HEADER TRANSCRIPTION/DNA/RNA 05-MAR-15 4YLP
TITLE E. COLI TRANSCRIPTION INITIATION COMPLEX - 16-BP SPACER AND 5-NT RNA
CAVEAT 4YLP ENTRY CONTAINS IMPROPER NUCLEOTIDE LINKAGES.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA-DIRECTED RNA POLYMERASE SUBUNIT ALPHA;
COMPND 3 CHAIN: A, B, G, H, M, N;
COMPND 4 FRAGMENT: N-TERMINAL DOMAIN (UNP RESIDUES 1-235);
COMPND 5 SYNONYM: RNAP SUBUNIT ALPHA, RNA POLYMERASE SUBUNIT ALPHA,
COMPND 6 TRANSCRIPTASE SUBUNIT ALPHA;
COMPND 7 EC: 2.7.7.6;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: DNA-DIRECTED RNA POLYMERASE SUBUNIT BETA;
COMPND 11 CHAIN: C, I, O;
COMPND 12 SYNONYM: RNAP SUBUNIT BETA, RNA POLYMERASE SUBUNIT BETA,
COMPND 13 TRANSCRIPTASE SUBUNIT BETA;
COMPND 14 EC: 2.7.7.6;
COMPND 15 ENGINEERED: YES;
COMPND 16 MOL_ID: 3;
COMPND 17 MOLECULE: DNA-DIRECTED RNA POLYMERASE SUBUNIT BETA';
COMPND 18 CHAIN: D, J, P;
COMPND 19 SYNONYM: RNAP SUBUNIT BETA', RNA POLYMERASE SUBUNIT BETA',
COMPND 20 TRANSCRIPTASE SUBUNIT BETA';
COMPND 21 EC: 2.7.7.6;
COMPND 22 ENGINEERED: YES;
COMPND 23 MOL_ID: 4;
COMPND 24 MOLECULE: DNA-DIRECTED RNA POLYMERASE SUBUNIT OMEGA;
COMPND 25 CHAIN: E, K, Q;
COMPND 26 SYNONYM: RNAP OMEGA SUBUNIT, RNA POLYMERASE OMEGA SUBUNIT,
COMPND 27 TRANSCRIPTASE SUBUNIT OMEGA;
COMPND 28 EC: 2.7.7.6;
COMPND 29 ENGINEERED: YES;
COMPND 30 MOL_ID: 5;
COMPND 31 MOLECULE: RNA POLYMERASE SIGMA FACTOR RPOD;
COMPND 32 CHAIN: F, L, R;
COMPND 33 SYNONYM: SIGMA-70;
COMPND 34 ENGINEERED: YES;
COMPND 35 MOL_ID: 6;
COMPND 36 MOLECULE: NT STRAND DNA (49-MER);
COMPND 37 CHAIN: 1, 4, 7;
COMPND 38 ENGINEERED: YES;
COMPND 39 MOL_ID: 7;
COMPND 40 MOLECULE: T STRAND DNA (49-MER);
COMPND 41 CHAIN: 2, 5, 8;
COMPND 42 ENGINEERED: YES;
COMPND 43 MOL_ID: 8;
COMPND 44 MOLECULE: RNA (5'-R(*(GTP))-R(P*AP*GP*UP*C)-3');
COMPND 45 CHAIN: 3, 6, 9;
COMPND 46 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: RPOA, ECE24377A_3778;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 MOL_ID: 2;
SOURCE 8 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 9 ORGANISM_TAXID: 562;
SOURCE 10 GENE: RPOB, ECE24377A_4528;
SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 12 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 13 MOL_ID: 3;
SOURCE 14 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 15 ORGANISM_TAXID: 562;
SOURCE 16 GENE: RPOC, ECE24377A_4529;
SOURCE 17 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 18 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 19 MOL_ID: 4;
SOURCE 20 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 21 ORGANISM_TAXID: 562;
SOURCE 22 GENE: RPOZ, ECE24377A_4152;
SOURCE 23 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 24 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 25 MOL_ID: 5;
SOURCE 26 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 27 ORGANISM_TAXID: 562;
SOURCE 28 GENE: RPOD, ALT, B3067, JW3039;
SOURCE 29 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 30 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 31 MOL_ID: 6;
SOURCE 32 SYNTHETIC: YES;
SOURCE 33 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 34 ORGANISM_TAXID: 32630;
SOURCE 35 MOL_ID: 7;
SOURCE 36 SYNTHETIC: YES;
SOURCE 37 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 38 ORGANISM_TAXID: 32630;
SOURCE 39 MOL_ID: 8;
SOURCE 40 SYNTHETIC: YES;
SOURCE 41 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 42 ORGANISM_TAXID: 32630
KEYWDS RNA POLYMERASE, INITIATION COMPLEX, DNA BUBBLE, TRANSCRIPTION-DNA-RNA
KEYWDS 2 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.ZUO,T.A.STEITZ
REVDAT 6 25-DEC-19 4YLP 1 REMARK
REVDAT 5 06-SEP-17 4YLP 1 REMARK
REVDAT 4 14-SEP-16 4YLP 1 COMPND
REVDAT 3 20-MAY-15 4YLP 1 JRNL
REVDAT 2 29-APR-15 4YLP 1 JRNL
REVDAT 1 22-APR-15 4YLP 0
JRNL AUTH Y.ZUO,T.A.STEITZ
JRNL TITL CRYSTAL STRUCTURES OF THE E. COLI TRANSCRIPTION INITIATION
JRNL TITL 2 COMPLEXES WITH A COMPLETE BUBBLE.
JRNL REF MOL.CELL V. 58 534 2015
JRNL REFN ISSN 1097-2765
JRNL PMID 25866247
JRNL DOI 10.1016/J.MOLCEL.2015.03.010
REMARK 2
REMARK 2 RESOLUTION. 5.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0073
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 5.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.98
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 3 NUMBER OF REFLECTIONS : 64596
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) : 0.235
REMARK 3 R VALUE (WORKING SET) : 0.231
REMARK 3 FREE R VALUE : 0.313
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3384
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) : 5.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 5.64
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4099
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 86.07
REMARK 3 BIN R VALUE (WORKING SET) : 0.3740
REMARK 3 BIN FREE R VALUE SET COUNT : 219
REMARK 3 BIN FREE R VALUE : 0.4080
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 88284
REMARK 3 NUCLEIC ACID ATOMS : 6375
REMARK 3 HETEROGEN ATOMS : 9
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 198.8
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.96000
REMARK 3 B22 (A**2) : 0.15000
REMARK 3 B33 (A**2) : -0.98000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.37000
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): 2.135
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 3.017
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 740.950
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.945
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.896
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 96712 ; 0.011 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES):131896 ; 1.547 ; 1.913
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 11223 ; 6.541 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 4215 ;27.887 ;24.107
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 16674 ;21.308 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 831 ;16.610 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 14712 ; 0.114 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 70272 ; 0.007 ; 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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 33
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 6 232 B 6 232 245 0.17 0.05
REMARK 3 2 A 6 235 G 6 235 261 0.13 0.05
REMARK 3 3 A 6 232 H 6 232 240 0.17 0.05
REMARK 3 4 A 6 235 M 6 235 260 0.12 0.05
REMARK 3 5 A 6 232 N 6 232 238 0.18 0.05
REMARK 3 6 B 6 232 G 6 232 244 0.15 0.05
REMARK 3 7 B 6 233 H 6 233 269 0.11 0.05
REMARK 3 8 B 6 232 M 6 232 247 0.15 0.05
REMARK 3 9 B 6 233 N 6 233 265 0.09 0.05
REMARK 3 10 C 2 1342 I 2 1342 1675 0.14 0.05
REMARK 3 11 C 2 1342 O 2 1342 1641 0.13 0.05
REMARK 3 12 D 15 1376 J 15 1376 1699 0.14 0.05
REMARK 3 13 D 15 1376 P 15 1376 1680 0.14 0.05
REMARK 3 14 E 2 91 K 2 91 102 0.11 0.05
REMARK 3 15 E 2 91 Q 2 91 104 0.14 0.05
REMARK 3 16 F 79 613 L 79 613 652 0.14 0.05
REMARK 3 17 F 79 613 R 79 613 662 0.13 0.05
REMARK 3 18 1 12 60 4 12 60 231 0.10 0.05
REMARK 3 19 1 12 60 7 12 60 225 0.11 0.05
REMARK 3 20 2 3 51 5 3 51 204 0.13 0.05
REMARK 3 21 2 3 51 8 3 51 209 0.11 0.05
REMARK 3 22 G 6 232 H 6 232 240 0.15 0.05
REMARK 3 23 G 6 235 M 6 235 267 0.10 0.05
REMARK 3 24 G 6 232 N 6 232 240 0.16 0.05
REMARK 3 25 H 6 232 M 6 232 238 0.15 0.05
REMARK 3 26 H 6 233 N 6 233 257 0.11 0.05
REMARK 3 27 I 2 1342 O 2 1342 1644 0.13 0.05
REMARK 3 28 J 15 1376 P 15 1376 1680 0.13 0.05
REMARK 3 29 K 2 91 Q 2 91 100 0.15 0.05
REMARK 3 30 L 79 613 R 79 613 658 0.12 0.05
REMARK 3 31 4 12 60 7 12 60 225 0.14 0.05
REMARK 3 32 5 3 51 8 3 51 204 0.14 0.05
REMARK 3 33 M 6 232 N 6 232 242 0.16 0.05
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 45
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 4
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 6 A 51
REMARK 3 RESIDUE RANGE : A 179 A 235
REMARK 3 RESIDUE RANGE : B 6 B 51
REMARK 3 RESIDUE RANGE : B 179 B 233
REMARK 3 ORIGIN FOR THE GROUP (A): -58.1310 -5.2800 239.7840
REMARK 3 T TENSOR
REMARK 3 T11: 1.3830 T22: 0.4662
REMARK 3 T33: 1.4011 T12: -0.2301
REMARK 3 T13: 0.2987 T23: -0.1754
REMARK 3 L TENSOR
REMARK 3 L11: 6.8611 L22: 1.4203
REMARK 3 L33: 6.5835 L12: 0.9844
REMARK 3 L13: 1.8082 L23: -0.5993
REMARK 3 S TENSOR
REMARK 3 S11: -0.3942 S12: -0.5831 S13: -0.1386
REMARK 3 S21: 0.0154 S22: -0.0419 S23: 0.2494
REMARK 3 S31: 0.4041 S32: 0.2178 S33: 0.4360
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 52 A 178
REMARK 3 ORIGIN FOR THE GROUP (A): -51.4820 -0.1940 203.9350
REMARK 3 T TENSOR
REMARK 3 T11: 1.1781 T22: 0.7951
REMARK 3 T33: 1.1724 T12: 0.1521
REMARK 3 T13: 0.2251 T23: -0.4435
REMARK 3 L TENSOR
REMARK 3 L11: 8.1246 L22: 6.9140
REMARK 3 L33: 5.2021 L12: -1.9853
REMARK 3 L13: 2.3030 L23: -1.4447
REMARK 3 S TENSOR
REMARK 3 S11: 0.0498 S12: -0.3834 S13: -0.0468
REMARK 3 S21: 0.2634 S22: 0.0403 S23: -0.2748
REMARK 3 S31: 0.0471 S32: -0.5042 S33: -0.0902
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 : B 52 B 178
REMARK 3 ORIGIN FOR THE GROUP (A): -66.2320 -2.3870 275.6850
REMARK 3 T TENSOR
REMARK 3 T11: 1.1818 T22: 1.1339
REMARK 3 T33: 1.4281 T12: -0.3408
REMARK 3 T13: 0.3620 T23: 0.3206
REMARK 3 L TENSOR
REMARK 3 L11: 7.0356 L22: 6.9244
REMARK 3 L33: 10.3822 L12: -1.1025
REMARK 3 L13: 0.0110 L23: 1.2122
REMARK 3 S TENSOR
REMARK 3 S11: -0.4857 S12: -0.1921 S13: 0.3438
REMARK 3 S21: -0.4801 S22: 0.2178 S23: 1.0368
REMARK 3 S31: 0.4335 S32: 0.3918 S33: 0.2678
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 6
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 2 C 28
REMARK 3 RESIDUE RANGE : C 146 C 152
REMARK 3 RESIDUE RANGE : C 445 C 455
REMARK 3 RESIDUE RANGE : C 517 C 831
REMARK 3 RESIDUE RANGE : C 1057 C 1241
REMARK 3 RESIDUE RANGE : D 501 D 790
REMARK 3 ORIGIN FOR THE GROUP (A): -56.0610 34.6280 226.8570
REMARK 3 T TENSOR
REMARK 3 T11: 1.2322 T22: 0.1153
REMARK 3 T33: 1.1198 T12: -0.1298
REMARK 3 T13: 0.8501 T23: -0.1436
REMARK 3 L TENSOR
REMARK 3 L11: 2.7766 L22: 2.0793
REMARK 3 L33: 4.9125 L12: -0.2101
REMARK 3 L13: 0.7688 L23: -2.0629
REMARK 3 S TENSOR
REMARK 3 S11: 0.2374 S12: 0.3141 S13: 0.2166
REMARK 3 S21: 0.4427 S22: 0.0544 S23: 0.7635
REMARK 3 S31: -0.8672 S32: -0.2672 S33: -0.2918
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 9
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 1242 C 1320
REMARK 3 RESIDUE RANGE : D 343 D 500
REMARK 3 RESIDUE RANGE : D 791 D 943
REMARK 3 RESIDUE RANGE : D 1129 D 1153
REMARK 3 RESIDUE RANGE : D 1213 D 1317
REMARK 3 RESIDUE RANGE : D 1345 D 1376
REMARK 3 RESIDUE RANGE : D 1502 D 1503
REMARK 3 RESIDUE RANGE : E 2 E 91
REMARK 3 RESIDUE RANGE : F 505 F 529
REMARK 3 ORIGIN FOR THE GROUP (A): -16.9160 28.8840 247.6120
REMARK 3 T TENSOR
REMARK 3 T11: 0.5420 T22: 0.5798
REMARK 3 T33: 1.7447 T12: -0.1975
REMARK 3 T13: 0.5883 T23: 0.1804
REMARK 3 L TENSOR
REMARK 3 L11: 1.8788 L22: 6.1327
REMARK 3 L33: 4.5057 L12: -0.3825
REMARK 3 L13: 0.0765 L23: 0.1142
REMARK 3 S TENSOR
REMARK 3 S11: 0.0111 S12: -0.8065 S13: -0.0102
REMARK 3 S21: 0.2245 S22: -0.0843 S23: -0.8911
REMARK 3 S31: -0.6276 S32: 0.2663 S33: 0.0731
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 : 2 12 2 21
REMARK 3 RESIDUE RANGE : 3 13 3 17
REMARK 3 ORIGIN FOR THE GROUP (A): -27.1640 34.0710 219.7950
REMARK 3 T TENSOR
REMARK 3 T11: 3.3660 T22: 1.5050
REMARK 3 T33: 2.0432 T12: -0.2098
REMARK 3 T13: 0.1781 T23: 0.1646
REMARK 3 L TENSOR
REMARK 3 L11: 15.9589 L22: 1.7792
REMARK 3 L33: 0.1071 L12: 4.5856
REMARK 3 L13: -1.0142 L23: -0.2342
REMARK 3 S TENSOR
REMARK 3 S11: -0.5230 S12: 0.1328 S13: 0.4667
REMARK 3 S21: -1.3406 S22: 0.2678 S23: 0.2933
REMARK 3 S31: -0.0341 S32: 0.0281 S33: 0.2551
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 832 C 891
REMARK 3 RESIDUE RANGE : C 912 C 1056
REMARK 3 ORIGIN FOR THE GROUP (A): -35.5550 18.1780 185.4620
REMARK 3 T TENSOR
REMARK 3 T11: 1.3370 T22: 0.9762
REMARK 3 T33: 1.3058 T12: 0.1581
REMARK 3 T13: 0.2766 T23: -0.1492
REMARK 3 L TENSOR
REMARK 3 L11: 4.9299 L22: 0.9976
REMARK 3 L33: 5.0522 L12: -0.6742
REMARK 3 L13: 4.3505 L23: -1.0067
REMARK 3 S TENSOR
REMARK 3 S11: -0.1071 S12: 1.2121 S13: -0.2785
REMARK 3 S21: 0.0493 S22: -0.2083 S23: -0.0465
REMARK 3 S31: -0.2502 S32: 0.3547 S33: 0.3154
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 4
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 892 C 911
REMARK 3 RESIDUE RANGE : F 530 F 613
REMARK 3 RESIDUE RANGE : 1 12 1 36
REMARK 3 RESIDUE RANGE : 2 27 2 51
REMARK 3 ORIGIN FOR THE GROUP (A): 12.9810 4.9270 202.4320
REMARK 3 T TENSOR
REMARK 3 T11: 2.8438 T22: 2.1150
REMARK 3 T33: 2.9163 T12: 0.3939
REMARK 3 T13: 0.6911 T23: -0.2868
REMARK 3 L TENSOR
REMARK 3 L11: 1.4776 L22: 0.6029
REMARK 3 L33: 0.3479 L12: -0.8809
REMARK 3 L13: 0.4340 L23: -0.2335
REMARK 3 S TENSOR
REMARK 3 S11: 0.7075 S12: 0.7787 S13: -0.5210
REMARK 3 S21: -0.1895 S22: -0.3889 S23: 0.0421
REMARK 3 S31: 0.0495 S32: 0.8195 S33: -0.3185
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 29 C 145
REMARK 3 RESIDUE RANGE : C 456 C 516
REMARK 3 ORIGIN FOR THE GROUP (A): -27.9860 51.7490 185.9740
REMARK 3 T TENSOR
REMARK 3 T11: 2.0795 T22: 1.8966
REMARK 3 T33: 2.5396 T12: -0.0776
REMARK 3 T13: 0.8222 T23: 0.1632
REMARK 3 L TENSOR
REMARK 3 L11: 5.5323 L22: 5.5970
REMARK 3 L33: 6.2508 L12: 4.9688
REMARK 3 L13: -2.0615 L23: 0.4006
REMARK 3 S TENSOR
REMARK 3 S11: -0.3032 S12: 1.0639 S13: -0.4678
REMARK 3 S21: -0.4673 S22: 0.5479 S23: -0.8113
REMARK 3 S31: -1.0842 S32: -0.2576 S33: -0.2447
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 153 C 226
REMARK 3 RESIDUE RANGE : C 337 C 444
REMARK 3 RESIDUE RANGE : 1 47 1 51
REMARK 3 ORIGIN FOR THE GROUP (A): -25.8190 77.5240 212.3730
REMARK 3 T TENSOR
REMARK 3 T11: 1.4544 T22: 0.8909
REMARK 3 T33: 1.6094 T12: 0.0034
REMARK 3 T13: 0.2541 T23: 0.2203
REMARK 3 L TENSOR
REMARK 3 L11: 4.7271 L22: 3.1251
REMARK 3 L33: 7.8004 L12: 3.5185
REMARK 3 L13: -2.1982 L23: 0.1898
REMARK 3 S TENSOR
REMARK 3 S11: -0.6957 S12: -0.2502 S13: -0.3357
REMARK 3 S21: -0.3177 S22: 0.1620 S23: -0.1385
REMARK 3 S31: 0.9808 S32: 1.0427 S33: 0.5338
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 227 C 336
REMARK 3 ORIGIN FOR THE GROUP (A): -33.6910 107.9980 222.6880
REMARK 3 T TENSOR
REMARK 3 T11: 1.8891 T22: 1.2862
REMARK 3 T33: 2.1591 T12: -0.0988
REMARK 3 T13: 0.1254 T23: 0.0506
REMARK 3 L TENSOR
REMARK 3 L11: 1.7218 L22: 2.1376
REMARK 3 L33: 8.9960 L12: -0.3189
REMARK 3 L13: -2.1462 L23: -3.0977
REMARK 3 S TENSOR
REMARK 3 S11: 0.1578 S12: 0.3107 S13: -0.2169
REMARK 3 S21: 0.5862 S22: -0.2657 S23: -0.2924
REMARK 3 S31: -1.8498 S32: -0.1963 S33: 0.1079
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 : D 1154 D 1212
REMARK 3 ORIGIN FOR THE GROUP (A): -20.5510 77.8790 262.9260
REMARK 3 T TENSOR
REMARK 3 T11: 1.9891 T22: 1.4090
REMARK 3 T33: 1.3376 T12: -0.2134
REMARK 3 T13: -0.1279 T23: -0.1324
REMARK 3 L TENSOR
REMARK 3 L11: 10.2982 L22: 3.9665
REMARK 3 L33: 2.7879 L12: -3.9769
REMARK 3 L13: -5.0111 L23: 2.8209
REMARK 3 S TENSOR
REMARK 3 S11: -0.5469 S12: -0.5939 S13: 0.1921
REMARK 3 S21: -0.5408 S22: 0.5592 S23: 0.4671
REMARK 3 S31: -0.1095 S32: 0.3206 S33: -0.0123
REMARK 3
REMARK 3 TLS GROUP : 13
REMARK 3 NUMBER OF COMPONENTS GROUP : 10
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 1321 C 1342
REMARK 3 RESIDUE RANGE : D 15 D 342
REMARK 3 RESIDUE RANGE : D 1318 D 1344
REMARK 3 RESIDUE RANGE : D 1501 D 1501
REMARK 3 RESIDUE RANGE : F 79 F 136
REMARK 3 RESIDUE RANGE : F 356 F 504
REMARK 3 RESIDUE RANGE : 1 37 1 46
REMARK 3 RESIDUE RANGE : 2 22 2 26
REMARK 3 RESIDUE RANGE : 1 52 1 60
REMARK 3 RESIDUE RANGE : 2 3 2 11
REMARK 3 ORIGIN FOR THE GROUP (A): 6.2130 52.6950 212.0720
REMARK 3 T TENSOR
REMARK 3 T11: 1.2143 T22: 1.2163
REMARK 3 T33: 2.6732 T12: -0.3025
REMARK 3 T13: 0.8085 T23: 0.0410
REMARK 3 L TENSOR
REMARK 3 L11: 1.4608 L22: 2.9026
REMARK 3 L33: 4.4552 L12: 0.7325
REMARK 3 L13: -0.8747 L23: -1.6791
REMARK 3 S TENSOR
REMARK 3 S11: 0.0563 S12: 0.5160 S13: 0.6214
REMARK 3 S21: -0.6109 S22: -0.0482 S23: -0.3464
REMARK 3 S31: -0.6248 S32: -0.0314 S33: -0.0081
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 : F 137 F 355
REMARK 3 ORIGIN FOR THE GROUP (A): 48.6190 57.5530 198.5870
REMARK 3 T TENSOR
REMARK 3 T11: 4.3066 T22: 3.3320
REMARK 3 T33: 3.3721 T12: -0.3456
REMARK 3 T13: -0.7680 T23: -0.1161
REMARK 3 L TENSOR
REMARK 3 L11: 4.2176 L22: 0.1708
REMARK 3 L33: 0.7904 L12: 0.2764
REMARK 3 L13: -1.7310 L23: -0.0642
REMARK 3 S TENSOR
REMARK 3 S11: 0.0564 S12: -0.4006 S13: 0.0884
REMARK 3 S21: 0.5053 S22: 0.4534 S23: -0.3049
REMARK 3 S31: 0.2909 S32: 0.0596 S33: -0.5099
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 : D 944 D 1128
REMARK 3 ORIGIN FOR THE GROUP (A): -43.6960 76.8170 257.6970
REMARK 3 T TENSOR
REMARK 3 T11: 2.1470 T22: 2.1461
REMARK 3 T33: 2.3022 T12: -0.1022
REMARK 3 T13: 0.0540 T23: -0.1329
REMARK 3 L TENSOR
REMARK 3 L11: 3.4577 L22: 1.4513
REMARK 3 L33: 3.7972 L12: -1.1181
REMARK 3 L13: 1.1017 L23: 1.5541
REMARK 3 S TENSOR
REMARK 3 S11: -0.0329 S12: -0.0848 S13: 0.4353
REMARK 3 S21: -0.3303 S22: -0.1885 S23: -0.0213
REMARK 3 S31: -0.2586 S32: -0.1856 S33: 0.2214
REMARK 3
REMARK 3 TLS GROUP : 16
REMARK 3 NUMBER OF COMPONENTS GROUP : 4
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : G 6 G 51
REMARK 3 RESIDUE RANGE : G 179 G 235
REMARK 3 RESIDUE RANGE : H 6 H 51
REMARK 3 RESIDUE RANGE : H 179 H 233
REMARK 3 ORIGIN FOR THE GROUP (A): -98.4900 67.0490 157.6560
REMARK 3 T TENSOR
REMARK 3 T11: 1.4581 T22: 0.3521
REMARK 3 T33: 1.5957 T12: 0.1915
REMARK 3 T13: 0.0907 T23: -0.2009
REMARK 3 L TENSOR
REMARK 3 L11: 13.1928 L22: 0.3265
REMARK 3 L33: 6.2642 L12: -1.3146
REMARK 3 L13: -0.7444 L23: -0.0839
REMARK 3 S TENSOR
REMARK 3 S11: -0.1817 S12: 0.5476 S13: -0.4805
REMARK 3 S21: 0.1577 S22: 0.1639 S23: 0.1974
REMARK 3 S31: 0.1076 S32: -0.3228 S33: 0.0177
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 : G 52 G 178
REMARK 3 ORIGIN FOR THE GROUP (A): -70.3150 70.1130 181.2120
REMARK 3 T TENSOR
REMARK 3 T11: 1.1834 T22: 0.8302
REMARK 3 T33: 1.5724 T12: 0.5427
REMARK 3 T13: 0.2793 T23: 0.1973
REMARK 3 L TENSOR
REMARK 3 L11: 5.7671 L22: 4.4700
REMARK 3 L33: 9.2521 L12: 4.4408
REMARK 3 L13: 2.8745 L23: 2.5643
REMARK 3 S TENSOR
REMARK 3 S11: -0.5329 S12: 0.5197 S13: -0.4929
REMARK 3 S21: 0.0162 S22: 0.3399 S23: -0.0282
REMARK 3 S31: 0.7447 S32: -0.3420 S33: 0.1931
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 : H 52 H 178
REMARK 3 ORIGIN FOR THE GROUP (A):-126.1580 72.0270 133.4040
REMARK 3 T TENSOR
REMARK 3 T11: 1.4548 T22: 1.2793
REMARK 3 T33: 1.5836 T12: -0.0846
REMARK 3 T13: 0.2491 T23: -0.1478
REMARK 3 L TENSOR
REMARK 3 L11: 9.1767 L22: 3.9878
REMARK 3 L33: 6.5331 L12: -4.4011
REMARK 3 L13: 4.8924 L23: -0.4214
REMARK 3 S TENSOR
REMARK 3 S11: 0.0299 S12: 0.7365 S13: -0.2436
REMARK 3 S21: -0.0973 S22: 0.2429 S23: 0.4364
REMARK 3 S31: 0.5295 S32: 0.2239 S33: -0.2729
REMARK 3
REMARK 3 TLS GROUP : 19
REMARK 3 NUMBER OF COMPONENTS GROUP : 6
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : I 2 I 28
REMARK 3 RESIDUE RANGE : I 146 I 152
REMARK 3 RESIDUE RANGE : I 445 I 455
REMARK 3 RESIDUE RANGE : I 517 I 831
REMARK 3 RESIDUE RANGE : I 1057 I 1241
REMARK 3 RESIDUE RANGE : J 501 J 790
REMARK 3 ORIGIN FOR THE GROUP (A): -84.6370 106.1310 165.1010
REMARK 3 T TENSOR
REMARK 3 T11: 1.4152 T22: 0.2073
REMARK 3 T33: 1.5724 T12: 0.0363
REMARK 3 T13: 0.8200 T23: 0.0161
REMARK 3 L TENSOR
REMARK 3 L11: 5.2053 L22: 2.5537
REMARK 3 L33: 3.7836 L12: 2.4731
REMARK 3 L13: 1.7489 L23: 1.2671
REMARK 3 S TENSOR
REMARK 3 S11: -0.3991 S12: 0.2811 S13: 0.7695
REMARK 3 S21: -1.1325 S22: 0.1319 S23: 0.1562
REMARK 3 S31: -0.3930 S32: 0.8301 S33: 0.2671
REMARK 3
REMARK 3 TLS GROUP : 20
REMARK 3 NUMBER OF COMPONENTS GROUP : 9
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : I 1242 I 1320
REMARK 3 RESIDUE RANGE : J 343 J 500
REMARK 3 RESIDUE RANGE : J 791 J 943
REMARK 3 RESIDUE RANGE : J 1129 J 1153
REMARK 3 RESIDUE RANGE : J 1213 J 1317
REMARK 3 RESIDUE RANGE : J 1345 J 1376
REMARK 3 RESIDUE RANGE : J 1502 J 1503
REMARK 3 RESIDUE RANGE : K 2 K 91
REMARK 3 RESIDUE RANGE : L 505 L 529
REMARK 3 ORIGIN FOR THE GROUP (A):-121.9650 104.7640 188.9480
REMARK 3 T TENSOR
REMARK 3 T11: 0.8382 T22: 0.1156
REMARK 3 T33: 0.9401 T12: 0.0150
REMARK 3 T13: 0.8775 T23: 0.0068
REMARK 3 L TENSOR
REMARK 3 L11: 3.7956 L22: 5.3149
REMARK 3 L33: 3.8258 L12: -0.9362
REMARK 3 L13: 1.5413 L23: -0.0897
REMARK 3 S TENSOR
REMARK 3 S11: 0.0502 S12: 0.1335 S13: 0.2791
REMARK 3 S21: 0.0254 S22: -0.1060 S23: 0.1409
REMARK 3 S31: -0.1170 S32: -0.5404 S33: 0.0558
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 : 5 12 5 21
REMARK 3 RESIDUE RANGE : 6 13 6 17
REMARK 3 ORIGIN FOR THE GROUP (A): -91.9840 106.7140 193.7800
REMARK 3 T TENSOR
REMARK 3 T11: 2.7367 T22: 1.8534
REMARK 3 T33: 2.1501 T12: -0.2084
REMARK 3 T13: -0.1544 T23: 0.2655
REMARK 3 L TENSOR
REMARK 3 L11: 1.0923 L22: 7.9958
REMARK 3 L33: 5.0914 L12: -1.5219
REMARK 3 L13: -2.2923 L23: 3.9518
REMARK 3 S TENSOR
REMARK 3 S11: 0.4613 S12: -0.1189 S13: 0.3658
REMARK 3 S21: 0.6031 S22: 0.7009 S23: -3.0910
REMARK 3 S31: -0.2311 S32: 0.0033 S33: -1.1623
REMARK 3
REMARK 3 TLS GROUP : 22
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : I 832 I 891
REMARK 3 RESIDUE RANGE : I 912 I 1056
REMARK 3 ORIGIN FOR THE GROUP (A): -59.7950 88.0020 203.6340
REMARK 3 T TENSOR
REMARK 3 T11: 1.6586 T22: 1.2674
REMARK 3 T33: 1.6656 T12: -0.0206
REMARK 3 T13: 0.1995 T23: 0.1184
REMARK 3 L TENSOR
REMARK 3 L11: 8.8902 L22: 0.2446
REMARK 3 L33: 1.6384 L12: 0.8347
REMARK 3 L13: -3.4157 L23: -0.3928
REMARK 3 S TENSOR
REMARK 3 S11: 0.2233 S12: -0.3632 S13: -0.0596
REMARK 3 S21: 0.2385 S22: -0.1406 S23: -0.0880
REMARK 3 S31: -0.2606 S32: 0.7486 S33: -0.0826
REMARK 3
REMARK 3 TLS GROUP : 23
REMARK 3 NUMBER OF COMPONENTS GROUP : 4
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : I 892 I 911
REMARK 3 RESIDUE RANGE : L 530 L 613
REMARK 3 RESIDUE RANGE : 4 12 4 36
REMARK 3 RESIDUE RANGE : 5 27 5 51
REMARK 3 ORIGIN FOR THE GROUP (A):-100.5430 79.7540 238.2170
REMARK 3 T TENSOR
REMARK 3 T11: 2.1850 T22: 1.3755
REMARK 3 T33: 2.2921 T12: 0.5372
REMARK 3 T13: 0.4802 T23: 0.0383
REMARK 3 L TENSOR
REMARK 3 L11: 2.9303 L22: 6.6537
REMARK 3 L33: 0.4740 L12: 3.1152
REMARK 3 L13: -0.2356 L23: -1.1788
REMARK 3 S TENSOR
REMARK 3 S11: 0.4641 S12: -0.9248 S13: -0.0622
REMARK 3 S21: 0.3125 S22: -0.9845 S23: -0.5924
REMARK 3 S31: 0.2309 S32: 0.4531 S33: 0.5204
REMARK 3
REMARK 3 TLS GROUP : 24
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : I 29 I 145
REMARK 3 RESIDUE RANGE : I 456 I 516
REMARK 3 ORIGIN FOR THE GROUP (A): -61.7060 122.1350 209.2780
REMARK 3 T TENSOR
REMARK 3 T11: 1.4266 T22: 1.3573
REMARK 3 T33: 1.6063 T12: 0.1554
REMARK 3 T13: 0.0740 T23: 0.0695
REMARK 3 L TENSOR
REMARK 3 L11: 3.2685 L22: 4.2427
REMARK 3 L33: 3.9480 L12: 2.9550
REMARK 3 L13: 3.0370 L23: 2.9950
REMARK 3 S TENSOR
REMARK 3 S11: -0.1318 S12: -0.7406 S13: 0.3000
REMARK 3 S21: 0.4554 S22: -0.0399 S23: -0.3011
REMARK 3 S31: -0.1232 S32: 0.2413 S33: 0.1716
REMARK 3
REMARK 3 TLS GROUP : 25
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : I 153 I 226
REMARK 3 RESIDUE RANGE : I 337 I 444
REMARK 3 RESIDUE RANGE : 4 47 4 51
REMARK 3 ORIGIN FOR THE GROUP (A): -82.7660 149.8640 197.4230
REMARK 3 T TENSOR
REMARK 3 T11: 1.4641 T22: 0.6306
REMARK 3 T33: 1.4799 T12: -0.3216
REMARK 3 T13: 0.3706 T23: 0.0478
REMARK 3 L TENSOR
REMARK 3 L11: 4.4037 L22: 4.0334
REMARK 3 L33: 10.1615 L12: 0.1067
REMARK 3 L13: 6.1449 L23: 2.6280
REMARK 3 S TENSOR
REMARK 3 S11: 0.4420 S12: -0.5221 S13: -0.2052
REMARK 3 S21: 0.3984 S22: 0.0092 S23: 0.1423
REMARK 3 S31: 0.6902 S32: -0.7686 S33: -0.4512
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 : I 227 I 336
REMARK 3 ORIGIN FOR THE GROUP (A): -83.9770 180.0800 183.9720
REMARK 3 T TENSOR
REMARK 3 T11: 1.5849 T22: 1.5339
REMARK 3 T33: 1.7834 T12: 0.0076
REMARK 3 T13: 0.0597 T23: -0.0102
REMARK 3 L TENSOR
REMARK 3 L11: 0.4061 L22: 0.5404
REMARK 3 L33: 13.9004 L12: 0.2632
REMARK 3 L13: 1.1857 L23: -0.1416
REMARK 3 S TENSOR
REMARK 3 S11: -0.0076 S12: 0.1049 S13: -0.0814
REMARK 3 S21: 0.2227 S22: -0.3012 S23: 0.3896
REMARK 3 S31: 0.1759 S32: -0.1366 S33: 0.3089
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 : J 1154 J 1212
REMARK 3 ORIGIN FOR THE GROUP (A):-129.5570 153.4270 176.7010
REMARK 3 T TENSOR
REMARK 3 T11: 1.7399 T22: 0.6996
REMARK 3 T33: 1.4078 T12: 0.1813
REMARK 3 T13: -0.0865 T23: 0.2638
REMARK 3 L TENSOR
REMARK 3 L11: 20.6343 L22: 13.7165
REMARK 3 L33: 8.3139 L12: -7.3977
REMARK 3 L13: -9.8453 L23: -2.6944
REMARK 3 S TENSOR
REMARK 3 S11: 0.2683 S12: -0.5378 S13: -0.3319
REMARK 3 S21: -0.7537 S22: -0.2494 S23: -0.0277
REMARK 3 S31: -0.0720 S32: 0.3865 S33: -0.0189
REMARK 3
REMARK 3 TLS GROUP : 28
REMARK 3 NUMBER OF COMPONENTS GROUP : 10
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : I 1321 I 1342
REMARK 3 RESIDUE RANGE : J 15 J 342
REMARK 3 RESIDUE RANGE : J 1318 J 1344
REMARK 3 RESIDUE RANGE : J 1501 J 1501
REMARK 3 RESIDUE RANGE : L 79 L 136
REMARK 3 RESIDUE RANGE : L 356 L 504
REMARK 3 RESIDUE RANGE : 4 37 4 46
REMARK 3 RESIDUE RANGE : 5 22 5 26
REMARK 3 RESIDUE RANGE : 4 52 4 60
REMARK 3 RESIDUE RANGE : 5 3 5 11
REMARK 3 ORIGIN FOR THE GROUP (A):-100.5200 127.3640 225.9590
REMARK 3 T TENSOR
REMARK 3 T11: 2.1838 T22: 0.5141
REMARK 3 T33: 1.5829 T12: -0.0615
REMARK 3 T13: 0.5743 T23: -0.1000
REMARK 3 L TENSOR
REMARK 3 L11: 4.1067 L22: 3.2231
REMARK 3 L33: 3.2603 L12: 1.8356
REMARK 3 L13: 1.7004 L23: 1.0801
REMARK 3 S TENSOR
REMARK 3 S11: -0.0886 S12: -0.0883 S13: 0.2661
REMARK 3 S21: 1.1840 S22: 0.2514 S23: -0.6733
REMARK 3 S31: -0.8295 S32: 1.0520 S33: -0.1629
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 : L 137 L 355
REMARK 3 ORIGIN FOR THE GROUP (A):-108.9880 133.7010 269.5670
REMARK 3 T TENSOR
REMARK 3 T11: 3.1552 T22: 2.9370
REMARK 3 T33: 4.3786 T12: 0.1909
REMARK 3 T13: -0.2373 T23: 0.1456
REMARK 3 L TENSOR
REMARK 3 L11: 0.9832 L22: 0.6178
REMARK 3 L33: 3.1524 L12: -0.6500
REMARK 3 L13: -0.9807 L23: 1.1764
REMARK 3 S TENSOR
REMARK 3 S11: -0.0130 S12: -1.1099 S13: -0.9584
REMARK 3 S21: 0.0753 S22: 0.5872 S23: 0.4232
REMARK 3 S31: 0.5138 S32: 0.3485 S33: -0.5743
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 : J 944 J 1128
REMARK 3 ORIGIN FOR THE GROUP (A):-113.6470 151.5740 159.3160
REMARK 3 T TENSOR
REMARK 3 T11: 3.3236 T22: 2.2842
REMARK 3 T33: 3.1411 T12: 0.0257
REMARK 3 T13: 0.3465 T23: 0.2748
REMARK 3 L TENSOR
REMARK 3 L11: 6.8318 L22: 2.3084
REMARK 3 L33: 2.7805 L12: -2.9842
REMARK 3 L13: -2.1674 L23: -0.3290
REMARK 3 S TENSOR
REMARK 3 S11: -0.0203 S12: 0.1382 S13: 1.3704
REMARK 3 S21: -0.6099 S22: -0.0927 S23: -0.8062
REMARK 3 S31: -0.3231 S32: -0.0399 S33: 0.1130
REMARK 3
REMARK 3 TLS GROUP : 31
REMARK 3 NUMBER OF COMPONENTS GROUP : 4
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : M 6 M 51
REMARK 3 RESIDUE RANGE : M 179 M 235
REMARK 3 RESIDUE RANGE : N 6 N 51
REMARK 3 RESIDUE RANGE : N 179 N 233
REMARK 3 ORIGIN FOR THE GROUP (A):-112.1720 36.9370 76.2710
REMARK 3 T TENSOR
REMARK 3 T11: 1.8189 T22: 1.0341
REMARK 3 T33: 1.7306 T12: -0.3089
REMARK 3 T13: 0.1342 T23: -0.1376
REMARK 3 L TENSOR
REMARK 3 L11: 5.6981 L22: 0.2708
REMARK 3 L33: 7.8127 L12: 0.6861
REMARK 3 L13: -0.2211 L23: -1.0802
REMARK 3 S TENSOR
REMARK 3 S11: -0.2611 S12: 0.0719 S13: 0.0009
REMARK 3 S21: -0.1402 S22: 0.3058 S23: 0.0955
REMARK 3 S31: 0.1964 S32: -0.8101 S33: -0.0447
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 : M 52 M 178
REMARK 3 ORIGIN FOR THE GROUP (A): -79.6830 38.7540 58.9670
REMARK 3 T TENSOR
REMARK 3 T11: 1.5016 T22: 1.2100
REMARK 3 T33: 1.4093 T12: -0.1478
REMARK 3 T13: 0.0583 T23: -0.3690
REMARK 3 L TENSOR
REMARK 3 L11: 5.0142 L22: 2.2300
REMARK 3 L33: 5.9633 L12: -2.6661
REMARK 3 L13: 3.3310 L23: -1.2760
REMARK 3 S TENSOR
REMARK 3 S11: 0.0226 S12: 0.0539 S13: -0.1851
REMARK 3 S21: -0.0659 S22: 0.0142 S23: -0.0146
REMARK 3 S31: 0.1443 S32: 0.0064 S33: -0.0367
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 : N 52 N 178
REMARK 3 ORIGIN FOR THE GROUP (A):-145.3000 42.9170 91.7900
REMARK 3 T TENSOR
REMARK 3 T11: 1.5715 T22: 1.8098
REMARK 3 T33: 2.1348 T12: -0.0426
REMARK 3 T13: 0.1182 T23: -0.0100
REMARK 3 L TENSOR
REMARK 3 L11: 6.9646 L22: 3.0878
REMARK 3 L33: 11.6833 L12: 1.7686
REMARK 3 L13: -0.8460 L23: 3.9935
REMARK 3 S TENSOR
REMARK 3 S11: -0.1234 S12: 0.5996 S13: -1.0569
REMARK 3 S21: -0.7949 S22: -0.3454 S23: 0.3920
REMARK 3 S31: -0.8613 S32: -1.3232 S33: 0.4687
REMARK 3
REMARK 3 TLS GROUP : 34
REMARK 3 NUMBER OF COMPONENTS GROUP : 6
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : O 2 O 28
REMARK 3 RESIDUE RANGE : O 146 O 152
REMARK 3 RESIDUE RANGE : O 445 O 455
REMARK 3 RESIDUE RANGE : O 517 O 831
REMARK 3 RESIDUE RANGE : O 1057 O 1241
REMARK 3 RESIDUE RANGE : P 501 P 790
REMARK 3 ORIGIN FOR THE GROUP (A): -99.4240 75.3290 64.9370
REMARK 3 T TENSOR
REMARK 3 T11: 1.2249 T22: 0.8032
REMARK 3 T33: 1.9043 T12: -0.0230
REMARK 3 T13: 0.6033 T23: -0.1169
REMARK 3 L TENSOR
REMARK 3 L11: 3.6211 L22: 1.0979
REMARK 3 L33: 3.2784 L12: 1.4176
REMARK 3 L13: -0.7207 L23: -1.3237
REMARK 3 S TENSOR
REMARK 3 S11: 0.1411 S12: 0.9271 S13: 0.7031
REMARK 3 S21: -0.1093 S22: 0.3522 S23: 0.8238
REMARK 3 S31: -0.0006 S32: -0.5370 S33: -0.4933
REMARK 3
REMARK 3 TLS GROUP : 35
REMARK 3 NUMBER OF COMPONENTS GROUP : 9
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : O 1242 O 1320
REMARK 3 RESIDUE RANGE : P 343 P 500
REMARK 3 RESIDUE RANGE : P 791 P 943
REMARK 3 RESIDUE RANGE : P 1129 P 1153
REMARK 3 RESIDUE RANGE : P 1213 P 1317
REMARK 3 RESIDUE RANGE : P 1345 P 1376
REMARK 3 RESIDUE RANGE : P 1502 P 1503
REMARK 3 RESIDUE RANGE : Q 2 Q 91
REMARK 3 RESIDUE RANGE : R 505 R 529
REMARK 3 ORIGIN FOR THE GROUP (A): -91.1260 75.2180 108.5060
REMARK 3 T TENSOR
REMARK 3 T11: 1.0735 T22: 0.3396
REMARK 3 T33: 1.0503 T12: -0.1852
REMARK 3 T13: 0.2875 T23: 0.0372
REMARK 3 L TENSOR
REMARK 3 L11: 4.7805 L22: 5.5964
REMARK 3 L33: 2.4482 L12: -0.5885
REMARK 3 L13: -0.8755 L23: 0.2402
REMARK 3 S TENSOR
REMARK 3 S11: 0.0992 S12: -0.2656 S13: -0.0739
REMARK 3 S21: 0.3061 S22: -0.0565 S23: -0.0001
REMARK 3 S31: -0.1325 S32: -0.7433 S33: -0.0426
REMARK 3
REMARK 3 TLS GROUP : 36
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : 8 12 8 21
REMARK 3 RESIDUE RANGE : 9 13 9 17
REMARK 3 ORIGIN FOR THE GROUP (A): -75.2290 76.3130 83.5000
REMARK 3 T TENSOR
REMARK 3 T11: 1.8384 T22: 1.8992
REMARK 3 T33: 2.4230 T12: -0.1612
REMARK 3 T13: 0.1972 T23: 0.0685
REMARK 3 L TENSOR
REMARK 3 L11: 4.4511 L22: 12.6411
REMARK 3 L33: 5.5320 L12: 5.8916
REMARK 3 L13: 4.8997 L23: 5.7506
REMARK 3 S TENSOR
REMARK 3 S11: -0.3689 S12: 0.7435 S13: 0.1964
REMARK 3 S21: -1.0788 S22: 0.0054 S23: -0.5343
REMARK 3 S31: -0.2094 S32: 0.7764 S33: 0.3635
REMARK 3
REMARK 3 TLS GROUP : 37
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : O 832 O 891
REMARK 3 RESIDUE RANGE : O 912 O 1056
REMARK 3 ORIGIN FOR THE GROUP (A): -54.4180 56.3760 57.3230
REMARK 3 T TENSOR
REMARK 3 T11: 1.5963 T22: 1.1959
REMARK 3 T33: 1.6140 T12: 0.1073
REMARK 3 T13: -0.1073 T23: -0.0178
REMARK 3 L TENSOR
REMARK 3 L11: 0.8408 L22: 0.1240
REMARK 3 L33: 5.0139 L12: -0.0700
REMARK 3 L13: 0.7881 L23: -0.0152
REMARK 3 S TENSOR
REMARK 3 S11: 0.1175 S12: 0.6574 S13: 0.0460
REMARK 3 S21: -0.1139 S22: -0.2000 S23: 0.1879
REMARK 3 S31: 0.1613 S32: 0.8111 S33: 0.0824
REMARK 3
REMARK 3 TLS GROUP : 38
REMARK 3 NUMBER OF COMPONENTS GROUP : 4
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : O 892 O 911
REMARK 3 RESIDUE RANGE : R 530 R 613
REMARK 3 RESIDUE RANGE : 7 12 7 36
REMARK 3 RESIDUE RANGE : 8 27 8 51
REMARK 3 ORIGIN FOR THE GROUP (A): -37.4170 49.6570 107.3350
REMARK 3 T TENSOR
REMARK 3 T11: 2.3096 T22: 1.4889
REMARK 3 T33: 2.4013 T12: 0.3252
REMARK 3 T13: 0.3176 T23: -0.1872
REMARK 3 L TENSOR
REMARK 3 L11: 0.9219 L22: 1.8301
REMARK 3 L33: 1.5089 L12: -0.1548
REMARK 3 L13: -0.4006 L23: -0.8653
REMARK 3 S TENSOR
REMARK 3 S11: 0.2557 S12: 0.6829 S13: -0.1228
REMARK 3 S21: 0.3528 S22: -0.3538 S23: -0.3263
REMARK 3 S31: 0.0827 S32: 0.7146 S33: 0.0981
REMARK 3
REMARK 3 TLS GROUP : 39
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : O 29 O 145
REMARK 3 RESIDUE RANGE : O 456 O 516
REMARK 3 ORIGIN FOR THE GROUP (A): -49.4810 90.5440 60.1450
REMARK 3 T TENSOR
REMARK 3 T11: 1.5742 T22: 1.5498
REMARK 3 T33: 1.4035 T12: 0.0041
REMARK 3 T13: 0.1042 T23: -0.0725
REMARK 3 L TENSOR
REMARK 3 L11: 4.6279 L22: 1.0896
REMARK 3 L33: 0.4691 L12: 0.6648
REMARK 3 L13: -1.2608 L23: -0.2391
REMARK 3 S TENSOR
REMARK 3 S11: -0.1179 S12: -0.2686 S13: 0.2233
REMARK 3 S21: -0.0201 S22: 0.2200 S23: -0.6310
REMARK 3 S31: -0.1568 S32: 0.4021 S33: -0.1020
REMARK 3
REMARK 3 TLS GROUP : 40
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : O 153 O 226
REMARK 3 RESIDUE RANGE : O 337 O 444
REMARK 3 RESIDUE RANGE : 7 47 7 51
REMARK 3 ORIGIN FOR THE GROUP (A): -68.0580 119.0610 74.2020
REMARK 3 T TENSOR
REMARK 3 T11: 1.7081 T22: 0.9089
REMARK 3 T33: 1.2941 T12: 0.0610
REMARK 3 T13: -0.0401 T23: 0.3823
REMARK 3 L TENSOR
REMARK 3 L11: 14.4635 L22: 5.6913
REMARK 3 L33: 0.4314 L12: 0.5289
REMARK 3 L13: -2.2531 L23: -0.0905
REMARK 3 S TENSOR
REMARK 3 S11: -0.0907 S12: -0.8065 S13: -1.0824
REMARK 3 S21: 0.2402 S22: -0.1667 S23: -0.0250
REMARK 3 S31: -0.3391 S32: 0.1720 S33: 0.2574
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 : O 227 O 336
REMARK 3 ORIGIN FOR THE GROUP (A): -81.1950 149.2960 70.1290
REMARK 3 T TENSOR
REMARK 3 T11: 2.1824 T22: 1.3320
REMARK 3 T33: 2.2154 T12: 0.2174
REMARK 3 T13: 0.0597 T23: 0.1301
REMARK 3 L TENSOR
REMARK 3 L11: 1.4840 L22: 0.1311
REMARK 3 L33: 0.9422 L12: 0.2066
REMARK 3 L13: -1.1380 L23: -0.1751
REMARK 3 S TENSOR
REMARK 3 S11: 0.1202 S12: 0.7620 S13: -0.1715
REMARK 3 S21: 0.4748 S22: 0.1291 S23: 0.0996
REMARK 3 S31: -0.0765 S32: -0.5663 S33: -0.2493
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 : P 1154 P 1212
REMARK 3 ORIGIN FOR THE GROUP (A):-104.6470 124.5910 108.6740
REMARK 3 T TENSOR
REMARK 3 T11: 2.2003 T22: 0.8373
REMARK 3 T33: 1.8011 T12: 0.0609
REMARK 3 T13: 0.3519 T23: -0.2626
REMARK 3 L TENSOR
REMARK 3 L11: 6.8895 L22: 2.2905
REMARK 3 L33: 11.6019 L12: -2.4677
REMARK 3 L13: 1.1846 L23: -4.3201
REMARK 3 S TENSOR
REMARK 3 S11: 0.8551 S12: 0.8435 S13: 0.2187
REMARK 3 S21: 0.0162 S22: -0.4270 S23: 0.0203
REMARK 3 S31: -1.8418 S32: 0.4078 S33: -0.4281
REMARK 3
REMARK 3 TLS GROUP : 43
REMARK 3 NUMBER OF COMPONENTS GROUP : 10
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : O 1321 O 1342
REMARK 3 RESIDUE RANGE : P 15 P 342
REMARK 3 RESIDUE RANGE : P 1318 P 1344
REMARK 3 RESIDUE RANGE : P 1501 P 1501
REMARK 3 RESIDUE RANGE : R 79 R 136
REMARK 3 RESIDUE RANGE : R 356 R 504
REMARK 3 RESIDUE RANGE : 7 37 7 46
REMARK 3 RESIDUE RANGE : 8 22 8 26
REMARK 3 RESIDUE RANGE : 7 52 7 60
REMARK 3 RESIDUE RANGE : 8 3 8 11
REMARK 3 ORIGIN FOR THE GROUP (A): -48.4440 97.1390 102.0260
REMARK 3 T TENSOR
REMARK 3 T11: 1.8938 T22: 0.2152
REMARK 3 T33: 1.9153 T12: -0.2692
REMARK 3 T13: -0.0085 T23: 0.2980
REMARK 3 L TENSOR
REMARK 3 L11: 5.6954 L22: 2.7669
REMARK 3 L33: 2.5342 L12: 0.4743
REMARK 3 L13: -1.0277 L23: -0.2396
REMARK 3 S TENSOR
REMARK 3 S11: -0.1230 S12: 0.8538 S13: 0.6684
REMARK 3 S21: 0.2337 S22: -0.0836 S23: -1.1045
REMARK 3 S31: -0.4295 S32: 0.0847 S33: 0.2065
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 : R 137 R 355
REMARK 3 ORIGIN FOR THE GROUP (A): -10.9570 104.9370 125.5920
REMARK 3 T TENSOR
REMARK 3 T11: 4.3659 T22: 3.4009
REMARK 3 T33: 3.5010 T12: 0.2866
REMARK 3 T13: 0.3412 T23: -0.4882
REMARK 3 L TENSOR
REMARK 3 L11: 1.7769 L22: 1.6562
REMARK 3 L33: 1.7555 L12: 1.4802
REMARK 3 L13: 1.4263 L23: 1.6801
REMARK 3 S TENSOR
REMARK 3 S11: -0.9013 S12: 0.1209 S13: -0.3338
REMARK 3 S21: 0.1241 S22: 1.0462 S23: -0.4710
REMARK 3 S31: 0.4260 S32: 1.1341 S33: -0.1448
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 : P 944 P 1128
REMARK 3 ORIGIN FOR THE GROUP (A):-114.2360 121.7210 89.2070
REMARK 3 T TENSOR
REMARK 3 T11: 2.7907 T22: 3.1029
REMARK 3 T33: 2.9949 T12: 0.0789
REMARK 3 T13: 0.0262 T23: 0.2720
REMARK 3 L TENSOR
REMARK 3 L11: 1.3776 L22: 0.4485
REMARK 3 L33: 0.5299 L12: -0.1935
REMARK 3 L13: -0.1006 L23: 0.1434
REMARK 3 S TENSOR
REMARK 3 S11: 0.4435 S12: -0.4797 S13: -0.5997
REMARK 3 S21: -0.2780 S22: -0.8122 S23: -0.0626
REMARK 3 S31: -0.4405 S32: 0.3961 S33: 0.3686
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4YLP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-MAR-15.
REMARK 100 THE DEPOSITION ID IS D_1000207354.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-SEP-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X25
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.1
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 69757
REMARK 200 RESOLUTION RANGE HIGH (A) : 5.500
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 3.400
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.3000
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: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 67.63
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.80
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 7% PEG3350, 150 MM MAGNESIUM CHLORIDE,
REMARK 280 100 MM HEPES SODIUM, PH 7.0, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 102.49400
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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: NONAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, 1, 2, 3
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: NONAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H, I, J, K, L, 4, 5, 6
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: NONAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: M, N, O, P, Q, R, 7, 8, 9
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 -6
REMARK 465 HIS A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 HIS A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 GLN A 2
REMARK 465 GLY A 3
REMARK 465 SER A 4
REMARK 465 VAL A 5
REMARK 465 ALA B -6
REMARK 465 HIS B -5
REMARK 465 HIS B -4
REMARK 465 HIS B -3
REMARK 465 HIS B -2
REMARK 465 HIS B -1
REMARK 465 HIS B 0
REMARK 465 MET B 1
REMARK 465 GLN B 2
REMARK 465 GLY B 3
REMARK 465 SER B 4
REMARK 465 VAL B 5
REMARK 465 LEU B 234
REMARK 465 ARG B 235
REMARK 465 MET C 1
REMARK 465 MET D 1
REMARK 465 LYS D 2
REMARK 465 ASP D 3
REMARK 465 LEU D 4
REMARK 465 LEU D 5
REMARK 465 LYS D 6
REMARK 465 PHE D 7
REMARK 465 LEU D 8
REMARK 465 LYS D 9
REMARK 465 ALA D 10
REMARK 465 GLN D 11
REMARK 465 THR D 12
REMARK 465 LYS D 13
REMARK 465 THR D 14
REMARK 465 GLU D 1377
REMARK 465 ALA D 1378
REMARK 465 PRO D 1379
REMARK 465 ALA D 1380
REMARK 465 ALA D 1381
REMARK 465 PRO D 1382
REMARK 465 GLN D 1383
REMARK 465 VAL D 1384
REMARK 465 THR D 1385
REMARK 465 ALA D 1386
REMARK 465 GLU D 1387
REMARK 465 ASP D 1388
REMARK 465 ALA D 1389
REMARK 465 SER D 1390
REMARK 465 ALA D 1391
REMARK 465 SER D 1392
REMARK 465 LEU D 1393
REMARK 465 ALA D 1394
REMARK 465 GLU D 1395
REMARK 465 LEU D 1396
REMARK 465 LEU D 1397
REMARK 465 ASN D 1398
REMARK 465 ALA D 1399
REMARK 465 GLY D 1400
REMARK 465 LEU D 1401
REMARK 465 GLY D 1402
REMARK 465 GLY D 1403
REMARK 465 SER D 1404
REMARK 465 ASP D 1405
REMARK 465 ASN D 1406
REMARK 465 GLU D 1407
REMARK 465 MET F -14
REMARK 465 ARG F -13
REMARK 465 GLY F -12
REMARK 465 SER F -11
REMARK 465 HIS F -10
REMARK 465 HIS F -9
REMARK 465 HIS F -8
REMARK 465 HIS F -7
REMARK 465 HIS F -6
REMARK 465 HIS F -5
REMARK 465 THR F -4
REMARK 465 ASP F -3
REMARK 465 GLN F -2
REMARK 465 PHE F -1
REMARK 465 THR F 0
REMARK 465 MET F 1
REMARK 465 GLU F 2
REMARK 465 GLN F 3
REMARK 465 ASN F 4
REMARK 465 PRO F 5
REMARK 465 GLN F 6
REMARK 465 SER F 7
REMARK 465 GLN F 8
REMARK 465 LEU F 9
REMARK 465 LYS F 10
REMARK 465 LEU F 11
REMARK 465 LEU F 12
REMARK 465 VAL F 13
REMARK 465 THR F 14
REMARK 465 ARG F 15
REMARK 465 GLY F 16
REMARK 465 LYS F 17
REMARK 465 GLU F 18
REMARK 465 GLN F 19
REMARK 465 GLY F 20
REMARK 465 TYR F 21
REMARK 465 LEU F 22
REMARK 465 THR F 23
REMARK 465 TYR F 24
REMARK 465 ALA F 25
REMARK 465 GLU F 26
REMARK 465 VAL F 27
REMARK 465 ASN F 28
REMARK 465 ASP F 29
REMARK 465 HIS F 30
REMARK 465 LEU F 31
REMARK 465 PRO F 32
REMARK 465 GLU F 33
REMARK 465 ASP F 34
REMARK 465 ILE F 35
REMARK 465 VAL F 36
REMARK 465 ASP F 37
REMARK 465 SER F 38
REMARK 465 ASP F 39
REMARK 465 GLN F 40
REMARK 465 ILE F 41
REMARK 465 GLU F 42
REMARK 465 ASP F 43
REMARK 465 ILE F 44
REMARK 465 ILE F 45
REMARK 465 GLN F 46
REMARK 465 MET F 47
REMARK 465 ILE F 48
REMARK 465 ASN F 49
REMARK 465 ASP F 50
REMARK 465 MET F 51
REMARK 465 GLY F 52
REMARK 465 ILE F 53
REMARK 465 GLN F 54
REMARK 465 VAL F 55
REMARK 465 MET F 56
REMARK 465 GLU F 57
REMARK 465 GLU F 58
REMARK 465 ALA F 59
REMARK 465 PRO F 60
REMARK 465 ASP F 61
REMARK 465 ALA F 62
REMARK 465 ASP F 63
REMARK 465 ASP F 64
REMARK 465 LEU F 65
REMARK 465 MET F 66
REMARK 465 LEU F 67
REMARK 465 ALA F 68
REMARK 465 GLU F 69
REMARK 465 ASN F 70
REMARK 465 THR F 71
REMARK 465 ALA F 72
REMARK 465 ASP F 73
REMARK 465 GLU F 74
REMARK 465 ASP F 75
REMARK 465 ALA F 76
REMARK 465 ALA F 77
REMARK 465 GLU F 78
REMARK 465 GLU F 172
REMARK 465 ASP F 173
REMARK 465 LEU F 174
REMARK 465 ALA F 175
REMARK 465 PRO F 176
REMARK 465 THR F 177
REMARK 465 ALA F 178
REMARK 465 THR F 179
REMARK 465 HIS F 180
REMARK 465 VAL F 181
REMARK 465 GLY F 182
REMARK 465 SER F 183
REMARK 465 GLU F 184
REMARK 465 LEU F 185
REMARK 465 SER F 186
REMARK 465 GLN F 187
REMARK 465 GLU F 188
REMARK 465 ASP F 189
REMARK 465 LEU F 190
REMARK 465 ASP F 191
REMARK 465 ASP F 192
REMARK 465 ASP F 193
REMARK 465 GLU F 194
REMARK 465 ASP F 195
REMARK 465 GLU F 196
REMARK 465 ASP F 197
REMARK 465 GLU F 198
REMARK 465 GLU F 199
REMARK 465 ASP F 200
REMARK 465 GLY F 201
REMARK 465 ASP F 202
REMARK 465 ASP F 203
REMARK 465 ASP F 204
REMARK 465 SER F 205
REMARK 465 ALA F 206
REMARK 465 ASP F 207
REMARK 465 ASP F 208
REMARK 465 ASP F 209
REMARK 465 ALA G -6
REMARK 465 HIS G -5
REMARK 465 HIS G -4
REMARK 465 HIS G -3
REMARK 465 HIS G -2
REMARK 465 HIS G -1
REMARK 465 HIS G 0
REMARK 465 MET G 1
REMARK 465 GLN G 2
REMARK 465 GLY G 3
REMARK 465 SER G 4
REMARK 465 VAL G 5
REMARK 465 ALA H -6
REMARK 465 HIS H -5
REMARK 465 HIS H -4
REMARK 465 HIS H -3
REMARK 465 HIS H -2
REMARK 465 HIS H -1
REMARK 465 HIS H 0
REMARK 465 MET H 1
REMARK 465 GLN H 2
REMARK 465 GLY H 3
REMARK 465 SER H 4
REMARK 465 VAL H 5
REMARK 465 LEU H 234
REMARK 465 ARG H 235
REMARK 465 MET I 1
REMARK 465 MET J 1
REMARK 465 LYS J 2
REMARK 465 ASP J 3
REMARK 465 LEU J 4
REMARK 465 LEU J 5
REMARK 465 LYS J 6
REMARK 465 PHE J 7
REMARK 465 LEU J 8
REMARK 465 LYS J 9
REMARK 465 ALA J 10
REMARK 465 GLN J 11
REMARK 465 THR J 12
REMARK 465 LYS J 13
REMARK 465 THR J 14
REMARK 465 GLU J 1377
REMARK 465 ALA J 1378
REMARK 465 PRO J 1379
REMARK 465 ALA J 1380
REMARK 465 ALA J 1381
REMARK 465 PRO J 1382
REMARK 465 GLN J 1383
REMARK 465 VAL J 1384
REMARK 465 THR J 1385
REMARK 465 ALA J 1386
REMARK 465 GLU J 1387
REMARK 465 ASP J 1388
REMARK 465 ALA J 1389
REMARK 465 SER J 1390
REMARK 465 ALA J 1391
REMARK 465 SER J 1392
REMARK 465 LEU J 1393
REMARK 465 ALA J 1394
REMARK 465 GLU J 1395
REMARK 465 LEU J 1396
REMARK 465 LEU J 1397
REMARK 465 ASN J 1398
REMARK 465 ALA J 1399
REMARK 465 GLY J 1400
REMARK 465 LEU J 1401
REMARK 465 GLY J 1402
REMARK 465 GLY J 1403
REMARK 465 SER J 1404
REMARK 465 ASP J 1405
REMARK 465 ASN J 1406
REMARK 465 GLU J 1407
REMARK 465 MET L -14
REMARK 465 ARG L -13
REMARK 465 GLY L -12
REMARK 465 SER L -11
REMARK 465 HIS L -10
REMARK 465 HIS L -9
REMARK 465 HIS L -8
REMARK 465 HIS L -7
REMARK 465 HIS L -6
REMARK 465 HIS L -5
REMARK 465 THR L -4
REMARK 465 ASP L -3
REMARK 465 GLN L -2
REMARK 465 PHE L -1
REMARK 465 THR L 0
REMARK 465 MET L 1
REMARK 465 GLU L 2
REMARK 465 GLN L 3
REMARK 465 ASN L 4
REMARK 465 PRO L 5
REMARK 465 GLN L 6
REMARK 465 SER L 7
REMARK 465 GLN L 8
REMARK 465 LEU L 9
REMARK 465 LYS L 10
REMARK 465 LEU L 11
REMARK 465 LEU L 12
REMARK 465 VAL L 13
REMARK 465 THR L 14
REMARK 465 ARG L 15
REMARK 465 GLY L 16
REMARK 465 LYS L 17
REMARK 465 GLU L 18
REMARK 465 GLN L 19
REMARK 465 GLY L 20
REMARK 465 TYR L 21
REMARK 465 LEU L 22
REMARK 465 THR L 23
REMARK 465 TYR L 24
REMARK 465 ALA L 25
REMARK 465 GLU L 26
REMARK 465 VAL L 27
REMARK 465 ASN L 28
REMARK 465 ASP L 29
REMARK 465 HIS L 30
REMARK 465 LEU L 31
REMARK 465 PRO L 32
REMARK 465 GLU L 33
REMARK 465 ASP L 34
REMARK 465 ILE L 35
REMARK 465 VAL L 36
REMARK 465 ASP L 37
REMARK 465 SER L 38
REMARK 465 ASP L 39
REMARK 465 GLN L 40
REMARK 465 ILE L 41
REMARK 465 GLU L 42
REMARK 465 ASP L 43
REMARK 465 ILE L 44
REMARK 465 ILE L 45
REMARK 465 GLN L 46
REMARK 465 MET L 47
REMARK 465 ILE L 48
REMARK 465 ASN L 49
REMARK 465 ASP L 50
REMARK 465 MET L 51
REMARK 465 GLY L 52
REMARK 465 ILE L 53
REMARK 465 GLN L 54
REMARK 465 VAL L 55
REMARK 465 MET L 56
REMARK 465 GLU L 57
REMARK 465 GLU L 58
REMARK 465 ALA L 59
REMARK 465 PRO L 60
REMARK 465 ASP L 61
REMARK 465 ALA L 62
REMARK 465 ASP L 63
REMARK 465 ASP L 64
REMARK 465 LEU L 65
REMARK 465 MET L 66
REMARK 465 LEU L 67
REMARK 465 ALA L 68
REMARK 465 GLU L 69
REMARK 465 ASN L 70
REMARK 465 THR L 71
REMARK 465 ALA L 72
REMARK 465 ASP L 73
REMARK 465 GLU L 74
REMARK 465 ASP L 75
REMARK 465 ALA L 76
REMARK 465 ALA L 77
REMARK 465 GLU L 78
REMARK 465 GLU L 172
REMARK 465 ASP L 173
REMARK 465 LEU L 174
REMARK 465 ALA L 175
REMARK 465 PRO L 176
REMARK 465 THR L 177
REMARK 465 ALA L 178
REMARK 465 THR L 179
REMARK 465 HIS L 180
REMARK 465 VAL L 181
REMARK 465 GLY L 182
REMARK 465 SER L 183
REMARK 465 GLU L 184
REMARK 465 LEU L 185
REMARK 465 SER L 186
REMARK 465 GLN L 187
REMARK 465 GLU L 188
REMARK 465 ASP L 189
REMARK 465 LEU L 190
REMARK 465 ASP L 191
REMARK 465 ASP L 192
REMARK 465 ASP L 193
REMARK 465 GLU L 194
REMARK 465 ASP L 195
REMARK 465 GLU L 196
REMARK 465 ASP L 197
REMARK 465 GLU L 198
REMARK 465 GLU L 199
REMARK 465 ASP L 200
REMARK 465 GLY L 201
REMARK 465 ASP L 202
REMARK 465 ASP L 203
REMARK 465 ASP L 204
REMARK 465 SER L 205
REMARK 465 ALA L 206
REMARK 465 ASP L 207
REMARK 465 ASP L 208
REMARK 465 ASP L 209
REMARK 465 ALA M -6
REMARK 465 HIS M -5
REMARK 465 HIS M -4
REMARK 465 HIS M -3
REMARK 465 HIS M -2
REMARK 465 HIS M -1
REMARK 465 HIS M 0
REMARK 465 MET M 1
REMARK 465 GLN M 2
REMARK 465 GLY M 3
REMARK 465 SER M 4
REMARK 465 VAL M 5
REMARK 465 ALA N -6
REMARK 465 HIS N -5
REMARK 465 HIS N -4
REMARK 465 HIS N -3
REMARK 465 HIS N -2
REMARK 465 HIS N -1
REMARK 465 HIS N 0
REMARK 465 MET N 1
REMARK 465 GLN N 2
REMARK 465 GLY N 3
REMARK 465 SER N 4
REMARK 465 VAL N 5
REMARK 465 LEU N 234
REMARK 465 ARG N 235
REMARK 465 MET O 1
REMARK 465 MET P 1
REMARK 465 LYS P 2
REMARK 465 ASP P 3
REMARK 465 LEU P 4
REMARK 465 LEU P 5
REMARK 465 LYS P 6
REMARK 465 PHE P 7
REMARK 465 LEU P 8
REMARK 465 LYS P 9
REMARK 465 ALA P 10
REMARK 465 GLN P 11
REMARK 465 THR P 12
REMARK 465 LYS P 13
REMARK 465 THR P 14
REMARK 465 GLU P 1377
REMARK 465 ALA P 1378
REMARK 465 PRO P 1379
REMARK 465 ALA P 1380
REMARK 465 ALA P 1381
REMARK 465 PRO P 1382
REMARK 465 GLN P 1383
REMARK 465 VAL P 1384
REMARK 465 THR P 1385
REMARK 465 ALA P 1386
REMARK 465 GLU P 1387
REMARK 465 ASP P 1388
REMARK 465 ALA P 1389
REMARK 465 SER P 1390
REMARK 465 ALA P 1391
REMARK 465 SER P 1392
REMARK 465 LEU P 1393
REMARK 465 ALA P 1394
REMARK 465 GLU P 1395
REMARK 465 LEU P 1396
REMARK 465 LEU P 1397
REMARK 465 ASN P 1398
REMARK 465 ALA P 1399
REMARK 465 GLY P 1400
REMARK 465 LEU P 1401
REMARK 465 GLY P 1402
REMARK 465 GLY P 1403
REMARK 465 SER P 1404
REMARK 465 ASP P 1405
REMARK 465 ASN P 1406
REMARK 465 GLU P 1407
REMARK 465 MET R -14
REMARK 465 ARG R -13
REMARK 465 GLY R -12
REMARK 465 SER R -11
REMARK 465 HIS R -10
REMARK 465 HIS R -9
REMARK 465 HIS R -8
REMARK 465 HIS R -7
REMARK 465 HIS R -6
REMARK 465 HIS R -5
REMARK 465 THR R -4
REMARK 465 ASP R -3
REMARK 465 GLN R -2
REMARK 465 PHE R -1
REMARK 465 THR R 0
REMARK 465 MET R 1
REMARK 465 GLU R 2
REMARK 465 GLN R 3
REMARK 465 ASN R 4
REMARK 465 PRO R 5
REMARK 465 GLN R 6
REMARK 465 SER R 7
REMARK 465 GLN R 8
REMARK 465 LEU R 9
REMARK 465 LYS R 10
REMARK 465 LEU R 11
REMARK 465 LEU R 12
REMARK 465 VAL R 13
REMARK 465 THR R 14
REMARK 465 ARG R 15
REMARK 465 GLY R 16
REMARK 465 LYS R 17
REMARK 465 GLU R 18
REMARK 465 GLN R 19
REMARK 465 GLY R 20
REMARK 465 TYR R 21
REMARK 465 LEU R 22
REMARK 465 THR R 23
REMARK 465 TYR R 24
REMARK 465 ALA R 25
REMARK 465 GLU R 26
REMARK 465 VAL R 27
REMARK 465 ASN R 28
REMARK 465 ASP R 29
REMARK 465 HIS R 30
REMARK 465 LEU R 31
REMARK 465 PRO R 32
REMARK 465 GLU R 33
REMARK 465 ASP R 34
REMARK 465 ILE R 35
REMARK 465 VAL R 36
REMARK 465 ASP R 37
REMARK 465 SER R 38
REMARK 465 ASP R 39
REMARK 465 GLN R 40
REMARK 465 ILE R 41
REMARK 465 GLU R 42
REMARK 465 ASP R 43
REMARK 465 ILE R 44
REMARK 465 ILE R 45
REMARK 465 GLN R 46
REMARK 465 MET R 47
REMARK 465 ILE R 48
REMARK 465 ASN R 49
REMARK 465 ASP R 50
REMARK 465 MET R 51
REMARK 465 GLY R 52
REMARK 465 ILE R 53
REMARK 465 GLN R 54
REMARK 465 VAL R 55
REMARK 465 MET R 56
REMARK 465 GLU R 57
REMARK 465 GLU R 58
REMARK 465 ALA R 59
REMARK 465 PRO R 60
REMARK 465 ASP R 61
REMARK 465 ALA R 62
REMARK 465 ASP R 63
REMARK 465 ASP R 64
REMARK 465 LEU R 65
REMARK 465 MET R 66
REMARK 465 LEU R 67
REMARK 465 ALA R 68
REMARK 465 GLU R 69
REMARK 465 ASN R 70
REMARK 465 THR R 71
REMARK 465 ALA R 72
REMARK 465 ASP R 73
REMARK 465 GLU R 74
REMARK 465 ASP R 75
REMARK 465 ALA R 76
REMARK 465 ALA R 77
REMARK 465 GLU R 78
REMARK 465 GLU R 172
REMARK 465 ASP R 173
REMARK 465 LEU R 174
REMARK 465 ALA R 175
REMARK 465 PRO R 176
REMARK 465 THR R 177
REMARK 465 ALA R 178
REMARK 465 THR R 179
REMARK 465 HIS R 180
REMARK 465 VAL R 181
REMARK 465 GLY R 182
REMARK 465 SER R 183
REMARK 465 GLU R 184
REMARK 465 LEU R 185
REMARK 465 SER R 186
REMARK 465 GLN R 187
REMARK 465 GLU R 188
REMARK 465 ASP R 189
REMARK 465 LEU R 190
REMARK 465 ASP R 191
REMARK 465 ASP R 192
REMARK 465 ASP R 193
REMARK 465 GLU R 194
REMARK 465 ASP R 195
REMARK 465 GLU R 196
REMARK 465 ASP R 197
REMARK 465 GLU R 198
REMARK 465 GLU R 199
REMARK 465 ASP R 200
REMARK 465 GLY R 201
REMARK 465 ASP R 202
REMARK 465 ASP R 203
REMARK 465 ASP R 204
REMARK 465 SER R 205
REMARK 465 ALA R 206
REMARK 465 ASP R 207
REMARK 465 ASP R 208
REMARK 465 ASP R 209
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 OP1 C 6 17 MG MG J 1503 1.13
REMARK 500 SG CYS P 88 ZN ZN P 1501 1.39
REMARK 500 SG CYS J 814 ZN ZN J 1502 1.51
REMARK 500 SG CYS P 70 ZN ZN P 1501 1.52
REMARK 500 OD2 ASP P 462 MG MG P 1503 1.61
REMARK 500 O ASP C 342 ND2 ASN C 437 1.62
REMARK 500 NZ LYS O 1073 OP1 U 9 16 1.65
REMARK 500 CG1 VAL J 421 O HIS J 469 1.70
REMARK 500 NH2 ARG D 425 O2' U 3 16 1.72
REMARK 500 OG1 THR I 1286 OE2 GLU J 479 1.77
REMARK 500 O THR D 703 CB SER D 718 1.77
REMARK 500 NH2 ARG O 402 O SER O 417 1.77
REMARK 500 NH2 ARG C 452 OE1 GLU C 458 1.78
REMARK 500 OG1 THR F 583 OP2 DT 1 14 1.81
REMARK 500 OD1 ASN B 84 NH1 ARG D 551 1.84
REMARK 500 OD2 ASP C 14 NH2 ARG C 1156 1.86
REMARK 500 O PRO C 560 NH2 ARG D 780 1.87
REMARK 500 O ASN F 396 N GLY F 398 1.88
REMARK 500 O PHE J 17 NH1 ARG J 1355 1.90
REMARK 500 NH2 ARG P 515 O SER P 718 1.93
REMARK 500 O ALA M 112 CD1 ILE M 115 1.93
REMARK 500 NH1 ARG J 275 O MET J 298 1.93
REMARK 500 NZ LYS I 755 O GLN I 767 1.94
REMARK 500 OH TYR J 1282 NH2 ARG J 1304 1.95
REMARK 500 O VAL J 1226 OG1 THR J 1230 1.95
REMARK 500 OG1 THR J 392 OG SER L 609 1.96
REMARK 500 N GLY J 711 OH TYR P 1302 1.96
REMARK 500 O GLY F 564 O MET F 567 1.96
REMARK 500 O VAL P 1226 OG1 THR P 1230 1.97
REMARK 500 SD MET P 1095 NH2 ARG P 1173 1.97
REMARK 500 O ALA D 946 N SER D 948 1.97
REMARK 500 O LYS J 1348 CD1 ILE J 1352 1.98
REMARK 500 O VAL D 1226 OG1 THR D 1230 1.99
REMARK 500 O ILE R 511 N6 DA 8 19 1.99
REMARK 500 O ALA J 482 ND2 ASN J 488 1.99
REMARK 500 O LEU H 39 CG LEU H 43 2.00
REMARK 500 O GLY R 564 O MET R 567 2.00
REMARK 500 NH2 ARG I 540 O1G GTP 6 13 2.01
REMARK 500 O HIS R 518 N GLY R 520 2.01
REMARK 500 NZ LYS I 593 OG1 THR I 595 2.01
REMARK 500 O SER J 1164 CD1 LEU J 1175 2.02
REMARK 500 OG SER J 34 ND1 HIS J 104 2.02
REMARK 500 NH1 ARG C 542 C7 DT 1 50 2.03
REMARK 500 O SER P 1321 OG SER P 1324 2.03
REMARK 500 NZ LYS O 118 O ASP O 485 2.03
REMARK 500 O SER J 1321 OG SER J 1324 2.03
REMARK 500 O SER D 1321 OG SER D 1324 2.04
REMARK 500 O LEU I 1291 NZ LYS J 345 2.05
REMARK 500 NH2 ARG I 452 OE1 GLU I 458 2.05
REMARK 500 O PRO O 110 N GLY O 112 2.05
REMARK 500
REMARK 500 THIS ENTRY HAS 126 CLOSE CONTACTS
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O5' DG 2 3 O3' DT 2 51 2657 1.64
REMARK 500 NH2 ARG D 1174 OP1 DA 1 17 2657 2.10
REMARK 500 O5' DA 7 12 O3' DC 7 60 2546 2.13
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 LYS D 955 CE LYS D 955 NZ 0.274
REMARK 500 SER I 638 CB SER I 638 OG 0.209
REMARK 500 ARG K 91 C ARG K 91 O 0.141
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 LEU A 39 CA - CB - CG ANGL. DEV. = -17.5 DEGREES
REMARK 500 LEU B 228 CA - CB - CG ANGL. DEV. = -18.6 DEGREES
REMARK 500 PRO C 560 C - N - CA ANGL. DEV. = 9.1 DEGREES
REMARK 500 LEU C 587 CA - CB - CG ANGL. DEV. = -14.7 DEGREES
REMARK 500 LEU C 693 CA - CB - CG ANGL. DEV. = -15.6 DEGREES
REMARK 500 PRO D 121 C - N - CD ANGL. DEV. = -13.5 DEGREES
REMARK 500 LEU D 239 CA - CB - CG ANGL. DEV. = -19.3 DEGREES
REMARK 500 LEU D 423 CA - CB - CG ANGL. DEV. = -15.0 DEGREES
REMARK 500 PRO D 530 C - N - CA ANGL. DEV. = 11.1 DEGREES
REMARK 500 ILE D 737 CB - CA - C ANGL. DEV. = -13.3 DEGREES
REMARK 500 LEU D 770 CA - CB - CG ANGL. DEV. = 14.8 DEGREES
REMARK 500 LEU H 13 CA - CB - CG ANGL. DEV. = 14.6 DEGREES
REMARK 500 LEU H 47 CA - CB - CG ANGL. DEV. = -15.6 DEGREES
REMARK 500 LEU J 120 CA - CB - CG ANGL. DEV. = 14.1 DEGREES
REMARK 500 PRO J 121 C - N - CD ANGL. DEV. = -21.6 DEGREES
REMARK 500 LEU J 239 CA - CB - CG ANGL. DEV. = -15.5 DEGREES
REMARK 500 LEU J 268 CA - CB - CG ANGL. DEV. = -13.9 DEGREES
REMARK 500 PRO J 530 C - N - CA ANGL. DEV. = 9.8 DEGREES
REMARK 500 VAL J 885 CB - CA - C ANGL. DEV. = -11.5 DEGREES
REMARK 500 PRO J1217 C - N - CA ANGL. DEV. = 11.3 DEGREES
REMARK 500 PRO L 325 C - N - CA ANGL. DEV. = 9.9 DEGREES
REMARK 500 LEU M 83 CA - CB - CG ANGL. DEV. = 14.3 DEGREES
REMARK 500 PRO N 30 C - N - CD ANGL. DEV. = -19.9 DEGREES
REMARK 500 ILE O1308 CB - CA - C ANGL. DEV. = -12.3 DEGREES
REMARK 500 LEU O1327 CA - CB - CG ANGL. DEV. = 15.5 DEGREES
REMARK 500 PRO P 121 C - N - CD ANGL. DEV. = -14.4 DEGREES
REMARK 500 PRO P 530 C - N - CA ANGL. DEV. = 9.5 DEGREES
REMARK 500 LEU P1243 CA - CB - CG ANGL. DEV. = 14.5 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 VAL A 14 -80.53 -114.43
REMARK 500 VAL A 19 -79.98 -80.50
REMARK 500 GLN A 93 -101.22 -75.24
REMARK 500 THR A 134 -81.80 -86.13
REMARK 500 SER A 161 45.51 -107.09
REMARK 500 GLU A 162 81.21 -69.94
REMARK 500 GLN A 194 -41.28 -130.03
REMARK 500 ASP A 197 32.51 -88.24
REMARK 500 THR A 210 -83.97 -3.04
REMARK 500 VAL B 14 -85.95 -118.33
REMARK 500 ILE B 16 48.54 -147.95
REMARK 500 ALA B 55 -175.64 163.87
REMARK 500 GLN B 93 -100.99 -99.30
REMARK 500 ASP B 118 124.75 62.68
REMARK 500 THR B 134 -74.36 -79.34
REMARK 500 HIS B 160 -71.03 -41.52
REMARK 500 SER B 161 56.34 -115.42
REMARK 500 ASP B 164 98.20 -55.47
REMARK 500 ARG B 191 82.38 56.97
REMARK 500 GLU B 193 106.77 -29.70
REMARK 500 GLN B 194 -50.80 91.61
REMARK 500 VAL C 21 -71.59 -80.41
REMARK 500 TYR C 26 102.50 -44.41
REMARK 500 VAL C 71 -64.37 -96.20
REMARK 500 ARG C 107 -71.53 -63.96
REMARK 500 PRO C 110 -71.44 -39.94
REMARK 500 GLU C 111 55.25 -145.67
REMARK 500 THR C 113 22.43 -62.00
REMARK 500 LYS C 163 -63.11 69.77
REMARK 500 HIS C 165 146.32 110.03
REMARK 500 TYR C 179 -70.85 -57.73
REMARK 500 ARG C 200 58.33 21.07
REMARK 500 PHE C 224 -73.71 -66.63
REMARK 500 ASP C 234 -124.17 63.10
REMARK 500 GLU C 244 39.67 -79.10
REMARK 500 ARG C 247 102.05 -30.08
REMARK 500 ASN C 258 -93.34 57.47
REMARK 500 LYS C 265 85.13 -65.78
REMARK 500 ASP C 281 60.05 78.28
REMARK 500 GLU C 286 75.65 -112.20
REMARK 500 PRO C 288 -148.42 -74.81
REMARK 500 LYS C 295 -167.99 -79.75
REMARK 500 ALA C 298 -72.67 -77.80
REMARK 500 ASN C 314 46.53 80.10
REMARK 500 LYS C 331 30.98 -91.61
REMARK 500 ASN C 339 45.92 -106.56
REMARK 500 ASP C 340 -145.71 47.22
REMARK 500 LEU C 341 -90.15 51.23
REMARK 500 PRO C 345 34.78 -74.11
REMARK 500 ASN C 357 -90.37 -101.96
REMARK 500
REMARK 500 THIS ENTRY HAS 601 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 GLU P 1276 GLY P 1277 149.39
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 D1501 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 70 SG
REMARK 620 2 CYS D 72 SG 111.9
REMARK 620 3 CYS D 85 SG 98.9 107.4
REMARK 620 4 CYS D 88 SG 105.5 138.5 83.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D1503 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 460 OD1
REMARK 620 2 ASP D 462 OD1 90.3
REMARK 620 3 ASP D 464 OD1 110.7 82.2
REMARK 620 4 ASP D 464 OD2 72.1 114.3 50.8
REMARK 620 5 U 3 16 O3' 113.8 151.0 102.7 89.5
REMARK 620 6 C 3 17 OP1 85.1 91.4 162.8 145.1 75.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D1502 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 814 SG
REMARK 620 2 CYS D 895 SG 102.6
REMARK 620 3 CYS D 898 SG 118.9 87.4
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN J1501 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS J 70 SG
REMARK 620 2 CYS J 72 SG 136.5
REMARK 620 3 CYS J 85 SG 95.8 81.9
REMARK 620 4 CYS J 88 SG 111.6 110.3 78.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG J1503 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP J 460 OD1
REMARK 620 2 ASP J 460 OD2 47.1
REMARK 620 3 ASP J 462 OD1 81.3 92.6
REMARK 620 4 ASP J 462 OD2 100.4 74.4 48.4
REMARK 620 5 U 6 16 O3' 86.6 121.8 116.4 160.9
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN J1502 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ARG J 883 NH2
REMARK 620 2 CYS J 888 SG 178.7
REMARK 620 3 CYS J 895 SG 81.5 97.3
REMARK 620 4 CYS J 898 SG 93.8 85.4 83.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG P1503 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP P 460 OD2
REMARK 620 2 ASP P 462 OD1 86.5
REMARK 620 3 C 9 17 OP1 71.6 91.7
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN P1502 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS P 814 SG
REMARK 620 2 CYS P 888 SG 90.6
REMARK 620 3 CYS P 895 SG 94.4 102.9
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN D 1501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN D 1502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG D 1503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN J 1501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN J 1502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG J 1503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN P 1501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN P 1502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG P 1503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for nucleotide GTP 3 13
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for nucleotide GTP 6 13
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for nucleotide GTP 9 13
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4YLN RELATED DB: PDB
REMARK 900 RELATED ID: 4YLO RELATED DB: PDB
DBREF 4YLP A 1 235 UNP A7ZSI4 RPOA_ECO24 1 235
DBREF 4YLP B 1 235 UNP A7ZSI4 RPOA_ECO24 1 235
DBREF 4YLP C 1 1342 UNP A7ZUK1 RPOB_ECO24 1 1342
DBREF 4YLP D 1 1407 UNP A7ZUK2 RPOC_ECO24 1 1407
DBREF 4YLP E 2 91 UNP A7ZTK1 RPOZ_ECO24 2 91
DBREF 4YLP F 1 613 UNP P00579 RPOD_ECOLI 1 613
DBREF 4YLP 1 12 60 PDB 4YLP 4YLP 12 60
DBREF 4YLP 2 3 51 PDB 4YLP 4YLP 3 51
DBREF 4YLP 3 13 17 PDB 4YLP 4YLP 13 17
DBREF 4YLP G 1 235 UNP A7ZSI4 RPOA_ECO24 1 235
DBREF 4YLP H 1 235 UNP A7ZSI4 RPOA_ECO24 1 235
DBREF 4YLP I 1 1342 UNP A7ZUK1 RPOB_ECO24 1 1342
DBREF 4YLP J 1 1407 UNP A7ZUK2 RPOC_ECO24 1 1407
DBREF 4YLP K 2 91 UNP A7ZTK1 RPOZ_ECO24 2 91
DBREF 4YLP L 1 613 UNP P00579 RPOD_ECOLI 1 613
DBREF 4YLP 4 12 60 PDB 4YLP 4YLP 12 60
DBREF 4YLP 5 3 51 PDB 4YLP 4YLP 3 51
DBREF 4YLP 6 13 17 PDB 4YLP 4YLP 13 17
DBREF 4YLP M 1 235 UNP A7ZSI4 RPOA_ECO24 1 235
DBREF 4YLP N 1 235 UNP A7ZSI4 RPOA_ECO24 1 235
DBREF 4YLP O 1 1342 UNP A7ZUK1 RPOB_ECO24 1 1342
DBREF 4YLP P 1 1407 UNP A7ZUK2 RPOC_ECO24 1 1407
DBREF 4YLP Q 2 91 UNP A7ZTK1 RPOZ_ECO24 2 91
DBREF 4YLP R 1 613 UNP P00579 RPOD_ECOLI 1 613
DBREF 4YLP 7 12 60 PDB 4YLP 4YLP 12 60
DBREF 4YLP 8 3 51 PDB 4YLP 4YLP 3 51
DBREF 4YLP 9 13 17 PDB 4YLP 4YLP 13 17
SEQADV 4YLP ALA A -6 UNP A7ZSI4 EXPRESSION TAG
SEQADV 4YLP HIS A -5 UNP A7ZSI4 EXPRESSION TAG
SEQADV 4YLP HIS A -4 UNP A7ZSI4 EXPRESSION TAG
SEQADV 4YLP HIS A -3 UNP A7ZSI4 EXPRESSION TAG
SEQADV 4YLP HIS A -2 UNP A7ZSI4 EXPRESSION TAG
SEQADV 4YLP HIS A -1 UNP A7ZSI4 EXPRESSION TAG
SEQADV 4YLP HIS A 0 UNP A7ZSI4 EXPRESSION TAG
SEQADV 4YLP ALA B -6 UNP A7ZSI4 EXPRESSION TAG
SEQADV 4YLP HIS B -5 UNP A7ZSI4 EXPRESSION TAG
SEQADV 4YLP HIS B -4 UNP A7ZSI4 EXPRESSION TAG
SEQADV 4YLP HIS B -3 UNP A7ZSI4 EXPRESSION TAG
SEQADV 4YLP HIS B -2 UNP A7ZSI4 EXPRESSION TAG
SEQADV 4YLP HIS B -1 UNP A7ZSI4 EXPRESSION TAG
SEQADV 4YLP HIS B 0 UNP A7ZSI4 EXPRESSION TAG
SEQADV 4YLP MET F -14 UNP P00579 EXPRESSION TAG
SEQADV 4YLP ARG F -13 UNP P00579 EXPRESSION TAG
SEQADV 4YLP GLY F -12 UNP P00579 EXPRESSION TAG
SEQADV 4YLP SER F -11 UNP P00579 EXPRESSION TAG
SEQADV 4YLP HIS F -10 UNP P00579 EXPRESSION TAG
SEQADV 4YLP HIS F -9 UNP P00579 EXPRESSION TAG
SEQADV 4YLP HIS F -8 UNP P00579 EXPRESSION TAG
SEQADV 4YLP HIS F -7 UNP P00579 EXPRESSION TAG
SEQADV 4YLP HIS F -6 UNP P00579 EXPRESSION TAG
SEQADV 4YLP HIS F -5 UNP P00579 EXPRESSION TAG
SEQADV 4YLP THR F -4 UNP P00579 EXPRESSION TAG
SEQADV 4YLP ASP F -3 UNP P00579 EXPRESSION TAG
SEQADV 4YLP GLN F -2 UNP P00579 EXPRESSION TAG
SEQADV 4YLP PHE F -1 UNP P00579 EXPRESSION TAG
SEQADV 4YLP THR F 0 UNP P00579 EXPRESSION TAG
SEQADV 4YLP ALA G -6 UNP A7ZSI4 EXPRESSION TAG
SEQADV 4YLP HIS G -5 UNP A7ZSI4 EXPRESSION TAG
SEQADV 4YLP HIS G -4 UNP A7ZSI4 EXPRESSION TAG
SEQADV 4YLP HIS G -3 UNP A7ZSI4 EXPRESSION TAG
SEQADV 4YLP HIS G -2 UNP A7ZSI4 EXPRESSION TAG
SEQADV 4YLP HIS G -1 UNP A7ZSI4 EXPRESSION TAG
SEQADV 4YLP HIS G 0 UNP A7ZSI4 EXPRESSION TAG
SEQADV 4YLP ALA H -6 UNP A7ZSI4 EXPRESSION TAG
SEQADV 4YLP HIS H -5 UNP A7ZSI4 EXPRESSION TAG
SEQADV 4YLP HIS H -4 UNP A7ZSI4 EXPRESSION TAG
SEQADV 4YLP HIS H -3 UNP A7ZSI4 EXPRESSION TAG
SEQADV 4YLP HIS H -2 UNP A7ZSI4 EXPRESSION TAG
SEQADV 4YLP HIS H -1 UNP A7ZSI4 EXPRESSION TAG
SEQADV 4YLP HIS H 0 UNP A7ZSI4 EXPRESSION TAG
SEQADV 4YLP MET L -14 UNP P00579 EXPRESSION TAG
SEQADV 4YLP ARG L -13 UNP P00579 EXPRESSION TAG
SEQADV 4YLP GLY L -12 UNP P00579 EXPRESSION TAG
SEQADV 4YLP SER L -11 UNP P00579 EXPRESSION TAG
SEQADV 4YLP HIS L -10 UNP P00579 EXPRESSION TAG
SEQADV 4YLP HIS L -9 UNP P00579 EXPRESSION TAG
SEQADV 4YLP HIS L -8 UNP P00579 EXPRESSION TAG
SEQADV 4YLP HIS L -7 UNP P00579 EXPRESSION TAG
SEQADV 4YLP HIS L -6 UNP P00579 EXPRESSION TAG
SEQADV 4YLP HIS L -5 UNP P00579 EXPRESSION TAG
SEQADV 4YLP THR L -4 UNP P00579 EXPRESSION TAG
SEQADV 4YLP ASP L -3 UNP P00579 EXPRESSION TAG
SEQADV 4YLP GLN L -2 UNP P00579 EXPRESSION TAG
SEQADV 4YLP PHE L -1 UNP P00579 EXPRESSION TAG
SEQADV 4YLP THR L 0 UNP P00579 EXPRESSION TAG
SEQADV 4YLP ALA M -6 UNP A7ZSI4 EXPRESSION TAG
SEQADV 4YLP HIS M -5 UNP A7ZSI4 EXPRESSION TAG
SEQADV 4YLP HIS M -4 UNP A7ZSI4 EXPRESSION TAG
SEQADV 4YLP HIS M -3 UNP A7ZSI4 EXPRESSION TAG
SEQADV 4YLP HIS M -2 UNP A7ZSI4 EXPRESSION TAG
SEQADV 4YLP HIS M -1 UNP A7ZSI4 EXPRESSION TAG
SEQADV 4YLP HIS M 0 UNP A7ZSI4 EXPRESSION TAG
SEQADV 4YLP ALA N -6 UNP A7ZSI4 EXPRESSION TAG
SEQADV 4YLP HIS N -5 UNP A7ZSI4 EXPRESSION TAG
SEQADV 4YLP HIS N -4 UNP A7ZSI4 EXPRESSION TAG
SEQADV 4YLP HIS N -3 UNP A7ZSI4 EXPRESSION TAG
SEQADV 4YLP HIS N -2 UNP A7ZSI4 EXPRESSION TAG
SEQADV 4YLP HIS N -1 UNP A7ZSI4 EXPRESSION TAG
SEQADV 4YLP HIS N 0 UNP A7ZSI4 EXPRESSION TAG
SEQADV 4YLP MET R -14 UNP P00579 EXPRESSION TAG
SEQADV 4YLP ARG R -13 UNP P00579 EXPRESSION TAG
SEQADV 4YLP GLY R -12 UNP P00579 EXPRESSION TAG
SEQADV 4YLP SER R -11 UNP P00579 EXPRESSION TAG
SEQADV 4YLP HIS R -10 UNP P00579 EXPRESSION TAG
SEQADV 4YLP HIS R -9 UNP P00579 EXPRESSION TAG
SEQADV 4YLP HIS R -8 UNP P00579 EXPRESSION TAG
SEQADV 4YLP HIS R -7 UNP P00579 EXPRESSION TAG
SEQADV 4YLP HIS R -6 UNP P00579 EXPRESSION TAG
SEQADV 4YLP HIS R -5 UNP P00579 EXPRESSION TAG
SEQADV 4YLP THR R -4 UNP P00579 EXPRESSION TAG
SEQADV 4YLP ASP R -3 UNP P00579 EXPRESSION TAG
SEQADV 4YLP GLN R -2 UNP P00579 EXPRESSION TAG
SEQADV 4YLP PHE R -1 UNP P00579 EXPRESSION TAG
SEQADV 4YLP THR R 0 UNP P00579 EXPRESSION TAG
SEQRES 1 A 242 ALA HIS HIS HIS HIS HIS HIS MET GLN GLY SER VAL THR
SEQRES 2 A 242 GLU PHE LEU LYS PRO ARG LEU VAL ASP ILE GLU GLN VAL
SEQRES 3 A 242 SER SER THR HIS ALA LYS VAL THR LEU GLU PRO LEU GLU
SEQRES 4 A 242 ARG GLY PHE GLY HIS THR LEU GLY ASN ALA LEU ARG ARG
SEQRES 5 A 242 ILE LEU LEU SER SER MET PRO GLY CYS ALA VAL THR GLU
SEQRES 6 A 242 VAL GLU ILE ASP GLY VAL LEU HIS GLU TYR SER THR LYS
SEQRES 7 A 242 GLU GLY VAL GLN GLU ASP ILE LEU GLU ILE LEU LEU ASN
SEQRES 8 A 242 LEU LYS GLY LEU ALA VAL ARG VAL GLN GLY LYS ASP GLU
SEQRES 9 A 242 VAL ILE LEU THR LEU ASN LYS SER GLY ILE GLY PRO VAL
SEQRES 10 A 242 THR ALA ALA ASP ILE THR HIS ASP GLY ASP VAL GLU ILE
SEQRES 11 A 242 VAL LYS PRO GLN HIS VAL ILE CYS HIS LEU THR ASP GLU
SEQRES 12 A 242 ASN ALA SER ILE SER MET ARG ILE LYS VAL GLN ARG GLY
SEQRES 13 A 242 ARG GLY TYR VAL PRO ALA SER THR ARG ILE HIS SER GLU
SEQRES 14 A 242 GLU ASP GLU ARG PRO ILE GLY ARG LEU LEU VAL ASP ALA
SEQRES 15 A 242 CYS TYR SER PRO VAL GLU ARG ILE ALA TYR ASN VAL GLU
SEQRES 16 A 242 ALA ALA ARG VAL GLU GLN ARG THR ASP LEU ASP LYS LEU
SEQRES 17 A 242 VAL ILE GLU MET GLU THR ASN GLY THR ILE ASP PRO GLU
SEQRES 18 A 242 GLU ALA ILE ARG ARG ALA ALA THR ILE LEU ALA GLU GLN
SEQRES 19 A 242 LEU GLU ALA PHE VAL ASP LEU ARG
SEQRES 1 B 242 ALA HIS HIS HIS HIS HIS HIS MET GLN GLY SER VAL THR
SEQRES 2 B 242 GLU PHE LEU LYS PRO ARG LEU VAL ASP ILE GLU GLN VAL
SEQRES 3 B 242 SER SER THR HIS ALA LYS VAL THR LEU GLU PRO LEU GLU
SEQRES 4 B 242 ARG GLY PHE GLY HIS THR LEU GLY ASN ALA LEU ARG ARG
SEQRES 5 B 242 ILE LEU LEU SER SER MET PRO GLY CYS ALA VAL THR GLU
SEQRES 6 B 242 VAL GLU ILE ASP GLY VAL LEU HIS GLU TYR SER THR LYS
SEQRES 7 B 242 GLU GLY VAL GLN GLU ASP ILE LEU GLU ILE LEU LEU ASN
SEQRES 8 B 242 LEU LYS GLY LEU ALA VAL ARG VAL GLN GLY LYS ASP GLU
SEQRES 9 B 242 VAL ILE LEU THR LEU ASN LYS SER GLY ILE GLY PRO VAL
SEQRES 10 B 242 THR ALA ALA ASP ILE THR HIS ASP GLY ASP VAL GLU ILE
SEQRES 11 B 242 VAL LYS PRO GLN HIS VAL ILE CYS HIS LEU THR ASP GLU
SEQRES 12 B 242 ASN ALA SER ILE SER MET ARG ILE LYS VAL GLN ARG GLY
SEQRES 13 B 242 ARG GLY TYR VAL PRO ALA SER THR ARG ILE HIS SER GLU
SEQRES 14 B 242 GLU ASP GLU ARG PRO ILE GLY ARG LEU LEU VAL ASP ALA
SEQRES 15 B 242 CYS TYR SER PRO VAL GLU ARG ILE ALA TYR ASN VAL GLU
SEQRES 16 B 242 ALA ALA ARG VAL GLU GLN ARG THR ASP LEU ASP LYS LEU
SEQRES 17 B 242 VAL ILE GLU MET GLU THR ASN GLY THR ILE ASP PRO GLU
SEQRES 18 B 242 GLU ALA ILE ARG ARG ALA ALA THR ILE LEU ALA GLU GLN
SEQRES 19 B 242 LEU GLU ALA PHE VAL ASP LEU ARG
SEQRES 1 C 1342 MET VAL TYR SER TYR THR GLU LYS LYS ARG ILE ARG LYS
SEQRES 2 C 1342 ASP PHE GLY LYS ARG PRO GLN VAL LEU ASP VAL PRO TYR
SEQRES 3 C 1342 LEU LEU SER ILE GLN LEU ASP SER PHE GLN LYS PHE ILE
SEQRES 4 C 1342 GLU GLN ASP PRO GLU GLY GLN TYR GLY LEU GLU ALA ALA
SEQRES 5 C 1342 PHE ARG SER VAL PHE PRO ILE GLN SER TYR SER GLY ASN
SEQRES 6 C 1342 SER GLU LEU GLN TYR VAL SER TYR ARG LEU GLY GLU PRO
SEQRES 7 C 1342 VAL PHE ASP VAL GLN GLU CYS GLN ILE ARG GLY VAL THR
SEQRES 8 C 1342 TYR SER ALA PRO LEU ARG VAL LYS LEU ARG LEU VAL ILE
SEQRES 9 C 1342 TYR GLU ARG GLU ALA PRO GLU GLY THR VAL LYS ASP ILE
SEQRES 10 C 1342 LYS GLU GLN GLU VAL TYR MET GLY GLU ILE PRO LEU MET
SEQRES 11 C 1342 THR ASP ASN GLY THR PHE VAL ILE ASN GLY THR GLU ARG
SEQRES 12 C 1342 VAL ILE VAL SER GLN LEU HIS ARG SER PRO GLY VAL PHE
SEQRES 13 C 1342 PHE ASP SER ASP LYS GLY LYS THR HIS SER SER GLY LYS
SEQRES 14 C 1342 VAL LEU TYR ASN ALA ARG ILE ILE PRO TYR ARG GLY SER
SEQRES 15 C 1342 TRP LEU ASP PHE GLU PHE ASP PRO LYS ASP ASN LEU PHE
SEQRES 16 C 1342 VAL ARG ILE ASP ARG ARG ARG LYS LEU PRO ALA THR ILE
SEQRES 17 C 1342 ILE LEU ARG ALA LEU ASN TYR THR THR GLU GLN ILE LEU
SEQRES 18 C 1342 ASP LEU PHE PHE GLU LYS VAL ILE PHE GLU ILE ARG ASP
SEQRES 19 C 1342 ASN LYS LEU GLN MET GLU LEU VAL PRO GLU ARG LEU ARG
SEQRES 20 C 1342 GLY GLU THR ALA SER PHE ASP ILE GLU ALA ASN GLY LYS
SEQRES 21 C 1342 VAL TYR VAL GLU LYS GLY ARG ARG ILE THR ALA ARG HIS
SEQRES 22 C 1342 ILE ARG GLN LEU GLU LYS ASP ASP VAL LYS LEU ILE GLU
SEQRES 23 C 1342 VAL PRO VAL GLU TYR ILE ALA GLY LYS VAL VAL ALA LYS
SEQRES 24 C 1342 ASP TYR ILE ASP GLU SER THR GLY GLU LEU ILE CYS ALA
SEQRES 25 C 1342 ALA ASN MET GLU LEU SER LEU ASP LEU LEU ALA LYS LEU
SEQRES 26 C 1342 SER GLN SER GLY HIS LYS ARG ILE GLU THR LEU PHE THR
SEQRES 27 C 1342 ASN ASP LEU ASP HIS GLY PRO TYR ILE SER GLU THR LEU
SEQRES 28 C 1342 ARG VAL ASP PRO THR ASN ASP ARG LEU SER ALA LEU VAL
SEQRES 29 C 1342 GLU ILE TYR ARG MET MET ARG PRO GLY GLU PRO PRO THR
SEQRES 30 C 1342 ARG GLU ALA ALA GLU SER LEU PHE GLU ASN LEU PHE PHE
SEQRES 31 C 1342 SER GLU ASP ARG TYR ASP LEU SER ALA VAL GLY ARG MET
SEQRES 32 C 1342 LYS PHE ASN ARG SER LEU LEU ARG GLU GLU ILE GLU GLY
SEQRES 33 C 1342 SER GLY ILE LEU SER LYS ASP ASP ILE ILE ASP VAL MET
SEQRES 34 C 1342 LYS LYS LEU ILE ASP ILE ARG ASN GLY LYS GLY GLU VAL
SEQRES 35 C 1342 ASP ASP ILE ASP HIS LEU GLY ASN ARG ARG ILE ARG SER
SEQRES 36 C 1342 VAL GLY GLU MET ALA GLU ASN GLN PHE ARG VAL GLY LEU
SEQRES 37 C 1342 VAL ARG VAL GLU ARG ALA VAL LYS GLU ARG LEU SER LEU
SEQRES 38 C 1342 GLY ASP LEU ASP THR LEU MET PRO GLN ASP MET ILE ASN
SEQRES 39 C 1342 ALA LYS PRO ILE SER ALA ALA VAL LYS GLU PHE PHE GLY
SEQRES 40 C 1342 SER SER GLN LEU SER GLN PHE MET ASP GLN ASN ASN PRO
SEQRES 41 C 1342 LEU SER GLU ILE THR HIS LYS ARG ARG ILE SER ALA LEU
SEQRES 42 C 1342 GLY PRO GLY GLY LEU THR ARG GLU ARG ALA GLY PHE GLU
SEQRES 43 C 1342 VAL ARG ASP VAL HIS PRO THR HIS TYR GLY ARG VAL CYS
SEQRES 44 C 1342 PRO ILE GLU THR PRO GLU GLY PRO ASN ILE GLY LEU ILE
SEQRES 45 C 1342 ASN SER LEU SER VAL TYR ALA GLN THR ASN GLU TYR GLY
SEQRES 46 C 1342 PHE LEU GLU THR PRO TYR ARG LYS VAL THR ASP GLY VAL
SEQRES 47 C 1342 VAL THR ASP GLU ILE HIS TYR LEU SER ALA ILE GLU GLU
SEQRES 48 C 1342 GLY ASN TYR VAL ILE ALA GLN ALA ASN SER ASN LEU ASP
SEQRES 49 C 1342 GLU GLU GLY HIS PHE VAL GLU ASP LEU VAL THR CYS ARG
SEQRES 50 C 1342 SER LYS GLY GLU SER SER LEU PHE SER ARG ASP GLN VAL
SEQRES 51 C 1342 ASP TYR MET ASP VAL SER THR GLN GLN VAL VAL SER VAL
SEQRES 52 C 1342 GLY ALA SER LEU ILE PRO PHE LEU GLU HIS ASP ASP ALA
SEQRES 53 C 1342 ASN ARG ALA LEU MET GLY ALA ASN MET GLN ARG GLN ALA
SEQRES 54 C 1342 VAL PRO THR LEU ARG ALA ASP LYS PRO LEU VAL GLY THR
SEQRES 55 C 1342 GLY MET GLU ARG ALA VAL ALA VAL ASP SER GLY VAL THR
SEQRES 56 C 1342 ALA VAL ALA LYS ARG GLY GLY VAL VAL GLN TYR VAL ASP
SEQRES 57 C 1342 ALA SER ARG ILE VAL ILE LYS VAL ASN GLU ASP GLU MET
SEQRES 58 C 1342 TYR PRO GLY GLU ALA GLY ILE ASP ILE TYR ASN LEU THR
SEQRES 59 C 1342 LYS TYR THR ARG SER ASN GLN ASN THR CYS ILE ASN GLN
SEQRES 60 C 1342 MET PRO CYS VAL SER LEU GLY GLU PRO VAL GLU ARG GLY
SEQRES 61 C 1342 ASP VAL LEU ALA ASP GLY PRO SER THR ASP LEU GLY GLU
SEQRES 62 C 1342 LEU ALA LEU GLY GLN ASN MET ARG VAL ALA PHE MET PRO
SEQRES 63 C 1342 TRP ASN GLY TYR ASN PHE GLU ASP SER ILE LEU VAL SER
SEQRES 64 C 1342 GLU ARG VAL VAL GLN GLU ASP ARG PHE THR THR ILE HIS
SEQRES 65 C 1342 ILE GLN GLU LEU ALA CYS VAL SER ARG ASP THR LYS LEU
SEQRES 66 C 1342 GLY PRO GLU GLU ILE THR ALA ASP ILE PRO ASN VAL GLY
SEQRES 67 C 1342 GLU ALA ALA LEU SER LYS LEU ASP GLU SER GLY ILE VAL
SEQRES 68 C 1342 TYR ILE GLY ALA GLU VAL THR GLY GLY ASP ILE LEU VAL
SEQRES 69 C 1342 GLY LYS VAL THR PRO LYS GLY GLU THR GLN LEU THR PRO
SEQRES 70 C 1342 GLU GLU LYS LEU LEU ARG ALA ILE PHE GLY GLU LYS ALA
SEQRES 71 C 1342 SER ASP VAL LYS ASP SER SER LEU ARG VAL PRO ASN GLY
SEQRES 72 C 1342 VAL SER GLY THR VAL ILE ASP VAL GLN VAL PHE THR ARG
SEQRES 73 C 1342 ASP GLY VAL GLU LYS ASP LYS ARG ALA LEU GLU ILE GLU
SEQRES 74 C 1342 GLU MET GLN LEU LYS GLN ALA LYS LYS ASP LEU SER GLU
SEQRES 75 C 1342 GLU LEU GLN ILE LEU GLU ALA GLY LEU PHE SER ARG ILE
SEQRES 76 C 1342 ARG ALA VAL LEU VAL ALA GLY GLY VAL GLU ALA GLU LYS
SEQRES 77 C 1342 LEU ASP LYS LEU PRO ARG ASP ARG TRP LEU GLU LEU GLY
SEQRES 78 C 1342 LEU THR ASP GLU GLU LYS GLN ASN GLN LEU GLU GLN LEU
SEQRES 79 C 1342 ALA GLU GLN TYR ASP GLU LEU LYS HIS GLU PHE GLU LYS
SEQRES 80 C 1342 LYS LEU GLU ALA LYS ARG ARG LYS ILE THR GLN GLY ASP
SEQRES 81 C 1342 ASP LEU ALA PRO GLY VAL LEU LYS ILE VAL LYS VAL TYR
SEQRES 82 C 1342 LEU ALA VAL LYS ARG ARG ILE GLN PRO GLY ASP LYS MET
SEQRES 83 C 1342 ALA GLY ARG HIS GLY ASN LYS GLY VAL ILE SER LYS ILE
SEQRES 84 C 1342 ASN PRO ILE GLU ASP MET PRO TYR ASP GLU ASN GLY THR
SEQRES 85 C 1342 PRO VAL ASP ILE VAL LEU ASN PRO LEU GLY VAL PRO SER
SEQRES 86 C 1342 ARG MET ASN ILE GLY GLN ILE LEU GLU THR HIS LEU GLY
SEQRES 87 C 1342 MET ALA ALA LYS GLY ILE GLY ASP LYS ILE ASN ALA MET
SEQRES 88 C 1342 LEU LYS GLN GLN GLN GLU VAL ALA LYS LEU ARG GLU PHE
SEQRES 89 C 1342 ILE GLN ARG ALA TYR ASP LEU GLY ALA ASP VAL ARG GLN
SEQRES 90 C 1342 LYS VAL ASP LEU SER THR PHE SER ASP GLU GLU VAL MET
SEQRES 91 C 1342 ARG LEU ALA GLU ASN LEU ARG LYS GLY MET PRO ILE ALA
SEQRES 92 C 1342 THR PRO VAL PHE ASP GLY ALA LYS GLU ALA GLU ILE LYS
SEQRES 93 C 1342 GLU LEU LEU LYS LEU GLY ASP LEU PRO THR SER GLY GLN
SEQRES 94 C 1342 ILE ARG LEU TYR ASP GLY ARG THR GLY GLU GLN PHE GLU
SEQRES 95 C 1342 ARG PRO VAL THR VAL GLY TYR MET TYR MET LEU LYS LEU
SEQRES 96 C 1342 ASN HIS LEU VAL ASP ASP LYS MET HIS ALA ARG SER THR
SEQRES 97 C 1342 GLY SER TYR SER LEU VAL THR GLN GLN PRO LEU GLY GLY
SEQRES 98 C 1342 LYS ALA GLN PHE GLY GLY GLN ARG PHE GLY GLU MET GLU
SEQRES 99 C 1342 VAL TRP ALA LEU GLU ALA TYR GLY ALA ALA TYR THR LEU
SEQRES 100 C 1342 GLN GLU MET LEU THR VAL LYS SER ASP ASP VAL ASN GLY
SEQRES 101 C 1342 ARG THR LYS MET TYR LYS ASN ILE VAL ASP GLY ASN HIS
SEQRES 102 C 1342 GLN MET GLU PRO GLY MET PRO GLU SER PHE ASN VAL LEU
SEQRES 103 C 1342 LEU LYS GLU ILE ARG SER LEU GLY ILE ASN ILE GLU LEU
SEQRES 104 C 1342 GLU ASP GLU
SEQRES 1 D 1407 MET LYS ASP LEU LEU LYS PHE LEU LYS ALA GLN THR LYS
SEQRES 2 D 1407 THR GLU GLU PHE ASP ALA ILE LYS ILE ALA LEU ALA SER
SEQRES 3 D 1407 PRO ASP MET ILE ARG SER TRP SER PHE GLY GLU VAL LYS
SEQRES 4 D 1407 LYS PRO GLU THR ILE ASN TYR ARG THR PHE LYS PRO GLU
SEQRES 5 D 1407 ARG ASP GLY LEU PHE CYS ALA ARG ILE PHE GLY PRO VAL
SEQRES 6 D 1407 LYS ASP TYR GLU CYS LEU CYS GLY LYS TYR LYS ARG LEU
SEQRES 7 D 1407 LYS HIS ARG GLY VAL ILE CYS GLU LYS CYS GLY VAL GLU
SEQRES 8 D 1407 VAL THR GLN THR LYS VAL ARG ARG GLU ARG MET GLY HIS
SEQRES 9 D 1407 ILE GLU LEU ALA SER PRO THR ALA HIS ILE TRP PHE LEU
SEQRES 10 D 1407 LYS SER LEU PRO SER ARG ILE GLY LEU LEU LEU ASP MET
SEQRES 11 D 1407 PRO LEU ARG ASP ILE GLU ARG VAL LEU TYR PHE GLU SER
SEQRES 12 D 1407 TYR VAL VAL ILE GLU GLY GLY MET THR ASN LEU GLU ARG
SEQRES 13 D 1407 GLN GLN ILE LEU THR GLU GLU GLN TYR LEU ASP ALA LEU
SEQRES 14 D 1407 GLU GLU PHE GLY ASP GLU PHE ASP ALA LYS MET GLY ALA
SEQRES 15 D 1407 GLU ALA ILE GLN ALA LEU LEU LYS SER MET ASP LEU GLU
SEQRES 16 D 1407 GLN GLU CYS GLU GLN LEU ARG GLU GLU LEU ASN GLU THR
SEQRES 17 D 1407 ASN SER GLU THR LYS ARG LYS LYS LEU THR LYS ARG ILE
SEQRES 18 D 1407 LYS LEU LEU GLU ALA PHE VAL GLN SER GLY ASN LYS PRO
SEQRES 19 D 1407 GLU TRP MET ILE LEU THR VAL LEU PRO VAL LEU PRO PRO
SEQRES 20 D 1407 ASP LEU ARG PRO LEU VAL PRO LEU ASP GLY GLY ARG PHE
SEQRES 21 D 1407 ALA THR SER ASP LEU ASN ASP LEU TYR ARG ARG VAL ILE
SEQRES 22 D 1407 ASN ARG ASN ASN ARG LEU LYS ARG LEU LEU ASP LEU ALA
SEQRES 23 D 1407 ALA PRO ASP ILE ILE VAL ARG ASN GLU LYS ARG MET LEU
SEQRES 24 D 1407 GLN GLU ALA VAL ASP ALA LEU LEU ASP ASN GLY ARG ARG
SEQRES 25 D 1407 GLY ARG ALA ILE THR GLY SER ASN LYS ARG PRO LEU LYS
SEQRES 26 D 1407 SER LEU ALA ASP MET ILE LYS GLY LYS GLN GLY ARG PHE
SEQRES 27 D 1407 ARG GLN ASN LEU LEU GLY LYS ARG VAL ASP TYR SER GLY
SEQRES 28 D 1407 ARG SER VAL ILE THR VAL GLY PRO TYR LEU ARG LEU HIS
SEQRES 29 D 1407 GLN CYS GLY LEU PRO LYS LYS MET ALA LEU GLU LEU PHE
SEQRES 30 D 1407 LYS PRO PHE ILE TYR GLY LYS LEU GLU LEU ARG GLY LEU
SEQRES 31 D 1407 ALA THR THR ILE LYS ALA ALA LYS LYS MET VAL GLU ARG
SEQRES 32 D 1407 GLU GLU ALA VAL VAL TRP ASP ILE LEU ASP GLU VAL ILE
SEQRES 33 D 1407 ARG GLU HIS PRO VAL LEU LEU ASN ARG ALA PRO THR LEU
SEQRES 34 D 1407 HIS ARG LEU GLY ILE GLN ALA PHE GLU PRO VAL LEU ILE
SEQRES 35 D 1407 GLU GLY LYS ALA ILE GLN LEU HIS PRO LEU VAL CYS ALA
SEQRES 36 D 1407 ALA TYR ASN ALA ASP PHE ASP GLY ASP GLN MET ALA VAL
SEQRES 37 D 1407 HIS VAL PRO LEU THR LEU GLU ALA GLN LEU GLU ALA ARG
SEQRES 38 D 1407 ALA LEU MET MET SER THR ASN ASN ILE LEU SER PRO ALA
SEQRES 39 D 1407 ASN GLY GLU PRO ILE ILE VAL PRO SER GLN ASP VAL VAL
SEQRES 40 D 1407 LEU GLY LEU TYR TYR MET THR ARG ASP CYS VAL ASN ALA
SEQRES 41 D 1407 LYS GLY GLU GLY MET VAL LEU THR GLY PRO LYS GLU ALA
SEQRES 42 D 1407 GLU ARG LEU TYR ARG SER GLY LEU ALA SER LEU HIS ALA
SEQRES 43 D 1407 ARG VAL LYS VAL ARG ILE THR GLU TYR GLU LYS ASP ALA
SEQRES 44 D 1407 ASN GLY GLU LEU VAL ALA LYS THR SER LEU LYS ASP THR
SEQRES 45 D 1407 THR VAL GLY ARG ALA ILE LEU TRP MET ILE VAL PRO LYS
SEQRES 46 D 1407 GLY LEU PRO TYR SER ILE VAL ASN GLN ALA LEU GLY LYS
SEQRES 47 D 1407 LYS ALA ILE SER LYS MET LEU ASN THR CYS TYR ARG ILE
SEQRES 48 D 1407 LEU GLY LEU LYS PRO THR VAL ILE PHE ALA ASP GLN ILE
SEQRES 49 D 1407 MET TYR THR GLY PHE ALA TYR ALA ALA ARG SER GLY ALA
SEQRES 50 D 1407 SER VAL GLY ILE ASP ASP MET VAL ILE PRO GLU LYS LYS
SEQRES 51 D 1407 HIS GLU ILE ILE SER GLU ALA GLU ALA GLU VAL ALA GLU
SEQRES 52 D 1407 ILE GLN GLU GLN PHE GLN SER GLY LEU VAL THR ALA GLY
SEQRES 53 D 1407 GLU ARG TYR ASN LYS VAL ILE ASP ILE TRP ALA ALA ALA
SEQRES 54 D 1407 ASN ASP ARG VAL SER LYS ALA MET MET ASP ASN LEU GLN
SEQRES 55 D 1407 THR GLU THR VAL ILE ASN ARG ASP GLY GLN GLU GLU LYS
SEQRES 56 D 1407 GLN VAL SER PHE ASN SER ILE TYR MET MET ALA ASP SER
SEQRES 57 D 1407 GLY ALA ARG GLY SER ALA ALA GLN ILE ARG GLN LEU ALA
SEQRES 58 D 1407 GLY MET ARG GLY LEU MET ALA LYS PRO ASP GLY SER ILE
SEQRES 59 D 1407 ILE GLU THR PRO ILE THR ALA ASN PHE ARG GLU GLY LEU
SEQRES 60 D 1407 ASN VAL LEU GLN TYR PHE ILE SER THR HIS GLY ALA ARG
SEQRES 61 D 1407 LYS GLY LEU ALA ASP THR ALA LEU LYS THR ALA ASN SER
SEQRES 62 D 1407 GLY TYR LEU THR ARG ARG LEU VAL ASP VAL ALA GLN ASP
SEQRES 63 D 1407 LEU VAL VAL THR GLU ASP ASP CYS GLY THR HIS GLU GLY
SEQRES 64 D 1407 ILE MET MET THR PRO VAL ILE GLU GLY GLY ASP VAL LYS
SEQRES 65 D 1407 GLU PRO LEU ARG ASP ARG VAL LEU GLY ARG VAL THR ALA
SEQRES 66 D 1407 GLU ASP VAL LEU LYS PRO GLY THR ALA ASP ILE LEU VAL
SEQRES 67 D 1407 PRO ARG ASN THR LEU LEU HIS GLU GLN TRP CYS ASP LEU
SEQRES 68 D 1407 LEU GLU GLU ASN SER VAL ASP ALA VAL LYS VAL ARG SER
SEQRES 69 D 1407 VAL VAL SER CYS ASP THR ASP PHE GLY VAL CYS ALA HIS
SEQRES 70 D 1407 CYS TYR GLY ARG ASP LEU ALA ARG GLY HIS ILE ILE ASN
SEQRES 71 D 1407 LYS GLY GLU ALA ILE GLY VAL ILE ALA ALA GLN SER ILE
SEQRES 72 D 1407 GLY GLU PRO GLY THR GLN LEU THR MET ARG THR PHE HIS
SEQRES 73 D 1407 ILE GLY GLY ALA ALA SER ARG ALA ALA ALA GLU SER SER
SEQRES 74 D 1407 ILE GLN VAL LYS ASN LYS GLY SER ILE LYS LEU SER ASN
SEQRES 75 D 1407 VAL LYS SER VAL VAL ASN SER SER GLY LYS LEU VAL ILE
SEQRES 76 D 1407 THR SER ARG ASN THR GLU LEU LYS LEU ILE ASP GLU PHE
SEQRES 77 D 1407 GLY ARG THR LYS GLU SER TYR LYS VAL PRO TYR GLY ALA
SEQRES 78 D 1407 VAL LEU ALA LYS GLY ASP GLY GLU GLN VAL ALA GLY GLY
SEQRES 79 D 1407 GLU THR VAL ALA ASN TRP ASP PRO HIS THR MET PRO VAL
SEQRES 80 D 1407 ILE THR GLU VAL SER GLY PHE VAL ARG PHE THR ASP MET
SEQRES 81 D 1407 ILE ASP GLY GLN THR ILE THR ARG GLN THR ASP GLU LEU
SEQRES 82 D 1407 THR GLY LEU SER SER LEU VAL VAL LEU ASP SER ALA GLU
SEQRES 83 D 1407 ARG THR ALA GLY GLY LYS ASP LEU ARG PRO ALA LEU LYS
SEQRES 84 D 1407 ILE VAL ASP ALA GLN GLY ASN ASP VAL LEU ILE PRO GLY
SEQRES 85 D 1407 THR ASP MET PRO ALA GLN TYR PHE LEU PRO GLY LYS ALA
SEQRES 86 D 1407 ILE VAL GLN LEU GLU ASP GLY VAL GLN ILE SER SER GLY
SEQRES 87 D 1407 ASP THR LEU ALA ARG ILE PRO GLN GLU SER GLY GLY THR
SEQRES 88 D 1407 LYS ASP ILE THR GLY GLY LEU PRO ARG VAL ALA ASP LEU
SEQRES 89 D 1407 PHE GLU ALA ARG ARG PRO LYS GLU PRO ALA ILE LEU ALA
SEQRES 90 D 1407 GLU ILE SER GLY ILE VAL SER PHE GLY LYS GLU THR LYS
SEQRES 91 D 1407 GLY LYS ARG ARG LEU VAL ILE THR PRO VAL ASP GLY SER
SEQRES 92 D 1407 ASP PRO TYR GLU GLU MET ILE PRO LYS TRP ARG GLN LEU
SEQRES 93 D 1407 ASN VAL PHE GLU GLY GLU ARG VAL GLU ARG GLY ASP VAL
SEQRES 94 D 1407 ILE SER ASP GLY PRO GLU ALA PRO HIS ASP ILE LEU ARG
SEQRES 95 D 1407 LEU ARG GLY VAL HIS ALA VAL THR ARG TYR ILE VAL ASN
SEQRES 96 D 1407 GLU VAL GLN ASP VAL TYR ARG LEU GLN GLY VAL LYS ILE
SEQRES 97 D 1407 ASN ASP LYS HIS ILE GLU VAL ILE VAL ARG GLN MET LEU
SEQRES 98 D 1407 ARG LYS ALA THR ILE VAL ASN ALA GLY SER SER ASP PHE
SEQRES 99 D 1407 LEU GLU GLY GLU GLN VAL GLU TYR SER ARG VAL LYS ILE
SEQRES 100 D 1407 ALA ASN ARG GLU LEU GLU ALA ASN GLY LYS VAL GLY ALA
SEQRES 101 D 1407 THR TYR SER ARG ASP LEU LEU GLY ILE THR LYS ALA SER
SEQRES 102 D 1407 LEU ALA THR GLU SER PHE ILE SER ALA ALA SER PHE GLN
SEQRES 103 D 1407 GLU THR THR ARG VAL LEU THR GLU ALA ALA VAL ALA GLY
SEQRES 104 D 1407 LYS ARG ASP GLU LEU ARG GLY LEU LYS GLU ASN VAL ILE
SEQRES 105 D 1407 VAL GLY ARG LEU ILE PRO ALA GLY THR GLY TYR ALA TYR
SEQRES 106 D 1407 HIS GLN ASP ARG MET ARG ARG ARG ALA ALA GLY GLU ALA
SEQRES 107 D 1407 PRO ALA ALA PRO GLN VAL THR ALA GLU ASP ALA SER ALA
SEQRES 108 D 1407 SER LEU ALA GLU LEU LEU ASN ALA GLY LEU GLY GLY SER
SEQRES 109 D 1407 ASP ASN GLU
SEQRES 1 E 90 ALA ARG VAL THR VAL GLN ASP ALA VAL GLU LYS ILE GLY
SEQRES 2 E 90 ASN ARG PHE ASP LEU VAL LEU VAL ALA ALA ARG ARG ALA
SEQRES 3 E 90 ARG GLN MET GLN VAL GLY GLY LYS ASP PRO LEU VAL PRO
SEQRES 4 E 90 GLU GLU ASN ASP LYS THR THR VAL ILE ALA LEU ARG GLU
SEQRES 5 E 90 ILE GLU GLU GLY LEU ILE ASN ASN GLN ILE LEU ASP VAL
SEQRES 6 E 90 ARG GLU ARG GLN GLU GLN GLN GLU GLN GLU ALA ALA GLU
SEQRES 7 E 90 LEU GLN ALA VAL THR ALA ILE ALA GLU GLY ARG ARG
SEQRES 1 F 628 MET ARG GLY SER HIS HIS HIS HIS HIS HIS THR ASP GLN
SEQRES 2 F 628 PHE THR MET GLU GLN ASN PRO GLN SER GLN LEU LYS LEU
SEQRES 3 F 628 LEU VAL THR ARG GLY LYS GLU GLN GLY TYR LEU THR TYR
SEQRES 4 F 628 ALA GLU VAL ASN ASP HIS LEU PRO GLU ASP ILE VAL ASP
SEQRES 5 F 628 SER ASP GLN ILE GLU ASP ILE ILE GLN MET ILE ASN ASP
SEQRES 6 F 628 MET GLY ILE GLN VAL MET GLU GLU ALA PRO ASP ALA ASP
SEQRES 7 F 628 ASP LEU MET LEU ALA GLU ASN THR ALA ASP GLU ASP ALA
SEQRES 8 F 628 ALA GLU ALA ALA ALA GLN VAL LEU SER SER VAL GLU SER
SEQRES 9 F 628 GLU ILE GLY ARG THR THR ASP PRO VAL ARG MET TYR MET
SEQRES 10 F 628 ARG GLU MET GLY THR VAL GLU LEU LEU THR ARG GLU GLY
SEQRES 11 F 628 GLU ILE ASP ILE ALA LYS ARG ILE GLU ASP GLY ILE ASN
SEQRES 12 F 628 GLN VAL GLN CYS SER VAL ALA GLU TYR PRO GLU ALA ILE
SEQRES 13 F 628 THR TYR LEU LEU GLU GLN TYR ASP ARG VAL GLU ALA GLU
SEQRES 14 F 628 GLU ALA ARG LEU SER ASP LEU ILE THR GLY PHE VAL ASP
SEQRES 15 F 628 PRO ASN ALA GLU GLU ASP LEU ALA PRO THR ALA THR HIS
SEQRES 16 F 628 VAL GLY SER GLU LEU SER GLN GLU ASP LEU ASP ASP ASP
SEQRES 17 F 628 GLU ASP GLU ASP GLU GLU ASP GLY ASP ASP ASP SER ALA
SEQRES 18 F 628 ASP ASP ASP ASN SER ILE ASP PRO GLU LEU ALA ARG GLU
SEQRES 19 F 628 LYS PHE ALA GLU LEU ARG ALA GLN TYR VAL VAL THR ARG
SEQRES 20 F 628 ASP THR ILE LYS ALA LYS GLY ARG SER HIS ALA THR ALA
SEQRES 21 F 628 GLN GLU GLU ILE LEU LYS LEU SER GLU VAL PHE LYS GLN
SEQRES 22 F 628 PHE ARG LEU VAL PRO LYS GLN PHE ASP TYR LEU VAL ASN
SEQRES 23 F 628 SER MET ARG VAL MET MET ASP ARG VAL ARG THR GLN GLU
SEQRES 24 F 628 ARG LEU ILE MET LYS LEU CYS VAL GLU GLN CYS LYS MET
SEQRES 25 F 628 PRO LYS LYS ASN PHE ILE THR LEU PHE THR GLY ASN GLU
SEQRES 26 F 628 THR SER ASP THR TRP PHE ASN ALA ALA ILE ALA MET ASN
SEQRES 27 F 628 LYS PRO TRP SER GLU LYS LEU HIS ASP VAL SER GLU GLU
SEQRES 28 F 628 VAL HIS ARG ALA LEU GLN LYS LEU GLN GLN ILE GLU GLU
SEQRES 29 F 628 GLU THR GLY LEU THR ILE GLU GLN VAL LYS ASP ILE ASN
SEQRES 30 F 628 ARG ARG MET SER ILE GLY GLU ALA LYS ALA ARG ARG ALA
SEQRES 31 F 628 LYS LYS GLU MET VAL GLU ALA ASN LEU ARG LEU VAL ILE
SEQRES 32 F 628 SER ILE ALA LYS LYS TYR THR ASN ARG GLY LEU GLN PHE
SEQRES 33 F 628 LEU ASP LEU ILE GLN GLU GLY ASN ILE GLY LEU MET LYS
SEQRES 34 F 628 ALA VAL ASP LYS PHE GLU TYR ARG ARG GLY TYR LYS PHE
SEQRES 35 F 628 SER THR TYR ALA THR TRP TRP ILE ARG GLN ALA ILE THR
SEQRES 36 F 628 ARG SER ILE ALA ASP GLN ALA ARG THR ILE ARG ILE PRO
SEQRES 37 F 628 VAL HIS MET ILE GLU THR ILE ASN LYS LEU ASN ARG ILE
SEQRES 38 F 628 SER ARG GLN MET LEU GLN GLU MET GLY ARG GLU PRO THR
SEQRES 39 F 628 PRO GLU GLU LEU ALA GLU ARG MET LEU MET PRO GLU ASP
SEQRES 40 F 628 LYS ILE ARG LYS VAL LEU LYS ILE ALA LYS GLU PRO ILE
SEQRES 41 F 628 SER MET GLU THR PRO ILE GLY ASP ASP GLU ASP SER HIS
SEQRES 42 F 628 LEU GLY ASP PHE ILE GLU ASP THR THR LEU GLU LEU PRO
SEQRES 43 F 628 LEU ASP SER ALA THR THR GLU SER LEU ARG ALA ALA THR
SEQRES 44 F 628 HIS ASP VAL LEU ALA GLY LEU THR ALA ARG GLU ALA LYS
SEQRES 45 F 628 VAL LEU ARG MET ARG PHE GLY ILE ASP MET ASN THR ASP
SEQRES 46 F 628 TYR THR LEU GLU GLU VAL GLY LYS GLN PHE ASP VAL THR
SEQRES 47 F 628 ARG GLU ARG ILE ARG GLN ILE GLU ALA LYS ALA LEU ARG
SEQRES 48 F 628 LYS LEU ARG HIS PRO SER ARG SER GLU VAL LEU ARG SER
SEQRES 49 F 628 PHE LEU ASP ASP
SEQRES 1 1 49 DA DC DT DT DG DA DC DA DT DC DC DA DC
SEQRES 2 1 49 DC DT DC DA DC DG DT DA DT DG DC DT DA
SEQRES 3 1 49 DT DA DA DT DG DT DG DT DG DC DA DG DT
SEQRES 4 1 49 DC DT DG DA DC DG DC DG DG DC
SEQRES 1 2 49 DG DC DC DG DC DG DT DC DA DG DA DC DT
SEQRES 2 2 49 DC DG DT DA DG DG DA DT DT DA DT DA DG
SEQRES 3 2 49 DC DA DT DA DC DG DT DG DA DG DG DT DG
SEQRES 4 2 49 DG DA DT DG DT DC DA DA DG DT
SEQRES 1 3 5 GTP A G U C
SEQRES 1 G 242 ALA HIS HIS HIS HIS HIS HIS MET GLN GLY SER VAL THR
SEQRES 2 G 242 GLU PHE LEU LYS PRO ARG LEU VAL ASP ILE GLU GLN VAL
SEQRES 3 G 242 SER SER THR HIS ALA LYS VAL THR LEU GLU PRO LEU GLU
SEQRES 4 G 242 ARG GLY PHE GLY HIS THR LEU GLY ASN ALA LEU ARG ARG
SEQRES 5 G 242 ILE LEU LEU SER SER MET PRO GLY CYS ALA VAL THR GLU
SEQRES 6 G 242 VAL GLU ILE ASP GLY VAL LEU HIS GLU TYR SER THR LYS
SEQRES 7 G 242 GLU GLY VAL GLN GLU ASP ILE LEU GLU ILE LEU LEU ASN
SEQRES 8 G 242 LEU LYS GLY LEU ALA VAL ARG VAL GLN GLY LYS ASP GLU
SEQRES 9 G 242 VAL ILE LEU THR LEU ASN LYS SER GLY ILE GLY PRO VAL
SEQRES 10 G 242 THR ALA ALA ASP ILE THR HIS ASP GLY ASP VAL GLU ILE
SEQRES 11 G 242 VAL LYS PRO GLN HIS VAL ILE CYS HIS LEU THR ASP GLU
SEQRES 12 G 242 ASN ALA SER ILE SER MET ARG ILE LYS VAL GLN ARG GLY
SEQRES 13 G 242 ARG GLY TYR VAL PRO ALA SER THR ARG ILE HIS SER GLU
SEQRES 14 G 242 GLU ASP GLU ARG PRO ILE GLY ARG LEU LEU VAL ASP ALA
SEQRES 15 G 242 CYS TYR SER PRO VAL GLU ARG ILE ALA TYR ASN VAL GLU
SEQRES 16 G 242 ALA ALA ARG VAL GLU GLN ARG THR ASP LEU ASP LYS LEU
SEQRES 17 G 242 VAL ILE GLU MET GLU THR ASN GLY THR ILE ASP PRO GLU
SEQRES 18 G 242 GLU ALA ILE ARG ARG ALA ALA THR ILE LEU ALA GLU GLN
SEQRES 19 G 242 LEU GLU ALA PHE VAL ASP LEU ARG
SEQRES 1 H 242 ALA HIS HIS HIS HIS HIS HIS MET GLN GLY SER VAL THR
SEQRES 2 H 242 GLU PHE LEU LYS PRO ARG LEU VAL ASP ILE GLU GLN VAL
SEQRES 3 H 242 SER SER THR HIS ALA LYS VAL THR LEU GLU PRO LEU GLU
SEQRES 4 H 242 ARG GLY PHE GLY HIS THR LEU GLY ASN ALA LEU ARG ARG
SEQRES 5 H 242 ILE LEU LEU SER SER MET PRO GLY CYS ALA VAL THR GLU
SEQRES 6 H 242 VAL GLU ILE ASP GLY VAL LEU HIS GLU TYR SER THR LYS
SEQRES 7 H 242 GLU GLY VAL GLN GLU ASP ILE LEU GLU ILE LEU LEU ASN
SEQRES 8 H 242 LEU LYS GLY LEU ALA VAL ARG VAL GLN GLY LYS ASP GLU
SEQRES 9 H 242 VAL ILE LEU THR LEU ASN LYS SER GLY ILE GLY PRO VAL
SEQRES 10 H 242 THR ALA ALA ASP ILE THR HIS ASP GLY ASP VAL GLU ILE
SEQRES 11 H 242 VAL LYS PRO GLN HIS VAL ILE CYS HIS LEU THR ASP GLU
SEQRES 12 H 242 ASN ALA SER ILE SER MET ARG ILE LYS VAL GLN ARG GLY
SEQRES 13 H 242 ARG GLY TYR VAL PRO ALA SER THR ARG ILE HIS SER GLU
SEQRES 14 H 242 GLU ASP GLU ARG PRO ILE GLY ARG LEU LEU VAL ASP ALA
SEQRES 15 H 242 CYS TYR SER PRO VAL GLU ARG ILE ALA TYR ASN VAL GLU
SEQRES 16 H 242 ALA ALA ARG VAL GLU GLN ARG THR ASP LEU ASP LYS LEU
SEQRES 17 H 242 VAL ILE GLU MET GLU THR ASN GLY THR ILE ASP PRO GLU
SEQRES 18 H 242 GLU ALA ILE ARG ARG ALA ALA THR ILE LEU ALA GLU GLN
SEQRES 19 H 242 LEU GLU ALA PHE VAL ASP LEU ARG
SEQRES 1 I 1342 MET VAL TYR SER TYR THR GLU LYS LYS ARG ILE ARG LYS
SEQRES 2 I 1342 ASP PHE GLY LYS ARG PRO GLN VAL LEU ASP VAL PRO TYR
SEQRES 3 I 1342 LEU LEU SER ILE GLN LEU ASP SER PHE GLN LYS PHE ILE
SEQRES 4 I 1342 GLU GLN ASP PRO GLU GLY GLN TYR GLY LEU GLU ALA ALA
SEQRES 5 I 1342 PHE ARG SER VAL PHE PRO ILE GLN SER TYR SER GLY ASN
SEQRES 6 I 1342 SER GLU LEU GLN TYR VAL SER TYR ARG LEU GLY GLU PRO
SEQRES 7 I 1342 VAL PHE ASP VAL GLN GLU CYS GLN ILE ARG GLY VAL THR
SEQRES 8 I 1342 TYR SER ALA PRO LEU ARG VAL LYS LEU ARG LEU VAL ILE
SEQRES 9 I 1342 TYR GLU ARG GLU ALA PRO GLU GLY THR VAL LYS ASP ILE
SEQRES 10 I 1342 LYS GLU GLN GLU VAL TYR MET GLY GLU ILE PRO LEU MET
SEQRES 11 I 1342 THR ASP ASN GLY THR PHE VAL ILE ASN GLY THR GLU ARG
SEQRES 12 I 1342 VAL ILE VAL SER GLN LEU HIS ARG SER PRO GLY VAL PHE
SEQRES 13 I 1342 PHE ASP SER ASP LYS GLY LYS THR HIS SER SER GLY LYS
SEQRES 14 I 1342 VAL LEU TYR ASN ALA ARG ILE ILE PRO TYR ARG GLY SER
SEQRES 15 I 1342 TRP LEU ASP PHE GLU PHE ASP PRO LYS ASP ASN LEU PHE
SEQRES 16 I 1342 VAL ARG ILE ASP ARG ARG ARG LYS LEU PRO ALA THR ILE
SEQRES 17 I 1342 ILE LEU ARG ALA LEU ASN TYR THR THR GLU GLN ILE LEU
SEQRES 18 I 1342 ASP LEU PHE PHE GLU LYS VAL ILE PHE GLU ILE ARG ASP
SEQRES 19 I 1342 ASN LYS LEU GLN MET GLU LEU VAL PRO GLU ARG LEU ARG
SEQRES 20 I 1342 GLY GLU THR ALA SER PHE ASP ILE GLU ALA ASN GLY LYS
SEQRES 21 I 1342 VAL TYR VAL GLU LYS GLY ARG ARG ILE THR ALA ARG HIS
SEQRES 22 I 1342 ILE ARG GLN LEU GLU LYS ASP ASP VAL LYS LEU ILE GLU
SEQRES 23 I 1342 VAL PRO VAL GLU TYR ILE ALA GLY LYS VAL VAL ALA LYS
SEQRES 24 I 1342 ASP TYR ILE ASP GLU SER THR GLY GLU LEU ILE CYS ALA
SEQRES 25 I 1342 ALA ASN MET GLU LEU SER LEU ASP LEU LEU ALA LYS LEU
SEQRES 26 I 1342 SER GLN SER GLY HIS LYS ARG ILE GLU THR LEU PHE THR
SEQRES 27 I 1342 ASN ASP LEU ASP HIS GLY PRO TYR ILE SER GLU THR LEU
SEQRES 28 I 1342 ARG VAL ASP PRO THR ASN ASP ARG LEU SER ALA LEU VAL
SEQRES 29 I 1342 GLU ILE TYR ARG MET MET ARG PRO GLY GLU PRO PRO THR
SEQRES 30 I 1342 ARG GLU ALA ALA GLU SER LEU PHE GLU ASN LEU PHE PHE
SEQRES 31 I 1342 SER GLU ASP ARG TYR ASP LEU SER ALA VAL GLY ARG MET
SEQRES 32 I 1342 LYS PHE ASN ARG SER LEU LEU ARG GLU GLU ILE GLU GLY
SEQRES 33 I 1342 SER GLY ILE LEU SER LYS ASP ASP ILE ILE ASP VAL MET
SEQRES 34 I 1342 LYS LYS LEU ILE ASP ILE ARG ASN GLY LYS GLY GLU VAL
SEQRES 35 I 1342 ASP ASP ILE ASP HIS LEU GLY ASN ARG ARG ILE ARG SER
SEQRES 36 I 1342 VAL GLY GLU MET ALA GLU ASN GLN PHE ARG VAL GLY LEU
SEQRES 37 I 1342 VAL ARG VAL GLU ARG ALA VAL LYS GLU ARG LEU SER LEU
SEQRES 38 I 1342 GLY ASP LEU ASP THR LEU MET PRO GLN ASP MET ILE ASN
SEQRES 39 I 1342 ALA LYS PRO ILE SER ALA ALA VAL LYS GLU PHE PHE GLY
SEQRES 40 I 1342 SER SER GLN LEU SER GLN PHE MET ASP GLN ASN ASN PRO
SEQRES 41 I 1342 LEU SER GLU ILE THR HIS LYS ARG ARG ILE SER ALA LEU
SEQRES 42 I 1342 GLY PRO GLY GLY LEU THR ARG GLU ARG ALA GLY PHE GLU
SEQRES 43 I 1342 VAL ARG ASP VAL HIS PRO THR HIS TYR GLY ARG VAL CYS
SEQRES 44 I 1342 PRO ILE GLU THR PRO GLU GLY PRO ASN ILE GLY LEU ILE
SEQRES 45 I 1342 ASN SER LEU SER VAL TYR ALA GLN THR ASN GLU TYR GLY
SEQRES 46 I 1342 PHE LEU GLU THR PRO TYR ARG LYS VAL THR ASP GLY VAL
SEQRES 47 I 1342 VAL THR ASP GLU ILE HIS TYR LEU SER ALA ILE GLU GLU
SEQRES 48 I 1342 GLY ASN TYR VAL ILE ALA GLN ALA ASN SER ASN LEU ASP
SEQRES 49 I 1342 GLU GLU GLY HIS PHE VAL GLU ASP LEU VAL THR CYS ARG
SEQRES 50 I 1342 SER LYS GLY GLU SER SER LEU PHE SER ARG ASP GLN VAL
SEQRES 51 I 1342 ASP TYR MET ASP VAL SER THR GLN GLN VAL VAL SER VAL
SEQRES 52 I 1342 GLY ALA SER LEU ILE PRO PHE LEU GLU HIS ASP ASP ALA
SEQRES 53 I 1342 ASN ARG ALA LEU MET GLY ALA ASN MET GLN ARG GLN ALA
SEQRES 54 I 1342 VAL PRO THR LEU ARG ALA ASP LYS PRO LEU VAL GLY THR
SEQRES 55 I 1342 GLY MET GLU ARG ALA VAL ALA VAL ASP SER GLY VAL THR
SEQRES 56 I 1342 ALA VAL ALA LYS ARG GLY GLY VAL VAL GLN TYR VAL ASP
SEQRES 57 I 1342 ALA SER ARG ILE VAL ILE LYS VAL ASN GLU ASP GLU MET
SEQRES 58 I 1342 TYR PRO GLY GLU ALA GLY ILE ASP ILE TYR ASN LEU THR
SEQRES 59 I 1342 LYS TYR THR ARG SER ASN GLN ASN THR CYS ILE ASN GLN
SEQRES 60 I 1342 MET PRO CYS VAL SER LEU GLY GLU PRO VAL GLU ARG GLY
SEQRES 61 I 1342 ASP VAL LEU ALA ASP GLY PRO SER THR ASP LEU GLY GLU
SEQRES 62 I 1342 LEU ALA LEU GLY GLN ASN MET ARG VAL ALA PHE MET PRO
SEQRES 63 I 1342 TRP ASN GLY TYR ASN PHE GLU ASP SER ILE LEU VAL SER
SEQRES 64 I 1342 GLU ARG VAL VAL GLN GLU ASP ARG PHE THR THR ILE HIS
SEQRES 65 I 1342 ILE GLN GLU LEU ALA CYS VAL SER ARG ASP THR LYS LEU
SEQRES 66 I 1342 GLY PRO GLU GLU ILE THR ALA ASP ILE PRO ASN VAL GLY
SEQRES 67 I 1342 GLU ALA ALA LEU SER LYS LEU ASP GLU SER GLY ILE VAL
SEQRES 68 I 1342 TYR ILE GLY ALA GLU VAL THR GLY GLY ASP ILE LEU VAL
SEQRES 69 I 1342 GLY LYS VAL THR PRO LYS GLY GLU THR GLN LEU THR PRO
SEQRES 70 I 1342 GLU GLU LYS LEU LEU ARG ALA ILE PHE GLY GLU LYS ALA
SEQRES 71 I 1342 SER ASP VAL LYS ASP SER SER LEU ARG VAL PRO ASN GLY
SEQRES 72 I 1342 VAL SER GLY THR VAL ILE ASP VAL GLN VAL PHE THR ARG
SEQRES 73 I 1342 ASP GLY VAL GLU LYS ASP LYS ARG ALA LEU GLU ILE GLU
SEQRES 74 I 1342 GLU MET GLN LEU LYS GLN ALA LYS LYS ASP LEU SER GLU
SEQRES 75 I 1342 GLU LEU GLN ILE LEU GLU ALA GLY LEU PHE SER ARG ILE
SEQRES 76 I 1342 ARG ALA VAL LEU VAL ALA GLY GLY VAL GLU ALA GLU LYS
SEQRES 77 I 1342 LEU ASP LYS LEU PRO ARG ASP ARG TRP LEU GLU LEU GLY
SEQRES 78 I 1342 LEU THR ASP GLU GLU LYS GLN ASN GLN LEU GLU GLN LEU
SEQRES 79 I 1342 ALA GLU GLN TYR ASP GLU LEU LYS HIS GLU PHE GLU LYS
SEQRES 80 I 1342 LYS LEU GLU ALA LYS ARG ARG LYS ILE THR GLN GLY ASP
SEQRES 81 I 1342 ASP LEU ALA PRO GLY VAL LEU LYS ILE VAL LYS VAL TYR
SEQRES 82 I 1342 LEU ALA VAL LYS ARG ARG ILE GLN PRO GLY ASP LYS MET
SEQRES 83 I 1342 ALA GLY ARG HIS GLY ASN LYS GLY VAL ILE SER LYS ILE
SEQRES 84 I 1342 ASN PRO ILE GLU ASP MET PRO TYR ASP GLU ASN GLY THR
SEQRES 85 I 1342 PRO VAL ASP ILE VAL LEU ASN PRO LEU GLY VAL PRO SER
SEQRES 86 I 1342 ARG MET ASN ILE GLY GLN ILE LEU GLU THR HIS LEU GLY
SEQRES 87 I 1342 MET ALA ALA LYS GLY ILE GLY ASP LYS ILE ASN ALA MET
SEQRES 88 I 1342 LEU LYS GLN GLN GLN GLU VAL ALA LYS LEU ARG GLU PHE
SEQRES 89 I 1342 ILE GLN ARG ALA TYR ASP LEU GLY ALA ASP VAL ARG GLN
SEQRES 90 I 1342 LYS VAL ASP LEU SER THR PHE SER ASP GLU GLU VAL MET
SEQRES 91 I 1342 ARG LEU ALA GLU ASN LEU ARG LYS GLY MET PRO ILE ALA
SEQRES 92 I 1342 THR PRO VAL PHE ASP GLY ALA LYS GLU ALA GLU ILE LYS
SEQRES 93 I 1342 GLU LEU LEU LYS LEU GLY ASP LEU PRO THR SER GLY GLN
SEQRES 94 I 1342 ILE ARG LEU TYR ASP GLY ARG THR GLY GLU GLN PHE GLU
SEQRES 95 I 1342 ARG PRO VAL THR VAL GLY TYR MET TYR MET LEU LYS LEU
SEQRES 96 I 1342 ASN HIS LEU VAL ASP ASP LYS MET HIS ALA ARG SER THR
SEQRES 97 I 1342 GLY SER TYR SER LEU VAL THR GLN GLN PRO LEU GLY GLY
SEQRES 98 I 1342 LYS ALA GLN PHE GLY GLY GLN ARG PHE GLY GLU MET GLU
SEQRES 99 I 1342 VAL TRP ALA LEU GLU ALA TYR GLY ALA ALA TYR THR LEU
SEQRES 100 I 1342 GLN GLU MET LEU THR VAL LYS SER ASP ASP VAL ASN GLY
SEQRES 101 I 1342 ARG THR LYS MET TYR LYS ASN ILE VAL ASP GLY ASN HIS
SEQRES 102 I 1342 GLN MET GLU PRO GLY MET PRO GLU SER PHE ASN VAL LEU
SEQRES 103 I 1342 LEU LYS GLU ILE ARG SER LEU GLY ILE ASN ILE GLU LEU
SEQRES 104 I 1342 GLU ASP GLU
SEQRES 1 J 1407 MET LYS ASP LEU LEU LYS PHE LEU LYS ALA GLN THR LYS
SEQRES 2 J 1407 THR GLU GLU PHE ASP ALA ILE LYS ILE ALA LEU ALA SER
SEQRES 3 J 1407 PRO ASP MET ILE ARG SER TRP SER PHE GLY GLU VAL LYS
SEQRES 4 J 1407 LYS PRO GLU THR ILE ASN TYR ARG THR PHE LYS PRO GLU
SEQRES 5 J 1407 ARG ASP GLY LEU PHE CYS ALA ARG ILE PHE GLY PRO VAL
SEQRES 6 J 1407 LYS ASP TYR GLU CYS LEU CYS GLY LYS TYR LYS ARG LEU
SEQRES 7 J 1407 LYS HIS ARG GLY VAL ILE CYS GLU LYS CYS GLY VAL GLU
SEQRES 8 J 1407 VAL THR GLN THR LYS VAL ARG ARG GLU ARG MET GLY HIS
SEQRES 9 J 1407 ILE GLU LEU ALA SER PRO THR ALA HIS ILE TRP PHE LEU
SEQRES 10 J 1407 LYS SER LEU PRO SER ARG ILE GLY LEU LEU LEU ASP MET
SEQRES 11 J 1407 PRO LEU ARG ASP ILE GLU ARG VAL LEU TYR PHE GLU SER
SEQRES 12 J 1407 TYR VAL VAL ILE GLU GLY GLY MET THR ASN LEU GLU ARG
SEQRES 13 J 1407 GLN GLN ILE LEU THR GLU GLU GLN TYR LEU ASP ALA LEU
SEQRES 14 J 1407 GLU GLU PHE GLY ASP GLU PHE ASP ALA LYS MET GLY ALA
SEQRES 15 J 1407 GLU ALA ILE GLN ALA LEU LEU LYS SER MET ASP LEU GLU
SEQRES 16 J 1407 GLN GLU CYS GLU GLN LEU ARG GLU GLU LEU ASN GLU THR
SEQRES 17 J 1407 ASN SER GLU THR LYS ARG LYS LYS LEU THR LYS ARG ILE
SEQRES 18 J 1407 LYS LEU LEU GLU ALA PHE VAL GLN SER GLY ASN LYS PRO
SEQRES 19 J 1407 GLU TRP MET ILE LEU THR VAL LEU PRO VAL LEU PRO PRO
SEQRES 20 J 1407 ASP LEU ARG PRO LEU VAL PRO LEU ASP GLY GLY ARG PHE
SEQRES 21 J 1407 ALA THR SER ASP LEU ASN ASP LEU TYR ARG ARG VAL ILE
SEQRES 22 J 1407 ASN ARG ASN ASN ARG LEU LYS ARG LEU LEU ASP LEU ALA
SEQRES 23 J 1407 ALA PRO ASP ILE ILE VAL ARG ASN GLU LYS ARG MET LEU
SEQRES 24 J 1407 GLN GLU ALA VAL ASP ALA LEU LEU ASP ASN GLY ARG ARG
SEQRES 25 J 1407 GLY ARG ALA ILE THR GLY SER ASN LYS ARG PRO LEU LYS
SEQRES 26 J 1407 SER LEU ALA ASP MET ILE LYS GLY LYS GLN GLY ARG PHE
SEQRES 27 J 1407 ARG GLN ASN LEU LEU GLY LYS ARG VAL ASP TYR SER GLY
SEQRES 28 J 1407 ARG SER VAL ILE THR VAL GLY PRO TYR LEU ARG LEU HIS
SEQRES 29 J 1407 GLN CYS GLY LEU PRO LYS LYS MET ALA LEU GLU LEU PHE
SEQRES 30 J 1407 LYS PRO PHE ILE TYR GLY LYS LEU GLU LEU ARG GLY LEU
SEQRES 31 J 1407 ALA THR THR ILE LYS ALA ALA LYS LYS MET VAL GLU ARG
SEQRES 32 J 1407 GLU GLU ALA VAL VAL TRP ASP ILE LEU ASP GLU VAL ILE
SEQRES 33 J 1407 ARG GLU HIS PRO VAL LEU LEU ASN ARG ALA PRO THR LEU
SEQRES 34 J 1407 HIS ARG LEU GLY ILE GLN ALA PHE GLU PRO VAL LEU ILE
SEQRES 35 J 1407 GLU GLY LYS ALA ILE GLN LEU HIS PRO LEU VAL CYS ALA
SEQRES 36 J 1407 ALA TYR ASN ALA ASP PHE ASP GLY ASP GLN MET ALA VAL
SEQRES 37 J 1407 HIS VAL PRO LEU THR LEU GLU ALA GLN LEU GLU ALA ARG
SEQRES 38 J 1407 ALA LEU MET MET SER THR ASN ASN ILE LEU SER PRO ALA
SEQRES 39 J 1407 ASN GLY GLU PRO ILE ILE VAL PRO SER GLN ASP VAL VAL
SEQRES 40 J 1407 LEU GLY LEU TYR TYR MET THR ARG ASP CYS VAL ASN ALA
SEQRES 41 J 1407 LYS GLY GLU GLY MET VAL LEU THR GLY PRO LYS GLU ALA
SEQRES 42 J 1407 GLU ARG LEU TYR ARG SER GLY LEU ALA SER LEU HIS ALA
SEQRES 43 J 1407 ARG VAL LYS VAL ARG ILE THR GLU TYR GLU LYS ASP ALA
SEQRES 44 J 1407 ASN GLY GLU LEU VAL ALA LYS THR SER LEU LYS ASP THR
SEQRES 45 J 1407 THR VAL GLY ARG ALA ILE LEU TRP MET ILE VAL PRO LYS
SEQRES 46 J 1407 GLY LEU PRO TYR SER ILE VAL ASN GLN ALA LEU GLY LYS
SEQRES 47 J 1407 LYS ALA ILE SER LYS MET LEU ASN THR CYS TYR ARG ILE
SEQRES 48 J 1407 LEU GLY LEU LYS PRO THR VAL ILE PHE ALA ASP GLN ILE
SEQRES 49 J 1407 MET TYR THR GLY PHE ALA TYR ALA ALA ARG SER GLY ALA
SEQRES 50 J 1407 SER VAL GLY ILE ASP ASP MET VAL ILE PRO GLU LYS LYS
SEQRES 51 J 1407 HIS GLU ILE ILE SER GLU ALA GLU ALA GLU VAL ALA GLU
SEQRES 52 J 1407 ILE GLN GLU GLN PHE GLN SER GLY LEU VAL THR ALA GLY
SEQRES 53 J 1407 GLU ARG TYR ASN LYS VAL ILE ASP ILE TRP ALA ALA ALA
SEQRES 54 J 1407 ASN ASP ARG VAL SER LYS ALA MET MET ASP ASN LEU GLN
SEQRES 55 J 1407 THR GLU THR VAL ILE ASN ARG ASP GLY GLN GLU GLU LYS
SEQRES 56 J 1407 GLN VAL SER PHE ASN SER ILE TYR MET MET ALA ASP SER
SEQRES 57 J 1407 GLY ALA ARG GLY SER ALA ALA GLN ILE ARG GLN LEU ALA
SEQRES 58 J 1407 GLY MET ARG GLY LEU MET ALA LYS PRO ASP GLY SER ILE
SEQRES 59 J 1407 ILE GLU THR PRO ILE THR ALA ASN PHE ARG GLU GLY LEU
SEQRES 60 J 1407 ASN VAL LEU GLN TYR PHE ILE SER THR HIS GLY ALA ARG
SEQRES 61 J 1407 LYS GLY LEU ALA ASP THR ALA LEU LYS THR ALA ASN SER
SEQRES 62 J 1407 GLY TYR LEU THR ARG ARG LEU VAL ASP VAL ALA GLN ASP
SEQRES 63 J 1407 LEU VAL VAL THR GLU ASP ASP CYS GLY THR HIS GLU GLY
SEQRES 64 J 1407 ILE MET MET THR PRO VAL ILE GLU GLY GLY ASP VAL LYS
SEQRES 65 J 1407 GLU PRO LEU ARG ASP ARG VAL LEU GLY ARG VAL THR ALA
SEQRES 66 J 1407 GLU ASP VAL LEU LYS PRO GLY THR ALA ASP ILE LEU VAL
SEQRES 67 J 1407 PRO ARG ASN THR LEU LEU HIS GLU GLN TRP CYS ASP LEU
SEQRES 68 J 1407 LEU GLU GLU ASN SER VAL ASP ALA VAL LYS VAL ARG SER
SEQRES 69 J 1407 VAL VAL SER CYS ASP THR ASP PHE GLY VAL CYS ALA HIS
SEQRES 70 J 1407 CYS TYR GLY ARG ASP LEU ALA ARG GLY HIS ILE ILE ASN
SEQRES 71 J 1407 LYS GLY GLU ALA ILE GLY VAL ILE ALA ALA GLN SER ILE
SEQRES 72 J 1407 GLY GLU PRO GLY THR GLN LEU THR MET ARG THR PHE HIS
SEQRES 73 J 1407 ILE GLY GLY ALA ALA SER ARG ALA ALA ALA GLU SER SER
SEQRES 74 J 1407 ILE GLN VAL LYS ASN LYS GLY SER ILE LYS LEU SER ASN
SEQRES 75 J 1407 VAL LYS SER VAL VAL ASN SER SER GLY LYS LEU VAL ILE
SEQRES 76 J 1407 THR SER ARG ASN THR GLU LEU LYS LEU ILE ASP GLU PHE
SEQRES 77 J 1407 GLY ARG THR LYS GLU SER TYR LYS VAL PRO TYR GLY ALA
SEQRES 78 J 1407 VAL LEU ALA LYS GLY ASP GLY GLU GLN VAL ALA GLY GLY
SEQRES 79 J 1407 GLU THR VAL ALA ASN TRP ASP PRO HIS THR MET PRO VAL
SEQRES 80 J 1407 ILE THR GLU VAL SER GLY PHE VAL ARG PHE THR ASP MET
SEQRES 81 J 1407 ILE ASP GLY GLN THR ILE THR ARG GLN THR ASP GLU LEU
SEQRES 82 J 1407 THR GLY LEU SER SER LEU VAL VAL LEU ASP SER ALA GLU
SEQRES 83 J 1407 ARG THR ALA GLY GLY LYS ASP LEU ARG PRO ALA LEU LYS
SEQRES 84 J 1407 ILE VAL ASP ALA GLN GLY ASN ASP VAL LEU ILE PRO GLY
SEQRES 85 J 1407 THR ASP MET PRO ALA GLN TYR PHE LEU PRO GLY LYS ALA
SEQRES 86 J 1407 ILE VAL GLN LEU GLU ASP GLY VAL GLN ILE SER SER GLY
SEQRES 87 J 1407 ASP THR LEU ALA ARG ILE PRO GLN GLU SER GLY GLY THR
SEQRES 88 J 1407 LYS ASP ILE THR GLY GLY LEU PRO ARG VAL ALA ASP LEU
SEQRES 89 J 1407 PHE GLU ALA ARG ARG PRO LYS GLU PRO ALA ILE LEU ALA
SEQRES 90 J 1407 GLU ILE SER GLY ILE VAL SER PHE GLY LYS GLU THR LYS
SEQRES 91 J 1407 GLY LYS ARG ARG LEU VAL ILE THR PRO VAL ASP GLY SER
SEQRES 92 J 1407 ASP PRO TYR GLU GLU MET ILE PRO LYS TRP ARG GLN LEU
SEQRES 93 J 1407 ASN VAL PHE GLU GLY GLU ARG VAL GLU ARG GLY ASP VAL
SEQRES 94 J 1407 ILE SER ASP GLY PRO GLU ALA PRO HIS ASP ILE LEU ARG
SEQRES 95 J 1407 LEU ARG GLY VAL HIS ALA VAL THR ARG TYR ILE VAL ASN
SEQRES 96 J 1407 GLU VAL GLN ASP VAL TYR ARG LEU GLN GLY VAL LYS ILE
SEQRES 97 J 1407 ASN ASP LYS HIS ILE GLU VAL ILE VAL ARG GLN MET LEU
SEQRES 98 J 1407 ARG LYS ALA THR ILE VAL ASN ALA GLY SER SER ASP PHE
SEQRES 99 J 1407 LEU GLU GLY GLU GLN VAL GLU TYR SER ARG VAL LYS ILE
SEQRES 100 J 1407 ALA ASN ARG GLU LEU GLU ALA ASN GLY LYS VAL GLY ALA
SEQRES 101 J 1407 THR TYR SER ARG ASP LEU LEU GLY ILE THR LYS ALA SER
SEQRES 102 J 1407 LEU ALA THR GLU SER PHE ILE SER ALA ALA SER PHE GLN
SEQRES 103 J 1407 GLU THR THR ARG VAL LEU THR GLU ALA ALA VAL ALA GLY
SEQRES 104 J 1407 LYS ARG ASP GLU LEU ARG GLY LEU LYS GLU ASN VAL ILE
SEQRES 105 J 1407 VAL GLY ARG LEU ILE PRO ALA GLY THR GLY TYR ALA TYR
SEQRES 106 J 1407 HIS GLN ASP ARG MET ARG ARG ARG ALA ALA GLY GLU ALA
SEQRES 107 J 1407 PRO ALA ALA PRO GLN VAL THR ALA GLU ASP ALA SER ALA
SEQRES 108 J 1407 SER LEU ALA GLU LEU LEU ASN ALA GLY LEU GLY GLY SER
SEQRES 109 J 1407 ASP ASN GLU
SEQRES 1 K 90 ALA ARG VAL THR VAL GLN ASP ALA VAL GLU LYS ILE GLY
SEQRES 2 K 90 ASN ARG PHE ASP LEU VAL LEU VAL ALA ALA ARG ARG ALA
SEQRES 3 K 90 ARG GLN MET GLN VAL GLY GLY LYS ASP PRO LEU VAL PRO
SEQRES 4 K 90 GLU GLU ASN ASP LYS THR THR VAL ILE ALA LEU ARG GLU
SEQRES 5 K 90 ILE GLU GLU GLY LEU ILE ASN ASN GLN ILE LEU ASP VAL
SEQRES 6 K 90 ARG GLU ARG GLN GLU GLN GLN GLU GLN GLU ALA ALA GLU
SEQRES 7 K 90 LEU GLN ALA VAL THR ALA ILE ALA GLU GLY ARG ARG
SEQRES 1 L 628 MET ARG GLY SER HIS HIS HIS HIS HIS HIS THR ASP GLN
SEQRES 2 L 628 PHE THR MET GLU GLN ASN PRO GLN SER GLN LEU LYS LEU
SEQRES 3 L 628 LEU VAL THR ARG GLY LYS GLU GLN GLY TYR LEU THR TYR
SEQRES 4 L 628 ALA GLU VAL ASN ASP HIS LEU PRO GLU ASP ILE VAL ASP
SEQRES 5 L 628 SER ASP GLN ILE GLU ASP ILE ILE GLN MET ILE ASN ASP
SEQRES 6 L 628 MET GLY ILE GLN VAL MET GLU GLU ALA PRO ASP ALA ASP
SEQRES 7 L 628 ASP LEU MET LEU ALA GLU ASN THR ALA ASP GLU ASP ALA
SEQRES 8 L 628 ALA GLU ALA ALA ALA GLN VAL LEU SER SER VAL GLU SER
SEQRES 9 L 628 GLU ILE GLY ARG THR THR ASP PRO VAL ARG MET TYR MET
SEQRES 10 L 628 ARG GLU MET GLY THR VAL GLU LEU LEU THR ARG GLU GLY
SEQRES 11 L 628 GLU ILE ASP ILE ALA LYS ARG ILE GLU ASP GLY ILE ASN
SEQRES 12 L 628 GLN VAL GLN CYS SER VAL ALA GLU TYR PRO GLU ALA ILE
SEQRES 13 L 628 THR TYR LEU LEU GLU GLN TYR ASP ARG VAL GLU ALA GLU
SEQRES 14 L 628 GLU ALA ARG LEU SER ASP LEU ILE THR GLY PHE VAL ASP
SEQRES 15 L 628 PRO ASN ALA GLU GLU ASP LEU ALA PRO THR ALA THR HIS
SEQRES 16 L 628 VAL GLY SER GLU LEU SER GLN GLU ASP LEU ASP ASP ASP
SEQRES 17 L 628 GLU ASP GLU ASP GLU GLU ASP GLY ASP ASP ASP SER ALA
SEQRES 18 L 628 ASP ASP ASP ASN SER ILE ASP PRO GLU LEU ALA ARG GLU
SEQRES 19 L 628 LYS PHE ALA GLU LEU ARG ALA GLN TYR VAL VAL THR ARG
SEQRES 20 L 628 ASP THR ILE LYS ALA LYS GLY ARG SER HIS ALA THR ALA
SEQRES 21 L 628 GLN GLU GLU ILE LEU LYS LEU SER GLU VAL PHE LYS GLN
SEQRES 22 L 628 PHE ARG LEU VAL PRO LYS GLN PHE ASP TYR LEU VAL ASN
SEQRES 23 L 628 SER MET ARG VAL MET MET ASP ARG VAL ARG THR GLN GLU
SEQRES 24 L 628 ARG LEU ILE MET LYS LEU CYS VAL GLU GLN CYS LYS MET
SEQRES 25 L 628 PRO LYS LYS ASN PHE ILE THR LEU PHE THR GLY ASN GLU
SEQRES 26 L 628 THR SER ASP THR TRP PHE ASN ALA ALA ILE ALA MET ASN
SEQRES 27 L 628 LYS PRO TRP SER GLU LYS LEU HIS ASP VAL SER GLU GLU
SEQRES 28 L 628 VAL HIS ARG ALA LEU GLN LYS LEU GLN GLN ILE GLU GLU
SEQRES 29 L 628 GLU THR GLY LEU THR ILE GLU GLN VAL LYS ASP ILE ASN
SEQRES 30 L 628 ARG ARG MET SER ILE GLY GLU ALA LYS ALA ARG ARG ALA
SEQRES 31 L 628 LYS LYS GLU MET VAL GLU ALA ASN LEU ARG LEU VAL ILE
SEQRES 32 L 628 SER ILE ALA LYS LYS TYR THR ASN ARG GLY LEU GLN PHE
SEQRES 33 L 628 LEU ASP LEU ILE GLN GLU GLY ASN ILE GLY LEU MET LYS
SEQRES 34 L 628 ALA VAL ASP LYS PHE GLU TYR ARG ARG GLY TYR LYS PHE
SEQRES 35 L 628 SER THR TYR ALA THR TRP TRP ILE ARG GLN ALA ILE THR
SEQRES 36 L 628 ARG SER ILE ALA ASP GLN ALA ARG THR ILE ARG ILE PRO
SEQRES 37 L 628 VAL HIS MET ILE GLU THR ILE ASN LYS LEU ASN ARG ILE
SEQRES 38 L 628 SER ARG GLN MET LEU GLN GLU MET GLY ARG GLU PRO THR
SEQRES 39 L 628 PRO GLU GLU LEU ALA GLU ARG MET LEU MET PRO GLU ASP
SEQRES 40 L 628 LYS ILE ARG LYS VAL LEU LYS ILE ALA LYS GLU PRO ILE
SEQRES 41 L 628 SER MET GLU THR PRO ILE GLY ASP ASP GLU ASP SER HIS
SEQRES 42 L 628 LEU GLY ASP PHE ILE GLU ASP THR THR LEU GLU LEU PRO
SEQRES 43 L 628 LEU ASP SER ALA THR THR GLU SER LEU ARG ALA ALA THR
SEQRES 44 L 628 HIS ASP VAL LEU ALA GLY LEU THR ALA ARG GLU ALA LYS
SEQRES 45 L 628 VAL LEU ARG MET ARG PHE GLY ILE ASP MET ASN THR ASP
SEQRES 46 L 628 TYR THR LEU GLU GLU VAL GLY LYS GLN PHE ASP VAL THR
SEQRES 47 L 628 ARG GLU ARG ILE ARG GLN ILE GLU ALA LYS ALA LEU ARG
SEQRES 48 L 628 LYS LEU ARG HIS PRO SER ARG SER GLU VAL LEU ARG SER
SEQRES 49 L 628 PHE LEU ASP ASP
SEQRES 1 4 49 DA DC DT DT DG DA DC DA DT DC DC DA DC
SEQRES 2 4 49 DC DT DC DA DC DG DT DA DT DG DC DT DA
SEQRES 3 4 49 DT DA DA DT DG DT DG DT DG DC DA DG DT
SEQRES 4 4 49 DC DT DG DA DC DG DC DG DG DC
SEQRES 1 5 49 DG DC DC DG DC DG DT DC DA DG DA DC DT
SEQRES 2 5 49 DC DG DT DA DG DG DA DT DT DA DT DA DG
SEQRES 3 5 49 DC DA DT DA DC DG DT DG DA DG DG DT DG
SEQRES 4 5 49 DG DA DT DG DT DC DA DA DG DT
SEQRES 1 6 5 GTP A G U C
SEQRES 1 M 242 ALA HIS HIS HIS HIS HIS HIS MET GLN GLY SER VAL THR
SEQRES 2 M 242 GLU PHE LEU LYS PRO ARG LEU VAL ASP ILE GLU GLN VAL
SEQRES 3 M 242 SER SER THR HIS ALA LYS VAL THR LEU GLU PRO LEU GLU
SEQRES 4 M 242 ARG GLY PHE GLY HIS THR LEU GLY ASN ALA LEU ARG ARG
SEQRES 5 M 242 ILE LEU LEU SER SER MET PRO GLY CYS ALA VAL THR GLU
SEQRES 6 M 242 VAL GLU ILE ASP GLY VAL LEU HIS GLU TYR SER THR LYS
SEQRES 7 M 242 GLU GLY VAL GLN GLU ASP ILE LEU GLU ILE LEU LEU ASN
SEQRES 8 M 242 LEU LYS GLY LEU ALA VAL ARG VAL GLN GLY LYS ASP GLU
SEQRES 9 M 242 VAL ILE LEU THR LEU ASN LYS SER GLY ILE GLY PRO VAL
SEQRES 10 M 242 THR ALA ALA ASP ILE THR HIS ASP GLY ASP VAL GLU ILE
SEQRES 11 M 242 VAL LYS PRO GLN HIS VAL ILE CYS HIS LEU THR ASP GLU
SEQRES 12 M 242 ASN ALA SER ILE SER MET ARG ILE LYS VAL GLN ARG GLY
SEQRES 13 M 242 ARG GLY TYR VAL PRO ALA SER THR ARG ILE HIS SER GLU
SEQRES 14 M 242 GLU ASP GLU ARG PRO ILE GLY ARG LEU LEU VAL ASP ALA
SEQRES 15 M 242 CYS TYR SER PRO VAL GLU ARG ILE ALA TYR ASN VAL GLU
SEQRES 16 M 242 ALA ALA ARG VAL GLU GLN ARG THR ASP LEU ASP LYS LEU
SEQRES 17 M 242 VAL ILE GLU MET GLU THR ASN GLY THR ILE ASP PRO GLU
SEQRES 18 M 242 GLU ALA ILE ARG ARG ALA ALA THR ILE LEU ALA GLU GLN
SEQRES 19 M 242 LEU GLU ALA PHE VAL ASP LEU ARG
SEQRES 1 N 242 ALA HIS HIS HIS HIS HIS HIS MET GLN GLY SER VAL THR
SEQRES 2 N 242 GLU PHE LEU LYS PRO ARG LEU VAL ASP ILE GLU GLN VAL
SEQRES 3 N 242 SER SER THR HIS ALA LYS VAL THR LEU GLU PRO LEU GLU
SEQRES 4 N 242 ARG GLY PHE GLY HIS THR LEU GLY ASN ALA LEU ARG ARG
SEQRES 5 N 242 ILE LEU LEU SER SER MET PRO GLY CYS ALA VAL THR GLU
SEQRES 6 N 242 VAL GLU ILE ASP GLY VAL LEU HIS GLU TYR SER THR LYS
SEQRES 7 N 242 GLU GLY VAL GLN GLU ASP ILE LEU GLU ILE LEU LEU ASN
SEQRES 8 N 242 LEU LYS GLY LEU ALA VAL ARG VAL GLN GLY LYS ASP GLU
SEQRES 9 N 242 VAL ILE LEU THR LEU ASN LYS SER GLY ILE GLY PRO VAL
SEQRES 10 N 242 THR ALA ALA ASP ILE THR HIS ASP GLY ASP VAL GLU ILE
SEQRES 11 N 242 VAL LYS PRO GLN HIS VAL ILE CYS HIS LEU THR ASP GLU
SEQRES 12 N 242 ASN ALA SER ILE SER MET ARG ILE LYS VAL GLN ARG GLY
SEQRES 13 N 242 ARG GLY TYR VAL PRO ALA SER THR ARG ILE HIS SER GLU
SEQRES 14 N 242 GLU ASP GLU ARG PRO ILE GLY ARG LEU LEU VAL ASP ALA
SEQRES 15 N 242 CYS TYR SER PRO VAL GLU ARG ILE ALA TYR ASN VAL GLU
SEQRES 16 N 242 ALA ALA ARG VAL GLU GLN ARG THR ASP LEU ASP LYS LEU
SEQRES 17 N 242 VAL ILE GLU MET GLU THR ASN GLY THR ILE ASP PRO GLU
SEQRES 18 N 242 GLU ALA ILE ARG ARG ALA ALA THR ILE LEU ALA GLU GLN
SEQRES 19 N 242 LEU GLU ALA PHE VAL ASP LEU ARG
SEQRES 1 O 1342 MET VAL TYR SER TYR THR GLU LYS LYS ARG ILE ARG LYS
SEQRES 2 O 1342 ASP PHE GLY LYS ARG PRO GLN VAL LEU ASP VAL PRO TYR
SEQRES 3 O 1342 LEU LEU SER ILE GLN LEU ASP SER PHE GLN LYS PHE ILE
SEQRES 4 O 1342 GLU GLN ASP PRO GLU GLY GLN TYR GLY LEU GLU ALA ALA
SEQRES 5 O 1342 PHE ARG SER VAL PHE PRO ILE GLN SER TYR SER GLY ASN
SEQRES 6 O 1342 SER GLU LEU GLN TYR VAL SER TYR ARG LEU GLY GLU PRO
SEQRES 7 O 1342 VAL PHE ASP VAL GLN GLU CYS GLN ILE ARG GLY VAL THR
SEQRES 8 O 1342 TYR SER ALA PRO LEU ARG VAL LYS LEU ARG LEU VAL ILE
SEQRES 9 O 1342 TYR GLU ARG GLU ALA PRO GLU GLY THR VAL LYS ASP ILE
SEQRES 10 O 1342 LYS GLU GLN GLU VAL TYR MET GLY GLU ILE PRO LEU MET
SEQRES 11 O 1342 THR ASP ASN GLY THR PHE VAL ILE ASN GLY THR GLU ARG
SEQRES 12 O 1342 VAL ILE VAL SER GLN LEU HIS ARG SER PRO GLY VAL PHE
SEQRES 13 O 1342 PHE ASP SER ASP LYS GLY LYS THR HIS SER SER GLY LYS
SEQRES 14 O 1342 VAL LEU TYR ASN ALA ARG ILE ILE PRO TYR ARG GLY SER
SEQRES 15 O 1342 TRP LEU ASP PHE GLU PHE ASP PRO LYS ASP ASN LEU PHE
SEQRES 16 O 1342 VAL ARG ILE ASP ARG ARG ARG LYS LEU PRO ALA THR ILE
SEQRES 17 O 1342 ILE LEU ARG ALA LEU ASN TYR THR THR GLU GLN ILE LEU
SEQRES 18 O 1342 ASP LEU PHE PHE GLU LYS VAL ILE PHE GLU ILE ARG ASP
SEQRES 19 O 1342 ASN LYS LEU GLN MET GLU LEU VAL PRO GLU ARG LEU ARG
SEQRES 20 O 1342 GLY GLU THR ALA SER PHE ASP ILE GLU ALA ASN GLY LYS
SEQRES 21 O 1342 VAL TYR VAL GLU LYS GLY ARG ARG ILE THR ALA ARG HIS
SEQRES 22 O 1342 ILE ARG GLN LEU GLU LYS ASP ASP VAL LYS LEU ILE GLU
SEQRES 23 O 1342 VAL PRO VAL GLU TYR ILE ALA GLY LYS VAL VAL ALA LYS
SEQRES 24 O 1342 ASP TYR ILE ASP GLU SER THR GLY GLU LEU ILE CYS ALA
SEQRES 25 O 1342 ALA ASN MET GLU LEU SER LEU ASP LEU LEU ALA LYS LEU
SEQRES 26 O 1342 SER GLN SER GLY HIS LYS ARG ILE GLU THR LEU PHE THR
SEQRES 27 O 1342 ASN ASP LEU ASP HIS GLY PRO TYR ILE SER GLU THR LEU
SEQRES 28 O 1342 ARG VAL ASP PRO THR ASN ASP ARG LEU SER ALA LEU VAL
SEQRES 29 O 1342 GLU ILE TYR ARG MET MET ARG PRO GLY GLU PRO PRO THR
SEQRES 30 O 1342 ARG GLU ALA ALA GLU SER LEU PHE GLU ASN LEU PHE PHE
SEQRES 31 O 1342 SER GLU ASP ARG TYR ASP LEU SER ALA VAL GLY ARG MET
SEQRES 32 O 1342 LYS PHE ASN ARG SER LEU LEU ARG GLU GLU ILE GLU GLY
SEQRES 33 O 1342 SER GLY ILE LEU SER LYS ASP ASP ILE ILE ASP VAL MET
SEQRES 34 O 1342 LYS LYS LEU ILE ASP ILE ARG ASN GLY LYS GLY GLU VAL
SEQRES 35 O 1342 ASP ASP ILE ASP HIS LEU GLY ASN ARG ARG ILE ARG SER
SEQRES 36 O 1342 VAL GLY GLU MET ALA GLU ASN GLN PHE ARG VAL GLY LEU
SEQRES 37 O 1342 VAL ARG VAL GLU ARG ALA VAL LYS GLU ARG LEU SER LEU
SEQRES 38 O 1342 GLY ASP LEU ASP THR LEU MET PRO GLN ASP MET ILE ASN
SEQRES 39 O 1342 ALA LYS PRO ILE SER ALA ALA VAL LYS GLU PHE PHE GLY
SEQRES 40 O 1342 SER SER GLN LEU SER GLN PHE MET ASP GLN ASN ASN PRO
SEQRES 41 O 1342 LEU SER GLU ILE THR HIS LYS ARG ARG ILE SER ALA LEU
SEQRES 42 O 1342 GLY PRO GLY GLY LEU THR ARG GLU ARG ALA GLY PHE GLU
SEQRES 43 O 1342 VAL ARG ASP VAL HIS PRO THR HIS TYR GLY ARG VAL CYS
SEQRES 44 O 1342 PRO ILE GLU THR PRO GLU GLY PRO ASN ILE GLY LEU ILE
SEQRES 45 O 1342 ASN SER LEU SER VAL TYR ALA GLN THR ASN GLU TYR GLY
SEQRES 46 O 1342 PHE LEU GLU THR PRO TYR ARG LYS VAL THR ASP GLY VAL
SEQRES 47 O 1342 VAL THR ASP GLU ILE HIS TYR LEU SER ALA ILE GLU GLU
SEQRES 48 O 1342 GLY ASN TYR VAL ILE ALA GLN ALA ASN SER ASN LEU ASP
SEQRES 49 O 1342 GLU GLU GLY HIS PHE VAL GLU ASP LEU VAL THR CYS ARG
SEQRES 50 O 1342 SER LYS GLY GLU SER SER LEU PHE SER ARG ASP GLN VAL
SEQRES 51 O 1342 ASP TYR MET ASP VAL SER THR GLN GLN VAL VAL SER VAL
SEQRES 52 O 1342 GLY ALA SER LEU ILE PRO PHE LEU GLU HIS ASP ASP ALA
SEQRES 53 O 1342 ASN ARG ALA LEU MET GLY ALA ASN MET GLN ARG GLN ALA
SEQRES 54 O 1342 VAL PRO THR LEU ARG ALA ASP LYS PRO LEU VAL GLY THR
SEQRES 55 O 1342 GLY MET GLU ARG ALA VAL ALA VAL ASP SER GLY VAL THR
SEQRES 56 O 1342 ALA VAL ALA LYS ARG GLY GLY VAL VAL GLN TYR VAL ASP
SEQRES 57 O 1342 ALA SER ARG ILE VAL ILE LYS VAL ASN GLU ASP GLU MET
SEQRES 58 O 1342 TYR PRO GLY GLU ALA GLY ILE ASP ILE TYR ASN LEU THR
SEQRES 59 O 1342 LYS TYR THR ARG SER ASN GLN ASN THR CYS ILE ASN GLN
SEQRES 60 O 1342 MET PRO CYS VAL SER LEU GLY GLU PRO VAL GLU ARG GLY
SEQRES 61 O 1342 ASP VAL LEU ALA ASP GLY PRO SER THR ASP LEU GLY GLU
SEQRES 62 O 1342 LEU ALA LEU GLY GLN ASN MET ARG VAL ALA PHE MET PRO
SEQRES 63 O 1342 TRP ASN GLY TYR ASN PHE GLU ASP SER ILE LEU VAL SER
SEQRES 64 O 1342 GLU ARG VAL VAL GLN GLU ASP ARG PHE THR THR ILE HIS
SEQRES 65 O 1342 ILE GLN GLU LEU ALA CYS VAL SER ARG ASP THR LYS LEU
SEQRES 66 O 1342 GLY PRO GLU GLU ILE THR ALA ASP ILE PRO ASN VAL GLY
SEQRES 67 O 1342 GLU ALA ALA LEU SER LYS LEU ASP GLU SER GLY ILE VAL
SEQRES 68 O 1342 TYR ILE GLY ALA GLU VAL THR GLY GLY ASP ILE LEU VAL
SEQRES 69 O 1342 GLY LYS VAL THR PRO LYS GLY GLU THR GLN LEU THR PRO
SEQRES 70 O 1342 GLU GLU LYS LEU LEU ARG ALA ILE PHE GLY GLU LYS ALA
SEQRES 71 O 1342 SER ASP VAL LYS ASP SER SER LEU ARG VAL PRO ASN GLY
SEQRES 72 O 1342 VAL SER GLY THR VAL ILE ASP VAL GLN VAL PHE THR ARG
SEQRES 73 O 1342 ASP GLY VAL GLU LYS ASP LYS ARG ALA LEU GLU ILE GLU
SEQRES 74 O 1342 GLU MET GLN LEU LYS GLN ALA LYS LYS ASP LEU SER GLU
SEQRES 75 O 1342 GLU LEU GLN ILE LEU GLU ALA GLY LEU PHE SER ARG ILE
SEQRES 76 O 1342 ARG ALA VAL LEU VAL ALA GLY GLY VAL GLU ALA GLU LYS
SEQRES 77 O 1342 LEU ASP LYS LEU PRO ARG ASP ARG TRP LEU GLU LEU GLY
SEQRES 78 O 1342 LEU THR ASP GLU GLU LYS GLN ASN GLN LEU GLU GLN LEU
SEQRES 79 O 1342 ALA GLU GLN TYR ASP GLU LEU LYS HIS GLU PHE GLU LYS
SEQRES 80 O 1342 LYS LEU GLU ALA LYS ARG ARG LYS ILE THR GLN GLY ASP
SEQRES 81 O 1342 ASP LEU ALA PRO GLY VAL LEU LYS ILE VAL LYS VAL TYR
SEQRES 82 O 1342 LEU ALA VAL LYS ARG ARG ILE GLN PRO GLY ASP LYS MET
SEQRES 83 O 1342 ALA GLY ARG HIS GLY ASN LYS GLY VAL ILE SER LYS ILE
SEQRES 84 O 1342 ASN PRO ILE GLU ASP MET PRO TYR ASP GLU ASN GLY THR
SEQRES 85 O 1342 PRO VAL ASP ILE VAL LEU ASN PRO LEU GLY VAL PRO SER
SEQRES 86 O 1342 ARG MET ASN ILE GLY GLN ILE LEU GLU THR HIS LEU GLY
SEQRES 87 O 1342 MET ALA ALA LYS GLY ILE GLY ASP LYS ILE ASN ALA MET
SEQRES 88 O 1342 LEU LYS GLN GLN GLN GLU VAL ALA LYS LEU ARG GLU PHE
SEQRES 89 O 1342 ILE GLN ARG ALA TYR ASP LEU GLY ALA ASP VAL ARG GLN
SEQRES 90 O 1342 LYS VAL ASP LEU SER THR PHE SER ASP GLU GLU VAL MET
SEQRES 91 O 1342 ARG LEU ALA GLU ASN LEU ARG LYS GLY MET PRO ILE ALA
SEQRES 92 O 1342 THR PRO VAL PHE ASP GLY ALA LYS GLU ALA GLU ILE LYS
SEQRES 93 O 1342 GLU LEU LEU LYS LEU GLY ASP LEU PRO THR SER GLY GLN
SEQRES 94 O 1342 ILE ARG LEU TYR ASP GLY ARG THR GLY GLU GLN PHE GLU
SEQRES 95 O 1342 ARG PRO VAL THR VAL GLY TYR MET TYR MET LEU LYS LEU
SEQRES 96 O 1342 ASN HIS LEU VAL ASP ASP LYS MET HIS ALA ARG SER THR
SEQRES 97 O 1342 GLY SER TYR SER LEU VAL THR GLN GLN PRO LEU GLY GLY
SEQRES 98 O 1342 LYS ALA GLN PHE GLY GLY GLN ARG PHE GLY GLU MET GLU
SEQRES 99 O 1342 VAL TRP ALA LEU GLU ALA TYR GLY ALA ALA TYR THR LEU
SEQRES 100 O 1342 GLN GLU MET LEU THR VAL LYS SER ASP ASP VAL ASN GLY
SEQRES 101 O 1342 ARG THR LYS MET TYR LYS ASN ILE VAL ASP GLY ASN HIS
SEQRES 102 O 1342 GLN MET GLU PRO GLY MET PRO GLU SER PHE ASN VAL LEU
SEQRES 103 O 1342 LEU LYS GLU ILE ARG SER LEU GLY ILE ASN ILE GLU LEU
SEQRES 104 O 1342 GLU ASP GLU
SEQRES 1 P 1407 MET LYS ASP LEU LEU LYS PHE LEU LYS ALA GLN THR LYS
SEQRES 2 P 1407 THR GLU GLU PHE ASP ALA ILE LYS ILE ALA LEU ALA SER
SEQRES 3 P 1407 PRO ASP MET ILE ARG SER TRP SER PHE GLY GLU VAL LYS
SEQRES 4 P 1407 LYS PRO GLU THR ILE ASN TYR ARG THR PHE LYS PRO GLU
SEQRES 5 P 1407 ARG ASP GLY LEU PHE CYS ALA ARG ILE PHE GLY PRO VAL
SEQRES 6 P 1407 LYS ASP TYR GLU CYS LEU CYS GLY LYS TYR LYS ARG LEU
SEQRES 7 P 1407 LYS HIS ARG GLY VAL ILE CYS GLU LYS CYS GLY VAL GLU
SEQRES 8 P 1407 VAL THR GLN THR LYS VAL ARG ARG GLU ARG MET GLY HIS
SEQRES 9 P 1407 ILE GLU LEU ALA SER PRO THR ALA HIS ILE TRP PHE LEU
SEQRES 10 P 1407 LYS SER LEU PRO SER ARG ILE GLY LEU LEU LEU ASP MET
SEQRES 11 P 1407 PRO LEU ARG ASP ILE GLU ARG VAL LEU TYR PHE GLU SER
SEQRES 12 P 1407 TYR VAL VAL ILE GLU GLY GLY MET THR ASN LEU GLU ARG
SEQRES 13 P 1407 GLN GLN ILE LEU THR GLU GLU GLN TYR LEU ASP ALA LEU
SEQRES 14 P 1407 GLU GLU PHE GLY ASP GLU PHE ASP ALA LYS MET GLY ALA
SEQRES 15 P 1407 GLU ALA ILE GLN ALA LEU LEU LYS SER MET ASP LEU GLU
SEQRES 16 P 1407 GLN GLU CYS GLU GLN LEU ARG GLU GLU LEU ASN GLU THR
SEQRES 17 P 1407 ASN SER GLU THR LYS ARG LYS LYS LEU THR LYS ARG ILE
SEQRES 18 P 1407 LYS LEU LEU GLU ALA PHE VAL GLN SER GLY ASN LYS PRO
SEQRES 19 P 1407 GLU TRP MET ILE LEU THR VAL LEU PRO VAL LEU PRO PRO
SEQRES 20 P 1407 ASP LEU ARG PRO LEU VAL PRO LEU ASP GLY GLY ARG PHE
SEQRES 21 P 1407 ALA THR SER ASP LEU ASN ASP LEU TYR ARG ARG VAL ILE
SEQRES 22 P 1407 ASN ARG ASN ASN ARG LEU LYS ARG LEU LEU ASP LEU ALA
SEQRES 23 P 1407 ALA PRO ASP ILE ILE VAL ARG ASN GLU LYS ARG MET LEU
SEQRES 24 P 1407 GLN GLU ALA VAL ASP ALA LEU LEU ASP ASN GLY ARG ARG
SEQRES 25 P 1407 GLY ARG ALA ILE THR GLY SER ASN LYS ARG PRO LEU LYS
SEQRES 26 P 1407 SER LEU ALA ASP MET ILE LYS GLY LYS GLN GLY ARG PHE
SEQRES 27 P 1407 ARG GLN ASN LEU LEU GLY LYS ARG VAL ASP TYR SER GLY
SEQRES 28 P 1407 ARG SER VAL ILE THR VAL GLY PRO TYR LEU ARG LEU HIS
SEQRES 29 P 1407 GLN CYS GLY LEU PRO LYS LYS MET ALA LEU GLU LEU PHE
SEQRES 30 P 1407 LYS PRO PHE ILE TYR GLY LYS LEU GLU LEU ARG GLY LEU
SEQRES 31 P 1407 ALA THR THR ILE LYS ALA ALA LYS LYS MET VAL GLU ARG
SEQRES 32 P 1407 GLU GLU ALA VAL VAL TRP ASP ILE LEU ASP GLU VAL ILE
SEQRES 33 P 1407 ARG GLU HIS PRO VAL LEU LEU ASN ARG ALA PRO THR LEU
SEQRES 34 P 1407 HIS ARG LEU GLY ILE GLN ALA PHE GLU PRO VAL LEU ILE
SEQRES 35 P 1407 GLU GLY LYS ALA ILE GLN LEU HIS PRO LEU VAL CYS ALA
SEQRES 36 P 1407 ALA TYR ASN ALA ASP PHE ASP GLY ASP GLN MET ALA VAL
SEQRES 37 P 1407 HIS VAL PRO LEU THR LEU GLU ALA GLN LEU GLU ALA ARG
SEQRES 38 P 1407 ALA LEU MET MET SER THR ASN ASN ILE LEU SER PRO ALA
SEQRES 39 P 1407 ASN GLY GLU PRO ILE ILE VAL PRO SER GLN ASP VAL VAL
SEQRES 40 P 1407 LEU GLY LEU TYR TYR MET THR ARG ASP CYS VAL ASN ALA
SEQRES 41 P 1407 LYS GLY GLU GLY MET VAL LEU THR GLY PRO LYS GLU ALA
SEQRES 42 P 1407 GLU ARG LEU TYR ARG SER GLY LEU ALA SER LEU HIS ALA
SEQRES 43 P 1407 ARG VAL LYS VAL ARG ILE THR GLU TYR GLU LYS ASP ALA
SEQRES 44 P 1407 ASN GLY GLU LEU VAL ALA LYS THR SER LEU LYS ASP THR
SEQRES 45 P 1407 THR VAL GLY ARG ALA ILE LEU TRP MET ILE VAL PRO LYS
SEQRES 46 P 1407 GLY LEU PRO TYR SER ILE VAL ASN GLN ALA LEU GLY LYS
SEQRES 47 P 1407 LYS ALA ILE SER LYS MET LEU ASN THR CYS TYR ARG ILE
SEQRES 48 P 1407 LEU GLY LEU LYS PRO THR VAL ILE PHE ALA ASP GLN ILE
SEQRES 49 P 1407 MET TYR THR GLY PHE ALA TYR ALA ALA ARG SER GLY ALA
SEQRES 50 P 1407 SER VAL GLY ILE ASP ASP MET VAL ILE PRO GLU LYS LYS
SEQRES 51 P 1407 HIS GLU ILE ILE SER GLU ALA GLU ALA GLU VAL ALA GLU
SEQRES 52 P 1407 ILE GLN GLU GLN PHE GLN SER GLY LEU VAL THR ALA GLY
SEQRES 53 P 1407 GLU ARG TYR ASN LYS VAL ILE ASP ILE TRP ALA ALA ALA
SEQRES 54 P 1407 ASN ASP ARG VAL SER LYS ALA MET MET ASP ASN LEU GLN
SEQRES 55 P 1407 THR GLU THR VAL ILE ASN ARG ASP GLY GLN GLU GLU LYS
SEQRES 56 P 1407 GLN VAL SER PHE ASN SER ILE TYR MET MET ALA ASP SER
SEQRES 57 P 1407 GLY ALA ARG GLY SER ALA ALA GLN ILE ARG GLN LEU ALA
SEQRES 58 P 1407 GLY MET ARG GLY LEU MET ALA LYS PRO ASP GLY SER ILE
SEQRES 59 P 1407 ILE GLU THR PRO ILE THR ALA ASN PHE ARG GLU GLY LEU
SEQRES 60 P 1407 ASN VAL LEU GLN TYR PHE ILE SER THR HIS GLY ALA ARG
SEQRES 61 P 1407 LYS GLY LEU ALA ASP THR ALA LEU LYS THR ALA ASN SER
SEQRES 62 P 1407 GLY TYR LEU THR ARG ARG LEU VAL ASP VAL ALA GLN ASP
SEQRES 63 P 1407 LEU VAL VAL THR GLU ASP ASP CYS GLY THR HIS GLU GLY
SEQRES 64 P 1407 ILE MET MET THR PRO VAL ILE GLU GLY GLY ASP VAL LYS
SEQRES 65 P 1407 GLU PRO LEU ARG ASP ARG VAL LEU GLY ARG VAL THR ALA
SEQRES 66 P 1407 GLU ASP VAL LEU LYS PRO GLY THR ALA ASP ILE LEU VAL
SEQRES 67 P 1407 PRO ARG ASN THR LEU LEU HIS GLU GLN TRP CYS ASP LEU
SEQRES 68 P 1407 LEU GLU GLU ASN SER VAL ASP ALA VAL LYS VAL ARG SER
SEQRES 69 P 1407 VAL VAL SER CYS ASP THR ASP PHE GLY VAL CYS ALA HIS
SEQRES 70 P 1407 CYS TYR GLY ARG ASP LEU ALA ARG GLY HIS ILE ILE ASN
SEQRES 71 P 1407 LYS GLY GLU ALA ILE GLY VAL ILE ALA ALA GLN SER ILE
SEQRES 72 P 1407 GLY GLU PRO GLY THR GLN LEU THR MET ARG THR PHE HIS
SEQRES 73 P 1407 ILE GLY GLY ALA ALA SER ARG ALA ALA ALA GLU SER SER
SEQRES 74 P 1407 ILE GLN VAL LYS ASN LYS GLY SER ILE LYS LEU SER ASN
SEQRES 75 P 1407 VAL LYS SER VAL VAL ASN SER SER GLY LYS LEU VAL ILE
SEQRES 76 P 1407 THR SER ARG ASN THR GLU LEU LYS LEU ILE ASP GLU PHE
SEQRES 77 P 1407 GLY ARG THR LYS GLU SER TYR LYS VAL PRO TYR GLY ALA
SEQRES 78 P 1407 VAL LEU ALA LYS GLY ASP GLY GLU GLN VAL ALA GLY GLY
SEQRES 79 P 1407 GLU THR VAL ALA ASN TRP ASP PRO HIS THR MET PRO VAL
SEQRES 80 P 1407 ILE THR GLU VAL SER GLY PHE VAL ARG PHE THR ASP MET
SEQRES 81 P 1407 ILE ASP GLY GLN THR ILE THR ARG GLN THR ASP GLU LEU
SEQRES 82 P 1407 THR GLY LEU SER SER LEU VAL VAL LEU ASP SER ALA GLU
SEQRES 83 P 1407 ARG THR ALA GLY GLY LYS ASP LEU ARG PRO ALA LEU LYS
SEQRES 84 P 1407 ILE VAL ASP ALA GLN GLY ASN ASP VAL LEU ILE PRO GLY
SEQRES 85 P 1407 THR ASP MET PRO ALA GLN TYR PHE LEU PRO GLY LYS ALA
SEQRES 86 P 1407 ILE VAL GLN LEU GLU ASP GLY VAL GLN ILE SER SER GLY
SEQRES 87 P 1407 ASP THR LEU ALA ARG ILE PRO GLN GLU SER GLY GLY THR
SEQRES 88 P 1407 LYS ASP ILE THR GLY GLY LEU PRO ARG VAL ALA ASP LEU
SEQRES 89 P 1407 PHE GLU ALA ARG ARG PRO LYS GLU PRO ALA ILE LEU ALA
SEQRES 90 P 1407 GLU ILE SER GLY ILE VAL SER PHE GLY LYS GLU THR LYS
SEQRES 91 P 1407 GLY LYS ARG ARG LEU VAL ILE THR PRO VAL ASP GLY SER
SEQRES 92 P 1407 ASP PRO TYR GLU GLU MET ILE PRO LYS TRP ARG GLN LEU
SEQRES 93 P 1407 ASN VAL PHE GLU GLY GLU ARG VAL GLU ARG GLY ASP VAL
SEQRES 94 P 1407 ILE SER ASP GLY PRO GLU ALA PRO HIS ASP ILE LEU ARG
SEQRES 95 P 1407 LEU ARG GLY VAL HIS ALA VAL THR ARG TYR ILE VAL ASN
SEQRES 96 P 1407 GLU VAL GLN ASP VAL TYR ARG LEU GLN GLY VAL LYS ILE
SEQRES 97 P 1407 ASN ASP LYS HIS ILE GLU VAL ILE VAL ARG GLN MET LEU
SEQRES 98 P 1407 ARG LYS ALA THR ILE VAL ASN ALA GLY SER SER ASP PHE
SEQRES 99 P 1407 LEU GLU GLY GLU GLN VAL GLU TYR SER ARG VAL LYS ILE
SEQRES 100 P 1407 ALA ASN ARG GLU LEU GLU ALA ASN GLY LYS VAL GLY ALA
SEQRES 101 P 1407 THR TYR SER ARG ASP LEU LEU GLY ILE THR LYS ALA SER
SEQRES 102 P 1407 LEU ALA THR GLU SER PHE ILE SER ALA ALA SER PHE GLN
SEQRES 103 P 1407 GLU THR THR ARG VAL LEU THR GLU ALA ALA VAL ALA GLY
SEQRES 104 P 1407 LYS ARG ASP GLU LEU ARG GLY LEU LYS GLU ASN VAL ILE
SEQRES 105 P 1407 VAL GLY ARG LEU ILE PRO ALA GLY THR GLY TYR ALA TYR
SEQRES 106 P 1407 HIS GLN ASP ARG MET ARG ARG ARG ALA ALA GLY GLU ALA
SEQRES 107 P 1407 PRO ALA ALA PRO GLN VAL THR ALA GLU ASP ALA SER ALA
SEQRES 108 P 1407 SER LEU ALA GLU LEU LEU ASN ALA GLY LEU GLY GLY SER
SEQRES 109 P 1407 ASP ASN GLU
SEQRES 1 Q 90 ALA ARG VAL THR VAL GLN ASP ALA VAL GLU LYS ILE GLY
SEQRES 2 Q 90 ASN ARG PHE ASP LEU VAL LEU VAL ALA ALA ARG ARG ALA
SEQRES 3 Q 90 ARG GLN MET GLN VAL GLY GLY LYS ASP PRO LEU VAL PRO
SEQRES 4 Q 90 GLU GLU ASN ASP LYS THR THR VAL ILE ALA LEU ARG GLU
SEQRES 5 Q 90 ILE GLU GLU GLY LEU ILE ASN ASN GLN ILE LEU ASP VAL
SEQRES 6 Q 90 ARG GLU ARG GLN GLU GLN GLN GLU GLN GLU ALA ALA GLU
SEQRES 7 Q 90 LEU GLN ALA VAL THR ALA ILE ALA GLU GLY ARG ARG
SEQRES 1 R 628 MET ARG GLY SER HIS HIS HIS HIS HIS HIS THR ASP GLN
SEQRES 2 R 628 PHE THR MET GLU GLN ASN PRO GLN SER GLN LEU LYS LEU
SEQRES 3 R 628 LEU VAL THR ARG GLY LYS GLU GLN GLY TYR LEU THR TYR
SEQRES 4 R 628 ALA GLU VAL ASN ASP HIS LEU PRO GLU ASP ILE VAL ASP
SEQRES 5 R 628 SER ASP GLN ILE GLU ASP ILE ILE GLN MET ILE ASN ASP
SEQRES 6 R 628 MET GLY ILE GLN VAL MET GLU GLU ALA PRO ASP ALA ASP
SEQRES 7 R 628 ASP LEU MET LEU ALA GLU ASN THR ALA ASP GLU ASP ALA
SEQRES 8 R 628 ALA GLU ALA ALA ALA GLN VAL LEU SER SER VAL GLU SER
SEQRES 9 R 628 GLU ILE GLY ARG THR THR ASP PRO VAL ARG MET TYR MET
SEQRES 10 R 628 ARG GLU MET GLY THR VAL GLU LEU LEU THR ARG GLU GLY
SEQRES 11 R 628 GLU ILE ASP ILE ALA LYS ARG ILE GLU ASP GLY ILE ASN
SEQRES 12 R 628 GLN VAL GLN CYS SER VAL ALA GLU TYR PRO GLU ALA ILE
SEQRES 13 R 628 THR TYR LEU LEU GLU GLN TYR ASP ARG VAL GLU ALA GLU
SEQRES 14 R 628 GLU ALA ARG LEU SER ASP LEU ILE THR GLY PHE VAL ASP
SEQRES 15 R 628 PRO ASN ALA GLU GLU ASP LEU ALA PRO THR ALA THR HIS
SEQRES 16 R 628 VAL GLY SER GLU LEU SER GLN GLU ASP LEU ASP ASP ASP
SEQRES 17 R 628 GLU ASP GLU ASP GLU GLU ASP GLY ASP ASP ASP SER ALA
SEQRES 18 R 628 ASP ASP ASP ASN SER ILE ASP PRO GLU LEU ALA ARG GLU
SEQRES 19 R 628 LYS PHE ALA GLU LEU ARG ALA GLN TYR VAL VAL THR ARG
SEQRES 20 R 628 ASP THR ILE LYS ALA LYS GLY ARG SER HIS ALA THR ALA
SEQRES 21 R 628 GLN GLU GLU ILE LEU LYS LEU SER GLU VAL PHE LYS GLN
SEQRES 22 R 628 PHE ARG LEU VAL PRO LYS GLN PHE ASP TYR LEU VAL ASN
SEQRES 23 R 628 SER MET ARG VAL MET MET ASP ARG VAL ARG THR GLN GLU
SEQRES 24 R 628 ARG LEU ILE MET LYS LEU CYS VAL GLU GLN CYS LYS MET
SEQRES 25 R 628 PRO LYS LYS ASN PHE ILE THR LEU PHE THR GLY ASN GLU
SEQRES 26 R 628 THR SER ASP THR TRP PHE ASN ALA ALA ILE ALA MET ASN
SEQRES 27 R 628 LYS PRO TRP SER GLU LYS LEU HIS ASP VAL SER GLU GLU
SEQRES 28 R 628 VAL HIS ARG ALA LEU GLN LYS LEU GLN GLN ILE GLU GLU
SEQRES 29 R 628 GLU THR GLY LEU THR ILE GLU GLN VAL LYS ASP ILE ASN
SEQRES 30 R 628 ARG ARG MET SER ILE GLY GLU ALA LYS ALA ARG ARG ALA
SEQRES 31 R 628 LYS LYS GLU MET VAL GLU ALA ASN LEU ARG LEU VAL ILE
SEQRES 32 R 628 SER ILE ALA LYS LYS TYR THR ASN ARG GLY LEU GLN PHE
SEQRES 33 R 628 LEU ASP LEU ILE GLN GLU GLY ASN ILE GLY LEU MET LYS
SEQRES 34 R 628 ALA VAL ASP LYS PHE GLU TYR ARG ARG GLY TYR LYS PHE
SEQRES 35 R 628 SER THR TYR ALA THR TRP TRP ILE ARG GLN ALA ILE THR
SEQRES 36 R 628 ARG SER ILE ALA ASP GLN ALA ARG THR ILE ARG ILE PRO
SEQRES 37 R 628 VAL HIS MET ILE GLU THR ILE ASN LYS LEU ASN ARG ILE
SEQRES 38 R 628 SER ARG GLN MET LEU GLN GLU MET GLY ARG GLU PRO THR
SEQRES 39 R 628 PRO GLU GLU LEU ALA GLU ARG MET LEU MET PRO GLU ASP
SEQRES 40 R 628 LYS ILE ARG LYS VAL LEU LYS ILE ALA LYS GLU PRO ILE
SEQRES 41 R 628 SER MET GLU THR PRO ILE GLY ASP ASP GLU ASP SER HIS
SEQRES 42 R 628 LEU GLY ASP PHE ILE GLU ASP THR THR LEU GLU LEU PRO
SEQRES 43 R 628 LEU ASP SER ALA THR THR GLU SER LEU ARG ALA ALA THR
SEQRES 44 R 628 HIS ASP VAL LEU ALA GLY LEU THR ALA ARG GLU ALA LYS
SEQRES 45 R 628 VAL LEU ARG MET ARG PHE GLY ILE ASP MET ASN THR ASP
SEQRES 46 R 628 TYR THR LEU GLU GLU VAL GLY LYS GLN PHE ASP VAL THR
SEQRES 47 R 628 ARG GLU ARG ILE ARG GLN ILE GLU ALA LYS ALA LEU ARG
SEQRES 48 R 628 LYS LEU ARG HIS PRO SER ARG SER GLU VAL LEU ARG SER
SEQRES 49 R 628 PHE LEU ASP ASP
SEQRES 1 7 49 DA DC DT DT DG DA DC DA DT DC DC DA DC
SEQRES 2 7 49 DC DT DC DA DC DG DT DA DT DG DC DT DA
SEQRES 3 7 49 DT DA DA DT DG DT DG DT DG DC DA DG DT
SEQRES 4 7 49 DC DT DG DA DC DG DC DG DG DC
SEQRES 1 8 49 DG DC DC DG DC DG DT DC DA DG DA DC DT
SEQRES 2 8 49 DC DG DT DA DG DG DA DT DT DA DT DA DG
SEQRES 3 8 49 DC DA DT DA DC DG DT DG DA DG DG DT DG
SEQRES 4 8 49 DG DA DT DG DT DC DA DA DG DT
SEQRES 1 9 5 GTP A G U C
HET GTP 3 13 32
HET GTP 6 13 32
HET GTP 9 13 32
HET ZN D1501 1
HET ZN D1502 1
HET MG D1503 1
HET ZN J1501 1
HET ZN J1502 1
HET MG J1503 1
HET ZN P1501 1
HET ZN P1502 1
HET MG P1503 1
HETNAM GTP GUANOSINE-5'-TRIPHOSPHATE
HETNAM ZN ZINC ION
HETNAM MG MAGNESIUM ION
FORMUL 9 GTP 3(C10 H16 N5 O14 P3)
FORMUL 28 ZN 6(ZN 2+)
FORMUL 30 MG 3(MG 2+)
HELIX 1 AA1 GLY A 34 MET A 51 1 18
HELIX 2 AA2 ASP A 77 GLY A 87 1 11
HELIX 3 AA3 PRO A 154 SER A 161 1 8
HELIX 4 AA4 ASP A 212 LEU A 234 1 23
HELIX 5 AA5 GLY B 34 SER B 50 1 17
HELIX 6 AA6 ASP B 77 GLY B 87 1 11
HELIX 7 AA7 ALA B 113 ILE B 115 5 3
HELIX 8 AA8 PRO B 154 SER B 161 1 8
HELIX 9 AA9 ASP B 212 ASP B 233 1 22
HELIX 10 AB1 SER C 4 ARG C 10 1 7
HELIX 11 AB2 SER C 29 GLU C 40 1 12
HELIX 12 AB3 TYR C 47 PHE C 57 1 11
HELIX 13 AB4 ASP C 81 GLY C 89 1 9
HELIX 14 AB5 ALA C 206 LEU C 213 1 8
HELIX 15 AB6 THR C 216 PHE C 225 1 10
HELIX 16 AB7 VAL C 242 LEU C 246 5 5
HELIX 17 AB8 THR C 270 ASP C 281 1 12
HELIX 18 AB9 SER C 318 GLY C 329 1 12
HELIX 19 AC1 PRO C 345 ASP C 354 1 10
HELIX 20 AC2 ASP C 358 ARG C 371 1 14
HELIX 21 AC3 THR C 377 PHE C 390 1 14
HELIX 22 AC4 LEU C 397 LEU C 409 1 13
HELIX 23 AC5 SER C 421 GLY C 438 1 18
HELIX 24 AC6 VAL C 456 GLY C 482 1 27
HELIX 25 AC7 MET C 488 ILE C 493 1 6
HELIX 26 AC8 ALA C 495 SER C 509 1 15
HELIX 27 AC9 ASN C 519 ARG C 528 1 10
HELIX 28 AD1 GLY C 544 ASP C 549 1 6
HELIX 29 AD2 HIS C 551 TYR C 555 5 5
HELIX 30 AD3 SER C 607 GLY C 612 1 6
HELIX 31 AD4 ASP C 648 VAL C 650 5 3
HELIX 32 AD5 SER C 656 VAL C 661 5 6
HELIX 33 AD6 SER C 662 ILE C 668 1 7
HELIX 34 AD7 PHE C 670 ASP C 674 5 5
HELIX 35 AD8 ASP C 675 GLN C 688 1 14
HELIX 36 AD9 GLY C 703 GLY C 713 1 11
HELIX 37 AE1 GLU C 820 GLU C 825 1 6
HELIX 38 AE2 GLY C 858 LEU C 865 1 8
HELIX 39 AE3 THR C 896 GLY C 907 1 12
HELIX 40 AE4 ASP C 942 VAL C 980 1 39
HELIX 41 AE5 ALA C 986 LYS C 991 1 6
HELIX 42 AE6 GLU C 1006 GLN C 1038 1 33
HELIX 43 AE7 ASN C 1099 VAL C 1103 5 5
HELIX 44 AE8 ILE C 1109 GLN C 1134 1 26
HELIX 45 AE9 GLU C 1137 ASP C 1150 1 14
HELIX 46 AF1 SER C 1165 ARG C 1177 1 13
HELIX 47 AF2 LYS C 1191 GLY C 1202 1 12
HELIX 48 AF3 LEU C 1238 MET C 1243 1 6
HELIX 49 AF4 GLY C 1260 PHE C 1265 1 6
HELIX 50 AF5 GLY C 1271 TYR C 1281 1 11
HELIX 51 AF6 ALA C 1283 THR C 1292 1 10
HELIX 52 AF7 ASP C 1297 ASP C 1310 1 14
HELIX 53 AF8 PRO C 1320 LEU C 1333 1 14
HELIX 54 AF9 SER D 26 TRP D 33 1 8
HELIX 55 AG1 CYS D 58 GLY D 63 1 6
HELIX 56 AG2 GLN D 94 GLU D 100 5 7
HELIX 57 AG3 ILE D 114 SER D 119 1 6
HELIX 58 AG4 SER D 122 ASP D 129 1 8
HELIX 59 AG5 PRO D 131 TYR D 140 1 10
HELIX 60 AG6 THR D 161 GLU D 170 1 10
HELIX 61 AG7 MET D 180 MET D 192 1 13
HELIX 62 AG8 ASP D 193 GLU D 207 1 15
HELIX 63 AG9 SER D 210 GLY D 231 1 22
HELIX 64 AH1 LYS D 233 TRP D 236 5 4
HELIX 65 AH2 PRO D 246 ARG D 250 5 5
HELIX 66 AH3 SER D 263 ALA D 286 1 24
HELIX 67 AH4 PRO D 288 ASP D 308 1 21
HELIX 68 AH5 SER D 326 GLY D 333 1 8
HELIX 69 AH6 GLY D 336 LEU D 342 1 7
HELIX 70 AH7 LYS D 370 PHE D 377 1 8
HELIX 71 AH8 PHE D 377 ARG D 388 1 12
HELIX 72 AH9 THR D 393 ARG D 403 1 11
HELIX 73 AI1 GLU D 405 ARG D 417 1 13
HELIX 74 AI2 HIS D 430 LEU D 432 5 3
HELIX 75 AI3 HIS D 450 LEU D 452 5 3
HELIX 76 AI4 VAL D 453 ASN D 458 1 6
HELIX 77 AI5 THR D 473 LEU D 483 1 11
HELIX 78 AI6 MET D 485 ASN D 489 5 5
HELIX 79 AI7 SER D 503 ARG D 515 1 13
HELIX 80 AI8 GLY D 529 SER D 539 1 11
HELIX 81 AI9 VAL D 574 VAL D 583 1 10
HELIX 82 AJ1 PRO D 588 VAL D 592 5 5
HELIX 83 AJ2 GLY D 597 LEU D 612 1 16
HELIX 84 AJ3 GLY D 613 GLY D 636 1 24
HELIX 85 AJ4 GLY D 640 MET D 644 5 5
HELIX 86 AJ5 LYS D 649 SER D 670 1 22
HELIX 87 AJ6 THR D 674 THR D 703 1 30
HELIX 88 AJ7 ASN D 720 GLY D 729 1 10
HELIX 89 AJ8 SER D 733 GLY D 742 1 10
HELIX 90 AJ9 ASN D 768 ALA D 804 1 37
HELIX 91 AK1 PRO D 834 LEU D 840 1 7
HELIX 92 AK2 HIS D 865 SER D 876 1 12
HELIX 93 AK3 ALA D 896 GLY D 900 1 5
HELIX 94 AK4 ALA D 914 ILE D 937 1 24
HELIX 95 AK5 LYS D 1132 GLU D 1146 1 15
HELIX 96 AK6 ALA D 1216 GLY D 1225 1 10
HELIX 97 AK7 GLY D 1225 GLN D 1244 1 20
HELIX 98 AK8 ASN D 1249 LEU D 1261 1 13
HELIX 99 AK9 TYR D 1282 GLY D 1296 1 15
HELIX 100 AL1 GLY D 1308 THR D 1316 1 9
HELIX 101 AL2 SER D 1318 GLN D 1326 1 9
HELIX 102 AL3 GLU D 1327 GLY D 1339 1 13
HELIX 103 AL4 GLY D 1346 GLY D 1354 1 9
HELIX 104 AL5 GLY D 1360 ALA D 1375 1 16
HELIX 105 AL6 VAL E 6 GLY E 14 1 9
HELIX 106 AL7 ASN E 15 GLY E 33 1 19
HELIX 107 AL8 LYS E 45 GLY E 57 1 13
HELIX 108 AL9 ASN E 60 ARG E 91 1 32
HELIX 109 AM1 ALA F 80 ILE F 91 1 12
HELIX 110 AM2 ASP F 96 GLY F 106 1 11
HELIX 111 AM3 GLU F 114 TYR F 137 1 24
HELIX 112 AM4 TYR F 137 GLU F 154 1 18
HELIX 113 AM5 ASP F 160 PHE F 165 1 6
HELIX 114 AM6 ASP F 213 ALA F 237 1 25
HELIX 115 AM7 HIS F 242 GLN F 258 1 17
HELIX 116 AM8 VAL F 262 GLU F 293 1 32
HELIX 117 AM9 PRO F 298 GLU F 310 1 13
HELIX 118 AN1 ASP F 313 ALA F 321 1 9
HELIX 119 AN2 LEU F 330 ASP F 332 5 3
HELIX 120 AN3 VAL F 333 GLY F 352 1 20
HELIX 121 AN4 THR F 354 ASN F 383 1 30
HELIX 122 AN5 ASN F 383 TYR F 394 1 12
HELIX 123 AN6 GLN F 400 PHE F 419 1 20
HELIX 124 AN7 GLU F 420 GLY F 424 5 5
HELIX 125 AN8 LYS F 426 GLN F 446 1 21
HELIX 126 AN9 PRO F 453 GLY F 475 1 23
HELIX 127 AO1 THR F 479 LEU F 488 1 10
HELIX 128 AO2 PRO F 490 ALA F 501 1 12
HELIX 129 AO3 HIS F 518 PHE F 522 5 5
HELIX 130 AO4 LEU F 530 LEU F 551 1 22
HELIX 131 AO5 THR F 552 PHE F 563 1 12
HELIX 132 AO6 THR F 572 ASP F 581 1 10
HELIX 133 AO7 ARG F 584 HIS F 600 1 17
HELIX 134 AO8 HIS F 600 SER F 609 1 10
HELIX 135 AO9 PHE F 610 ASP F 613 5 4
HELIX 136 AP1 GLY G 34 MET G 51 1 18
HELIX 137 AP2 ASP G 77 GLY G 87 1 11
HELIX 138 AP3 ALA G 113 ILE G 115 5 3
HELIX 139 AP4 PRO G 154 SER G 161 1 8
HELIX 140 AP5 ASP G 212 LEU G 234 1 23
HELIX 141 AP6 GLY H 34 MET H 51 1 18
HELIX 142 AP7 ASP H 77 GLY H 87 1 11
HELIX 143 AP8 ALA H 113 ILE H 115 5 3
HELIX 144 AP9 PRO H 154 HIS H 160 1 7
HELIX 145 AQ1 ASP H 212 ASP H 233 1 22
HELIX 146 AQ2 SER I 4 ARG I 10 1 7
HELIX 147 AQ3 LEU I 28 GLU I 40 1 13
HELIX 148 AQ4 TYR I 47 PHE I 57 1 11
HELIX 149 AQ5 ASP I 81 GLY I 89 1 9
HELIX 150 AQ6 ALA I 206 LEU I 213 1 8
HELIX 151 AQ7 THR I 216 PHE I 225 1 10
HELIX 152 AQ8 VAL I 242 LEU I 246 5 5
HELIX 153 AQ9 THR I 270 ASP I 281 1 12
HELIX 154 AR1 SER I 318 GLY I 329 1 12
HELIX 155 AR2 PRO I 345 ASP I 354 1 10
HELIX 156 AR3 ASP I 358 ARG I 371 1 14
HELIX 157 AR4 THR I 377 SER I 391 1 15
HELIX 158 AR5 LEU I 397 LEU I 410 1 14
HELIX 159 AR6 SER I 421 GLY I 438 1 18
HELIX 160 AR7 SER I 455 GLY I 482 1 28
HELIX 161 AR8 MET I 488 ILE I 493 1 6
HELIX 162 AR9 ALA I 495 SER I 509 1 15
HELIX 163 AS1 ASN I 519 ARG I 528 1 10
HELIX 164 AS2 GLY I 544 ASP I 549 1 6
HELIX 165 AS3 HIS I 551 TYR I 555 5 5
HELIX 166 AS4 SER I 607 TYR I 614 1 8
HELIX 167 AS5 ASP I 648 VAL I 650 5 3
HELIX 168 AS6 SER I 656 VAL I 661 5 6
HELIX 169 AS7 SER I 662 ILE I 668 1 7
HELIX 170 AS8 PHE I 670 ASP I 674 5 5
HELIX 171 AS9 ASP I 675 ARG I 687 1 13
HELIX 172 AT1 MET I 704 GLY I 713 1 10
HELIX 173 AT2 GLU I 820 GLU I 825 1 6
HELIX 174 AT3 GLY I 858 LYS I 864 1 7
HELIX 175 AT4 THR I 896 GLY I 907 1 12
HELIX 176 AT5 ASP I 942 VAL I 980 1 39
HELIX 177 AT6 GLU I 985 LEU I 992 1 8
HELIX 178 AT7 GLU I 1005 GLN I 1038 1 34
HELIX 179 AT8 PRO I 1100 VAL I 1103 5 4
HELIX 180 AT9 ILE I 1109 GLN I 1134 1 26
HELIX 181 AU1 GLU I 1137 ASP I 1150 1 14
HELIX 182 AU2 SER I 1165 ARG I 1177 1 13
HELIX 183 AU3 LYS I 1191 GLY I 1202 1 12
HELIX 184 AU4 LEU I 1238 MET I 1243 1 6
HELIX 185 AU5 GLY I 1261 PHE I 1265 5 5
HELIX 186 AU6 GLY I 1271 TYR I 1281 1 11
HELIX 187 AU7 ALA I 1283 THR I 1292 1 10
HELIX 188 AU8 ASP I 1297 ASP I 1310 1 14
HELIX 189 AU9 PRO I 1320 LEU I 1333 1 14
HELIX 190 AV1 SER J 26 TRP J 33 1 8
HELIX 191 AV2 CYS J 58 GLY J 63 1 6
HELIX 192 AV3 GLN J 94 GLU J 100 5 7
HELIX 193 AV4 ILE J 114 SER J 119 1 6
HELIX 194 AV5 SER J 122 LEU J 128 1 7
HELIX 195 AV6 PRO J 131 TYR J 140 1 10
HELIX 196 AV7 THR J 161 GLU J 170 1 10
HELIX 197 AV8 GLY J 181 MET J 192 1 12
HELIX 198 AV9 ASP J 193 THR J 208 1 16
HELIX 199 AW1 SER J 210 GLY J 231 1 22
HELIX 200 AW2 LYS J 233 TRP J 236 5 4
HELIX 201 AW3 PRO J 246 ARG J 250 5 5
HELIX 202 AW4 SER J 263 LEU J 285 1 23
HELIX 203 AW5 PRO J 288 ASN J 309 1 22
HELIX 204 AW6 SER J 326 GLY J 333 1 8
HELIX 205 AW7 GLY J 336 LEU J 342 1 7
HELIX 206 AW8 LYS J 370 PHE J 377 1 8
HELIX 207 AW9 PHE J 377 ARG J 388 1 12
HELIX 208 AX1 THR J 393 ARG J 403 1 11
HELIX 209 AX2 GLU J 405 ARG J 417 1 13
HELIX 210 AX3 HIS J 430 LEU J 432 5 3
HELIX 211 AX4 VAL J 453 ASN J 458 1 6
HELIX 212 AX5 THR J 473 LEU J 483 1 11
HELIX 213 AX6 MET J 485 ASN J 489 5 5
HELIX 214 AX7 SER J 503 ARG J 515 1 13
HELIX 215 AX8 GLY J 529 SER J 539 1 11
HELIX 216 AX9 VAL J 574 VAL J 583 1 10
HELIX 217 AY1 PRO J 588 VAL J 592 5 5
HELIX 218 AY2 GLY J 597 LEU J 612 1 16
HELIX 219 AY3 GLY J 613 GLY J 636 1 24
HELIX 220 AY4 GLY J 640 MET J 644 5 5
HELIX 221 AY5 LYS J 649 GLN J 667 1 19
HELIX 222 AY6 THR J 674 THR J 703 1 30
HELIX 223 AY7 ASN J 720 GLY J 729 1 10
HELIX 224 AY8 SER J 733 GLY J 742 1 10
HELIX 225 AY9 ASN J 768 ALA J 804 1 37
HELIX 226 AZ1 PRO J 834 LEU J 840 1 7
HELIX 227 AZ2 HIS J 865 SER J 876 1 12
HELIX 228 AZ3 ALA J 896 GLY J 900 1 5
HELIX 229 AZ4 ALA J 914 THR J 934 1 21
HELIX 230 AZ5 ASP J 1133 GLU J 1146 1 14
HELIX 231 AZ6 ALA J 1216 GLY J 1225 1 10
HELIX 232 AZ7 GLY J 1225 GLN J 1244 1 20
HELIX 233 AZ8 ASP J 1250 LEU J 1261 1 12
HELIX 234 AZ9 TYR J 1282 ASN J 1295 1 14
HELIX 235 BA1 GLY J 1308 THR J 1316 1 9
HELIX 236 BA2 SER J 1318 GLN J 1326 1 9
HELIX 237 BA3 GLU J 1327 GLY J 1339 1 13
HELIX 238 BA4 GLY J 1346 GLY J 1354 1 9
HELIX 239 BA5 GLY J 1360 ALA J 1375 1 16
HELIX 240 BA6 VAL K 6 GLY K 14 1 9
HELIX 241 BA7 ASN K 15 GLY K 34 1 20
HELIX 242 BA8 LYS K 45 GLU K 56 1 12
HELIX 243 BA9 ASN K 60 ARG K 91 1 32
HELIX 244 BB1 ALA L 80 ILE L 91 1 12
HELIX 245 BB2 ASP L 96 GLY L 106 1 11
HELIX 246 BB3 ARG L 113 TYR L 137 1 25
HELIX 247 BB4 TYR L 137 GLU L 154 1 18
HELIX 248 BB5 ASP L 160 PHE L 165 1 6
HELIX 249 BB6 ASP L 213 ALA L 237 1 25
HELIX 250 BB7 HIS L 242 GLN L 258 1 17
HELIX 251 BB8 VAL L 262 CYS L 295 1 34
HELIX 252 BB9 PRO L 298 ASN L 309 1 12
HELIX 253 BC1 ASP L 313 MET L 322 1 10
HELIX 254 BC2 ASN L 323 GLU L 328 5 6
HELIX 255 BC3 LEU L 330 ASP L 332 5 3
HELIX 256 BC4 VAL L 333 GLY L 352 1 20
HELIX 257 BC5 THR L 354 ASN L 383 1 30
HELIX 258 BC6 ASN L 383 LYS L 393 1 11
HELIX 259 BC7 GLN L 400 PHE L 419 1 20
HELIX 260 BC8 GLU L 420 GLY L 424 5 5
HELIX 261 BC9 LYS L 426 GLN L 446 1 21
HELIX 262 BD1 PRO L 453 GLY L 475 1 23
HELIX 263 BD2 THR L 479 LEU L 488 1 10
HELIX 264 BD3 PRO L 490 LYS L 502 1 13
HELIX 265 BD4 HIS L 518 PHE L 522 5 5
HELIX 266 BD5 LEU L 530 ALA L 549 1 20
HELIX 267 BD6 THR L 552 PHE L 563 1 12
HELIX 268 BD7 THR L 572 ASP L 581 1 10
HELIX 269 BD8 ARG L 584 HIS L 600 1 17
HELIX 270 BD9 SER L 604 PHE L 610 1 7
HELIX 271 BE1 GLY M 34 MET M 51 1 18
HELIX 272 BE2 ASP M 77 GLY M 87 1 11
HELIX 273 BE3 ALA M 113 ILE M 115 5 3
HELIX 274 BE4 PRO M 154 SER M 161 1 8
HELIX 275 BE5 ASP M 212 LEU M 234 1 23
HELIX 276 BE6 GLY N 34 MET N 51 1 18
HELIX 277 BE7 ASP N 77 GLY N 87 1 11
HELIX 278 BE8 ALA N 113 ILE N 115 5 3
HELIX 279 BE9 PRO N 154 SER N 161 1 8
HELIX 280 BF1 ASP N 212 ASP N 233 1 22
HELIX 281 BF2 SER O 4 ARG O 10 1 7
HELIX 282 BF3 LEU O 28 GLU O 40 1 13
HELIX 283 BF4 TYR O 47 PHE O 57 1 11
HELIX 284 BF5 ASP O 81 GLY O 89 1 9
HELIX 285 BF6 ALA O 206 LEU O 213 1 8
HELIX 286 BF7 THR O 216 PHE O 225 1 10
HELIX 287 BF8 VAL O 242 ARG O 247 1 6
HELIX 288 BF9 THR O 270 ASP O 281 1 12
HELIX 289 BG1 SER O 318 GLY O 329 1 12
HELIX 290 BG2 PRO O 345 ASP O 354 1 10
HELIX 291 BG3 ASP O 358 ARG O 371 1 14
HELIX 292 BG4 THR O 377 SER O 391 1 15
HELIX 293 BG5 LEU O 397 LEU O 409 1 13
HELIX 294 BG6 SER O 421 GLY O 438 1 18
HELIX 295 BG7 SER O 455 GLY O 482 1 28
HELIX 296 BG8 MET O 488 ILE O 493 1 6
HELIX 297 BG9 ALA O 495 SER O 509 1 15
HELIX 298 BH1 ASN O 519 ARG O 528 1 10
HELIX 299 BH2 GLY O 544 ASP O 549 1 6
HELIX 300 BH3 HIS O 551 TYR O 555 5 5
HELIX 301 BH4 SER O 607 TYR O 614 1 8
HELIX 302 BH5 ASP O 648 VAL O 650 5 3
HELIX 303 BH6 SER O 656 VAL O 661 5 6
HELIX 304 BH7 SER O 662 ILE O 668 1 7
HELIX 305 BH8 PHE O 670 ASP O 674 5 5
HELIX 306 BH9 ASP O 675 ALA O 689 1 15
HELIX 307 BI1 GLY O 703 GLY O 713 1 11
HELIX 308 BI2 GLU O 820 GLU O 825 1 6
HELIX 309 BI3 GLY O 858 SER O 863 1 6
HELIX 310 BI4 THR O 896 GLY O 907 1 12
HELIX 311 BI5 ASP O 942 VAL O 980 1 39
HELIX 312 BI6 GLU O 985 LEU O 992 1 8
HELIX 313 BI7 GLU O 1006 GLU O 1016 1 11
HELIX 314 BI8 GLU O 1016 GLN O 1038 1 23
HELIX 315 BI9 PRO O 1100 VAL O 1103 5 4
HELIX 316 BJ1 ILE O 1109 GLN O 1134 1 26
HELIX 317 BJ2 GLU O 1137 ASP O 1150 1 14
HELIX 318 BJ3 SER O 1165 ARG O 1177 1 13
HELIX 319 BJ4 LYS O 1191 GLY O 1202 1 12
HELIX 320 BJ5 LEU O 1238 MET O 1243 1 6
HELIX 321 BJ6 GLY O 1271 TYR O 1281 1 11
HELIX 322 BJ7 ALA O 1283 THR O 1292 1 10
HELIX 323 BJ8 ASP O 1297 ASP O 1310 1 14
HELIX 324 BJ9 PRO O 1320 LEU O 1333 1 14
HELIX 325 BK1 SER P 26 TRP P 33 1 8
HELIX 326 BK2 CYS P 58 GLY P 63 1 6
HELIX 327 BK3 GLN P 94 GLU P 100 5 7
HELIX 328 BK4 ILE P 114 SER P 119 1 6
HELIX 329 BK5 SER P 122 LEU P 128 1 7
HELIX 330 BK6 PRO P 131 TYR P 140 1 10
HELIX 331 BK7 THR P 161 GLU P 170 1 10
HELIX 332 BK8 GLY P 181 SER P 191 1 11
HELIX 333 BK9 ASP P 193 THR P 208 1 16
HELIX 334 BL1 SER P 210 GLY P 231 1 22
HELIX 335 BL2 LYS P 233 TRP P 236 5 4
HELIX 336 BL3 PRO P 246 ARG P 250 5 5
HELIX 337 BL4 SER P 263 LEU P 285 1 23
HELIX 338 BL5 PRO P 288 ASP P 308 1 21
HELIX 339 BL6 SER P 326 GLY P 333 1 8
HELIX 340 BL7 GLY P 336 LEU P 342 1 7
HELIX 341 BL8 LYS P 370 PHE P 377 1 8
HELIX 342 BL9 PHE P 377 GLY P 389 1 13
HELIX 343 BM1 THR P 393 GLU P 404 1 12
HELIX 344 BM2 GLU P 405 ARG P 417 1 13
HELIX 345 BM3 HIS P 430 LEU P 432 5 3
HELIX 346 BM4 HIS P 450 LEU P 452 5 3
HELIX 347 BM5 VAL P 453 ASN P 458 1 6
HELIX 348 BM6 THR P 473 LEU P 483 1 11
HELIX 349 BM7 MET P 485 ASN P 489 5 5
HELIX 350 BM8 SER P 503 ARG P 515 1 13
HELIX 351 BM9 GLY P 529 SER P 539 1 11
HELIX 352 BN1 VAL P 574 VAL P 583 1 10
HELIX 353 BN2 PRO P 588 VAL P 592 5 5
HELIX 354 BN3 GLY P 597 LEU P 612 1 16
HELIX 355 BN4 GLY P 613 GLY P 636 1 24
HELIX 356 BN5 LYS P 649 SER P 670 1 22
HELIX 357 BN6 THR P 674 THR P 703 1 30
HELIX 358 BN7 ASN P 720 GLY P 729 1 10
HELIX 359 BN8 SER P 733 GLY P 742 1 10
HELIX 360 BN9 ASN P 768 ALA P 804 1 37
HELIX 361 BO1 PRO P 834 LEU P 840 1 7
HELIX 362 BO2 HIS P 865 SER P 876 1 12
HELIX 363 BO3 ALA P 896 GLY P 900 1 5
HELIX 364 BO4 ALA P 914 HIS P 936 1 23
HELIX 365 BO5 LYS P 1132 GLU P 1146 1 15
HELIX 366 BO6 ALA P 1216 GLY P 1225 1 10
HELIX 367 BO7 GLY P 1225 GLY P 1245 1 21
HELIX 368 BO8 ASN P 1249 LEU P 1261 1 13
HELIX 369 BO9 TYR P 1282 GLY P 1296 1 15
HELIX 370 BP1 GLY P 1308 THR P 1316 1 9
HELIX 371 BP2 SER P 1318 GLN P 1326 1 9
HELIX 372 BP3 GLU P 1327 GLY P 1339 1 13
HELIX 373 BP4 GLY P 1346 GLY P 1354 1 9
HELIX 374 BP5 GLY P 1360 ALA P 1375 1 16
HELIX 375 BP6 VAL Q 6 GLY Q 14 1 9
HELIX 376 BP7 ASN Q 15 VAL Q 32 1 18
HELIX 377 BP8 LYS Q 45 GLY Q 57 1 13
HELIX 378 BP9 ASN Q 60 ARG Q 91 1 32
HELIX 379 BQ1 ALA R 80 ILE R 91 1 12
HELIX 380 BQ2 ASP R 96 GLY R 106 1 11
HELIX 381 BQ3 GLU R 114 TYR R 137 1 24
HELIX 382 BQ4 TYR R 137 GLU R 154 1 18
HELIX 383 BQ5 ASP R 160 PHE R 165 1 6
HELIX 384 BQ6 ASP R 213 ALA R 237 1 25
HELIX 385 BQ7 HIS R 242 GLN R 258 1 17
HELIX 386 BQ8 VAL R 262 CYS R 295 1 34
HELIX 387 BQ9 PRO R 298 ASN R 309 1 12
HELIX 388 BR1 ASP R 313 MET R 322 1 10
HELIX 389 BR2 ASN R 323 GLU R 328 5 6
HELIX 390 BR3 VAL R 333 GLY R 352 1 20
HELIX 391 BR4 THR R 354 ASN R 383 1 30
HELIX 392 BR5 ASN R 383 THR R 395 1 13
HELIX 393 BR6 GLN R 400 PHE R 419 1 20
HELIX 394 BR7 GLU R 420 GLY R 424 5 5
HELIX 395 BR8 LYS R 426 GLN R 446 1 21
HELIX 396 BR9 PRO R 453 GLY R 475 1 23
HELIX 397 BS1 THR R 479 LEU R 488 1 10
HELIX 398 BS2 PRO R 490 ALA R 501 1 12
HELIX 399 BS3 HIS R 518 ILE R 523 5 6
HELIX 400 BS4 LEU R 530 GLY R 550 1 21
HELIX 401 BS5 ALA R 553 GLY R 564 1 12
HELIX 402 BS6 THR R 572 ASP R 581 1 10
HELIX 403 BS7 ARG R 584 HIS R 600 1 17
HELIX 404 BS8 SER R 604 SER R 609 1 6
HELIX 405 BS9 PHE R 610 ASP R 612 5 3
SHEET 1 AA1 4 ARG A 12 GLN A 18 0
SHEET 2 AA1 4 HIS A 23 LEU A 31 -1 O THR A 27 N VAL A 14
SHEET 3 AA1 4 ASP A 199 THR A 207 -1 O ASP A 199 N LEU A 31
SHEET 4 AA1 4 VAL A 180 ALA A 189 -1 N GLU A 188 O LYS A 200
SHEET 1 AA2 5 ILE A 115 THR A 116 0
SHEET 2 AA2 5 GLU A 97 SER A 105 -1 N THR A 101 O THR A 116
SHEET 3 AA2 5 SER A 139 ARG A 150 -1 O VAL A 146 N VAL A 98
SHEET 4 AA2 5 PRO A 52 ILE A 61 -1 N GLY A 53 O GLY A 149
SHEET 5 AA2 5 LEU A 171 LEU A 172 -1 O LEU A 171 N VAL A 59
SHEET 1 AA3 2 VAL A 90 VAL A 92 0
SHEET 2 AA3 2 VAL A 121 ILE A 123 -1 O GLU A 122 N ARG A 91
SHEET 1 AA4 2 GLY A 108 THR A 111 0
SHEET 2 AA4 2 VAL A 129 LEU A 133 -1 O CYS A 131 N VAL A 110
SHEET 1 AA5 2 TYR A 152 VAL A 153 0
SHEET 2 AA5 2 ALA A 175 CYS A 176 -1 O ALA A 175 N VAL A 153
SHEET 1 AA6 4 ARG B 12 GLN B 18 0
SHEET 2 AA6 4 HIS B 23 LEU B 31 -1 O LYS B 25 N GLU B 17
SHEET 3 AA6 4 ASP B 199 THR B 207 -1 O ILE B 203 N VAL B 26
SHEET 4 AA6 4 VAL B 180 ASN B 186 -1 N ALA B 184 O GLU B 204
SHEET 1 AA7 4 GLU B 97 SER B 105 0
SHEET 2 AA7 4 SER B 139 ARG B 150 -1 O ILE B 144 N LEU B 100
SHEET 3 AA7 4 PRO B 52 ILE B 61 -1 N THR B 57 O LYS B 145
SHEET 4 AA7 4 LEU B 171 LEU B 172 -1 O LEU B 171 N VAL B 59
SHEET 1 AA8 2 VAL B 90 ARG B 91 0
SHEET 2 AA8 2 GLU B 122 ILE B 123 -1 O GLU B 122 N ARG B 91
SHEET 1 AA9 2 GLY B 108 THR B 111 0
SHEET 2 AA9 2 VAL B 129 LEU B 133 -1 O CYS B 131 N VAL B 110
SHEET 1 AB1 2 TYR B 152 VAL B 153 0
SHEET 2 AB1 2 ALA B 175 CYS B 176 -1 O ALA B 175 N VAL B 153
SHEET 1 AB2 3 LYS C 13 ASP C 14 0
SHEET 2 AB2 3 ILE C1182 ALA C1183 1 O ALA C1183 N LYS C 13
SHEET 3 AB2 3 VAL C 700 GLY C 701 1 N GLY C 701 O ILE C1182
SHEET 1 AB3 4 ILE C 59 GLN C 60 0
SHEET 2 AB3 4 SER C 66 LEU C 75 -1 O LEU C 68 N ILE C 59
SHEET 3 AB3 4 SER C 93 ILE C 104 -1 O VAL C 103 N GLU C 67
SHEET 4 AB3 4 ASP C 116 PRO C 128 -1 O LYS C 118 N LEU C 102
SHEET 1 AB4 3 PHE C 136 ILE C 138 0
SHEET 2 AB4 3 THR C 141 ILE C 145 -1 O ARG C 143 N PHE C 136
SHEET 3 AB4 3 SER C 512 PHE C 514 -1 O GLN C 513 N VAL C 144
SHEET 1 AB5 4 ARG C 451 ARG C 454 0
SHEET 2 AB5 4 SER C 147 ARG C 151 -1 N GLN C 148 O ARG C 454
SHEET 3 AB5 4 ARG C 529 SER C 531 1 O SER C 531 N LEU C 149
SHEET 4 AB5 4 ILE C 572 SER C 574 -1 O ASN C 573 N ILE C 530
SHEET 1 AB6 5 GLY C 154 ASP C 160 0
SHEET 2 AB6 5 LEU C 171 ILE C 177 -1 O ASN C 173 N ASP C 158
SHEET 3 AB6 5 LEU C 184 PHE C 188 -1 O LEU C 184 N ILE C 176
SHEET 4 AB6 5 LEU C 194 ILE C 198 -1 O PHE C 195 N GLU C 187
SHEET 5 AB6 5 LYS C 203 PRO C 205 -1 O LEU C 204 N VAL C 196
SHEET 1 AB7 3 LYS C 236 MET C 239 0
SHEET 2 AB7 3 VAL C 228 ARG C 233 -1 N GLU C 231 O GLN C 238
SHEET 3 AB7 3 ILE C 333 THR C 335 -1 O THR C 335 N VAL C 228
SHEET 1 AB8 3 GLN C 580 THR C 581 0
SHEET 2 AB8 3 LEU C 587 THR C 595 -1 O GLU C 588 N GLN C 580
SHEET 3 AB8 3 VAL C 598 LEU C 606 -1 O HIS C 604 N TYR C 591
SHEET 1 AB9 6 GLN C 580 THR C 581 0
SHEET 2 AB9 6 LEU C 587 THR C 595 -1 O GLU C 588 N GLN C 580
SHEET 3 AB9 6 TYR C 652 MET C 653 -1 O MET C 653 N ARG C 592
SHEET 4 AB9 6 VAL C 615 ALA C 617 1 N ALA C 617 O TYR C 652
SHEET 5 AB9 6 LEU C 633 SER C 638 -1 O ARG C 637 N ILE C 616
SHEET 6 AB9 6 GLU C 641 SER C 646 -1 O PHE C 645 N VAL C 634
SHEET 1 AC1 3 ALA C 716 VAL C 717 0
SHEET 2 AC1 3 VAL C 782 ASP C 785 -1 O LEU C 783 N ALA C 716
SHEET 3 AC1 3 MET C 768 PRO C 769 -1 N MET C 768 O ASP C 785
SHEET 1 AC2 4 ILE C 748 ASN C 752 0
SHEET 2 AC2 4 ARG C 731 VAL C 736 -1 N ILE C 734 O ASP C 749
SHEET 3 AC2 4 GLY C 722 VAL C 727 -1 N TYR C 726 O VAL C 733
SHEET 4 AC2 4 PRO C 776 VAL C 777 -1 O VAL C 777 N GLY C 722
SHEET 1 AC3 2 THR C 757 ARG C 758 0
SHEET 2 AC3 2 CYS C 764 ILE C 765 -1 O ILE C 765 N THR C 757
SHEET 1 AC4 8 GLN C1209 ILE C1210 0
SHEET 2 AC4 8 VAL C1225 LYS C1234 -1 O VAL C1225 N ILE C1210
SHEET 3 AC4 8 LYS C1065 ALA C1067 -1 N ALA C1067 O LEU C1233
SHEET 4 AC4 8 LYS C1073 ASN C1080 -1 O GLY C1074 N MET C1066
SHEET 5 AC4 8 ILE C 816 SER C 819 1 N ILE C 816 O VAL C1075
SHEET 6 AC4 8 ILE C1096 LEU C1098 -1 O VAL C1097 N LEU C 817
SHEET 7 AC4 8 GLN C 798 PHE C 804 1 N ALA C 803 O ILE C1096
SHEET 8 AC4 8 VAL C1225 LYS C1234 -1 O MET C1232 N GLN C 798
SHEET 1 AC5 5 GLY C 846 PRO C 847 0
SHEET 2 AC5 5 THR C 830 THR C 843 -1 N THR C 843 O GLY C 846
SHEET 3 AC5 5 VAL C1046 ARG C1058 -1 O LYS C1048 N SER C 840
SHEET 4 AC5 5 GLY C 926 PHE C 934 -1 N GLN C 932 O LYS C1051
SHEET 5 AC5 5 GLU C 876 VAL C 877 -1 N VAL C 877 O GLY C 926
SHEET 1 AC6 2 ILE C 882 VAL C 884 0
SHEET 2 AC6 2 LEU C 918 ARG C 919 -1 O LEU C 918 N LEU C 883
SHEET 1 AC7 2 VAL C 887 PRO C 889 0
SHEET 2 AC7 2 VAL C 913 ASP C 915 -1 O LYS C 914 N THR C 888
SHEET 1 AC8 2 TYR C1087 ASP C1088 0
SHEET 2 AC8 2 LEU C1212 TYR C1213 -1 O TYR C1213 N TYR C1087
SHEET 1 AC9 8 HIS C1244 ARG C1246 0
SHEET 2 AC9 8 SER D 350 VAL D 357 -1 O SER D 350 N ARG C1246
SHEET 3 AC9 8 GLN D 465 HIS D 469 -1 O VAL D 468 N GLY D 351
SHEET 4 AC9 8 VAL D 421 ASN D 424 -1 N LEU D 422 O HIS D 469
SHEET 5 AC9 8 ILE D 434 ILE D 442 -1 O GLN D 435 N LEU D 423
SHEET 6 AC9 8 GLN D 365 PRO D 369 1 N CYS D 366 O VAL D 440
SHEET 7 AC9 8 ILE D 447 LEU D 449 -1 O GLN D 448 N GLY D 367
SHEET 8 AC9 8 SER D 350 VAL D 357 1 N THR D 356 O LEU D 449
SHEET 1 AD1 2 ARG C1269 PHE C1270 0
SHEET 2 AD1 2 LYS D 345 ARG D 346 -1 O LYS D 345 N PHE C1270
SHEET 1 AD2 3 ILE C1335 ASP C1341 0
SHEET 2 AD2 3 PHE D 17 LEU D 24 -1 O ASP D 18 N GLU C1340
SHEET 3 AD2 3 ARG D1341 ASP D1342 -1 O ASP D1342 N ILE D 20
SHEET 1 AD3 3 SER D 34 GLU D 37 0
SHEET 2 AD3 3 MET D 102 ALA D 112 1 O MET D 102 N PHE D 35
SHEET 3 AD3 3 ILE D 238 VAL D 244 -1 O LEU D 239 N THR D 111
SHEET 1 AD4 3 GLN D 158 LEU D 160 0
SHEET 2 AD4 3 TYR D 144 GLY D 149 -1 N TYR D 144 O LEU D 160
SHEET 3 AD4 3 PHE D 176 LYS D 179 -1 O LYS D 179 N VAL D 145
SHEET 1 AD5 3 LEU D 252 PRO D 254 0
SHEET 2 AD5 3 PHE D 260 THR D 262 -1 O ALA D 261 N VAL D 253
SHEET 3 AD5 3 ILE F 505 SER F 506 1 O ILE F 505 N THR D 262
SHEET 1 AD6 3 VAL D 526 LEU D 527 0
SHEET 2 AD6 3 ARG D 547 GLU D 554 1 O LYS D 549 N LEU D 527
SHEET 3 AD6 3 LYS D 566 THR D 573 -1 O LYS D 566 N GLU D 554
SHEET 1 AD7 2 VAL D 809 GLU D 811 0
SHEET 2 AD7 2 VAL D 894 CYS D 895 1 O VAL D 894 N THR D 810
SHEET 1 AD8 2 ILE D 820 MET D 822 0
SHEET 2 AD8 2 VAL D 880 VAL D 882 -1 O VAL D 882 N ILE D 820
SHEET 1 AD9 2 SER D 949 GLN D 951 0
SHEET 2 AD9 2 THR D1016 ASN D1019 -1 O ALA D1018 N ILE D 950
SHEET 1 AE1 2 VAL D 966 VAL D 967 0
SHEET 2 AE1 2 LEU D 973 VAL D 974 -1 O VAL D 974 N VAL D 966
SHEET 1 AE2 2 PRO D1026 ILE D1028 0
SHEET 2 AE2 2 THR D1120 ARG D1123 -1 O LEU D1121 N VAL D1027
SHEET 1 AE3 3 ILE D1080 VAL D1081 0
SHEET 2 AE3 3 GLY D1033 VAL D1035 -1 N PHE D1034 O VAL D1081
SHEET 3 AE3 3 GLN D1114 ILE D1115 -1 O ILE D1115 N GLY D1033
SHEET 1 AE4 3 ILE D1046 GLN D1049 0
SHEET 2 AE4 3 SER D1058 VAL D1061 -1 O SER D1058 N GLN D1049
SHEET 3 AE4 3 ILE D1106 VAL D1107 -1 O VAL D1107 N LEU D1059
SHEET 1 AE5 3 VAL D1163 SER D1164 0
SHEET 2 AE5 3 ARG D1174 ILE D1177 -1 O VAL D1176 N SER D1164
SHEET 3 AE5 3 GLU D1188 MET D1189 -1 O GLU D1188 N LEU D1175
SHEET 1 AE6 3 GLU D1276 GLU D1281 0
SHEET 2 AE6 3 LYS D1263 VAL D1267 -1 N ALA D1264 O VAL D1280
SHEET 3 AE6 3 THR D1301 ARG D1304 -1 O THR D1301 N VAL D1267
SHEET 1 AE7 4 ARG G 12 GLN G 18 0
SHEET 2 AE7 4 HIS G 23 LEU G 31 -1 O THR G 27 N ASP G 15
SHEET 3 AE7 4 ASP G 199 THR G 207 -1 O LEU G 201 N LEU G 28
SHEET 4 AE7 4 VAL G 180 ALA G 189 -1 N ALA G 184 O GLU G 204
SHEET 1 AE8 4 GLU G 97 SER G 105 0
SHEET 2 AE8 4 SER G 139 ARG G 150 -1 O VAL G 146 N VAL G 98
SHEET 3 AE8 4 PRO G 52 ILE G 61 -1 N THR G 57 O LYS G 145
SHEET 4 AE8 4 ARG G 170 LEU G 172 -1 O LEU G 171 N VAL G 59
SHEET 1 AE9 2 VAL G 90 VAL G 92 0
SHEET 2 AE9 2 VAL G 121 ILE G 123 -1 O GLU G 122 N ARG G 91
SHEET 1 AF1 2 GLY G 108 THR G 111 0
SHEET 2 AF1 2 VAL G 129 LEU G 133 -1 O CYS G 131 N VAL G 110
SHEET 1 AF2 2 TYR G 152 VAL G 153 0
SHEET 2 AF2 2 ALA G 175 CYS G 176 -1 O ALA G 175 N VAL G 153
SHEET 1 AF3 4 ARG H 12 GLU H 17 0
SHEET 2 AF3 4 HIS H 23 LEU H 31 -1 O LYS H 25 N GLU H 17
SHEET 3 AF3 4 ASP H 199 THR H 207 -1 O ILE H 203 N VAL H 26
SHEET 4 AF3 4 VAL H 180 ASN H 186 -1 N ARG H 182 O GLU H 206
SHEET 1 AF4 4 GLU H 97 SER H 105 0
SHEET 2 AF4 4 SER H 139 ARG H 150 -1 O VAL H 146 N VAL H 98
SHEET 3 AF4 4 PRO H 52 ILE H 61 -1 N THR H 57 O LYS H 145
SHEET 4 AF4 4 ARG H 170 LEU H 172 -1 O LEU H 171 N VAL H 59
SHEET 1 AF5 2 VAL H 90 VAL H 92 0
SHEET 2 AF5 2 VAL H 121 ILE H 123 -1 O GLU H 122 N ARG H 91
SHEET 1 AF6 2 GLY H 108 THR H 111 0
SHEET 2 AF6 2 VAL H 129 LEU H 133 -1 O LEU H 133 N GLY H 108
SHEET 1 AF7 2 TYR H 152 VAL H 153 0
SHEET 2 AF7 2 ALA H 175 CYS H 176 -1 O ALA H 175 N VAL H 153
SHEET 1 AF8 3 LYS I 13 ASP I 14 0
SHEET 2 AF8 3 ILE I1182 ALA I1183 1 O ALA I1183 N LYS I 13
SHEET 3 AF8 3 VAL I 700 GLY I 701 1 N GLY I 701 O ILE I1182
SHEET 1 AF9 4 ILE I 59 GLN I 60 0
SHEET 2 AF9 4 SER I 66 LEU I 75 -1 O LEU I 68 N ILE I 59
SHEET 3 AF9 4 SER I 93 ILE I 104 -1 O LYS I 99 N SER I 72
SHEET 4 AF9 4 ASP I 116 PRO I 128 -1 O LYS I 118 N LEU I 102
SHEET 1 AG1 3 PHE I 136 ILE I 138 0
SHEET 2 AG1 3 THR I 141 ILE I 145 -1 O ARG I 143 N PHE I 136
SHEET 3 AG1 3 SER I 512 PHE I 514 -1 O GLN I 513 N VAL I 144
SHEET 1 AG2 4 ARG I 451 ARG I 454 0
SHEET 2 AG2 4 SER I 147 ARG I 151 -1 N GLN I 148 O ARG I 454
SHEET 3 AG2 4 ARG I 529 SER I 531 1 O SER I 531 N LEU I 149
SHEET 4 AG2 4 ASN I 573 SER I 574 -1 O ASN I 573 N ILE I 530
SHEET 1 AG3 5 GLY I 154 ASP I 160 0
SHEET 2 AG3 5 LEU I 171 ILE I 177 -1 O ASN I 173 N ASP I 158
SHEET 3 AG3 5 LEU I 184 PHE I 188 -1 O PHE I 186 N ALA I 174
SHEET 4 AG3 5 LEU I 194 ILE I 198 -1 O PHE I 195 N GLU I 187
SHEET 5 AG3 5 LYS I 203 PRO I 205 -1 O LEU I 204 N VAL I 196
SHEET 1 AG4 4 LEU I 284 VAL I 287 0
SHEET 2 AG4 4 LYS I 236 GLU I 240 -1 N MET I 239 O ILE I 285
SHEET 3 AG4 4 LYS I 227 ARG I 233 -1 N ILE I 229 O GLU I 240
SHEET 4 AG4 4 GLU I 334 LEU I 336 -1 O THR I 335 N VAL I 228
SHEET 1 AG5 2 TYR I 301 ILE I 302 0
SHEET 2 AG5 2 LEU I 309 CYS I 311 -1 O CYS I 311 N TYR I 301
SHEET 1 AG6 3 GLN I 580 THR I 581 0
SHEET 2 AG6 3 LEU I 587 THR I 595 -1 O GLU I 588 N GLN I 580
SHEET 3 AG6 3 VAL I 598 LEU I 606 -1 O LEU I 606 N THR I 589
SHEET 1 AG7 6 GLN I 580 THR I 581 0
SHEET 2 AG7 6 LEU I 587 THR I 595 -1 O GLU I 588 N GLN I 580
SHEET 3 AG7 6 TYR I 652 ASP I 654 -1 O MET I 653 N ARG I 592
SHEET 4 AG7 6 ILE I 616 ALA I 617 1 N ALA I 617 O TYR I 652
SHEET 5 AG7 6 LEU I 633 SER I 638 -1 O ARG I 637 N ILE I 616
SHEET 6 AG7 6 GLU I 641 SER I 646 -1 O PHE I 645 N VAL I 634
SHEET 1 AG8 3 ALA I 716 VAL I 717 0
SHEET 2 AG8 3 VAL I 782 ASP I 785 -1 O LEU I 783 N ALA I 716
SHEET 3 AG8 3 MET I 768 PRO I 769 -1 N MET I 768 O ASP I 785
SHEET 1 AG9 4 ILE I 748 ASN I 752 0
SHEET 2 AG9 4 ARG I 731 VAL I 736 -1 N ILE I 734 O ASP I 749
SHEET 3 AG9 4 GLY I 721 VAL I 727 -1 N TYR I 726 O VAL I 733
SHEET 4 AG9 4 PRO I 776 GLU I 778 -1 O VAL I 777 N GLY I 722
SHEET 1 AH1 2 THR I 757 ARG I 758 0
SHEET 2 AH1 2 CYS I 764 ILE I 765 -1 O ILE I 765 N THR I 757
SHEET 1 AH2 8 GLN I1209 ILE I1210 0
SHEET 2 AH2 8 VAL I1225 LYS I1234 -1 O VAL I1225 N ILE I1210
SHEET 3 AH2 8 LYS I1065 ALA I1067 -1 N ALA I1067 O LEU I1233
SHEET 4 AH2 8 LYS I1073 ASN I1080 -1 O GLY I1074 N MET I1066
SHEET 5 AH2 8 ILE I 816 SER I 819 1 N ILE I 816 O SER I1077
SHEET 6 AH2 8 ILE I1096 LEU I1098 -1 O VAL I1097 N LEU I 817
SHEET 7 AH2 8 GLN I 798 PHE I 804 1 N ALA I 803 O ILE I1096
SHEET 8 AH2 8 VAL I1225 LYS I1234 -1 O GLY I1228 N VAL I 802
SHEET 1 AH3 5 GLY I 846 PRO I 847 0
SHEET 2 AH3 5 THR I 830 THR I 843 -1 N THR I 843 O GLY I 846
SHEET 3 AH3 5 VAL I1046 ARG I1058 -1 O VAL I1052 N LEU I 836
SHEET 4 AH3 5 GLY I 926 THR I 935 -1 N THR I 927 O ALA I1055
SHEET 5 AH3 5 GLU I 876 VAL I 877 -1 N VAL I 877 O GLY I 926
SHEET 1 AH4 2 ILE I 882 VAL I 884 0
SHEET 2 AH4 2 LEU I 918 ARG I 919 -1 O LEU I 918 N LEU I 883
SHEET 1 AH5 2 VAL I 887 THR I 888 0
SHEET 2 AH5 2 LYS I 914 ASP I 915 -1 O LYS I 914 N THR I 888
SHEET 1 AH6 2 TYR I1087 ASP I1088 0
SHEET 2 AH6 2 LEU I1212 TYR I1213 -1 O TYR I1213 N TYR I1087
SHEET 1 AH7 8 HIS I1244 ARG I1246 0
SHEET 2 AH7 8 SER J 350 VAL J 357 -1 O SER J 350 N ARG I1246
SHEET 3 AH7 8 GLN J 465 HIS J 469 -1 O VAL J 468 N GLY J 351
SHEET 4 AH7 8 VAL J 421 ASN J 424 -1 N LEU J 422 O HIS J 469
SHEET 5 AH7 8 ILE J 434 ILE J 442 -1 O GLN J 435 N LEU J 423
SHEET 6 AH7 8 GLN J 365 PRO J 369 1 N CYS J 366 O VAL J 440
SHEET 7 AH7 8 ILE J 447 LEU J 449 -1 O GLN J 448 N GLY J 367
SHEET 8 AH7 8 SER J 350 VAL J 357 1 N THR J 356 O LEU J 449
SHEET 1 AH8 2 ARG I1269 PHE I1270 0
SHEET 2 AH8 2 LYS J 345 ARG J 346 -1 O LYS J 345 N PHE I1270
SHEET 1 AH9 3 ILE I1335 ASP I1341 0
SHEET 2 AH9 3 PHE J 17 LEU J 24 -1 O ALA J 19 N GLU I1340
SHEET 3 AH9 3 ARG J1341 ASP J1342 -1 O ASP J1342 N ILE J 20
SHEET 1 AI1 3 SER J 34 GLU J 37 0
SHEET 2 AI1 3 MET J 102 ALA J 112 1 O MET J 102 N PHE J 35
SHEET 3 AI1 3 ILE J 238 VAL J 244 -1 O LEU J 239 N THR J 111
SHEET 1 AI2 3 ILE J 159 LEU J 160 0
SHEET 2 AI2 3 TYR J 144 GLY J 149 -1 N TYR J 144 O LEU J 160
SHEET 3 AI2 3 PHE J 176 LYS J 179 -1 O LYS J 179 N VAL J 145
SHEET 1 AI3 3 LEU J 252 PRO J 254 0
SHEET 2 AI3 3 PHE J 260 THR J 262 -1 O ALA J 261 N VAL J 253
SHEET 3 AI3 3 ILE L 505 SER L 506 1 O ILE L 505 N PHE J 260
SHEET 1 AI4 3 MET J 525 THR J 528 0
SHEET 2 AI4 3 ARG J 547 LYS J 557 1 O LYS J 549 N LEU J 527
SHEET 3 AI4 3 LEU J 563 THR J 573 -1 O THR J 572 N VAL J 548
SHEET 1 AI5 2 VAL J 809 GLU J 811 0
SHEET 2 AI5 2 VAL J 894 CYS J 895 1 O VAL J 894 N THR J 810
SHEET 1 AI6 2 ILE J 820 MET J 822 0
SHEET 2 AI6 2 VAL J 880 VAL J 882 -1 O VAL J 882 N ILE J 820
SHEET 1 AI7 2 SER J 949 GLN J 951 0
SHEET 2 AI7 2 THR J1016 ASN J1019 -1 O VAL J1017 N ILE J 950
SHEET 1 AI8 2 GLY J 956 SER J 957 0
SHEET 2 AI8 2 GLN J1010 VAL J1011 -1 O VAL J1011 N GLY J 956
SHEET 1 AI9 2 SER J 965 VAL J 967 0
SHEET 2 AI9 2 LEU J 973 ILE J 975 -1 O VAL J 974 N VAL J 966
SHEET 1 AJ1 2 THR J 980 LEU J 982 0
SHEET 2 AJ1 2 TYR J 995 VAL J 997 -1 O TYR J 995 N LEU J 982
SHEET 1 AJ2 2 MET J1025 ILE J1028 0
SHEET 2 AJ2 2 THR J1120 ILE J1124 -1 O ILE J1124 N MET J1025
SHEET 1 AJ3 2 PHE J1034 THR J1038 0
SHEET 2 AJ3 2 ALA J1077 VAL J1081 -1 O VAL J1081 N PHE J1034
SHEET 1 AJ4 2 GLN J1049 THR J1050 0
SHEET 2 AJ4 2 SER J1057 SER J1058 -1 O SER J1058 N GLN J1049
SHEET 1 AJ5 3 ILE J1162 PHE J1165 0
SHEET 2 AJ5 3 ARG J1174 THR J1178 -1 O VAL J1176 N SER J1164
SHEET 3 AJ5 3 TYR J1186 MET J1189 -1 O GLU J1188 N LEU J1175
SHEET 1 AJ6 3 GLN J1279 GLU J1281 0
SHEET 2 AJ6 3 LYS J1263 VAL J1267 -1 N ALA J1264 O VAL J1280
SHEET 3 AJ6 3 THR J1301 ARG J1304 -1 O THR J1301 N VAL J1267
SHEET 1 AJ7 2 ASN L 169 ALA L 170 0
SHEET 2 AJ7 2 PHE L 259 ARG L 260 -1 O ARG L 260 N ASN L 169
SHEET 1 AJ8 4 ARG M 12 GLN M 18 0
SHEET 2 AJ8 4 HIS M 23 LEU M 31 -1 O LYS M 25 N GLU M 17
SHEET 3 AJ8 4 ASP M 199 THR M 207 -1 O LEU M 201 N LEU M 28
SHEET 4 AJ8 4 VAL M 180 ALA M 189 -1 N GLU M 188 O LYS M 200
SHEET 1 AJ9 4 GLU M 97 SER M 105 0
SHEET 2 AJ9 4 SER M 139 ARG M 150 -1 O ILE M 144 N LEU M 100
SHEET 3 AJ9 4 PRO M 52 ILE M 61 -1 N THR M 57 O LYS M 145
SHEET 4 AJ9 4 ARG M 170 LEU M 172 -1 O LEU M 171 N VAL M 59
SHEET 1 AK1 2 VAL M 90 VAL M 92 0
SHEET 2 AK1 2 VAL M 121 ILE M 123 -1 O GLU M 122 N ARG M 91
SHEET 1 AK2 2 GLY M 108 THR M 111 0
SHEET 2 AK2 2 VAL M 129 LEU M 133 -1 O CYS M 131 N VAL M 110
SHEET 1 AK3 2 TYR M 152 VAL M 153 0
SHEET 2 AK3 2 ALA M 175 CYS M 176 -1 O ALA M 175 N VAL M 153
SHEET 1 AK4 4 ARG N 12 GLN N 18 0
SHEET 2 AK4 4 HIS N 23 LEU N 31 -1 O LYS N 25 N GLU N 17
SHEET 3 AK4 4 ASP N 199 THR N 207 -1 O ILE N 203 N VAL N 26
SHEET 4 AK4 4 VAL N 180 ASN N 186 -1 N ARG N 182 O GLU N 206
SHEET 1 AK5 4 GLU N 97 SER N 105 0
SHEET 2 AK5 4 SER N 139 ARG N 150 -1 O ILE N 144 N LEU N 100
SHEET 3 AK5 4 PRO N 52 ILE N 61 -1 N THR N 57 O LYS N 145
SHEET 4 AK5 4 ARG N 170 LEU N 172 -1 O LEU N 171 N VAL N 59
SHEET 1 AK6 2 VAL N 90 VAL N 92 0
SHEET 2 AK6 2 VAL N 121 ILE N 123 -1 O GLU N 122 N ARG N 91
SHEET 1 AK7 2 GLY N 108 THR N 111 0
SHEET 2 AK7 2 VAL N 129 LEU N 133 -1 O CYS N 131 N VAL N 110
SHEET 1 AK8 2 TYR N 152 VAL N 153 0
SHEET 2 AK8 2 ALA N 175 CYS N 176 -1 O ALA N 175 N VAL N 153
SHEET 1 AK9 3 LYS O 13 ASP O 14 0
SHEET 2 AK9 3 ILE O1182 ALA O1183 1 O ALA O1183 N LYS O 13
SHEET 3 AK9 3 VAL O 700 GLY O 701 1 N GLY O 701 O ILE O1182
SHEET 1 AL1 4 ILE O 59 GLN O 60 0
SHEET 2 AL1 4 SER O 66 LEU O 75 -1 O LEU O 68 N ILE O 59
SHEET 3 AL1 4 SER O 93 ILE O 104 -1 O VAL O 103 N GLU O 67
SHEET 4 AL1 4 ASP O 116 PRO O 128 -1 O LYS O 118 N LEU O 102
SHEET 1 AL2 3 PHE O 136 ILE O 138 0
SHEET 2 AL2 3 THR O 141 ILE O 145 -1 O THR O 141 N ILE O 138
SHEET 3 AL2 3 SER O 512 PHE O 514 -1 O GLN O 513 N VAL O 144
SHEET 1 AL3 5 ARG O 451 ARG O 454 0
SHEET 2 AL3 5 SER O 147 ARG O 151 -1 N GLN O 148 O ARG O 454
SHEET 3 AL3 5 ARG O 529 SER O 531 1 O SER O 531 N LEU O 149
SHEET 4 AL3 5 ILE O 572 LEU O 575 -1 O ASN O 573 N ILE O 530
SHEET 5 AL3 5 VAL O 558 CYS O 559 -1 N CYS O 559 O SER O 574
SHEET 1 AL4 5 GLY O 154 SER O 159 0
SHEET 2 AL4 5 TYR O 172 ILE O 177 -1 O ASN O 173 N ASP O 158
SHEET 3 AL4 5 LEU O 184 PHE O 188 -1 O PHE O 186 N ALA O 174
SHEET 4 AL4 5 LEU O 194 ILE O 198 -1 O PHE O 195 N GLU O 187
SHEET 5 AL4 5 LYS O 203 PRO O 205 -1 O LEU O 204 N VAL O 196
SHEET 1 AL5 4 ILE O 285 VAL O 287 0
SHEET 2 AL5 4 LYS O 236 MET O 239 -1 N LEU O 237 O VAL O 287
SHEET 3 AL5 4 VAL O 228 ARG O 233 -1 N GLU O 231 O GLN O 238
SHEET 4 AL5 4 ARG O 332 THR O 335 -1 O ILE O 333 N PHE O 230
SHEET 1 AL6 2 ILE O 255 GLU O 256 0
SHEET 2 AL6 2 VAL O 261 VAL O 263 -1 O TYR O 262 N ILE O 255
SHEET 1 AL7 2 VAL O 296 VAL O 297 0
SHEET 2 AL7 2 MET O 315 GLU O 316 -1 O MET O 315 N VAL O 297
SHEET 1 AL8 2 TYR O 301 ILE O 302 0
SHEET 2 AL8 2 LEU O 309 CYS O 311 -1 O CYS O 311 N TYR O 301
SHEET 1 AL9 3 GLN O 580 THR O 581 0
SHEET 2 AL9 3 LEU O 587 THR O 595 -1 O GLU O 588 N GLN O 580
SHEET 3 AL9 3 VAL O 598 LEU O 606 -1 O HIS O 604 N TYR O 591
SHEET 1 AM1 6 GLN O 580 THR O 581 0
SHEET 2 AM1 6 LEU O 587 THR O 595 -1 O GLU O 588 N GLN O 580
SHEET 3 AM1 6 TYR O 652 ASP O 654 -1 O MET O 653 N ARG O 592
SHEET 4 AM1 6 ILE O 616 ALA O 617 1 N ALA O 617 O TYR O 652
SHEET 5 AM1 6 LEU O 633 SER O 638 -1 O ARG O 637 N ILE O 616
SHEET 6 AM1 6 GLU O 641 SER O 646 -1 O PHE O 645 N VAL O 634
SHEET 1 AM2 3 ALA O 716 VAL O 717 0
SHEET 2 AM2 3 VAL O 782 ASP O 785 -1 O LEU O 783 N ALA O 716
SHEET 3 AM2 3 MET O 768 PRO O 769 -1 N MET O 768 O ASP O 785
SHEET 1 AM3 4 ILE O 748 ASN O 752 0
SHEET 2 AM3 4 ARG O 731 VAL O 736 -1 N ILE O 732 O TYR O 751
SHEET 3 AM3 4 GLY O 721 VAL O 727 -1 N VAL O 723 O LYS O 735
SHEET 4 AM3 4 PRO O 776 GLU O 778 -1 O VAL O 777 N GLY O 722
SHEET 1 AM4 2 THR O 757 ARG O 758 0
SHEET 2 AM4 2 CYS O 764 ILE O 765 -1 O ILE O 765 N THR O 757
SHEET 1 AM5 2 THR O 789 ASP O 790 0
SHEET 2 AM5 2 GLU O 793 LEU O 794 -1 O GLU O 793 N ASP O 790
SHEET 1 AM6 8 GLN O1209 ILE O1210 0
SHEET 2 AM6 8 VAL O1225 LYS O1234 -1 O VAL O1225 N ILE O1210
SHEET 3 AM6 8 LYS O1065 ALA O1067 -1 N ALA O1067 O LEU O1233
SHEET 4 AM6 8 LYS O1073 ASN O1080 -1 O GLY O1074 N MET O1066
SHEET 5 AM6 8 ILE O 816 SER O 819 1 N ILE O 816 O VAL O1075
SHEET 6 AM6 8 ILE O1096 LEU O1098 -1 O VAL O1097 N LEU O 817
SHEET 7 AM6 8 GLN O 798 PHE O 804 1 N ALA O 803 O ILE O1096
SHEET 8 AM6 8 VAL O1225 LYS O1234 -1 O MET O1232 N GLN O 798
SHEET 1 AM7 5 GLY O 846 PRO O 847 0
SHEET 2 AM7 5 THR O 830 THR O 843 -1 N THR O 843 O GLY O 846
SHEET 3 AM7 5 VAL O1046 ARG O1058 -1 O VAL O1052 N LEU O 836
SHEET 4 AM7 5 GLY O 926 THR O 935 -1 N GLN O 932 O LYS O1051
SHEET 5 AM7 5 GLU O 876 VAL O 877 -1 N VAL O 877 O GLY O 926
SHEET 1 AM8 2 ILE O 882 VAL O 884 0
SHEET 2 AM8 2 LEU O 918 ARG O 919 -1 O LEU O 918 N LEU O 883
SHEET 1 AM9 2 VAL O 887 PRO O 889 0
SHEET 2 AM9 2 VAL O 913 ASP O 915 -1 O LYS O 914 N THR O 888
SHEET 1 AN1 8 HIS O1244 ARG O1246 0
SHEET 2 AN1 8 SER P 350 VAL P 357 -1 O SER P 350 N ARG O1246
SHEET 3 AN1 8 GLN P 465 HIS P 469 -1 O VAL P 468 N GLY P 351
SHEET 4 AN1 8 VAL P 421 ASN P 424 -1 N LEU P 422 O HIS P 469
SHEET 5 AN1 8 ILE P 434 ILE P 442 -1 O GLN P 435 N LEU P 423
SHEET 6 AN1 8 GLN P 365 PRO P 369 1 N CYS P 366 O VAL P 440
SHEET 7 AN1 8 ILE P 447 LEU P 449 -1 O GLN P 448 N GLY P 367
SHEET 8 AN1 8 SER P 350 VAL P 357 1 N THR P 356 O LEU P 449
SHEET 1 AN2 2 ARG O1269 PHE O1270 0
SHEET 2 AN2 2 LYS P 345 ARG P 346 -1 O LYS P 345 N PHE O1270
SHEET 1 AN3 3 ILE O1335 ASP O1341 0
SHEET 2 AN3 3 PHE P 17 LEU P 24 -1 O ASP P 18 N GLU O1340
SHEET 3 AN3 3 ARG P1341 ASP P1342 -1 O ASP P1342 N ILE P 20
SHEET 1 AN4 3 SER P 34 GLU P 37 0
SHEET 2 AN4 3 MET P 102 ALA P 112 1 O MET P 102 N PHE P 35
SHEET 3 AN4 3 ILE P 238 VAL P 244 -1 O LEU P 239 N THR P 111
SHEET 1 AN5 3 ILE P 159 LEU P 160 0
SHEET 2 AN5 3 TYR P 144 GLY P 149 -1 N TYR P 144 O LEU P 160
SHEET 3 AN5 3 PHE P 176 LYS P 179 -1 O LYS P 179 N VAL P 145
SHEET 1 AN6 3 LEU P 252 PRO P 254 0
SHEET 2 AN6 3 PHE P 260 THR P 262 -1 O ALA P 261 N VAL P 253
SHEET 3 AN6 3 ILE R 505 SER R 506 1 O ILE R 505 N PHE P 260
SHEET 1 AN7 3 MET P 525 LEU P 527 0
SHEET 2 AN7 3 ARG P 547 LYS P 557 1 O LYS P 549 N LEU P 527
SHEET 3 AN7 3 LEU P 563 THR P 573 -1 O LYS P 570 N VAL P 550
SHEET 1 AN8 2 GLU P 704 VAL P 706 0
SHEET 2 AN8 2 LYS P 715 VAL P 717 -1 O GLN P 716 N THR P 705
SHEET 1 AN9 2 VAL P 809 GLU P 811 0
SHEET 2 AN9 2 VAL P 894 CYS P 895 1 O VAL P 894 N THR P 810
SHEET 1 AO1 2 ILE P 820 MET P 822 0
SHEET 2 AO1 2 VAL P 880 VAL P 882 -1 O VAL P 882 N ILE P 820
SHEET 1 AO2 2 SER P 965 VAL P 966 0
SHEET 2 AO2 2 VAL P 974 ILE P 975 -1 O VAL P 974 N VAL P 966
SHEET 1 AO3 2 GLU P 981 LEU P 982 0
SHEET 2 AO3 2 TYR P 995 LYS P 996 -1 O TYR P 995 N LEU P 982
SHEET 1 AO4 2 MET P1025 ILE P1028 0
SHEET 2 AO4 2 THR P1120 ILE P1124 -1 O LEU P1121 N VAL P1027
SHEET 1 AO5 3 PHE P1034 THR P1038 0
SHEET 2 AO5 3 ALA P1077 VAL P1081 -1 O VAL P1081 N PHE P1034
SHEET 3 AO5 3 GLN P1098 TYR P1099 -1 O TYR P1099 N LEU P1078
SHEET 1 AO6 2 ILE P1046 THR P1047 0
SHEET 2 AO6 2 VAL P1060 VAL P1061 -1 O VAL P1060 N THR P1047
SHEET 1 AO7 4 TYR P1186 MET P1189 0
SHEET 2 AO7 4 ARG P1174 THR P1178 -1 N ILE P1177 O TYR P1186
SHEET 3 AO7 4 GLY P1161 PHE P1165 -1 N SER P1164 O VAL P1176
SHEET 4 AO7 4 ARG P1203 VAL P1204 -1 O VAL P1204 N GLY P1161
SHEET 1 AO8 3 GLU P1276 GLU P1281 0
SHEET 2 AO8 3 LYS P1263 VAL P1267 -1 N ILE P1266 O GLY P1277
SHEET 3 AO8 3 THR P1301 ARG P1304 -1 O THR P1301 N VAL P1267
SSBOND 1 CYS D 85 CYS D 88 1555 1555 2.81
SSBOND 2 CYS J 85 CYS J 88 1555 1555 2.90
SSBOND 3 CYS P 70 CYS P 88 1555 1555 2.40
SSBOND 4 CYS P 85 CYS P 88 1555 1555 2.76
LINK SG CYS D 70 ZN ZN D1501 1555 1555 2.83
LINK SG CYS D 72 ZN ZN D1501 1555 1555 2.01
LINK SG CYS D 85 ZN ZN D1501 1555 1555 2.26
LINK SG CYS D 88 ZN ZN D1501 1555 1555 1.96
LINK OD1 ASP D 460 MG MG D1503 1555 1555 2.18
LINK OD1 ASP D 462 MG MG D1503 1555 1555 2.39
LINK OD1 ASP D 464 MG MG D1503 1555 1555 2.22
LINK OD2 ASP D 464 MG MG D1503 1555 1555 2.78
LINK SG CYS D 814 ZN ZN D1502 1555 1555 2.03
LINK SG CYS D 895 ZN ZN D1502 1555 1555 2.45
LINK SG CYS D 898 ZN ZN D1502 1555 1555 2.35
LINK O3' GTP 3 13 P A 3 14 1555 1555 1.61
LINK O3' U 3 16 MG MG D1503 1555 1555 1.91
LINK OP1 C 3 17 MG MG D1503 1555 1555 2.16
LINK SG CYS J 70 ZN ZN J1501 1555 1555 2.70
LINK SG CYS J 72 ZN ZN J1501 1555 1555 2.65
LINK SG CYS J 85 ZN ZN J1501 1555 1555 2.57
LINK SG CYS J 88 ZN ZN J1501 1555 1555 1.98
LINK OD1 ASP J 460 MG MG J1503 1555 1555 2.67
LINK OD2 ASP J 460 MG MG J1503 1555 1555 2.79
LINK OD1 ASP J 462 MG MG J1503 1555 1555 2.28
LINK OD2 ASP J 462 MG MG J1503 1555 1555 2.87
LINK NH2 ARG J 883 ZN ZN J1502 1555 1555 2.63
LINK SG CYS J 888 ZN ZN J1502 1555 1555 2.66
LINK SG CYS J 895 ZN ZN J1502 1555 1555 2.66
LINK SG CYS J 898 ZN ZN J1502 1555 1555 2.29
LINK O3' GTP 6 13 P A 6 14 1555 1555 1.60
LINK O3' U 6 16 MG MG J1503 1555 1555 2.54
LINK SG CYS P 85 ZN ZN P1501 1555 1555 2.69
LINK OD2 ASP P 460 MG MG P1503 1555 1555 2.36
LINK OD1 ASP P 462 MG MG P1503 1555 1555 2.96
LINK SG CYS P 814 ZN ZN P1502 1555 1555 1.95
LINK SG CYS P 888 ZN ZN P1502 1555 1555 2.41
LINK SG CYS P 895 ZN ZN P1502 1555 1555 2.80
LINK O3' GTP 9 13 P A 9 14 1555 1555 1.59
LINK OP1 C 9 17 MG MG P1503 1555 1555 2.59
CISPEP 1 GLU A 29 PRO A 30 0 -3.41
CISPEP 2 GLU B 29 PRO B 30 0 -11.89
CISPEP 3 PHE C 57 PRO C 58 0 2.16
CISPEP 4 LEU D 120 PRO D 121 0 -1.01
CISPEP 5 ALA D 426 PRO D 427 0 -0.30
CISPEP 6 GLU G 29 PRO G 30 0 -2.13
CISPEP 7 GLU H 29 PRO H 30 0 -17.21
CISPEP 8 PHE I 57 PRO I 58 0 -21.11
CISPEP 9 LEU J 120 PRO J 121 0 1.34
CISPEP 10 ALA J 426 PRO J 427 0 0.06
CISPEP 11 GLU M 29 PRO M 30 0 -8.62
CISPEP 12 GLU N 29 PRO N 30 0 -7.28
CISPEP 13 PHE O 57 PRO O 58 0 -8.96
CISPEP 14 LEU P 120 PRO P 121 0 1.70
CISPEP 15 ALA P 426 PRO P 427 0 0.70
SITE 1 AC1 4 CYS D 70 CYS D 72 CYS D 85 CYS D 88
SITE 1 AC2 6 CYS D 814 ARG D 883 CYS D 888 THR D 890
SITE 2 AC2 6 CYS D 895 CYS D 898
SITE 1 AC3 5 U 3 16 C 3 17 ASP D 460 ASP D 462
SITE 2 AC3 5 ASP D 464
SITE 1 AC4 5 CYS J 70 CYS J 72 GLY J 73 CYS J 85
SITE 2 AC4 5 CYS J 88
SITE 1 AC5 6 CYS J 814 THR J 816 ARG J 883 CYS J 888
SITE 2 AC5 6 CYS J 895 CYS J 898
SITE 1 AC6 6 U 6 16 C 6 17 LYS I1073 ASP J 460
SITE 2 AC6 6 ASP J 462 ASP J 464
SITE 1 AC7 5 CYS P 70 CYS P 72 LYS P 74 CYS P 85
SITE 2 AC7 5 CYS P 88
SITE 1 AC8 5 CYS P 814 ARG P 883 CYS P 888 CYS P 895
SITE 2 AC8 5 CYS P 898
SITE 1 AC9 4 C 9 17 ARG O1106 ASP P 460 ASP P 462
SITE 1 AD1 11 DT 2 15 DC 2 16 DG 2 17 G 3 15
SITE 2 AD1 11 ARG C 529 ASN C 568 ILE C 572 ARG C 687
SITE 3 AD1 11 GLN C 688 HIS C1237 ASP F 514
SITE 1 AD2 11 DC 5 16 DG 5 17 G 6 15 GLN I 510
SITE 2 AD2 11 ARG I 529 ARG I 540 PRO I 564 ARG I 687
SITE 3 AD2 11 GLN I 688 HIS I1237 ASP L 514
SITE 1 AD3 9 DC 8 16 G 9 15 GLN O 513 ARG O 529
SITE 2 AD3 9 ARG O 540 PRO O 564 ASN O 568 ASP R 513
SITE 3 AD3 9 ASP R 514
CRYST1 237.674 204.988 248.838 90.00 116.86 90.00 P 1 21 1 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 0.004207 0.000000 0.002130 0.00000
SCALE2 0.000000 0.004878 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004505 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
