HEADER HYDROLASE 30-JUN-16 5LEZ
TITLE HUMAN 20S PROTEASOME COMPLEX WITH OPROZOMIB IN MG-ACETATE AT 2.2
TITLE 2 ANGSTROM
CAVEAT 5LEZ 6V1 U 47 HAS WRONG CHIRALITY AT ATOM C1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-2;
COMPND 3 CHAIN: A, O;
COMPND 4 SYNONYM: MACROPAIN SUBUNIT C3,MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 5 SUBUNIT C3,PROTEASOME COMPONENT C3;
COMPND 6 EC: 3.4.25.1;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-4;
COMPND 9 CHAIN: B, P;
COMPND 10 SYNONYM: MACROPAIN SUBUNIT C9,MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 11 SUBUNIT C9,PROTEASOME COMPONENT C9,PROTEASOME SUBUNIT L;
COMPND 12 EC: 3.4.25.1;
COMPND 13 MOL_ID: 3;
COMPND 14 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-7;
COMPND 15 CHAIN: C, Q;
COMPND 16 SYNONYM: PROTEASOME SUBUNIT RC6-1,PROTEASOME SUBUNIT XAPC7;
COMPND 17 EC: 3.4.25.1;
COMPND 18 MOL_ID: 4;
COMPND 19 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-5;
COMPND 20 CHAIN: D, R;
COMPND 21 SYNONYM: MACROPAIN ZETA CHAIN,MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 22 ZETA CHAIN,PROTEASOME ZETA CHAIN;
COMPND 23 EC: 3.4.25.1;
COMPND 24 MOL_ID: 5;
COMPND 25 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-1;
COMPND 26 CHAIN: E, S;
COMPND 27 SYNONYM: 30 KDA PROSOMAL PROTEIN,PROS-30,MACROPAIN SUBUNIT C2,
COMPND 28 MULTICATALYTIC ENDOPEPTIDASE COMPLEX SUBUNIT C2,PROTEASOME COMPONENT
COMPND 29 C2,PROTEASOME NU CHAIN;
COMPND 30 EC: 3.4.25.1;
COMPND 31 MOL_ID: 6;
COMPND 32 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-3;
COMPND 33 CHAIN: F, T;
COMPND 34 SYNONYM: MACROPAIN SUBUNIT C8,MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 35 SUBUNIT C8,PROTEASOME COMPONENT C8;
COMPND 36 EC: 3.4.25.1;
COMPND 37 MOL_ID: 7;
COMPND 38 MOLECULE: PROTEASOME SUBUNIT ALPHA TYPE-6;
COMPND 39 CHAIN: G, U;
COMPND 40 SYNONYM: 27 KDA PROSOMAL PROTEIN,P27K,MACROPAIN IOTA CHAIN,
COMPND 41 MULTICATALYTIC ENDOPEPTIDASE COMPLEX IOTA CHAIN,PROTEASOME IOTA
COMPND 42 CHAIN;
COMPND 43 EC: 3.4.25.1;
COMPND 44 MOL_ID: 8;
COMPND 45 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-7;
COMPND 46 CHAIN: H, V;
COMPND 47 SYNONYM: MACROPAIN CHAIN Z,MULTICATALYTIC ENDOPEPTIDASE COMPLEX CHAIN
COMPND 48 Z,PROTEASOME SUBUNIT Z;
COMPND 49 EC: 3.4.25.1;
COMPND 50 MOL_ID: 9;
COMPND 51 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-3;
COMPND 52 CHAIN: I, W;
COMPND 53 SYNONYM: PROTEASOME CHAIN 13,PROTEASOME COMPONENT C10-II,PROTEASOME
COMPND 54 THETA CHAIN;
COMPND 55 EC: 3.4.25.1;
COMPND 56 MOL_ID: 10;
COMPND 57 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-2;
COMPND 58 CHAIN: J, X;
COMPND 59 SYNONYM: MACROPAIN SUBUNIT C7-I,MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 60 SUBUNIT C7-I,PROTEASOME COMPONENT C7-I;
COMPND 61 EC: 3.4.25.1;
COMPND 62 MOL_ID: 11;
COMPND 63 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-5;
COMPND 64 CHAIN: K, Y;
COMPND 65 SYNONYM: MACROPAIN EPSILON CHAIN,MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 66 EPSILON CHAIN,PROTEASOME CHAIN 6,PROTEASOME EPSILON CHAIN,PROTEASOME
COMPND 67 SUBUNIT MB1,PROTEASOME SUBUNIT X;
COMPND 68 EC: 3.4.25.1;
COMPND 69 MOL_ID: 12;
COMPND 70 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-1;
COMPND 71 CHAIN: L, Z;
COMPND 72 SYNONYM: MACROPAIN SUBUNIT C5,MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 73 SUBUNIT C5,PROTEASOME COMPONENT C5,PROTEASOME GAMMA CHAIN;
COMPND 74 EC: 3.4.25.1;
COMPND 75 MOL_ID: 13;
COMPND 76 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-4;
COMPND 77 CHAIN: M, a;
COMPND 78 SYNONYM: 26 KDA PROSOMAL PROTEIN,PROS-26,MACROPAIN BETA CHAIN,
COMPND 79 MULTICATALYTIC ENDOPEPTIDASE COMPLEX BETA CHAIN,PROTEASOME BETA
COMPND 80 CHAIN,PROTEASOME CHAIN 3,HSN3;
COMPND 81 EC: 3.4.25.1;
COMPND 82 MOL_ID: 14;
COMPND 83 MOLECULE: PROTEASOME SUBUNIT BETA TYPE-6;
COMPND 84 CHAIN: N, b;
COMPND 85 SYNONYM: MACROPAIN DELTA CHAIN,MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 86 DELTA CHAIN,PROTEASOME DELTA CHAIN,PROTEASOME SUBUNIT Y;
COMPND 87 EC: 3.4.25.1;
COMPND 88 MOL_ID: 15;
COMPND 89 MOLECULE: BOUND OPROZOMIB;
COMPND 90 CHAIN: c, d, e, f;
COMPND 91 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 CELL_LINE: HELA;
SOURCE 6 MOL_ID: 2;
SOURCE 7 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 8 ORGANISM_COMMON: HUMAN;
SOURCE 9 ORGANISM_TAXID: 9606;
SOURCE 10 CELL_LINE: HELA;
SOURCE 11 MOL_ID: 3;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 CELL_LINE: HELA;
SOURCE 16 MOL_ID: 4;
SOURCE 17 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 18 ORGANISM_COMMON: HUMAN;
SOURCE 19 ORGANISM_TAXID: 9606;
SOURCE 20 CELL_LINE: HELA;
SOURCE 21 MOL_ID: 5;
SOURCE 22 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 23 ORGANISM_COMMON: HUMAN;
SOURCE 24 ORGANISM_TAXID: 9606;
SOURCE 25 CELL_LINE: HELA;
SOURCE 26 MOL_ID: 6;
SOURCE 27 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 28 ORGANISM_COMMON: HUMAN;
SOURCE 29 ORGANISM_TAXID: 9606;
SOURCE 30 CELL_LINE: HELA;
SOURCE 31 MOL_ID: 7;
SOURCE 32 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 33 ORGANISM_COMMON: HUMAN;
SOURCE 34 ORGANISM_TAXID: 9606;
SOURCE 35 CELL_LINE: HELA;
SOURCE 36 MOL_ID: 8;
SOURCE 37 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 38 ORGANISM_COMMON: HUMAN;
SOURCE 39 ORGANISM_TAXID: 9606;
SOURCE 40 CELL_LINE: HELA;
SOURCE 41 MOL_ID: 9;
SOURCE 42 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 43 ORGANISM_COMMON: HUMAN;
SOURCE 44 ORGANISM_TAXID: 9606;
SOURCE 45 CELL_LINE: HELA;
SOURCE 46 MOL_ID: 10;
SOURCE 47 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 48 ORGANISM_COMMON: HUMAN;
SOURCE 49 ORGANISM_TAXID: 9606;
SOURCE 50 CELL_LINE: HELA;
SOURCE 51 MOL_ID: 11;
SOURCE 52 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 53 ORGANISM_COMMON: HUMAN;
SOURCE 54 ORGANISM_TAXID: 9606;
SOURCE 55 CELL_LINE: HELA;
SOURCE 56 MOL_ID: 12;
SOURCE 57 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 58 ORGANISM_COMMON: HUMAN;
SOURCE 59 ORGANISM_TAXID: 9606;
SOURCE 60 CELL_LINE: HELA;
SOURCE 61 MOL_ID: 13;
SOURCE 62 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 63 ORGANISM_COMMON: HUMAN;
SOURCE 64 ORGANISM_TAXID: 9606;
SOURCE 65 CELL_LINE: HELA;
SOURCE 66 MOL_ID: 14;
SOURCE 67 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 68 ORGANISM_COMMON: HUMAN;
SOURCE 69 ORGANISM_TAXID: 9606;
SOURCE 70 CELL_LINE: HELA;
SOURCE 71 MOL_ID: 15;
SOURCE 72 SYNTHETIC: YES;
SOURCE 73 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 74 ORGANISM_TAXID: 32630
KEYWDS PROTEASOME, MULTICATALYTIC PROTEINASE, NTN-HYDROLASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.SCHRADER,F.HENNEBERG,R.MATA,K.TITTMANN,T.R.SCHNEIDER,H.STARK,
AUTHOR 2 G.BOURENKOV,A.CHARI
REVDAT 4 10-JAN-24 5LEZ 1 REMARK
REVDAT 3 15-NOV-23 5LEZ 1 LINK ATOM
REVDAT 2 06-SEP-17 5LEZ 1 REMARK
REVDAT 1 17-AUG-16 5LEZ 0
JRNL AUTH J.SCHRADER,F.HENNEBERG,R.A.MATA,K.TITTMANN,T.R.SCHNEIDER,
JRNL AUTH 2 H.STARK,G.BOURENKOV,A.CHARI
JRNL TITL THE INHIBITION MECHANISM OF HUMAN 20S PROTEASOMES ENABLES
JRNL TITL 2 NEXT-GENERATION INHIBITOR DESIGN.
JRNL REF SCIENCE V. 353 594 2016
JRNL REFN ESSN 1095-9203
JRNL PMID 27493187
JRNL DOI 10.1126/SCIENCE.AAF8993
REMARK 2
REMARK 2 RESOLUTION. 2.19 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0103
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) : 2.19
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 170.81
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 351230
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) : 0.183
REMARK 3 R VALUE (WORKING SET) : 0.181
REMARK 3 FREE R VALUE : 0.222
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 18458
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) : 2.19
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.25
REMARK 3 REFLECTION IN BIN (WORKING SET) : 24262
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.63
REMARK 3 BIN R VALUE (WORKING SET) : 0.3450
REMARK 3 BIN FREE R VALUE SET COUNT : 1236
REMARK 3 BIN FREE R VALUE : 0.3600
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 47986
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 176
REMARK 3 SOLVENT ATOMS : 3717
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 63.61
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.72000
REMARK 3 B22 (A**2) : 0.15000
REMARK 3 B33 (A**2) : 0.57000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.245
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.191
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.190
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 15.560
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.967
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.946
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 49451 ; 0.015 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 46959 ; 0.005 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 66928 ; 1.746 ; 1.972
REMARK 3 BOND ANGLES OTHERS (DEGREES):107761 ; 1.310 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 6302 ; 7.212 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 2127 ;35.559 ;23.705
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 8267 ;16.013 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 341 ;17.835 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 7548 ; 0.103 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 56242 ; 0.008 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 11231 ; 0.005 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 25039 ; 1.262 ; 2.686
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 25034 ; 1.261 ; 2.685
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 31276 ; 2.050 ; 4.020
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 31277 ; 2.050 ; 4.020
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 24412 ; 2.040 ; 2.929
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 24413 ; 2.040 ; 2.929
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 35613 ; 2.828 ; 4.295
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 56704 ; 9.545 ;23.310
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 56705 ; 9.545 ;23.310
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 : 14
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 3 232 O 3 232 25878 0.07 0.05
REMARK 3 2 B 2 249 P 2 249 27676 0.08 0.05
REMARK 3 3 C 2 237 Q 2 237 24996 0.10 0.05
REMARK 3 4 D 9 241 R 9 241 26224 0.08 0.05
REMARK 3 5 E 4 236 S 4 236 27274 0.08 0.05
REMARK 3 6 F 6 243 T 6 243 27872 0.08 0.05
REMARK 3 7 G 2 245 U 2 245 26334 0.08 0.05
REMARK 3 8 H 1 220 V 1 220 24460 0.07 0.05
REMARK 3 9 I 1 204 W 1 204 25580 0.07 0.05
REMARK 3 10 J 1 196 X 1 196 24658 0.07 0.05
REMARK 3 11 K 1 199 Y 1 199 23384 0.08 0.05
REMARK 3 12 L 1 213 Z 1 213 24576 0.06 0.05
REMARK 3 13 M 1 216 a 1 216 24894 0.07 0.05
REMARK 3 14 N 1 201 b 1 201 23258 0.08 0.05
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 28
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 3 A 232
REMARK 3 ORIGIN FOR THE GROUP (A): 77.4554 206.9419 1.1335
REMARK 3 T TENSOR
REMARK 3 T11: 0.5234 T22: 0.3718
REMARK 3 T33: 0.1831 T12: 0.1726
REMARK 3 T13: 0.1385 T23: 0.0855
REMARK 3 L TENSOR
REMARK 3 L11: 1.7187 L22: 2.1370
REMARK 3 L33: 2.0109 L12: 0.3054
REMARK 3 L13: 0.5303 L23: 0.0572
REMARK 3 S TENSOR
REMARK 3 S11: -0.0683 S12: 0.1132 S13: 0.0987
REMARK 3 S21: -0.1699 S22: -0.0333 S23: -0.4839
REMARK 3 S31: 0.1093 S32: 0.7093 S33: 0.1016
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 2 B 249
REMARK 3 ORIGIN FOR THE GROUP (A): 65.5419 177.9502 0.0816
REMARK 3 T TENSOR
REMARK 3 T11: 0.8819 T22: 0.2003
REMARK 3 T33: 0.1988 T12: 0.2256
REMARK 3 T13: 0.1215 T23: -0.0212
REMARK 3 L TENSOR
REMARK 3 L11: 0.8815 L22: 2.1551
REMARK 3 L33: 1.4849 L12: -0.0996
REMARK 3 L13: 0.0744 L23: -0.3071
REMARK 3 S TENSOR
REMARK 3 S11: -0.0662 S12: 0.2134 S13: -0.2211
REMARK 3 S21: -0.2708 S22: -0.0507 S23: -0.3647
REMARK 3 S31: 0.3969 S32: 0.4327 S33: 0.1169
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 2 C 238
REMARK 3 ORIGIN FOR THE GROUP (A): 34.7477 169.9260 -3.8892
REMARK 3 T TENSOR
REMARK 3 T11: 1.0181 T22: 0.1469
REMARK 3 T33: 0.3284 T12: -0.0907
REMARK 3 T13: -0.0880 T23: -0.0444
REMARK 3 L TENSOR
REMARK 3 L11: 2.2502 L22: 2.8968
REMARK 3 L33: 2.1621 L12: 0.1300
REMARK 3 L13: 0.5932 L23: -0.4071
REMARK 3 S TENSOR
REMARK 3 S11: 0.0895 S12: 0.0345 S13: -0.6985
REMARK 3 S21: -0.3344 S22: 0.0167 S23: -0.0309
REMARK 3 S31: 0.6575 S32: -0.0621 S33: -0.1062
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 9 D 241
REMARK 3 ORIGIN FOR THE GROUP (A): 10.8903 188.5074 -8.1030
REMARK 3 T TENSOR
REMARK 3 T11: 0.8438 T22: 0.3787
REMARK 3 T33: 0.3812 T12: -0.1791
REMARK 3 T13: -0.2902 T23: 0.0283
REMARK 3 L TENSOR
REMARK 3 L11: 0.6449 L22: 1.3038
REMARK 3 L33: 2.1438 L12: 0.0057
REMARK 3 L13: -1.0594 L23: -0.0515
REMARK 3 S TENSOR
REMARK 3 S11: -0.0472 S12: 0.2156 S13: -0.2237
REMARK 3 S21: -0.2933 S22: 0.0093 S23: 0.2404
REMARK 3 S31: 0.4456 S32: -0.5249 S33: 0.0379
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 4 E 237
REMARK 3 ORIGIN FOR THE GROUP (A): 9.8310 219.9040 -9.0000
REMARK 3 T TENSOR
REMARK 3 T11: 0.5270 T22: 0.2944
REMARK 3 T33: 0.1906 T12: -0.0710
REMARK 3 T13: -0.1540 T23: 0.0306
REMARK 3 L TENSOR
REMARK 3 L11: 1.9825 L22: 0.9822
REMARK 3 L33: 1.4948 L12: -0.3044
REMARK 3 L13: -0.0458 L23: -0.0689
REMARK 3 S TENSOR
REMARK 3 S11: 0.0380 S12: 0.1504 S13: -0.2749
REMARK 3 S21: -0.1060 S22: -0.0258 S23: 0.2832
REMARK 3 S31: 0.2077 S32: -0.5827 S33: -0.0122
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : F 6 F 244
REMARK 3 ORIGIN FOR THE GROUP (A): 32.3940 240.1010 -7.5840
REMARK 3 T TENSOR
REMARK 3 T11: 0.4465 T22: 0.0924
REMARK 3 T33: 0.1615 T12: 0.0108
REMARK 3 T13: -0.0874 T23: 0.0505
REMARK 3 L TENSOR
REMARK 3 L11: 1.8745 L22: 1.8914
REMARK 3 L33: 1.2017 L12: -0.6097
REMARK 3 L13: -0.2685 L23: -0.1058
REMARK 3 S TENSOR
REMARK 3 S11: 0.0576 S12: 0.1620 S13: 0.2483
REMARK 3 S21: -0.1763 S22: -0.0561 S23: 0.2286
REMARK 3 S31: -0.1200 S32: -0.1231 S33: -0.0015
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 : G 2 G 245
REMARK 3 ORIGIN FOR THE GROUP (A): 64.0170 233.5870 -3.6720
REMARK 3 T TENSOR
REMARK 3 T11: 0.4287 T22: 0.2309
REMARK 3 T33: 0.1778 T12: 0.0236
REMARK 3 T13: 0.0626 T23: 0.1586
REMARK 3 L TENSOR
REMARK 3 L11: 0.9571 L22: 2.7175
REMARK 3 L33: 1.7792 L12: 0.2151
REMARK 3 L13: 0.1373 L23: 0.6937
REMARK 3 S TENSOR
REMARK 3 S11: 0.0685 S12: 0.2648 S13: 0.2613
REMARK 3 S21: -0.3618 S22: -0.1433 S23: -0.2181
REMARK 3 S31: -0.2178 S32: 0.4045 S33: 0.0749
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 : H 1 H 220
REMARK 3 ORIGIN FOR THE GROUP (A): 71.3520 213.9320 39.4390
REMARK 3 T TENSOR
REMARK 3 T11: 0.2738 T22: 0.3285
REMARK 3 T33: 0.1175 T12: -0.0144
REMARK 3 T13: 0.0640 T23: 0.1040
REMARK 3 L TENSOR
REMARK 3 L11: 0.3869 L22: 1.7442
REMARK 3 L33: 1.0350 L12: -0.0126
REMARK 3 L13: -0.0947 L23: -0.2505
REMARK 3 S TENSOR
REMARK 3 S11: -0.0116 S12: -0.0138 S13: -0.1230
REMARK 3 S21: 0.0039 S22: -0.1480 S23: -0.1676
REMARK 3 S31: 0.0240 S32: 0.5491 S33: 0.1596
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 : I 1 I 204
REMARK 3 ORIGIN FOR THE GROUP (A): 66.5710 186.5180 39.5490
REMARK 3 T TENSOR
REMARK 3 T11: 0.4611 T22: 0.2854
REMARK 3 T33: 0.1070 T12: 0.1947
REMARK 3 T13: 0.1189 T23: 0.1290
REMARK 3 L TENSOR
REMARK 3 L11: 0.3217 L22: 1.3099
REMARK 3 L33: 2.0204 L12: 0.2321
REMARK 3 L13: 0.5480 L23: -0.6626
REMARK 3 S TENSOR
REMARK 3 S11: 0.0360 S12: 0.0969 S13: -0.0118
REMARK 3 S21: -0.1890 S22: -0.2586 S23: -0.1867
REMARK 3 S31: 0.2788 S32: 0.6030 S33: 0.2225
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 : J 1 J 196
REMARK 3 ORIGIN FOR THE GROUP (A): 39.1290 170.2650 36.2700
REMARK 3 T TENSOR
REMARK 3 T11: 0.6951 T22: 0.0301
REMARK 3 T33: 0.1752 T12: 0.0133
REMARK 3 T13: -0.0079 T23: -0.0071
REMARK 3 L TENSOR
REMARK 3 L11: 1.0337 L22: 1.0288
REMARK 3 L33: 3.1718 L12: 0.4626
REMARK 3 L13: -0.1158 L23: -0.2882
REMARK 3 S TENSOR
REMARK 3 S11: -0.0557 S12: 0.0855 S13: -0.1183
REMARK 3 S21: -0.3000 S22: -0.0358 S23: 0.1972
REMARK 3 S31: 0.6796 S32: -0.1097 S33: 0.0915
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 : K 1 K 200
REMARK 3 ORIGIN FOR THE GROUP (A): 8.0340 180.7830 32.2280
REMARK 3 T TENSOR
REMARK 3 T11: 0.5300 T22: 0.2868
REMARK 3 T33: 0.3330 T12: -0.2726
REMARK 3 T13: -0.1851 T23: 0.1031
REMARK 3 L TENSOR
REMARK 3 L11: 1.0550 L22: 2.0313
REMARK 3 L33: 1.8327 L12: -0.2544
REMARK 3 L13: -0.5230 L23: 0.4096
REMARK 3 S TENSOR
REMARK 3 S11: -0.0313 S12: 0.1300 S13: -0.1742
REMARK 3 S21: -0.2584 S22: 0.0166 S23: 0.2946
REMARK 3 S31: 0.4216 S32: -0.5309 S33: 0.0147
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 : L 1 L 213
REMARK 3 ORIGIN FOR THE GROUP (A): -1.5750 210.2690 30.8530
REMARK 3 T TENSOR
REMARK 3 T11: 0.3777 T22: 0.5208
REMARK 3 T33: 0.3948 T12: -0.0920
REMARK 3 T13: -0.1546 T23: 0.1825
REMARK 3 L TENSOR
REMARK 3 L11: 0.9520 L22: 1.2517
REMARK 3 L33: 1.2397 L12: -0.1435
REMARK 3 L13: -0.4678 L23: 0.3854
REMARK 3 S TENSOR
REMARK 3 S11: 0.0071 S12: -0.0246 S13: -0.0177
REMARK 3 S21: -0.1859 S22: 0.0659 S23: 0.4652
REMARK 3 S31: -0.0355 S32: -0.6553 S33: -0.0730
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 : M 1 M 216
REMARK 3 ORIGIN FOR THE GROUP (A): 16.3020 237.9210 33.1160
REMARK 3 T TENSOR
REMARK 3 T11: 0.3981 T22: 0.1832
REMARK 3 T33: 0.2149 T12: 0.1021
REMARK 3 T13: -0.0142 T23: 0.0776
REMARK 3 L TENSOR
REMARK 3 L11: 0.9328 L22: 1.1625
REMARK 3 L33: 2.2222 L12: 0.2271
REMARK 3 L13: 0.0560 L23: 0.3285
REMARK 3 S TENSOR
REMARK 3 S11: -0.0182 S12: -0.0135 S13: 0.1471
REMARK 3 S21: 0.0306 S22: 0.1170 S23: 0.2378
REMARK 3 S31: -0.4173 S32: -0.4327 S33: -0.0988
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 : N 1 N 202
REMARK 3 ORIGIN FOR THE GROUP (A): 48.7740 241.4350 35.6530
REMARK 3 T TENSOR
REMARK 3 T11: 0.4304 T22: 0.0310
REMARK 3 T33: 0.0808 T12: -0.0988
REMARK 3 T13: 0.0077 T23: 0.0142
REMARK 3 L TENSOR
REMARK 3 L11: 1.7351 L22: 1.2464
REMARK 3 L33: 2.4266 L12: -0.4124
REMARK 3 L13: 0.2681 L23: -0.3296
REMARK 3 S TENSOR
REMARK 3 S11: 0.0343 S12: 0.0112 S13: 0.0886
REMARK 3 S21: 0.0169 S22: -0.0729 S23: -0.0122
REMARK 3 S31: -0.4025 S32: 0.1681 S33: 0.0387
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 : O 3 O 232
REMARK 3 ORIGIN FOR THE GROUP (A): -7.2410 225.9840 103.0230
REMARK 3 T TENSOR
REMARK 3 T11: 0.5436 T22: 0.6901
REMARK 3 T33: 0.5675 T12: 0.2464
REMARK 3 T13: 0.2599 T23: 0.0506
REMARK 3 L TENSOR
REMARK 3 L11: 1.1667 L22: 1.8281
REMARK 3 L33: 2.3320 L12: 0.1699
REMARK 3 L13: 0.5349 L23: -0.0104
REMARK 3 S TENSOR
REMARK 3 S11: -0.0549 S12: -0.1475 S13: 0.3208
REMARK 3 S21: 0.1545 S22: 0.0216 S23: 0.6198
REMARK 3 S31: -0.4727 S32: -0.6430 S33: 0.0333
REMARK 3
REMARK 3 TLS GROUP : 16
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : P 2 P 248
REMARK 3 ORIGIN FOR THE GROUP (A): -8.3110 194.6577 104.2640
REMARK 3 T TENSOR
REMARK 3 T11: 0.4112 T22: 0.8144
REMARK 3 T33: 0.5607 T12: -0.0387
REMARK 3 T13: 0.2228 T23: 0.1784
REMARK 3 L TENSOR
REMARK 3 L11: 0.9149 L22: 1.5169
REMARK 3 L33: 1.4918 L12: 0.3503
REMARK 3 L13: 0.2888 L23: 0.4633
REMARK 3 S TENSOR
REMARK 3 S11: -0.0415 S12: -0.2873 S13: -0.0068
REMARK 3 S21: 0.1975 S22: 0.0135 S23: 0.6238
REMARK 3 S31: -0.0107 S32: -0.8830 S33: 0.0279
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 : Q 2 Q 240
REMARK 3 ORIGIN FOR THE GROUP (A): 15.5155 174.6605 108.9933
REMARK 3 T TENSOR
REMARK 3 T11: 0.6065 T22: 0.3873
REMARK 3 T33: 0.5616 T12: -0.1281
REMARK 3 T13: 0.0572 T23: 0.1212
REMARK 3 L TENSOR
REMARK 3 L11: 3.0933 L22: 2.2353
REMARK 3 L33: 2.6359 L12: 0.2744
REMARK 3 L13: 0.6907 L23: 0.4935
REMARK 3 S TENSOR
REMARK 3 S11: 0.2474 S12: -0.1038 S13: -0.9069
REMARK 3 S21: 0.1811 S22: -0.0340 S23: 0.4648
REMARK 3 S31: 0.7292 S32: -0.5220 S33: -0.2134
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 : R 9 R 241
REMARK 3 ORIGIN FOR THE GROUP (A): 45.6739 181.5500 112.5668
REMARK 3 T TENSOR
REMARK 3 T11: 0.4515 T22: 0.2481
REMARK 3 T33: 0.2094 T12: -0.0168
REMARK 3 T13: 0.0822 T23: 0.1070
REMARK 3 L TENSOR
REMARK 3 L11: 0.7512 L22: 1.3256
REMARK 3 L33: 2.1210 L12: -0.0377
REMARK 3 L13: -0.3507 L23: -0.0296
REMARK 3 S TENSOR
REMARK 3 S11: -0.0640 S12: -0.1841 S13: -0.2947
REMARK 3 S21: 0.1669 S22: 0.0143 S23: 0.1414
REMARK 3 S31: 0.4000 S32: 0.0855 S33: 0.0497
REMARK 3
REMARK 3 TLS GROUP : 19
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : S 4 S 239
REMARK 3 ORIGIN FOR THE GROUP (A): 58.7606 210.1815 113.7620
REMARK 3 T TENSOR
REMARK 3 T11: 0.4836 T22: 0.3777
REMARK 3 T33: 0.1093 T12: -0.1412
REMARK 3 T13: -0.0105 T23: 0.0574
REMARK 3 L TENSOR
REMARK 3 L11: 1.7142 L22: 1.5082
REMARK 3 L33: 1.7019 L12: -0.1338
REMARK 3 L13: -0.0234 L23: -0.2340
REMARK 3 S TENSOR
REMARK 3 S11: -0.0529 S12: -0.4033 S13: -0.1351
REMARK 3 S21: 0.3194 S22: -0.0506 S23: -0.2287
REMARK 3 S31: -0.1211 S32: 0.5987 S33: 0.1035
REMARK 3
REMARK 3 TLS GROUP : 20
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : T 5 T 244
REMARK 3 ORIGIN FOR THE GROUP (A): 46.8258 237.8708 111.4932
REMARK 3 T TENSOR
REMARK 3 T11: 0.8026 T22: 0.2036
REMARK 3 T33: 0.1380 T12: -0.1387
REMARK 3 T13: 0.0875 T23: -0.0783
REMARK 3 L TENSOR
REMARK 3 L11: 2.3755 L22: 2.2125
REMARK 3 L33: 1.5548 L12: 0.7007
REMARK 3 L13: -0.9057 L23: 0.0199
REMARK 3 S TENSOR
REMARK 3 S11: 0.2140 S12: -0.4963 S13: 0.1179
REMARK 3 S21: 0.2153 S22: -0.1061 S23: -0.2097
REMARK 3 S31: -0.6557 S32: 0.3500 S33: -0.1079
REMARK 3
REMARK 3 TLS GROUP : 21
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : U 2 U 245
REMARK 3 ORIGIN FOR THE GROUP (A): 16.1670 244.8160 107.1851
REMARK 3 T TENSOR
REMARK 3 T11: 0.8783 T22: 0.3308
REMARK 3 T33: 0.3675 T12: 0.2141
REMARK 3 T13: 0.1627 T23: -0.0817
REMARK 3 L TENSOR
REMARK 3 L11: 1.7010 L22: 1.5221
REMARK 3 L33: 0.9921 L12: 0.3439
REMARK 3 L13: -0.0526 L23: -0.2108
REMARK 3 S TENSOR
REMARK 3 S11: -0.0741 S12: -0.2578 S13: 0.4416
REMARK 3 S21: 0.2607 S22: 0.0051 S23: 0.1812
REMARK 3 S31: -0.5953 S32: -0.2097 S33: 0.0690
REMARK 3
REMARK 3 TLS GROUP : 22
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : V 1 V 220
REMARK 3 ORIGIN FOR THE GROUP (A): 1.3273 230.5893 64.8677
REMARK 3 T TENSOR
REMARK 3 T11: 0.4041 T22: 0.4408
REMARK 3 T33: 0.3650 T12: 0.1898
REMARK 3 T13: 0.1166 T23: 0.0988
REMARK 3 L TENSOR
REMARK 3 L11: 0.9359 L22: 1.4883
REMARK 3 L33: 1.0396 L12: 0.3567
REMARK 3 L13: 0.0453 L23: -0.0875
REMARK 3 S TENSOR
REMARK 3 S11: 0.0078 S12: -0.0322 S13: 0.0142
REMARK 3 S21: 0.0849 S22: 0.1142 S23: 0.3317
REMARK 3 S31: -0.2444 S32: -0.5970 S33: -0.1220
REMARK 3
REMARK 3 TLS GROUP : 23
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : W 1 W 204
REMARK 3 ORIGIN FOR THE GROUP (A): -6.0788 203.0326 64.6968
REMARK 3 T TENSOR
REMARK 3 T11: 0.2692 T22: 0.6426
REMARK 3 T33: 0.5090 T12: -0.0412
REMARK 3 T13: 0.0618 T23: 0.2031
REMARK 3 L TENSOR
REMARK 3 L11: 0.5435 L22: 1.0872
REMARK 3 L33: 2.0361 L12: 0.0735
REMARK 3 L13: 0.5280 L23: 0.6087
REMARK 3 S TENSOR
REMARK 3 S11: -0.0146 S12: -0.0625 S13: 0.0437
REMARK 3 S21: 0.0126 S22: 0.0818 S23: 0.4209
REMARK 3 S31: -0.1177 S32: -0.8336 S33: -0.0672
REMARK 3
REMARK 3 TLS GROUP : 24
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : X 1 X 196
REMARK 3 ORIGIN FOR THE GROUP (A): 11.7436 176.7044 68.1642
REMARK 3 T TENSOR
REMARK 3 T11: 0.4189 T22: 0.2331
REMARK 3 T33: 0.3413 T12: -0.2283
REMARK 3 T13: -0.0148 T23: 0.0992
REMARK 3 L TENSOR
REMARK 3 L11: 0.7991 L22: 1.0521
REMARK 3 L33: 2.3381 L12: -0.2916
REMARK 3 L13: -0.2971 L23: 0.0378
REMARK 3 S TENSOR
REMARK 3 S11: -0.0319 S12: -0.0936 S13: -0.1132
REMARK 3 S21: -0.0204 S22: 0.1360 S23: 0.1592
REMARK 3 S31: 0.4598 S32: -0.3211 S33: -0.1041
REMARK 3
REMARK 3 TLS GROUP : 25
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : Y 1 Y 199
REMARK 3 ORIGIN FOR THE GROUP (A): 44.2968 173.2184 72.6744
REMARK 3 T TENSOR
REMARK 3 T11: 0.4371 T22: 0.0616
REMARK 3 T33: 0.1072 T12: 0.0494
REMARK 3 T13: 0.0402 T23: 0.0538
REMARK 3 L TENSOR
REMARK 3 L11: 1.4876 L22: 1.6936
REMARK 3 L33: 2.3902 L12: 0.5605
REMARK 3 L13: -0.4798 L23: -0.1760
REMARK 3 S TENSOR
REMARK 3 S11: -0.0130 S12: -0.2555 S13: -0.0895
REMARK 3 S21: 0.0202 S22: -0.0894 S23: 0.0716
REMARK 3 S31: 0.5544 S32: 0.1447 S33: 0.1023
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 : Z 1 Z 213
REMARK 3 ORIGIN FOR THE GROUP (A): 65.9180 196.0161 73.8396
REMARK 3 T TENSOR
REMARK 3 T11: 0.2355 T22: 0.3044
REMARK 3 T33: 0.1061 T12: 0.0004
REMARK 3 T13: 0.0437 T23: 0.1121
REMARK 3 L TENSOR
REMARK 3 L11: 0.9728 L22: 1.6375
REMARK 3 L33: 1.5682 L12: -0.1391
REMARK 3 L13: -0.5008 L23: -0.2143
REMARK 3 S TENSOR
REMARK 3 S11: 0.0286 S12: -0.0885 S13: 0.0014
REMARK 3 S21: 0.0584 S22: -0.1981 S23: -0.2294
REMARK 3 S31: 0.0722 S32: 0.6249 S33: 0.1695
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 : a 1 a 216
REMARK 3 ORIGIN FOR THE GROUP (A): 60.8025 228.6691 70.8451
REMARK 3 T TENSOR
REMARK 3 T11: 0.3955 T22: 0.1651
REMARK 3 T33: 0.0712 T12: -0.1764
REMARK 3 T13: -0.0015 T23: 0.0257
REMARK 3 L TENSOR
REMARK 3 L11: 0.8763 L22: 1.4266
REMARK 3 L33: 2.1810 L12: -0.0124
REMARK 3 L13: -0.3078 L23: -0.5893
REMARK 3 S TENSOR
REMARK 3 S11: 0.0364 S12: -0.0554 S13: 0.1015
REMARK 3 S21: 0.1410 S22: -0.1476 S23: -0.0927
REMARK 3 S31: -0.4554 S32: 0.4706 S33: 0.1112
REMARK 3
REMARK 3 TLS GROUP : 28
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : b 1 b 203
REMARK 3 ORIGIN FOR THE GROUP (A): 32.7143 245.5630 67.7579
REMARK 3 T TENSOR
REMARK 3 T11: 0.5902 T22: 0.0188
REMARK 3 T33: 0.1363 T12: 0.0399
REMARK 3 T13: 0.0584 T23: -0.0397
REMARK 3 L TENSOR
REMARK 3 L11: 1.8259 L22: 1.3913
REMARK 3 L33: 2.3752 L12: -0.0944
REMARK 3 L13: 0.1717 L23: -0.2536
REMARK 3 S TENSOR
REMARK 3 S11: 0.0108 S12: -0.0362 S13: 0.1056
REMARK 3 S21: 0.1636 S22: -0.0232 S23: 0.1377
REMARK 3 S31: -0.5263 S32: -0.1105 S33: 0.0124
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 5LEZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 04-JUL-16.
REMARK 100 THE DEPOSITION ID IS D_1200000583.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-NOV-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PETRA III, EMBL C/O DESY
REMARK 200 BEAMLINE : P14 (MX2)
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9763
REMARK 200 MONOCHROMATOR : SI (111)
REMARK 200 OPTICS : CRL TRANSFOCATOR
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 351230
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.190
REMARK 200 RESOLUTION RANGE LOW (A) : 170.810
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 7.150
REMARK 200 R MERGE (I) : 0.07800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.19
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.27
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.3
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 : 1.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: 5LE5
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.65
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BIS-TRIS, 0.2 M MAGNESIUM
REMARK 280 CHLORIDE, 10 % PEG3350, PH 6.5, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 56.93000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 157.61000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 101.61500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 157.61000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 56.93000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 101.61500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: 32-MERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 121790 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 211800 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -489.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J,
REMARK 350 AND CHAINS: K, L, M, N, O, P, Q, R, S,
REMARK 350 AND CHAINS: T, U, V, W, X, Y, Z, a, b, c,
REMARK 350 AND CHAINS: d, e, f
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 0
REMARK 465 ALA A 1
REMARK 465 GLU A 2
REMARK 465 ALA A 233
REMARK 465 MET B 1
REMARK 465 GLU B 250
REMARK 465 LYS B 251
REMARK 465 LYS B 252
REMARK 465 GLU B 253
REMARK 465 LYS B 254
REMARK 465 GLU B 255
REMARK 465 GLN B 256
REMARK 465 LYS B 257
REMARK 465 GLU B 258
REMARK 465 LYS B 259
REMARK 465 ASP B 260
REMARK 465 LYS B 261
REMARK 465 MET C 1
REMARK 465 ASN C 239
REMARK 465 GLU C 240
REMARK 465 LYS C 241
REMARK 465 LYS C 242
REMARK 465 LYS C 243
REMARK 465 GLN C 244
REMARK 465 LYS C 245
REMARK 465 LYS C 246
REMARK 465 ALA C 247
REMARK 465 SER C 248
REMARK 465 MET D 1
REMARK 465 PHE D 2
REMARK 465 LEU D 3
REMARK 465 THR D 4
REMARK 465 ARG D 5
REMARK 465 SER D 6
REMARK 465 GLU D 7
REMARK 465 TYR D 8
REMARK 465 MET E 1
REMARK 465 PHE E 2
REMARK 465 ARG E 3
REMARK 465 GLU E 238
REMARK 465 ARG E 239
REMARK 465 PRO E 240
REMARK 465 GLN E 241
REMARK 465 ARG E 242
REMARK 465 LYS E 243
REMARK 465 ALA E 244
REMARK 465 GLN E 245
REMARK 465 PRO E 246
REMARK 465 ALA E 247
REMARK 465 GLN E 248
REMARK 465 PRO E 249
REMARK 465 ALA E 250
REMARK 465 ASP E 251
REMARK 465 GLU E 252
REMARK 465 PRO E 253
REMARK 465 ALA E 254
REMARK 465 GLU E 255
REMARK 465 LYS E 256
REMARK 465 ALA E 257
REMARK 465 ASP E 258
REMARK 465 GLU E 259
REMARK 465 PRO E 260
REMARK 465 MET E 261
REMARK 465 GLU E 262
REMARK 465 HIS E 263
REMARK 465 MET F 0
REMARK 465 SER F 1
REMARK 465 SER F 2
REMARK 465 ILE F 3
REMARK 465 GLY F 4
REMARK 465 THR F 5
REMARK 465 GLU F 245
REMARK 465 GLU F 246
REMARK 465 ASP F 247
REMARK 465 GLU F 248
REMARK 465 SER F 249
REMARK 465 ASP F 250
REMARK 465 ASP F 251
REMARK 465 ASP F 252
REMARK 465 ASN F 253
REMARK 465 MET F 254
REMARK 465 MET G 1
REMARK 465 ASP G 246
REMARK 465 ILE H 221
REMARK 465 GLU H 222
REMARK 465 VAL H 223
REMARK 465 LEU H 224
REMARK 465 GLU H 225
REMARK 465 GLU H 226
REMARK 465 THR H 227
REMARK 465 VAL H 228
REMARK 465 GLN H 229
REMARK 465 THR H 230
REMARK 465 MET H 231
REMARK 465 ASP H 232
REMARK 465 THR H 233
REMARK 465 SER H 234
REMARK 465 MET I 0
REMARK 465 PRO J 197
REMARK 465 LYS J 198
REMARK 465 GLN J 199
REMARK 465 GLY J 200
REMARK 465 SER J 201
REMARK 465 GLY K 201
REMARK 465 SER K 202
REMARK 465 THR K 203
REMARK 465 PRO K 204
REMARK 465 GLY M 217
REMARK 465 PHE M 218
REMARK 465 GLU M 219
REMARK 465 PRO N 203
REMARK 465 PRO N 204
REMARK 465 ALA N 205
REMARK 465 MET O 0
REMARK 465 ALA O 1
REMARK 465 GLU O 2
REMARK 465 ALA O 233
REMARK 465 MET P 1
REMARK 465 ARG P 249
REMARK 465 GLU P 250
REMARK 465 LYS P 251
REMARK 465 LYS P 252
REMARK 465 GLU P 253
REMARK 465 LYS P 254
REMARK 465 GLU P 255
REMARK 465 GLN P 256
REMARK 465 LYS P 257
REMARK 465 GLU P 258
REMARK 465 LYS P 259
REMARK 465 ASP P 260
REMARK 465 LYS P 261
REMARK 465 MET Q 1
REMARK 465 GLN Q 200
REMARK 465 SER Q 201
REMARK 465 GLY Q 202
REMARK 465 GLY Q 203
REMARK 465 LYS Q 204
REMARK 465 LYS Q 242
REMARK 465 LYS Q 243
REMARK 465 GLN Q 244
REMARK 465 LYS Q 245
REMARK 465 LYS Q 246
REMARK 465 ALA Q 247
REMARK 465 SER Q 248
REMARK 465 MET R 1
REMARK 465 PHE R 2
REMARK 465 LEU R 3
REMARK 465 THR R 4
REMARK 465 ARG R 5
REMARK 465 SER R 6
REMARK 465 GLU R 7
REMARK 465 TYR R 8
REMARK 465 MET S 1
REMARK 465 PRO S 240
REMARK 465 GLN S 241
REMARK 465 ARG S 242
REMARK 465 LYS S 243
REMARK 465 ALA S 244
REMARK 465 GLN S 245
REMARK 465 PRO S 246
REMARK 465 ALA S 247
REMARK 465 GLN S 248
REMARK 465 PRO S 249
REMARK 465 ALA S 250
REMARK 465 ASP S 251
REMARK 465 GLU S 252
REMARK 465 PRO S 253
REMARK 465 ALA S 254
REMARK 465 GLU S 255
REMARK 465 LYS S 256
REMARK 465 ALA S 257
REMARK 465 ASP S 258
REMARK 465 GLU S 259
REMARK 465 PRO S 260
REMARK 465 MET S 261
REMARK 465 GLU S 262
REMARK 465 HIS S 263
REMARK 465 MET T 0
REMARK 465 SER T 1
REMARK 465 SER T 2
REMARK 465 ILE T 3
REMARK 465 GLY T 4
REMARK 465 GLU T 245
REMARK 465 GLU T 246
REMARK 465 ASP T 247
REMARK 465 GLU T 248
REMARK 465 SER T 249
REMARK 465 ASP T 250
REMARK 465 ASP T 251
REMARK 465 ASP T 252
REMARK 465 ASN T 253
REMARK 465 MET T 254
REMARK 465 MET U 1
REMARK 465 PHE U 187
REMARK 465 ASP U 188
REMARK 465 TRP U 189
REMARK 465 THR U 190
REMARK 465 PHE U 191
REMARK 465 GLU U 192
REMARK 465 ASP U 246
REMARK 465 ILE V 221
REMARK 465 GLU V 222
REMARK 465 VAL V 223
REMARK 465 LEU V 224
REMARK 465 GLU V 225
REMARK 465 GLU V 226
REMARK 465 THR V 227
REMARK 465 VAL V 228
REMARK 465 GLN V 229
REMARK 465 THR V 230
REMARK 465 MET V 231
REMARK 465 ASP V 232
REMARK 465 THR V 233
REMARK 465 SER V 234
REMARK 465 MET W 0
REMARK 465 PRO X 197
REMARK 465 LYS X 198
REMARK 465 GLN X 199
REMARK 465 GLY X 200
REMARK 465 SER X 201
REMARK 465 SER Y 200
REMARK 465 GLY Y 201
REMARK 465 SER Y 202
REMARK 465 THR Y 203
REMARK 465 PRO Y 204
REMARK 465 GLY a 217
REMARK 465 PHE a 218
REMARK 465 GLU a 219
REMARK 465 PRO b 204
REMARK 465 ALA b 205
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ARG A 3 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 52 CG CD CE NZ
REMARK 470 ARG A 59 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 140 CG CD OE1 OE2
REMARK 470 GLU A 179 CG CD OE1 OE2
REMARK 470 LYS A 195 CG CD CE NZ
REMARK 470 GLU A 199 CG CD OE1 OE2
REMARK 470 GLU B 15 CG CD OE1 OE2
REMARK 470 LYS B 54 CG CD CE NZ
REMARK 470 GLU B 181 CG CD OE1 OE2
REMARK 470 GLU B 183 CG CD OE1 OE2
REMARK 470 LYS B 199 CG CD CE NZ
REMARK 470 ASP B 202 CG OD1 OD2
REMARK 470 VAL B 203 CG1 CG2
REMARK 470 LYS B 205 CG CD CE NZ
REMARK 470 GLU B 209 CG CD OE1 OE2
REMARK 470 LYS B 210 CG CD CE NZ
REMARK 470 LYS B 246 CG CD CE NZ
REMARK 470 ARG C 38 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 47 CG CD CE NZ
REMARK 470 LYS C 48 CG CD CE NZ
REMARK 470 SER C 49 OG
REMARK 470 VAL C 50 CG1 CG2
REMARK 470 LYS C 52 CG CD CE NZ
REMARK 470 PHE C 138 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS C 166 CG CD CE NZ
REMARK 470 GLU C 170 CG CD OE1 OE2
REMARK 470 LYS C 174 CG CD CE NZ
REMARK 470 LYS C 189 CG CD CE NZ
REMARK 470 LYS C 193 CG CD CE NZ
REMARK 470 LEU C 196 CG CD1 CD2
REMARK 470 VAL C 199 CG1 CG2
REMARK 470 GLN C 200 CG CD OE1 NE2
REMARK 470 LYS C 204 CG CD CE NZ
REMARK 470 ILE C 206 CG1 CG2 CD1
REMARK 470 GLU C 207 CG CD OE1 OE2
REMARK 470 GLN C 215 CG CD OE1 NE2
REMARK 470 LYS C 218 CG CD CE NZ
REMARK 470 GLU C 223 CG CD OE1 OE2
REMARK 470 GLU C 224 CG CD OE1 OE2
REMARK 470 ILE C 232 CG1 CG2 CD1
REMARK 470 ASP D 129 CG OD1 OD2
REMARK 470 LYS D 149 CG CD CE NZ
REMARK 470 SER D 172 OG
REMARK 470 LYS D 187 CG CD CE NZ
REMARK 470 LYS D 192 CG CD CE NZ
REMARK 470 LYS D 196 CG CD CE NZ
REMARK 470 LYS D 209 CG CD CE NZ
REMARK 470 LYS E 41 CG CD CE NZ
REMARK 470 ARG E 51 CG CD NE CZ NH1 NH2
REMARK 470 GLN E 53 CG CD OE1 NE2
REMARK 470 SER E 54 OG
REMARK 470 GLU E 55 CG CD OE1 OE2
REMARK 470 HIS E 59 CG ND1 CD2 CE1 NE2
REMARK 470 LYS E 208 CG CD CE NZ
REMARK 470 GLU E 237 CG CD OE1 OE2
REMARK 470 GLU F 60 CG CD OE1 OE2
REMARK 470 LYS F 205 CG CD CE NZ
REMARK 470 LYS G 45 CG CD CE NZ
REMARK 470 GLU G 145 CG CD OE1 OE2
REMARK 470 GLU G 146 CG CD OE1 OE2
REMARK 470 LYS G 181 CG CD CE NZ
REMARK 470 GLU G 196 CG CD OE1 OE2
REMARK 470 LYS H 9 CG CD CE NZ
REMARK 470 LYS H 180 CG CD CE NZ
REMARK 470 ASN J 24 CG OD1 ND2
REMARK 470 GLU J 109 CG CD OE1 OE2
REMARK 470 GLU J 154 CG CD OE1 OE2
REMARK 470 LYS K 106 CG CD CE NZ
REMARK 470 ARG L 1 CG CD NE CZ NH1 NH2
REMARK 470 GLU L 18 CG CD OE1 OE2
REMARK 470 GLU L 162 CG CD OE1 OE2
REMARK 470 ARG L 173 CG CD NE CZ NH1 NH2
REMARK 470 LYS L 200 CG CD CE NZ
REMARK 470 ARG O 3 CG CD NE CZ NH1 NH2
REMARK 470 LYS O 17 CG CD CE NZ
REMARK 470 LYS O 50 CG CD CE NZ
REMARK 470 GLN O 51 CG CD OE1 NE2
REMARK 470 LYS O 52 CG CD CE NZ
REMARK 470 ILE O 54 CG1 CG2 CD1
REMARK 470 LYS O 69 CG CD CE NZ
REMARK 470 LYS O 164 CG CD CE NZ
REMARK 470 GLU O 174 CG CD OE1 OE2
REMARK 470 LYS O 175 CG CD CE NZ
REMARK 470 TYR O 177 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU O 179 CG CD OE1 OE2
REMARK 470 HIS O 188 CG ND1 CD2 CE1 NE2
REMARK 470 GLU P 15 CG CD OE1 OE2
REMARK 470 ASN P 51 CG OD1 ND2
REMARK 470 ILE P 52 CG1 CG2 CD1
REMARK 470 LYS P 199 CG CD CE NZ
REMARK 470 LYS P 205 CG CD CE NZ
REMARK 470 GLU P 209 CG CD OE1 OE2
REMARK 470 LYS P 210 CG CD CE NZ
REMARK 470 ARG P 226 CG CD NE CZ NH1 NH2
REMARK 470 LYS P 229 CG CD CE NZ
REMARK 470 LYS P 231 CG CD CE NZ
REMARK 470 GLU P 232 CG CD OE1 OE2
REMARK 470 LYS P 238 CG CD CE NZ
REMARK 470 LYS P 239 CG CD CE NZ
REMARK 470 ARG Q 38 CG CD NE CZ NH1 NH2
REMARK 470 LYS Q 47 CG CD CE NZ
REMARK 470 LYS Q 48 CG CD CE NZ
REMARK 470 SER Q 49 OG
REMARK 470 VAL Q 50 CG1 CG2
REMARK 470 LYS Q 52 CG CD CE NZ
REMARK 470 LYS Q 61 CG CD CE NZ
REMARK 470 PHE Q 138 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS Q 166 CG CD CE NZ
REMARK 470 LYS Q 174 CG CD CE NZ
REMARK 470 GLU Q 182 CG CD OE1 OE2
REMARK 470 LYS Q 189 CG CD CE NZ
REMARK 470 LYS Q 193 CG CD CE NZ
REMARK 470 GLU Q 207 CG CD OE1 OE2
REMARK 470 GLN Q 215 CG CD OE1 NE2
REMARK 470 LYS Q 218 CG CD CE NZ
REMARK 470 LYS Q 241 CG CD CE NZ
REMARK 470 GLU R 126 CG CD OE1 OE2
REMARK 470 ASP R 127 CG OD1 OD2
REMARK 470 ASP R 129 CG OD1 OD2
REMARK 470 LYS R 149 CG CD CE NZ
REMARK 470 GLU R 175 CG CD OE1 OE2
REMARK 470 GLU R 207 CG CD OE1 OE2
REMARK 470 GLU R 208 CG CD OE1 OE2
REMARK 470 LYS R 231 CG CD CE NZ
REMARK 470 LYS S 41 CG CD CE NZ
REMARK 470 GLN S 53 CG CD OE1 NE2
REMARK 470 LYS S 189 CG CD CE NZ
REMARK 470 LYS S 217 CG CD CE NZ
REMARK 470 ASP S 218 CG OD1 OD2
REMARK 470 LEU S 236 CG CD1 CD2
REMARK 470 GLU S 237 CG CD OE1 OE2
REMARK 470 GLU S 238 CG CD OE1 OE2
REMARK 470 ARG S 239 CG CD NE CZ NH1 NH2
REMARK 470 THR T 5 OG1 CG2
REMARK 470 LYS T 42 CG CD CE NZ
REMARK 470 LYS T 56 CG CD CE NZ
REMARK 470 GLU T 60 CG CD OE1 OE2
REMARK 470 ARG T 187 CG CD NE CZ NH1 NH2
REMARK 470 GLU T 234 CG CD OE1 OE2
REMARK 470 LYS T 244 CG CD CE NZ
REMARK 470 ARG U 3 CG CD NE CZ NH1 NH2
REMARK 470 LYS U 55 CG CD CE NZ
REMARK 470 LYS U 59 CG CD CE NZ
REMARK 470 GLU U 145 CG CD OE1 OE2
REMARK 470 GLU U 146 CG CD OE1 OE2
REMARK 470 GLN U 147 CG CD OE1 NE2
REMARK 470 VAL U 170 CG1 CG2
REMARK 470 LYS U 171 CG CD CE NZ
REMARK 470 LYS U 181 CG CD CE NZ
REMARK 470 LYS U 184 CG CD CE NZ
REMARK 470 LYS U 186 CG CD CE NZ
REMARK 470 GLN U 193 CG CD OE1 NE2
REMARK 470 ASP U 209 CG OD1 OD2
REMARK 470 LYS U 226 CG CD CE NZ
REMARK 470 LYS V 180 CG CD CE NZ
REMARK 470 LYS V 182 CG CD CE NZ
REMARK 470 LYS V 194 CG CD CE NZ
REMARK 470 LYS V 195 CG CD CE NZ
REMARK 470 ARG V 198 CG CD NE CZ NH1 NH2
REMARK 470 ARG V 201 CG CD NE CZ NH1 NH2
REMARK 470 ARG V 203 CG CD NE CZ NH1 NH2
REMARK 470 CYS V 204 SG
REMARK 470 GLU V 205 CG CD OE1 OE2
REMARK 470 LYS V 206 CG CD CE NZ
REMARK 470 GLU V 220 CG CD OE1 OE2
REMARK 470 HIS W 161 CG ND1 CD2 CE1 NE2
REMARK 470 LYS W 191 CG CD CE NZ
REMARK 470 GLU X 109 CG CD OE1 OE2
REMARK 470 GLU X 111 CG CD OE1 OE2
REMARK 470 ARG X 155 CG CD NE CZ NH1 NH2
REMARK 470 ARG Z 1 CG CD NE CZ NH1 NH2
REMARK 470 ASN Z 160 CG OD1 ND2
REMARK 470 VAL Z 161 CG1 CG2
REMARK 470 GLU Z 162 CG CD OE1 OE2
REMARK 470 LYS a 156 CG CD CE NZ
REMARK 470 GLU a 206 CG CD OE1 OE2
REMARK 470 VAL b 199 CG1 CG2
REMARK 470 OAS c 2 C2A OAC
REMARK 470 OAS c 3 C2A OAC
REMARK 470 OAS d 2 C2A OAC
REMARK 470 OAS d 3 C2A OAC
REMARK 470 OAS e 2 C2A OAC
REMARK 470 OAS e 3 C2A OAC
REMARK 470 OAS f 2 C2A OAC
REMARK 470 OAS f 3 C2A OAC
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH X 528 O HOH Y 545 1.91
REMARK 500 O HOH P 344 O HOH P 389 1.97
REMARK 500 O HOH E 401 O HOH E 429 2.03
REMARK 500 O ASP T 202 O LYS T 205 2.05
REMARK 500 O HOH B 308 O HOH B 410 2.09
REMARK 500 O HOH S 413 O HOH S 430 2.10
REMARK 500 O HOH D 337 O HOH D 357 2.13
REMARK 500 O VAL F 227 NH1 ARG F 232 2.14
REMARK 500 O HOH H 421 O HOH H 438 2.14
REMARK 500 OG1 THR D 96 O HOH D 301 2.17
REMARK 500 NH1 ARG a 86 OE1 GLU a 133 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH F 465 O HOH G 566 4475 2.06
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 GLU C 182 CD GLU C 182 OE2 0.093
REMARK 500 GLU G 108 CD GLU G 108 OE1 0.090
REMARK 500 GLU G 108 CD GLU G 108 OE2 0.069
REMARK 500 SER N 24 CB SER N 24 OG -0.084
REMARK 500 GLU R 25 CG GLU R 25 CD 0.091
REMARK 500 TYR T 7 N TYR T 7 CA 0.125
REMARK 500 GLU X 154 C GLU X 154 O 0.131
REMARK 500 SER Z 3 CB SER Z 3 OG 0.094
REMARK 500 GLU Z 31 CD GLU Z 31 OE2 0.069
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 ARG A 219 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG B 96 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 ARG B 96 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ARG C 5 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ARG D 168 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 GLU D 175 N - CA - C ANGL. DEV. = -16.8 DEGREES
REMARK 500 ARG E 122 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ASP F 43 CB - CG - OD1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 MET F 117 CG - SD - CE ANGL. DEV. = 10.1 DEGREES
REMARK 500 VAL F 190 CB - CA - C ANGL. DEV. = -12.5 DEGREES
REMARK 500 ARG G 11 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 ASP G 86 CB - CG - OD1 ANGL. DEV. = 6.1 DEGREES
REMARK 500 ARG G 117 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ASP H 28 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ARG H 72 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG H 72 NE - CZ - NH2 ANGL. DEV. = -4.6 DEGREES
REMARK 500 ASN I 17 C - N - CA ANGL. DEV. = 21.3 DEGREES
REMARK 500 ARG I 25 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ARG I 69 NE - CZ - NH1 ANGL. DEV. = 5.2 DEGREES
REMARK 500 ARG I 69 NE - CZ - NH2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 MET J 1 CB - CA - C ANGL. DEV. = 13.4 DEGREES
REMARK 500 ARG J 86 NE - CZ - NH1 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ARG J 86 NE - CZ - NH2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 ASP J 184 CB - CG - OD1 ANGL. DEV. = 7.0 DEGREES
REMARK 500 THR K 1 N - CA - CB ANGL. DEV. = 13.0 DEGREES
REMARK 500 ARG K 107 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ARG K 120 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 ARG K 120 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 ASP K 154 CB - CG - OD2 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ARG K 157 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ARG L 99 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 ARG L 99 NE - CZ - NH2 ANGL. DEV. = -4.9 DEGREES
REMARK 500 ARG M 99 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 ARG M 151 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 MET N 116 CG - SD - CE ANGL. DEV. = -10.4 DEGREES
REMARK 500 LEU O 181 CA - CB - CG ANGL. DEV. = 16.4 DEGREES
REMARK 500 ARG P 96 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 ARG Q 5 NE - CZ - NH2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 ASP R 84 CB - CG - OD1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 LEU R 121 C - N - CA ANGL. DEV. = 24.8 DEGREES
REMARK 500 ARG S 122 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ASP T 43 CB - CG - OD2 ANGL. DEV. = 6.4 DEGREES
REMARK 500 MET T 117 CG - SD - CE ANGL. DEV. = 10.0 DEGREES
REMARK 500 ARG U 88 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG U 117 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ASN W 17 C - N - CA ANGL. DEV. = 23.0 DEGREES
REMARK 500 ARG W 69 NE - CZ - NH1 ANGL. DEV. = 4.9 DEGREES
REMARK 500 ARG W 69 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 ARG X 86 NE - CZ - NH1 ANGL. DEV. = 4.9 DEGREES
REMARK 500 ARG X 86 NE - CZ - NH2 ANGL. DEV. = -4.5 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 62 ANGLE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 LYS A 50 82.40 -48.26
REMARK 500 LYS A 52 -150.21 -63.90
REMARK 500 SER A 53 126.97 2.61
REMARK 500 GLN A 122 -35.73 -142.82
REMARK 500 LYS A 175 42.78 -86.28
REMARK 500 ARG A 176 -29.57 -168.21
REMARK 500 PHE A 198 -76.96 -83.40
REMARK 500 GLU A 199 103.39 74.91
REMARK 500 GLN A 201 122.15 81.23
REMARK 500 ARG B 8 63.52 69.61
REMARK 500 GLU B 58 86.38 61.04
REMARK 500 ASN B 69 -159.75 -153.45
REMARK 500 SER B 204 -100.99 -130.55
REMARK 500 GLU B 248 -64.13 -103.84
REMARK 500 ASP C 13 -4.21 89.76
REMARK 500 LYS C 47 -83.26 4.96
REMARK 500 LYS C 48 -71.04 -80.12
REMARK 500 VAL C 50 -117.41 62.44
REMARK 500 ALA C 51 104.39 87.23
REMARK 500 LEU C 96 -70.17 -56.27
REMARK 500 VAL C 98 -21.74 -145.79
REMARK 500 GLU C 99 19.60 59.34
REMARK 500 LYS C 204 -79.23 109.76
REMARK 500 ASP C 214 -37.32 75.63
REMARK 500 SER C 216 170.57 70.73
REMARK 500 GLU C 237 -57.49 -135.81
REMARK 500 ARG D 53 69.51 76.18
REMARK 500 GLU D 125 31.54 -143.10
REMARK 500 GLU D 126 -30.46 -159.93
REMARK 500 GLU D 175 -82.72 -56.87
REMARK 500 PHE D 226 129.14 -38.60
REMARK 500 HIS E 59 113.68 108.31
REMARK 500 ALA E 151 -3.85 81.21
REMARK 500 ASP E 226 -124.54 57.44
REMARK 500 LEU E 236 55.98 -103.17
REMARK 500 SER F 62 166.86 -32.31
REMARK 500 ASN F 63 48.73 36.89
REMARK 500 ARG G 3 90.57 66.30
REMARK 500 GLU G 192 -56.82 -123.15
REMARK 500 ASP G 209 90.76 67.52
REMARK 500 GLU G 244 46.02 -84.93
REMARK 500 ASN H 30 58.73 -140.53
REMARK 500 SER H 171 -132.87 61.43
REMARK 500 TYR H 202 47.66 -104.18
REMARK 500 GLN I 30 -123.50 49.60
REMARK 500 ASP I 134 -68.39 -130.90
REMARK 500 ASN J 24 -119.93 65.54
REMARK 500 LEU J 175 77.83 -111.83
REMARK 500 ASP K 105 -159.90 -128.07
REMARK 500 PHE L 102 74.21 -159.61
REMARK 500
REMARK 500 THIS ENTRY HAS 126 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 D 175 GLY D 176 -142.00
REMARK 500 GLU D 175 GLY D 176 139.78
REMARK 500 GLY E 235 LEU E 236 146.95
REMARK 500 ASP F 206 LYS F 207 -149.88
REMARK 500 GLY I 78 ARG I 79 -124.83
REMARK 500 MET J 1 GLU J 2 -146.19
REMARK 500 MET J 1 GLU J 2 -148.14
REMARK 500 LYS P 54 LEU P 55 146.80
REMARK 500 GLU P 244 ALA P 245 -147.54
REMARK 500 ALA P 245 LYS P 246 52.09
REMARK 500 LYS Q 47 LYS Q 48 -144.25
REMARK 500 SER Q 49 VAL Q 50 -145.32
REMARK 500 PRO R 130 GLY R 131 144.46
REMARK 500 GLY W 78 ARG W 79 -124.00
REMARK 500 MET X 1 GLU X 2 -143.78
REMARK 500 ILE a 215 SER a 216 -126.43
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 THR X 148 11.39
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH E 447 DISTANCE = 6.71 ANGSTROMS
REMARK 525 HOH F 484 DISTANCE = 5.81 ANGSTROMS
REMARK 525 HOH F 485 DISTANCE = 7.13 ANGSTROMS
REMARK 525 HOH G 596 DISTANCE = 6.91 ANGSTROMS
REMARK 525 HOH H 556 DISTANCE = 6.28 ANGSTROMS
REMARK 525 HOH I 560 DISTANCE = 5.84 ANGSTROMS
REMARK 525 HOH I 561 DISTANCE = 6.93 ANGSTROMS
REMARK 525 HOH J 536 DISTANCE = 6.45 ANGSTROMS
REMARK 525 HOH O 394 DISTANCE = 6.20 ANGSTROMS
REMARK 525 HOH T 395 DISTANCE = 5.86 ANGSTROMS
REMARK 525 HOH V 514 DISTANCE = 5.81 ANGSTROMS
REMARK 525 HOH W 520 DISTANCE = 5.85 ANGSTROMS
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 K G 301 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR G 14 OG1
REMARK 620 2 TYR G 125 O 89.6
REMARK 620 3 ASN G 128 O 87.4 96.4
REMARK 620 4 MET G 131 O 162.5 107.0 96.0
REMARK 620 5 HOH G 440 O 78.4 155.6 104.1 84.1
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG H 301 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN H 91 OE1
REMARK 620 2 HOH H 454 O 75.9
REMARK 620 3 HOH H 528 O 93.5 88.4
REMARK 620 4 HOH N 412 O 83.9 92.6 176.9
REMARK 620 5 HOH N 434 O 102.2 178.1 91.4 87.5
REMARK 620 6 HOH N 435 O 164.1 88.9 90.8 92.2 93.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG H 302 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ILE H 163 O
REMARK 620 2 ASP H 166 O 115.0
REMARK 620 3 SER H 169 O 99.0 92.8
REMARK 620 4 ASP Z 213 O 105.5 135.9 97.3
REMARK 620 5 HOH Z 504 O 87.3 90.1 171.1 74.9
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG I 301 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 VAL I 174 O
REMARK 620 2 ASP I 177 O 86.7
REMARK 620 3 SER I 180 O 104.8 92.8
REMARK 620 4 HOH I 405 O 81.5 165.5 98.4
REMARK 620 5 HOH I 462 O 156.4 89.1 98.6 98.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG I 303 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP I 204 O
REMARK 620 2 HOH I 502 O 76.5
REMARK 620 3 THR Y 164 O 109.6 78.7
REMARK 620 4 ASP Y 167 O 138.2 87.8 104.7
REMARK 620 5 SER Y 170 O 98.5 175.0 103.5 95.9
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG J 301 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH J 404 O
REMARK 620 2 HOH J 422 O 86.8
REMARK 620 3 HOH J 448 O 91.9 90.7
REMARK 620 4 HOH J 516 O 92.3 178.2 90.8
REMARK 620 5 HOH J 529 O 87.6 87.7 178.3 90.8
REMARK 620 6 HOH K 485 O 177.2 90.8 89.5 90.1 90.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG K 301 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR K 164 O
REMARK 620 2 ASP K 167 O 103.5
REMARK 620 3 SER K 170 O 102.7 94.9
REMARK 620 4 HOH K 451 O 77.3 86.8 178.2
REMARK 620 5 ASP W 204 O 110.1 136.6 103.4 75.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K L 302 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA L 183 O
REMARK 620 2 ASP L 186 O 99.1
REMARK 620 3 THR L 189 O 98.3 81.7
REMARK 620 4 HOH L 436 O 91.4 163.9 84.8
REMARK 620 5 HOH L 475 O 57.4 124.1 144.6 71.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG L 303 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP L 213 O
REMARK 620 2 ILE V 163 O 103.7
REMARK 620 3 ASP V 166 O 137.2 116.7
REMARK 620 4 SER V 169 O 96.5 98.2 91.4
REMARK 620 5 HOH V 467 O 73.5 86.4 94.7 169.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K N 302 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 MET N 164 O
REMARK 620 2 ASP N 167 O 92.1
REMARK 620 3 SER N 170 O 98.0 73.1
REMARK 620 4 HOH N 480 O 142.5 119.8 109.3
REMARK 620 5 HOH N 516 O 92.3 82.3 153.6 74.6
REMARK 620 6 HOH N 540 O 90.7 168.8 95.7 62.1 108.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K U 302 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR U 14 OG1
REMARK 620 2 TYR U 125 O 89.7
REMARK 620 3 ASN U 128 O 87.7 96.1
REMARK 620 4 MET U 131 O 162.4 106.8 96.5
REMARK 620 5 HOH U 442 O 77.4 152.5 107.4 85.1
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG V 301 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN V 91 OE1
REMARK 620 2 HOH V 404 O 69.7
REMARK 620 3 HOH V 482 O 90.6 88.7
REMARK 620 4 HOH b 409 O 87.1 88.9 177.1
REMARK 620 5 HOH b 423 O 111.4 178.8 91.8 90.7
REMARK 620 6 HOH b 438 O 158.0 88.3 88.6 92.9 90.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG W 301 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 VAL W 174 O
REMARK 620 2 ASP W 177 O 85.7
REMARK 620 3 SER W 180 O 106.1 94.3
REMARK 620 4 HOH W 451 O 152.9 92.3 101.0
REMARK 620 5 HOH W 464 O 88.0 165.2 100.3 87.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG X 301 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH X 405 O
REMARK 620 2 HOH X 406 O 89.4
REMARK 620 3 HOH X 447 O 90.7 89.5
REMARK 620 4 HOH X 509 O 178.5 90.5 87.7
REMARK 620 5 HOH X 524 O 88.6 91.3 178.9 93.0
REMARK 620 6 HOH Y 515 O 89.5 178.2 89.1 90.6 90.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K Z 301 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA Z 183 O
REMARK 620 2 ASP Z 186 O 99.8
REMARK 620 3 THR Z 189 O 100.8 82.3
REMARK 620 4 HOH Z 429 O 95.0 162.9 86.5
REMARK 620 5 HOH Z 445 O 58.9 126.9 144.7 68.6
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K b 301 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 MET b 164 O
REMARK 620 2 ASP b 167 O 92.9
REMARK 620 3 SER b 170 O 97.7 72.2
REMARK 620 4 HOH b 461 O 140.8 121.3 109.9
REMARK 620 5 HOH b 478 O 91.4 84.2 155.1 75.3
REMARK 620 6 HOH b 497 O 97.8 165.9 97.2 52.6 104.6
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue K G 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG H 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG H 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE H 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG I 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE I 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG I 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG J 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG K 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE K 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE L 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue K L 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG L 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE N 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue K N 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE U 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue K U 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG V 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG W 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE W 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE Y 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue K Z 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE a 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue K b 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT c 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT d 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT e 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT f 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Ligand residues 6VA c 4 through
REMARK 800 6V9 c 1 bound to THR K 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Ligand 6VA c 4 bound to THR K 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Ligand residues 6VA d 4 through
REMARK 800 6V9 d 1 bound to THR N 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Ligand 6VA d 4 bound to THR N 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Ligand residues 6VA e 4 through
REMARK 800 6V9 e 1 bound to THR Y 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Ligand 6VA e 4 bound to THR Y 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Ligand residues 6VA f 4 through
REMARK 800 6V9 f 1 bound to THR b 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Ligand 6VA f 4 bound to THR b 1
DBREF 5LEZ A 0 233 UNP P25787 PSA2_HUMAN 1 234
DBREF 5LEZ B 1 261 UNP P25789 PSA4_HUMAN 1 261
DBREF 5LEZ C 1 248 UNP O14818 PSA7_HUMAN 1 248
DBREF 5LEZ D 1 241 UNP P28066 PSA5_HUMAN 1 241
DBREF 5LEZ E 1 263 UNP P25786 PSA1_HUMAN 1 263
DBREF 5LEZ F 0 254 UNP P25788 PSA3_HUMAN 1 255
DBREF 5LEZ G 1 246 UNP P60900 PSA6_HUMAN 1 246
DBREF 5LEZ H 1 234 UNP Q99436 PSB7_HUMAN 44 277
DBREF 5LEZ I 0 204 UNP P49720 PSB3_HUMAN 1 205
DBREF 5LEZ J 1 201 UNP P49721 PSB2_HUMAN 1 201
DBREF 5LEZ K 1 204 UNP P28074 PSB5_HUMAN 60 263
DBREF 5LEZ L 1 213 UNP P20618 PSB1_HUMAN 29 241
DBREF 5LEZ M 1 219 UNP P28070 PSB4_HUMAN 46 264
DBREF 5LEZ N 1 205 UNP P28072 PSB6_HUMAN 35 239
DBREF 5LEZ O 0 233 UNP P25787 PSA2_HUMAN 1 234
DBREF 5LEZ P 1 261 UNP P25789 PSA4_HUMAN 1 261
DBREF 5LEZ Q 1 248 UNP O14818 PSA7_HUMAN 1 248
DBREF 5LEZ R 1 241 UNP P28066 PSA5_HUMAN 1 241
DBREF 5LEZ S 1 263 UNP P25786 PSA1_HUMAN 1 263
DBREF 5LEZ T 0 254 UNP P25788 PSA3_HUMAN 1 255
DBREF 5LEZ U 1 246 UNP P60900 PSA6_HUMAN 1 246
DBREF 5LEZ V 1 234 UNP Q99436 PSB7_HUMAN 44 277
DBREF 5LEZ W 0 204 UNP P49720 PSB3_HUMAN 1 205
DBREF 5LEZ X 1 201 UNP P49721 PSB2_HUMAN 1 201
DBREF 5LEZ Y 1 204 UNP P28074 PSB5_HUMAN 60 263
DBREF 5LEZ Z 1 213 UNP P20618 PSB1_HUMAN 29 241
DBREF 5LEZ a 1 219 UNP P28070 PSB4_HUMAN 46 264
DBREF 5LEZ b 1 205 UNP P28072 PSB6_HUMAN 35 239
DBREF 5LEZ c 1 4 PDB 5LEZ 5LEZ 1 4
DBREF 5LEZ d 1 4 PDB 5LEZ 5LEZ 1 4
DBREF 5LEZ e 1 4 PDB 5LEZ 5LEZ 1 4
DBREF 5LEZ f 1 4 PDB 5LEZ 5LEZ 1 4
SEQRES 1 A 234 MET ALA GLU ARG GLY TYR SER PHE SER LEU THR THR PHE
SEQRES 2 A 234 SER PRO SER GLY LYS LEU VAL GLN ILE GLU TYR ALA LEU
SEQRES 3 A 234 ALA ALA VAL ALA GLY GLY ALA PRO SER VAL GLY ILE LYS
SEQRES 4 A 234 ALA ALA ASN GLY VAL VAL LEU ALA THR GLU LYS LYS GLN
SEQRES 5 A 234 LYS SER ILE LEU TYR ASP GLU ARG SER VAL HIS LYS VAL
SEQRES 6 A 234 GLU PRO ILE THR LYS HIS ILE GLY LEU VAL TYR SER GLY
SEQRES 7 A 234 MET GLY PRO ASP TYR ARG VAL LEU VAL HIS ARG ALA ARG
SEQRES 8 A 234 LYS LEU ALA GLN GLN TYR TYR LEU VAL TYR GLN GLU PRO
SEQRES 9 A 234 ILE PRO THR ALA GLN LEU VAL GLN ARG VAL ALA SER VAL
SEQRES 10 A 234 MET GLN GLU TYR THR GLN SER GLY GLY VAL ARG PRO PHE
SEQRES 11 A 234 GLY VAL SER LEU LEU ILE CYS GLY TRP ASN GLU GLY ARG
SEQRES 12 A 234 PRO TYR LEU PHE GLN SER ASP PRO SER GLY ALA TYR PHE
SEQRES 13 A 234 ALA TRP LYS ALA THR ALA MET GLY LYS ASN TYR VAL ASN
SEQRES 14 A 234 GLY LYS THR PHE LEU GLU LYS ARG TYR ASN GLU ASP LEU
SEQRES 15 A 234 GLU LEU GLU ASP ALA ILE HIS THR ALA ILE LEU THR LEU
SEQRES 16 A 234 LYS GLU SER PHE GLU GLY GLN MET THR GLU ASP ASN ILE
SEQRES 17 A 234 GLU VAL GLY ILE CYS ASN GLU ALA GLY PHE ARG ARG LEU
SEQRES 18 A 234 THR PRO THR GLU VAL LYS ASP TYR LEU ALA ALA ILE ALA
SEQRES 1 B 261 MET SER ARG ARG TYR ASP SER ARG THR THR ILE PHE SER
SEQRES 2 B 261 PRO GLU GLY ARG LEU TYR GLN VAL GLU TYR ALA MET GLU
SEQRES 3 B 261 ALA ILE GLY HIS ALA GLY THR CYS LEU GLY ILE LEU ALA
SEQRES 4 B 261 ASN ASP GLY VAL LEU LEU ALA ALA GLU ARG ARG ASN ILE
SEQRES 5 B 261 HIS LYS LEU LEU ASP GLU VAL PHE PHE SER GLU LYS ILE
SEQRES 6 B 261 TYR LYS LEU ASN GLU ASP MET ALA CYS SER VAL ALA GLY
SEQRES 7 B 261 ILE THR SER ASP ALA ASN VAL LEU THR ASN GLU LEU ARG
SEQRES 8 B 261 LEU ILE ALA GLN ARG TYR LEU LEU GLN TYR GLN GLU PRO
SEQRES 9 B 261 ILE PRO CYS GLU GLN LEU VAL THR ALA LEU CYS ASP ILE
SEQRES 10 B 261 LYS GLN ALA TYR THR GLN PHE GLY GLY LYS ARG PRO PHE
SEQRES 11 B 261 GLY VAL SER LEU LEU TYR ILE GLY TRP ASP LYS HIS TYR
SEQRES 12 B 261 GLY PHE GLN LEU TYR GLN SER ASP PRO SER GLY ASN TYR
SEQRES 13 B 261 GLY GLY TRP LYS ALA THR CYS ILE GLY ASN ASN SER ALA
SEQRES 14 B 261 ALA ALA VAL SER MET LEU LYS GLN ASP TYR LYS GLU GLY
SEQRES 15 B 261 GLU MET THR LEU LYS SER ALA LEU ALA LEU ALA ILE LYS
SEQRES 16 B 261 VAL LEU ASN LYS THR MET ASP VAL SER LYS LEU SER ALA
SEQRES 17 B 261 GLU LYS VAL GLU ILE ALA THR LEU THR ARG GLU ASN GLY
SEQRES 18 B 261 LYS THR VAL ILE ARG VAL LEU LYS GLN LYS GLU VAL GLU
SEQRES 19 B 261 GLN LEU ILE LYS LYS HIS GLU GLU GLU GLU ALA LYS ALA
SEQRES 20 B 261 GLU ARG GLU LYS LYS GLU LYS GLU GLN LYS GLU LYS ASP
SEQRES 21 B 261 LYS
SEQRES 1 C 248 MET SER TYR ASP ARG ALA ILE THR VAL PHE SER PRO ASP
SEQRES 2 C 248 GLY HIS LEU PHE GLN VAL GLU TYR ALA GLN GLU ALA VAL
SEQRES 3 C 248 LYS LYS GLY SER THR ALA VAL GLY VAL ARG GLY ARG ASP
SEQRES 4 C 248 ILE VAL VAL LEU GLY VAL GLU LYS LYS SER VAL ALA LYS
SEQRES 5 C 248 LEU GLN ASP GLU ARG THR VAL ARG LYS ILE YCM ALA LEU
SEQRES 6 C 248 ASP ASP ASN VAL CYS MET ALA PHE ALA GLY LEU THR ALA
SEQRES 7 C 248 ASP ALA ARG ILE VAL ILE ASN ARG ALA ARG VAL GLU CYS
SEQRES 8 C 248 GLN SER HIS ARG LEU THR VAL GLU ASP PRO VAL THR VAL
SEQRES 9 C 248 GLU TYR ILE THR ARG TYR ILE ALA SER LEU LYS GLN ARG
SEQRES 10 C 248 TYR THR GLN SER ASN GLY ARG ARG PRO PHE GLY ILE SER
SEQRES 11 C 248 ALA LEU ILE VAL GLY PHE ASP PHE ASP GLY THR PRO ARG
SEQRES 12 C 248 LEU TYR GLN THR ASP PRO SER GLY THR TYR HIS ALA TRP
SEQRES 13 C 248 LYS ALA ASN ALA ILE GLY ARG GLY ALA LYS SER VAL ARG
SEQRES 14 C 248 GLU PHE LEU GLU LYS ASN TYR THR ASP GLU ALA ILE GLU
SEQRES 15 C 248 THR ASP ASP LEU THR ILE LYS LEU VAL ILE LYS ALA LEU
SEQRES 16 C 248 LEU GLU VAL VAL GLN SER GLY GLY LYS ASN ILE GLU LEU
SEQRES 17 C 248 ALA VAL MET ARG ARG ASP GLN SER LEU LYS ILE LEU ASN
SEQRES 18 C 248 PRO GLU GLU ILE GLU LYS TYR VAL ALA GLU ILE GLU LYS
SEQRES 19 C 248 GLU LYS GLU GLU ASN GLU LYS LYS LYS GLN LYS LYS ALA
SEQRES 20 C 248 SER
SEQRES 1 D 241 MET PHE LEU THR ARG SER GLU TYR ASP ARG GLY VAL ASN
SEQRES 2 D 241 THR PHE SER PRO GLU GLY ARG LEU PHE GLN VAL GLU TYR
SEQRES 3 D 241 ALA ILE GLU ALA ILE LYS LEU GLY SER THR ALA ILE GLY
SEQRES 4 D 241 ILE GLN THR SER GLU GLY VAL CYS LEU ALA VAL GLU LYS
SEQRES 5 D 241 ARG ILE THR SER PRO LEU MET GLU PRO SER SER ILE GLU
SEQRES 6 D 241 LYS ILE VAL GLU ILE ASP ALA HIS ILE GLY CYS ALA MET
SEQRES 7 D 241 SER GLY LEU ILE ALA ASP ALA LYS THR LEU ILE ASP LYS
SEQRES 8 D 241 ALA ARG VAL GLU THR GLN ASN HIS TRP PHE THR TYR ASN
SEQRES 9 D 241 GLU THR MET THR VAL GLU SER VAL THR GLN ALA VAL SER
SEQRES 10 D 241 ASN LEU ALA LEU GLN PHE GLY GLU GLU ASP ALA ASP PRO
SEQRES 11 D 241 GLY ALA MET SER ARG PRO PHE GLY VAL ALA LEU LEU PHE
SEQRES 12 D 241 GLY GLY VAL ASP GLU LYS GLY PRO GLN LEU PHE HIS MET
SEQRES 13 D 241 ASP PRO SER GLY THR PHE VAL GLN CYS ASP ALA ARG ALA
SEQRES 14 D 241 ILE GLY SER ALA SER GLU GLY ALA GLN SER SER LEU GLN
SEQRES 15 D 241 GLU VAL TYR HIS LYS SER MET THR LEU LYS GLU ALA ILE
SEQRES 16 D 241 LYS SER SER LEU ILE ILE LEU LYS GLN VAL MET GLU GLU
SEQRES 17 D 241 LYS LEU ASN ALA THR ASN ILE GLU LEU ALA THR VAL GLN
SEQRES 18 D 241 PRO GLY GLN ASN PHE HIS MET PHE THR LYS GLU GLU LEU
SEQRES 19 D 241 GLU GLU VAL ILE LYS ASP ILE
SEQRES 1 E 263 MET PHE ARG ASN GLN TYR ASP ASN ASP VAL THR VAL TRP
SEQRES 2 E 263 SER PRO GLN GLY ARG ILE HIS GLN ILE GLU TYR ALA MET
SEQRES 3 E 263 GLU ALA VAL LYS GLN GLY SER ALA THR VAL GLY LEU LYS
SEQRES 4 E 263 SER LYS THR HIS ALA VAL LEU VAL ALA LEU LYS ARG ALA
SEQRES 5 E 263 GLN SER GLU LEU ALA ALA HIS GLN LYS LYS ILE LEU HIS
SEQRES 6 E 263 VAL ASP ASN HIS ILE GLY ILE SER ILE ALA GLY LEU THR
SEQRES 7 E 263 ALA ASP ALA ARG LEU LEU CYS ASN PHE MET ARG GLN GLU
SEQRES 8 E 263 CYS LEU ASP SER ARG PHE VAL PHE ASP ARG PRO LEU PRO
SEQRES 9 E 263 VAL SER ARG LEU VAL SER LEU ILE GLY SER LYS THR GLN
SEQRES 10 E 263 ILE PRO THR GLN ARG TYR GLY ARG ARG PRO TYR GLY VAL
SEQRES 11 E 263 GLY LEU LEU ILE ALA GLY TYR ASP ASP MET GLY PRO HIS
SEQRES 12 E 263 ILE PHE GLN THR 6V1 PRO SER ALA ASN TYR PHE ASP CYS
SEQRES 13 E 263 ARG ALA MET SER ILE GLY ALA ARG SER GLN SER ALA ARG
SEQRES 14 E 263 THR TYR LEU GLU ARG HIS MET SER GLU PHE MET GLU CYS
SEQRES 15 E 263 ASN LEU ASN GLU LEU VAL LYS HIS GLY LEU ARG ALA LEU
SEQRES 16 E 263 ARG GLU THR LEU PRO ALA GLU GLN ASP LEU THR THR LYS
SEQRES 17 E 263 ASN VAL SER ILE GLY ILE VAL GLY LYS ASP LEU GLU PHE
SEQRES 18 E 263 THR ILE TYR ASP ASP ASP ASP VAL SER PRO PHE LEU GLU
SEQRES 19 E 263 GLY LEU GLU GLU ARG PRO GLN ARG LYS ALA GLN PRO ALA
SEQRES 20 E 263 GLN PRO ALA ASP GLU PRO ALA GLU LYS ALA ASP GLU PRO
SEQRES 21 E 263 MET GLU HIS
SEQRES 1 F 255 MET SER SER ILE GLY THR GLY TYR ASP LEU SER ALA SER
SEQRES 2 F 255 THR PHE SER PRO ASP GLY ARG VAL PHE GLN VAL GLU TYR
SEQRES 3 F 255 ALA MET LYS ALA VAL GLU ASN SER SER THR ALA ILE GLY
SEQRES 4 F 255 ILE ARG CYS LYS ASP GLY VAL VAL PHE GLY VAL GLU LYS
SEQRES 5 F 255 LEU VAL LEU SER LYS LEU TYR GLU GLU GLY SER ASN LYS
SEQRES 6 F 255 ARG LEU PHE ASN VAL ASP ARG HIS VAL GLY MET ALA VAL
SEQRES 7 F 255 ALA GLY LEU LEU ALA ASP ALA ARG SER LEU ALA ASP ILE
SEQRES 8 F 255 ALA ARG GLU GLU ALA SER ASN PHE ARG SER ASN PHE GLY
SEQRES 9 F 255 TYR ASN ILE PRO LEU LYS HIS LEU ALA ASP ARG VAL ALA
SEQRES 10 F 255 MET TYR VAL HIS ALA TYR THR LEU TYR SER ALA VAL ARG
SEQRES 11 F 255 PRO PHE GLY CYS SER PHE MET LEU GLY SER TYR SER VAL
SEQRES 12 F 255 ASN ASP GLY ALA GLN LEU TYR MET ILE ASP PRO SER GLY
SEQRES 13 F 255 VAL SER TYR GLY TYR TRP GLY CYS ALA ILE GLY LYS ALA
SEQRES 14 F 255 ARG GLN ALA ALA LYS THR GLU ILE GLU LYS LEU GLN MET
SEQRES 15 F 255 LYS GLU MET THR CYS ARG ASP ILE VAL LYS GLU VAL ALA
SEQRES 16 F 255 LYS ILE ILE TYR ILE VAL HIS ASP GLU VAL LYS ASP LYS
SEQRES 17 F 255 ALA PHE GLU LEU GLU LEU SER TRP VAL GLY GLU LEU THR
SEQRES 18 F 255 ASN GLY ARG HIS GLU ILE VAL PRO LYS ASP ILE ARG GLU
SEQRES 19 F 255 GLU ALA GLU LYS TYR ALA LYS GLU SER LEU LYS GLU GLU
SEQRES 20 F 255 ASP GLU SER ASP ASP ASP ASN MET
SEQRES 1 G 246 MET SER ARG GLY SER SER ALA GLY PHE ASP ARG HIS ILE
SEQRES 2 G 246 THR ILE PHE SER PRO GLU GLY ARG LEU TYR GLN VAL GLU
SEQRES 3 G 246 TYR ALA PHE LYS ALA ILE ASN GLN GLY GLY LEU THR SER
SEQRES 4 G 246 VAL ALA VAL ARG GLY LYS ASP 6V1 ALA VAL ILE VAL THR
SEQRES 5 G 246 GLN LYS LYS VAL PRO ASP LYS LEU LEU ASP SER SER THR
SEQRES 6 G 246 VAL THR HIS LEU PHE LYS ILE THR GLU ASN ILE GLY CYS
SEQRES 7 G 246 VAL MET THR GLY MET THR ALA ASP SER ARG SER GLN VAL
SEQRES 8 G 246 GLN ARG ALA ARG TYR GLU ALA ALA ASN TRP LYS TYR LYS
SEQRES 9 G 246 TYR GLY TYR GLU ILE PRO VAL ASP MET LEU CYS LYS ARG
SEQRES 10 G 246 ILE ALA ASP ILE SER GLN VAL TYR THR GLN ASN ALA GLU
SEQRES 11 G 246 MET ARG PRO LEU GLY CYS YCM MET ILE LEU ILE GLY ILE
SEQRES 12 G 246 ASP GLU GLU GLN GLY PRO GLN VAL TYR LYS CYS ASP PRO
SEQRES 13 G 246 ALA GLY TYR TYR 6V1 GLY PHE LYS ALA THR ALA ALA GLY
SEQRES 14 G 246 VAL LYS GLN THR GLU SER THR SER PHE LEU GLU LYS LYS
SEQRES 15 G 246 VAL LYS LYS LYS PHE ASP TRP THR PHE GLU GLN THR VAL
SEQRES 16 G 246 GLU THR ALA ILE THR CYS LEU SER THR VAL LEU SER ILE
SEQRES 17 G 246 ASP PHE LYS PRO SER GLU ILE GLU VAL GLY VAL VAL THR
SEQRES 18 G 246 VAL GLU ASN PRO LYS PHE ARG ILE LEU THR GLU ALA GLU
SEQRES 19 G 246 ILE ASP ALA HIS LEU VAL ALA LEU ALA GLU ARG ASP
SEQRES 1 H 234 THR THR ILE ALA GLY VAL VAL TYR LYS ASP GLY ILE VAL
SEQRES 2 H 234 LEU GLY ALA ASP THR ARG ALA THR GLU GLY MET VAL VAL
SEQRES 3 H 234 ALA ASP LYS ASN CYS SER LYS ILE HIS PHE ILE SER PRO
SEQRES 4 H 234 ASN ILE TYR CYS CYS GLY ALA GLY THR ALA ALA ASP THR
SEQRES 5 H 234 ASP MET THR THR GLN LEU ILE SER SER ASN LEU GLU LEU
SEQRES 6 H 234 HIS SER LEU SER THR GLY ARG LEU PRO ARG VAL VAL THR
SEQRES 7 H 234 ALA ASN ARG MET LEU LYS GLN MET LEU PHE ARG TYR GLN
SEQRES 8 H 234 GLY TYR ILE GLY ALA ALA LEU VAL LEU GLY GLY VAL ASP
SEQRES 9 H 234 VAL THR GLY PRO HIS LEU TYR SER ILE TYR PRO HIS GLY
SEQRES 10 H 234 SER THR ASP LYS LEU PRO TYR VAL THR MET GLY SER GLY
SEQRES 11 H 234 SER LEU ALA ALA MET ALA VAL PHE GLU ASP LYS PHE ARG
SEQRES 12 H 234 PRO ASP MET GLU GLU GLU GLU ALA LYS ASN LEU VAL SER
SEQRES 13 H 234 GLU ALA ILE ALA ALA GLY ILE PHE ASN ASP LEU GLY SER
SEQRES 14 H 234 GLY SER ASN ILE ASP LEU CYS VAL ILE SER LYS ASN LYS
SEQRES 15 H 234 LEU ASP PHE LEU ARG PRO TYR THR VAL PRO ASN LYS LYS
SEQRES 16 H 234 GLY THR ARG LEU GLY ARG TYR ARG CYS GLU LYS GLY THR
SEQRES 17 H 234 THR ALA VAL LEU THR GLU LYS ILE THR PRO LEU GLU ILE
SEQRES 18 H 234 GLU VAL LEU GLU GLU THR VAL GLN THR MET ASP THR SER
SEQRES 1 I 205 MET SER ILE MET SER TYR ASN GLY GLY ALA VAL MET ALA
SEQRES 2 I 205 MET LYS GLY LYS ASN CYS VAL ALA ILE ALA ALA ASP ARG
SEQRES 3 I 205 ARG PHE GLY ILE GLN ALA GLN MET VAL THR THR ASP PHE
SEQRES 4 I 205 GLN LYS ILE PHE PRO MET GLY ASP ARG LEU TYR ILE GLY
SEQRES 5 I 205 LEU ALA GLY LEU ALA THR ASP VAL GLN THR VAL ALA GLN
SEQRES 6 I 205 ARG LEU LYS PHE ARG LEU ASN LEU TYR GLU LEU LYS GLU
SEQRES 7 I 205 GLY ARG GLN ILE LYS PRO TYR THR LEU MET SER MET VAL
SEQRES 8 I 205 ALA ASN LEU LEU TYR GLU LYS ARG PHE GLY PRO TYR TYR
SEQRES 9 I 205 THR GLU PRO VAL ILE ALA GLY LEU ASP PRO LYS THR PHE
SEQRES 10 I 205 LYS PRO PHE ILE CYS SER LEU ASP LEU ILE GLY CYS PRO
SEQRES 11 I 205 MET VAL THR ASP ASP PHE VAL VAL SER GLY THR CYS ALA
SEQRES 12 I 205 GLU GLN MET TYR GLY MET CYS GLU SER LEU TRP GLU PRO
SEQRES 13 I 205 ASN MET ASP PRO ASP HIS LEU PHE GLU THR ILE SER GLN
SEQRES 14 I 205 ALA MET LEU ASN ALA VAL ASP ARG ASP ALA VAL SER GLY
SEQRES 15 I 205 MET GLY VAL ILE VAL HIS ILE ILE GLU LYS ASP LYS ILE
SEQRES 16 I 205 THR THR ARG THR LEU LYS ALA ARG MET ASP
SEQRES 1 J 201 MET GLU TYR LEU ILE GLY ILE GLN GLY PRO ASP TYR VAL
SEQRES 2 J 201 LEU VAL ALA SER ASP ARG VAL ALA ALA SER ASN ILE VAL
SEQRES 3 J 201 GLN MET LYS ASP ASP HIS ASP LYS MET PHE LYS MET SER
SEQRES 4 J 201 GLU LYS ILE LEU LEU LEU CYS VAL GLY GLU ALA GLY ASP
SEQRES 5 J 201 THR VAL GLN PHE ALA GLU TYR ILE GLN LYS ASN VAL GLN
SEQRES 6 J 201 LEU TYR LYS MET ARG ASN GLY TYR GLU LEU SER PRO THR
SEQRES 7 J 201 ALA ALA ALA ASN PHE THR ARG ARG ASN LEU ALA ASP 6V1
SEQRES 8 J 201 LEU ARG SER ARG THR PRO TYR HIS VAL ASN LEU LEU LEU
SEQRES 9 J 201 ALA GLY TYR ASP GLU HIS GLU GLY PRO ALA LEU TYR TYR
SEQRES 10 J 201 MET ASP TYR LEU ALA ALA LEU ALA LYS ALA PRO PHE ALA
SEQRES 11 J 201 ALA HIS GLY TYR GLY ALA PHE LEU THR LEU SER ILE LEU
SEQRES 12 J 201 ASP ARG TYR TYR THR PRO THR ILE SER ARG GLU ARG ALA
SEQRES 13 J 201 VAL GLU LEU LEU ARG LYS CYS LEU GLU GLU LEU GLN LYS
SEQRES 14 J 201 ARG PHE ILE LEU ASN LEU PRO THR PHE SER VAL ARG ILE
SEQRES 15 J 201 ILE ASP LYS ASN GLY ILE HIS ASP LEU ASP ASN ILE SER
SEQRES 16 J 201 PHE PRO LYS GLN GLY SER
SEQRES 1 K 204 THR THR THR LEU ALA PHE LYS PHE ARG HIS GLY VAL ILE
SEQRES 2 K 204 VAL ALA ALA ASP SER ARG ALA THR ALA GLY ALA TYR ILE
SEQRES 3 K 204 ALA SER GLN THR VAL LYS LYS VAL ILE GLU ILE ASN PRO
SEQRES 4 K 204 TYR LEU LEU GLY THR MET ALA GLY GLY ALA ALA ASP CYS
SEQRES 5 K 204 SER PHE TRP GLU ARG LEU LEU ALA ARG GLN CYS ARG ILE
SEQRES 6 K 204 TYR GLU LEU ARG ASN LYS GLU ARG ILE SER VAL ALA ALA
SEQRES 7 K 204 ALA SER LYS LEU LEU ALA ASN MET VAL TYR GLN TYR LYS
SEQRES 8 K 204 GLY MET GLY LEU SER MET GLY THR MET ILE CYS GLY TRP
SEQRES 9 K 204 ASP LYS ARG GLY PRO GLY LEU TYR TYR VAL ASP SER GLU
SEQRES 10 K 204 GLY ASN ARG ILE SER GLY ALA THR PHE SER VAL GLY SER
SEQRES 11 K 204 GLY SER VAL TYR ALA TYR GLY VAL MET ASP ARG GLY TYR
SEQRES 12 K 204 SER TYR ASP LEU GLU VAL GLU GLN ALA TYR ASP LEU ALA
SEQRES 13 K 204 ARG ARG ALA ILE TYR GLN ALA THR TYR ARG ASP ALA TYR
SEQRES 14 K 204 SER GLY GLY ALA VAL ASN LEU TYR HIS VAL ARG GLU ASP
SEQRES 15 K 204 GLY TRP ILE ARG VAL SER SER ASP ASN VAL ALA ASP LEU
SEQRES 16 K 204 HIS GLU LYS TYR SER GLY SER THR PRO
SEQRES 1 L 213 ARG PHE SER PRO TYR VAL PHE ASN GLY GLY THR ILE LEU
SEQRES 2 L 213 ALA ILE ALA GLY GLU ASP PHE ALA ILE VAL ALA SER ASP
SEQRES 3 L 213 THR ARG LEU SER GLU GLY PHE SER ILE HIS THR ARG ASP
SEQRES 4 L 213 SER PRO LYS CYS TYR LYS LEU THR ASP LYS THR VAL ILE
SEQRES 5 L 213 GLY CYS SER GLY PHE HIS GLY ASP CYS LEU THR LEU THR
SEQRES 6 L 213 LYS ILE ILE GLU ALA ARG LEU LYS MET TYR LYS HIS SER
SEQRES 7 L 213 ASN ASN LYS ALA MET THR THR GLY ALA ILE ALA ALA MET
SEQRES 8 L 213 LEU SER THR ILE LEU TYR SER ARG ARG PHE PHE PRO TYR
SEQRES 9 L 213 TYR VAL TYR ASN ILE ILE GLY GLY LEU ASP GLU GLU GLY
SEQRES 10 L 213 LYS GLY ALA VAL TYR SER PHE ASP PRO VAL GLY SER TYR
SEQRES 11 L 213 GLN ARG ASP SER PHE LYS ALA GLY GLY SER ALA SER ALA
SEQRES 12 L 213 MET LEU GLN PRO LEU LEU ASP ASN GLN VAL GLY PHE LYS
SEQRES 13 L 213 ASN MET GLN ASN VAL GLU HIS VAL PRO LEU SER LEU ASP
SEQRES 14 L 213 ARG ALA MET ARG LEU VAL LYS ASP VAL PHE ILE SER ALA
SEQRES 15 L 213 ALA GLU ARG ASP VAL TYR THR GLY ASP ALA LEU ARG ILE
SEQRES 16 L 213 CYS ILE VAL THR LYS GLU GLY ILE ARG GLU GLU THR VAL
SEQRES 17 L 213 SER LEU ARG LYS ASP
SEQRES 1 M 219 THR GLN ASN PRO MET VAL THR GLY THR SER VAL LEU GLY
SEQRES 2 M 219 VAL LYS PHE GLU GLY GLY VAL VAL ILE ALA ALA ASP MET
SEQRES 3 M 219 LEU GLY SER TYR GLY SER LEU ALA ARG PHE ARG ASN ILE
SEQRES 4 M 219 SER ARG ILE MET ARG VAL ASN ASN SER THR MET LEU GLY
SEQRES 5 M 219 ALA SER GLY ASP TYR ALA ASP PHE GLN TYR LEU LYS GLN
SEQRES 6 M 219 VAL LEU GLY GLN MET VAL ILE ASP GLU GLU LEU LEU GLY
SEQRES 7 M 219 ASP GLY HIS SER TYR SER PRO ARG ALA ILE HIS SER TRP
SEQRES 8 M 219 LEU THR ARG ALA MET TYR SER ARG ARG SER LYS MET ASN
SEQRES 9 M 219 PRO LEU TRP ASN THR MET VAL ILE GLY GLY TYR ALA ASP
SEQRES 10 M 219 GLY GLU SER PHE LEU GLY TYR VAL ASP MET LEU GLY VAL
SEQRES 11 M 219 ALA TYR GLU ALA PRO SER LEU ALA THR GLY TYR GLY ALA
SEQRES 12 M 219 TYR LEU ALA GLN PRO LEU LEU ARG GLU VAL LEU GLU LYS
SEQRES 13 M 219 GLN PRO VAL LEU SER GLN THR GLU ALA ARG ASP LEU VAL
SEQRES 14 M 219 GLU ARG CYS MET ARG VAL LEU TYR TYR ARG ASP ALA ARG
SEQRES 15 M 219 SER TYR ASN ARG PHE GLN ILE ALA THR VAL THR GLU LYS
SEQRES 16 M 219 GLY VAL GLU ILE GLU GLY PRO LEU SER THR GLU THR ASN
SEQRES 17 M 219 TRP ASP ILE ALA HIS MET ILE SER GLY PHE GLU
SEQRES 1 N 205 THR THR ILE MET ALA VAL GLN PHE ASP GLY GLY VAL VAL
SEQRES 2 N 205 LEU GLY ALA ASP SER ARG THR THR THR GLY SER TYR ILE
SEQRES 3 N 205 ALA ASN ARG VAL THR ASP LYS LEU THR PRO ILE HIS ASP
SEQRES 4 N 205 ARG ILE PHE CYS CYS ARG SER GLY SER ALA ALA ASP THR
SEQRES 5 N 205 GLN ALA VAL ALA ASP ALA VAL THR TYR GLN LEU GLY PHE
SEQRES 6 N 205 HIS SER ILE GLU LEU ASN GLU PRO PRO LEU VAL HIS THR
SEQRES 7 N 205 ALA ALA SER LEU PHE LYS GLU MET CYS TYR ARG TYR ARG
SEQRES 8 N 205 GLU ASP LEU MET ALA GLY ILE ILE ILE ALA GLY TRP ASP
SEQRES 9 N 205 PRO GLN GLU GLY GLY GLN VAL TYR SER VAL PRO MET GLY
SEQRES 10 N 205 GLY MET MET VAL ARG GLN SER PHE ALA ILE GLY GLY SER
SEQRES 11 N 205 GLY SER SER TYR ILE TYR GLY TYR VAL ASP ALA THR TYR
SEQRES 12 N 205 ARG GLU GLY MET THR LYS GLU GLU CYS LEU GLN PHE THR
SEQRES 13 N 205 ALA ASN ALA LEU ALA LEU ALA MET GLU ARG ASP GLY SER
SEQRES 14 N 205 SER GLY GLY VAL ILE ARG LEU ALA ALA ILE ALA GLU SER
SEQRES 15 N 205 GLY VAL GLU ARG GLN VAL LEU LEU GLY ASP GLN ILE PRO
SEQRES 16 N 205 LYS PHE ALA VAL ALA THR LEU PRO PRO ALA
SEQRES 1 O 234 MET ALA GLU ARG GLY TYR SER PHE SER LEU THR THR PHE
SEQRES 2 O 234 SER PRO SER GLY LYS LEU VAL GLN ILE GLU TYR ALA LEU
SEQRES 3 O 234 ALA ALA VAL ALA GLY GLY ALA PRO SER VAL GLY ILE LYS
SEQRES 4 O 234 ALA ALA ASN GLY VAL VAL LEU ALA THR GLU LYS LYS GLN
SEQRES 5 O 234 LYS SER ILE LEU TYR ASP GLU ARG SER VAL HIS LYS VAL
SEQRES 6 O 234 GLU PRO ILE THR LYS HIS ILE GLY LEU VAL TYR SER GLY
SEQRES 7 O 234 MET GLY PRO ASP TYR ARG VAL LEU VAL HIS ARG ALA ARG
SEQRES 8 O 234 LYS LEU ALA GLN GLN TYR TYR LEU VAL TYR GLN GLU PRO
SEQRES 9 O 234 ILE PRO THR ALA GLN LEU VAL GLN ARG VAL ALA SER VAL
SEQRES 10 O 234 MET GLN GLU TYR THR GLN SER GLY GLY VAL ARG PRO PHE
SEQRES 11 O 234 GLY VAL SER LEU LEU ILE CYS GLY TRP ASN GLU GLY ARG
SEQRES 12 O 234 PRO TYR LEU PHE GLN SER ASP PRO SER GLY ALA TYR PHE
SEQRES 13 O 234 ALA TRP LYS ALA THR ALA MET GLY LYS ASN TYR VAL ASN
SEQRES 14 O 234 GLY LYS THR PHE LEU GLU LYS ARG TYR ASN GLU ASP LEU
SEQRES 15 O 234 GLU LEU GLU ASP ALA ILE HIS THR ALA ILE LEU THR LEU
SEQRES 16 O 234 LYS GLU SER PHE GLU GLY GLN MET THR GLU ASP ASN ILE
SEQRES 17 O 234 GLU VAL GLY ILE CYS ASN GLU ALA GLY PHE ARG ARG LEU
SEQRES 18 O 234 THR PRO THR GLU VAL LYS ASP TYR LEU ALA ALA ILE ALA
SEQRES 1 P 261 MET SER ARG ARG TYR ASP SER ARG THR THR ILE PHE SER
SEQRES 2 P 261 PRO GLU GLY ARG LEU TYR GLN VAL GLU TYR ALA MET GLU
SEQRES 3 P 261 ALA ILE GLY HIS ALA GLY THR CYS LEU GLY ILE LEU ALA
SEQRES 4 P 261 ASN ASP GLY VAL LEU LEU ALA ALA GLU ARG ARG ASN ILE
SEQRES 5 P 261 HIS LYS LEU LEU ASP GLU VAL PHE PHE SER GLU LYS ILE
SEQRES 6 P 261 TYR LYS LEU ASN GLU ASP MET ALA CYS SER VAL ALA GLY
SEQRES 7 P 261 ILE THR SER ASP ALA ASN VAL LEU THR ASN GLU LEU ARG
SEQRES 8 P 261 LEU ILE ALA GLN ARG TYR LEU LEU GLN TYR GLN GLU PRO
SEQRES 9 P 261 ILE PRO CYS GLU GLN LEU VAL THR ALA LEU CYS ASP ILE
SEQRES 10 P 261 LYS GLN ALA TYR THR GLN PHE GLY GLY LYS ARG PRO PHE
SEQRES 11 P 261 GLY VAL SER LEU LEU TYR ILE GLY TRP ASP LYS HIS TYR
SEQRES 12 P 261 GLY PHE GLN LEU TYR GLN SER ASP PRO SER GLY ASN TYR
SEQRES 13 P 261 GLY GLY TRP LYS ALA THR CYS ILE GLY ASN ASN SER ALA
SEQRES 14 P 261 ALA ALA VAL SER MET LEU LYS GLN ASP TYR LYS GLU GLY
SEQRES 15 P 261 GLU MET THR LEU LYS SER ALA LEU ALA LEU ALA ILE LYS
SEQRES 16 P 261 VAL LEU ASN LYS THR MET ASP VAL SER LYS LEU SER ALA
SEQRES 17 P 261 GLU LYS VAL GLU ILE ALA THR LEU THR ARG GLU ASN GLY
SEQRES 18 P 261 LYS THR VAL ILE ARG VAL LEU LYS GLN LYS GLU VAL GLU
SEQRES 19 P 261 GLN LEU ILE LYS LYS HIS GLU GLU GLU GLU ALA LYS ALA
SEQRES 20 P 261 GLU ARG GLU LYS LYS GLU LYS GLU GLN LYS GLU LYS ASP
SEQRES 21 P 261 LYS
SEQRES 1 Q 248 MET SER TYR ASP ARG ALA ILE THR VAL PHE SER PRO ASP
SEQRES 2 Q 248 GLY HIS LEU PHE GLN VAL GLU TYR ALA GLN GLU ALA VAL
SEQRES 3 Q 248 LYS LYS GLY SER THR ALA VAL GLY VAL ARG GLY ARG ASP
SEQRES 4 Q 248 ILE VAL VAL LEU GLY VAL GLU LYS LYS SER VAL ALA LYS
SEQRES 5 Q 248 LEU GLN ASP GLU ARG THR VAL ARG LYS ILE YCM ALA LEU
SEQRES 6 Q 248 ASP ASP ASN VAL CYS MET ALA PHE ALA GLY LEU THR ALA
SEQRES 7 Q 248 ASP ALA ARG ILE VAL ILE ASN ARG ALA ARG VAL GLU CYS
SEQRES 8 Q 248 GLN SER HIS ARG LEU THR VAL GLU ASP PRO VAL THR VAL
SEQRES 9 Q 248 GLU TYR ILE THR ARG TYR ILE ALA SER LEU LYS GLN ARG
SEQRES 10 Q 248 TYR THR GLN SER ASN GLY ARG ARG PRO PHE GLY ILE SER
SEQRES 11 Q 248 ALA LEU ILE VAL GLY PHE ASP PHE ASP GLY THR PRO ARG
SEQRES 12 Q 248 LEU TYR GLN THR ASP PRO SER GLY THR TYR HIS ALA TRP
SEQRES 13 Q 248 LYS ALA ASN ALA ILE GLY ARG GLY ALA LYS SER VAL ARG
SEQRES 14 Q 248 GLU PHE LEU GLU LYS ASN TYR THR ASP GLU ALA ILE GLU
SEQRES 15 Q 248 THR ASP ASP LEU THR ILE LYS LEU VAL ILE LYS ALA LEU
SEQRES 16 Q 248 LEU GLU VAL VAL GLN SER GLY GLY LYS ASN ILE GLU LEU
SEQRES 17 Q 248 ALA VAL MET ARG ARG ASP GLN SER LEU LYS ILE LEU ASN
SEQRES 18 Q 248 PRO GLU GLU ILE GLU LYS TYR VAL ALA GLU ILE GLU LYS
SEQRES 19 Q 248 GLU LYS GLU GLU ASN GLU LYS LYS LYS GLN LYS LYS ALA
SEQRES 20 Q 248 SER
SEQRES 1 R 241 MET PHE LEU THR ARG SER GLU TYR ASP ARG GLY VAL ASN
SEQRES 2 R 241 THR PHE SER PRO GLU GLY ARG LEU PHE GLN VAL GLU TYR
SEQRES 3 R 241 ALA ILE GLU ALA ILE LYS LEU GLY SER THR ALA ILE GLY
SEQRES 4 R 241 ILE GLN THR SER GLU GLY VAL CYS LEU ALA VAL GLU LYS
SEQRES 5 R 241 ARG ILE THR SER PRO LEU MET GLU PRO SER SER ILE GLU
SEQRES 6 R 241 LYS ILE VAL GLU ILE ASP ALA HIS ILE GLY CYS ALA MET
SEQRES 7 R 241 SER GLY LEU ILE ALA ASP ALA LYS THR LEU ILE ASP LYS
SEQRES 8 R 241 ALA ARG VAL GLU THR GLN ASN HIS TRP PHE THR TYR ASN
SEQRES 9 R 241 GLU THR MET THR VAL GLU SER VAL THR GLN ALA VAL SER
SEQRES 10 R 241 ASN LEU ALA LEU GLN PHE GLY GLU GLU ASP ALA ASP PRO
SEQRES 11 R 241 GLY ALA MET SER ARG PRO PHE GLY VAL ALA LEU LEU PHE
SEQRES 12 R 241 GLY GLY VAL ASP GLU LYS GLY PRO GLN LEU PHE HIS MET
SEQRES 13 R 241 ASP PRO SER GLY THR PHE VAL GLN CYS ASP ALA ARG ALA
SEQRES 14 R 241 ILE GLY SER ALA SER GLU GLY ALA GLN SER SER LEU GLN
SEQRES 15 R 241 GLU VAL TYR HIS LYS SER MET THR LEU LYS GLU ALA ILE
SEQRES 16 R 241 LYS SER SER LEU ILE ILE LEU LYS GLN VAL MET GLU GLU
SEQRES 17 R 241 LYS LEU ASN ALA THR ASN ILE GLU LEU ALA THR VAL GLN
SEQRES 18 R 241 PRO GLY GLN ASN PHE HIS MET PHE THR LYS GLU GLU LEU
SEQRES 19 R 241 GLU GLU VAL ILE LYS ASP ILE
SEQRES 1 S 263 MET PHE ARG ASN GLN TYR ASP ASN ASP VAL THR VAL TRP
SEQRES 2 S 263 SER PRO GLN GLY ARG ILE HIS GLN ILE GLU TYR ALA MET
SEQRES 3 S 263 GLU ALA VAL LYS GLN GLY SER ALA THR VAL GLY LEU LYS
SEQRES 4 S 263 SER LYS THR HIS ALA VAL LEU VAL ALA LEU LYS ARG ALA
SEQRES 5 S 263 GLN SER GLU LEU ALA ALA HIS GLN LYS LYS ILE LEU HIS
SEQRES 6 S 263 VAL ASP ASN HIS ILE GLY ILE SER ILE ALA GLY LEU THR
SEQRES 7 S 263 ALA ASP ALA ARG LEU LEU CYS ASN PHE MET ARG GLN GLU
SEQRES 8 S 263 CYS LEU ASP SER ARG PHE VAL PHE ASP ARG PRO LEU PRO
SEQRES 9 S 263 VAL SER ARG LEU VAL SER LEU ILE GLY SER LYS THR GLN
SEQRES 10 S 263 ILE PRO THR GLN ARG TYR GLY ARG ARG PRO TYR GLY VAL
SEQRES 11 S 263 GLY LEU LEU ILE ALA GLY TYR ASP ASP MET GLY PRO HIS
SEQRES 12 S 263 ILE PHE GLN THR 6V1 PRO SER ALA ASN TYR PHE ASP CYS
SEQRES 13 S 263 ARG ALA MET SER ILE GLY ALA ARG SER GLN SER ALA ARG
SEQRES 14 S 263 THR TYR LEU GLU ARG HIS MET SER GLU PHE MET GLU CYS
SEQRES 15 S 263 ASN LEU ASN GLU LEU VAL LYS HIS GLY LEU ARG ALA LEU
SEQRES 16 S 263 ARG GLU THR LEU PRO ALA GLU GLN ASP LEU THR THR LYS
SEQRES 17 S 263 ASN VAL SER ILE GLY ILE VAL GLY LYS ASP LEU GLU PHE
SEQRES 18 S 263 THR ILE TYR ASP ASP ASP ASP VAL SER PRO PHE LEU GLU
SEQRES 19 S 263 GLY LEU GLU GLU ARG PRO GLN ARG LYS ALA GLN PRO ALA
SEQRES 20 S 263 GLN PRO ALA ASP GLU PRO ALA GLU LYS ALA ASP GLU PRO
SEQRES 21 S 263 MET GLU HIS
SEQRES 1 T 255 MET SER SER ILE GLY THR GLY TYR ASP LEU SER ALA SER
SEQRES 2 T 255 THR PHE SER PRO ASP GLY ARG VAL PHE GLN VAL GLU TYR
SEQRES 3 T 255 ALA MET LYS ALA VAL GLU ASN SER SER THR ALA ILE GLY
SEQRES 4 T 255 ILE ARG CYS LYS ASP GLY VAL VAL PHE GLY VAL GLU LYS
SEQRES 5 T 255 LEU VAL LEU SER LYS LEU TYR GLU GLU GLY SER ASN LYS
SEQRES 6 T 255 ARG LEU PHE ASN VAL ASP ARG HIS VAL GLY MET ALA VAL
SEQRES 7 T 255 ALA GLY LEU LEU ALA ASP ALA ARG SER LEU ALA ASP ILE
SEQRES 8 T 255 ALA ARG GLU GLU ALA SER ASN PHE ARG SER ASN PHE GLY
SEQRES 9 T 255 TYR ASN ILE PRO LEU LYS HIS LEU ALA ASP ARG VAL ALA
SEQRES 10 T 255 MET TYR VAL HIS ALA TYR THR LEU TYR SER ALA VAL ARG
SEQRES 11 T 255 PRO PHE GLY CYS SER PHE MET LEU GLY SER TYR SER VAL
SEQRES 12 T 255 ASN ASP GLY ALA GLN LEU TYR MET ILE ASP PRO SER GLY
SEQRES 13 T 255 VAL SER TYR GLY TYR TRP GLY CYS ALA ILE GLY LYS ALA
SEQRES 14 T 255 ARG GLN ALA ALA LYS THR GLU ILE GLU LYS LEU GLN MET
SEQRES 15 T 255 LYS GLU MET THR CYS ARG ASP ILE VAL LYS GLU VAL ALA
SEQRES 16 T 255 LYS ILE ILE TYR ILE VAL HIS ASP GLU VAL LYS ASP LYS
SEQRES 17 T 255 ALA PHE GLU LEU GLU LEU SER TRP VAL GLY GLU LEU THR
SEQRES 18 T 255 ASN GLY ARG HIS GLU ILE VAL PRO LYS ASP ILE ARG GLU
SEQRES 19 T 255 GLU ALA GLU LYS TYR ALA LYS GLU SER LEU LYS GLU GLU
SEQRES 20 T 255 ASP GLU SER ASP ASP ASP ASN MET
SEQRES 1 U 246 MET SER ARG GLY SER SER ALA GLY PHE ASP ARG HIS ILE
SEQRES 2 U 246 THR ILE PHE SER PRO GLU GLY ARG LEU TYR GLN VAL GLU
SEQRES 3 U 246 TYR ALA PHE LYS ALA ILE ASN GLN GLY GLY LEU THR SER
SEQRES 4 U 246 VAL ALA VAL ARG GLY LYS ASP 6V1 ALA VAL ILE VAL THR
SEQRES 5 U 246 GLN LYS LYS VAL PRO ASP LYS LEU LEU ASP SER SER THR
SEQRES 6 U 246 VAL THR HIS LEU PHE LYS ILE THR GLU ASN ILE GLY CYS
SEQRES 7 U 246 VAL MET THR GLY MET THR ALA ASP SER ARG SER GLN VAL
SEQRES 8 U 246 GLN ARG ALA ARG TYR GLU ALA ALA ASN TRP LYS TYR LYS
SEQRES 9 U 246 TYR GLY TYR GLU ILE PRO VAL ASP MET LEU CYS LYS ARG
SEQRES 10 U 246 ILE ALA ASP ILE SER GLN VAL TYR THR GLN ASN ALA GLU
SEQRES 11 U 246 MET ARG PRO LEU GLY CYS YCM MET ILE LEU ILE GLY ILE
SEQRES 12 U 246 ASP GLU GLU GLN GLY PRO GLN VAL TYR LYS CYS ASP PRO
SEQRES 13 U 246 ALA GLY TYR TYR 6V1 GLY PHE LYS ALA THR ALA ALA GLY
SEQRES 14 U 246 VAL LYS GLN THR GLU SER THR SER PHE LEU GLU LYS LYS
SEQRES 15 U 246 VAL LYS LYS LYS PHE ASP TRP THR PHE GLU GLN THR VAL
SEQRES 16 U 246 GLU THR ALA ILE THR CYS LEU SER THR VAL LEU SER ILE
SEQRES 17 U 246 ASP PHE LYS PRO SER GLU ILE GLU VAL GLY VAL VAL THR
SEQRES 18 U 246 VAL GLU ASN PRO LYS PHE ARG ILE LEU THR GLU ALA GLU
SEQRES 19 U 246 ILE ASP ALA HIS LEU VAL ALA LEU ALA GLU ARG ASP
SEQRES 1 V 234 THR THR ILE ALA GLY VAL VAL TYR LYS ASP GLY ILE VAL
SEQRES 2 V 234 LEU GLY ALA ASP THR ARG ALA THR GLU GLY MET VAL VAL
SEQRES 3 V 234 ALA ASP LYS ASN CYS SER LYS ILE HIS PHE ILE SER PRO
SEQRES 4 V 234 ASN ILE TYR CYS CYS GLY ALA GLY THR ALA ALA ASP THR
SEQRES 5 V 234 ASP MET THR THR GLN LEU ILE SER SER ASN LEU GLU LEU
SEQRES 6 V 234 HIS SER LEU SER THR GLY ARG LEU PRO ARG VAL VAL THR
SEQRES 7 V 234 ALA ASN ARG MET LEU LYS GLN MET LEU PHE ARG TYR GLN
SEQRES 8 V 234 GLY TYR ILE GLY ALA ALA LEU VAL LEU GLY GLY VAL ASP
SEQRES 9 V 234 VAL THR GLY PRO HIS LEU TYR SER ILE TYR PRO HIS GLY
SEQRES 10 V 234 SER THR ASP LYS LEU PRO TYR VAL THR MET GLY SER GLY
SEQRES 11 V 234 SER LEU ALA ALA MET ALA VAL PHE GLU ASP LYS PHE ARG
SEQRES 12 V 234 PRO ASP MET GLU GLU GLU GLU ALA LYS ASN LEU VAL SER
SEQRES 13 V 234 GLU ALA ILE ALA ALA GLY ILE PHE ASN ASP LEU GLY SER
SEQRES 14 V 234 GLY SER ASN ILE ASP LEU CYS VAL ILE SER LYS ASN LYS
SEQRES 15 V 234 LEU ASP PHE LEU ARG PRO TYR THR VAL PRO ASN LYS LYS
SEQRES 16 V 234 GLY THR ARG LEU GLY ARG TYR ARG CYS GLU LYS GLY THR
SEQRES 17 V 234 THR ALA VAL LEU THR GLU LYS ILE THR PRO LEU GLU ILE
SEQRES 18 V 234 GLU VAL LEU GLU GLU THR VAL GLN THR MET ASP THR SER
SEQRES 1 W 205 MET SER ILE MET SER TYR ASN GLY GLY ALA VAL MET ALA
SEQRES 2 W 205 MET LYS GLY LYS ASN CYS VAL ALA ILE ALA ALA ASP ARG
SEQRES 3 W 205 ARG PHE GLY ILE GLN ALA GLN MET VAL THR THR ASP PHE
SEQRES 4 W 205 GLN LYS ILE PHE PRO MET GLY ASP ARG LEU TYR ILE GLY
SEQRES 5 W 205 LEU ALA GLY LEU ALA THR ASP VAL GLN THR VAL ALA GLN
SEQRES 6 W 205 ARG LEU LYS PHE ARG LEU ASN LEU TYR GLU LEU LYS GLU
SEQRES 7 W 205 GLY ARG GLN ILE LYS PRO TYR THR LEU MET SER MET VAL
SEQRES 8 W 205 ALA ASN LEU LEU TYR GLU LYS ARG PHE GLY PRO TYR TYR
SEQRES 9 W 205 THR GLU PRO VAL ILE ALA GLY LEU ASP PRO LYS THR PHE
SEQRES 10 W 205 LYS PRO PHE ILE CYS SER LEU ASP LEU ILE GLY CYS PRO
SEQRES 11 W 205 MET VAL THR ASP ASP PHE VAL VAL SER GLY THR CYS ALA
SEQRES 12 W 205 GLU GLN MET TYR GLY MET CYS GLU SER LEU TRP GLU PRO
SEQRES 13 W 205 ASN MET ASP PRO ASP HIS LEU PHE GLU THR ILE SER GLN
SEQRES 14 W 205 ALA MET LEU ASN ALA VAL ASP ARG ASP ALA VAL SER GLY
SEQRES 15 W 205 MET GLY VAL ILE VAL HIS ILE ILE GLU LYS ASP LYS ILE
SEQRES 16 W 205 THR THR ARG THR LEU LYS ALA ARG MET ASP
SEQRES 1 X 201 MET GLU TYR LEU ILE GLY ILE GLN GLY PRO ASP TYR VAL
SEQRES 2 X 201 LEU VAL ALA SER ASP ARG VAL ALA ALA SER ASN ILE VAL
SEQRES 3 X 201 GLN MET LYS ASP ASP HIS ASP LYS MET PHE LYS MET SER
SEQRES 4 X 201 GLU LYS ILE LEU LEU LEU CYS VAL GLY GLU ALA GLY ASP
SEQRES 5 X 201 THR VAL GLN PHE ALA GLU TYR ILE GLN LYS ASN VAL GLN
SEQRES 6 X 201 LEU TYR LYS MET ARG ASN GLY TYR GLU LEU SER PRO THR
SEQRES 7 X 201 ALA ALA ALA ASN PHE THR ARG ARG ASN LEU ALA ASP 6V1
SEQRES 8 X 201 LEU ARG SER ARG THR PRO TYR HIS VAL ASN LEU LEU LEU
SEQRES 9 X 201 ALA GLY TYR ASP GLU HIS GLU GLY PRO ALA LEU TYR TYR
SEQRES 10 X 201 MET ASP TYR LEU ALA ALA LEU ALA LYS ALA PRO PHE ALA
SEQRES 11 X 201 ALA HIS GLY TYR GLY ALA PHE LEU THR LEU SER ILE LEU
SEQRES 12 X 201 ASP ARG TYR TYR THR PRO THR ILE SER ARG GLU ARG ALA
SEQRES 13 X 201 VAL GLU LEU LEU ARG LYS CYS LEU GLU GLU LEU GLN LYS
SEQRES 14 X 201 ARG PHE ILE LEU ASN LEU PRO THR PHE SER VAL ARG ILE
SEQRES 15 X 201 ILE ASP LYS ASN GLY ILE HIS ASP LEU ASP ASN ILE SER
SEQRES 16 X 201 PHE PRO LYS GLN GLY SER
SEQRES 1 Y 204 THR THR THR LEU ALA PHE LYS PHE ARG HIS GLY VAL ILE
SEQRES 2 Y 204 VAL ALA ALA ASP SER ARG ALA THR ALA GLY ALA TYR ILE
SEQRES 3 Y 204 ALA SER GLN THR VAL LYS LYS VAL ILE GLU ILE ASN PRO
SEQRES 4 Y 204 TYR LEU LEU GLY THR MET ALA GLY GLY ALA ALA ASP CYS
SEQRES 5 Y 204 SER PHE TRP GLU ARG LEU LEU ALA ARG GLN CYS ARG ILE
SEQRES 6 Y 204 TYR GLU LEU ARG ASN LYS GLU ARG ILE SER VAL ALA ALA
SEQRES 7 Y 204 ALA SER LYS LEU LEU ALA ASN MET VAL TYR GLN TYR LYS
SEQRES 8 Y 204 GLY MET GLY LEU SER MET GLY THR MET ILE CYS GLY TRP
SEQRES 9 Y 204 ASP LYS ARG GLY PRO GLY LEU TYR TYR VAL ASP SER GLU
SEQRES 10 Y 204 GLY ASN ARG ILE SER GLY ALA THR PHE SER VAL GLY SER
SEQRES 11 Y 204 GLY SER VAL TYR ALA TYR GLY VAL MET ASP ARG GLY TYR
SEQRES 12 Y 204 SER TYR ASP LEU GLU VAL GLU GLN ALA TYR ASP LEU ALA
SEQRES 13 Y 204 ARG ARG ALA ILE TYR GLN ALA THR TYR ARG ASP ALA TYR
SEQRES 14 Y 204 SER GLY GLY ALA VAL ASN LEU TYR HIS VAL ARG GLU ASP
SEQRES 15 Y 204 GLY TRP ILE ARG VAL SER SER ASP ASN VAL ALA ASP LEU
SEQRES 16 Y 204 HIS GLU LYS TYR SER GLY SER THR PRO
SEQRES 1 Z 213 ARG PHE SER PRO TYR VAL PHE ASN GLY GLY THR ILE LEU
SEQRES 2 Z 213 ALA ILE ALA GLY GLU ASP PHE ALA ILE VAL ALA SER ASP
SEQRES 3 Z 213 THR ARG LEU SER GLU GLY PHE SER ILE HIS THR ARG ASP
SEQRES 4 Z 213 SER PRO LYS CYS TYR LYS LEU THR ASP LYS THR VAL ILE
SEQRES 5 Z 213 GLY CYS SER GLY PHE HIS GLY ASP CYS LEU THR LEU THR
SEQRES 6 Z 213 LYS ILE ILE GLU ALA ARG LEU LYS MET TYR LYS HIS SER
SEQRES 7 Z 213 ASN ASN LYS ALA MET THR THR GLY ALA ILE ALA ALA MET
SEQRES 8 Z 213 LEU SER THR ILE LEU TYR SER ARG ARG PHE PHE PRO TYR
SEQRES 9 Z 213 TYR VAL TYR ASN ILE ILE GLY GLY LEU ASP GLU GLU GLY
SEQRES 10 Z 213 LYS GLY ALA VAL TYR SER PHE ASP PRO VAL GLY SER TYR
SEQRES 11 Z 213 GLN ARG ASP SER PHE LYS ALA GLY GLY SER ALA SER ALA
SEQRES 12 Z 213 MET LEU GLN PRO LEU LEU ASP ASN GLN VAL GLY PHE LYS
SEQRES 13 Z 213 ASN MET GLN ASN VAL GLU HIS VAL PRO LEU SER LEU ASP
SEQRES 14 Z 213 ARG ALA MET ARG LEU VAL LYS ASP VAL PHE ILE SER ALA
SEQRES 15 Z 213 ALA GLU ARG ASP VAL TYR THR GLY ASP ALA LEU ARG ILE
SEQRES 16 Z 213 CYS ILE VAL THR LYS GLU GLY ILE ARG GLU GLU THR VAL
SEQRES 17 Z 213 SER LEU ARG LYS ASP
SEQRES 1 a 219 THR GLN ASN PRO MET VAL THR GLY THR SER VAL LEU GLY
SEQRES 2 a 219 VAL LYS PHE GLU GLY GLY VAL VAL ILE ALA ALA ASP MET
SEQRES 3 a 219 LEU GLY SER TYR GLY SER LEU ALA ARG PHE ARG ASN ILE
SEQRES 4 a 219 SER ARG ILE MET ARG VAL ASN ASN SER THR MET LEU GLY
SEQRES 5 a 219 ALA SER GLY ASP TYR ALA ASP PHE GLN TYR LEU LYS GLN
SEQRES 6 a 219 VAL LEU GLY GLN MET VAL ILE ASP GLU GLU LEU LEU GLY
SEQRES 7 a 219 ASP GLY HIS SER TYR SER PRO ARG ALA ILE HIS SER TRP
SEQRES 8 a 219 LEU THR ARG ALA MET TYR SER ARG ARG SER LYS MET ASN
SEQRES 9 a 219 PRO LEU TRP ASN THR MET VAL ILE GLY GLY TYR ALA ASP
SEQRES 10 a 219 GLY GLU SER PHE LEU GLY TYR VAL ASP MET LEU GLY VAL
SEQRES 11 a 219 ALA TYR GLU ALA PRO SER LEU ALA THR GLY TYR GLY ALA
SEQRES 12 a 219 TYR LEU ALA GLN PRO LEU LEU ARG GLU VAL LEU GLU LYS
SEQRES 13 a 219 GLN PRO VAL LEU SER GLN THR GLU ALA ARG ASP LEU VAL
SEQRES 14 a 219 GLU ARG CYS MET ARG VAL LEU TYR TYR ARG ASP ALA ARG
SEQRES 15 a 219 SER TYR ASN ARG PHE GLN ILE ALA THR VAL THR GLU LYS
SEQRES 16 a 219 GLY VAL GLU ILE GLU GLY PRO LEU SER THR GLU THR ASN
SEQRES 17 a 219 TRP ASP ILE ALA HIS MET ILE SER GLY PHE GLU
SEQRES 1 b 205 THR THR ILE MET ALA VAL GLN PHE ASP GLY GLY VAL VAL
SEQRES 2 b 205 LEU GLY ALA ASP SER ARG THR THR THR GLY SER TYR ILE
SEQRES 3 b 205 ALA ASN ARG VAL THR ASP LYS LEU THR PRO ILE HIS ASP
SEQRES 4 b 205 ARG ILE PHE CYS CYS ARG SER GLY SER ALA ALA ASP THR
SEQRES 5 b 205 GLN ALA VAL ALA ASP ALA VAL THR TYR GLN LEU GLY PHE
SEQRES 6 b 205 HIS SER ILE GLU LEU ASN GLU PRO PRO LEU VAL HIS THR
SEQRES 7 b 205 ALA ALA SER LEU PHE LYS GLU MET CYS TYR ARG TYR ARG
SEQRES 8 b 205 GLU ASP LEU MET ALA GLY ILE ILE ILE ALA GLY TRP ASP
SEQRES 9 b 205 PRO GLN GLU GLY GLY GLN VAL TYR SER VAL PRO MET GLY
SEQRES 10 b 205 GLY MET MET VAL ARG GLN SER PHE ALA ILE GLY GLY SER
SEQRES 11 b 205 GLY SER SER TYR ILE TYR GLY TYR VAL ASP ALA THR TYR
SEQRES 12 b 205 ARG GLU GLY MET THR LYS GLU GLU CYS LEU GLN PHE THR
SEQRES 13 b 205 ALA ASN ALA LEU ALA LEU ALA MET GLU ARG ASP GLY SER
SEQRES 14 b 205 SER GLY GLY VAL ILE ARG LEU ALA ALA ILE ALA GLU SER
SEQRES 15 b 205 GLY VAL GLU ARG GLN VAL LEU LEU GLY ASP GLN ILE PRO
SEQRES 16 b 205 LYS PHE ALA VAL ALA THR LEU PRO PRO ALA
SEQRES 1 c 4 6V9 OAS OAS 6VA
SEQRES 1 d 4 6V9 OAS OAS 6VA
SEQRES 1 e 4 6V9 OAS OAS 6VA
SEQRES 1 f 4 6V9 OAS OAS 6VA
MODRES 5LEZ YCM C 63 CYS MODIFIED RESIDUE
MODRES 5LEZ 6V1 E 148 CYS MODIFIED RESIDUE
MODRES 5LEZ 6V1 G 47 CYS MODIFIED RESIDUE
MODRES 5LEZ YCM G 137 CYS MODIFIED RESIDUE
MODRES 5LEZ 6V1 G 161 CYS MODIFIED RESIDUE
MODRES 5LEZ 6V1 J 91 CYS MODIFIED RESIDUE
MODRES 5LEZ YCM Q 63 CYS MODIFIED RESIDUE
MODRES 5LEZ 6V1 S 148 CYS MODIFIED RESIDUE
MODRES 5LEZ 6V1 U 47 CYS MODIFIED RESIDUE
MODRES 5LEZ YCM U 137 CYS MODIFIED RESIDUE
MODRES 5LEZ 6V1 U 161 CYS MODIFIED RESIDUE
MODRES 5LEZ 6V1 X 91 CYS MODIFIED RESIDUE
HET YCM C 63 10
HET 6V1 E 148 15
HET 6V1 G 47 15
HET YCM G 137 10
HET 6V1 G 161 15
HET 6V1 J 91 15
HET YCM Q 63 10
HET 6V1 S 148 15
HET 6V1 U 47 15
HET YCM U 137 10
HET 6V1 U 161 15
HET 6V1 X 91 15
HET 6V9 c 1 8
HET OAS c 2 7
HET OAS c 3 7
HET 6VA c 4 15
HET 6V9 d 1 8
HET OAS d 2 7
HET OAS d 3 7
HET 6VA d 4 15
HET 6V9 e 1 8
HET OAS e 2 7
HET OAS e 3 7
HET 6VA e 4 15
HET 6V9 f 1 8
HET OAS f 2 7
HET OAS f 3 7
HET 6VA f 4 15
HET K G 301 1
HET MG H 301 1
HET MG H 302 1
HET 1PE H 303 16
HET MG I 301 1
HET 1PE I 302 16
HET MG I 303 1
HET MG J 301 1
HET MG K 301 1
HET 1PE K 302 16
HET 1PE L 301 16
HET K L 302 1
HET MG L 303 1
HET 1PE N 301 16
HET K N 302 1
HET 1PE U 301 16
HET K U 302 1
HET MG V 301 1
HET MG W 301 1
HET 1PE W 302 16
HET MG X 301 1
HET 1PE Y 301 16
HET K Z 301 1
HET 1PE a 301 16
HET K b 301 1
HET ACT c 101 4
HET ACT d 101 4
HET ACT e 101 4
HET ACT f 101 4
HETNAM YCM S-(2-AMINO-2-OXOETHYL)-L-CYSTEINE
HETNAM 6V1 (2~{R})-2-AZANYL-3-[(3~{R})-1-ETHYL-2,5-
HETNAM 2 6V1 BIS(OXIDANYLIDENE)PYRROLIDIN-3-YL]SULFANYL-PROPANOIC
HETNAM 3 6V1 ACID
HETNAM 6V9 2-METHYL-1,3-THIAZOLE-5-CARBOXYLIC ACID
HETNAM OAS O-ACETYLSERINE
HETNAM 6VA (3~{R},4~{S})-4-AZANYL-2-METHYL-5-PHENYL-PENTANE-2,3-
HETNAM 2 6VA DIOL
HETNAM K POTASSIUM ION
HETNAM MG MAGNESIUM ION
HETNAM 1PE PENTAETHYLENE GLYCOL
HETNAM ACT ACETATE ION
HETSYN YCM CYSTEINE-S-ACETAMIDE
HETSYN 1PE PEG400
FORMUL 3 YCM 4(C5 H10 N2 O3 S)
FORMUL 5 6V1 8(C9 H14 N2 O4 S)
FORMUL 29 6V9 4(C5 H5 N O2 S)
FORMUL 29 OAS 8(C5 H9 N O4)
FORMUL 29 6VA 4(C12 H19 N O2)
FORMUL 33 K 6(K 1+)
FORMUL 34 MG 10(MG 2+)
FORMUL 36 1PE 9(C10 H22 O6)
FORMUL 58 ACT 4(C2 H3 O2 1-)
FORMUL 62 HOH *3717(H2 O)
HELIX 1 AA1 LEU A 18 GLY A 30 1 13
HELIX 2 AA2 ASP A 57 VAL A 61 5 5
HELIX 3 AA3 MET A 78 GLN A 101 1 24
HELIX 4 AA4 PRO A 105 TYR A 120 1 16
HELIX 5 AA5 ASN A 165 LYS A 175 1 11
HELIX 6 AA6 GLU A 182 GLU A 196 1 15
HELIX 7 AA7 THR A 221 ALA A 230 1 10
HELIX 8 AA8 LEU B 18 ALA B 31 1 14
HELIX 9 AA9 ILE B 79 GLN B 102 1 24
HELIX 10 AB1 PRO B 106 PHE B 124 1 19
HELIX 11 AB2 ASN B 167 TYR B 179 1 13
HELIX 12 AB3 THR B 185 MET B 201 1 17
HELIX 13 AB4 LYS B 229 LYS B 246 1 18
HELIX 14 AB5 LEU C 16 LYS C 28 1 13
HELIX 15 AB6 ASP C 55 ARG C 60 5 6
HELIX 16 AB7 LEU C 76 GLU C 99 1 24
HELIX 17 AB8 THR C 103 TYR C 118 1 16
HELIX 18 AB9 GLY C 164 TYR C 176 1 13
HELIX 19 AC1 THR C 183 GLU C 197 1 15
HELIX 20 AC2 ASN C 221 LYS C 234 1 14
HELIX 21 AC3 LEU D 21 LYS D 32 1 12
HELIX 22 AC4 GLU D 60 ILE D 64 5 5
HELIX 23 AC5 ASP D 84 ASN D 104 1 21
HELIX 24 AC6 THR D 108 ASN D 118 1 11
HELIX 25 AC7 ALA D 173 TYR D 185 1 13
HELIX 26 AC8 THR D 190 MET D 206 1 17
HELIX 27 AC9 THR D 230 LYS D 239 1 10
HELIX 28 AD1 ILE E 19 GLN E 31 1 13
HELIX 29 AD2 LEU E 77 ASP E 100 1 24
HELIX 30 AD3 PRO E 104 ILE E 118 1 15
HELIX 31 AD4 PRO E 119 ARG E 122 5 4
HELIX 32 AD5 ARG E 164 MET E 180 1 17
HELIX 33 AD6 ASN E 183 GLU E 197 1 15
HELIX 34 AD7 ASP E 225 ASP E 228 5 4
HELIX 35 AD8 VAL E 229 GLU E 234 1 6
HELIX 36 AD9 VAL F 20 ASN F 32 1 13
HELIX 37 AE1 LEU F 80 GLY F 103 1 24
HELIX 38 AE2 PRO F 107 TYR F 122 1 16
HELIX 39 AE3 ALA F 168 GLU F 177 1 10
HELIX 40 AE4 LYS F 178 LEU F 179 5 2
HELIX 41 AE5 GLN F 180 MET F 184 5 5
HELIX 42 AE6 THR F 185 HIS F 201 1 17
HELIX 43 AE7 LEU F 219 ASN F 221 5 3
HELIX 44 AE8 PRO F 228 LYS F 244 1 17
HELIX 45 AE9 LEU G 22 GLY G 35 1 14
HELIX 46 AF1 ASP G 62 VAL G 66 5 5
HELIX 47 AF2 MET G 83 GLY G 106 1 24
HELIX 48 AF3 PRO G 110 THR G 126 1 17
HELIX 49 AF4 LYS G 171 LYS G 186 1 16
HELIX 50 AF5 GLN G 193 SER G 207 1 15
HELIX 51 AF6 LYS G 211 SER G 213 5 3
HELIX 52 AF7 THR G 231 GLU G 244 1 14
HELIX 53 AF8 THR H 48 GLY H 71 1 24
HELIX 54 AF9 ARG H 75 TYR H 90 1 16
HELIX 55 AG1 GLY H 130 PHE H 142 1 13
HELIX 56 AG2 GLU H 147 ASP H 166 1 20
HELIX 57 AG3 SER I 1 TYR I 5 5 5
HELIX 58 AG4 LEU I 55 GLU I 77 1 23
HELIX 59 AG5 LYS I 82 GLU I 96 1 15
HELIX 60 AG6 CYS I 141 TRP I 153 1 13
HELIX 61 AG7 ASP I 158 ASP I 175 1 18
HELIX 62 AG8 GLY J 51 GLY J 72 1 22
HELIX 63 AG9 SER J 76 LEU J 92 1 17
HELIX 64 AH1 TYR J 134 TYR J 147 1 14
HELIX 65 AH2 SER J 152 PHE J 171 1 20
HELIX 66 AH3 GLY K 48 LYS K 71 1 24
HELIX 67 AH4 SER K 75 GLN K 89 1 15
HELIX 68 AH5 GLY K 131 TYR K 143 1 13
HELIX 69 AH6 GLU K 148 ASP K 167 1 20
HELIX 70 AH7 VAL K 192 SER K 200 1 9
HELIX 71 AH8 PHE L 57 ASN L 80 1 24
HELIX 72 AH9 THR L 84 ARG L 99 1 16
HELIX 73 AI1 ALA L 141 VAL L 153 1 13
HELIX 74 AI2 SER L 167 GLU L 184 1 18
HELIX 75 AI3 TYR M 57 LEU M 77 1 21
HELIX 76 AI4 SER M 84 LYS M 102 1 19
HELIX 77 AI5 TYR M 141 ALA M 146 1 6
HELIX 78 AI6 ALA M 146 GLN M 157 1 12
HELIX 79 AI7 SER M 161 ASP M 180 1 20
HELIX 80 AI8 TRP M 209 MET M 214 5 6
HELIX 81 AI9 SER N 48 ASN N 71 1 24
HELIX 82 AJ1 LEU N 75 TYR N 90 1 16
HELIX 83 AJ2 ARG N 91 LEU N 94 5 4
HELIX 84 AJ3 GLY N 129 TYR N 134 5 6
HELIX 85 AJ4 ILE N 135 TYR N 143 1 9
HELIX 86 AJ5 THR N 148 ASP N 167 1 20
HELIX 87 AJ6 LEU N 190 ILE N 194 5 5
HELIX 88 AJ7 LEU O 18 GLY O 30 1 13
HELIX 89 AJ8 ASP O 57 VAL O 61 5 5
HELIX 90 AJ9 MET O 78 GLN O 101 1 24
HELIX 91 AK1 PRO O 105 TYR O 120 1 16
HELIX 92 AK2 ASN O 165 LYS O 175 1 11
HELIX 93 AK3 GLU O 182 GLU O 196 1 15
HELIX 94 AK4 THR O 221 ALA O 230 1 10
HELIX 95 AK5 LEU P 18 ALA P 31 1 14
HELIX 96 AK6 ILE P 79 GLN P 102 1 24
HELIX 97 AK7 PRO P 106 PHE P 124 1 19
HELIX 98 AK8 ASN P 167 TYR P 179 1 13
HELIX 99 AK9 THR P 185 MET P 201 1 17
HELIX 100 AL1 LYS P 229 GLU P 244 1 16
HELIX 101 AL2 LEU Q 16 LYS Q 28 1 13
HELIX 102 AL3 ASP Q 55 ARG Q 60 5 6
HELIX 103 AL4 LEU Q 76 GLU Q 99 1 24
HELIX 104 AL5 THR Q 103 TYR Q 118 1 16
HELIX 105 AL6 GLY Q 164 TYR Q 176 1 13
HELIX 106 AL7 THR Q 183 GLU Q 197 1 15
HELIX 107 AL8 ASN Q 221 LYS Q 234 1 14
HELIX 108 AL9 LYS Q 234 ASN Q 239 1 6
HELIX 109 AM1 LEU R 21 LYS R 32 1 12
HELIX 110 AM2 GLU R 60 ILE R 64 5 5
HELIX 111 AM3 ASP R 84 ASN R 104 1 21
HELIX 112 AM4 THR R 108 ASN R 118 1 11
HELIX 113 AM5 ALA R 173 TYR R 185 1 13
HELIX 114 AM6 THR R 190 MET R 206 1 17
HELIX 115 AM7 THR R 230 LYS R 239 1 10
HELIX 116 AM8 ARG S 3 ASP S 7 5 5
HELIX 117 AM9 ILE S 19 GLN S 31 1 13
HELIX 118 AN1 LEU S 77 ASP S 100 1 24
HELIX 119 AN2 PRO S 104 ILE S 118 1 15
HELIX 120 AN3 PRO S 119 ARG S 122 5 4
HELIX 121 AN4 ARG S 164 MET S 180 1 17
HELIX 122 AN5 ASN S 183 GLU S 197 1 15
HELIX 123 AN6 ASP S 225 ASP S 228 5 4
HELIX 124 AN7 VAL S 229 GLU S 234 1 6
HELIX 125 AN8 VAL T 20 ASN T 32 1 13
HELIX 126 AN9 LEU T 80 GLY T 103 1 24
HELIX 127 AO1 PRO T 107 TYR T 122 1 16
HELIX 128 AO2 ALA T 168 GLU T 177 1 10
HELIX 129 AO3 LYS T 178 LEU T 179 5 2
HELIX 130 AO4 GLN T 180 MET T 184 5 5
HELIX 131 AO5 THR T 185 HIS T 201 1 17
HELIX 132 AO6 LEU T 219 ASN T 221 5 3
HELIX 133 AO7 PRO T 228 LYS T 244 1 17
HELIX 134 AO8 LEU U 22 GLY U 35 1 14
HELIX 135 AO9 ASP U 62 VAL U 66 5 5
HELIX 136 AP1 MET U 83 GLY U 106 1 24
HELIX 137 AP2 PRO U 110 ASN U 128 1 19
HELIX 138 AP3 LYS U 171 LYS U 184 1 14
HELIX 139 AP4 THR U 194 SER U 207 1 14
HELIX 140 AP5 LYS U 211 SER U 213 5 3
HELIX 141 AP6 THR U 231 GLU U 244 1 14
HELIX 142 AP7 THR V 48 GLY V 71 1 24
HELIX 143 AP8 ARG V 75 TYR V 90 1 16
HELIX 144 AP9 GLY V 130 PHE V 142 1 13
HELIX 145 AQ1 GLU V 147 ASP V 166 1 20
HELIX 146 AQ2 SER W 1 TYR W 5 5 5
HELIX 147 AQ3 LEU W 55 GLU W 77 1 23
HELIX 148 AQ4 LYS W 82 GLU W 96 1 15
HELIX 149 AQ5 CYS W 141 TRP W 153 1 13
HELIX 150 AQ6 ASP W 158 ASP W 175 1 18
HELIX 151 AQ7 GLY X 51 GLY X 72 1 22
HELIX 152 AQ8 SER X 76 ARG X 93 1 18
HELIX 153 AQ9 TYR X 134 TYR X 147 1 14
HELIX 154 AR1 SER X 152 PHE X 171 1 20
HELIX 155 AR2 GLY Y 48 LYS Y 71 1 24
HELIX 156 AR3 SER Y 75 GLN Y 89 1 15
HELIX 157 AR4 GLY Y 131 TYR Y 143 1 13
HELIX 158 AR5 GLU Y 148 ASP Y 167 1 20
HELIX 159 AR6 VAL Y 192 TYR Y 199 1 8
HELIX 160 AR7 PHE Z 57 ASN Z 80 1 24
HELIX 161 AR8 THR Z 84 ARG Z 99 1 16
HELIX 162 AR9 ALA Z 141 VAL Z 153 1 13
HELIX 163 AS1 SER Z 167 GLU Z 184 1 18
HELIX 164 AS2 TYR a 57 GLY a 78 1 22
HELIX 165 AS3 SER a 84 LYS a 102 1 19
HELIX 166 AS4 GLY a 140 ALA a 146 1 7
HELIX 167 AS5 ALA a 146 GLN a 157 1 12
HELIX 168 AS6 SER a 161 ASP a 180 1 20
HELIX 169 AS7 TRP a 209 MET a 214 5 6
HELIX 170 AS8 SER b 48 ASN b 71 1 24
HELIX 171 AS9 LEU b 75 TYR b 90 1 16
HELIX 172 AT1 ARG b 91 LEU b 94 5 4
HELIX 173 AT2 GLY b 129 TYR b 134 5 6
HELIX 174 AT3 ILE b 135 TYR b 143 1 9
HELIX 175 AT4 THR b 148 ASP b 167 1 20
HELIX 176 AT5 LEU b 190 ILE b 194 5 5
SHEET 1 AA1 5 ALA A 159 MET A 162 0
SHEET 2 AA1 5 SER A 34 LYS A 38 -1 N GLY A 36 O THR A 160
SHEET 3 AA1 5 VAL A 43 GLU A 48 -1 O ALA A 46 N VAL A 35
SHEET 4 AA1 5 ILE A 207 ASN A 213 -1 O GLY A 210 N LEU A 45
SHEET 5 AA1 5 GLY A 216 ARG A 219 -1 O ARG A 218 N ILE A 211
SHEET 1 AA2 5 GLU A 65 THR A 68 0
SHEET 2 AA2 5 ILE A 71 GLY A 77 -1 O ILE A 71 N ILE A 67
SHEET 3 AA2 5 VAL A 131 ASN A 139 -1 O LEU A 134 N VAL A 74
SHEET 4 AA2 5 ARG A 142 SER A 148 -1 O PHE A 146 N ILE A 135
SHEET 5 AA2 5 TYR A 154 ALA A 156 -1 O PHE A 155 N GLN A 147
SHEET 1 AA3 5 ALA B 161 ILE B 164 0
SHEET 2 AA3 5 CYS B 34 ALA B 39 -1 N GLY B 36 O THR B 162
SHEET 3 AA3 5 GLY B 42 GLU B 48 -1 O ALA B 46 N LEU B 35
SHEET 4 AA3 5 VAL B 211 GLU B 219 -1 O GLU B 212 N ALA B 47
SHEET 5 AA3 5 LYS B 222 VAL B 227 -1 O VAL B 224 N THR B 217
SHEET 1 AA4 5 ILE B 65 ASN B 69 0
SHEET 2 AA4 5 MET B 72 GLY B 78 -1 O CYS B 74 N TYR B 66
SHEET 3 AA4 5 VAL B 132 ASP B 140 -1 O ILE B 137 N ALA B 73
SHEET 4 AA4 5 GLY B 144 SER B 150 -1 O TYR B 148 N TYR B 136
SHEET 5 AA4 5 TYR B 156 GLY B 158 -1 O GLY B 157 N GLN B 149
SHEET 1 AA5 5 ALA C 158 ILE C 161 0
SHEET 2 AA5 5 ALA C 32 ARG C 36 -1 N GLY C 34 O ASN C 159
SHEET 3 AA5 5 ILE C 40 GLU C 46 -1 O GLY C 44 N VAL C 33
SHEET 4 AA5 5 ILE C 206 ARG C 212 -1 O ALA C 209 N LEU C 43
SHEET 5 AA5 5 SER C 216 ILE C 219 -1 O LYS C 218 N VAL C 210
SHEET 1 AA6 5 ILE C 62 ASP C 66 0
SHEET 2 AA6 5 VAL C 69 GLY C 75 -1 O VAL C 69 N LEU C 65
SHEET 3 AA6 5 ILE C 129 PHE C 136 -1 O LEU C 132 N ALA C 72
SHEET 4 AA6 5 PRO C 142 THR C 147 -1 O TYR C 145 N ILE C 133
SHEET 5 AA6 5 TYR C 153 ALA C 155 -1 O HIS C 154 N GLN C 146
SHEET 1 AA7 5 ALA D 167 ILE D 170 0
SHEET 2 AA7 5 ALA D 37 THR D 42 -1 N GLY D 39 O ARG D 168
SHEET 3 AA7 5 GLY D 45 GLU D 51 -1 O ALA D 49 N ILE D 38
SHEET 4 AA7 5 ILE D 215 GLN D 221 -1 O ALA D 218 N LEU D 48
SHEET 5 AA7 5 GLN D 224 MET D 228 -1 O HIS D 227 N THR D 219
SHEET 1 AA8 5 ILE D 67 ASP D 71 0
SHEET 2 AA8 5 ILE D 74 GLY D 80 -1 O ILE D 74 N ILE D 70
SHEET 3 AA8 5 VAL D 139 ASP D 147 -1 O GLY D 144 N GLY D 75
SHEET 4 AA8 5 GLY D 150 MET D 156 -1 O GLN D 152 N GLY D 145
SHEET 5 AA8 5 PHE D 162 GLN D 164 -1 O VAL D 163 N HIS D 155
SHEET 1 AA9 5 ALA E 158 ILE E 161 0
SHEET 2 AA9 5 THR E 35 LYS E 39 -1 N GLY E 37 O MET E 159
SHEET 3 AA9 5 HIS E 43 LEU E 49 -1 O VAL E 45 N LEU E 38
SHEET 4 AA9 5 VAL E 210 GLY E 216 -1 O SER E 211 N ALA E 48
SHEET 5 AA9 5 LEU E 219 TYR E 224 -1 O TYR E 224 N ILE E 212
SHEET 1 AB1 5 ILE E 63 ASP E 67 0
SHEET 2 AB1 5 ILE E 70 GLY E 76 -1 O ILE E 72 N LEU E 64
SHEET 3 AB1 5 VAL E 130 ASP E 138 -1 O LEU E 133 N SER E 73
SHEET 4 AB1 5 GLY E 141 THR E 147 -1 O PHE E 145 N ILE E 134
SHEET 5 AB1 5 TYR E 153 CYS E 156 -1 O CYS E 156 N ILE E 144
SHEET 1 AB2 5 GLY F 162 ILE F 165 0
SHEET 2 AB2 5 ALA F 36 ARG F 40 -1 N ALA F 36 O ILE F 165
SHEET 3 AB2 5 GLY F 44 LEU F 52 -1 O GLY F 48 N ILE F 37
SHEET 4 AB2 5 PHE F 209 GLY F 217 -1 O SER F 214 N PHE F 47
SHEET 5 AB2 5 GLU F 225 ILE F 226 -1 O GLU F 225 N TRP F 215
SHEET 1 AB3 5 LEU F 66 ASP F 70 0
SHEET 2 AB3 5 VAL F 73 GLY F 79 -1 O MET F 75 N PHE F 67
SHEET 3 AB3 5 CYS F 133 SER F 141 -1 O MET F 136 N ALA F 76
SHEET 4 AB3 5 GLY F 145 ILE F 151 -1 O ILE F 151 N PHE F 135
SHEET 5 AB3 5 SER F 157 GLY F 159 -1 O TYR F 158 N MET F 150
SHEET 1 AB4 5 ALA G 165 GLY G 169 0
SHEET 2 AB4 5 THR G 38 ARG G 43 -1 N ALA G 41 O THR G 166
SHEET 3 AB4 5 6V1 G 47 GLN G 53 -1 O VAL G 51 N VAL G 40
SHEET 4 AB4 5 ILE G 215 THR G 221 -1 O GLY G 218 N ILE G 50
SHEET 5 AB4 5 ARG G 228 ILE G 229 -1 O ARG G 228 N VAL G 219
SHEET 1 AB5 5 LEU G 69 THR G 73 0
SHEET 2 AB5 5 ILE G 76 GLY G 82 -1 O ILE G 76 N ILE G 72
SHEET 3 AB5 5 CYS G 136 ASP G 144 -1 O ILE G 141 N GLY G 77
SHEET 4 AB5 5 GLY G 148 CYS G 154 -1 O TYR G 152 N LEU G 140
SHEET 5 AB5 5 TYR G 160 GLY G 162 -1 O 6V1 G 161 N LYS G 153
SHEET 1 AB6 5 TYR H 124 MET H 127 0
SHEET 2 AB6 5 ILE H 3 TYR H 8 -1 N ILE H 3 O MET H 127
SHEET 3 AB6 5 GLY H 11 ASP H 17 -1 O GLY H 15 N ALA H 4
SHEET 4 AB6 5 ILE H 173 SER H 179 -1 O CYS H 176 N LEU H 14
SHEET 5 AB6 5 LEU H 183 THR H 190 -1 O LEU H 186 N LEU H 175
SHEET 1 AB7 2 ALA H 20 GLU H 22 0
SHEET 2 AB7 2 VAL H 25 ASP H 28 -1 O VAL H 25 N GLU H 22
SHEET 1 AB8 5 ILE H 34 SER H 38 0
SHEET 2 AB8 5 ILE H 41 GLY H 47 -1 O CYS H 43 N HIS H 35
SHEET 3 AB8 5 ALA H 96 ASP H 104 -1 O ALA H 97 N ALA H 46
SHEET 4 AB8 5 GLY H 107 ILE H 113 -1 O TYR H 111 N LEU H 100
SHEET 5 AB8 5 THR H 119 LYS H 121 -1 O ASP H 120 N SER H 112
SHEET 1 AB9 6 VAL H 211 PRO H 218 0
SHEET 2 AB9 6 LYS I 193 LEU I 199 -1 O ILE I 194 N THR H 217
SHEET 3 AB9 6 VAL I 184 GLU I 190 -1 N ILE I 188 O THR I 195
SHEET 4 AB9 6 CYS I 18 ASP I 24 -1 N ILE I 21 O HIS I 187
SHEET 5 AB9 6 ALA I 9 GLY I 15 -1 N GLY I 15 O CYS I 18
SHEET 6 AB9 6 PHE I 135 GLY I 139 -1 O SER I 138 N VAL I 10
SHEET 1 AC1 2 PHE I 27 ILE I 29 0
SHEET 2 AC1 2 GLN I 32 THR I 35 -1 O VAL I 34 N PHE I 27
SHEET 1 AC2 5 ILE I 41 PRO I 43 0
SHEET 2 AC2 5 LEU I 48 GLY I 54 -1 O ILE I 50 N PHE I 42
SHEET 3 AC2 5 THR I 104 LEU I 111 -1 O ALA I 109 N TYR I 49
SHEET 4 AC2 5 PRO I 118 LEU I 123 -1 O PHE I 119 N GLY I 110
SHEET 5 AC2 5 PRO I 129 VAL I 131 -1 O MET I 130 N SER I 122
SHEET 1 AC3 5 PHE J 129 HIS J 132 0
SHEET 2 AC3 5 LEU J 4 GLY J 9 -1 N GLY J 6 O ALA J 130
SHEET 3 AC3 5 TYR J 12 ASP J 18 -1 O LEU J 14 N ILE J 7
SHEET 4 AC3 5 THR J 177 ASP J 184 -1 O ARG J 181 N VAL J 15
SHEET 5 AC3 5 GLY J 187 ASP J 190 -1 O HIS J 189 N ILE J 182
SHEET 1 AC4 5 PHE J 129 HIS J 132 0
SHEET 2 AC4 5 LEU J 4 GLY J 9 -1 N GLY J 6 O ALA J 130
SHEET 3 AC4 5 TYR J 12 ASP J 18 -1 O LEU J 14 N ILE J 7
SHEET 4 AC4 5 THR J 177 ASP J 184 -1 O ARG J 181 N VAL J 15
SHEET 5 AC4 5 ILE J 194 SER J 195 -1 O ILE J 194 N PHE J 178
SHEET 1 AC5 2 ALA J 21 SER J 23 0
SHEET 2 AC5 2 VAL J 26 LYS J 29 -1 O MET J 28 N ALA J 21
SHEET 1 AC6 5 MET J 35 SER J 39 0
SHEET 2 AC6 5 ILE J 42 GLY J 48 -1 O LEU J 44 N PHE J 36
SHEET 3 AC6 5 VAL J 100 ASP J 108 -1 O LEU J 103 N LEU J 45
SHEET 4 AC6 5 GLY J 112 MET J 118 -1 O ALA J 114 N GLY J 106
SHEET 5 AC6 5 LEU J 124 LYS J 126 -1 O ALA J 125 N TYR J 117
SHEET 1 AC7 5 THR K 125 VAL K 128 0
SHEET 2 AC7 5 THR K 3 PHE K 8 -1 N ALA K 5 O PHE K 126
SHEET 3 AC7 5 GLY K 11 ALA K 16 -1 O ALA K 15 N LEU K 4
SHEET 4 AC7 5 ALA K 173 ARG K 180 -1 O VAL K 179 N VAL K 12
SHEET 5 AC7 5 GLY K 183 ASN K 191 -1 O ASP K 190 N VAL K 174
SHEET 1 AC8 2 ALA K 20 ALA K 22 0
SHEET 2 AC8 2 TYR K 25 SER K 28 -1 O SER K 28 N ALA K 20
SHEET 1 AC9 4 VAL K 34 ASN K 38 0
SHEET 2 AC9 4 LEU K 41 THR K 44 -1 O GLY K 43 N ILE K 35
SHEET 3 AC9 4 MET K 97 ASP K 105 -1 O CYS K 102 N LEU K 42
SHEET 4 AC9 4 ALA K 46 GLY K 47 -1 N ALA K 46 O GLY K 98
SHEET 1 AD1 5 VAL K 34 ASN K 38 0
SHEET 2 AD1 5 LEU K 41 THR K 44 -1 O GLY K 43 N ILE K 35
SHEET 3 AD1 5 MET K 97 ASP K 105 -1 O CYS K 102 N LEU K 42
SHEET 4 AD1 5 GLY K 108 ASP K 115 -1 O GLY K 110 N GLY K 103
SHEET 5 AD1 5 ARG K 120 SER K 122 -1 O ILE K 121 N TYR K 113
SHEET 1 AD2 5 PHE L 135 GLY L 139 0
SHEET 2 AD2 5 THR L 11 ALA L 16 -1 N ILE L 12 O GLY L 138
SHEET 3 AD2 5 ALA L 21 ASP L 26 -1 O ALA L 24 N LEU L 13
SHEET 4 AD2 5 ALA L 192 THR L 199 -1 O VAL L 198 N ALA L 21
SHEET 5 AD2 5 GLY L 202 SER L 209 -1 O VAL L 208 N LEU L 193
SHEET 1 AD3 2 LEU L 29 GLU L 31 0
SHEET 2 AD3 2 SER L 34 THR L 37 -1 O THR L 37 N LEU L 29
SHEET 1 AD4 5 CYS L 43 THR L 47 0
SHEET 2 AD4 5 THR L 50 GLY L 56 -1 O ILE L 52 N TYR L 44
SHEET 3 AD4 5 VAL L 106 LEU L 113 -1 O GLY L 111 N VAL L 51
SHEET 4 AD4 5 GLY L 119 PHE L 124 -1 O TYR L 122 N ILE L 110
SHEET 5 AD4 5 TYR L 130 ASP L 133 -1 O ASP L 133 N VAL L 121
SHEET 1 AD5 5 LEU M 33 PHE M 36 0
SHEET 2 AD5 5 GLY M 28 TYR M 30 -1 N GLY M 28 O PHE M 36
SHEET 3 AD5 5 VAL M 6 GLY M 8 -1 N THR M 7 O SER M 29
SHEET 4 AD5 5 THR M 49 ASP M 56 -1 O GLY M 55 N GLY M 8
SHEET 5 AD5 5 ILE M 42 ASN M 46 -1 N MET M 43 O LEU M 51
SHEET 1 AD6 7 LEU M 33 PHE M 36 0
SHEET 2 AD6 7 GLY M 28 TYR M 30 -1 N GLY M 28 O PHE M 36
SHEET 3 AD6 7 VAL M 6 GLY M 8 -1 N THR M 7 O SER M 29
SHEET 4 AD6 7 THR M 49 ASP M 56 -1 O GLY M 55 N GLY M 8
SHEET 5 AD6 7 ASN M 108 ALA M 116 -1 O GLY M 113 N MET M 50
SHEET 6 AD6 7 GLU M 119 VAL M 125 -1 O VAL M 125 N MET M 110
SHEET 7 AD6 7 ALA M 131 GLU M 133 -1 O TYR M 132 N TYR M 124
SHEET 1 AD7 5 SER M 136 ALA M 138 0
SHEET 2 AD7 5 VAL M 11 PHE M 16 -1 N GLY M 13 O LEU M 137
SHEET 3 AD7 5 GLY M 19 ASP M 25 -1 O GLY M 19 N PHE M 16
SHEET 4 AD7 5 PHE M 187 THR M 193 -1 O ALA M 190 N ILE M 22
SHEET 5 AD7 5 GLY M 196 LEU M 203 -1 O GLU M 200 N ILE M 189
SHEET 1 AD8 5 PHE N 125 GLY N 128 0
SHEET 2 AD8 5 ILE N 3 PHE N 8 -1 N ALA N 5 O ALA N 126
SHEET 3 AD8 5 GLY N 11 ALA N 16 -1 O GLY N 15 N MET N 4
SHEET 4 AD8 5 ILE N 174 ALA N 180 -1 O ILE N 179 N VAL N 12
SHEET 5 AD8 5 GLY N 183 LEU N 189 -1 O GLN N 187 N LEU N 176
SHEET 1 AD9 2 THR N 20 THR N 22 0
SHEET 2 AD9 2 TYR N 25 ASN N 28 -1 O TYR N 25 N THR N 22
SHEET 1 AE1 5 LEU N 34 HIS N 38 0
SHEET 2 AE1 5 ILE N 41 GLY N 47 -1 O ILE N 41 N ILE N 37
SHEET 3 AE1 5 ALA N 96 ASP N 104 -1 O ALA N 101 N PHE N 42
SHEET 4 AE1 5 GLY N 108 VAL N 114 -1 O TYR N 112 N ILE N 100
SHEET 5 AE1 5 VAL N 121 ARG N 122 -1 O VAL N 121 N SER N 113
SHEET 1 AE2 5 ALA O 159 MET O 162 0
SHEET 2 AE2 5 SER O 34 LYS O 38 -1 N GLY O 36 O THR O 160
SHEET 3 AE2 5 VAL O 43 GLU O 48 -1 O ALA O 46 N VAL O 35
SHEET 4 AE2 5 ILE O 207 ASN O 213 -1 O GLY O 210 N LEU O 45
SHEET 5 AE2 5 GLY O 216 ARG O 219 -1 O ARG O 218 N ILE O 211
SHEET 1 AE3 5 GLU O 65 THR O 68 0
SHEET 2 AE3 5 ILE O 71 GLY O 77 -1 O ILE O 71 N ILE O 67
SHEET 3 AE3 5 VAL O 131 TRP O 138 -1 O LEU O 134 N VAL O 74
SHEET 4 AE3 5 PRO O 143 SER O 148 -1 O PHE O 146 N ILE O 135
SHEET 5 AE3 5 TYR O 154 ALA O 156 -1 O PHE O 155 N GLN O 147
SHEET 1 AE4 5 ALA P 161 ILE P 164 0
SHEET 2 AE4 5 CYS P 34 ALA P 39 -1 N GLY P 36 O THR P 162
SHEET 3 AE4 5 GLY P 42 GLU P 48 -1 O ALA P 46 N LEU P 35
SHEET 4 AE4 5 VAL P 211 GLU P 219 -1 O LEU P 216 N VAL P 43
SHEET 5 AE4 5 LYS P 222 VAL P 227 -1 O VAL P 224 N THR P 217
SHEET 1 AE5 5 ILE P 65 ASN P 69 0
SHEET 2 AE5 5 MET P 72 GLY P 78 -1 O CYS P 74 N TYR P 66
SHEET 3 AE5 5 VAL P 132 ASP P 140 -1 O ILE P 137 N ALA P 73
SHEET 4 AE5 5 GLY P 144 SER P 150 -1 O TYR P 148 N TYR P 136
SHEET 5 AE5 5 TYR P 156 GLY P 158 -1 O GLY P 157 N GLN P 149
SHEET 1 AE6 5 ALA Q 158 ILE Q 161 0
SHEET 2 AE6 5 ALA Q 32 ARG Q 36 -1 N GLY Q 34 O ASN Q 159
SHEET 3 AE6 5 ILE Q 40 VAL Q 45 -1 O GLY Q 44 N VAL Q 33
SHEET 4 AE6 5 GLU Q 207 ARG Q 212 -1 O ALA Q 209 N LEU Q 43
SHEET 5 AE6 5 SER Q 216 LEU Q 220 -1 O LYS Q 218 N VAL Q 210
SHEET 1 AE7 5 ILE Q 62 ASP Q 66 0
SHEET 2 AE7 5 VAL Q 69 GLY Q 75 -1 O VAL Q 69 N LEU Q 65
SHEET 3 AE7 5 ILE Q 129 PHE Q 136 -1 O LEU Q 132 N ALA Q 72
SHEET 4 AE7 5 PRO Q 142 THR Q 147 -1 O TYR Q 145 N ILE Q 133
SHEET 5 AE7 5 TYR Q 153 ALA Q 155 -1 O HIS Q 154 N GLN Q 146
SHEET 1 AE8 5 ALA R 167 ILE R 170 0
SHEET 2 AE8 5 ALA R 37 THR R 42 -1 N GLY R 39 O ARG R 168
SHEET 3 AE8 5 GLY R 45 GLU R 51 -1 O ALA R 49 N ILE R 38
SHEET 4 AE8 5 ILE R 215 GLN R 221 -1 O ALA R 218 N LEU R 48
SHEET 5 AE8 5 GLN R 224 MET R 228 -1 O HIS R 227 N THR R 219
SHEET 1 AE9 5 ILE R 67 ASP R 71 0
SHEET 2 AE9 5 ILE R 74 GLY R 80 -1 O ILE R 74 N ILE R 70
SHEET 3 AE9 5 VAL R 139 ASP R 147 -1 O GLY R 144 N GLY R 75
SHEET 4 AE9 5 GLY R 150 MET R 156 -1 O GLN R 152 N GLY R 145
SHEET 5 AE9 5 PHE R 162 GLN R 164 -1 O VAL R 163 N HIS R 155
SHEET 1 AF1 5 ALA S 158 ILE S 161 0
SHEET 2 AF1 5 THR S 35 LYS S 39 -1 N GLY S 37 O MET S 159
SHEET 3 AF1 5 HIS S 43 LEU S 49 -1 O VAL S 45 N LEU S 38
SHEET 4 AF1 5 VAL S 210 GLY S 216 -1 O SER S 211 N ALA S 48
SHEET 5 AF1 5 LEU S 219 TYR S 224 -1 O TYR S 224 N ILE S 212
SHEET 1 AF2 5 ILE S 63 ASP S 67 0
SHEET 2 AF2 5 ILE S 70 GLY S 76 -1 O ILE S 72 N LEU S 64
SHEET 3 AF2 5 VAL S 130 ASP S 138 -1 O LEU S 133 N SER S 73
SHEET 4 AF2 5 GLY S 141 THR S 147 -1 O PHE S 145 N ILE S 134
SHEET 5 AF2 5 TYR S 153 CYS S 156 -1 O CYS S 156 N ILE S 144
SHEET 1 AF3 5 GLY T 162 ILE T 165 0
SHEET 2 AF3 5 ALA T 36 CYS T 41 -1 N ALA T 36 O ILE T 165
SHEET 3 AF3 5 GLY T 44 LEU T 52 -1 O GLY T 44 N CYS T 41
SHEET 4 AF3 5 PHE T 209 GLY T 217 -1 O SER T 214 N PHE T 47
SHEET 5 AF3 5 GLU T 225 ILE T 226 -1 O GLU T 225 N TRP T 215
SHEET 1 AF4 5 LEU T 66 ASP T 70 0
SHEET 2 AF4 5 VAL T 73 GLY T 79 -1 O MET T 75 N PHE T 67
SHEET 3 AF4 5 CYS T 133 SER T 141 -1 O MET T 136 N ALA T 76
SHEET 4 AF4 5 GLY T 145 ILE T 151 -1 O ILE T 151 N PHE T 135
SHEET 5 AF4 5 SER T 157 GLY T 159 -1 O TYR T 158 N MET T 150
SHEET 1 AF5 5 ALA U 165 GLY U 169 0
SHEET 2 AF5 5 THR U 38 ARG U 43 -1 N ALA U 41 O THR U 166
SHEET 3 AF5 5 6V1 U 47 GLN U 53 -1 O VAL U 51 N VAL U 40
SHEET 4 AF5 5 ILE U 215 THR U 221 -1 O GLY U 218 N ILE U 50
SHEET 5 AF5 5 ARG U 228 ILE U 229 -1 O ARG U 228 N VAL U 219
SHEET 1 AF6 5 LEU U 69 THR U 73 0
SHEET 2 AF6 5 ILE U 76 GLY U 82 -1 O ILE U 76 N ILE U 72
SHEET 3 AF6 5 CYS U 136 ASP U 144 -1 O YCM U 137 N THR U 81
SHEET 4 AF6 5 GLY U 148 CYS U 154 -1 O TYR U 152 N LEU U 140
SHEET 5 AF6 5 TYR U 160 GLY U 162 -1 O 6V1 U 161 N LYS U 153
SHEET 1 AF7 5 TYR V 124 MET V 127 0
SHEET 2 AF7 5 ILE V 3 TYR V 8 -1 N ILE V 3 O MET V 127
SHEET 3 AF7 5 GLY V 11 ASP V 17 -1 O GLY V 15 N ALA V 4
SHEET 4 AF7 5 ILE V 173 SER V 179 -1 O CYS V 176 N LEU V 14
SHEET 5 AF7 5 LEU V 183 THR V 190 -1 O LEU V 186 N LEU V 175
SHEET 1 AF8 2 ALA V 20 GLU V 22 0
SHEET 2 AF8 2 VAL V 25 ASP V 28 -1 O ALA V 27 N ALA V 20
SHEET 1 AF9 5 ILE V 34 SER V 38 0
SHEET 2 AF9 5 ILE V 41 GLY V 47 -1 O CYS V 43 N HIS V 35
SHEET 3 AF9 5 ALA V 96 ASP V 104 -1 O ALA V 97 N ALA V 46
SHEET 4 AF9 5 GLY V 107 ILE V 113 -1 O HIS V 109 N GLY V 102
SHEET 5 AF9 5 THR V 119 LYS V 121 -1 O ASP V 120 N SER V 112
SHEET 1 AG1 6 VAL V 211 PRO V 218 0
SHEET 2 AG1 6 LYS W 193 LEU W 199 -1 O THR W 196 N LYS V 215
SHEET 3 AG1 6 VAL W 184 GLU W 190 -1 N ILE W 188 O THR W 195
SHEET 4 AG1 6 CYS W 18 ASP W 24 -1 N ILE W 21 O HIS W 187
SHEET 5 AG1 6 ALA W 9 GLY W 15 -1 N MET W 13 O ALA W 20
SHEET 6 AG1 6 PHE W 135 GLY W 139 -1 O SER W 138 N VAL W 10
SHEET 1 AG2 2 PHE W 27 ILE W 29 0
SHEET 2 AG2 2 GLN W 32 THR W 35 -1 O VAL W 34 N PHE W 27
SHEET 1 AG3 5 ILE W 41 PRO W 43 0
SHEET 2 AG3 5 LEU W 48 GLY W 54 -1 O ILE W 50 N PHE W 42
SHEET 3 AG3 5 THR W 104 LEU W 111 -1 O ALA W 109 N TYR W 49
SHEET 4 AG3 5 PRO W 118 LEU W 123 -1 O PHE W 119 N GLY W 110
SHEET 5 AG3 5 PRO W 129 VAL W 131 -1 O MET W 130 N SER W 122
SHEET 1 AG4 5 PHE X 129 HIS X 132 0
SHEET 2 AG4 5 LEU X 4 GLY X 9 -1 N GLY X 6 O ALA X 130
SHEET 3 AG4 5 TYR X 12 ASP X 18 -1 O LEU X 14 N ILE X 7
SHEET 4 AG4 5 THR X 177 ASP X 184 -1 O SER X 179 N SER X 17
SHEET 5 AG4 5 GLY X 187 ASP X 190 -1 O HIS X 189 N ILE X 182
SHEET 1 AG5 5 PHE X 129 HIS X 132 0
SHEET 2 AG5 5 LEU X 4 GLY X 9 -1 N GLY X 6 O ALA X 130
SHEET 3 AG5 5 TYR X 12 ASP X 18 -1 O LEU X 14 N ILE X 7
SHEET 4 AG5 5 THR X 177 ASP X 184 -1 O SER X 179 N SER X 17
SHEET 5 AG5 5 ILE X 194 SER X 195 -1 O ILE X 194 N PHE X 178
SHEET 1 AG6 2 ALA X 21 SER X 23 0
SHEET 2 AG6 2 VAL X 26 LYS X 29 -1 O MET X 28 N ALA X 21
SHEET 1 AG7 5 MET X 35 SER X 39 0
SHEET 2 AG7 5 ILE X 42 GLY X 48 -1 O LEU X 44 N PHE X 36
SHEET 3 AG7 5 VAL X 100 ASP X 108 -1 O LEU X 103 N LEU X 45
SHEET 4 AG7 5 GLY X 112 MET X 118 -1 O ALA X 114 N GLY X 106
SHEET 5 AG7 5 LEU X 124 LYS X 126 -1 O ALA X 125 N TYR X 117
SHEET 1 AG8 5 THR Y 125 VAL Y 128 0
SHEET 2 AG8 5 THR Y 3 PHE Y 8 -1 N ALA Y 5 O PHE Y 126
SHEET 3 AG8 5 GLY Y 11 ALA Y 16 -1 O ALA Y 15 N LEU Y 4
SHEET 4 AG8 5 ALA Y 173 ARG Y 180 -1 O VAL Y 179 N VAL Y 12
SHEET 5 AG8 5 GLY Y 183 ASN Y 191 -1 O ASP Y 190 N VAL Y 174
SHEET 1 AG9 2 ALA Y 20 ALA Y 22 0
SHEET 2 AG9 2 TYR Y 25 SER Y 28 -1 O SER Y 28 N ALA Y 20
SHEET 1 AH1 4 VAL Y 34 ASN Y 38 0
SHEET 2 AH1 4 LEU Y 41 THR Y 44 -1 O GLY Y 43 N ILE Y 35
SHEET 3 AH1 4 MET Y 97 ASP Y 105 -1 O CYS Y 102 N LEU Y 42
SHEET 4 AH1 4 ALA Y 46 GLY Y 47 -1 N ALA Y 46 O GLY Y 98
SHEET 1 AH2 5 VAL Y 34 ASN Y 38 0
SHEET 2 AH2 5 LEU Y 41 THR Y 44 -1 O GLY Y 43 N ILE Y 35
SHEET 3 AH2 5 MET Y 97 ASP Y 105 -1 O CYS Y 102 N LEU Y 42
SHEET 4 AH2 5 GLY Y 108 ASP Y 115 -1 O GLY Y 110 N GLY Y 103
SHEET 5 AH2 5 ARG Y 120 SER Y 122 -1 O ILE Y 121 N TYR Y 113
SHEET 1 AH3 5 PHE Z 135 GLY Z 139 0
SHEET 2 AH3 5 THR Z 11 ALA Z 16 -1 N ILE Z 12 O GLY Z 138
SHEET 3 AH3 5 ALA Z 21 ASP Z 26 -1 O ALA Z 24 N LEU Z 13
SHEET 4 AH3 5 ALA Z 192 THR Z 199 -1 O VAL Z 198 N ALA Z 21
SHEET 5 AH3 5 GLY Z 202 SER Z 209 -1 O VAL Z 208 N LEU Z 193
SHEET 1 AH4 2 LEU Z 29 GLU Z 31 0
SHEET 2 AH4 2 SER Z 34 THR Z 37 -1 O THR Z 37 N LEU Z 29
SHEET 1 AH5 5 CYS Z 43 THR Z 47 0
SHEET 2 AH5 5 THR Z 50 GLY Z 56 -1 O ILE Z 52 N TYR Z 44
SHEET 3 AH5 5 VAL Z 106 LEU Z 113 -1 O ILE Z 109 N GLY Z 53
SHEET 4 AH5 5 GLY Z 119 PHE Z 124 -1 O TYR Z 122 N ILE Z 110
SHEET 5 AH5 5 TYR Z 130 ASP Z 133 -1 O ASP Z 133 N VAL Z 121
SHEET 1 AH6 5 LEU a 33 PHE a 36 0
SHEET 2 AH6 5 GLY a 28 TYR a 30 -1 N GLY a 28 O PHE a 36
SHEET 3 AH6 5 VAL a 6 GLY a 8 -1 N THR a 7 O SER a 29
SHEET 4 AH6 5 THR a 49 ASP a 56 -1 O GLY a 55 N GLY a 8
SHEET 5 AH6 5 ILE a 42 ASN a 46 -1 N MET a 43 O LEU a 51
SHEET 1 AH7 7 LEU a 33 PHE a 36 0
SHEET 2 AH7 7 GLY a 28 TYR a 30 -1 N GLY a 28 O PHE a 36
SHEET 3 AH7 7 VAL a 6 GLY a 8 -1 N THR a 7 O SER a 29
SHEET 4 AH7 7 THR a 49 ASP a 56 -1 O GLY a 55 N GLY a 8
SHEET 5 AH7 7 ASN a 108 ALA a 116 -1 O GLY a 113 N MET a 50
SHEET 6 AH7 7 GLU a 119 VAL a 125 -1 O VAL a 125 N MET a 110
SHEET 7 AH7 7 ALA a 131 GLU a 133 -1 O TYR a 132 N TYR a 124
SHEET 1 AH8 5 SER a 136 ALA a 138 0
SHEET 2 AH8 5 VAL a 11 PHE a 16 -1 N GLY a 13 O LEU a 137
SHEET 3 AH8 5 GLY a 19 ASP a 25 -1 O GLY a 19 N PHE a 16
SHEET 4 AH8 5 PHE a 187 THR a 193 -1 O ALA a 190 N ILE a 22
SHEET 5 AH8 5 GLY a 196 LEU a 203 -1 O GLU a 200 N ILE a 189
SHEET 1 AH9 5 PHE b 125 GLY b 128 0
SHEET 2 AH9 5 ILE b 3 PHE b 8 -1 N ALA b 5 O ALA b 126
SHEET 3 AH9 5 GLY b 11 ALA b 16 -1 O GLY b 15 N MET b 4
SHEET 4 AH9 5 ILE b 174 ALA b 180 -1 O ILE b 179 N VAL b 12
SHEET 5 AH9 5 GLY b 183 LEU b 189 -1 O GLN b 187 N LEU b 176
SHEET 1 AI1 2 THR b 20 THR b 22 0
SHEET 2 AI1 2 TYR b 25 ASN b 28 -1 O ASN b 28 N THR b 20
SHEET 1 AI2 5 LEU b 34 HIS b 38 0
SHEET 2 AI2 5 ILE b 41 GLY b 47 -1 O ILE b 41 N ILE b 37
SHEET 3 AI2 5 ALA b 96 ASP b 104 -1 O ALA b 101 N PHE b 42
SHEET 4 AI2 5 GLY b 108 VAL b 114 -1 O TYR b 112 N ILE b 100
SHEET 5 AI2 5 VAL b 121 ARG b 122 -1 O VAL b 121 N SER b 113
LINK C ILE C 62 N YCM C 63 1555 1555 1.33
LINK C YCM C 63 N ALA C 64 1555 1555 1.34
LINK C THR E 147 N 6V1 E 148 1555 1555 1.33
LINK C 6V1 E 148 N PRO E 149 1555 1555 1.34
LINK C ASP G 46 N 6V1 G 47 1555 1555 1.33
LINK C 6V1 G 47 N ALA G 48 1555 1555 1.32
LINK C CYS G 136 N YCM G 137 1555 1555 1.31
LINK C YCM G 137 N MET G 138 1555 1555 1.32
LINK C TYR G 160 N 6V1 G 161 1555 1555 1.32
LINK C 6V1 G 161 N GLY G 162 1555 1555 1.32
LINK C ASP J 90 N 6V1 J 91 1555 1555 1.32
LINK C 6V1 J 91 N LEU J 92 1555 1555 1.33
LINK N THR K 1 C23 6VA c 4 1555 1555 1.53
LINK OG1 THR K 1 C 6VA c 4 1555 1555 1.42
LINK N THR N 1 C23 6VA d 4 1555 1555 1.50
LINK OG1 THR N 1 C 6VA d 4 1555 1555 1.44
LINK C ILE Q 62 N YCM Q 63 1555 1555 1.34
LINK C YCM Q 63 N ALA Q 64 1555 1555 1.33
LINK C THR S 147 N 6V1 S 148 1555 1555 1.34
LINK C 6V1 S 148 N PRO S 149 1555 1555 1.35
LINK C ASP U 46 N 6V1 U 47 1555 1555 1.33
LINK C 6V1 U 47 N ALA U 48 1555 1555 1.33
LINK C CYS U 136 N YCM U 137 1555 1555 1.32
LINK C YCM U 137 N MET U 138 1555 1555 1.33
LINK C TYR U 160 N 6V1 U 161 1555 1555 1.32
LINK C 6V1 U 161 N GLY U 162 1555 1555 1.34
LINK C ASP X 90 N 6V1 X 91 1555 1555 1.32
LINK C 6V1 X 91 N LEU X 92 1555 1555 1.33
LINK N THR Y 1 C23 6VA e 4 1555 1555 1.53
LINK OG1 THR Y 1 C 6VA e 4 1555 1555 1.39
LINK N THR b 1 C23 6VA f 4 1555 1555 1.51
LINK OG1 THR b 1 C 6VA f 4 1555 1555 1.44
LINK C 6V9 c 1 N OAS c 2 1555 1555 1.32
LINK C OAS c 2 N OAS c 3 1555 1555 1.32
LINK C OAS c 3 N 6VA c 4 1555 1555 1.32
LINK C 6V9 d 1 N OAS d 2 1555 1555 1.33
LINK C OAS d 2 N OAS d 3 1555 1555 1.34
LINK C OAS d 3 N 6VA d 4 1555 1555 1.35
LINK C 6V9 e 1 N OAS e 2 1555 1555 1.32
LINK C OAS e 2 N OAS e 3 1555 1555 1.35
LINK C OAS e 3 N 6VA e 4 1555 1555 1.34
LINK C 6V9 f 1 N OAS f 2 1555 1555 1.33
LINK C OAS f 2 N OAS f 3 1555 1555 1.33
LINK C OAS f 3 N 6VA f 4 1555 1555 1.33
LINK OG1 THR G 14 K K G 301 1555 1555 2.75
LINK O TYR G 125 K K G 301 1555 1555 2.53
LINK O ASN G 128 K K G 301 1555 1555 2.56
LINK O MET G 131 K K G 301 1555 1555 2.52
LINK K K G 301 O HOH G 440 1555 1555 2.60
LINK OE1 GLN H 91 MG MG H 301 1555 1555 2.38
LINK O ILE H 163 MG MG H 302 1555 1555 2.19
LINK O ASP H 166 MG MG H 302 1555 1555 2.20
LINK O SER H 169 MG MG H 302 1555 1555 2.19
LINK MG MG H 301 O HOH H 454 1555 1555 2.18
LINK MG MG H 301 O HOH H 528 1555 1555 2.16
LINK MG MG H 301 O HOH N 412 1555 1555 2.20
LINK MG MG H 301 O HOH N 434 1555 1555 2.20
LINK MG MG H 301 O HOH N 435 1555 1555 2.19
LINK MG MG H 302 O ASP Z 213 1555 1555 2.21
LINK MG MG H 302 O HOH Z 504 1555 1555 2.68
LINK O VAL I 174 MG MG I 301 1555 1555 2.18
LINK O ASP I 177 MG MG I 301 1555 1555 2.21
LINK O SER I 180 MG MG I 301 1555 1555 2.20
LINK O ASP I 204 MG MG I 303 1555 1555 2.16
LINK MG MG I 301 O HOH I 405 1555 1555 2.61
LINK MG MG I 301 O HOH I 462 1555 1555 2.31
LINK MG MG I 303 O HOH I 502 1555 1555 2.67
LINK MG MG I 303 O THR Y 164 1555 1555 2.21
LINK MG MG I 303 O ASP Y 167 1555 1555 2.18
LINK MG MG I 303 O SER Y 170 1555 1555 2.23
LINK MG MG J 301 O HOH J 404 1555 1555 2.19
LINK MG MG J 301 O HOH J 422 1555 1555 2.18
LINK MG MG J 301 O HOH J 448 1555 1555 2.19
LINK MG MG J 301 O HOH J 516 1555 1555 2.16
LINK MG MG J 301 O HOH J 529 1555 1555 2.18
LINK MG MG J 301 O HOH K 485 1555 1555 2.17
LINK O THR K 164 MG MG K 301 1555 1555 2.22
LINK O ASP K 167 MG MG K 301 1555 1555 2.19
LINK O SER K 170 MG MG K 301 1555 1555 2.22
LINK MG MG K 301 O HOH K 451 1555 1555 2.78
LINK MG MG K 301 O ASP W 204 1555 1555 2.18
LINK O ALA L 183 K K L 302 1555 1555 2.58
LINK O ASP L 186 K K L 302 1555 1555 2.63
LINK O THR L 189 K K L 302 1555 1555 2.62
LINK O ASP L 213 MG MG L 303 1555 1555 2.21
LINK K K L 302 O HOH L 436 1555 1555 2.55
LINK K K L 302 O HOH L 475 1555 1555 3.34
LINK MG MG L 303 O ILE V 163 1555 1555 2.20
LINK MG MG L 303 O ASP V 166 1555 1555 2.20
LINK MG MG L 303 O SER V 169 1555 1555 2.20
LINK MG MG L 303 O HOH V 467 1555 1555 2.76
LINK O MET N 164 K K N 302 1555 1555 2.54
LINK O ASP N 167 K K N 302 1555 1555 2.61
LINK O SER N 170 K K N 302 1555 1555 2.57
LINK K K N 302 O HOH N 480 1555 1555 3.31
LINK K K N 302 O HOH N 516 1555 1555 2.56
LINK K K N 302 O HOH N 540 1555 1555 2.35
LINK OG1 THR U 14 K K U 302 1555 1555 2.76
LINK O TYR U 125 K K U 302 1555 1555 2.55
LINK O ASN U 128 K K U 302 1555 1555 2.55
LINK O MET U 131 K K U 302 1555 1555 2.52
LINK K K U 302 O HOH U 442 1555 1555 2.82
LINK OE1 GLN V 91 MG MG V 301 1555 1555 2.26
LINK MG MG V 301 O HOH V 404 1555 1555 2.18
LINK MG MG V 301 O HOH V 482 1555 1555 2.16
LINK MG MG V 301 O HOH b 409 1555 1555 2.18
LINK MG MG V 301 O HOH b 423 1555 1555 2.20
LINK MG MG V 301 O HOH b 438 1555 1555 2.20
LINK O VAL W 174 MG MG W 301 1555 1555 2.19
LINK O ASP W 177 MG MG W 301 1555 1555 2.19
LINK O SER W 180 MG MG W 301 1555 1555 2.18
LINK MG MG W 301 O HOH W 451 1555 1555 2.08
LINK MG MG W 301 O HOH W 464 1555 1555 2.27
LINK MG MG X 301 O HOH X 405 1555 1555 2.17
LINK MG MG X 301 O HOH X 406 1555 1555 2.18
LINK MG MG X 301 O HOH X 447 1555 1555 2.18
LINK MG MG X 301 O HOH X 509 1555 1555 2.17
LINK MG MG X 301 O HOH X 524 1555 1555 2.18
LINK MG MG X 301 O HOH Y 515 1555 1555 2.19
LINK O ALA Z 183 K K Z 301 1555 1555 2.57
LINK O ASP Z 186 K K Z 301 1555 1555 2.63
LINK O THR Z 189 K K Z 301 1555 1555 2.59
LINK K K Z 301 O HOH Z 429 1555 1555 2.44
LINK K K Z 301 O HOH Z 445 1555 1555 3.34
LINK O MET b 164 K K b 301 1555 1555 2.55
LINK O ASP b 167 K K b 301 1555 1555 2.61
LINK O SER b 170 K K b 301 1555 1555 2.59
LINK K K b 301 O HOH b 461 1555 1555 3.26
LINK K K b 301 O HOH b 478 1555 1555 2.53
LINK K K b 301 O HOH b 497 1555 1555 2.46
CISPEP 1 VAL B 203 SER B 204 0 -6.10
CISPEP 2 LYS C 47 LYS C 48 0 0.29
CISPEP 3 GLY C 202 GLY C 203 0 -1.81
CISPEP 4 GLY C 203 LYS C 204 0 -7.95
CISPEP 5 ARG H 187 PRO H 188 0 -4.28
CISPEP 6 ARG H 187 PRO H 188 0 -4.28
CISPEP 7 GLY M 201 PRO M 202 0 -8.12
CISPEP 8 ILE P 52 HIS P 53 0 -18.42
CISPEP 9 LEU Q 220 ASN Q 221 0 29.01
CISPEP 10 GLU S 234 GLY S 235 0 -10.83
CISPEP 11 GLU S 238 ARG S 239 0 -21.59
CISPEP 12 GLY T 6 TYR T 7 0 -21.14
CISPEP 13 ARG V 187 PRO V 188 0 -6.78
CISPEP 14 GLY a 201 PRO a 202 0 -1.17
CISPEP 15 GLY a 201 PRO a 202 0 3.76
SITE 1 AC1 5 THR G 14 TYR G 125 ASN G 128 MET G 131
SITE 2 AC1 5 HOH G 440
SITE 1 AC2 7 GLN H 91 HOH H 454 HOH H 528 ASP N 51
SITE 2 AC2 7 HOH N 412 HOH N 434 HOH N 435
SITE 1 AC3 5 ILE H 163 ASP H 166 SER H 169 ASP Z 213
SITE 2 AC3 5 HOH Z 504
SITE 1 AC4 3 TYR H 90 TYR I 95 GLU I 96
SITE 1 AC5 5 VAL I 174 ASP I 177 SER I 180 HOH I 405
SITE 2 AC5 5 HOH I 462
SITE 1 AC6 4 GLU I 96 LYS I 97 HOH I 504 ASP J 90
SITE 1 AC7 5 ASP I 204 HOH I 502 THR Y 164 ASP Y 167
SITE 2 AC7 5 SER Y 170
SITE 1 AC8 6 HOH J 404 HOH J 422 HOH J 448 HOH J 516
SITE 2 AC8 6 HOH J 529 HOH K 485
SITE 1 AC9 5 THR K 164 ASP K 167 SER K 170 HOH K 451
SITE 2 AC9 5 ASP W 204
SITE 1 AD1 3 HOH K 491 SER L 98 PHE L 101
SITE 1 AD2 1 PHE L 33
SITE 1 AD3 4 ALA L 183 ASP L 186 THR L 189 HOH L 436
SITE 1 AD4 5 ASP L 213 ILE V 163 ASP V 166 SER V 169
SITE 2 AD4 5 HOH V 467
SITE 1 AD5 4 TYR G 103 GLN H 91 TYR N 90 HOH N 441
SITE 1 AD6 5 MET N 164 ASP N 167 SER N 170 HOH N 516
SITE 2 AD6 5 HOH N 540
SITE 1 AD7 4 TYR U 103 HOH U 493 GLN V 91 LEU b 94
SITE 1 AD8 5 THR U 14 TYR U 125 ASN U 128 MET U 131
SITE 2 AD8 5 HOH U 442
SITE 1 AD9 7 GLN V 91 HOH V 404 HOH V 482 ASP b 51
SITE 2 AD9 7 HOH b 409 HOH b 423 HOH b 438
SITE 1 AE1 5 VAL W 174 ASP W 177 SER W 180 HOH W 451
SITE 2 AE1 5 HOH W 464
SITE 1 AE2 4 GLU W 96 LYS W 97 HOH W 443 HOH W 459
SITE 1 AE3 6 HOH X 405 HOH X 406 HOH X 447 HOH X 509
SITE 2 AE3 6 HOH X 524 HOH Y 515
SITE 1 AE4 5 HOH Y 440 HOH Y 466 TYR Z 97 SER Z 98
SITE 2 AE4 5 PHE Z 101
SITE 1 AE5 4 ALA Z 183 ASP Z 186 THR Z 189 HOH Z 429
SITE 1 AE6 3 THR N 22 HOH a 483 HOH a 501
SITE 1 AE7 5 MET b 164 ASP b 167 SER b 170 HOH b 478
SITE 2 AE7 5 HOH b 497
SITE 1 AE8 4 GLY K 47 GLY K 129 SER K 130 6VA c 4
SITE 1 AE9 4 THR N 1 GLY N 129 SER N 130 6VA d 4
SITE 1 AF1 3 GLY Y 129 SER Y 130 6VA e 4
SITE 1 AF2 4 THR b 1 GLY b 129 SER b 130 6VA f 4
SITE 1 AF3 16 THR K 1 ARG K 19 ALA K 20 THR K 21
SITE 2 AF3 16 VAL K 31 MET K 45 ALA K 46 GLY K 47
SITE 3 AF3 16 ALA K 49 SER K 130 TYR K 169 ASP L 125
SITE 4 AF3 16 VAL L 127 HOH L 409 ACT c 101 HOH c 201
SITE 1 AF4 11 THR K 1 ARG K 19 VAL K 31 MET K 45
SITE 2 AF4 11 ALA K 46 GLY K 47 ALA K 49 SER K 130
SITE 3 AF4 11 TYR K 169 OAS c 3 ACT c 101
SITE 1 AF5 17 TYR H 114 HIS H 116 THR N 1 ARG N 19
SITE 2 AF5 17 THR N 20 THR N 21 THR N 22 THR N 31
SITE 3 AF5 17 ARG N 45 SER N 46 GLY N 47 ALA N 49
SITE 4 AF5 17 SER N 130 SER N 169 HOH N 428 ACT d 101
SITE 5 AF5 17 HOH d 501
SITE 1 AF6 13 THR N 1 ARG N 19 THR N 20 THR N 31
SITE 2 AF6 13 ARG N 45 SER N 46 GLY N 47 ALA N 49
SITE 3 AF6 13 SER N 130 SER N 169 HOH N 428 OAS d 3
SITE 4 AF6 13 ACT d 101
SITE 1 AF7 16 THR Y 1 ARG Y 19 ALA Y 20 THR Y 21
SITE 2 AF7 16 VAL Y 31 MET Y 45 ALA Y 46 GLY Y 47
SITE 3 AF7 16 ALA Y 49 SER Y 130 TYR Y 169 ASP Z 125
SITE 4 AF7 16 VAL Z 127 HOH Z 415 ACT e 101 HOH e 201
SITE 1 AF8 11 THR Y 1 ARG Y 19 VAL Y 31 MET Y 45
SITE 2 AF8 11 ALA Y 46 GLY Y 47 ALA Y 49 SER Y 130
SITE 3 AF8 11 TYR Y 169 OAS e 3 ACT e 101
SITE 1 AF9 17 TYR V 114 HIS V 116 THR b 1 ARG b 19
SITE 2 AF9 17 THR b 20 THR b 21 THR b 22 THR b 31
SITE 3 AF9 17 ARG b 45 SER b 46 GLY b 47 ALA b 49
SITE 4 AF9 17 SER b 130 SER b 169 HOH b 408 ACT f 101
SITE 5 AF9 17 HOH f 201
SITE 1 AG1 13 THR b 1 ARG b 19 THR b 20 THR b 31
SITE 2 AG1 13 ARG b 45 SER b 46 GLY b 47 ALA b 49
SITE 3 AG1 13 SER b 130 SER b 169 HOH b 408 OAS f 3
SITE 4 AG1 13 ACT f 101
CRYST1 113.860 203.230 315.220 90.00 90.00 90.00 P 21 21 21 16
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.008783 0.000000 0.000000 0.00000
SCALE2 0.000000 0.004921 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003172 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
