG D 102 O ALA D 112
SHEET 6 K 6 ASP D 52 ILE D 57 -1 N GLY D 53 O ILE D 97
SHEET 1 L 5 GLU D 226 THR D 231 0
SHEET 2 L 5 VAL D 203 GLU D 211 1 N LEU D 204 O GLU D 226
SHEET 3 L 5 ASP D 259 ASP D 265 1 O ILE D 261 N VAL D 203
SHEET 4 L 5 SER D 312 LEU D 320 1 O SER D 312 N VAL D 260
SHEET 5 L 5 ARG D 305 ASN D 306 -1 N ARG D 305 O LEU D 313
SHEET 1 M 7 GLU D 226 THR D 231 0
SHEET 2 M 7 VAL D 203 GLU D 211 1 N LEU D 204 O GLU D 226
SHEET 3 M 7 ASP D 259 ASP D 265 1 O ILE D 261 N VAL D 203
SHEET 4 M 7 SER D 312 LEU D 320 1 O SER D 312 N VAL D 260
SHEET 5 M 7 ARG D 173 ALA D 178 1 N ILE D 176 O ALA D 317
SHEET 6 M 7 MET D 341 HIS D 344 1 O LEU D 343 N VAL D 177
SHEET 7 M 7 GLY D 364 THR D 365 -1 O GLY D 364 N GLU D 342
SHEET 1 N 6 PHE E 50 ILE E 57 0
SHEET 2 N 6 GLY E 63 ARG E 66 -1 O ARG E 66 N VAL E 54
SHEET 3 N 6 ILE E 79 VAL E 81 -1 O VAL E 81 N GLY E 63
SHEET 4 N 6 ALA E 112 VAL E 119 1 O LEU E 113 N TYR E 80
SHEET 5 N 6 THR E 96 ARG E 102 -1 N SER E 98 O GLU E 118
SHEET 6 N 6 PHE E 50 ILE E 57 -1 N GLY E 53 O ILE E 97
SHEET 1 O 2 ARG E 144 LEU E 145 0
SHEET 2 O 2 ILE E 168 GLY E 169 -1 O ILE E 168 N LEU E 145
SHEET 1 P 5 GLU E 226 THR E 231 0
SHEET 2 P 5 VAL E 203 GLU E 211 1 N VAL E 206 O VAL E 228
SHEET 3 P 5 ASP E 259 ASP E 265 1 O ILE E 261 N MET E 205
SHEET 4 P 5 SER E 312 LEU E 320 1 O THR E 314 N ILE E 262
SHEET 5 P 5 ARG E 305 ASN E 306 -1 N ARG E 305 O LEU E 313
SHEET 1 Q 7 GLU E 226 THR E 231 0
SHEET 2 Q 7 VAL E 203 GLU E 211 1 N VAL E 206 O VAL E 228
SHEET 3 Q 7 ASP E 259 ASP E 265 1 O ILE E 261 N MET E 205
SHEET 4 Q 7 SER E 312 LEU E 320 1 O THR E 314 N ILE E 262
SHEET 5 Q 7 ARG E 173 ALA E 178 1 N ILE E 176 O ALA E 319
SHEET 6 Q 7 MET E 341 HIS E 344 1 O MET E 341 N LEU E 175
SHEET 7 Q 7 GLY E 364 THR E 365 -1 O GLY E 364 N GLU E 342
SHEET 1 R 7 GLU F 118 VAL F 119 0
SHEET 2 R 7 THR F 96 ARG F 102 -1 N SER F 98 O GLU F 118
SHEET 3 R 7 ALA F 112 LEU F 113 -1 O ALA F 112 N ARG F 102
SHEET 4 R 7 ILE F 79 VAL F 81 1 N TYR F 80 O LEU F 113
SHEET 5 R 7 GLY F 63 ARG F 66 -1 N GLY F 63 O VAL F 81
SHEET 6 R 7 PHE F 50 ILE F 57 -1 N GLU F 56 O PHE F 64
SHEET 7 R 7 THR F 96 ARG F 102 -1 O GLY F 99 N GLY F 51
SHEET 1 S 2 ARG F 144 LEU F 145 0
SHEET 2 S 2 ILE F 168 GLY F 169 -1 O ILE F 168 N LEU F 145
SHEET 1 T 5 GLU F 226 THR F 231 0
SHEET 2 T 5 VAL F 203 GLU F 211 1 N VAL F 206 O VAL F 228
SHEET 3 T 5 ASP F 259 ASP F 265 1 O ILE F 261 N MET F 205
SHEET 4 T 5 SER F 312 LEU F 320 1 O THR F 314 N ILE F 262
SHEET 5 T 5 ARG F 305 ASN F 306 -1 N ARG F 305 O LEU F 313
SHEET 1 U 7 GLU F 226 THR F 231 0
SHEET 2 U 7 VAL F 203 GLU F 211 1 N VAL F 206 O VAL F 228
SHEET 3 U 7 ASP F 259 ASP F 265 1 O ILE F 261 N MET F 205
SHEET 4 U 7 SER F 312 LEU F 320 1 O THR F 314 N ILE F 262
SHEET 5 U 7 ARG F 173 ALA F 178 1 N ALA F 178 O ALA F 319
SHEET 6 U 7 MET F 341 HIS F 344 1 O LEU F 343 N LEU F 175
SHEET 7 U 7 GLY F 364 THR F 365 -1 O GLY F 364 N GLU F 342
SHEET 1 V 2 LEU F 285 THR F 286 0
SHEET 2 V 2 VAL F 289 ASP F 290 -1 O VAL F 289 N THR F 286
LINK MG MG A1601 OG1 THR A 185 1555 1555 2.33
LINK MG MG A1601 O2B AGS A1600 1555 1555 2.30
LINK MG MG A1601 O2G AGS A1600 1555 1555 2.43
LINK MG MG B2601 OG1 THR B 185 1555 1555 2.24
LINK MG MG B2601 O2G AGS B2600 1555 1555 2.91
LINK MG MG B2601 O HOH B2702 1555 1555 3.10
LINK MG MG B2601 O6 FPD B2701 1555 1555 3.13
LINK MG MG B2601 NZ LYS B 184 1555 1555 2.93
LINK MG MG C3601 OG1 THR C 185 1555 1555 2.65
LINK MG MG C3601 OD2 ASP C 265 1555 1555 2.66
LINK MG MG D4601 O2B AGS D4600 1555 1555 2.80
LINK MG MG D4601 OG1 THR D 185 1555 1555 2.35
LINK MG MG D4601 O2G AGS D4600 1555 1555 2.19
LINK NH2 ARG E 366 S1G AGS E6600 1555 1555 1.65
LINK CZ ARG E 366 S1G AGS E6600 1555 1555 1.93
LINK MG MG E5601 OG1 THR E 185 1555 1555 2.43
LINK MG MG F6601 O6 FPD F6701 1555 1555 3.15
LINK MG MG F6601 O2B AGS E6600 1555 1555 2.56
LINK MG MG F6601 O2G AGS E6600 1555 1555 2.49
LINK MG MG F6601 OG1 THR F 185 1555 1555 2.24
CISPEP 1 PHE B 355 PRO B 356 0 -11.89
CISPEP 2 PHE C 355 PRO C 356 0 -9.09
SITE 1 AC1 4 LYS A 184 THR A 185 GLU A 215 AGS A1600
SITE 1 AC2 5 LYS B 184 THR B 185 AGS B2600 FPD B2701
SITE 2 AC2 5 HOH B2702
SITE 1 AC3 4 LYS C 184 THR C 185 ASP C 265 AGS C3600
SITE 1 AC4 3 THR D 185 ARG D 212 AGS D4600
SITE 1 AC5 5 LYS E 184 THR E 185 GLU E 211 GLU E 215
SITE 2 AC5 5 AGS E5600
SITE 1 AC6 4 AGS E6600 LYS F 184 THR F 185 FPD F6701
SITE 1 AC7 9 THR A 158 LYS A 181 ALA A 182 GLY A 183
SITE 2 AC7 9 LYS A 184 THR A 185 MET A 186 PHE A 355
SITE 3 AC7 9 MG A1601
SITE 1 AC8 12 ARG A 366 THR B 158 PRO B 180 LYS B 181
SITE 2 AC8 12 ALA B 182 GLY B 183 LYS B 184 THR B 185
SITE 3 AC8 12 MET B 186 PHE B 355 MG B2601 HOH B2702
SITE 1 AC9 16 LYS A 336 GLY A 337 GLU A 342 ARG A 366
SITE 2 AC9 16 PRO B 180 LYS B 181 LYS B 184 ASP B 210
SITE 3 AC9 16 GLU B 211 ARG B 212 ASP B 265 SER B 266
SITE 4 AC9 16 ARG B 269 LEU B 320 THR B 323 MG B2601
SITE 1 BC1 11 ARG B 366 THR C 158 LYS C 181 ALA C 182
SITE 2 BC1 11 GLY C 183 LYS C 184 THR C 185 MET C 186
SITE 3 BC1 11 ARG C 212 PHE C 355 MG C3601
SITE 1 BC2 14 LYS B 336 GLY B 337 GLU B 342 ARG B 366
SITE 2 BC2 14 LYS C 181 LYS C 184 ASP C 210 GLU C 211
SITE 3 BC2 14 ARG C 212 ASP C 265 SER C 266 ARG C 269
SITE 4 BC2 14 LEU C 320 THR C 323
SITE 1 BC3 12 ARG C 366 THR D 158 LYS D 181 ALA D 182
SITE 2 BC3 12 GLY D 183 LYS D 184 THR D 185 MET D 186
SITE 3 BC3 12 ARG D 212 PHE D 355 MG D4601 FPD D4701
SITE 1 BC4 16 LYS C 336 GLY C 337 GLU C 342 ARG C 366
SITE 2 BC4 16 LYS D 181 LYS D 184 ILE D 209 ASP D 210
SITE 3 BC4 16 GLU D 211 ARG D 212 ASP D 265 SER D 266
SITE 4 BC4 16 ARG D 269 LEU D 320 THR D 323 AGS D4600
SITE 1 BC5 12 ARG D 366 THR E 158 LYS E 181 ALA E 182
SITE 2 BC5 12 GLY E 183 LYS E 184 THR E 185 MET E 186
SITE 3 BC5 12 ARG E 353 PHE E 355 MG E5601 FPD E5701
SITE 1 BC6 15 GLY D 337 GLU D 342 ARG D 366 PRO E 180
SITE 2 BC6 15 LYS E 181 LYS E 184 ASP E 210 GLU E 211
SITE 3 BC6 15 ARG E 212 ASP E 265 SER E 266 ARG E 269
SITE 4 BC6 15 LEU E 320 THR E 323 AGS E5600
SITE 1 BC7 11 ARG E 366 THR F 158 LYS F 181 ALA F 182
SITE 2 BC7 11 GLY F 183 LYS F 184 THR F 185 MET F 186
SITE 3 BC7 11 PHE F 355 MG F6601 FPD F6701
SITE 1 BC8 13 GLY E 337 GLU E 342 AGS E6600 PRO F 180
SITE 2 BC8 13 LYS F 181 LYS F 184 ILE F 209 GLU F 211
SITE 3 BC8 13 ASP F 265 SER F 266 ARG F 269 LEU F 320
SITE 4 BC8 13 MG F6601
CRYST1 119.477 206.935 148.607 90.00 96.95 90.00 C 1 2 1 24
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.008370 0.000000 0.001020 0.00000
SCALE2 0.000000 0.004832 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006779 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
