HEADER HYDROLASE 01-SEP-08 3ECQ
TITLE ENDO-ALPHA-N-ACETYLGALACTOSAMINIDASE FROM STREPTOCOCCUS PNEUMONIAE:
TITLE 2 SEMET STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ENDO-ALPHA-N-ACETYLGALACTOSAMINIDASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 40-1567;
COMPND 5 SYNONYM: PROTEIN SPR0328;
COMPND 6 EC: 3.2.1.97;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOCOCCUS PNEUMONIAE;
SOURCE 3 ORGANISM_TAXID: 171101;
SOURCE 4 STRAIN: R6;
SOURCE 5 GENE: SPR0328;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PCWORI+
KEYWDS DISTORTED (BETA/ALPHA)8 (TIM) BARREL GLYCOSIDE HYDROLASE DOMAIN, CELL
KEYWDS 2 WALL, PEPTIDOGLYCAN-ANCHOR, SECRETED, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.E.C.CAINES,H.ZHU,M.VUCKOVIC,N.C.J.STRYNADKA
REVDAT 5 13-JUL-11 3ECQ 1 VERSN
REVDAT 4 09-JUN-09 3ECQ 1 REVDAT
REVDAT 3 24-FEB-09 3ECQ 1 VERSN
REVDAT 2 30-DEC-08 3ECQ 1 JRNL
REVDAT 1 09-SEP-08 3ECQ 0
JRNL AUTH M.E.CAINES,H.ZHU,M.VUCKOVIC,L.M.WILLIS,S.G.WITHERS,
JRNL AUTH 2 W.W.WAKARCHUK,N.C.STRYNADKA
JRNL TITL THE STRUCTURAL BASIS FOR T-ANTIGEN HYDROLYSIS BY
JRNL TITL 2 STREPTOCOCCUS PNEUMONIAE: A TARGET FOR STRUCTURE-BASED
JRNL TITL 3 VACCINE DESIGN.
JRNL REF J.BIOL.CHEM. V. 283 31279 2008
JRNL REFN ISSN 0021-9258
JRNL PMID 18784084
JRNL DOI 10.1074/JBC.C800150200
REMARK 2
REMARK 2 RESOLUTION. 2.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD WITH PHASES
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 112.51
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 83381
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) : 0.192
REMARK 3 R VALUE (WORKING SET) : 0.190
REMARK 3 FREE R VALUE : 0.235
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4164
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.98
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5616
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.46
REMARK 3 BIN R VALUE (WORKING SET) : 0.3510
REMARK 3 BIN FREE R VALUE SET COUNT : 298
REMARK 3 BIN FREE R VALUE : 0.4030
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 21250
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 18
REMARK 3 SOLVENT ATOMS : 97
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 71.87
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 57.32
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.99000
REMARK 3 B22 (A**2) : 0.91000
REMARK 3 B33 (A**2) : 0.08000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.360
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.268
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 30.846
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.941
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.907
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 21735 ; 0.010 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 14463 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 29429 ; 1.225 ; 1.926
REMARK 3 BOND ANGLES OTHERS (DEGREES): 35240 ; 0.823 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2679 ; 6.587 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 1091 ;38.550 ;25.087
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 3681 ;16.777 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 94 ;18.645 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 3139 ; 0.071 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 24571 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 4427 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 4296 ; 0.207 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 14667 ; 0.189 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 10506 ; 0.186 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 12015 ; 0.086 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 555 ; 0.136 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): 1 ; 0.022 ; 0.200
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 18 ; 0.187 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 15 ; 0.125 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 45 ; 0.168 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 3 ; 0.331 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 13241 ; 0.286 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 5536 ; 0.080 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 21276 ; 0.625 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 8901 ; 1.313 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 8152 ; 2.069 ; 4.500
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 7
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 122 A 307 2
REMARK 3 1 B 122 B 307 2
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 1080 ; 0.030 ; 0.050
REMARK 3 MEDIUM POSITIONAL 1 A (A): 1366 ; 0.410 ; 0.500
REMARK 3 TIGHT THERMAL 1 A (A**2): 1080 ; 0.030 ; 0.500
REMARK 3 MEDIUM THERMAL 1 A (A**2): 1366 ; 0.200 ; 2.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 2
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 330 A 354 2
REMARK 3 1 B 330 B 354 2
REMARK 3 2 A 360 A 601 2
REMARK 3 2 B 360 B 601 2
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 2 A (A): 1578 ; 0.030 ; 0.050
REMARK 3 MEDIUM POSITIONAL 2 A (A): 1938 ; 0.340 ; 0.500
REMARK 3 TIGHT THERMAL 2 A (A**2): 1578 ; 0.040 ; 0.500
REMARK 3 MEDIUM THERMAL 2 A (A**2): 1938 ; 0.280 ; 2.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 3
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 6
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 602 A 655 2
REMARK 3 1 B 602 B 655 2
REMARK 3 2 A 661 A 721 2
REMARK 3 2 B 661 B 721 2
REMARK 3 3 A 730 A 796 2
REMARK 3 3 B 730 B 796 2
REMARK 3 4 A 800 A 808 2
REMARK 3 4 B 800 B 808 2
REMARK 3 5 A 818 A 859 2
REMARK 3 5 B 818 B 859 2
REMARK 3 6 A 874 A 893 2
REMARK 3 6 B 874 B 893 2
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 3 A (A): 1481 ; 0.040 ; 0.050
REMARK 3 MEDIUM POSITIONAL 3 A (A): 1927 ; 0.330 ; 0.500
REMARK 3 TIGHT THERMAL 3 A (A**2): 1481 ; 0.050 ; 0.500
REMARK 3 MEDIUM THERMAL 3 A (A**2): 1927 ; 0.320 ; 2.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 4
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 2
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 894 A 907 2
REMARK 3 1 B 894 B 907 2
REMARK 3 2 A 914 A 1043 2
REMARK 3 2 B 914 B 1043 2
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 4 A (A): 851 ; 0.030 ; 0.050
REMARK 3 MEDIUM POSITIONAL 4 A (A): 1119 ; 0.320 ; 0.500
REMARK 3 TIGHT THERMAL 4 A (A**2): 851 ; 0.040 ; 0.500
REMARK 3 MEDIUM THERMAL 4 A (A**2): 1119 ; 0.260 ; 2.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 5
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 1058 A 1213 2
REMARK 3 1 B 1058 B 1213 2
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 5 A (A): 923 ; 0.030 ; 0.050
REMARK 3 MEDIUM POSITIONAL 5 A (A): 1098 ; 0.360 ; 0.500
REMARK 3 TIGHT THERMAL 5 A (A**2): 923 ; 0.050 ; 0.500
REMARK 3 MEDIUM THERMAL 5 A (A**2): 1098 ; 0.310 ; 2.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 6
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 2
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 1214 A 1339 2
REMARK 3 1 B 1214 B 1339 2
REMARK 3 2 A 1349 A 1417 2
REMARK 3 2 B 1349 B 1417 2
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 6 A (A): 1143 ; 0.030 ; 0.050
REMARK 3 MEDIUM POSITIONAL 6 A (A): 1456 ; 0.280 ; 0.500
REMARK 3 TIGHT THERMAL 6 A (A**2): 1143 ; 0.050 ; 0.500
REMARK 3 MEDIUM THERMAL 6 A (A**2): 1456 ; 0.310 ; 2.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 7
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 2
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 1421 A 1434 2
REMARK 3 1 B 1421 B 1434 2
REMARK 3 2 A 1451 A 1476 2
REMARK 3 2 B 1451 B 1476 2
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 7 A (A): 239 ; 0.030 ; 0.050
REMARK 3 MEDIUM POSITIONAL 7 A (A): 277 ; 0.430 ; 0.500
REMARK 3 TIGHT THERMAL 7 A (A**2): 239 ; 0.030 ; 0.500
REMARK 3 MEDIUM THERMAL 7 A (A**2): 277 ; 0.200 ; 2.000
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 14
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 119 A 307
REMARK 3 ORIGIN FOR THE GROUP (A): 54.7330 62.3063 13.1170
REMARK 3 T TENSOR
REMARK 3 T11: 0.0717 T22: -0.0694
REMARK 3 T33: -0.0809 T12: 0.1583
REMARK 3 T13: 0.1009 T23: -0.0179
REMARK 3 L TENSOR
REMARK 3 L11: 3.2285 L22: 6.7896
REMARK 3 L33: 4.4139 L12: -0.1150
REMARK 3 L13: -1.1668 L23: -1.1069
REMARK 3 S TENSOR
REMARK 3 S11: 0.1301 S12: 0.2391 S13: 0.0967
REMARK 3 S21: 0.1149 S22: 0.0326 S23: 0.7406
REMARK 3 S31: -0.5430 S32: -0.3907 S33: -0.1628
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 319 A 601
REMARK 3 ORIGIN FOR THE GROUP (A): 85.9593 41.4699 33.2672
REMARK 3 T TENSOR
REMARK 3 T11: -0.2172 T22: -0.1376
REMARK 3 T33: 0.2329 T12: -0.0037
REMARK 3 T13: -0.0270 T23: -0.2635
REMARK 3 L TENSOR
REMARK 3 L11: 1.6930 L22: 1.2298
REMARK 3 L33: 1.3906 L12: 0.3101
REMARK 3 L13: -0.3832 L23: 0.2578
REMARK 3 S TENSOR
REMARK 3 S11: 0.0709 S12: -0.1837 S13: 0.1288
REMARK 3 S21: 0.0482 S22: 0.1041 S23: -0.5938
REMARK 3 S31: -0.1656 S32: 0.3898 S33: -0.1750
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 602 A 893
REMARK 3 ORIGIN FOR THE GROUP (A): 58.1285 28.2216 19.3914
REMARK 3 T TENSOR
REMARK 3 T11: -0.1598 T22: -0.2092
REMARK 3 T33: -0.1054 T12: 0.0455
REMARK 3 T13: 0.0558 T23: -0.0939
REMARK 3 L TENSOR
REMARK 3 L11: 0.3338 L22: 0.9337
REMARK 3 L33: 1.1946 L12: 0.1881
REMARK 3 L13: -0.3617 L23: 0.6113
REMARK 3 S TENSOR
REMARK 3 S11: 0.0620 S12: 0.1630 S13: 0.0279
REMARK 3 S21: -0.1556 S22: 0.0645 S23: -0.0217
REMARK 3 S31: -0.0348 S32: -0.3328 S33: -0.1265
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 894 A 1057
REMARK 3 ORIGIN FOR THE GROUP (A): 73.6327 21.9381 -3.4228
REMARK 3 T TENSOR
REMARK 3 T11: -0.0904 T22: -0.1148
REMARK 3 T33: -0.0382 T12: 0.0338
REMARK 3 T13: 0.2284 T23: -0.1632
REMARK 3 L TENSOR
REMARK 3 L11: 1.4312 L22: 1.8535
REMARK 3 L33: 1.6646 L12: 0.1047
REMARK 3 L13: 0.4260 L23: 1.2585
REMARK 3 S TENSOR
REMARK 3 S11: 0.0681 S12: 0.2473 S13: -0.0721
REMARK 3 S21: -0.3509 S22: 0.1310 S23: -0.5428
REMARK 3 S31: -0.0705 S32: 0.2723 S33: -0.1991
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1058 A 1213
REMARK 3 ORIGIN FOR THE GROUP (A): 34.8646 10.8131 3.8767
REMARK 3 T TENSOR
REMARK 3 T11: -0.1689 T22: -0.2081
REMARK 3 T33: -0.3605 T12: -0.1057
REMARK 3 T13: 0.0900 T23: -0.0948
REMARK 3 L TENSOR
REMARK 3 L11: 1.9329 L22: 1.7905
REMARK 3 L33: 1.8811 L12: -0.6788
REMARK 3 L13: -0.7256 L23: 0.0104
REMARK 3 S TENSOR
REMARK 3 S11: 0.0216 S12: 0.2941 S13: -0.1049
REMARK 3 S21: -0.2257 S22: 0.0716 S23: -0.1876
REMARK 3 S31: 0.2866 S32: -0.0826 S33: -0.0932
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1214 A 1417
REMARK 3 ORIGIN FOR THE GROUP (A): 23.9635 29.5415 20.2595
REMARK 3 T TENSOR
REMARK 3 T11: -0.2839 T22: -0.1326
REMARK 3 T33: -0.2854 T12: -0.0110
REMARK 3 T13: 0.1307 T23: -0.0214
REMARK 3 L TENSOR
REMARK 3 L11: 1.5321 L22: 1.8526
REMARK 3 L33: 2.0770 L12: 0.3666
REMARK 3 L13: 0.1455 L23: 0.7639
REMARK 3 S TENSOR
REMARK 3 S11: 0.0139 S12: -0.0252 S13: 0.2152
REMARK 3 S21: 0.1069 S22: -0.0193 S23: 0.2545
REMARK 3 S31: -0.0137 S32: -0.4422 S33: 0.0055
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1418 A 1476
REMARK 3 ORIGIN FOR THE GROUP (A): -1.0814 32.0645 20.4993
REMARK 3 T TENSOR
REMARK 3 T11: 0.0169 T22: 0.3738
REMARK 3 T33: 0.3690 T12: 0.0931
REMARK 3 T13: 0.1267 T23: 0.0768
REMARK 3 L TENSOR
REMARK 3 L11: 12.2032 L22: 9.7960
REMARK 3 L33: 14.0906 L12: 1.7120
REMARK 3 L13: 1.1614 L23: 10.2931
REMARK 3 S TENSOR
REMARK 3 S11: -0.5038 S12: 0.1376 S13: 1.1371
REMARK 3 S21: -0.4793 S22: 0.0127 S23: 0.3492
REMARK 3 S31: -1.0693 S32: -0.9605 S33: 0.4911
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 122 B 307
REMARK 3 ORIGIN FOR THE GROUP (A): 49.4068 23.1371 -43.5874
REMARK 3 T TENSOR
REMARK 3 T11: 0.3712 T22: 0.3353
REMARK 3 T33: 0.5600 T12: 0.1132
REMARK 3 T13: -0.0587 T23: -0.1292
REMARK 3 L TENSOR
REMARK 3 L11: 2.6081 L22: 3.4333
REMARK 3 L33: 3.2038 L12: 1.1827
REMARK 3 L13: 0.3446 L23: 0.9031
REMARK 3 S TENSOR
REMARK 3 S11: 0.0125 S12: 0.2775 S13: -0.6135
REMARK 3 S21: 0.5005 S22: 0.1150 S23: -0.6857
REMARK 3 S31: 0.2735 S32: 0.4725 S33: -0.1275
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 318 B 601
REMARK 3 ORIGIN FOR THE GROUP (A): 21.1809 45.1892 -22.9321
REMARK 3 T TENSOR
REMARK 3 T11: -0.1684 T22: -0.1637
REMARK 3 T33: -0.1557 T12: -0.0339
REMARK 3 T13: 0.0033 T23: -0.0031
REMARK 3 L TENSOR
REMARK 3 L11: 2.2836 L22: 1.9585
REMARK 3 L33: 2.0708 L12: 0.2269
REMARK 3 L13: -0.1171 L23: -1.2713
REMARK 3 S TENSOR
REMARK 3 S11: -0.0511 S12: 0.0574 S13: 0.0066
REMARK 3 S21: -0.1764 S22: 0.0835 S23: 0.3615
REMARK 3 S31: 0.3337 S32: -0.4042 S33: -0.0325
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 602 B 893
REMARK 3 ORIGIN FOR THE GROUP (A): 49.7098 58.0662 -36.2605
REMARK 3 T TENSOR
REMARK 3 T11: -0.1211 T22: -0.0816
REMARK 3 T33: -0.1295 T12: 0.0548
REMARK 3 T13: -0.0055 T23: 0.0608
REMARK 3 L TENSOR
REMARK 3 L11: 0.8699 L22: 2.2155
REMARK 3 L33: 1.6034 L12: 0.6634
REMARK 3 L13: 0.1050 L23: -1.3324
REMARK 3 S TENSOR
REMARK 3 S11: 0.0436 S12: 0.3798 S13: 0.0178
REMARK 3 S21: -0.2786 S22: -0.0972 S23: -0.4999
REMARK 3 S31: 0.0492 S32: 0.4611 S33: 0.0536
REMARK 3
REMARK 3 TLS GROUP : 11
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 894 B 1057
REMARK 3 ORIGIN FOR THE GROUP (A): 34.4872 65.6795 -58.7807
REMARK 3 T TENSOR
REMARK 3 T11: 0.1077 T22: 0.2622
REMARK 3 T33: -0.1114 T12: -0.0343
REMARK 3 T13: -0.1591 T23: 0.2551
REMARK 3 L TENSOR
REMARK 3 L11: 2.5919 L22: 2.1848
REMARK 3 L33: 2.1782 L12: 1.2710
REMARK 3 L13: -0.8669 L23: -1.3652
REMARK 3 S TENSOR
REMARK 3 S11: -0.2196 S12: 0.8195 S13: 0.5824
REMARK 3 S21: -0.6476 S22: 0.4060 S23: 0.4572
REMARK 3 S31: 0.3461 S32: -0.5118 S33: -0.1864
REMARK 3
REMARK 3 TLS GROUP : 12
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 1058 B 1213
REMARK 3 ORIGIN FOR THE GROUP (A): 73.7950 74.9191 -51.1443
REMARK 3 T TENSOR
REMARK 3 T11: -0.1119 T22: -0.1649
REMARK 3 T33: -0.2604 T12: -0.0455
REMARK 3 T13: 0.0817 T23: -0.0149
REMARK 3 L TENSOR
REMARK 3 L11: 1.6910 L22: 1.6015
REMARK 3 L33: 1.6509 L12: -0.9035
REMARK 3 L13: 0.3902 L23: 0.4254
REMARK 3 S TENSOR
REMARK 3 S11: 0.1770 S12: 0.3904 S13: -0.0932
REMARK 3 S21: -0.2500 S22: 0.1939 S23: 0.1606
REMARK 3 S31: -0.3791 S32: 0.0594 S33: -0.3709
REMARK 3
REMARK 3 TLS GROUP : 13
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 1214 B 1417
REMARK 3 ORIGIN FOR THE GROUP (A): 83.6644 55.0316 -35.5462
REMARK 3 T TENSOR
REMARK 3 T11: -0.2831 T22: -0.1740
REMARK 3 T33: 0.0706 T12: -0.0281
REMARK 3 T13: -0.1734 T23: -0.1051
REMARK 3 L TENSOR
REMARK 3 L11: 2.2754 L22: 1.4421
REMARK 3 L33: 2.3926 L12: 0.5348
REMARK 3 L13: -0.2841 L23: -0.6129
REMARK 3 S TENSOR
REMARK 3 S11: 0.3007 S12: 0.0389 S13: -0.6923
REMARK 3 S21: 0.0605 S22: 0.0765 S23: -0.2889
REMARK 3 S31: 0.1358 S32: 0.2629 S33: -0.3772
REMARK 3
REMARK 3 TLS GROUP : 14
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 1418 B 1481
REMARK 3 ORIGIN FOR THE GROUP (A): 106.5463 45.9045 -38.6047
REMARK 3 T TENSOR
REMARK 3 T11: 0.0535 T22: 0.5470
REMARK 3 T33: 0.3985 T12: 0.1289
REMARK 3 T13: -0.2203 T23: -0.3460
REMARK 3 L TENSOR
REMARK 3 L11: 6.7846 L22: 7.7689
REMARK 3 L33: 5.4419 L12: -0.6010
REMARK 3 L13: -0.8573 L23: -2.2425
REMARK 3 S TENSOR
REMARK 3 S11: 0.0706 S12: 0.5610 S13: -1.0351
REMARK 3 S21: -0.6792 S22: -0.1737 S23: 0.4653
REMARK 3 S31: 0.7789 S32: 0.2558 S33: 0.1031
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:
REMARK 3 HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
REMARK 3 THE ATOM RECORDS CONTAIN FULL B-FACTORS.
REMARK 3 THE ANISOU RECORDS RESULT FROM TLS REFINEMENT
REMARK 4
REMARK 4 3ECQ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-SEP-08.
REMARK 100 THE RCSB ID CODE IS RCSB049158.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-SEP-06
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.2.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL, SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 83445
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900
REMARK 200 RESOLUTION RANGE LOW (A) : 112.509
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 6.800
REMARK 200 R MERGE (I) : 0.11000
REMARK 200 R SYM (I) : 0.11000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.1300
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.06
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.4
REMARK 200 DATA REDUNDANCY IN SHELL : 6.30
REMARK 200 R MERGE FOR SHELL (I) : 0.59200
REMARK 200 R SYM FOR SHELL (I) : 0.59200
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.93
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.73
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 29% (W/V) PEG MME 2000, 0.2 M LITHIUM
REMARK 280 CITRATE, 0.1 M AMMONIUM ACETATE, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 294K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 105.30550
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 79.10450
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 105.30550
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 79.10450
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A 37
REMARK 465 SER A 38
REMARK 465 MSE A 39
REMARK 465 SER A 40
REMARK 465 VAL A 41
REMARK 465 GLN A 42
REMARK 465 SER A 43
REMARK 465 GLY A 44
REMARK 465 SER A 45
REMARK 465 THR A 46
REMARK 465 ALA A 47
REMARK 465 ASN A 48
REMARK 465 LEU A 49
REMARK 465 PRO A 50
REMARK 465 ALA A 51
REMARK 465 ASP A 52
REMARK 465 LEU A 53
REMARK 465 ALA A 54
REMARK 465 THR A 55
REMARK 465 ALA A 56
REMARK 465 LEU A 57
REMARK 465 ALA A 58
REMARK 465 THR A 59
REMARK 465 ALA A 60
REMARK 465 LYS A 61
REMARK 465 GLU A 62
REMARK 465 ASN A 63
REMARK 465 ASP A 64
REMARK 465 GLY A 65
REMARK 465 HIS A 66
REMARK 465 ASP A 67
REMARK 465 PHE A 68
REMARK 465 GLU A 69
REMARK 465 ALA A 70
REMARK 465 PRO A 71
REMARK 465 LYS A 72
REMARK 465 VAL A 73
REMARK 465 GLY A 74
REMARK 465 GLU A 75
REMARK 465 ASP A 76
REMARK 465 GLN A 77
REMARK 465 GLY A 78
REMARK 465 SER A 79
REMARK 465 PRO A 80
REMARK 465 GLU A 81
REMARK 465 VAL A 82
REMARK 465 THR A 83
REMARK 465 ASP A 84
REMARK 465 GLY A 85
REMARK 465 PRO A 86
REMARK 465 LYS A 87
REMARK 465 THR A 88
REMARK 465 GLU A 89
REMARK 465 GLU A 90
REMARK 465 GLU A 91
REMARK 465 LEU A 92
REMARK 465 LEU A 93
REMARK 465 ALA A 94
REMARK 465 LEU A 95
REMARK 465 GLU A 96
REMARK 465 LYS A 97
REMARK 465 GLU A 98
REMARK 465 LYS A 99
REMARK 465 PRO A 100
REMARK 465 ALA A 101
REMARK 465 GLU A 102
REMARK 465 GLU A 103
REMARK 465 LYS A 104
REMARK 465 PRO A 105
REMARK 465 LYS A 106
REMARK 465 GLU A 107
REMARK 465 ASP A 108
REMARK 465 LYS A 109
REMARK 465 PRO A 110
REMARK 465 ALA A 111
REMARK 465 ALA A 112
REMARK 465 ALA A 113
REMARK 465 LYS A 114
REMARK 465 PRO A 115
REMARK 465 GLU A 116
REMARK 465 THR A 117
REMARK 465 PRO A 118
REMARK 465 GLY A 308
REMARK 465 VAL A 309
REMARK 465 LYS A 310
REMARK 465 THR A 311
REMARK 465 GLU A 312
REMARK 465 ASP A 313
REMARK 465 THR A 314
REMARK 465 PRO A 315
REMARK 465 ALA A 316
REMARK 465 GLU A 317
REMARK 465 LYS A 318
REMARK 465 THR A 1440
REMARK 465 ASN A 1441
REMARK 465 TYR A 1442
REMARK 465 THR A 1443
REMARK 465 LYS A 1444
REMARK 465 GLU A 1445
REMARK 465 SER A 1446
REMARK 465 MSE A 1447
REMARK 465 ASP A 1448
REMARK 465 ALA A 1449
REMARK 465 LEU A 1450
REMARK 465 GLU A 1477
REMARK 465 ALA A 1478
REMARK 465 LEU A 1479
REMARK 465 LYS A 1480
REMARK 465 ASN A 1481
REMARK 465 ALA A 1482
REMARK 465 LEU A 1483
REMARK 465 VAL A 1484
REMARK 465 GLN A 1485
REMARK 465 LYS A 1486
REMARK 465 LYS A 1487
REMARK 465 THR A 1488
REMARK 465 ALA A 1489
REMARK 465 LEU A 1490
REMARK 465 VAL A 1491
REMARK 465 ALA A 1492
REMARK 465 ASP A 1493
REMARK 465 ASP A 1494
REMARK 465 PHE A 1495
REMARK 465 ALA A 1496
REMARK 465 SER A 1497
REMARK 465 LEU A 1498
REMARK 465 THR A 1499
REMARK 465 ALA A 1500
REMARK 465 PRO A 1501
REMARK 465 ALA A 1502
REMARK 465 GLN A 1503
REMARK 465 ALA A 1504
REMARK 465 GLN A 1505
REMARK 465 GLU A 1506
REMARK 465 GLY A 1507
REMARK 465 LEU A 1508
REMARK 465 ALA A 1509
REMARK 465 ASN A 1510
REMARK 465 ALA A 1511
REMARK 465 PHE A 1512
REMARK 465 ASP A 1513
REMARK 465 GLY A 1514
REMARK 465 ASN A 1515
REMARK 465 LEU A 1516
REMARK 465 SER A 1517
REMARK 465 SER A 1518
REMARK 465 LEU A 1519
REMARK 465 TRP A 1520
REMARK 465 HIS A 1521
REMARK 465 THR A 1522
REMARK 465 SER A 1523
REMARK 465 TRP A 1524
REMARK 465 GLY A 1525
REMARK 465 GLY A 1526
REMARK 465 GLY A 1527
REMARK 465 ASP A 1528
REMARK 465 VAL A 1529
REMARK 465 GLY A 1530
REMARK 465 LYS A 1531
REMARK 465 PRO A 1532
REMARK 465 ALA A 1533
REMARK 465 THR A 1534
REMARK 465 MSE A 1535
REMARK 465 VAL A 1536
REMARK 465 LEU A 1537
REMARK 465 LYS A 1538
REMARK 465 GLU A 1539
REMARK 465 ALA A 1540
REMARK 465 THR A 1541
REMARK 465 GLU A 1542
REMARK 465 ILE A 1543
REMARK 465 THR A 1544
REMARK 465 GLY A 1545
REMARK 465 LEU A 1546
REMARK 465 ARG A 1547
REMARK 465 TYR A 1548
REMARK 465 VAL A 1549
REMARK 465 PRO A 1550
REMARK 465 ARG A 1551
REMARK 465 GLY A 1552
REMARK 465 SER A 1553
REMARK 465 GLY A 1554
REMARK 465 SER A 1555
REMARK 465 ASN A 1556
REMARK 465 GLY A 1557
REMARK 465 ASN A 1558
REMARK 465 LEU A 1559
REMARK 465 ARG A 1560
REMARK 465 ASP A 1561
REMARK 465 VAL A 1562
REMARK 465 LYS A 1563
REMARK 465 LEU A 1564
REMARK 465 VAL A 1565
REMARK 465 VAL A 1566
REMARK 465 THR A 1567
REMARK 465 GLY B 37
REMARK 465 SER B 38
REMARK 465 MSE B 39
REMARK 465 SER B 40
REMARK 465 VAL B 41
REMARK 465 GLN B 42
REMARK 465 SER B 43
REMARK 465 GLY B 44
REMARK 465 SER B 45
REMARK 465 THR B 46
REMARK 465 ALA B 47
REMARK 465 ASN B 48
REMARK 465 LEU B 49
REMARK 465 PRO B 50
REMARK 465 ALA B 51
REMARK 465 ASP B 52
REMARK 465 LEU B 53
REMARK 465 ALA B 54
REMARK 465 THR B 55
REMARK 465 ALA B 56
REMARK 465 LEU B 57
REMARK 465 ALA B 58
REMARK 465 THR B 59
REMARK 465 ALA B 60
REMARK 465 LYS B 61
REMARK 465 GLU B 62
REMARK 465 ASN B 63
REMARK 465 ASP B 64
REMARK 465 GLY B 65
REMARK 465 HIS B 66
REMARK 465 ASP B 67
REMARK 465 PHE B 68
REMARK 465 GLU B 69
REMARK 465 ALA B 70
REMARK 465 PRO B 71
REMARK 465 LYS B 72
REMARK 465 VAL B 73
REMARK 465 GLY B 74
REMARK 465 GLU B 75
REMARK 465 ASP B 76
REMARK 465 GLN B 77
REMARK 465 GLY B 78
REMARK 465 SER B 79
REMARK 465 PRO B 80
REMARK 465 GLU B 81
REMARK 465 VAL B 82
REMARK 465 THR B 83
REMARK 465 ASP B 84
REMARK 465 GLY B 85
REMARK 465 PRO B 86
REMARK 465 LYS B 87
REMARK 465 THR B 88
REMARK 465 GLU B 89
REMARK 465 GLU B 90
REMARK 465 GLU B 91
REMARK 465 LEU B 92
REMARK 465 LEU B 93
REMARK 465 ALA B 94
REMARK 465 LEU B 95
REMARK 465 GLU B 96
REMARK 465 LYS B 97
REMARK 465 GLU B 98
REMARK 465 LYS B 99
REMARK 465 PRO B 100
REMARK 465 ALA B 101
REMARK 465 GLU B 102
REMARK 465 GLU B 103
REMARK 465 LYS B 104
REMARK 465 PRO B 105
REMARK 465 LYS B 106
REMARK 465 GLU B 107
REMARK 465 ASP B 108
REMARK 465 LYS B 109
REMARK 465 PRO B 110
REMARK 465 ALA B 111
REMARK 465 ALA B 112
REMARK 465 ALA B 113
REMARK 465 LYS B 114
REMARK 465 PRO B 115
REMARK 465 GLU B 116
REMARK 465 THR B 117
REMARK 465 PRO B 118
REMARK 465 LYS B 119
REMARK 465 THR B 120
REMARK 465 VAL B 121
REMARK 465 SER B 223
REMARK 465 PRO B 224
REMARK 465 THR B 225
REMARK 465 GLY B 308
REMARK 465 VAL B 309
REMARK 465 LYS B 310
REMARK 465 THR B 311
REMARK 465 GLU B 312
REMARK 465 ASP B 313
REMARK 465 THR B 314
REMARK 465 PRO B 315
REMARK 465 ALA B 316
REMARK 465 GLU B 317
REMARK 465 ALA B 1482
REMARK 465 LEU B 1483
REMARK 465 VAL B 1484
REMARK 465 GLN B 1485
REMARK 465 LYS B 1486
REMARK 465 LYS B 1487
REMARK 465 THR B 1488
REMARK 465 ALA B 1489
REMARK 465 LEU B 1490
REMARK 465 VAL B 1491
REMARK 465 ALA B 1492
REMARK 465 ASP B 1493
REMARK 465 ASP B 1494
REMARK 465 PHE B 1495
REMARK 465 ALA B 1496
REMARK 465 SER B 1497
REMARK 465 LEU B 1498
REMARK 465 THR B 1499
REMARK 465 ALA B 1500
REMARK 465 PRO B 1501
REMARK 465 ALA B 1502
REMARK 465 GLN B 1503
REMARK 465 ALA B 1504
REMARK 465 GLN B 1505
REMARK 465 GLU B 1506
REMARK 465 GLY B 1507
REMARK 465 LEU B 1508
REMARK 465 ALA B 1509
REMARK 465 ASN B 1510
REMARK 465 ALA B 1511
REMARK 465 PHE B 1512
REMARK 465 ASP B 1513
REMARK 465 GLY B 1514
REMARK 465 ASN B 1515
REMARK 465 LEU B 1516
REMARK 465 SER B 1517
REMARK 465 SER B 1518
REMARK 465 LEU B 1519
REMARK 465 TRP B 1520
REMARK 465 HIS B 1521
REMARK 465 THR B 1522
REMARK 465 SER B 1523
REMARK 465 TRP B 1524
REMARK 465 GLY B 1525
REMARK 465 GLY B 1526
REMARK 465 GLY B 1527
REMARK 465 ASP B 1528
REMARK 465 VAL B 1529
REMARK 465 GLY B 1530
REMARK 465 LYS B 1531
REMARK 465 PRO B 1532
REMARK 465 ALA B 1533
REMARK 465 THR B 1534
REMARK 465 MSE B 1535
REMARK 465 VAL B 1536
REMARK 465 LEU B 1537
REMARK 465 LYS B 1538
REMARK 465 GLU B 1539
REMARK 465 ALA B 1540
REMARK 465 THR B 1541
REMARK 465 GLU B 1542
REMARK 465 ILE B 1543
REMARK 465 THR B 1544
REMARK 465 GLY B 1545
REMARK 465 LEU B 1546
REMARK 465 ARG B 1547
REMARK 465 TYR B 1548
REMARK 465 VAL B 1549
REMARK 465 PRO B 1550
REMARK 465 ARG B 1551
REMARK 465 GLY B 1552
REMARK 465 SER B 1553
REMARK 465 GLY B 1554
REMARK 465 SER B 1555
REMARK 465 ASN B 1556
REMARK 465 GLY B 1557
REMARK 465 ASN B 1558
REMARK 465 LEU B 1559
REMARK 465 ARG B 1560
REMARK 465 ASP B 1561
REMARK 465 VAL B 1562
REMARK 465 LYS B 1563
REMARK 465 LEU B 1564
REMARK 465 VAL B 1565
REMARK 465 VAL B 1566
REMARK 465 THR B 1567
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 GLN A 133 33.33 -96.50
REMARK 500 LYS A 143 -139.47 61.15
REMARK 500 ALA A 159 -102.45 -101.06
REMARK 500 ASP A 293 -129.62 44.70
REMARK 500 PHE A 347 139.19 -170.89
REMARK 500 PHE A 367 86.09 -150.03
REMARK 500 ASN A 368 50.08 -91.53
REMARK 500 ASN A 405 81.13 -164.39
REMARK 500 ASP A 416 -118.62 46.56
REMARK 500 THR A 504 -165.76 -106.16
REMARK 500 TRP A 551 -113.83 -152.96
REMARK 500 LYS A 556 48.57 34.62
REMARK 500 ARG A 613 148.97 -172.06
REMARK 500 SER A 654 -131.35 57.96
REMARK 500 LEU A 662 -40.65 87.72
REMARK 500 ASN A 708 140.72 -177.68
REMARK 500 PRO A 716 -50.69 -29.67
REMARK 500 TRP A 726 -85.60 -140.57
REMARK 500 VAL A 765 -39.88 73.33
REMARK 500 TYR A 816 108.92 -167.76
REMARK 500 LYS A 822 -149.48 -104.41
REMARK 500 ALA A 839 22.27 -150.32
REMARK 500 GLU A 865 48.22 -104.57
REMARK 500 LYS A1003 35.22 -95.59
REMARK 500 ASP A1026 71.86 28.29
REMARK 500 GLN A1062 -38.58 -34.58
REMARK 500 ASN A1147 -157.18 -97.08
REMARK 500 HIS A1160 43.74 -109.94
REMARK 500 ASN A1190 44.11 -141.77
REMARK 500 GLU A1208 81.36 68.49
REMARK 500 SER A1217 78.46 -153.83
REMARK 500 ASP A1254 86.12 -60.24
REMARK 500 ARG A1256 36.00 -94.20
REMARK 500 SER A1293 32.73 71.49
REMARK 500 ARG A1342 129.51 -37.70
REMARK 500 GLN B 133 35.31 -96.89
REMARK 500 LYS B 143 -137.64 61.38
REMARK 500 ASP B 157 -159.20 -140.83
REMARK 500 ALA B 159 -103.13 -98.88
REMARK 500 ASP B 293 -129.44 47.12
REMARK 500 PHE B 347 137.71 -172.02
REMARK 500 ASN B 368 51.12 -91.83
REMARK 500 LYS B 384 119.48 -160.14
REMARK 500 ASN B 405 81.88 -164.30
REMARK 500 ASP B 416 -117.09 45.27
REMARK 500 THR B 504 -168.43 -108.44
REMARK 500 GLN B 516 34.68 -97.31
REMARK 500 TRP B 551 -110.95 -150.25
REMARK 500 LYS B 556 46.85 34.80
REMARK 500 ARG B 613 144.37 -174.71
REMARK 500
REMARK 500 THIS ENTRY HAS 69 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 GLY A 1377 ASP A 1378 -146.51
REMARK 500 GLY B 1377 ASP B 1378 -147.84
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 2000
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 2001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 2002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 2003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 2000
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 2001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 2002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 2003
DBREF 3ECQ A 40 1567 UNP Q8DR60 Q8DR60_STRR6 40 1567
DBREF 3ECQ B 40 1567 UNP Q8DR60 Q8DR60_STRR6 40 1567
SEQADV 3ECQ GLY A 37 UNP Q8DR60 EXPRESSION TAG
SEQADV 3ECQ SER A 38 UNP Q8DR60 EXPRESSION TAG
SEQADV 3ECQ MSE A 39 UNP Q8DR60 EXPRESSION TAG
SEQADV 3ECQ GLY B 37 UNP Q8DR60 EXPRESSION TAG
SEQADV 3ECQ SER B 38 UNP Q8DR60 EXPRESSION TAG
SEQADV 3ECQ MSE B 39 UNP Q8DR60 EXPRESSION TAG
SEQRES 1 A 1531 GLY SER MSE SER VAL GLN SER GLY SER THR ALA ASN LEU
SEQRES 2 A 1531 PRO ALA ASP LEU ALA THR ALA LEU ALA THR ALA LYS GLU
SEQRES 3 A 1531 ASN ASP GLY HIS ASP PHE GLU ALA PRO LYS VAL GLY GLU
SEQRES 4 A 1531 ASP GLN GLY SER PRO GLU VAL THR ASP GLY PRO LYS THR
SEQRES 5 A 1531 GLU GLU GLU LEU LEU ALA LEU GLU LYS GLU LYS PRO ALA
SEQRES 6 A 1531 GLU GLU LYS PRO LYS GLU ASP LYS PRO ALA ALA ALA LYS
SEQRES 7 A 1531 PRO GLU THR PRO LYS THR VAL THR PRO GLU TRP GLN THR
SEQRES 8 A 1531 VAL GLU LYS LYS GLU GLN GLN GLY THR VAL THR ILE ARG
SEQRES 9 A 1531 GLU GLU LYS GLY VAL ARG TYR ASN GLN LEU SER SER THR
SEQRES 10 A 1531 ALA GLN ASN ASP ASN ALA GLY LYS PRO ALA LEU PHE GLU
SEQRES 11 A 1531 LYS LYS GLY LEU THR VAL ASP ALA ASN GLY ASN ALA THR
SEQRES 12 A 1531 VAL ASP LEU THR PHE LYS ASP ASP SER GLU LYS GLY LYS
SEQRES 13 A 1531 SER ARG PHE GLY VAL PHE LEU LYS PHE LYS ASP THR LYS
SEQRES 14 A 1531 ASN ASN VAL PHE VAL GLY TYR ASP LYS ASP GLY TRP PHE
SEQRES 15 A 1531 TRP GLU TYR LYS SER PRO THR THR SER THR TRP TYR ARG
SEQRES 16 A 1531 GLY SER ARG VAL ALA ALA PRO GLU THR GLY SER THR ASN
SEQRES 17 A 1531 ARG LEU SER ILE THR LEU LYS SER ASP GLY GLN LEU ASN
SEQRES 18 A 1531 ALA SER ASN ASN ASP VAL ASN LEU PHE ASP THR VAL THR
SEQRES 19 A 1531 LEU PRO ALA ALA VAL ASN ASP HIS LEU LYS ASN GLU LYS
SEQRES 20 A 1531 LYS ILE LEU LEU LYS ALA GLY SER TYR ASP ASP GLU ARG
SEQRES 21 A 1531 THR VAL VAL SER VAL LYS THR ASP ASN GLN GLU GLY VAL
SEQRES 22 A 1531 LYS THR GLU ASP THR PRO ALA GLU LYS GLU THR GLY PRO
SEQRES 23 A 1531 GLU VAL ASP ASP SER LYS VAL THR TYR ASP THR ILE GLN
SEQRES 24 A 1531 SER LYS VAL LEU LYS ALA VAL ILE ASP GLN ALA PHE PRO
SEQRES 25 A 1531 ARG VAL LYS GLU TYR SER LEU ASN GLY HIS THR LEU PRO
SEQRES 26 A 1531 GLY GLN VAL GLN GLN PHE ASN GLN VAL PHE ILE ASN ASN
SEQRES 27 A 1531 HIS ARG ILE THR PRO GLU VAL THR TYR LYS LYS ILE ASN
SEQRES 28 A 1531 GLU THR THR ALA GLU TYR LEU MSE LYS LEU ARG ASP ASP
SEQRES 29 A 1531 ALA HIS LEU ILE ASN ALA GLU MSE THR VAL ARG LEU GLN
SEQRES 30 A 1531 VAL VAL ASP ASN GLN LEU HIS PHE ASP VAL THR LYS ILE
SEQRES 31 A 1531 VAL ASN HIS ASN GLN VAL THR PRO GLY GLN LYS ILE ASP
SEQRES 32 A 1531 ASP GLU ARG LYS LEU LEU SER SER ILE SER PHE LEU GLY
SEQRES 33 A 1531 ASN ALA LEU VAL SER VAL SER SER ASP GLN THR GLY ALA
SEQRES 34 A 1531 LYS PHE ASP GLY ALA THR MSE SER ASN ASN THR HIS VAL
SEQRES 35 A 1531 SER GLY ASP ASP HIS ILE ASP VAL THR ASN PRO MSE LYS
SEQRES 36 A 1531 ASP LEU ALA LYS GLY TYR MSE TYR GLY PHE VAL SER THR
SEQRES 37 A 1531 ASP LYS LEU ALA ALA GLY VAL TRP SER ASN SER GLN ASN
SEQRES 38 A 1531 SER TYR GLY GLY GLY SER ASN ASP TRP THR ARG LEU THR
SEQRES 39 A 1531 ALA TYR LYS GLU THR VAL GLY ASN ALA ASN TYR VAL GLY
SEQRES 40 A 1531 ILE HIS SER SER GLU TRP GLN TRP GLU LYS ALA TYR LYS
SEQRES 41 A 1531 GLY ILE VAL PHE PRO GLU TYR THR LYS GLU LEU PRO SER
SEQRES 42 A 1531 ALA LYS VAL VAL ILE THR GLU ASP ALA ASN ALA ASP LYS
SEQRES 43 A 1531 LYS VAL ASP TRP GLN ASP GLY ALA ILE ALA TYR ARG SER
SEQRES 44 A 1531 ILE MSE ASN ASN PRO GLN GLY TRP LYS LYS VAL LYS ASP
SEQRES 45 A 1531 ILE THR ALA TYR ARG ILE ALA MSE ASN PHE GLY SER GLN
SEQRES 46 A 1531 ALA GLN ASN PRO PHE LEU MSE THR LEU ASP GLY ILE LYS
SEQRES 47 A 1531 LYS ILE ASN LEU HIS THR ASP GLY LEU GLY GLN GLY VAL
SEQRES 48 A 1531 LEU LEU LYS GLY TYR GLY SER GLU GLY HIS ASP SER GLY
SEQRES 49 A 1531 HIS LEU ASN TYR ALA ASP ILE GLY LYS ARG ILE GLY GLY
SEQRES 50 A 1531 VAL GLU ASP PHE LYS THR LEU ILE GLU LYS ALA LYS LYS
SEQRES 51 A 1531 TYR GLY ALA HIS LEU GLY ILE HIS VAL ASN ALA SER GLU
SEQRES 52 A 1531 THR TYR PRO GLU SER LYS TYR PHE ASN GLU LYS ILE LEU
SEQRES 53 A 1531 ARG LYS ASN PRO ASP GLY SER TYR SER TYR GLY TRP ASN
SEQRES 54 A 1531 TRP LEU ASP GLN GLY ILE ASN ILE ASP ALA ALA TYR ASP
SEQRES 55 A 1531 LEU ALA HIS GLY ARG LEU ALA ARG TRP GLU ASP LEU LYS
SEQRES 56 A 1531 LYS LYS LEU GLY ASP GLY LEU ASP PHE ILE TYR VAL ASP
SEQRES 57 A 1531 VAL TRP GLY ASN GLY GLN SER GLY ASP ASN GLY ALA TRP
SEQRES 58 A 1531 ALA THR HIS VAL LEU ALA LYS GLU ILE ASN LYS GLN GLY
SEQRES 59 A 1531 TRP ARG PHE ALA ILE GLU TRP GLY HIS GLY GLY GLU TYR
SEQRES 60 A 1531 ASP SER THR PHE HIS HIS TRP ALA ALA ASP LEU THR TYR
SEQRES 61 A 1531 GLY GLY TYR THR ASN LYS GLY ILE ASN SER ALA ILE THR
SEQRES 62 A 1531 ARG PHE ILE ARG ASN HIS GLN LYS ASP ALA TRP VAL GLY
SEQRES 63 A 1531 ASP TYR ARG SER TYR GLY GLY ALA ALA ASN TYR PRO LEU
SEQRES 64 A 1531 LEU GLY GLY TYR SER MSE LYS ASP PHE GLU GLY TRP GLN
SEQRES 65 A 1531 GLY ARG SER ASP TYR ASN GLY TYR VAL THR ASN LEU PHE
SEQRES 66 A 1531 ALA HIS ASP VAL MSE THR LYS TYR PHE GLN HIS PHE THR
SEQRES 67 A 1531 VAL SER LYS TRP GLU ASN GLY THR PRO VAL THR MSE THR
SEQRES 68 A 1531 ASP ASN GLY SER THR TYR LYS TRP THR PRO GLU MSE ARG
SEQRES 69 A 1531 VAL GLU LEU VAL ASP ALA ASP ASN ASN LYS VAL VAL VAL
SEQRES 70 A 1531 THR ARG LYS SER ASN ASP VAL ASN SER PRO GLN TYR ARG
SEQRES 71 A 1531 GLU ARG THR VAL THR LEU ASN GLY ARG VAL ILE GLN ASP
SEQRES 72 A 1531 GLY SER ALA TYR LEU THR PRO TRP ASN TRP ASP ALA ASN
SEQRES 73 A 1531 GLY LYS LYS LEU SER THR ASP LYS GLU LYS MSE TYR TYR
SEQRES 74 A 1531 PHE ASN THR GLN ALA GLY ALA THR THR TRP THR LEU PRO
SEQRES 75 A 1531 SER ASP TRP ALA LYS SER LYS VAL TYR LEU TYR LYS LEU
SEQRES 76 A 1531 THR ASP GLN GLY LYS THR GLU GLU GLN GLU LEU THR VAL
SEQRES 77 A 1531 LYS ASP GLY LYS ILE THR LEU ASP LEU LEU ALA ASN GLN
SEQRES 78 A 1531 PRO TYR VAL LEU TYR ARG SER LYS GLN THR ASN PRO GLU
SEQRES 79 A 1531 MSE SER TRP SER GLU GLY MSE HIS ILE TYR ASP GLN GLY
SEQRES 80 A 1531 PHE ASN SER GLY THR LEU LYS HIS TRP THR ILE SER GLY
SEQRES 81 A 1531 ASP ALA SER LYS ALA GLU ILE VAL LYS SER GLN GLY ALA
SEQRES 82 A 1531 ASN ASP MSE LEU ARG ILE GLN GLY ASN LYS GLU LYS VAL
SEQRES 83 A 1531 SER LEU THR GLN LYS LEU THR GLY LEU LYS PRO ASN THR
SEQRES 84 A 1531 LYS TYR ALA VAL TYR VAL GLY VAL ASP ASN ARG SER ASN
SEQRES 85 A 1531 ALA LYS ALA SER ILE THR VAL ASN THR GLY GLU LYS GLU
SEQRES 86 A 1531 VAL THR THR TYR THR ASN LYS SER LEU ALA LEU ASN TYR
SEQRES 87 A 1531 VAL LYS ALA TYR ALA HIS ASN THR ARG ARG ASN ASN ALA
SEQRES 88 A 1531 THR VAL ASP ASP THR SER TYR PHE GLN ASN MSE TYR ALA
SEQRES 89 A 1531 PHE PHE THR THR GLY SER ASP VAL SER ASN VAL THR LEU
SEQRES 90 A 1531 THR LEU SER ARG GLU ALA GLY ASP GLU ALA THR TYR PHE
SEQRES 91 A 1531 ASP GLU ILE ARG THR PHE GLU ASN ASN SER SER MSE TYR
SEQRES 92 A 1531 GLY ASP LYS HIS ASP THR GLY LYS GLY THR PHE LYS GLN
SEQRES 93 A 1531 ASP PHE GLU ASN VAL ALA GLN GLY ILE PHE PRO PHE VAL
SEQRES 94 A 1531 VAL GLY GLY VAL GLU GLY VAL GLU ASP ASN ARG THR HIS
SEQRES 95 A 1531 LEU SER GLU LYS HIS ASP PRO TYR THR GLN ARG GLY TRP
SEQRES 96 A 1531 ASN GLY LYS LYS VAL ASP ASP VAL ILE GLU GLY ASN TRP
SEQRES 97 A 1531 SER LEU LYS THR ASN GLY LEU VAL SER ARG ARG ASN LEU
SEQRES 98 A 1531 VAL TYR GLN THR ILE PRO GLN ASN PHE ARG PHE GLU ALA
SEQRES 99 A 1531 GLY LYS THR TYR ARG VAL THR PHE GLU TYR GLU ALA GLY
SEQRES 100 A 1531 SER ASP ASN THR TYR ALA PHE VAL VAL GLY LYS GLY GLU
SEQRES 101 A 1531 PHE GLN SER GLY ARG ARG GLY THR GLN ALA SER ASN LEU
SEQRES 102 A 1531 GLU MSE HIS GLU LEU PRO ASN THR TRP THR ASP SER LYS
SEQRES 103 A 1531 LYS ALA LYS LYS ALA THR PHE LEU VAL THR GLY ALA GLU
SEQRES 104 A 1531 THR GLY ASP THR TRP VAL GLY ILE TYR SER THR GLY ASN
SEQRES 105 A 1531 ALA SER ASN THR ARG GLY ASP SER GLY GLY ASN ALA ASN
SEQRES 106 A 1531 PHE ARG GLY TYR ASN ASP PHE MSE MSE ASP ASN LEU GLN
SEQRES 107 A 1531 ILE GLU GLU ILE THR LEU THR GLY LYS MSE LEU THR GLU
SEQRES 108 A 1531 ASN ALA LEU LYS ASN TYR LEU PRO THR VAL ALA MSE THR
SEQRES 109 A 1531 ASN TYR THR LYS GLU SER MSE ASP ALA LEU LYS GLU ALA
SEQRES 110 A 1531 VAL PHE ASN LEU SER GLN ALA ASP ASP ASP ILE SER VAL
SEQRES 111 A 1531 GLU GLU ALA ARG ALA GLU ILE ALA LYS ILE GLU ALA LEU
SEQRES 112 A 1531 LYS ASN ALA LEU VAL GLN LYS LYS THR ALA LEU VAL ALA
SEQRES 113 A 1531 ASP ASP PHE ALA SER LEU THR ALA PRO ALA GLN ALA GLN
SEQRES 114 A 1531 GLU GLY LEU ALA ASN ALA PHE ASP GLY ASN LEU SER SER
SEQRES 115 A 1531 LEU TRP HIS THR SER TRP GLY GLY GLY ASP VAL GLY LYS
SEQRES 116 A 1531 PRO ALA THR MSE VAL LEU LYS GLU ALA THR GLU ILE THR
SEQRES 117 A 1531 GLY LEU ARG TYR VAL PRO ARG GLY SER GLY SER ASN GLY
SEQRES 118 A 1531 ASN LEU ARG ASP VAL LYS LEU VAL VAL THR
SEQRES 1 B 1531 GLY SER MSE SER VAL GLN SER GLY SER THR ALA ASN LEU
SEQRES 2 B 1531 PRO ALA ASP LEU ALA THR ALA LEU ALA THR ALA LYS GLU
SEQRES 3 B 1531 ASN ASP GLY HIS ASP PHE GLU ALA PRO LYS VAL GLY GLU
SEQRES 4 B 1531 ASP GLN GLY SER PRO GLU VAL THR ASP GLY PRO LYS THR
SEQRES 5 B 1531 GLU GLU GLU LEU LEU ALA LEU GLU LYS GLU LYS PRO ALA
SEQRES 6 B 1531 GLU GLU LYS PRO LYS GLU ASP LYS PRO ALA ALA ALA LYS
SEQRES 7 B 1531 PRO GLU THR PRO LYS THR VAL THR PRO GLU TRP GLN THR
SEQRES 8 B 1531 VAL GLU LYS LYS GLU GLN GLN GLY THR VAL THR ILE ARG
SEQRES 9 B 1531 GLU GLU LYS GLY VAL ARG TYR ASN GLN LEU SER SER THR
SEQRES 10 B 1531 ALA GLN ASN ASP ASN ALA GLY LYS PRO ALA LEU PHE GLU
SEQRES 11 B 1531 LYS LYS GLY LEU THR VAL ASP ALA ASN GLY ASN ALA THR
SEQRES 12 B 1531 VAL ASP LEU THR PHE LYS ASP ASP SER GLU LYS GLY LYS
SEQRES 13 B 1531 SER ARG PHE GLY VAL PHE LEU LYS PHE LYS ASP THR LYS
SEQRES 14 B 1531 ASN ASN VAL PHE VAL GLY TYR ASP LYS ASP GLY TRP PHE
SEQRES 15 B 1531 TRP GLU TYR LYS SER PRO THR THR SER THR TRP TYR ARG
SEQRES 16 B 1531 GLY SER ARG VAL ALA ALA PRO GLU THR GLY SER THR ASN
SEQRES 17 B 1531 ARG LEU SER ILE THR LEU LYS SER ASP GLY GLN LEU ASN
SEQRES 18 B 1531 ALA SER ASN ASN ASP VAL ASN LEU PHE ASP THR VAL THR
SEQRES 19 B 1531 LEU PRO ALA ALA VAL ASN ASP HIS LEU LYS ASN GLU LYS
SEQRES 20 B 1531 LYS ILE LEU LEU LYS ALA GLY SER TYR ASP ASP GLU ARG
SEQRES 21 B 1531 THR VAL VAL SER VAL LYS THR ASP ASN GLN GLU GLY VAL
SEQRES 22 B 1531 LYS THR GLU ASP THR PRO ALA GLU LYS GLU THR GLY PRO
SEQRES 23 B 1531 GLU VAL ASP ASP SER LYS VAL THR TYR ASP THR ILE GLN
SEQRES 24 B 1531 SER LYS VAL LEU LYS ALA VAL ILE ASP GLN ALA PHE PRO
SEQRES 25 B 1531 ARG VAL LYS GLU TYR SER LEU ASN GLY HIS THR LEU PRO
SEQRES 26 B 1531 GLY GLN VAL GLN GLN PHE ASN GLN VAL PHE ILE ASN ASN
SEQRES 27 B 1531 HIS ARG ILE THR PRO GLU VAL THR TYR LYS LYS ILE ASN
SEQRES 28 B 1531 GLU THR THR ALA GLU TYR LEU MSE LYS LEU ARG ASP ASP
SEQRES 29 B 1531 ALA HIS LEU ILE ASN ALA GLU MSE THR VAL ARG LEU GLN
SEQRES 30 B 1531 VAL VAL ASP ASN GLN LEU HIS PHE ASP VAL THR LYS ILE
SEQRES 31 B 1531 VAL ASN HIS ASN GLN VAL THR PRO GLY GLN LYS ILE ASP
SEQRES 32 B 1531 ASP GLU ARG LYS LEU LEU SER SER ILE SER PHE LEU GLY
SEQRES 33 B 1531 ASN ALA LEU VAL SER VAL SER SER ASP GLN THR GLY ALA
SEQRES 34 B 1531 LYS PHE ASP GLY ALA THR MSE SER ASN ASN THR HIS VAL
SEQRES 35 B 1531 SER GLY ASP ASP HIS ILE ASP VAL THR ASN PRO MSE LYS
SEQRES 36 B 1531 ASP LEU ALA LYS GLY TYR MSE TYR GLY PHE VAL SER THR
SEQRES 37 B 1531 ASP LYS LEU ALA ALA GLY VAL TRP SER ASN SER GLN ASN
SEQRES 38 B 1531 SER TYR GLY GLY GLY SER ASN ASP TRP THR ARG LEU THR
SEQRES 39 B 1531 ALA TYR LYS GLU THR VAL GLY ASN ALA ASN TYR VAL GLY
SEQRES 40 B 1531 ILE HIS SER SER GLU TRP GLN TRP GLU LYS ALA TYR LYS
SEQRES 41 B 1531 GLY ILE VAL PHE PRO GLU TYR THR LYS GLU LEU PRO SER
SEQRES 42 B 1531 ALA LYS VAL VAL ILE THR GLU ASP ALA ASN ALA ASP LYS
SEQRES 43 B 1531 LYS VAL ASP TRP GLN ASP GLY ALA ILE ALA TYR ARG SER
SEQRES 44 B 1531 ILE MSE ASN ASN PRO GLN GLY TRP LYS LYS VAL LYS ASP
SEQRES 45 B 1531 ILE THR ALA TYR ARG ILE ALA MSE ASN PHE GLY SER GLN
SEQRES 46 B 1531 ALA GLN ASN PRO PHE LEU MSE THR LEU ASP GLY ILE LYS
SEQRES 47 B 1531 LYS ILE ASN LEU HIS THR ASP GLY LEU GLY GLN GLY VAL
SEQRES 48 B 1531 LEU LEU LYS GLY TYR GLY SER GLU GLY HIS ASP SER GLY
SEQRES 49 B 1531 HIS LEU ASN TYR ALA ASP ILE GLY LYS ARG ILE GLY GLY
SEQRES 50 B 1531 VAL GLU ASP PHE LYS THR LEU ILE GLU LYS ALA LYS LYS
SEQRES 51 B 1531 TYR GLY ALA HIS LEU GLY ILE HIS VAL ASN ALA SER GLU
SEQRES 52 B 1531 THR TYR PRO GLU SER LYS TYR PHE ASN GLU LYS ILE LEU
SEQRES 53 B 1531 ARG LYS ASN PRO ASP GLY SER TYR SER TYR GLY TRP ASN
SEQRES 54 B 1531 TRP LEU ASP GLN GLY ILE ASN ILE ASP ALA ALA TYR ASP
SEQRES 55 B 1531 LEU ALA HIS GLY ARG LEU ALA ARG TRP GLU ASP LEU LYS
SEQRES 56 B 1531 LYS LYS LEU GLY ASP GLY LEU ASP PHE ILE TYR VAL ASP
SEQRES 57 B 1531 VAL TRP GLY ASN GLY GLN SER GLY ASP ASN GLY ALA TRP
SEQRES 58 B 1531 ALA THR HIS VAL LEU ALA LYS GLU ILE ASN LYS GLN GLY
SEQRES 59 B 1531 TRP ARG PHE ALA ILE GLU TRP GLY HIS GLY GLY GLU TYR
SEQRES 60 B 1531 ASP SER THR PHE HIS HIS TRP ALA ALA ASP LEU THR TYR
SEQRES 61 B 1531 GLY GLY TYR THR ASN LYS GLY ILE ASN SER ALA ILE THR
SEQRES 62 B 1531 ARG PHE ILE ARG ASN HIS GLN LYS ASP ALA TRP VAL GLY
SEQRES 63 B 1531 ASP TYR ARG SER TYR GLY GLY ALA ALA ASN TYR PRO LEU
SEQRES 64 B 1531 LEU GLY GLY TYR SER MSE LYS ASP PHE GLU GLY TRP GLN
SEQRES 65 B 1531 GLY ARG SER ASP TYR ASN GLY TYR VAL THR ASN LEU PHE
SEQRES 66 B 1531 ALA HIS ASP VAL MSE THR LYS TYR PHE GLN HIS PHE THR
SEQRES 67 B 1531 VAL SER LYS TRP GLU ASN GLY THR PRO VAL THR MSE THR
SEQRES 68 B 1531 ASP ASN GLY SER THR TYR LYS TRP THR PRO GLU MSE ARG
SEQRES 69 B 1531 VAL GLU LEU VAL ASP ALA ASP ASN ASN LYS VAL VAL VAL
SEQRES 70 B 1531 THR ARG LYS SER ASN ASP VAL ASN SER PRO GLN TYR ARG
SEQRES 71 B 1531 GLU ARG THR VAL THR LEU ASN GLY ARG VAL ILE GLN ASP
SEQRES 72 B 1531 GLY SER ALA TYR LEU THR PRO TRP ASN TRP ASP ALA ASN
SEQRES 73 B 1531 GLY LYS LYS LEU SER THR ASP LYS GLU LYS MSE TYR TYR
SEQRES 74 B 1531 PHE ASN THR GLN ALA GLY ALA THR THR TRP THR LEU PRO
SEQRES 75 B 1531 SER ASP TRP ALA LYS SER LYS VAL TYR LEU TYR LYS LEU
SEQRES 76 B 1531 THR ASP GLN GLY LYS THR GLU GLU GLN GLU LEU THR VAL
SEQRES 77 B 1531 LYS ASP GLY LYS ILE THR LEU ASP LEU LEU ALA ASN GLN
SEQRES 78 B 1531 PRO TYR VAL LEU TYR ARG SER LYS GLN THR ASN PRO GLU
SEQRES 79 B 1531 MSE SER TRP SER GLU GLY MSE HIS ILE TYR ASP GLN GLY
SEQRES 80 B 1531 PHE ASN SER GLY THR LEU LYS HIS TRP THR ILE SER GLY
SEQRES 81 B 1531 ASP ALA SER LYS ALA GLU ILE VAL LYS SER GLN GLY ALA
SEQRES 82 B 1531 ASN ASP MSE LEU ARG ILE GLN GLY ASN LYS GLU LYS VAL
SEQRES 83 B 1531 SER LEU THR GLN LYS LEU THR GLY LEU LYS PRO ASN THR
SEQRES 84 B 1531 LYS TYR ALA VAL TYR VAL GLY VAL ASP ASN ARG SER ASN
SEQRES 85 B 1531 ALA LYS ALA SER ILE THR VAL ASN THR GLY GLU LYS GLU
SEQRES 86 B 1531 VAL THR THR TYR THR ASN LYS SER LEU ALA LEU ASN TYR
SEQRES 87 B 1531 VAL LYS ALA TYR ALA HIS ASN THR ARG ARG ASN ASN ALA
SEQRES 88 B 1531 THR VAL ASP ASP THR SER TYR PHE GLN ASN MSE TYR ALA
SEQRES 89 B 1531 PHE PHE THR THR GLY SER ASP VAL SER ASN VAL THR LEU
SEQRES 90 B 1531 THR LEU SER ARG GLU ALA GLY ASP GLU ALA THR TYR PHE
SEQRES 91 B 1531 ASP GLU ILE ARG THR PHE GLU ASN ASN SER SER MSE TYR
SEQRES 92 B 1531 GLY ASP LYS HIS ASP THR GLY LYS GLY THR PHE LYS GLN
SEQRES 93 B 1531 ASP PHE GLU ASN VAL ALA GLN GLY ILE PHE PRO PHE VAL
SEQRES 94 B 1531 VAL GLY GLY VAL GLU GLY VAL GLU ASP ASN ARG THR HIS
SEQRES 95 B 1531 LEU SER GLU LYS HIS ASP PRO TYR THR GLN ARG GLY TRP
SEQRES 96 B 1531 ASN GLY LYS LYS VAL ASP ASP VAL ILE GLU GLY ASN TRP
SEQRES 97 B 1531 SER LEU LYS THR ASN GLY LEU VAL SER ARG ARG ASN LEU
SEQRES 98 B 1531 VAL TYR GLN THR ILE PRO GLN ASN PHE ARG PHE GLU ALA
SEQRES 99 B 1531 GLY LYS THR TYR ARG VAL THR PHE GLU TYR GLU ALA GLY
SEQRES 100 B 1531 SER ASP ASN THR TYR ALA PHE VAL VAL GLY LYS GLY GLU
SEQRES 101 B 1531 PHE GLN SER GLY ARG ARG GLY THR GLN ALA SER ASN LEU
SEQRES 102 B 1531 GLU MSE HIS GLU LEU PRO ASN THR TRP THR ASP SER LYS
SEQRES 103 B 1531 LYS ALA LYS LYS ALA THR PHE LEU VAL THR GLY ALA GLU
SEQRES 104 B 1531 THR GLY ASP THR TRP VAL GLY ILE TYR SER THR GLY ASN
SEQRES 105 B 1531 ALA SER ASN THR ARG GLY ASP SER GLY GLY ASN ALA ASN
SEQRES 106 B 1531 PHE ARG GLY TYR ASN ASP PHE MSE MSE ASP ASN LEU GLN
SEQRES 107 B 1531 ILE GLU GLU ILE THR LEU THR GLY LYS MSE LEU THR GLU
SEQRES 108 B 1531 ASN ALA LEU LYS ASN TYR LEU PRO THR VAL ALA MSE THR
SEQRES 109 B 1531 ASN TYR THR LYS GLU SER MSE ASP ALA LEU LYS GLU ALA
SEQRES 110 B 1531 VAL PHE ASN LEU SER GLN ALA ASP ASP ASP ILE SER VAL
SEQRES 111 B 1531 GLU GLU ALA ARG ALA GLU ILE ALA LYS ILE GLU ALA LEU
SEQRES 112 B 1531 LYS ASN ALA LEU VAL GLN LYS LYS THR ALA LEU VAL ALA
SEQRES 113 B 1531 ASP ASP PHE ALA SER LEU THR ALA PRO ALA GLN ALA GLN
SEQRES 114 B 1531 GLU GLY LEU ALA ASN ALA PHE ASP GLY ASN LEU SER SER
SEQRES 115 B 1531 LEU TRP HIS THR SER TRP GLY GLY GLY ASP VAL GLY LYS
SEQRES 116 B 1531 PRO ALA THR MSE VAL LEU LYS GLU ALA THR GLU ILE THR
SEQRES 117 B 1531 GLY LEU ARG TYR VAL PRO ARG GLY SER GLY SER ASN GLY
SEQRES 118 B 1531 ASN LEU ARG ASP VAL LYS LEU VAL VAL THR
MODRES 3ECQ MSE A 395 MET SELENOMETHIONINE
MODRES 3ECQ MSE A 408 MET SELENOMETHIONINE
MODRES 3ECQ MSE A 472 MET SELENOMETHIONINE
MODRES 3ECQ MSE A 490 MET SELENOMETHIONINE
MODRES 3ECQ MSE A 498 MET SELENOMETHIONINE
MODRES 3ECQ MSE A 597 MET SELENOMETHIONINE
MODRES 3ECQ MSE A 616 MET SELENOMETHIONINE
MODRES 3ECQ MSE A 628 MET SELENOMETHIONINE
MODRES 3ECQ MSE A 861 MET SELENOMETHIONINE
MODRES 3ECQ MSE A 886 MET SELENOMETHIONINE
MODRES 3ECQ MSE A 906 MET SELENOMETHIONINE
MODRES 3ECQ MSE A 919 MET SELENOMETHIONINE
MODRES 3ECQ MSE A 983 MET SELENOMETHIONINE
MODRES 3ECQ MSE A 1051 MET SELENOMETHIONINE
MODRES 3ECQ MSE A 1057 MET SELENOMETHIONINE
MODRES 3ECQ MSE A 1092 MET SELENOMETHIONINE
MODRES 3ECQ MSE A 1178 MET SELENOMETHIONINE
MODRES 3ECQ MSE A 1218 MET SELENOMETHIONINE
MODRES 3ECQ MSE A 1351 MET SELENOMETHIONINE
MODRES 3ECQ MSE A 1409 MET SELENOMETHIONINE
MODRES 3ECQ MSE A 1410 MET SELENOMETHIONINE
MODRES 3ECQ MSE A 1424 MET SELENOMETHIONINE
MODRES 3ECQ MSE A 1439 MET SELENOMETHIONINE
MODRES 3ECQ MSE B 395 MET SELENOMETHIONINE
MODRES 3ECQ MSE B 408 MET SELENOMETHIONINE
MODRES 3ECQ MSE B 472 MET SELENOMETHIONINE
MODRES 3ECQ MSE B 490 MET SELENOMETHIONINE
MODRES 3ECQ MSE B 498 MET SELENOMETHIONINE
MODRES 3ECQ MSE B 597 MET SELENOMETHIONINE
MODRES 3ECQ MSE B 616 MET SELENOMETHIONINE
MODRES 3ECQ MSE B 628 MET SELENOMETHIONINE
MODRES 3ECQ MSE B 861 MET SELENOMETHIONINE
MODRES 3ECQ MSE B 886 MET SELENOMETHIONINE
MODRES 3ECQ MSE B 906 MET SELENOMETHIONINE
MODRES 3ECQ MSE B 919 MET SELENOMETHIONINE
MODRES 3ECQ MSE B 983 MET SELENOMETHIONINE
MODRES 3ECQ MSE B 1051 MET SELENOMETHIONINE
MODRES 3ECQ MSE B 1057 MET SELENOMETHIONINE
MODRES 3ECQ MSE B 1092 MET SELENOMETHIONINE
MODRES 3ECQ MSE B 1178 MET SELENOMETHIONINE
MODRES 3ECQ MSE B 1218 MET SELENOMETHIONINE
MODRES 3ECQ MSE B 1351 MET SELENOMETHIONINE
MODRES 3ECQ MSE B 1409 MET SELENOMETHIONINE
MODRES 3ECQ MSE B 1410 MET SELENOMETHIONINE
MODRES 3ECQ MSE B 1424 MET SELENOMETHIONINE
MODRES 3ECQ MSE B 1439 MET SELENOMETHIONINE
MODRES 3ECQ MSE B 1447 MET SELENOMETHIONINE
HET MSE A 395 8
HET MSE A 408 8
HET MSE A 472 8
HET MSE A 490 8
HET MSE A 498 8
HET MSE A 597 8
HET MSE A 616 8
HET MSE A 628 8
HET MSE A 861 8
HET MSE A 886 8
HET MSE A 906 8
HET MSE A 919 8
HET MSE A 983 8
HET MSE A1051 8
HET MSE A1057 8
HET MSE A1092 8
HET MSE A1178 8
HET MSE A1218 8
HET MSE A1351 8
HET MSE A1409 8
HET MSE A1410 8
HET MSE A1424 8
HET MSE A1439 8
HET MSE B 395 8
HET MSE B 408 8
HET MSE B 472 8
HET MSE B 490 8
HET MSE B 498 8
HET MSE B 597 8
HET MSE B 616 8
HET MSE B 628 8
HET MSE B 861 8
HET MSE B 886 8
HET MSE B 906 8
HET MSE B 919 8
HET MSE B 983 8
HET MSE B1051 8
HET MSE B1057 8
HET MSE B1092 8
HET MSE B1178 8
HET MSE B1218 8
HET MSE B1351 8
HET MSE B1409 8
HET MSE B1410 8
HET MSE B1424 8
HET MSE B1439 8
HET MSE B1447 8
HET CA A2000 1
HET CA A2001 1
HET NA A2002 1
HET GOL A2003 6
HET CA B2000 1
HET CA B2001 1
HET NA B2002 1
HET GOL B2003 6
HETNAM MSE SELENOMETHIONINE
HETNAM CA CALCIUM ION
HETNAM NA SODIUM ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 1 MSE 47(C5 H11 N O2 SE)
FORMUL 3 CA 4(CA 2+)
FORMUL 5 NA 2(NA 1+)
FORMUL 6 GOL 2(C3 H8 O3)
FORMUL 11 HOH *97(H2 O)
HELIX 1 1 LYS A 130 GLN A 134 5 5
HELIX 2 2 PRO A 272 LYS A 280 1 9
HELIX 3 3 ASP A 400 LEU A 403 5 4
HELIX 4 4 ASP A 440 LEU A 444 5 5
HELIX 5 5 GLY A 521 ASP A 525 5 5
HELIX 6 6 PRO A 561 LYS A 565 5 5
HELIX 7 7 ASP A 585 ARG A 594 1 10
HELIX 8 8 GLY A 602 LYS A 607 5 6
HELIX 9 9 PRO A 625 ASP A 641 1 17
HELIX 10 10 GLY A 668 ILE A 671 5 4
HELIX 11 11 GLY A 672 LYS A 686 1 15
HELIX 12 12 ASP A 734 HIS A 741 1 8
HELIX 13 13 GLY A 742 GLY A 755 1 14
HELIX 14 14 GLY A 775 LYS A 788 1 14
HELIX 15 15 HIS A 808 ASP A 813 1 6
HELIX 16 16 SER A 826 ASN A 834 1 9
HELIX 17 17 TYR A 844 ASN A 852 5 9
HELIX 18 18 GLY A 866 ARG A 870 5 5
HELIX 19 19 TYR A 873 GLN A 891 1 19
HELIX 20 20 SER A 942 ARG A 946 5 5
HELIX 21 21 SER A 977 LYS A 980 5 4
HELIX 22 22 PRO A 998 LYS A 1003 1 6
HELIX 23 23 ASP A 1077 SER A 1079 5 3
HELIX 24 24 ARG A 1163 ALA A 1167 5 5
HELIX 25 25 GLY A 1270 LYS A 1274 5 5
HELIX 26 26 GLN A 1345 LEU A 1349 5 5
HELIX 27 27 SER A 1396 GLY A 1404 1 9
HELIX 28 28 THR A 1421 ALA A 1438 1 18
HELIX 29 29 LYS A 1451 GLN A 1459 1 9
HELIX 30 30 SER A 1465 ILE A 1476 1 12
HELIX 31 31 LYS B 130 GLN B 134 5 5
HELIX 32 32 PRO B 272 LYS B 280 1 9
HELIX 33 33 ASP B 400 LEU B 403 5 4
HELIX 34 34 ASP B 440 LEU B 444 5 5
HELIX 35 35 GLY B 521 ASP B 525 5 5
HELIX 36 36 PRO B 561 LYS B 565 5 5
HELIX 37 37 ASP B 585 ARG B 594 1 10
HELIX 38 38 GLY B 602 LYS B 607 5 6
HELIX 39 39 PRO B 625 ASP B 641 1 17
HELIX 40 40 GLY B 668 ILE B 671 5 4
HELIX 41 41 GLY B 672 LYS B 686 1 15
HELIX 42 42 ASN B 708 LEU B 712 5 5
HELIX 43 43 ASP B 734 HIS B 741 1 8
HELIX 44 44 GLY B 742 GLY B 755 1 14
HELIX 45 45 GLY B 775 GLN B 789 1 15
HELIX 46 46 HIS B 808 ASP B 813 1 6
HELIX 47 47 SER B 826 ASN B 834 1 9
HELIX 48 48 TYR B 844 ASN B 852 5 9
HELIX 49 49 ASP B 872 GLN B 891 1 20
HELIX 50 50 SER B 942 ARG B 946 5 5
HELIX 51 51 SER B 977 LYS B 980 5 4
HELIX 52 52 PRO B 998 LYS B 1003 1 6
HELIX 53 53 ASP B 1077 SER B 1079 5 3
HELIX 54 54 ARG B 1163 ALA B 1167 5 5
HELIX 55 55 GLY B 1248 GLY B 1251 5 4
HELIX 56 56 GLY B 1270 LYS B 1274 5 5
HELIX 57 57 GLN B 1345 LEU B 1349 5 5
HELIX 58 58 SER B 1396 GLY B 1404 1 9
HELIX 59 59 THR B 1421 ALA B 1438 1 18
HELIX 60 60 THR B 1443 GLN B 1459 1 17
HELIX 61 61 SER B 1465 ASN B 1481 1 17
SHEET 1 A 7 TRP A 125 THR A 127 0
SHEET 2 A 7 ALA A 163 LYS A 167 -1 O GLU A 166 N GLN A 126
SHEET 3 A 7 LYS A 284 ALA A 289 -1 O LEU A 287 N PHE A 165
SHEET 4 A 7 PHE A 195 ASP A 203 -1 N PHE A 198 O LEU A 286
SHEET 5 A 7 ASN A 206 ASP A 213 -1 O VAL A 210 N VAL A 197
SHEET 6 A 7 GLY A 216 LYS A 222 -1 O PHE A 218 N GLY A 211
SHEET 7 A 7 THR A 228 TRP A 229 -1 O THR A 228 N TYR A 221
SHEET 1 B 7 THR A 136 GLU A 142 0
SHEET 2 B 7 VAL A 145 SER A 151 -1 O GLN A 149 N THR A 138
SHEET 3 B 7 VAL A 298 LYS A 302 -1 O VAL A 299 N LEU A 150
SHEET 4 B 7 ALA A 178 ASP A 186 -1 N LYS A 185 O SER A 300
SHEET 5 B 7 THR A 243 LEU A 250 -1 O ASN A 244 N PHE A 184
SHEET 6 B 7 GLN A 255 ASN A 260 -1 O ASN A 257 N THR A 249
SHEET 7 B 7 VAL A 263 ASN A 264 -1 O VAL A 263 N ASN A 260
SHEET 1 C 7 THR A 136 GLU A 142 0
SHEET 2 C 7 VAL A 145 SER A 151 -1 O GLN A 149 N THR A 138
SHEET 3 C 7 VAL A 298 LYS A 302 -1 O VAL A 299 N LEU A 150
SHEET 4 C 7 ALA A 178 ASP A 186 -1 N LYS A 185 O SER A 300
SHEET 5 C 7 THR A 243 LEU A 250 -1 O ASN A 244 N PHE A 184
SHEET 6 C 7 GLN A 255 ASN A 260 -1 O ASN A 257 N THR A 249
SHEET 7 C 7 VAL A 269 THR A 270 -1 O VAL A 269 N LEU A 256
SHEET 1 D 4 TYR A 331 GLN A 335 0
SHEET 2 D 4 LEU A 339 ASP A 344 -1 O ALA A 341 N ILE A 334
SHEET 3 D 4 VAL A 350 LEU A 355 -1 O LYS A 351 N VAL A 342
SHEET 4 D 4 HIS A 358 PRO A 361 -1 O LEU A 360 N TYR A 353
SHEET 1 E 4 HIS A 375 ILE A 377 0
SHEET 2 E 4 VAL A 370 ILE A 372 -1 N VAL A 370 O ILE A 377
SHEET 3 E 4 SER A 447 SER A 449 -1 O SER A 449 N PHE A 371
SHEET 4 E 4 TRP A 549 GLN A 550 -1 O TRP A 549 N ILE A 448
SHEET 1 F 9 GLU A 380 ASN A 387 0
SHEET 2 F 9 THR A 390 ASP A 399 -1 O LYS A 396 N GLU A 380
SHEET 3 F 9 ILE A 404 VAL A 415 -1 O ALA A 406 N LEU A 397
SHEET 4 F 9 GLN A 418 ASN A 428 -1 O HIS A 420 N GLN A 413
SHEET 5 F 9 SER A 569 THR A 575 -1 O ALA A 570 N PHE A 421
SHEET 6 F 9 ALA A 508 SER A 513 -1 N TRP A 512 O LYS A 571
SHEET 7 F 9 TYR A 499 SER A 503 -1 N VAL A 502 O ALA A 509
SHEET 8 F 9 LYS A 466 ALA A 470 -1 N LYS A 466 O SER A 503
SHEET 9 F 9 ASP A 481 ASP A 485 -1 O ILE A 484 N PHE A 467
SHEET 1 G 4 VAL A 456 SER A 459 0
SHEET 2 G 4 ALA A 539 SER A 546 -1 O ILE A 544 N VAL A 456
SHEET 3 G 4 LEU A 529 VAL A 536 -1 N THR A 530 O HIS A 545
SHEET 4 G 4 ALA A 494 TYR A 497 -1 N TYR A 497 O LEU A 529
SHEET 1 H 2 ALA A 554 TYR A 555 0
SHEET 2 H 2 ILE A 558 VAL A 559 -1 O ILE A 558 N TYR A 555
SHEET 1 I 5 ILE A 609 MSE A 616 0
SHEET 2 I 5 GLY A 644 LYS A 650 1 O GLY A 646 N ALA A 611
SHEET 3 I 5 ALA A 689 ASN A 696 1 O GLY A 692 N LEU A 649
SHEET 4 I 5 PHE A 760 ASP A 764 1 O TYR A 762 N VAL A 695
SHEET 5 I 5 ARG A 792 ILE A 795 1 O ARG A 792 N ILE A 761
SHEET 1 J 3 GLU A 699 THR A 700 0
SHEET 2 J 3 GLN A 729 ASN A 732 -1 O ILE A 731 N THR A 700
SHEET 3 J 3 TYR A 722 ASN A 725 -1 N TRP A 724 O GLY A 730
SHEET 1 K10 THR A 894 ASN A 900 0
SHEET 2 K10 GLU A 918 VAL A 924 -1 O MSE A 919 N GLU A 899
SHEET 3 K10 LYS A 930 ARG A 935 -1 O ARG A 935 N MSE A 919
SHEET 4 K10 ARG A 948 LEU A 952 -1 O THR A 951 N VAL A 932
SHEET 5 K10 ARG A 955 ASP A 959 -1 O ARG A 955 N LEU A 952
SHEET 6 K10 ALA A 962 TRP A 967 -1 O LEU A 964 N ILE A 957
SHEET 7 K10 LYS A 982 ASN A 987 -1 O LYS A 982 N TRP A 967
SHEET 8 K10 TYR A1039 TYR A1042 -1 O LEU A1041 N MSE A 983
SHEET 9 K10 TYR A1007 THR A1012 -1 N TYR A1007 O TYR A1042
SHEET 10 K10 GLY A1015 GLU A1021 -1 O GLN A1020 N LEU A1008
SHEET 1 L 2 VAL A 904 ASP A 908 0
SHEET 2 L 2 SER A 911 TRP A 915 -1 O TRP A 915 N VAL A 904
SHEET 1 M 2 ALA A 992 THR A 996 0
SHEET 2 M 2 LYS A1028 ASP A1032 -1 O LEU A1031 N THR A 993
SHEET 1 N 5 THR A1073 SER A1075 0
SHEET 2 N 5 VAL A1102 LYS A1107 -1 O THR A1105 N THR A1073
SHEET 3 N 5 THR A1192 ARG A1197 -1 O LEU A1193 N GLN A1106
SHEET 4 N 5 ALA A1131 ASN A1136 -1 N SER A1132 O SER A1196
SHEET 5 N 5 GLU A1141 THR A1146 -1 O THR A1146 N ALA A1131
SHEET 1 O 5 ALA A1081 LYS A1085 0
SHEET 2 O 5 ASP A1091 ILE A1095 -1 O MSE A1092 N VAL A1084
SHEET 3 O 5 THR A1204 GLU A1213 -1 O PHE A1206 N LEU A1093
SHEET 4 O 5 LYS A1116 ASN A1125 -1 N ALA A1118 O PHE A1212
SHEET 5 O 5 GLN A1176 THR A1183 -1 O PHE A1182 N TYR A1117
SHEET 1 P 4 PHE A1230 GLN A1232 0
SHEET 2 P 4 ASP A1407 ILE A1418 -1 O ILE A1415 N PHE A1230
SHEET 3 P 4 TRP A1284 ASN A1289 -1 N THR A1288 O PHE A1408
SHEET 4 P 4 THR A1257 GLU A1261 -1 N HIS A1258 O LYS A1287
SHEET 1 Q 4 PHE A1230 GLN A1232 0
SHEET 2 Q 4 ASP A1407 ILE A1418 -1 O ILE A1415 N PHE A1230
SHEET 3 Q 4 THR A1313 ALA A1322 -1 N ARG A1315 O GLU A1416
SHEET 4 Q 4 LYS A1365 THR A1372 -1 O VAL A1371 N TYR A1314
SHEET 1 R 5 PHE A1244 VAL A1246 0
SHEET 2 R 5 ASN A1296 THR A1301 -1 O GLN A1300 N VAL A1245
SHEET 3 R 5 THR A1379 SER A1385 -1 O SER A1385 N ASN A1296
SHEET 4 R 5 TYR A1328 LYS A1334 -1 N ALA A1329 O TYR A1384
SHEET 5 R 5 GLU A1350 GLU A1353 -1 O HIS A1352 N PHE A1330
SHEET 1 S 7 TRP B 125 THR B 127 0
SHEET 2 S 7 ALA B 163 LYS B 167 -1 O GLU B 166 N GLN B 126
SHEET 3 S 7 LYS B 284 ALA B 289 -1 O LEU B 287 N PHE B 165
SHEET 4 S 7 PHE B 195 ASP B 203 -1 N PHE B 198 O LEU B 286
SHEET 5 S 7 ASN B 206 ASP B 213 -1 O VAL B 210 N VAL B 197
SHEET 6 S 7 GLY B 216 LYS B 222 -1 O PHE B 218 N GLY B 211
SHEET 7 S 7 THR B 228 TRP B 229 -1 O THR B 228 N TYR B 221
SHEET 1 T 7 THR B 136 GLU B 142 0
SHEET 2 T 7 VAL B 145 SER B 151 -1 O GLN B 149 N THR B 138
SHEET 3 T 7 VAL B 298 LYS B 302 -1 O VAL B 299 N LEU B 150
SHEET 4 T 7 ALA B 178 ASP B 186 -1 N LYS B 185 O SER B 300
SHEET 5 T 7 THR B 243 LEU B 250 -1 O ASN B 244 N PHE B 184
SHEET 6 T 7 GLN B 255 ASN B 260 -1 O SER B 259 N SER B 247
SHEET 7 T 7 VAL B 263 ASN B 264 -1 O VAL B 263 N ASN B 260
SHEET 1 U 7 THR B 136 GLU B 142 0
SHEET 2 U 7 VAL B 145 SER B 151 -1 O GLN B 149 N THR B 138
SHEET 3 U 7 VAL B 298 LYS B 302 -1 O VAL B 299 N LEU B 150
SHEET 4 U 7 ALA B 178 ASP B 186 -1 N LYS B 185 O SER B 300
SHEET 5 U 7 THR B 243 LEU B 250 -1 O ASN B 244 N PHE B 184
SHEET 6 U 7 GLN B 255 ASN B 260 -1 O SER B 259 N SER B 247
SHEET 7 U 7 VAL B 269 THR B 270 -1 O VAL B 269 N LEU B 256
SHEET 1 V 4 TYR B 331 GLN B 335 0
SHEET 2 V 4 LEU B 339 ASP B 344 -1 O ALA B 341 N ILE B 334
SHEET 3 V 4 VAL B 350 LEU B 355 -1 O LYS B 351 N VAL B 342
SHEET 4 V 4 HIS B 358 PRO B 361 -1 O LEU B 360 N TYR B 353
SHEET 1 W 4 HIS B 375 ILE B 377 0
SHEET 2 W 4 VAL B 370 ILE B 372 -1 N VAL B 370 O ILE B 377
SHEET 3 W 4 SER B 447 SER B 449 -1 O SER B 449 N PHE B 371
SHEET 4 W 4 TRP B 549 GLN B 550 -1 O TRP B 549 N ILE B 448
SHEET 1 X 9 GLU B 380 LYS B 385 0
SHEET 2 X 9 THR B 390 ASP B 399 -1 O LYS B 396 N GLU B 380
SHEET 3 X 9 ILE B 404 VAL B 415 -1 O LEU B 412 N ALA B 391
SHEET 4 X 9 GLN B 418 ASN B 428 -1 O HIS B 420 N GLN B 413
SHEET 5 X 9 SER B 569 THR B 575 -1 O ALA B 570 N PHE B 421
SHEET 6 X 9 ALA B 508 SER B 513 -1 N TRP B 512 O LYS B 571
SHEET 7 X 9 TYR B 499 SER B 503 -1 N VAL B 502 O ALA B 509
SHEET 8 X 9 LYS B 466 ALA B 470 -1 N ASP B 468 O PHE B 501
SHEET 9 X 9 ASP B 481 ASP B 485 -1 O ILE B 484 N PHE B 467
SHEET 1 Y 4 VAL B 456 SER B 459 0
SHEET 2 Y 4 ALA B 539 SER B 546 -1 O ILE B 544 N VAL B 456
SHEET 3 Y 4 LEU B 529 VAL B 536 -1 N THR B 530 O HIS B 545
SHEET 4 Y 4 ALA B 494 TYR B 497 -1 N TYR B 497 O LEU B 529
SHEET 1 Z 2 ALA B 554 TYR B 555 0
SHEET 2 Z 2 ILE B 558 VAL B 559 -1 O ILE B 558 N TYR B 555
SHEET 1 AA 5 ILE B 609 MSE B 616 0
SHEET 2 AA 5 GLY B 644 LYS B 650 1 O GLY B 646 N ALA B 611
SHEET 3 AA 5 ALA B 689 ASN B 696 1 O GLY B 692 N LEU B 649
SHEET 4 AA 5 PHE B 760 ASP B 764 1 O TYR B 762 N VAL B 695
SHEET 5 AA 5 ARG B 792 ILE B 795 1 O ARG B 792 N ILE B 761
SHEET 1 AB 2 GLU B 699 THR B 700 0
SHEET 2 AB 2 ILE B 731 ASN B 732 -1 O ILE B 731 N THR B 700
SHEET 1 AC10 THR B 894 ASN B 900 0
SHEET 2 AC10 GLU B 918 VAL B 924 -1 O VAL B 924 N THR B 894
SHEET 3 AC10 LYS B 930 ARG B 935 -1 O VAL B 933 N VAL B 921
SHEET 4 AC10 ARG B 948 LEU B 952 -1 O THR B 949 N THR B 934
SHEET 5 AC10 ARG B 955 ASP B 959 -1 O ARG B 955 N LEU B 952
SHEET 6 AC10 ALA B 962 TRP B 967 -1 O LEU B 964 N ILE B 957
SHEET 7 AC10 LYS B 982 ASN B 987 -1 O LYS B 982 N TRP B 967
SHEET 8 AC10 TYR B1039 TYR B1042 -1 O LEU B1041 N MSE B 983
SHEET 9 AC10 TYR B1007 THR B1012 -1 N TYR B1007 O TYR B1042
SHEET 10 AC10 GLY B1015 GLU B1021 -1 O GLN B1020 N LEU B1008
SHEET 1 AD 2 VAL B 904 ASP B 908 0
SHEET 2 AD 2 SER B 911 TRP B 915 -1 O TRP B 915 N VAL B 904
SHEET 1 AE 2 ALA B 992 THR B 996 0
SHEET 2 AE 2 LYS B1028 ASP B1032 -1 O LEU B1031 N THR B 993
SHEET 1 AF 5 THR B1073 SER B1075 0
SHEET 2 AF 5 VAL B1102 LYS B1107 -1 O THR B1105 N THR B1073
SHEET 3 AF 5 THR B1192 ARG B1197 -1 O LEU B1193 N GLN B1106
SHEET 4 AF 5 ALA B1131 ASN B1136 -1 N THR B1134 O THR B1194
SHEET 5 AF 5 GLU B1141 THR B1146 -1 O THR B1146 N ALA B1131
SHEET 1 AG 5 ALA B1081 LYS B1085 0
SHEET 2 AG 5 ASP B1091 ILE B1095 -1 O MSE B1092 N VAL B1084
SHEET 3 AG 5 THR B1204 GLU B1213 -1 O PHE B1206 N LEU B1093
SHEET 4 AG 5 LYS B1116 ASN B1125 -1 N TYR B1120 O ARG B1210
SHEET 5 AG 5 GLN B1176 THR B1183 -1 O MSE B1178 N VAL B1121
SHEET 1 AH 4 PHE B1230 GLN B1232 0
SHEET 2 AH 4 ASP B1407 ILE B1418 -1 O ILE B1415 N PHE B1230
SHEET 3 AH 4 TRP B1284 ASN B1289 -1 N THR B1288 O PHE B1408
SHEET 4 AH 4 THR B1257 GLU B1261 -1 N SER B1260 O SER B1285
SHEET 1 AI 4 PHE B1230 GLN B1232 0
SHEET 2 AI 4 ASP B1407 ILE B1418 -1 O ILE B1415 N PHE B1230
SHEET 3 AI 4 THR B1313 ALA B1322 -1 N ARG B1315 O GLU B1416
SHEET 4 AI 4 LYS B1365 THR B1372 -1 O VAL B1371 N TYR B1314
SHEET 1 AJ 5 PHE B1244 VAL B1246 0
SHEET 2 AJ 5 ASN B1296 THR B1301 -1 O GLN B1300 N VAL B1245
SHEET 3 AJ 5 THR B1379 SER B1385 -1 O SER B1385 N ASN B1296
SHEET 4 AJ 5 TYR B1328 LYS B1334 -1 N GLY B1333 O TRP B1380
SHEET 5 AJ 5 GLU B1350 GLU B1353 -1 O HIS B1352 N PHE B1330
LINK C LEU A 394 N MSE A 395 1555 1555 1.33
LINK C MSE A 395 N LYS A 396 1555 1555 1.32
LINK C GLU A 407 N MSE A 408 1555 1555 1.33
LINK C MSE A 408 N THR A 409 1555 1555 1.33
LINK C THR A 471 N MSE A 472 1555 1555 1.33
LINK C MSE A 472 N SER A 473 1555 1555 1.33
LINK C PRO A 489 N MSE A 490 1555 1555 1.33
LINK C MSE A 490 N LYS A 491 1555 1555 1.33
LINK C TYR A 497 N MSE A 498 1555 1555 1.33
LINK C MSE A 498 N TYR A 499 1555 1555 1.32
LINK C ILE A 596 N MSE A 597 1555 1555 1.32
LINK C MSE A 597 N ASN A 598 1555 1555 1.32
LINK C ALA A 615 N MSE A 616 1555 1555 1.33
LINK C MSE A 616 N ASN A 617 1555 1555 1.33
LINK C LEU A 627 N MSE A 628 1555 1555 1.33
LINK C MSE A 628 N THR A 629 1555 1555 1.33
LINK C SER A 860 N MSE A 861 1555 1555 1.32
LINK C MSE A 861 N LYS A 862 1555 1555 1.33
LINK C VAL A 885 N MSE A 886 1555 1555 1.33
LINK C MSE A 886 N THR A 887 1555 1555 1.33
LINK C THR A 905 N MSE A 906 1555 1555 1.33
LINK C MSE A 906 N THR A 907 1555 1555 1.33
LINK C GLU A 918 N MSE A 919 1555 1555 1.32
LINK C MSE A 919 N ARG A 920 1555 1555 1.33
LINK C LYS A 982 N MSE A 983 1555 1555 1.33
LINK C MSE A 983 N TYR A 984 1555 1555 1.33
LINK C GLU A1050 N MSE A1051 1555 1555 1.33
LINK C MSE A1051 N SER A1052 1555 1555 1.32
LINK C GLY A1056 N MSE A1057 1555 1555 1.34
LINK C MSE A1057 N HIS A1058 1555 1555 1.33
LINK C ASP A1091 N MSE A1092 1555 1555 1.34
LINK C MSE A1092 N LEU A1093 1555 1555 1.33
LINK C ASN A1177 N MSE A1178 1555 1555 1.32
LINK C MSE A1178 N TYR A1179 1555 1555 1.33
LINK C SER A1217 N MSE A1218 1555 1555 1.32
LINK C MSE A1218 N TYR A1219 1555 1555 1.33
LINK C GLU A1350 N MSE A1351 1555 1555 1.33
LINK C MSE A1351 N HIS A1352 1555 1555 1.32
LINK C PHE A1408 N MSE A1409 1555 1555 1.33
LINK C MSE A1409 N MSE A1410 1555 1555 1.32
LINK C MSE A1410 N ASP A1411 1555 1555 1.33
LINK C LYS A1423 N MSE A1424 1555 1555 1.32
LINK C MSE A1424 N LEU A1425 1555 1555 1.33
LINK C ALA A1438 N MSE A1439 1555 1555 1.34
LINK C LEU B 394 N MSE B 395 1555 1555 1.33
LINK C MSE B 395 N LYS B 396 1555 1555 1.33
LINK C GLU B 407 N MSE B 408 1555 1555 1.32
LINK C MSE B 408 N THR B 409 1555 1555 1.33
LINK C THR B 471 N MSE B 472 1555 1555 1.33
LINK C MSE B 472 N SER B 473 1555 1555 1.33
LINK C PRO B 489 N MSE B 490 1555 1555 1.33
LINK C MSE B 490 N LYS B 491 1555 1555 1.33
LINK C TYR B 497 N MSE B 498 1555 1555 1.33
LINK C MSE B 498 N TYR B 499 1555 1555 1.33
LINK C ILE B 596 N MSE B 597 1555 1555 1.33
LINK C MSE B 597 N ASN B 598 1555 1555 1.33
LINK C ALA B 615 N MSE B 616 1555 1555 1.34
LINK C MSE B 616 N ASN B 617 1555 1555 1.33
LINK C LEU B 627 N MSE B 628 1555 1555 1.33
LINK C MSE B 628 N THR B 629 1555 1555 1.33
LINK C SER B 860 N MSE B 861 1555 1555 1.33
LINK C MSE B 861 N LYS B 862 1555 1555 1.35
LINK C VAL B 885 N MSE B 886 1555 1555 1.33
LINK C MSE B 886 N THR B 887 1555 1555 1.33
LINK C THR B 905 N MSE B 906 1555 1555 1.34
LINK C MSE B 906 N THR B 907 1555 1555 1.33
LINK C GLU B 918 N MSE B 919 1555 1555 1.32
LINK C MSE B 919 N ARG B 920 1555 1555 1.32
LINK C LYS B 982 N MSE B 983 1555 1555 1.33
LINK C MSE B 983 N TYR B 984 1555 1555 1.33
LINK C GLU B1050 N MSE B1051 1555 1555 1.33
LINK C MSE B1051 N SER B1052 1555 1555 1.32
LINK C GLY B1056 N MSE B1057 1555 1555 1.33
LINK C MSE B1057 N HIS B1058 1555 1555 1.33
LINK C ASP B1091 N MSE B1092 1555 1555 1.34
LINK C MSE B1092 N LEU B1093 1555 1555 1.34
LINK C ASN B1177 N MSE B1178 1555 1555 1.32
LINK C MSE B1178 N TYR B1179 1555 1555 1.32
LINK C SER B1217 N MSE B1218 1555 1555 1.32
LINK C MSE B1218 N TYR B1219 1555 1555 1.33
LINK C GLU B1350 N MSE B1351 1555 1555 1.33
LINK C MSE B1351 N HIS B1352 1555 1555 1.33
LINK C PHE B1408 N MSE B1409 1555 1555 1.33
LINK C MSE B1409 N MSE B1410 1555 1555 1.32
LINK C MSE B1410 N ASP B1411 1555 1555 1.33
LINK C LYS B1423 N MSE B1424 1555 1555 1.32
LINK C MSE B1424 N LEU B1425 1555 1555 1.33
LINK C ALA B1438 N MSE B1439 1555 1555 1.34
LINK C MSE B1439 N THR B1440 1555 1555 1.33
LINK C SER B1446 N MSE B1447 1555 1555 1.33
LINK C MSE B1447 N ASP B1448 1555 1555 1.33
CISPEP 1 ASN A 488 PRO A 489 0 4.80
CISPEP 2 PHE A 1242 PRO A 1243 0 7.43
CISPEP 3 ASP A 1264 PRO A 1265 0 -2.75
CISPEP 4 ASN B 488 PRO B 489 0 3.48
CISPEP 5 PHE B 1242 PRO B 1243 0 10.46
CISPEP 6 ASP B 1264 PRO B 1265 0 -3.26
SITE 1 AC1 5 ASP A 577 ASN A 579 ASP A 581 LYS A 583
SITE 2 AC1 5 ASP A 588
SITE 1 AC2 6 ASP A1233 GLU A1235 GLU A1281 TRP A1284
SITE 2 AC2 6 ASP A1411 HOH A2004
SITE 1 AC3 3 GLU A 703 ASP A 728 HIS A1258
SITE 1 AC4 6 ASP A 813 THR A 815 LYS A 862 ASP A 863
SITE 2 AC4 6 TRP A 867 ARG A 870
SITE 1 AC5 6 ASP B 577 ASN B 579 ASP B 581 LYS B 583
SITE 2 AC5 6 ASP B 588 HOH B2009
SITE 1 AC6 6 ASP B1233 GLU B1235 GLU B1281 TRP B1284
SITE 2 AC6 6 ASP B1411 HOH B2014
SITE 1 AC7 3 GLU B 703 ASP B 728 HIS B1258
SITE 1 AC8 7 ASP B 813 THR B 815 LYS B 862 ASP B 863
SITE 2 AC8 7 TRP B 867 GLN B 868 ARG B 870
CRYST1 210.611 158.209 112.436 90.00 90.00 90.00 P 21 21 2 8
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 0.004748 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006321 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008894 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
