HEADER TRANSFERASE 12-OCT-16 5TMF
TITLE RE-REFINEMENT OF THERMUS THERMOPHILUS RNA POLYMERASE
CAVEAT 5TMF NE6 C 1201 HAS WRONG CHIRALITY AT ATOM C3
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA-DIRECTED RNA POLYMERASE SUBUNIT ALPHA;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: RNAP SUBUNIT ALPHA,RNA POLYMERASE SUBUNIT ALPHA,
COMPND 5 TRANSCRIPTASE SUBUNIT ALPHA;
COMPND 6 EC: 2.7.7.6;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: DNA-DIRECTED RNA POLYMERASE SUBUNIT BETA;
COMPND 9 CHAIN: C;
COMPND 10 SYNONYM: RNAP SUBUNIT BETA,RNA POLYMERASE SUBUNIT BETA,TRANSCRIPTASE
COMPND 11 SUBUNIT BETA;
COMPND 12 EC: 2.7.7.6;
COMPND 13 MOL_ID: 3;
COMPND 14 MOLECULE: DNA-DIRECTED RNA POLYMERASE SUBUNIT BETA';
COMPND 15 CHAIN: D;
COMPND 16 SYNONYM: RNAP SUBUNIT BETA',RNA POLYMERASE SUBUNIT BETA',
COMPND 17 TRANSCRIPTASE SUBUNIT BETA';
COMPND 18 EC: 2.7.7.6;
COMPND 19 MOL_ID: 4;
COMPND 20 MOLECULE: DNA-DIRECTED RNA POLYMERASE SUBUNIT OMEGA;
COMPND 21 CHAIN: E;
COMPND 22 SYNONYM: RNAP OMEGA SUBUNIT,RNA POLYMERASE OMEGA SUBUNIT,
COMPND 23 TRANSCRIPTASE SUBUNIT OMEGA;
COMPND 24 EC: 2.7.7.6;
COMPND 25 MOL_ID: 5;
COMPND 26 MOLECULE: RNA POLYMERASE SIGMA FACTOR SIGA;
COMPND 27 CHAIN: F
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 3 ORGANISM_TAXID: 274;
SOURCE 4 MOL_ID: 2;
SOURCE 5 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 6 ORGANISM_TAXID: 274;
SOURCE 7 MOL_ID: 3;
SOURCE 8 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 9 ORGANISM_TAXID: 274;
SOURCE 10 MOL_ID: 4;
SOURCE 11 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 12 ORGANISM_TAXID: 274;
SOURCE 13 MOL_ID: 5;
SOURCE 14 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 15 ORGANISM_TAXID: 274
KEYWDS SYMMETRY DOWNSHIFTING, VALIDATION OF SPACE GROUP, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.WANG
REVDAT 5 06-MAR-24 5TMF 1 REMARK
REVDAT 4 25-DEC-19 5TMF 1 REMARK
REVDAT 3 20-FEB-19 5TMF 1 REMARK
REVDAT 2 27-SEP-17 5TMF 1 REMARK
REVDAT 1 23-NOV-16 5TMF 0
JRNL AUTH J.WANG
JRNL TITL ON THE VALIDATION OF CRYSTALLOGRAPHIC SYMMETRY AND THE
JRNL TITL 2 QUALITY OF STRUCTURES.
JRNL REF PROTEIN SCI. V. 24 621 2015
JRNL REFN ESSN 1469-896X
JRNL PMID 25352397
JRNL DOI 10.1002/PRO.2595
REMARK 0
REMARK 0 THIS ENTRY 5TMF REFLECTS AN ALTERNATIVE MODELING OF THE
REMARK 0 STRUCTURAL DATA IN R3DXJSF ORIGINAL DATA DETERMINED BY
REMARK 0 AUTHOR: K.DAS,E.ARNOLD.
REMARK 0 ORIGINAL DATA REFERENCE 1
REMARK 0 PDB ID: 3DXJ
REMARK 0 AUTH J.MUKHOPADHYAY,K.DAS,S.ISMAIL,D.KOPPSTEIN,M.JANG,B.HUDSON,
REMARK 0 AUTH 2 S.SARAFIANOS,S.TUSKE,J.PATEL,R.JANSEN,H.IRSCHIK,E.ARNOLD,
REMARK 0 AUTH 3 R.H.EBRIGHT
REMARK 0 TITL THE RNA POLYMERASE "SWITCH REGION" IS A TARGET FOR
REMARK 0 TITL 2 INHIBITORS.
REMARK 0 REF CELL V. 135 295 2008
REMARK 0 REFN ISSN 1097-4172
REMARK 0 PMID 18957204
REMARK 0 DOI 10.1016/J.CELL.2008.09.033
REMARK 2
REMARK 2 RESOLUTION. 3.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.80
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.8
REMARK 3 NUMBER OF REFLECTIONS : 149560
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) : 0.203
REMARK 3 R VALUE (WORKING SET) : 0.203
REMARK 3 FREE R VALUE : 0.234
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 0.800
REMARK 3 FREE R VALUE TEST SET COUNT : 1206
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) : 3.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.07
REMARK 3 REFLECTION IN BIN (WORKING SET) : 8213
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 72.05
REMARK 3 BIN R VALUE (WORKING SET) : 0.4160
REMARK 3 BIN FREE R VALUE SET COUNT : 81
REMARK 3 BIN FREE R VALUE : 0.3970
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 27985
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 44
REMARK 3 SOLVENT ATOMS : 49
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 129.0
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.65000
REMARK 3 B22 (A**2) : 1.65000
REMARK 3 B33 (A**2) : -3.29000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.115
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.066
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.951
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.925
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 28533 ; 0.009 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 38574 ; 1.311 ; 1.990
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 3532 ; 6.571 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 1332 ;37.861 ;23.438
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 5176 ;21.462 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 292 ;18.038 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 4335 ; 0.092 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 21545 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 17619 ; 3.316 ; 6.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 28492 ; 5.823 ; 8.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 10914 ; 5.970 ; 8.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 10082 ; 9.881 ;12.000
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TWIN DETAILS
REMARK 3 NUMBER OF TWIN DOMAINS : 2
REMARK 3 TWIN DOMAIN : 1
REMARK 3 TWIN OPERATOR : H, K, L
REMARK 3 TWIN FRACTION : 0.956
REMARK 3 TWIN DOMAIN : 2
REMARK 3 TWIN OPERATOR : -H-K, K, -L
REMARK 3 TWIN FRACTION : 0.044
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 25
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 49
REMARK 3 RESIDUE RANGE : A 172 A 231
REMARK 3 ORIGIN FOR THE GROUP (A): -6.9410 134.7030 -31.0420
REMARK 3 T TENSOR
REMARK 3 T11: 0.4930 T22: 0.1847
REMARK 3 T33: 0.1465 T12: 0.0423
REMARK 3 T13: 0.0056 T23: -0.1521
REMARK 3 L TENSOR
REMARK 3 L11: 2.1897 L22: 4.6451
REMARK 3 L33: 3.5511 L12: 0.0925
REMARK 3 L13: 0.2509 L23: -0.2558
REMARK 3 S TENSOR
REMARK 3 S11: 0.1247 S12: 0.5095 S13: -0.5167
REMARK 3 S21: -0.0756 S22: -0.0530 S23: -0.1390
REMARK 3 S31: 0.6601 S32: 0.2760 S33: -0.0716
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 50 A 171
REMARK 3 ORIGIN FOR THE GROUP (A): -30.1080 158.4300 -43.1660
REMARK 3 T TENSOR
REMARK 3 T11: 0.5301 T22: 0.1594
REMARK 3 T33: 0.0373 T12: -0.1910
REMARK 3 T13: -0.0656 T23: -0.0177
REMARK 3 L TENSOR
REMARK 3 L11: 3.6606 L22: 4.0879
REMARK 3 L33: 3.8482 L12: -2.2355
REMARK 3 L13: 0.4481 L23: -0.3181
REMARK 3 S TENSOR
REMARK 3 S11: 0.0369 S12: 0.3606 S13: -0.1235
REMARK 3 S21: -0.6683 S22: -0.1155 S23: 0.1075
REMARK 3 S31: -0.2457 S32: 0.0874 S33: 0.0785
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 1 B 49
REMARK 3 RESIDUE RANGE : B 172 B 238
REMARK 3 ORIGIN FOR THE GROUP (A): 4.3450 144.7970 -26.2970
REMARK 3 T TENSOR
REMARK 3 T11: 0.1702 T22: 0.4023
REMARK 3 T33: 0.1517 T12: 0.0631
REMARK 3 T13: 0.0548 T23: -0.0665
REMARK 3 L TENSOR
REMARK 3 L11: 3.5834 L22: 3.4924
REMARK 3 L33: 3.2689 L12: 1.0557
REMARK 3 L13: 0.3203 L23: 0.7029
REMARK 3 S TENSOR
REMARK 3 S11: -0.1232 S12: 0.5268 S13: 0.1819
REMARK 3 S21: -0.2890 S22: 0.1862 S23: -0.3053
REMARK 3 S31: 0.1967 S32: 0.9102 S33: -0.0631
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 : B 50 B 171
REMARK 3 ORIGIN FOR THE GROUP (A): 24.1700 122.7270 -7.2630
REMARK 3 T TENSOR
REMARK 3 T11: 1.1810 T22: 1.1442
REMARK 3 T33: 0.8783 T12: 1.1259
REMARK 3 T13: -0.0383 T23: -0.2315
REMARK 3 L TENSOR
REMARK 3 L11: 7.9628 L22: 3.8879
REMARK 3 L33: 12.1718 L12: -1.1718
REMARK 3 L13: 2.9547 L23: -2.9477
REMARK 3 S TENSOR
REMARK 3 S11: 0.3000 S12: 0.1386 S13: -0.9731
REMARK 3 S21: -0.4924 S22: -0.3602 S23: -0.4167
REMARK 3 S31: 2.3908 S32: 2.3448 S33: 0.0601
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 1 C 8
REMARK 3 RESIDUE RANGE : C 669 C 704
REMARK 3 RESIDUE RANGE : C 829 C 1004
REMARK 3 ORIGIN FOR THE GROUP (A): -23.5500 146.0960 -11.8790
REMARK 3 T TENSOR
REMARK 3 T11: 0.3798 T22: 0.0417
REMARK 3 T33: 0.1929 T12: -0.0939
REMARK 3 T13: -0.0007 T23: -0.0259
REMARK 3 L TENSOR
REMARK 3 L11: 1.2242 L22: 1.1347
REMARK 3 L33: 1.8920 L12: -0.3425
REMARK 3 L13: 0.0802 L23: -0.2247
REMARK 3 S TENSOR
REMARK 3 S11: -0.0491 S12: 0.1287 S13: -0.0894
REMARK 3 S21: -0.0782 S22: 0.0570 S23: 0.0728
REMARK 3 S31: 0.3789 S32: -0.0844 S33: -0.0079
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 9 C 16
REMARK 3 RESIDUE RANGE : C 390 C 540
REMARK 3 ORIGIN FOR THE GROUP (A): -48.6590 161.5990 8.1040
REMARK 3 T TENSOR
REMARK 3 T11: 0.0853 T22: 0.2126
REMARK 3 T33: 0.1982 T12: -0.0060
REMARK 3 T13: 0.0176 T23: 0.0330
REMARK 3 L TENSOR
REMARK 3 L11: 1.5636 L22: 3.7213
REMARK 3 L33: 2.4607 L12: 1.0697
REMARK 3 L13: -0.2924 L23: -1.2126
REMARK 3 S TENSOR
REMARK 3 S11: -0.0445 S12: -0.2410 S13: 0.0536
REMARK 3 S21: 0.1350 S22: 0.0851 S23: 0.1522
REMARK 3 S31: -0.1642 S32: -0.4440 S33: -0.0407
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 17 C 142
REMARK 3 RESIDUE RANGE : C 324 C 389
REMARK 3 ORIGIN FOR THE GROUP (A): -60.2250 190.7520 -4.8250
REMARK 3 T TENSOR
REMARK 3 T11: 0.6472 T22: 0.5103
REMARK 3 T33: 0.4486 T12: 0.5447
REMARK 3 T13: 0.0353 T23: 0.1192
REMARK 3 L TENSOR
REMARK 3 L11: 1.3165 L22: 3.1221
REMARK 3 L33: 2.5896 L12: 0.4620
REMARK 3 L13: -0.5663 L23: -0.0189
REMARK 3 S TENSOR
REMARK 3 S11: 0.0672 S12: 0.2787 S13: 0.3896
REMARK 3 S21: 0.2200 S22: 0.1548 S23: 0.7171
REMARK 3 S31: -1.1380 S32: -1.0603 S33: -0.2221
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 : C 143 C 323
REMARK 3 ORIGIN FOR THE GROUP (A): -59.7110 188.6220 28.9030
REMARK 3 T TENSOR
REMARK 3 T11: 1.6934 T22: 0.3698
REMARK 3 T33: 0.8216 T12: 0.1937
REMARK 3 T13: 0.3464 T23: -0.3363
REMARK 3 L TENSOR
REMARK 3 L11: 5.3893 L22: 15.5302
REMARK 3 L33: 4.6030 L12: -5.1510
REMARK 3 L13: -0.3002 L23: -0.2070
REMARK 3 S TENSOR
REMARK 3 S11: -0.2609 S12: 0.0146 S13: 0.0796
REMARK 3 S21: 2.8072 S22: -0.6645 S23: 2.1933
REMARK 3 S31: -1.8433 S32: -0.8110 S33: 0.9254
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 541 C 668
REMARK 3 ORIGIN FOR THE GROUP (A): -45.7120 160.7540 -18.9700
REMARK 3 T TENSOR
REMARK 3 T11: 0.2087 T22: 0.2397
REMARK 3 T33: 0.2094 T12: -0.0824
REMARK 3 T13: -0.0909 T23: -0.0011
REMARK 3 L TENSOR
REMARK 3 L11: 2.3770 L22: 1.2584
REMARK 3 L33: 5.6979 L12: -1.0328
REMARK 3 L13: 1.7798 L23: -0.8181
REMARK 3 S TENSOR
REMARK 3 S11: 0.0970 S12: 0.0544 S13: -0.2117
REMARK 3 S21: -0.1456 S22: -0.0011 S23: 0.2535
REMARK 3 S31: -0.0658 S32: -0.8206 S33: -0.0958
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 : C 705 C 828
REMARK 3 ORIGIN FOR THE GROUP (A): -26.7920 194.0110 -32.9400
REMARK 3 T TENSOR
REMARK 3 T11: 0.6703 T22: 0.0952
REMARK 3 T33: 0.2194 T12: -0.0803
REMARK 3 T13: -0.1918 T23: 0.0850
REMARK 3 L TENSOR
REMARK 3 L11: 5.7128 L22: 4.8136
REMARK 3 L33: 2.6340 L12: 2.9119
REMARK 3 L13: -0.4184 L23: -1.9031
REMARK 3 S TENSOR
REMARK 3 S11: -0.2166 S12: 0.2566 S13: 0.5858
REMARK 3 S21: -0.7166 S22: 0.0808 S23: 0.2376
REMARK 3 S31: -0.2031 S32: -0.2006 S33: 0.1358
REMARK 3
REMARK 3 TLS GROUP : 11
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 1005 C 1119
REMARK 3 ORIGIN FOR THE GROUP (A): -5.9760 198.2230 -5.1900
REMARK 3 T TENSOR
REMARK 3 T11: 0.6118 T22: 0.2118
REMARK 3 T33: 0.3504 T12: -0.2593
REMARK 3 T13: -0.3008 T23: 0.1905
REMARK 3 L TENSOR
REMARK 3 L11: 0.9479 L22: 2.3470
REMARK 3 L33: 1.4024 L12: 0.2115
REMARK 3 L13: -0.1000 L23: 0.6844
REMARK 3 S TENSOR
REMARK 3 S11: -0.2199 S12: 0.1384 S13: 0.1933
REMARK 3 S21: -0.3310 S22: -0.0657 S23: -0.0644
REMARK 3 S31: -0.4867 S32: 0.4047 S33: 0.2856
REMARK 3
REMARK 3 TLS GROUP : 12
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 2 D 11
REMARK 3 RESIDUE RANGE : D 1089 D 1481
REMARK 3 ORIGIN FOR THE GROUP (A): -3.0860 181.4100 28.1080
REMARK 3 T TENSOR
REMARK 3 T11: 0.4217 T22: 0.1015
REMARK 3 T33: 0.2224 T12: -0.0836
REMARK 3 T13: -0.2092 T23: -0.0172
REMARK 3 L TENSOR
REMARK 3 L11: 0.8554 L22: 1.4927
REMARK 3 L33: 1.9122 L12: -0.0640
REMARK 3 L13: -0.0432 L23: -0.7407
REMARK 3 S TENSOR
REMARK 3 S11: -0.1489 S12: -0.1585 S13: 0.2127
REMARK 3 S21: 0.3326 S22: 0.0082 S23: -0.0206
REMARK 3 S31: -0.4062 S32: 0.2467 S33: 0.1406
REMARK 3
REMARK 3 TLS GROUP : 13
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 12 D 100
REMARK 3 RESIDUE RANGE : D 514 D 617
REMARK 3 ORIGIN FOR THE GROUP (A): -22.4290 217.6150 -2.2510
REMARK 3 T TENSOR
REMARK 3 T11: 0.6024 T22: 0.1163
REMARK 3 T33: 0.3012 T12: -0.1955
REMARK 3 T13: -0.1848 T23: 0.1500
REMARK 3 L TENSOR
REMARK 3 L11: 1.5831 L22: 1.9200
REMARK 3 L33: 2.4104 L12: -0.9335
REMARK 3 L13: -0.1926 L23: 0.1878
REMARK 3 S TENSOR
REMARK 3 S11: 0.0862 S12: 0.0528 S13: 0.1068
REMARK 3 S21: 0.1283 S22: 0.0689 S23: -0.0885
REMARK 3 S31: 0.1002 S32: -0.1474 S33: -0.1551
REMARK 3
REMARK 3 TLS GROUP : 14
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 111 D 164
REMARK 3 RESIDUE RANGE : D 449 D 513
REMARK 3 ORIGIN FOR THE GROUP (A): -20.2770 223.8300 30.2290
REMARK 3 T TENSOR
REMARK 3 T11: 1.0965 T22: 0.2212
REMARK 3 T33: 0.1387 T12: -0.1580
REMARK 3 T13: -0.2846 T23: 0.0274
REMARK 3 L TENSOR
REMARK 3 L11: 7.4419 L22: 3.5967
REMARK 3 L33: 2.6347 L12: -2.2818
REMARK 3 L13: 1.3017 L23: -0.2998
REMARK 3 S TENSOR
REMARK 3 S11: -0.0858 S12: -1.0332 S13: 0.2586
REMARK 3 S21: 0.9675 S22: 0.3137 S23: -0.5552
REMARK 3 S31: -0.0142 S32: -0.4594 S33: -0.2278
REMARK 3
REMARK 3 TLS GROUP : 15
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 165 D 216
REMARK 3 RESIDUE RANGE : D 340 D 396
REMARK 3 ORIGIN FOR THE GROUP (A): -57.0660 257.0150 26.6520
REMARK 3 T TENSOR
REMARK 3 T11: 0.8486 T22: 0.7733
REMARK 3 T33: 0.4650 T12: 0.0572
REMARK 3 T13: 0.5696 T23: -0.0055
REMARK 3 L TENSOR
REMARK 3 L11: 7.7138 L22: 7.0530
REMARK 3 L33: 2.3552 L12: -5.1110
REMARK 3 L13: 2.8851 L23: -2.7602
REMARK 3 S TENSOR
REMARK 3 S11: -0.3989 S12: -0.5881 S13: 0.1790
REMARK 3 S21: 1.3568 S22: 0.3518 S23: 0.9302
REMARK 3 S31: -0.0113 S32: -0.9266 S33: 0.0471
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 217 D 339
REMARK 3 ORIGIN FOR THE GROUP (A): -77.9400 289.3480 33.3320
REMARK 3 T TENSOR
REMARK 3 T11: 0.8307 T22: 0.9841
REMARK 3 T33: 0.9930 T12: 0.2642
REMARK 3 T13: 0.4858 T23: -0.0899
REMARK 3 L TENSOR
REMARK 3 L11: 1.4945 L22: 2.1153
REMARK 3 L33: 2.9823 L12: -1.7712
REMARK 3 L13: 2.0769 L23: -2.5001
REMARK 3 S TENSOR
REMARK 3 S11: -0.1227 S12: -0.2997 S13: 0.0229
REMARK 3 S21: 0.2085 S22: 0.3868 S23: 0.0882
REMARK 3 S31: -0.3385 S32: -0.4751 S33: -0.2641
REMARK 3
REMARK 3 TLS GROUP : 17
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 397 D 448
REMARK 3 ORIGIN FOR THE GROUP (A): -34.4450 256.8340 29.3890
REMARK 3 T TENSOR
REMARK 3 T11: 0.7235 T22: 0.1333
REMARK 3 T33: 0.1439 T12: 0.0354
REMARK 3 T13: 0.0838 T23: -0.0788
REMARK 3 L TENSOR
REMARK 3 L11: 12.0491 L22: 14.0597
REMARK 3 L33: 17.2009 L12: 0.6480
REMARK 3 L13: 2.8220 L23: 6.9112
REMARK 3 S TENSOR
REMARK 3 S11: -0.4359 S12: -0.0727 S13: -0.1624
REMARK 3 S21: 1.0305 S22: 0.2652 S23: -0.4047
REMARK 3 S31: -0.3445 S32: 0.6183 S33: 0.1706
REMARK 3
REMARK 3 TLS GROUP : 18
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 618 D 776
REMARK 3 ORIGIN FOR THE GROUP (A): -4.2040 177.2030 -13.2490
REMARK 3 T TENSOR
REMARK 3 T11: 0.3442 T22: 0.1180
REMARK 3 T33: 0.1734 T12: -0.1497
REMARK 3 T13: -0.0776 T23: 0.0902
REMARK 3 L TENSOR
REMARK 3 L11: 1.6035 L22: 2.7773
REMARK 3 L33: 2.7252 L12: 0.1147
REMARK 3 L13: 1.1388 L23: 0.3819
REMARK 3 S TENSOR
REMARK 3 S11: -0.3013 S12: 0.2770 S13: 0.0904
REMARK 3 S21: -0.4044 S22: 0.1098 S23: -0.1994
REMARK 3 S31: -0.3459 S32: 0.3658 S33: 0.1914
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 777 D 946
REMARK 3 ORIGIN FOR THE GROUP (A): 4.5010 140.9640 2.8870
REMARK 3 T TENSOR
REMARK 3 T11: 0.4671 T22: 0.2313
REMARK 3 T33: 0.2486 T12: 0.2039
REMARK 3 T13: -0.1103 T23: 0.0031
REMARK 3 L TENSOR
REMARK 3 L11: 2.8192 L22: 4.6764
REMARK 3 L33: 1.7123 L12: -0.0672
REMARK 3 L13: -0.1155 L23: 0.4386
REMARK 3 S TENSOR
REMARK 3 S11: 0.0491 S12: 0.0318 S13: -0.4556
REMARK 3 S21: 0.2717 S22: 0.0790 S23: -0.2262
REMARK 3 S31: 0.5517 S32: 0.5915 S33: -0.1281
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 947 D 1088
REMARK 3 ORIGIN FOR THE GROUP (A): -28.3180 148.8780 18.3950
REMARK 3 T TENSOR
REMARK 3 T11: 0.3077 T22: 0.0729
REMARK 3 T33: 0.1491 T12: -0.0801
REMARK 3 T13: -0.0118 T23: 0.0642
REMARK 3 L TENSOR
REMARK 3 L11: 2.9281 L22: 0.7551
REMARK 3 L33: 3.4829 L12: -0.6427
REMARK 3 L13: -1.7426 L23: 0.5552
REMARK 3 S TENSOR
REMARK 3 S11: -0.1242 S12: -0.2171 S13: -0.1095
REMARK 3 S21: 0.0204 S22: 0.0572 S23: -0.0338
REMARK 3 S31: 0.3472 S32: -0.0894 S33: 0.0669
REMARK 3
REMARK 3 TLS GROUP : 21
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 2 E 96
REMARK 3 RESIDUE RANGE : D 1482 D 1505
REMARK 3 ORIGIN FOR THE GROUP (A): 21.4570 186.2310 -9.8150
REMARK 3 T TENSOR
REMARK 3 T11: 0.2818 T22: 0.8857
REMARK 3 T33: 0.4791 T12: -0.4164
REMARK 3 T13: -0.1354 T23: 0.3503
REMARK 3 L TENSOR
REMARK 3 L11: 6.7915 L22: 2.3786
REMARK 3 L33: 2.1831 L12: 1.8786
REMARK 3 L13: -2.4246 L23: -0.1412
REMARK 3 S TENSOR
REMARK 3 S11: -0.2007 S12: 0.4936 S13: 0.3140
REMARK 3 S21: -0.1953 S22: 0.1356 S23: -0.6554
REMARK 3 S31: -0.4198 S32: 0.8152 S33: 0.0650
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 : F 73 F 256
REMARK 3 ORIGIN FOR THE GROUP (A): -40.0060 240.8750 9.5490
REMARK 3 T TENSOR
REMARK 3 T11: 0.3067 T22: 0.2621
REMARK 3 T33: 0.0434 T12: -0.0504
REMARK 3 T13: -0.0031 T23: 0.1006
REMARK 3 L TENSOR
REMARK 3 L11: 1.7102 L22: 6.8792
REMARK 3 L33: 2.5735 L12: -0.1103
REMARK 3 L13: 0.6994 L23: 1.5170
REMARK 3 S TENSOR
REMARK 3 S11: 0.0015 S12: -0.3305 S13: -0.1520
REMARK 3 S21: 0.5092 S22: 0.1063 S23: 0.1585
REMARK 3 S31: 0.0518 S32: -0.1555 S33: -0.1079
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 : F 257 F 313
REMARK 3 ORIGIN FOR THE GROUP (A): -48.9040 213.3320 -18.8140
REMARK 3 T TENSOR
REMARK 3 T11: 0.5191 T22: 0.2965
REMARK 3 T33: 0.3932 T12: -0.2460
REMARK 3 T13: -0.2927 T23: 0.2531
REMARK 3 L TENSOR
REMARK 3 L11: 12.4564 L22: 4.7982
REMARK 3 L33: 4.3602 L12: 3.0878
REMARK 3 L13: 3.2809 L23: 2.5065
REMARK 3 S TENSOR
REMARK 3 S11: 0.4085 S12: -0.1362 S13: -0.4417
REMARK 3 S21: -0.0211 S22: -0.1865 S23: 0.5003
REMARK 3 S31: 0.7219 S32: -0.6865 S33: -0.2220
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 314 F 339
REMARK 3 ORIGIN FOR THE GROUP (A): -25.5650 198.6970 -7.8220
REMARK 3 T TENSOR
REMARK 3 T11: 0.9166 T22: 0.1266
REMARK 3 T33: 0.5709 T12: -0.3225
REMARK 3 T13: -0.3549 T23: 0.1507
REMARK 3 L TENSOR
REMARK 3 L11: 9.1077 L22: 2.9952
REMARK 3 L33: 20.0518 L12: -3.9459
REMARK 3 L13: -5.3818 L23: -2.2486
REMARK 3 S TENSOR
REMARK 3 S11: 0.0669 S12: -0.0672 S13: -0.5359
REMARK 3 S21: 0.1750 S22: -0.0959 S23: 0.2009
REMARK 3 S31: -0.2048 S32: 0.2437 S33: 0.0290
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 : F 340 F 423
REMARK 3 ORIGIN FOR THE GROUP (A): -1.9140 213.2030 -40.4320
REMARK 3 T TENSOR
REMARK 3 T11: 0.8642 T22: 0.3869
REMARK 3 T33: 0.3379 T12: 0.0448
REMARK 3 T13: 0.3611 T23: 0.2770
REMARK 3 L TENSOR
REMARK 3 L11: 2.8647 L22: 6.6566
REMARK 3 L33: 12.3275 L12: 1.3514
REMARK 3 L13: 0.8601 L23: -3.3734
REMARK 3 S TENSOR
REMARK 3 S11: 0.4495 S12: 0.5228 S13: 0.4569
REMARK 3 S21: -0.5347 S22: 0.2260 S23: 0.1023
REMARK 3 S31: -1.0383 S32: -0.2607 S33: -0.6754
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS. L-TEST AND OTHER TWINNING STATISTICAL TESTS HAVE
REMARK 3 SHOWN THAT THE 3DXJ DATA WERE PARTIALLY TWINNED, BUT NOT
REMARK 3 PERFECTLY TWINNED. GIVEN THE PROBLEM OF PARTIAL TWINNING IN THE
REMARK 3 DATA, MODEL REFINEMENT WAS INDEED VERY CHALLENGING. SIX
REMARK 3 INDEPENDENT ATTEMPTS OF MODEL REFINEMENT WERE MADE AFTER PROPER
REMARK 3 CRYSTALLOGRAPHIC ORIGIN SHIFT, STARTING WITH SIX DIFFERENT
REMARK 3 PARTIAL MODELS ACCORDING TO THE NOTES IN AUTHOR'S NOTEBOOK. ALL
REMARK 3 APPEAR TO HAVE CONVERGED TO SIMILAR CRYSTALLOGRAPHIC R-FACTOR
REMARK 3 AND FREE R-FACTOR, EVEN THOUGH THE NUMBER OF ATOMS IN THE FINAL
REMARK 3 COORDINATES VARIED SLIGHTLY AMONG THEM. AT THE TIME OF
REMARK 3 SUBMISSION OF THIS ENTRY, THE FILES FOR TWO OF THE SIX ATTEMPTS
REMARK 3 HAVE BEEN LOCATED, BUT THE REMAINING FOUR FILES HAVE NOT. IT
REMARK 3 APPEARS THAT THERE MIGHT BE A MIX-UP IN NUMBER OF ATOMS AMONG
REMARK 3 THESE FILES WHEN REPORTING THE NUMBER OF ATOMS AND R-FACTORS.
REMARK 4
REMARK 4 5TMF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-OCT-16.
REMARK 100 THE DEPOSITION ID IS D_1000224492.
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 : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : NULL
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
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) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
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: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: AUTHOR USED THE SF DATA FROM ENTRY 3DXJ.
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 73.78
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.69
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MES, MAGNESIUM FORMATE, PEG
REMARK 280 8000,SPERMINE, PH 5.85, EVAPORATION, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 167.25333
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 83.62667
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 125.44000
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 41.81333
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 209.06667
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 45640 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 153980 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -225.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, 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 ALA A 232
REMARK 465 VAL A 233
REMARK 465 ALA A 234
REMARK 465 ALA A 235
REMARK 465 PRO A 236
REMARK 465 GLU A 237
REMARK 465 GLU A 238
REMARK 465 ALA A 239
REMARK 465 LYS A 240
REMARK 465 GLU A 241
REMARK 465 PRO A 242
REMARK 465 GLU A 243
REMARK 465 ALA A 244
REMARK 465 PRO A 245
REMARK 465 PRO A 246
REMARK 465 GLU A 247
REMARK 465 GLN A 248
REMARK 465 GLU A 249
REMARK 465 GLU A 250
REMARK 465 GLU A 251
REMARK 465 LEU A 252
REMARK 465 ASP A 253
REMARK 465 LEU A 254
REMARK 465 PRO A 255
REMARK 465 LEU A 256
REMARK 465 GLU A 257
REMARK 465 GLU A 258
REMARK 465 LEU A 259
REMARK 465 GLY A 260
REMARK 465 LEU A 261
REMARK 465 SER A 262
REMARK 465 THR A 263
REMARK 465 ARG A 264
REMARK 465 VAL A 265
REMARK 465 LEU A 266
REMARK 465 HIS A 267
REMARK 465 SER A 268
REMARK 465 LEU A 269
REMARK 465 LYS A 270
REMARK 465 GLU A 271
REMARK 465 GLU A 272
REMARK 465 GLY A 273
REMARK 465 ILE A 274
REMARK 465 GLU A 275
REMARK 465 SER A 276
REMARK 465 VAL A 277
REMARK 465 ARG A 278
REMARK 465 ALA A 279
REMARK 465 LEU A 280
REMARK 465 LEU A 281
REMARK 465 ALA A 282
REMARK 465 LEU A 283
REMARK 465 ASN A 284
REMARK 465 LEU A 285
REMARK 465 LYS A 286
REMARK 465 ASP A 287
REMARK 465 LEU A 288
REMARK 465 LYS A 289
REMARK 465 ASN A 290
REMARK 465 ILE A 291
REMARK 465 PRO A 292
REMARK 465 GLY A 293
REMARK 465 ILE A 294
REMARK 465 GLY A 295
REMARK 465 GLU A 296
REMARK 465 ARG A 297
REMARK 465 SER A 298
REMARK 465 LEU A 299
REMARK 465 GLU A 300
REMARK 465 GLU A 301
REMARK 465 ILE A 302
REMARK 465 LYS A 303
REMARK 465 GLU A 304
REMARK 465 ALA A 305
REMARK 465 LEU A 306
REMARK 465 GLU A 307
REMARK 465 LYS A 308
REMARK 465 LYS A 309
REMARK 465 GLY A 310
REMARK 465 PHE A 311
REMARK 465 THR A 312
REMARK 465 LEU A 313
REMARK 465 LYS A 314
REMARK 465 GLU A 315
REMARK 465 ALA B 239
REMARK 465 LYS B 240
REMARK 465 GLU B 241
REMARK 465 PRO B 242
REMARK 465 GLU B 243
REMARK 465 ALA B 244
REMARK 465 PRO B 245
REMARK 465 PRO B 246
REMARK 465 GLU B 247
REMARK 465 GLN B 248
REMARK 465 GLU B 249
REMARK 465 GLU B 250
REMARK 465 GLU B 251
REMARK 465 LEU B 252
REMARK 465 ASP B 253
REMARK 465 LEU B 254
REMARK 465 PRO B 255
REMARK 465 LEU B 256
REMARK 465 GLU B 257
REMARK 465 GLU B 258
REMARK 465 LEU B 259
REMARK 465 GLY B 260
REMARK 465 LEU B 261
REMARK 465 SER B 262
REMARK 465 THR B 263
REMARK 465 ARG B 264
REMARK 465 VAL B 265
REMARK 465 LEU B 266
REMARK 465 HIS B 267
REMARK 465 SER B 268
REMARK 465 LEU B 269
REMARK 465 LYS B 270
REMARK 465 GLU B 271
REMARK 465 GLU B 272
REMARK 465 GLY B 273
REMARK 465 ILE B 274
REMARK 465 GLU B 275
REMARK 465 SER B 276
REMARK 465 VAL B 277
REMARK 465 ARG B 278
REMARK 465 ALA B 279
REMARK 465 LEU B 280
REMARK 465 LEU B 281
REMARK 465 ALA B 282
REMARK 465 LEU B 283
REMARK 465 ASN B 284
REMARK 465 LEU B 285
REMARK 465 LYS B 286
REMARK 465 ASP B 287
REMARK 465 LEU B 288
REMARK 465 LYS B 289
REMARK 465 ASN B 290
REMARK 465 ILE B 291
REMARK 465 PRO B 292
REMARK 465 GLY B 293
REMARK 465 ILE B 294
REMARK 465 GLY B 295
REMARK 465 GLU B 296
REMARK 465 ARG B 297
REMARK 465 SER B 298
REMARK 465 LEU B 299
REMARK 465 GLU B 300
REMARK 465 GLU B 301
REMARK 465 ILE B 302
REMARK 465 LYS B 303
REMARK 465 GLU B 304
REMARK 465 ALA B 305
REMARK 465 LEU B 306
REMARK 465 GLU B 307
REMARK 465 LYS B 308
REMARK 465 LYS B 309
REMARK 465 GLY B 310
REMARK 465 PHE B 311
REMARK 465 THR B 312
REMARK 465 LEU B 313
REMARK 465 LYS B 314
REMARK 465 GLU B 315
REMARK 465 MET D 1
REMARK 465 LYS D 1506
REMARK 465 GLU D 1507
REMARK 465 ARG D 1508
REMARK 465 PRO D 1509
REMARK 465 ALA D 1510
REMARK 465 ALA D 1511
REMARK 465 ARG D 1512
REMARK 465 ARG D 1513
REMARK 465 GLY D 1514
REMARK 465 VAL D 1515
REMARK 465 LYS D 1516
REMARK 465 ARG D 1517
REMARK 465 GLU D 1518
REMARK 465 GLN D 1519
REMARK 465 PRO D 1520
REMARK 465 GLY D 1521
REMARK 465 LYS D 1522
REMARK 465 GLN D 1523
REMARK 465 ALA D 1524
REMARK 465 MET E 1
REMARK 465 ARG E 97
REMARK 465 GLU E 98
REMARK 465 GLU E 99
REMARK 465 MET F 1
REMARK 465 LYS F 2
REMARK 465 LYS F 3
REMARK 465 SER F 4
REMARK 465 LYS F 5
REMARK 465 ARG F 6
REMARK 465 LYS F 7
REMARK 465 ASN F 8
REMARK 465 ALA F 9
REMARK 465 GLN F 10
REMARK 465 ALA F 11
REMARK 465 GLN F 12
REMARK 465 GLU F 13
REMARK 465 ALA F 14
REMARK 465 GLN F 15
REMARK 465 GLU F 16
REMARK 465 THR F 17
REMARK 465 GLU F 18
REMARK 465 VAL F 19
REMARK 465 LEU F 20
REMARK 465 VAL F 21
REMARK 465 GLN F 22
REMARK 465 GLU F 23
REMARK 465 GLU F 24
REMARK 465 ALA F 25
REMARK 465 GLU F 26
REMARK 465 GLU F 27
REMARK 465 LEU F 28
REMARK 465 PRO F 29
REMARK 465 GLU F 30
REMARK 465 PHE F 31
REMARK 465 PRO F 32
REMARK 465 GLU F 33
REMARK 465 GLY F 34
REMARK 465 GLU F 35
REMARK 465 PRO F 36
REMARK 465 ASP F 37
REMARK 465 PRO F 38
REMARK 465 ASP F 39
REMARK 465 LEU F 40
REMARK 465 GLU F 41
REMARK 465 ASP F 42
REMARK 465 PRO F 43
REMARK 465 ASP F 44
REMARK 465 LEU F 45
REMARK 465 THR F 46
REMARK 465 LEU F 47
REMARK 465 GLU F 48
REMARK 465 ASP F 49
REMARK 465 ASP F 50
REMARK 465 LEU F 51
REMARK 465 LEU F 52
REMARK 465 ASP F 53
REMARK 465 LEU F 54
REMARK 465 PRO F 55
REMARK 465 GLU F 56
REMARK 465 GLU F 57
REMARK 465 GLY F 58
REMARK 465 GLU F 59
REMARK 465 GLY F 60
REMARK 465 LEU F 61
REMARK 465 ASP F 62
REMARK 465 LEU F 63
REMARK 465 GLU F 64
REMARK 465 GLU F 65
REMARK 465 GLU F 66
REMARK 465 GLU F 67
REMARK 465 GLU F 68
REMARK 465 ASP F 69
REMARK 465 LEU F 70
REMARK 465 PRO F 71
REMARK 465 ILE F 72
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 O LEU D 520 NH1 ARG D 525 2.00
REMARK 500 O LEU C 737 N GLU C 739 2.04
REMARK 500 NH2 ARG F 256 O ILE F 310 2.09
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 ARG A 14 86.73 -154.83
REMARK 500 GLN A 16 -51.61 -130.13
REMARK 500 GLU A 59 -75.48 -31.14
REMARK 500 LEU A 101 103.92 -160.52
REMARK 500 LYS A 159 43.77 -108.44
REMARK 500 ASN A 227 74.58 66.36
REMARK 500 PRO A 228 -160.70 -76.59
REMARK 500 ASP B 3 -151.97 -96.10
REMARK 500 SER B 4 -85.82 -64.45
REMARK 500 LYS B 5 -112.61 -123.20
REMARK 500 ARG B 30 123.92 -35.32
REMARK 500 LYS B 83 -9.35 -58.78
REMARK 500 ALA B 118 -144.46 41.42
REMARK 500 ASP B 119 31.16 -88.64
REMARK 500 GLU B 133 -69.71 -136.30
REMARK 500 ILE B 158 88.15 55.92
REMARK 500 ASP B 160 -109.01 -91.22
REMARK 500 ASN B 163 18.34 -142.45
REMARK 500 SER B 226 -49.26 -134.45
REMARK 500 ASN B 227 70.37 -107.15
REMARK 500 ARG C 28 30.75 -94.40
REMARK 500 ASP C 33 -117.37 -85.11
REMARK 500 GLU C 37 -96.61 43.42
REMARK 500 ARG C 39 110.40 -161.84
REMARK 500 GLU C 40 137.43 78.72
REMARK 500 ASN C 41 -96.27 -84.58
REMARK 500 VAL C 42 -75.70 44.23
REMARK 500 PRO C 79 164.61 -42.47
REMARK 500 GLN C 80 -73.02 -59.25
REMARK 500 ASP C 81 1.98 -68.99
REMARK 500 LEU C 98 -70.83 -104.05
REMARK 500 GLN C 99 107.26 84.47
REMARK 500 THR C 105 80.14 52.43
REMARK 500 GLU C 110 -170.16 -62.38
REMARK 500 ASP C 111 -144.06 -142.37
REMARK 500 PHE C 114 32.36 -79.48
REMARK 500 LEU C 115 84.89 -68.02
REMARK 500 ALA C 153 33.09 -77.94
REMARK 500 PRO C 155 43.50 -93.70
REMARK 500 ARG C 157 -165.27 -119.88
REMARK 500 GLU C 177 142.69 -32.13
REMARK 500 ASN C 179 56.08 -96.88
REMARK 500 VAL C 181 -132.81 -113.77
REMARK 500 VAL C 186 -66.12 -104.49
REMARK 500 ASN C 187 -118.63 -92.72
REMARK 500 ARG C 189 81.94 -66.27
REMARK 500 VAL C 194 -102.97 0.80
REMARK 500 LEU C 195 -70.82 23.12
REMARK 500 THR C 206 -41.44 -130.92
REMARK 500 LEU C 207 -3.25 -143.38
REMARK 500
REMARK 500 THIS ENTRY HAS 314 RAMACHANDRAN OUTLIERS.
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 ZN D1601 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 58 SG
REMARK 620 2 CYS D 60 SG 97.6
REMARK 620 3 CYS D 73 SG 122.8 117.8
REMARK 620 4 CYS D 76 SG 113.8 120.6 86.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D1605 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 739 OD1
REMARK 620 2 ASP D 741 OD1 66.0
REMARK 620 3 ASP D 741 OD2 66.5 46.3
REMARK 620 4 ASP D 743 OD1 87.8 75.9 121.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D1602 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D1112 SG
REMARK 620 2 CYS D1194 SG 117.3
REMARK 620 3 CYS D1201 SG 101.4 121.2
REMARK 620 4 CYS D1204 SG 115.0 105.3 94.9
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 PO4 A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NE6 C 1201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN D 1601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN D 1602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 D 1603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG D 1604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG D 1605
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3DXJ RELATED DB: PDB
REMARK 900 RE-REFINEMENT OF THE PDB ENTRY 3DXJ
DBREF 5TMF A 1 315 UNP Q9Z9H6 RPOA_THETH 1 315
DBREF 5TMF B 1 315 UNP Q9Z9H6 RPOA_THETH 1 315
DBREF 5TMF C 1 1119 UNP Q8RQE9 RPOB_THET8 1 1119
DBREF 5TMF D 1 1524 UNP Q8RQE8 RPOC_THET8 1 1524
DBREF 5TMF E 1 99 UNP Q72ID6 RPOZ_THET2 1 99
DBREF 5TMF F 1 423 UNP Q72L95 SIGA_THET2 1 423
SEQADV 5TMF GLU E 61 UNP Q72ID6 VAL 61 CONFLICT
SEQADV 5TMF ILE E 92 UNP Q72ID6 LEU 92 CONFLICT
SEQADV 5TMF GLY E 95 UNP Q72ID6 VAL 95 CONFLICT
SEQADV 5TMF THR F 46 UNP Q72L95 ALA 46 CONFLICT
SEQRES 1 A 315 MET LEU ASP SER LYS LEU LYS ALA PRO VAL PHE THR VAL
SEQRES 2 A 315 ARG THR GLN GLY ARG GLU TYR GLY GLU PHE VAL LEU GLU
SEQRES 3 A 315 PRO LEU GLU ARG GLY PHE GLY VAL THR LEU GLY ASN PRO
SEQRES 4 A 315 LEU ARG ARG ILE LEU LEU SER SER ILE PRO GLY THR ALA
SEQRES 5 A 315 VAL THR SER VAL TYR ILE GLU ASP VAL LEU HIS GLU PHE
SEQRES 6 A 315 SER THR ILE PRO GLY VAL LYS GLU ASP VAL VAL GLU ILE
SEQRES 7 A 315 ILE LEU ASN LEU LYS GLU LEU VAL VAL ARG PHE LEU ASN
SEQRES 8 A 315 PRO SER LEU GLN THR VAL THR LEU LEU LEU LYS ALA GLU
SEQRES 9 A 315 GLY PRO LYS GLU VAL LYS ALA ARG ASP PHE LEU PRO VAL
SEQRES 10 A 315 ALA ASP VAL GLU ILE MET ASN PRO ASP LEU HIS ILE ALA
SEQRES 11 A 315 THR LEU GLU GLU GLY GLY ARG LEU ASN MET GLU VAL ARG
SEQRES 12 A 315 VAL ASP ARG GLY VAL GLY TYR VAL PRO ALA GLU LYS HIS
SEQRES 13 A 315 GLY ILE LYS ASP ARG ILE ASN ALA ILE PRO VAL ASP ALA
SEQRES 14 A 315 VAL PHE SER PRO VAL ARG ARG VAL ALA PHE GLN VAL GLU
SEQRES 15 A 315 ASP THR ARG LEU GLY GLN ARG THR ASP LEU ASP LYS LEU
SEQRES 16 A 315 THR LEU ARG ILE TRP THR ASP GLY SER VAL THR PRO LEU
SEQRES 17 A 315 GLU ALA LEU ASN GLN ALA VAL GLU ILE LEU ARG GLU HIS
SEQRES 18 A 315 LEU THR TYR PHE SER ASN PRO GLN ALA ALA ALA VAL ALA
SEQRES 19 A 315 ALA PRO GLU GLU ALA LYS GLU PRO GLU ALA PRO PRO GLU
SEQRES 20 A 315 GLN GLU GLU GLU LEU ASP LEU PRO LEU GLU GLU LEU GLY
SEQRES 21 A 315 LEU SER THR ARG VAL LEU HIS SER LEU LYS GLU GLU GLY
SEQRES 22 A 315 ILE GLU SER VAL ARG ALA LEU LEU ALA LEU ASN LEU LYS
SEQRES 23 A 315 ASP LEU LYS ASN ILE PRO GLY ILE GLY GLU ARG SER LEU
SEQRES 24 A 315 GLU GLU ILE LYS GLU ALA LEU GLU LYS LYS GLY PHE THR
SEQRES 25 A 315 LEU LYS GLU
SEQRES 1 B 315 MET LEU ASP SER LYS LEU LYS ALA PRO VAL PHE THR VAL
SEQRES 2 B 315 ARG THR GLN GLY ARG GLU TYR GLY GLU PHE VAL LEU GLU
SEQRES 3 B 315 PRO LEU GLU ARG GLY PHE GLY VAL THR LEU GLY ASN PRO
SEQRES 4 B 315 LEU ARG ARG ILE LEU LEU SER SER ILE PRO GLY THR ALA
SEQRES 5 B 315 VAL THR SER VAL TYR ILE GLU ASP VAL LEU HIS GLU PHE
SEQRES 6 B 315 SER THR ILE PRO GLY VAL LYS GLU ASP VAL VAL GLU ILE
SEQRES 7 B 315 ILE LEU ASN LEU LYS GLU LEU VAL VAL ARG PHE LEU ASN
SEQRES 8 B 315 PRO SER LEU GLN THR VAL THR LEU LEU LEU LYS ALA GLU
SEQRES 9 B 315 GLY PRO LYS GLU VAL LYS ALA ARG ASP PHE LEU PRO VAL
SEQRES 10 B 315 ALA ASP VAL GLU ILE MET ASN PRO ASP LEU HIS ILE ALA
SEQRES 11 B 315 THR LEU GLU GLU GLY GLY ARG LEU ASN MET GLU VAL ARG
SEQRES 12 B 315 VAL ASP ARG GLY VAL GLY TYR VAL PRO ALA GLU LYS HIS
SEQRES 13 B 315 GLY ILE LYS ASP ARG ILE ASN ALA ILE PRO VAL ASP ALA
SEQRES 14 B 315 VAL PHE SER PRO VAL ARG ARG VAL ALA PHE GLN VAL GLU
SEQRES 15 B 315 ASP THR ARG LEU GLY GLN ARG THR ASP LEU ASP LYS LEU
SEQRES 16 B 315 THR LEU ARG ILE TRP THR ASP GLY SER VAL THR PRO LEU
SEQRES 17 B 315 GLU ALA LEU ASN GLN ALA VAL GLU ILE LEU ARG GLU HIS
SEQRES 18 B 315 LEU THR TYR PHE SER ASN PRO GLN ALA ALA ALA VAL ALA
SEQRES 19 B 315 ALA PRO GLU GLU ALA LYS GLU PRO GLU ALA PRO PRO GLU
SEQRES 20 B 315 GLN GLU GLU GLU LEU ASP LEU PRO LEU GLU GLU LEU GLY
SEQRES 21 B 315 LEU SER THR ARG VAL LEU HIS SER LEU LYS GLU GLU GLY
SEQRES 22 B 315 ILE GLU SER VAL ARG ALA LEU LEU ALA LEU ASN LEU LYS
SEQRES 23 B 315 ASP LEU LYS ASN ILE PRO GLY ILE GLY GLU ARG SER LEU
SEQRES 24 B 315 GLU GLU ILE LYS GLU ALA LEU GLU LYS LYS GLY PHE THR
SEQRES 25 B 315 LEU LYS GLU
SEQRES 1 C 1119 MET GLU ILE LYS ARG PHE GLY ARG ILE ARG GLU VAL ILE
SEQRES 2 C 1119 PRO LEU PRO PRO LEU THR GLU ILE GLN VAL GLU SER TYR
SEQRES 3 C 1119 ARG ARG ALA LEU GLN ALA ASP VAL PRO PRO GLU LYS ARG
SEQRES 4 C 1119 GLU ASN VAL GLY ILE GLN ALA ALA PHE ARG GLU THR PHE
SEQRES 5 C 1119 PRO ILE GLU GLU GLU ASP LYS GLY LYS GLY GLY LEU VAL
SEQRES 6 C 1119 LEU ASP PHE LEU GLU TYR ARG LEU GLY GLU PRO PRO PHE
SEQRES 7 C 1119 PRO GLN ASP GLU CYS ARG GLU LYS ASP LEU THR TYR GLN
SEQRES 8 C 1119 ALA PRO LEU TYR ALA ARG LEU GLN LEU ILE HIS LYS ASP
SEQRES 9 C 1119 THR GLY LEU ILE LYS GLU ASP GLU VAL PHE LEU GLY HIS
SEQRES 10 C 1119 ILE PRO LEU MET THR GLU ASP GLY SER PHE ILE ILE ASN
SEQRES 11 C 1119 GLY ALA ASP ARG VAL ILE VAL SER GLN ILE HIS ARG SER
SEQRES 12 C 1119 PRO GLY VAL TYR PHE THR PRO ASP PRO ALA ARG PRO GLY
SEQRES 13 C 1119 ARG TYR ILE ALA SER ILE ILE PRO LEU PRO LYS ARG GLY
SEQRES 14 C 1119 PRO TRP ILE ASP LEU GLU VAL GLU PRO ASN GLY VAL VAL
SEQRES 15 C 1119 SER MET LYS VAL ASN LYS ARG LYS PHE PRO LEU VAL LEU
SEQRES 16 C 1119 LEU LEU ARG VAL LEU GLY TYR ASP GLN GLU THR LEU ALA
SEQRES 17 C 1119 ARG GLU LEU GLY ALA TYR GLY GLU LEU VAL GLN GLY LEU
SEQRES 18 C 1119 MET ASP GLU SER VAL PHE ALA MET ARG PRO GLU GLU ALA
SEQRES 19 C 1119 LEU ILE ARG LEU PHE THR LEU LEU ARG PRO GLY ASP PRO
SEQRES 20 C 1119 PRO LYS ARG ASP LYS ALA VAL ALA TYR VAL TYR GLY LEU
SEQRES 21 C 1119 ILE ALA ASP PRO ARG ARG TYR ASP LEU GLY GLU ALA GLY
SEQRES 22 C 1119 ARG TYR LYS ALA GLU GLU LYS LEU GLY ILE ARG LEU SER
SEQRES 23 C 1119 GLY ARG THR LEU ALA ARG PHE GLU ASP GLY GLU PHE LYS
SEQRES 24 C 1119 ASP GLU VAL PHE LEU PRO THR LEU ARG TYR LEU PHE ALA
SEQRES 25 C 1119 LEU THR ALA GLY VAL PRO GLY HIS GLU VAL ASP ASP ILE
SEQRES 26 C 1119 ASP HIS LEU GLY ASN ARG ARG ILE ARG THR VAL GLY GLU
SEQRES 27 C 1119 LEU MET THR ASP GLN PHE ARG VAL GLY LEU ALA ARG LEU
SEQRES 28 C 1119 ALA ARG GLY VAL ARG GLU ARG MET LEU MET GLY SER GLU
SEQRES 29 C 1119 ASP SER LEU THR PRO ALA LYS LEU VAL ASN SER ARG PRO
SEQRES 30 C 1119 LEU GLU ALA ALA ILE ARG GLU PHE PHE SER ARG SER GLN
SEQRES 31 C 1119 LEU SER GLN PHE LYS ASP GLU THR ASN PRO LEU SER SER
SEQRES 32 C 1119 LEU ARG HIS LYS ARG ARG ILE SER ALA LEU GLY PRO GLY
SEQRES 33 C 1119 GLY LEU THR ARG GLU ARG ALA GLY PHE ASP VAL ARG ASP
SEQRES 34 C 1119 VAL HIS ARG THR HIS TYR GLY ARG ILE CYS PRO VAL GLU
SEQRES 35 C 1119 THR PRO GLU GLY ALA ASN ILE GLY LEU ILE THR SER LEU
SEQRES 36 C 1119 ALA ALA TYR ALA ARG VAL ASP GLU LEU GLY PHE ILE ARG
SEQRES 37 C 1119 THR PRO TYR ARG ARG VAL VAL GLY GLY VAL VAL THR ASP
SEQRES 38 C 1119 GLU VAL VAL TYR MET THR ALA THR GLU GLU ASP ARG TYR
SEQRES 39 C 1119 THR ILE ALA GLN ALA ASN THR PRO LEU GLU GLY ASN ARG
SEQRES 40 C 1119 ILE ALA ALA GLU ARG VAL VAL ALA ARG ARG LYS GLY GLU
SEQRES 41 C 1119 PRO VAL ILE VAL SER PRO GLU GLU VAL GLU PHE MET ASP
SEQRES 42 C 1119 VAL SER PRO LYS GLN VAL PHE SER VAL ASN THR ASN LEU
SEQRES 43 C 1119 ILE PRO PHE LEU GLU HIS ASP ASP ALA ASN ARG ALA LEU
SEQRES 44 C 1119 MET GLY SER ASN MET GLN THR GLN ALA VAL PRO LEU ILE
SEQRES 45 C 1119 ARG ALA GLN ALA PRO VAL VAL MET THR GLY LEU GLU GLU
SEQRES 46 C 1119 ARG VAL VAL ARG ASP SER LEU ALA ALA LEU TYR ALA GLU
SEQRES 47 C 1119 GLU ASP GLY GLU VAL ALA LYS VAL ASP GLY ASN ARG ILE
SEQRES 48 C 1119 VAL VAL ARG TYR GLU ASP GLY ARG LEU VAL GLU TYR PRO
SEQRES 49 C 1119 LEU ARG ARG PHE TYR ARG SER ASN GLN GLY THR ALA LEU
SEQRES 50 C 1119 ASP GLN ARG PRO ARG VAL VAL VAL GLY GLN ARG VAL ARG
SEQRES 51 C 1119 LYS GLY ASP LEU LEU ALA ASP GLY PRO ALA SER GLU ASN
SEQRES 52 C 1119 GLY PHE LEU ALA LEU GLY GLN ASN VAL LEU VAL ALA ILE
SEQRES 53 C 1119 MET PRO PHE ASP GLY TYR ASN PHE GLU ASP ALA ILE VAL
SEQRES 54 C 1119 ILE SER GLU GLU LEU LEU LYS ARG ASP PHE TYR THR SER
SEQRES 55 C 1119 ILE HIS ILE GLU ARG TYR GLU ILE GLU ALA ARG ASP THR
SEQRES 56 C 1119 LYS LEU GLY PRO GLU ARG ILE THR ARG ASP ILE PRO HIS
SEQRES 57 C 1119 LEU SER GLU ALA ALA LEU ARG ASP LEU ASP GLU GLU GLY
SEQRES 58 C 1119 VAL VAL ARG ILE GLY ALA GLU VAL LYS PRO GLY ASP ILE
SEQRES 59 C 1119 LEU VAL GLY ARG THR SER PHE LYS GLY GLU SER GLU PRO
SEQRES 60 C 1119 THR PRO GLU GLU ARG LEU LEU ARG SER ILE PHE GLY GLU
SEQRES 61 C 1119 LYS ALA ARG ASP VAL LYS ASP THR SER LEU ARG VAL PRO
SEQRES 62 C 1119 PRO GLY GLU GLY GLY ILE VAL VAL ARG THR VAL ARG LEU
SEQRES 63 C 1119 ARG ARG GLY ASP PRO GLY VAL GLU LEU LYS PRO GLY VAL
SEQRES 64 C 1119 ARG GLU VAL VAL ARG VAL TYR VAL ALA GLN LYS ARG LYS
SEQRES 65 C 1119 LEU GLN VAL GLY ASP LYS LEU ALA ASN ARG HIS GLY ASN
SEQRES 66 C 1119 LYS GLY VAL VAL ALA LYS ILE LEU PRO VAL GLU ASP MET
SEQRES 67 C 1119 PRO HIS LEU PRO ASP GLY THR PRO VAL ASP VAL ILE LEU
SEQRES 68 C 1119 ASN PRO LEU GLY VAL PRO SER ARG MET ASN LEU GLY GLN
SEQRES 69 C 1119 ILE LEU GLU THR HIS LEU GLY LEU ALA GLY TYR PHE LEU
SEQRES 70 C 1119 GLY GLN ARG TYR ILE SER PRO ILE PHE ASP GLY ALA LYS
SEQRES 71 C 1119 GLU PRO GLU ILE LYS GLU LEU LEU ALA GLN ALA PHE GLU
SEQRES 72 C 1119 VAL TYR PHE GLY LYS ARG LYS GLY GLU GLY PHE GLY VAL
SEQRES 73 C 1119 ASP LYS ARG GLU VAL GLU VAL LEU ARG ARG ALA GLU LYS
SEQRES 74 C 1119 LEU GLY LEU VAL THR PRO GLY LYS THR PRO GLU GLU GLN
SEQRES 75 C 1119 LEU LYS GLU LEU PHE LEU GLN GLY LYS VAL VAL LEU TYR
SEQRES 76 C 1119 ASP GLY ARG THR GLY GLU PRO ILE GLU GLY PRO ILE VAL
SEQRES 77 C 1119 VAL GLY GLN MET PHE ILE MET LYS LEU TYR HIS MET VAL
SEQRES 78 C 1119 GLU ASP LYS MET HIS ALA ARG SER THR GLY PRO TYR SER
SEQRES 79 C 1119 LEU ILE THR GLN GLN PRO LEU GLY GLY LYS ALA GLN PHE
SEQRES 80 C 1119 GLY GLY GLN ARG PHE GLY GLU MET GLU VAL TRP ALA LEU
SEQRES 81 C 1119 GLU ALA TYR GLY ALA ALA HIS THR LEU GLN GLU MET LEU
SEQRES 82 C 1119 THR LEU LYS SER ASP ASP ILE GLU GLY ARG ASN ALA ALA
SEQRES 83 C 1119 TYR GLU ALA ILE ILE LYS GLY GLU ASP VAL PRO GLU PRO
SEQRES 84 C 1119 SER VAL PRO GLU SER PHE ARG VAL LEU VAL LYS GLU LEU
SEQRES 85 C 1119 GLN ALA LEU ALA LEU ASP VAL GLN THR LEU ASP GLU LYS
SEQRES 86 C 1119 ASP ASN PRO VAL ASP ILE PHE GLU GLY LEU ALA SER LYS
SEQRES 87 C 1119 ARG
SEQRES 1 D 1524 MET LYS LYS GLU VAL ARG LYS VAL ARG ILE ALA LEU ALA
SEQRES 2 D 1524 SER PRO GLU LYS ILE ARG SER TRP SER TYR GLY GLU VAL
SEQRES 3 D 1524 GLU LYS PRO GLU THR ILE ASN TYR ARG THR LEU LYS PRO
SEQRES 4 D 1524 GLU ARG ASP GLY LEU PHE ASP GLU ARG ILE PHE GLY PRO
SEQRES 5 D 1524 ILE LYS ASP TYR GLU CYS ALA CYS GLY LYS TYR LYS ARG
SEQRES 6 D 1524 GLN ARG PHE GLU GLY LYS VAL CYS GLU ARG CYS GLY VAL
SEQRES 7 D 1524 GLU VAL THR LYS SER ILE VAL ARG ARG TYR ARG MET GLY
SEQRES 8 D 1524 HIS ILE GLU LEU ALA THR PRO ALA ALA HIS ILE TRP PHE
SEQRES 9 D 1524 VAL LYS ASP VAL PRO SER LYS ILE GLY THR LEU LEU ASP
SEQRES 10 D 1524 LEU SER ALA THR GLU LEU GLU GLN VAL LEU TYR PHE SER
SEQRES 11 D 1524 LYS TYR ILE VAL LEU ASP PRO LYS GLY ALA ILE LEU ASN
SEQRES 12 D 1524 GLY VAL PRO VAL GLU LYS ARG GLN LEU LEU THR ASP GLU
SEQRES 13 D 1524 GLU TYR ARG GLU LEU ARG TYR GLY LYS GLN GLU THR TYR
SEQRES 14 D 1524 PRO LEU PRO PRO GLY VAL ASP ALA LEU VAL LYS ASP GLY
SEQRES 15 D 1524 GLU GLU VAL VAL LYS GLY GLN GLU LEU ALA PRO GLY VAL
SEQRES 16 D 1524 VAL SER ARG LEU ASP GLY VAL ALA LEU TYR ARG PHE PRO
SEQRES 17 D 1524 ARG ARG VAL ARG VAL GLU TYR VAL LYS LYS GLU ARG ALA
SEQRES 18 D 1524 GLY LEU ARG LEU PRO LEU ALA ALA TRP VAL GLU LYS GLU
SEQRES 19 D 1524 ALA TYR LYS PRO GLY GLU ILE LEU ALA GLU LEU PRO GLU
SEQRES 20 D 1524 PRO TYR LEU PHE ARG ALA GLU GLU GLU GLY VAL VAL GLU
SEQRES 21 D 1524 LEU LYS GLU LEU GLU GLU GLY ALA PHE LEU VAL LEU ARG
SEQRES 22 D 1524 ARG GLU ASP GLU PRO VAL ALA THR TYR PHE LEU PRO VAL
SEQRES 23 D 1524 GLY MET THR PRO LEU VAL VAL HIS GLY GLU ILE VAL GLU
SEQRES 24 D 1524 LYS GLY GLN PRO LEU ALA GLU ALA LYS GLY LEU LEU ARG
SEQRES 25 D 1524 MET PRO ARG GLN VAL ARG ALA ALA GLN VAL GLU ALA GLU
SEQRES 26 D 1524 GLU GLU GLY GLU THR VAL TYR LEU THR LEU PHE LEU GLU
SEQRES 27 D 1524 TRP THR GLU PRO LYS ASP TYR ARG VAL GLN PRO HIS MET
SEQRES 28 D 1524 ASN VAL VAL VAL PRO GLU GLY ALA ARG VAL GLU ALA GLY
SEQRES 29 D 1524 ASP LYS ILE VAL ALA ALA ILE ASP PRO GLU GLU GLU VAL
SEQRES 30 D 1524 ILE ALA GLU ALA GLU GLY VAL VAL HIS LEU HIS GLU PRO
SEQRES 31 D 1524 ALA SER ILE LEU VAL VAL LYS ALA ARG VAL TYR PRO PHE
SEQRES 32 D 1524 GLU ASP ASP VAL GLU VAL SER THR GLY ASP ARG VAL ALA
SEQRES 33 D 1524 PRO GLY ASP VAL LEU ALA ASP GLY GLY LYS VAL LYS SER
SEQRES 34 D 1524 ASP VAL TYR GLY ARG VAL GLU VAL ASP LEU VAL ARG ASN
SEQRES 35 D 1524 VAL VAL ARG VAL VAL GLU SER TYR ASP ILE ASP ALA ARG
SEQRES 36 D 1524 MET GLY ALA GLU ALA ILE GLN GLN LEU LEU LYS GLU LEU
SEQRES 37 D 1524 ASP LEU GLU ALA LEU GLU LYS GLU LEU LEU GLU GLU MET
SEQRES 38 D 1524 LYS HIS PRO SER ARG ALA ARG ARG ALA LYS ALA ARG LYS
SEQRES 39 D 1524 ARG LEU GLU VAL VAL ARG ALA PHE LEU ASP SER GLY ASN
SEQRES 40 D 1524 ARG PRO GLU TRP MET ILE LEU GLU ALA VAL PRO VAL LEU
SEQRES 41 D 1524 PRO PRO ASP LEU ARG PRO MET VAL GLN VAL ASP GLY GLY
SEQRES 42 D 1524 ARG PHE ALA THR SER ASP LEU ASN ASP LEU TYR ARG ARG
SEQRES 43 D 1524 LEU ILE ASN ARG ASN ASN ARG LEU LYS LYS LEU LEU ALA
SEQRES 44 D 1524 GLN GLY ALA PRO GLU ILE ILE ILE ARG ASN GLU LYS ARG
SEQRES 45 D 1524 MET LEU GLN GLU ALA VAL ASP ALA LEU LEU ASP ASN GLY
SEQRES 46 D 1524 ARG ARG GLY ALA PRO VAL THR ASN PRO GLY SER ASP ARG
SEQRES 47 D 1524 PRO LEU ARG SER LEU THR ASP ILE LEU SER GLY LYS GLN
SEQRES 48 D 1524 GLY ARG PHE ARG GLN ASN LEU LEU GLY LYS ARG VAL ASP
SEQRES 49 D 1524 TYR SER GLY ARG SER VAL ILE VAL VAL GLY PRO GLN LEU
SEQRES 50 D 1524 LYS LEU HIS GLN CYS GLY LEU PRO LYS ARG MET ALA LEU
SEQRES 51 D 1524 GLU LEU PHE LYS PRO PHE LEU LEU LYS LYS MET GLU GLU
SEQRES 52 D 1524 LYS GLY ILE ALA PRO ASN VAL LYS ALA ALA ARG ARG MET
SEQRES 53 D 1524 LEU GLU ARG GLN ARG ASP ILE LYS ASP GLU VAL TRP ASP
SEQRES 54 D 1524 ALA LEU GLU GLU VAL ILE HIS GLY LYS VAL VAL LEU LEU
SEQRES 55 D 1524 ASN ARG ALA PRO THR LEU HIS ARG LEU GLY ILE GLN ALA
SEQRES 56 D 1524 PHE GLN PRO VAL LEU VAL GLU GLY GLN SER ILE GLN LEU
SEQRES 57 D 1524 HIS PRO LEU VAL CYS GLU ALA PHE ASN ALA ASP PHE ASP
SEQRES 58 D 1524 GLY ASP GLN MET ALA VAL HIS VAL PRO LEU SER SER PHE
SEQRES 59 D 1524 ALA GLN ALA GLU ALA ARG ILE GLN MET LEU SER ALA HIS
SEQRES 60 D 1524 ASN LEU LEU SER PRO ALA SER GLY GLU PRO LEU ALA LYS
SEQRES 61 D 1524 PRO SER ARG ASP ILE ILE LEU GLY LEU TYR TYR ILE THR
SEQRES 62 D 1524 GLN VAL ARG LYS GLU LYS LYS GLY ALA GLY LEU GLU PHE
SEQRES 63 D 1524 ALA THR PRO GLU GLU ALA LEU ALA ALA HIS GLU ARG GLY
SEQRES 64 D 1524 GLU VAL ALA LEU ASN ALA PRO ILE LYS VAL ALA GLY ARG
SEQRES 65 D 1524 GLU THR SER VAL GLY ARG LEU LYS TYR VAL PHE ALA ASN
SEQRES 66 D 1524 PRO ASP GLU ALA LEU LEU ALA VAL ALA HIS GLY ILE VAL
SEQRES 67 D 1524 ASP LEU GLN ASP VAL VAL THR VAL ARG TYR MET GLY LYS
SEQRES 68 D 1524 ARG LEU GLU THR SER PRO GLY ARG ILE LEU PHE ALA ARG
SEQRES 69 D 1524 ILE VAL ALA GLU ALA VAL GLU ASP GLU LYS VAL ALA TRP
SEQRES 70 D 1524 GLU LEU ILE GLN LEU ASP VAL PRO GLN GLU LYS ASN SER
SEQRES 71 D 1524 LEU LYS ASP LEU VAL TYR GLN ALA PHE LEU ARG LEU GLY
SEQRES 72 D 1524 MET GLU LYS THR ALA ARG LEU LEU ASP ALA LEU LYS TYR
SEQRES 73 D 1524 TYR GLY PHE THR PHE SER THR THR SER GLY ILE THR ILE
SEQRES 74 D 1524 GLY ILE ASP ASP ALA VAL ILE PRO GLU GLU LYS LYS GLN
SEQRES 75 D 1524 TYR LEU GLU GLU ALA ASP ARG LYS LEU LEU GLN ILE GLU
SEQRES 76 D 1524 GLN ALA TYR GLU MET GLY PHE LEU THR ASP ARG GLU ARG
SEQRES 77 D 1524 TYR ASP GLN ILE LEU GLN LEU TRP THR GLU THR THR GLU
SEQRES 78 D 1524 LYS VAL THR GLN ALA VAL PHE LYS ASN PHE GLU GLU ASN
SEQRES 79 D 1524 TYR PRO PHE ASN PRO LEU TYR VAL MET ALA GLN SER GLY
SEQRES 80 D 1524 ALA ARG GLY ASN PRO GLN GLN ILE ARG GLN LEU CYS GLY
SEQRES 81 D 1524 LEU ARG GLY LEU MET GLN LYS PRO SER GLY GLU THR PHE
SEQRES 82 D 1524 GLU VAL PRO VAL ARG SER SER PHE ARG GLU GLY LEU THR
SEQRES 83 D 1524 VAL LEU GLU TYR PHE ILE SER SER HIS GLY ALA ARG LYS
SEQRES 84 D 1524 GLY GLY ALA ASP THR ALA LEU ARG THR ALA ASP SER GLY
SEQRES 85 D 1524 TYR LEU THR ARG LYS LEU VAL ASP VAL THR HIS GLU ILE
SEQRES 86 D 1524 VAL VAL ARG GLU ALA ASP CYS GLY THR THR ASN TYR ILE
SEQRES 87 D 1524 SER VAL PRO LEU PHE GLN PRO ASP GLU VAL THR ARG SER
SEQRES 88 D 1524 LEU ARG LEU ARG LYS ARG ALA ASP ILE GLU ALA GLY LEU
SEQRES 89 D 1524 TYR GLY ARG VAL LEU ALA ARG GLU VAL GLU VAL LEU GLY
SEQRES 90 D 1524 VAL ARG LEU GLU GLU GLY ARG TYR LEU SER MET ASP ASP
SEQRES 91 D 1524 VAL HIS LEU LEU ILE LYS ALA ALA GLU ALA GLY GLU ILE
SEQRES 92 D 1524 GLN GLU VAL PRO VAL ARG SER PRO LEU THR CYS GLN THR
SEQRES 93 D 1524 ARG TYR GLY VAL CYS GLN LYS CYS TYR GLY TYR ASP LEU
SEQRES 94 D 1524 SER MET ALA ARG PRO VAL SER ILE GLY GLU ALA VAL GLY
SEQRES 95 D 1524 ILE VAL ALA ALA GLN SER ILE GLY GLU PRO GLY THR GLN
SEQRES 96 D 1524 LEU THR MET ARG THR PHE HIS THR GLY GLY VAL ALA GLY
SEQRES 97 D 1524 ALA ALA ASP ILE THR GLN GLY LEU PRO ARG VAL ILE GLU
SEQRES 98 D 1524 LEU PHE GLU ALA ARG ARG PRO LYS ALA LYS ALA VAL ILE
SEQRES 99 D 1524 SER GLU ILE ASP GLY VAL VAL ARG ILE GLU GLU THR GLU
SEQRES 100 D 1524 GLU LYS LEU SER VAL PHE VAL GLU SER GLU GLY PHE SER
SEQRES 101 D 1524 LYS GLU TYR LYS LEU PRO LYS GLU ALA ARG LEU LEU VAL
SEQRES 102 D 1524 LYS ASP GLY ASP TYR VAL GLU ALA GLY GLN PRO LEU THR
SEQRES 103 D 1524 ARG GLY ALA ILE ASP PRO HIS GLN LEU LEU GLU ALA LYS
SEQRES 104 D 1524 GLY PRO GLU ALA VAL GLU ARG TYR LEU VAL GLU GLU ILE
SEQRES 105 D 1524 GLN LYS VAL TYR ARG ALA GLN GLY VAL LYS LEU HIS ASP
SEQRES 106 D 1524 LYS HIS ILE GLU ILE VAL VAL ARG GLN MET MET LYS TYR
SEQRES 107 D 1524 VAL GLU VAL THR ASP PRO GLY ASP SER ARG LEU LEU GLU
SEQRES 108 D 1524 GLY GLN VAL LEU GLU LYS TRP ASP VAL GLU ALA LEU ASN
SEQRES 109 D 1524 GLU ARG LEU ILE ALA GLU GLY LYS THR PRO VAL ALA TRP
SEQRES 110 D 1524 LYS PRO LEU LEU MET GLY VAL THR LYS SER ALA LEU SER
SEQRES 111 D 1524 THR LYS SER TRP LEU SER ALA ALA SER PHE GLN ASN THR
SEQRES 112 D 1524 THR HIS VAL LEU THR GLU ALA ALA ILE ALA GLY LYS LYS
SEQRES 113 D 1524 ASP GLU LEU ILE GLY LEU LYS GLU ASN VAL ILE LEU GLY
SEQRES 114 D 1524 ARG LEU ILE PRO ALA GLY THR GLY SER ASP PHE VAL ARG
SEQRES 115 D 1524 PHE THR GLN VAL VAL ASP GLN LYS THR LEU LYS ALA ILE
SEQRES 116 D 1524 GLU GLU ALA ARG LYS GLU ALA VAL GLU ALA LYS GLU ARG
SEQRES 117 D 1524 PRO ALA ALA ARG ARG GLY VAL LYS ARG GLU GLN PRO GLY
SEQRES 118 D 1524 LYS GLN ALA
SEQRES 1 E 99 MET ALA GLU PRO GLY ILE ASP LYS LEU PHE GLY MET VAL
SEQRES 2 E 99 ASP SER LYS TYR ARG LEU THR VAL VAL VAL ALA LYS ARG
SEQRES 3 E 99 ALA GLN GLN LEU LEU ARG HIS GLY PHE LYS ASN THR VAL
SEQRES 4 E 99 LEU GLU PRO GLU GLU ARG PRO LYS MET GLN THR LEU GLU
SEQRES 5 E 99 GLY LEU PHE ASP ASP PRO ASN ALA GLU THR TRP ALA MET
SEQRES 6 E 99 LYS GLU LEU LEU THR GLY ARG LEU VAL PHE GLY GLU ASN
SEQRES 7 E 99 LEU VAL PRO GLU ASP ARG LEU GLN LYS GLU MET GLU ARG
SEQRES 8 E 99 ILE TYR PRO GLY GLU ARG GLU GLU
SEQRES 1 F 423 MET LYS LYS SER LYS ARG LYS ASN ALA GLN ALA GLN GLU
SEQRES 2 F 423 ALA GLN GLU THR GLU VAL LEU VAL GLN GLU GLU ALA GLU
SEQRES 3 F 423 GLU LEU PRO GLU PHE PRO GLU GLY GLU PRO ASP PRO ASP
SEQRES 4 F 423 LEU GLU ASP PRO ASP LEU THR LEU GLU ASP ASP LEU LEU
SEQRES 5 F 423 ASP LEU PRO GLU GLU GLY GLU GLY LEU ASP LEU GLU GLU
SEQRES 6 F 423 GLU GLU GLU ASP LEU PRO ILE PRO LYS ILE SER THR SER
SEQRES 7 F 423 ASP PRO VAL ARG GLN TYR LEU HIS GLU ILE GLY GLN VAL
SEQRES 8 F 423 PRO LEU LEU THR LEU GLU GLU GLU VAL GLU LEU ALA ARG
SEQRES 9 F 423 LYS VAL GLU GLU GLY MET GLU ALA ILE LYS LYS LEU SER
SEQRES 10 F 423 GLU ILE THR GLY LEU ASP PRO ASP LEU ILE ARG GLU VAL
SEQRES 11 F 423 VAL ARG ALA LYS ILE LEU GLY SER ALA ARG VAL ARG HIS
SEQRES 12 F 423 ILE PRO GLY LEU LYS GLU THR LEU ASP PRO LYS THR VAL
SEQRES 13 F 423 GLU GLU ILE ASP GLN LYS LEU LYS SER LEU PRO LYS GLU
SEQRES 14 F 423 HIS LYS ARG TYR LEU HIS ILE ALA ARG GLU GLY GLU ALA
SEQRES 15 F 423 ALA ARG GLN HIS LEU ILE GLU ALA ASN LEU ARG LEU VAL
SEQRES 16 F 423 VAL SER ILE ALA LYS LYS TYR THR GLY ARG GLY LEU SER
SEQRES 17 F 423 PHE LEU ASP LEU ILE GLN GLU GLY ASN GLN GLY LEU ILE
SEQRES 18 F 423 ARG ALA VAL GLU LYS PHE GLU TYR LYS ARG ARG PHE LYS
SEQRES 19 F 423 PHE SER THR TYR ALA THR TRP TRP ILE ARG GLN ALA ILE
SEQRES 20 F 423 ASN ARG ALA ILE ALA ASP GLN ALA ARG THR ILE ARG ILE
SEQRES 21 F 423 PRO VAL HIS MET VAL GLU THR ILE ASN LYS LEU SER ARG
SEQRES 22 F 423 THR ALA ARG GLN LEU GLN GLN GLU LEU GLY ARG GLU PRO
SEQRES 23 F 423 THR TYR GLU GLU ILE ALA GLU ALA MET GLY PRO GLY TRP
SEQRES 24 F 423 ASP ALA LYS ARG VAL GLU GLU THR LEU LYS ILE ALA GLN
SEQRES 25 F 423 GLU PRO VAL SER LEU GLU THR PRO ILE GLY ASP GLU LYS
SEQRES 26 F 423 ASP SER PHE TYR GLY ASP PHE ILE PRO ASP GLU HIS LEU
SEQRES 27 F 423 PRO SER PRO VAL ASP ALA ALA THR GLN SER LEU LEU SER
SEQRES 28 F 423 GLU GLU LEU GLU LYS ALA LEU SER LYS LEU SER GLU ARG
SEQRES 29 F 423 GLU ALA MET VAL LEU LYS LEU ARG LYS GLY LEU ILE ASP
SEQRES 30 F 423 GLY ARG GLU HIS THR LEU GLU GLU VAL GLY ALA PHE PHE
SEQRES 31 F 423 GLY VAL THR ARG GLU ARG ILE ARG GLN ILE GLU ASN LYS
SEQRES 32 F 423 ALA LEU ARG LYS LEU LYS TYR HIS GLU SER ARG THR ARG
SEQRES 33 F 423 LYS LEU ARG ASP PHE LEU ASP
HET PO4 A 401 5
HET NE6 C1201 30
HET ZN D1601 1
HET ZN D1602 1
HET PO4 D1603 5
HET MG D1604 1
HET MG D1605 1
HETNAM PO4 PHOSPHATE ION
HETNAM NE6 METHYL [(1E,5R)-5-{(3S)-3-[(2E,4E)-2,5-DIMETHYLOCTA-2,
HETNAM 2 NE6 4-DIENOYL]-2,4-DIOXO-3,4-DIHYDRO-2H-PYRAN-6-
HETNAM 3 NE6 YL}HEXYLIDENE]CARBAMATE
HETNAM ZN ZINC ION
HETNAM MG MAGNESIUM ION
FORMUL 7 PO4 2(O4 P 3-)
FORMUL 8 NE6 C23 H31 N O6
FORMUL 9 ZN 2(ZN 2+)
FORMUL 12 MG 2(MG 2+)
FORMUL 14 HOH *49(H2 O)
HELIX 1 AA1 GLY A 31 ILE A 48 1 18
HELIX 2 AA2 ASP A 74 GLU A 84 1 11
HELIX 3 AA3 ARG A 112 PHE A 114 5 3
HELIX 4 AA4 PRO A 152 HIS A 156 5 5
HELIX 5 AA5 THR A 206 GLU A 220 1 15
HELIX 6 AA6 HIS A 221 SER A 226 5 6
HELIX 7 AA7 GLY B 31 SER B 47 1 17
HELIX 8 AA8 ASP B 74 LYS B 83 1 10
HELIX 9 AA9 THR B 206 THR B 223 1 18
HELIX 10 AB1 THR C 19 GLN C 31 1 13
HELIX 11 AB2 GLY C 43 PHE C 52 1 10
HELIX 12 AB3 PRO C 79 LYS C 86 1 8
HELIX 13 AB4 LEU C 195 LEU C 200 1 6
HELIX 14 AB5 ASP C 203 ALA C 208 1 6
HELIX 15 AB6 PRO C 231 ARG C 237 1 7
HELIX 16 AB7 LEU C 238 LEU C 242 5 5
HELIX 17 AB8 PRO C 247 ASP C 251 5 5
HELIX 18 AB9 ALA C 272 LEU C 281 1 10
HELIX 19 AC1 VAL C 302 THR C 314 1 13
HELIX 20 AC2 THR C 335 MET C 361 1 27
HELIX 21 AC3 SER C 375 SER C 389 1 15
HELIX 22 AC4 ASN C 399 ARG C 408 1 10
HELIX 23 AC5 HIS C 431 TYR C 435 5 5
HELIX 24 AC6 THR C 487 ASP C 492 1 6
HELIX 25 AC7 SER C 525 VAL C 529 5 5
HELIX 26 AC8 SER C 535 PHE C 540 5 6
HELIX 27 AC9 SER C 541 LEU C 546 1 6
HELIX 28 AD1 PHE C 549 ASP C 553 5 5
HELIX 29 AD2 ASP C 554 ALA C 568 1 15
HELIX 30 AD3 LEU C 583 SER C 591 1 9
HELIX 31 AD4 GLU C 692 ARG C 697 1 6
HELIX 32 AD5 GLY C 763 GLU C 766 5 4
HELIX 33 AD6 THR C 768 ILE C 777 1 10
HELIX 34 AD7 ASN C 872 VAL C 876 5 5
HELIX 35 AD8 LEU C 882 GLY C 898 1 17
HELIX 36 AD9 LYS C 910 PHE C 926 1 17
HELIX 37 AE1 ASP C 937 LEU C 950 1 14
HELIX 38 AE2 THR C 958 LEU C 968 1 11
HELIX 39 AE3 MET C 1000 LYS C 1004 5 5
HELIX 40 AE4 GLU C 1034 GLY C 1044 1 11
HELIX 41 AE5 ALA C 1045 THR C 1054 1 10
HELIX 42 AE6 ASP C 1059 LYS C 1072 1 14
HELIX 43 AE7 PRO C 1082 ALA C 1094 1 13
HELIX 44 AE8 SER D 14 SER D 22 1 9
HELIX 45 AE9 ASP D 46 GLY D 51 1 6
HELIX 46 AF1 LYS D 82 TYR D 88 5 7
HELIX 47 AF2 ILE D 102 ASP D 107 1 6
HELIX 48 AF3 SER D 110 ASP D 117 1 8
HELIX 49 AF4 SER D 119 TYR D 128 1 10
HELIX 50 AF5 THR D 154 ARG D 162 1 9
HELIX 51 AF6 LEU D 178 GLY D 182 5 5
HELIX 52 AF7 MET D 456 LEU D 468 1 13
HELIX 53 AF8 ASP D 469 GLU D 479 1 11
HELIX 54 AF9 SER D 485 LYS D 491 1 7
HELIX 55 AG1 ARG D 493 GLY D 506 1 14
HELIX 56 AG2 ARG D 508 TRP D 511 5 4
HELIX 57 AG3 PRO D 521 ARG D 525 5 5
HELIX 58 AG4 SER D 538 GLY D 561 1 24
HELIX 59 AG5 PRO D 563 ASP D 583 1 21
HELIX 60 AG6 SER D 602 GLY D 609 1 8
HELIX 61 AG7 LYS D 646 PHE D 653 1 8
HELIX 62 AG8 PHE D 653 LYS D 664 1 12
HELIX 63 AG9 ASN D 669 GLU D 678 1 10
HELIX 64 AH1 ARG D 679 ILE D 683 5 5
HELIX 65 AH2 ASP D 685 ILE D 695 1 11
HELIX 66 AH3 HIS D 709 LEU D 711 5 3
HELIX 67 AH4 HIS D 729 LEU D 731 5 3
HELIX 68 AH5 VAL D 732 ASN D 737 1 6
HELIX 69 AH6 SER D 752 GLN D 762 1 11
HELIX 70 AH7 LEU D 764 ASN D 768 5 5
HELIX 71 AH8 ARG D 783 GLN D 794 1 12
HELIX 72 AH9 ALA D 807 ARG D 818 1 12
HELIX 73 AI1 ASN D 845 HIS D 855 1 11
HELIX 74 AI2 SER D 876 VAL D 890 1 15
HELIX 75 AI3 ASP D 892 GLU D 898 1 7
HELIX 76 AI4 GLU D 907 LEU D 922 1 16
HELIX 77 AI5 MET D 924 GLY D 946 1 23
HELIX 78 AI6 GLY D 950 ALA D 954 5 5
HELIX 79 AI7 GLU D 959 MET D 980 1 22
HELIX 80 AI8 THR D 984 TYR D 1015 1 32
HELIX 81 AI9 ASN D 1018 SER D 1026 1 9
HELIX 82 AJ1 ASN D 1031 GLY D 1040 1 10
HELIX 83 AJ2 THR D 1066 ALA D 1085 1 20
HELIX 84 AJ3 SER D 1091 HIS D 1103 1 13
HELIX 85 AJ4 LYS D 1136 TYR D 1145 1 10
HELIX 86 AJ5 SER D 1167 ALA D 1180 1 14
HELIX 87 AJ6 CYS D 1201 GLY D 1206 1 6
HELIX 88 AJ7 ALA D 1220 THR D 1234 1 15
HELIX 89 AJ8 GLY D 1255 GLU D 1264 1 10
HELIX 90 AJ9 ASP D 1331 ALA D 1358 1 28
HELIX 91 AK1 HIS D 1364 MET D 1376 1 13
HELIX 92 AK2 GLY D 1423 SER D 1430 1 8
HELIX 93 AK3 SER D 1433 ALA D 1438 1 6
HELIX 94 AK4 ASN D 1442 GLY D 1454 1 13
HELIX 95 AK5 LEU D 1462 ILE D 1467 1 6
HELIX 96 AK6 ALA D 1474 GLY D 1477 5 4
HELIX 97 AK7 SER D 1478 PHE D 1483 1 6
HELIX 98 AK8 LYS D 1490 LYS D 1493 5 4
HELIX 99 AK9 ALA D 1494 LYS D 1500 1 7
HELIX 100 AL1 GLY E 5 MET E 12 1 8
HELIX 101 AL2 SER E 15 HIS E 33 1 19
HELIX 102 AL3 GLU E 41 ARG E 45 5 5
HELIX 103 AL4 ASN E 59 THR E 70 1 12
HELIX 104 AL5 GLU E 88 TYR E 93 1 6
HELIX 105 AL6 ASP F 79 LEU F 85 1 7
HELIX 106 AL7 THR F 95 GLY F 121 1 27
HELIX 107 AL8 ASP F 123 GLY F 137 1 15
HELIX 108 AL9 LYS F 154 SER F 165 1 12
HELIX 109 AM1 PRO F 167 ASN F 191 1 25
HELIX 110 AM2 ASN F 191 LYS F 200 1 10
HELIX 111 AM3 SER F 208 PHE F 227 1 20
HELIX 112 AM4 LYS F 234 ALA F 255 1 22
HELIX 113 AM5 PRO F 261 GLY F 283 1 23
HELIX 114 AM6 THR F 287 GLY F 296 1 10
HELIX 115 AM7 ASP F 300 GLN F 312 1 13
HELIX 116 AM8 PHE F 328 ILE F 333 5 6
HELIX 117 AM9 SER F 340 LYS F 360 1 21
HELIX 118 AN1 SER F 362 LYS F 373 1 12
HELIX 119 AN2 HIS F 381 VAL F 386 1 6
HELIX 120 AN3 THR F 393 GLU F 395 5 3
HELIX 121 AN4 ARG F 396 THR F 415 1 20
HELIX 122 AN5 LYS F 417 LEU F 422 5 6
SHEET 1 AA1 4 VAL A 10 THR A 15 0
SHEET 2 AA1 4 TYR A 20 LEU A 28 -1 O GLU A 26 N VAL A 10
SHEET 3 AA1 4 ARG A 189 THR A 201 -1 O LEU A 197 N PHE A 23
SHEET 4 AA1 4 VAL A 174 LEU A 186 -1 N GLN A 180 O THR A 196
SHEET 1 AA2 4 THR A 96 ALA A 103 0
SHEET 2 AA2 4 LEU A 138 GLY A 147 -1 O VAL A 144 N VAL A 97
SHEET 3 AA2 4 GLY A 50 ILE A 58 -1 N SER A 55 O ARG A 143
SHEET 4 AA2 4 ALA A 164 PRO A 166 -1 O ILE A 165 N VAL A 56
SHEET 1 AA3 2 VAL A 87 PHE A 89 0
SHEET 2 AA3 2 VAL A 120 ILE A 122 -1 O GLU A 121 N ARG A 88
SHEET 1 AA4 2 LYS A 107 LYS A 110 0
SHEET 2 AA4 2 HIS A 128 LEU A 132 -1 O LEU A 132 N LYS A 107
SHEET 1 AA5 2 TYR A 150 VAL A 151 0
SHEET 2 AA5 2 ALA A 169 VAL A 170 -1 O ALA A 169 N VAL A 151
SHEET 1 AA6 4 VAL B 10 GLN B 16 0
SHEET 2 AA6 4 TYR B 20 LEU B 28 -1 O VAL B 24 N THR B 12
SHEET 3 AA6 4 ARG B 189 THR B 201 -1 O ASP B 193 N LEU B 28
SHEET 4 AA6 4 VAL B 174 LEU B 186 -1 N ALA B 178 O ARG B 198
SHEET 1 AA7 4 THR B 96 GLU B 104 0
SHEET 2 AA7 4 ARG B 137 VAL B 148 -1 O VAL B 144 N VAL B 97
SHEET 3 AA7 4 PRO B 49 ILE B 58 -1 N THR B 54 O ARG B 143
SHEET 4 AA7 4 ILE B 165 PRO B 166 -1 O ILE B 165 N VAL B 56
SHEET 1 AA8 2 VAL B 87 PHE B 89 0
SHEET 2 AA8 2 VAL B 120 ILE B 122 -1 O GLU B 121 N ARG B 88
SHEET 1 AA9 2 GLU B 108 VAL B 109 0
SHEET 2 AA9 2 ALA B 130 THR B 131 -1 O ALA B 130 N VAL B 109
SHEET 1 AB1 2 TYR B 150 VAL B 151 0
SHEET 2 AB1 2 ALA B 169 VAL B 170 -1 O ALA B 169 N VAL B 151
SHEET 1 AB2 3 GLU C 2 ARG C 5 0
SHEET 2 AB2 3 GLN C 899 ILE C 902 1 O ILE C 902 N LYS C 4
SHEET 3 AB2 3 VAL C 579 MET C 580 1 N MET C 580 O TYR C 901
SHEET 1 AB3 3 ILE C 54 GLU C 56 0
SHEET 2 AB3 3 LEU C 64 LEU C 66 -1 O LEU C 66 N ILE C 54
SHEET 3 AB3 3 LEU C 100 ILE C 101 -1 O ILE C 101 N VAL C 65
SHEET 1 AB4 3 ARG C 72 LEU C 73 0
SHEET 2 AB4 3 GLN C 91 TYR C 95 -1 O TYR C 95 N ARG C 72
SHEET 3 AB4 3 HIS C 117 PRO C 119 -1 O ILE C 118 N ALA C 92
SHEET 1 AB5 3 PHE C 127 ILE C 129 0
SHEET 2 AB5 3 ALA C 132 ILE C 136 -1 O ALA C 132 N ILE C 129
SHEET 3 AB5 3 SER C 392 PHE C 394 -1 O GLN C 393 N VAL C 135
SHEET 1 AB6 4 ARG C 331 ARG C 334 0
SHEET 2 AB6 4 SER C 138 ARG C 142 -1 N GLN C 139 O ARG C 334
SHEET 3 AB6 4 ARG C 409 SER C 411 1 O SER C 411 N SER C 138
SHEET 4 AB6 4 THR C 453 SER C 454 -1 O THR C 453 N ILE C 410
SHEET 1 AB7 5 GLY C 145 PRO C 150 0
SHEET 2 AB7 5 TYR C 158 ILE C 163 -1 O ILE C 163 N GLY C 145
SHEET 3 AB7 5 ILE C 172 LEU C 174 -1 O LEU C 174 N ALA C 160
SHEET 4 AB7 5 SER C 183 LYS C 185 -1 O LYS C 185 N ASP C 173
SHEET 5 AB7 5 LYS C 190 PRO C 192 -1 O PHE C 191 N MET C 184
SHEET 1 AB8 3 ARG C 460 VAL C 461 0
SHEET 2 AB8 3 ILE C 467 VAL C 475 -1 O ARG C 468 N ARG C 460
SHEET 3 AB8 3 VAL C 478 MET C 486 -1 O VAL C 484 N TYR C 471
SHEET 1 AB9 6 ARG C 460 VAL C 461 0
SHEET 2 AB9 6 ILE C 467 VAL C 475 -1 O ARG C 468 N ARG C 460
SHEET 3 AB9 6 PHE C 531 ASP C 533 -1 O MET C 532 N ARG C 472
SHEET 4 AB9 6 THR C 495 ALA C 497 1 N ALA C 497 O PHE C 531
SHEET 5 AB9 6 VAL C 513 ARG C 517 -1 O ARG C 516 N ILE C 496
SHEET 6 AB9 6 GLU C 520 VAL C 524 -1 O VAL C 524 N VAL C 513
SHEET 1 AC1 2 LEU C 503 GLU C 504 0
SHEET 2 AC1 2 ARG C 507 ILE C 508 -1 O ARG C 507 N GLU C 504
SHEET 1 AC2 3 LEU C 595 TYR C 596 0
SHEET 2 AC2 3 LEU C 654 ASP C 657 -1 O LEU C 655 N LEU C 595
SHEET 3 AC2 3 ARG C 640 PRO C 641 -1 N ARG C 640 O ASP C 657
SHEET 1 AC3 4 LEU C 620 PRO C 624 0
SHEET 2 AC3 4 ARG C 610 TYR C 615 -1 N ILE C 611 O TYR C 623
SHEET 3 AC3 4 GLY C 601 ASP C 607 -1 N ALA C 604 O VAL C 612
SHEET 4 AC3 4 ARG C 648 VAL C 649 -1 O VAL C 649 N GLY C 601
SHEET 1 AC4 2 TYR C 629 ARG C 630 0
SHEET 2 AC4 2 ALA C 636 LEU C 637 -1 O LEU C 637 N TYR C 629
SHEET 1 AC5 2 SER C 661 GLU C 662 0
SHEET 2 AC5 2 PHE C 665 LEU C 666 -1 O PHE C 665 N GLU C 662
SHEET 1 AC6 8 LYS C 971 VAL C 972 0
SHEET 2 AC6 8 ILE C 987 LYS C 996 -1 O ILE C 987 N VAL C 972
SHEET 3 AC6 8 LYS C 838 ALA C 840 -1 N ALA C 840 O MET C 995
SHEET 4 AC6 8 LYS C 846 LEU C 853 -1 O GLY C 847 N LEU C 839
SHEET 5 AC6 8 ILE C 688 SER C 691 1 N ILE C 688 O ALA C 850
SHEET 6 AC6 8 VAL C 869 LEU C 871 -1 O ILE C 870 N VAL C 689
SHEET 7 AC6 8 GLN C 670 ILE C 676 1 N LEU C 673 O VAL C 869
SHEET 8 AC6 8 ILE C 987 LYS C 996 -1 O ILE C 994 N GLN C 670
SHEET 1 AC7 4 SER C 702 ARG C 713 0
SHEET 2 AC7 4 VAL C 819 ARG C 831 -1 O ARG C 820 N ALA C 712
SHEET 3 AC7 4 GLY C 798 ARG C 807 -1 N VAL C 804 O ARG C 824
SHEET 4 AC7 4 GLU C 748 VAL C 749 -1 N VAL C 749 O GLY C 798
SHEET 1 AC8 3 ARG C 721 ILE C 722 0
SHEET 2 AC8 3 ARG C 758 PHE C 761 -1 O THR C 759 N ARG C 721
SHEET 3 AC8 3 VAL C 785 ASP C 787 -1 O LYS C 786 N SER C 760
SHEET 1 AC9 2 ILE C 754 VAL C 756 0
SHEET 2 AC9 2 LEU C 790 ARG C 791 -1 O LEU C 790 N LEU C 755
SHEET 1 AD1 8 HIS C1006 ARG C1008 0
SHEET 2 AD1 8 SER D 626 VAL D 633 -1 O SER D 626 N ARG C1008
SHEET 3 AD1 8 GLN D 744 HIS D 748 -1 O VAL D 747 N GLY D 627
SHEET 4 AD1 8 VAL D 700 ASN D 703 -1 N ASN D 703 O ALA D 746
SHEET 5 AD1 8 ILE D 713 VAL D 721 -1 O PHE D 716 N VAL D 700
SHEET 6 AD1 8 GLN D 641 PRO D 645 1 N LEU D 644 O VAL D 721
SHEET 7 AD1 8 ILE D 726 LEU D 728 -1 O GLN D 727 N GLY D 643
SHEET 8 AD1 8 SER D 626 VAL D 633 1 N VAL D 632 O LEU D 728
SHEET 1 AD2 2 GLN C1030 GLY C1033 0
SHEET 2 AD2 2 GLY D 620 VAL D 623 -1 O LYS D 621 N PHE C1032
SHEET 1 AD3 3 LEU C1097 LEU C1102 0
SHEET 2 AD3 3 LYS D 7 LEU D 12 -1 O LYS D 7 N LEU C1102
SHEET 3 AD3 3 LYS D1456 GLU D1458 -1 O ASP D1457 N VAL D 8
SHEET 1 AD4 2 GLY D 91 ALA D 100 0
SHEET 2 AD4 2 ILE D 513 VAL D 519 -1 O LEU D 514 N ALA D 99
SHEET 1 AD5 3 LEU D 152 LEU D 153 0
SHEET 2 AD5 3 TYR D 132 ASP D 136 -1 N TYR D 132 O LEU D 153
SHEET 3 AD5 3 ASP D 453 ARG D 455 -1 O ASP D 453 N ASP D 136
SHEET 1 AD6 2 GLN D 166 PRO D 170 0
SHEET 2 AD6 2 SER D 392 VAL D 396 -1 O ILE D 393 N TYR D 169
SHEET 1 AD7 3 PHE D 336 GLU D 341 0
SHEET 2 AD7 3 ARG D 210 ARG D 220 -1 N TYR D 215 O GLU D 341
SHEET 3 AD7 3 ASP D 344 ARG D 346 -1 O TYR D 345 N VAL D 211
SHEET 1 AD8 4 PHE D 336 GLU D 341 0
SHEET 2 AD8 4 ARG D 210 ARG D 220 -1 N TYR D 215 O GLU D 341
SHEET 3 AD8 4 GLY D 383 LEU D 387 -1 O HIS D 386 N ARG D 212
SHEET 4 AD8 4 ARG D 360 VAL D 361 -1 N VAL D 361 O GLY D 383
SHEET 1 AD9 2 LEU D 223 LEU D 225 0
SHEET 2 AD9 2 VAL D 331 LEU D 333 -1 O LEU D 333 N LEU D 223
SHEET 1 AE1 3 ASN D 352 VAL D 353 0
SHEET 2 AE1 3 LYS D 366 ALA D 369 -1 O ALA D 369 N ASN D 352
SHEET 3 AE1 3 VAL D 377 ILE D 378 -1 O VAL D 377 N ILE D 367
SHEET 1 AE2 4 ALA D 398 TYR D 401 0
SHEET 2 AE2 4 VAL D 444 GLU D 448 -1 O VAL D 444 N TYR D 401
SHEET 3 AE2 4 GLY D 433 VAL D 435 -1 N ARG D 434 O VAL D 447
SHEET 4 AE2 4 ARG D 414 VAL D 415 -1 N VAL D 415 O GLY D 433
SHEET 1 AE3 3 MET D 527 GLN D 529 0
SHEET 2 AE3 3 PHE D 535 THR D 537 -1 O ALA D 536 N VAL D 528
SHEET 3 AE3 3 VAL F 315 SER F 316 1 O VAL F 315 N THR D 537
SHEET 1 AE4 3 VAL D 842 PHE D 843 0
SHEET 2 AE4 3 VAL D 864 TYR D 868 1 O THR D 865 N PHE D 843
SHEET 3 AE4 3 LYS D 871 THR D 875 -1 O THR D 875 N VAL D 864
SHEET 1 AE5 3 ILE D1118 PRO D1121 0
SHEET 2 AE5 3 GLU D1185 ARG D1189 -1 O VAL D1188 N ILE D1118
SHEET 3 AE5 3 VAL D1148 LEU D1149 -1 N VAL D1148 O ARG D1189
SHEET 1 AE6 2 VAL D1153 VAL D1155 0
SHEET 2 AE6 2 VAL D1158 LEU D1160 -1 O LEU D1160 N VAL D1153
SHEET 1 AE7 4 SER D1300 LYS D1304 0
SHEET 2 AE7 4 LEU D1290 GLU D1295 -1 N VAL D1292 O TYR D1303
SHEET 3 AE7 4 GLY D1279 GLU D1285 -1 N ARG D1282 O PHE D1293
SHEET 4 AE7 4 TYR D1318 VAL D1319 -1 O VAL D1319 N GLY D1279
SHEET 1 AE8 3 GLY D1392 VAL D1394 0
SHEET 2 AE8 3 TYR D1378 ASP D1383 -1 N VAL D1379 O GLN D1393
SHEET 3 AE8 3 ALA D1416 PRO D1419 -1 O LYS D1418 N GLU D1380
SHEET 1 AE9 2 GLN D1485 ASP D1488 0
SHEET 2 AE9 2 LEU E 73 GLY E 76 -1 O GLY E 76 N GLN D1485
LINK SG CYS D 58 ZN ZN D1601 1555 1555 2.40
LINK SG CYS D 60 ZN ZN D1601 1555 1555 2.38
LINK SG CYS D 73 ZN ZN D1601 1555 1555 2.40
LINK SG CYS D 76 ZN ZN D1601 1555 1555 2.38
LINK OD1 ASP D 739 MG MG D1605 1555 1555 2.73
LINK OD1 ASP D 741 MG MG D1605 1555 1555 2.58
LINK OD2 ASP D 741 MG MG D1605 1555 1555 2.98
LINK OD1 ASP D 743 MG MG D1605 1555 1555 2.61
LINK O LYS D 840 MG MG D1604 1555 1555 2.21
LINK SG CYS D1112 ZN ZN D1602 1555 1555 2.39
LINK SG CYS D1194 ZN ZN D1602 1555 1555 2.38
LINK SG CYS D1201 ZN ZN D1602 1555 1555 2.39
LINK SG CYS D1204 ZN ZN D1602 1555 1555 2.40
CISPEP 1 GLU A 26 PRO A 27 0 -12.04
CISPEP 2 LEU B 2 ASP B 3 0 -0.01
CISPEP 3 GLU B 26 PRO B 27 0 -5.11
CISPEP 4 PHE C 52 PRO C 53 0 3.37
CISPEP 5 ARG C 243 PRO C 244 0 6.65
CISPEP 6 VAL D 108 PRO D 109 0 1.59
CISPEP 7 GLU D 247 PRO D 248 0 -12.89
CISPEP 8 ALA D 416 PRO D 417 0 0.40
CISPEP 9 ARG D 613 PHE D 614 0 6.68
CISPEP 10 ARG D 615 GLN D 616 0 -18.05
CISPEP 11 ALA D 705 PRO D 706 0 -2.58
CISPEP 12 VAL D 836 GLY D 837 0 27.17
CISPEP 13 ALA D 1265 ARG D 1266 0 -7.86
CISPEP 14 GLU F 313 PRO F 314 0 6.52
SITE 1 AC1 5 THR A 51 ALA A 52 LYS A 83 LEU A 85
SITE 2 AC1 5 VAL A 170
SITE 1 AC2 11 PHE C1032 VAL C1037 TRP C1038 GLU C1041
SITE 2 AC2 11 SER C1084 PHE D 614 LEU D 619 VAL D1099
SITE 3 AC2 11 HIS D1103 LYS D1463 ILE D1467
SITE 1 AC3 4 CYS D 58 CYS D 60 CYS D 73 CYS D 76
SITE 1 AC4 5 CYS D1112 CYS D1194 GLN D1195 CYS D1201
SITE 2 AC4 5 CYS D1204
SITE 1 AC5 2 ASP D 952 TYR D1015
SITE 1 AC6 2 ASP B 168 LYS D 840
SITE 1 AC7 3 ASP D 739 ASP D 741 ASP D 743
CRYST1 235.090 235.090 250.880 90.00 90.00 120.00 P 65 12
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.004254 0.002456 0.000000 0.00000
SCALE2 0.000000 0.004912 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003986 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
