HEADER CHAPERONE 29-MAR-04 1SVT
TITLE CRYSTAL STRUCTURE OF GROEL14-GROES7-(ADP-ALFX)7
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GROEL PROTEIN;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H, I, J, K, L, M, N;
COMPND 4 SYNONYM: PROTEIN CPN60, 60 KDA CHAPERONIN;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: GROES PROTEIN;
COMPND 8 CHAIN: O, P, Q, R, S, T, U;
COMPND 9 SYNONYM: PROTEIN CPN10, 10 KDA CHAPERONIN;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: GROL, GROEL, MOPA, B4143, C5227, Z5748, ECS5124, SF4297,
SOURCE 5 S4564;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: DH5 ALPHA;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 11 ORGANISM_TAXID: 562;
SOURCE 12 GENE: GROS, GROES, MOPB, B4142, C5226, Z5747, ECS5123, SF4296,
SOURCE 13 S4563;
SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 16 EXPRESSION_SYSTEM_STRAIN: DH5 ALPHA
KEYWDS CHAPERONIN, PROTEIN FOLDING, CHAPERONE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.CHAUDHRY,A.L.HORWICH,A.T.BRUNGER,P.D.ADAMS
REVDAT 3 13-JUL-11 1SVT 1 VERSN
REVDAT 2 24-FEB-09 1SVT 1 VERSN
REVDAT 1 01-MAR-05 1SVT 0
JRNL AUTH C.CHAUDHRY,A.L.HORWICH,A.T.BRUNGER,P.D.ADAMS
JRNL TITL EXPLORING THE STRUCTURAL DYNAMICS OF THE E.COLI CHAPERONIN
JRNL TITL 2 GROEL USING TRANSLATION-LIBRATION-SCREW CRYSTALLOGRAPHIC
JRNL TITL 3 REFINEMENT OF INTERMEDIATE STATES.
JRNL REF J.MOL.BIOL. V. 342 229 2004
JRNL REFN ISSN 0022-2836
JRNL PMID 15313620
JRNL DOI 10.1016/J.JMB.2004.07.015
REMARK 2
REMARK 2 RESOLUTION. 2.81 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.81
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.39
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 231127
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : 0.248
REMARK 3 R VALUE (WORKING SET) : 0.247
REMARK 3 FREE R VALUE : 0.274
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.983
REMARK 3 FREE R VALUE TEST SET COUNT : 4675
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) : 2.81
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.88
REMARK 3 REFLECTION IN BIN (WORKING SET) : 8725
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.4270
REMARK 3 BIN FREE R VALUE SET COUNT : 161
REMARK 3 BIN FREE R VALUE : 0.5180
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 59073
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 231
REMARK 3 SOLVENT ATOMS : 194
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 2.54
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -4.33100
REMARK 3 B22 (A**2) : -3.72500
REMARK 3 B33 (A**2) : 8.05600
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): 1.983
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.393
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.405
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 24.496
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.896
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.875
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 59717 ; 0.027 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 80633 ; 2.039 ; 1.989
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 7994 ; 6.242 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 9800 ; 0.123 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 43302 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 29 ; 0.264 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 54 ; 0.324 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 1772 ; 0.173 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 39508 ; 0.218 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 63266 ; 0.386 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 20209 ; 0.840 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 17367 ; 1.235 ; 4.500
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 7
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B C D E F G
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 3
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 2 A 135 1
REMARK 3 1 B 2 B 135 1
REMARK 3 1 C 2 C 135 1
REMARK 3 1 D 2 D 135 1
REMARK 3 1 E 2 E 135 1
REMARK 3 1 F 2 F 135 1
REMARK 3 1 G 2 G 135 1
REMARK 3 2 A 410 A 525 1
REMARK 3 2 B 410 B 525 1
REMARK 3 2 C 410 C 525 1
REMARK 3 2 D 410 D 525 1
REMARK 3 2 E 410 E 525 1
REMARK 3 2 F 410 F 525 1
REMARK 3 2 G 410 G 525 1
REMARK 3 3 A 600 A 603 1
REMARK 3 3 B 600 B 603 1
REMARK 3 3 C 600 C 603 1
REMARK 3 3 D 600 D 603 1
REMARK 3 3 E 600 E 603 1
REMARK 3 3 F 600 F 603 1
REMARK 3 3 G 600 G 603 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 1843 ; 0.094 ; 0.050
REMARK 3 TIGHT POSITIONAL 1 B (A): 1843 ; 0.083 ; 0.050
REMARK 3 TIGHT POSITIONAL 1 C (A): 1843 ; 0.097 ; 0.050
REMARK 3 TIGHT POSITIONAL 1 D (A): 1843 ; 0.091 ; 0.050
REMARK 3 TIGHT POSITIONAL 1 E (A): 1843 ; 0.077 ; 0.050
REMARK 3 TIGHT POSITIONAL 1 F (A): 1843 ; 0.078 ; 0.050
REMARK 3 TIGHT POSITIONAL 1 G (A): 1843 ; 0.095 ; 0.050
REMARK 3 TIGHT THERMAL 1 A (A**2): 1843 ; 0.148 ; 0.500
REMARK 3 TIGHT THERMAL 1 B (A**2): 1843 ; 0.132 ; 0.500
REMARK 3 TIGHT THERMAL 1 C (A**2): 1843 ; 0.161 ; 0.500
REMARK 3 TIGHT THERMAL 1 D (A**2): 1843 ; 0.147 ; 0.500
REMARK 3 TIGHT THERMAL 1 E (A**2): 1843 ; 0.120 ; 0.500
REMARK 3 TIGHT THERMAL 1 F (A**2): 1843 ; 0.122 ; 0.500
REMARK 3 TIGHT THERMAL 1 G (A**2): 1843 ; 0.144 ; 0.500
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : A B C D E F G
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 2
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 136 A 190 1
REMARK 3 1 B 136 B 190 1
REMARK 3 1 C 136 C 190 1
REMARK 3 1 D 136 D 190 1
REMARK 3 1 E 136 E 190 1
REMARK 3 1 F 136 F 190 1
REMARK 3 1 G 136 G 190 1
REMARK 3 2 A 375 A 409 1
REMARK 3 2 B 375 B 409 1
REMARK 3 2 C 375 C 409 1
REMARK 3 2 D 375 D 409 1
REMARK 3 2 E 375 E 409 1
REMARK 3 2 F 375 F 409 1
REMARK 3 2 G 375 G 409 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 2 A (A): 647 ; 0.076 ; 0.050
REMARK 3 TIGHT POSITIONAL 2 B (A): 647 ; 0.068 ; 0.050
REMARK 3 TIGHT POSITIONAL 2 C (A): 647 ; 0.072 ; 0.050
REMARK 3 TIGHT POSITIONAL 2 D (A): 647 ; 0.074 ; 0.050
REMARK 3 TIGHT POSITIONAL 2 E (A): 647 ; 0.063 ; 0.050
REMARK 3 TIGHT POSITIONAL 2 F (A): 647 ; 0.059 ; 0.050
REMARK 3 TIGHT POSITIONAL 2 G (A): 647 ; 0.070 ; 0.050
REMARK 3 TIGHT THERMAL 2 A (A**2): 647 ; 0.109 ; 0.500
REMARK 3 TIGHT THERMAL 2 B (A**2): 647 ; 0.085 ; 0.500
REMARK 3 TIGHT THERMAL 2 C (A**2): 647 ; 0.096 ; 0.500
REMARK 3 TIGHT THERMAL 2 D (A**2): 647 ; 0.096 ; 0.500
REMARK 3 TIGHT THERMAL 2 E (A**2): 647 ; 0.083 ; 0.500
REMARK 3 TIGHT THERMAL 2 F (A**2): 647 ; 0.086 ; 0.500
REMARK 3 TIGHT THERMAL 2 G (A**2): 647 ; 0.092 ; 0.500
REMARK 3
REMARK 3 NCS GROUP NUMBER : 3
REMARK 3 CHAIN NAMES : A B C D E F G
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 191 A 374 1
REMARK 3 1 B 191 B 374 1
REMARK 3 1 C 191 C 374 1
REMARK 3 1 D 191 D 374 1
REMARK 3 1 E 191 E 374 1
REMARK 3 1 F 191 F 374 1
REMARK 3 1 G 191 G 374 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 3 A (A): 1398 ; 0.034 ; 0.050
REMARK 3 TIGHT POSITIONAL 3 B (A): 1398 ; 0.031 ; 0.050
REMARK 3 TIGHT POSITIONAL 3 C (A): 1398 ; 0.033 ; 0.050
REMARK 3 TIGHT POSITIONAL 3 D (A): 1398 ; 0.030 ; 0.050
REMARK 3 TIGHT POSITIONAL 3 E (A): 1398 ; 0.029 ; 0.050
REMARK 3 TIGHT POSITIONAL 3 F (A): 1398 ; 0.026 ; 0.050
REMARK 3 TIGHT POSITIONAL 3 G (A): 1398 ; 0.029 ; 0.050
REMARK 3 TIGHT THERMAL 3 A (A**2): 1398 ; 0.033 ; 0.500
REMARK 3 TIGHT THERMAL 3 B (A**2): 1398 ; 0.029 ; 0.500
REMARK 3 TIGHT THERMAL 3 C (A**2): 1398 ; 0.032 ; 0.500
REMARK 3 TIGHT THERMAL 3 D (A**2): 1398 ; 0.030 ; 0.500
REMARK 3 TIGHT THERMAL 3 E (A**2): 1398 ; 0.027 ; 0.500
REMARK 3 TIGHT THERMAL 3 F (A**2): 1398 ; 0.025 ; 0.500
REMARK 3 TIGHT THERMAL 3 G (A**2): 1398 ; 0.027 ; 0.500
REMARK 3
REMARK 3 NCS GROUP NUMBER : 4
REMARK 3 CHAIN NAMES : H I J K L M N
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 2
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 H 2 H 135 1
REMARK 3 1 I 2 I 135 1
REMARK 3 1 J 2 J 135 1
REMARK 3 1 K 2 K 135 1
REMARK 3 1 L 2 L 135 1
REMARK 3 1 M 2 M 135 1
REMARK 3 1 N 2 N 135 1
REMARK 3 2 H 410 H 525 1
REMARK 3 2 I 410 I 525 1
REMARK 3 2 J 410 J 525 1
REMARK 3 2 K 410 K 525 1
REMARK 3 2 L 410 L 525 1
REMARK 3 2 M 410 M 525 1
REMARK 3 2 N 410 N 525 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 4 H (A): 1811 ; 0.088 ; 0.050
REMARK 3 TIGHT POSITIONAL 4 I (A): 1811 ; 0.107 ; 0.050
REMARK 3 TIGHT POSITIONAL 4 J (A): 1811 ; 0.092 ; 0.050
REMARK 3 TIGHT POSITIONAL 4 K (A): 1811 ; 0.081 ; 0.050
REMARK 3 TIGHT POSITIONAL 4 L (A): 1811 ; 0.083 ; 0.050
REMARK 3 TIGHT POSITIONAL 4 M (A): 1811 ; 0.099 ; 0.050
REMARK 3 TIGHT POSITIONAL 4 N (A): 1811 ; 0.092 ; 0.050
REMARK 3 TIGHT THERMAL 4 H (A**2): 1811 ; 0.138 ; 0.500
REMARK 3 TIGHT THERMAL 4 I (A**2): 1811 ; 0.199 ; 0.500
REMARK 3 TIGHT THERMAL 4 J (A**2): 1811 ; 0.141 ; 0.500
REMARK 3 TIGHT THERMAL 4 K (A**2): 1811 ; 0.130 ; 0.500
REMARK 3 TIGHT THERMAL 4 L (A**2): 1811 ; 0.122 ; 0.500
REMARK 3 TIGHT THERMAL 4 M (A**2): 1811 ; 0.139 ; 0.500
REMARK 3 TIGHT THERMAL 4 N (A**2): 1811 ; 0.139 ; 0.500
REMARK 3
REMARK 3 NCS GROUP NUMBER : 5
REMARK 3 CHAIN NAMES : H I J K L M N
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 2
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 H 136 H 190 1
REMARK 3 1 I 136 I 190 1
REMARK 3 1 J 136 J 190 1
REMARK 3 1 K 136 K 190 1
REMARK 3 1 L 136 L 190 1
REMARK 3 1 M 136 M 190 1
REMARK 3 1 N 136 N 190 1
REMARK 3 2 H 375 H 409 1
REMARK 3 2 I 375 I 409 1
REMARK 3 2 J 375 J 409 1
REMARK 3 2 K 375 K 409 1
REMARK 3 2 L 375 L 409 1
REMARK 3 2 M 375 M 409 1
REMARK 3 2 N 375 N 409 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 5 H (A): 647 ; 0.054 ; 0.050
REMARK 3 TIGHT POSITIONAL 5 I (A): 647 ; 0.064 ; 0.050
REMARK 3 TIGHT POSITIONAL 5 J (A): 647 ; 0.060 ; 0.050
REMARK 3 TIGHT POSITIONAL 5 K (A): 647 ; 0.049 ; 0.050
REMARK 3 TIGHT POSITIONAL 5 L (A): 647 ; 0.046 ; 0.050
REMARK 3 TIGHT POSITIONAL 5 M (A): 647 ; 0.060 ; 0.050
REMARK 3 TIGHT POSITIONAL 5 N (A): 647 ; 0.059 ; 0.050
REMARK 3 TIGHT THERMAL 5 H (A**2): 647 ; 0.073 ; 0.500
REMARK 3 TIGHT THERMAL 5 I (A**2): 647 ; 0.084 ; 0.500
REMARK 3 TIGHT THERMAL 5 J (A**2): 647 ; 0.083 ; 0.500
REMARK 3 TIGHT THERMAL 5 K (A**2): 647 ; 0.067 ; 0.500
REMARK 3 TIGHT THERMAL 5 L (A**2): 647 ; 0.058 ; 0.500
REMARK 3 TIGHT THERMAL 5 M (A**2): 647 ; 0.080 ; 0.500
REMARK 3 TIGHT THERMAL 5 N (A**2): 647 ; 0.082 ; 0.500
REMARK 3
REMARK 3 NCS GROUP NUMBER : 6
REMARK 3 CHAIN NAMES : H I J K L M N
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 H 191 H 374 1
REMARK 3 1 I 191 I 374 1
REMARK 3 1 J 191 J 374 1
REMARK 3 1 K 191 K 374 1
REMARK 3 1 L 191 L 374 1
REMARK 3 1 M 191 M 374 1
REMARK 3 1 N 191 N 374 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 6 H (A): 1398 ; 0.038 ; 0.050
REMARK 3 TIGHT POSITIONAL 6 I (A): 1398 ; 0.040 ; 0.050
REMARK 3 TIGHT POSITIONAL 6 J (A): 1398 ; 0.042 ; 0.050
REMARK 3 TIGHT POSITIONAL 6 K (A): 1398 ; 0.037 ; 0.050
REMARK 3 TIGHT POSITIONAL 6 L (A): 1398 ; 0.036 ; 0.050
REMARK 3 TIGHT POSITIONAL 6 M (A): 1398 ; 0.036 ; 0.050
REMARK 3 TIGHT POSITIONAL 6 N (A): 1398 ; 0.036 ; 0.050
REMARK 3 TIGHT THERMAL 6 H (A**2): 1398 ; 0.041 ; 0.500
REMARK 3 TIGHT THERMAL 6 I (A**2): 1398 ; 0.049 ; 0.500
REMARK 3 TIGHT THERMAL 6 J (A**2): 1398 ; 0.048 ; 0.500
REMARK 3 TIGHT THERMAL 6 K (A**2): 1398 ; 0.038 ; 0.500
REMARK 3 TIGHT THERMAL 6 L (A**2): 1398 ; 0.040 ; 0.500
REMARK 3 TIGHT THERMAL 6 M (A**2): 1398 ; 0.042 ; 0.500
REMARK 3 TIGHT THERMAL 6 N (A**2): 1398 ; 0.043 ; 0.500
REMARK 3
REMARK 3 NCS GROUP NUMBER : 7
REMARK 3 CHAIN NAMES : O P Q R S T U
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 O 1 O 97 1
REMARK 3 1 P 1 P 97 1
REMARK 3 1 Q 1 Q 97 1
REMARK 3 1 R 1 R 97 1
REMARK 3 1 S 1 S 97 1
REMARK 3 1 T 1 T 97 1
REMARK 3 1 U 1 U 97 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 7 O (A): 728 ; 0.030 ; 0.050
REMARK 3 TIGHT POSITIONAL 7 P (A): 728 ; 0.030 ; 0.050
REMARK 3 TIGHT POSITIONAL 7 Q (A): 728 ; 0.029 ; 0.050
REMARK 3 TIGHT POSITIONAL 7 R (A): 728 ; 0.030 ; 0.050
REMARK 3 TIGHT POSITIONAL 7 S (A): 728 ; 0.027 ; 0.050
REMARK 3 TIGHT POSITIONAL 7 T (A): 728 ; 0.028 ; 0.050
REMARK 3 TIGHT POSITIONAL 7 U (A): 728 ; 0.031 ; 0.050
REMARK 3 TIGHT THERMAL 7 O (A**2): 728 ; 0.033 ; 0.500
REMARK 3 TIGHT THERMAL 7 P (A**2): 728 ; 0.031 ; 0.500
REMARK 3 TIGHT THERMAL 7 Q (A**2): 728 ; 0.029 ; 0.500
REMARK 3 TIGHT THERMAL 7 R (A**2): 728 ; 0.032 ; 0.500
REMARK 3 TIGHT THERMAL 7 S (A**2): 728 ; 0.026 ; 0.500
REMARK 3 TIGHT THERMAL 7 T (A**2): 728 ; 0.027 ; 0.500
REMARK 3 TIGHT THERMAL 7 U (A**2): 728 ; 0.032 ; 0.500
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 49
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 2 A 135
REMARK 3 RESIDUE RANGE : A 410 A 525
REMARK 3 RESIDUE RANGE : A 600 A 603
REMARK 3 ORIGIN FOR THE GROUP (A): 33.2740 -53.5180 -12.3710
REMARK 3 T TENSOR
REMARK 3 T11: 0.3516 T22: 0.3814
REMARK 3 T33: 0.3869 T12: -0.0340
REMARK 3 T13: 0.0061 T23: -0.0461
REMARK 3 L TENSOR
REMARK 3 L11: 3.9413 L22: 3.4049
REMARK 3 L33: 0.4307 L12: -0.5851
REMARK 3 L13: 0.2788 L23: -0.4602
REMARK 3 S TENSOR
REMARK 3 S11: -0.0335 S12: 0.0546 S13: -0.1040
REMARK 3 S21: 0.0557 S22: 0.0995 S23: 0.0187
REMARK 3 S31: 0.0254 S32: -0.0874 S33: -0.0661
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 136 A 190
REMARK 3 RESIDUE RANGE : A 375 A 409
REMARK 3 ORIGIN FOR THE GROUP (A): 17.1540 -46.6580 -28.0540
REMARK 3 T TENSOR
REMARK 3 T11: 0.4906 T22: 0.7616
REMARK 3 T33: 0.6163 T12: 0.0237
REMARK 3 T13: -0.1242 T23: -0.0450
REMARK 3 L TENSOR
REMARK 3 L11: 9.3003 L22: 5.2463
REMARK 3 L33: 2.9806 L12: 6.2404
REMARK 3 L13: 0.3986 L23: -0.6283
REMARK 3 S TENSOR
REMARK 3 S11: -0.0040 S12: 0.2691 S13: -0.2369
REMARK 3 S21: -0.5703 S22: 0.2423 S23: -0.2565
REMARK 3 S31: 0.2917 S32: -0.7736 S33: -0.2383
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 191 A 374
REMARK 3 ORIGIN FOR THE GROUP (A): 27.8820 -35.0130 -48.9510
REMARK 3 T TENSOR
REMARK 3 T11: 1.8854 T22: 1.9684
REMARK 3 T33: 1.4926 T12: -0.3694
REMARK 3 T13: 0.3299 T23: -0.6224
REMARK 3 L TENSOR
REMARK 3 L11: 8.1547 L22: 6.4438
REMARK 3 L33: 13.4691 L12: 2.5083
REMARK 3 L13: -4.4496 L23: 0.1236
REMARK 3 S TENSOR
REMARK 3 S11: 0.7414 S12: -1.2187 S13: 0.9749
REMARK 3 S21: 1.0424 S22: -0.9627 S23: 1.1595
REMARK 3 S31: -0.4118 S32: -0.4474 S33: 0.2213
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 2 B 135
REMARK 3 RESIDUE RANGE : B 410 B 525
REMARK 3 RESIDUE RANGE : B 600 B 603
REMARK 3 ORIGIN FOR THE GROUP (A): 51.6430 -89.0510 -12.5440
REMARK 3 T TENSOR
REMARK 3 T11: 0.3617 T22: 0.3866
REMARK 3 T33: 0.5085 T12: -0.0157
REMARK 3 T13: 0.0477 T23: -0.1293
REMARK 3 L TENSOR
REMARK 3 L11: 5.2110 L22: 3.1261
REMARK 3 L33: 0.5960 L12: 0.0288
REMARK 3 L13: 0.4883 L23: -0.3110
REMARK 3 S TENSOR
REMARK 3 S11: -0.0409 S12: -0.0844 S13: -0.0162
REMARK 3 S21: -0.0254 S22: -0.0154 S23: 0.0039
REMARK 3 S31: 0.1782 S32: -0.0927 S33: 0.0563
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 136 B 190
REMARK 3 RESIDUE RANGE : B 375 B 409
REMARK 3 ORIGIN FOR THE GROUP (A): 35.9900 -97.3790 -28.1780
REMARK 3 T TENSOR
REMARK 3 T11: 0.6662 T22: 0.7498
REMARK 3 T33: 0.9582 T12: -0.1284
REMARK 3 T13: 0.0998 T23: -0.2076
REMARK 3 L TENSOR
REMARK 3 L11: 3.1060 L22: 13.3476
REMARK 3 L33: 3.5547 L12: -1.0690
REMARK 3 L13: 0.6254 L23: -0.4932
REMARK 3 S TENSOR
REMARK 3 S11: 0.1439 S12: 0.4175 S13: -0.6924
REMARK 3 S21: -0.5577 S22: -0.1793 S23: 0.2772
REMARK 3 S31: 0.8849 S32: -0.3407 S33: 0.0354
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 : B 191 B 374
REMARK 3 ORIGIN FOR THE GROUP (A): 33.8320 -81.7480 -48.9890
REMARK 3 T TENSOR
REMARK 3 T11: 2.0339 T22: 2.1476
REMARK 3 T33: 1.8574 T12: 0.0732
REMARK 3 T13: 0.5473 T23: 0.0852
REMARK 3 L TENSOR
REMARK 3 L11: 4.5233 L22: 9.4789
REMARK 3 L33: 16.4721 L12: 1.3055
REMARK 3 L13: -1.8687 L23: -5.7471
REMARK 3 S TENSOR
REMARK 3 S11: 0.2599 S12: -0.7547 S13: -0.7544
REMARK 3 S21: 1.6450 S22: 0.3304 S23: 1.3145
REMARK 3 S31: 0.5470 S32: -0.7288 S33: -0.5903
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 2 C 135
REMARK 3 RESIDUE RANGE : C 410 C 525
REMARK 3 RESIDUE RANGE : C 600 C 603
REMARK 3 ORIGIN FOR THE GROUP (A): 91.0140 -96.6650 -12.5790
REMARK 3 T TENSOR
REMARK 3 T11: 0.3691 T22: 0.3838
REMARK 3 T33: 0.1251 T12: 0.0087
REMARK 3 T13: 0.1199 T23: -0.0116
REMARK 3 L TENSOR
REMARK 3 L11: 5.2231 L22: 5.0094
REMARK 3 L33: 0.2864 L12: 1.0749
REMARK 3 L13: 0.4958 L23: 0.2332
REMARK 3 S TENSOR
REMARK 3 S11: 0.0803 S12: -0.0046 S13: 0.0219
REMARK 3 S21: 0.0675 S22: -0.0390 S23: 0.3022
REMARK 3 S31: 0.0753 S32: 0.0894 S33: -0.0413
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 136 C 190
REMARK 3 RESIDUE RANGE : C 375 C 409
REMARK 3 ORIGIN FOR THE GROUP (A): 87.9080-114.0110 -28.3630
REMARK 3 T TENSOR
REMARK 3 T11: 0.6244 T22: 0.6046
REMARK 3 T33: 1.0680 T12: -0.0280
REMARK 3 T13: 0.1400 T23: -0.0937
REMARK 3 L TENSOR
REMARK 3 L11: 4.2376 L22: 10.4353
REMARK 3 L33: 4.2092 L12: -4.7754
REMARK 3 L13: 1.1821 L23: -0.5463
REMARK 3 S TENSOR
REMARK 3 S11: 0.1033 S12: 1.0712 S13: 0.1916
REMARK 3 S21: -0.4677 S22: -0.1795 S23: -1.4869
REMARK 3 S31: 0.5847 S32: 0.5770 S33: 0.0762
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 191 C 374
REMARK 3 ORIGIN FOR THE GROUP (A): 74.1890-105.8580 -48.8800
REMARK 3 T TENSOR
REMARK 3 T11: 1.9436 T22: 2.0602
REMARK 3 T33: 1.5912 T12: 0.0718
REMARK 3 T13: 0.3423 T23: 0.4206
REMARK 3 L TENSOR
REMARK 3 L11: 7.4144 L22: 4.9019
REMARK 3 L33: 13.7942 L12: -1.5977
REMARK 3 L13: 1.4593 L23: -4.1173
REMARK 3 S TENSOR
REMARK 3 S11: -0.3257 S12: -1.4649 S13: -1.6741
REMARK 3 S21: 0.7331 S22: 0.5651 S23: 0.3363
REMARK 3 S31: 0.4060 S32: -0.4075 S33: -0.2394
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 2 D 135
REMARK 3 RESIDUE RANGE : D 410 D 525
REMARK 3 RESIDUE RANGE : D 600 D 603
REMARK 3 ORIGIN FOR THE GROUP (A): 121.5020 -70.6900 -12.2560
REMARK 3 T TENSOR
REMARK 3 T11: 0.2982 T22: 0.4302
REMARK 3 T33: 0.3444 T12: -0.0085
REMARK 3 T13: 0.0232 T23: 0.0721
REMARK 3 L TENSOR
REMARK 3 L11: 3.8078 L22: 4.0793
REMARK 3 L33: 0.4725 L12: -0.0120
REMARK 3 L13: -0.0315 L23: 0.1963
REMARK 3 S TENSOR
REMARK 3 S11: -0.0239 S12: 0.0958 S13: 0.1465
REMARK 3 S21: 0.0956 S22: -0.0011 S23: 0.1378
REMARK 3 S31: -0.0125 S32: 0.0531 S33: 0.0249
REMARK 3
REMARK 3 TLS GROUP : 11
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 136 D 190
REMARK 3 RESIDUE RANGE : D 375 D 409
REMARK 3 ORIGIN FOR THE GROUP (A): 133.0160 -83.9570 -27.8400
REMARK 3 T TENSOR
REMARK 3 T11: 0.4785 T22: 0.8082
REMARK 3 T33: 0.9688 T12: 0.0233
REMARK 3 T13: 0.1129 T23: 0.0563
REMARK 3 L TENSOR
REMARK 3 L11: 10.7910 L22: 4.0960
REMARK 3 L33: 3.3261 L12: 0.1256
REMARK 3 L13: 0.5477 L23: 0.8737
REMARK 3 S TENSOR
REMARK 3 S11: -0.1293 S12: 0.6492 S13: 1.2725
REMARK 3 S21: -0.3323 S22: 0.2222 S23: -0.7122
REMARK 3 S31: 0.0499 S32: 0.9464 S33: -0.0929
REMARK 3
REMARK 3 TLS GROUP : 12
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 191 D 374
REMARK 3 ORIGIN FOR THE GROUP (A): 118.3470 -89.7600 -48.6900
REMARK 3 T TENSOR
REMARK 3 T11: 1.7374 T22: 2.2743
REMARK 3 T33: 1.7910 T12: -0.2512
REMARK 3 T13: -0.1926 T23: 0.7876
REMARK 3 L TENSOR
REMARK 3 L11: 8.5146 L22: 4.8780
REMARK 3 L33: 14.5790 L12: 0.6627
REMARK 3 L13: 4.1777 L23: -0.9614
REMARK 3 S TENSOR
REMARK 3 S11: 0.6303 S12: -1.6305 S13: -1.5545
REMARK 3 S21: 0.7189 S22: -0.4539 S23: -0.9617
REMARK 3 S31: 0.9001 S32: 0.6046 S33: -0.1763
REMARK 3
REMARK 3 TLS GROUP : 13
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 2 E 135
REMARK 3 RESIDUE RANGE : E 410 E 525
REMARK 3 RESIDUE RANGE : E 600 E 603
REMARK 3 ORIGIN FOR THE GROUP (A): 120.4420 -30.6350 -12.4330
REMARK 3 T TENSOR
REMARK 3 T11: 0.3669 T22: 0.4727
REMARK 3 T33: 0.7828 T12: -0.0477
REMARK 3 T13: -0.0455 T23: 0.1480
REMARK 3 L TENSOR
REMARK 3 L11: 4.3975 L22: 3.2221
REMARK 3 L33: 0.6994 L12: -0.9019
REMARK 3 L13: -0.3805 L23: 0.4441
REMARK 3 S TENSOR
REMARK 3 S11: -0.0487 S12: -0.0112 S13: 0.1598
REMARK 3 S21: -0.0310 S22: 0.0227 S23: -0.0849
REMARK 3 S31: -0.1603 S32: 0.1310 S33: 0.0260
REMARK 3
REMARK 3 TLS GROUP : 14
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 136 E 190
REMARK 3 RESIDUE RANGE : E 375 E 409
REMARK 3 ORIGIN FOR THE GROUP (A): 138.1980 -30.0230 -27.9880
REMARK 3 T TENSOR
REMARK 3 T11: 0.6135 T22: 0.9062
REMARK 3 T33: 1.1213 T12: -0.0474
REMARK 3 T13: 0.0927 T23: 0.2792
REMARK 3 L TENSOR
REMARK 3 L11: 2.9415 L22: 11.5171
REMARK 3 L33: 4.5528 L12: 5.5779
REMARK 3 L13: -1.2450 L23: 1.1023
REMARK 3 S TENSOR
REMARK 3 S11: 0.3959 S12: 0.3470 S13: 0.1762
REMARK 3 S21: -0.8529 S22: -0.0373 S23: 0.2146
REMARK 3 S31: -0.9274 S32: 0.7219 S33: -0.3586
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 : E 191 E 374
REMARK 3 ORIGIN FOR THE GROUP (A): 133.2630 -45.0750 -48.7940
REMARK 3 T TENSOR
REMARK 3 T11: 2.1852 T22: 2.1504
REMARK 3 T33: 2.0024 T12: -0.0575
REMARK 3 T13: -0.5652 T23: 0.2604
REMARK 3 L TENSOR
REMARK 3 L11: 5.3821 L22: 8.2286
REMARK 3 L33: 15.5491 L12: 1.4727
REMARK 3 L13: 4.7924 L23: 4.4908
REMARK 3 S TENSOR
REMARK 3 S11: 0.2751 S12: -0.5882 S13: 0.1408
REMARK 3 S21: 1.6266 S22: 0.2852 S23: -1.9611
REMARK 3 S31: -0.1514 S32: 0.7906 S33: -0.5603
REMARK 3
REMARK 3 TLS GROUP : 16
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : F 2 F 135
REMARK 3 RESIDUE RANGE : F 410 F 525
REMARK 3 RESIDUE RANGE : F 600 F 603
REMARK 3 ORIGIN FOR THE GROUP (A): 88.3940 -6.5470 -12.6060
REMARK 3 T TENSOR
REMARK 3 T11: 0.4585 T22: 0.4258
REMARK 3 T33: 0.7974 T12: -0.0081
REMARK 3 T13: -0.1285 T23: 0.1143
REMARK 3 L TENSOR
REMARK 3 L11: 3.7994 L22: 3.3271
REMARK 3 L33: 0.6312 L12: 0.5400
REMARK 3 L13: -0.4793 L23: 0.0515
REMARK 3 S TENSOR
REMARK 3 S11: -0.0036 S12: 0.0105 S13: 0.2515
REMARK 3 S21: -0.0439 S22: -0.0211 S23: -0.2698
REMARK 3 S31: -0.2326 S32: 0.0341 S33: 0.0246
REMARK 3
REMARK 3 TLS GROUP : 17
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : F 136 F 190
REMARK 3 RESIDUE RANGE : F 375 F 409
REMARK 3 ORIGIN FOR THE GROUP (A): 98.9510 7.7850 -28.1850
REMARK 3 T TENSOR
REMARK 3 T11: 0.7498 T22: 0.8368
REMARK 3 T33: 1.6595 T12: -0.1385
REMARK 3 T13: 0.0217 T23: 0.2724
REMARK 3 L TENSOR
REMARK 3 L11: 6.6496 L22: 10.5892
REMARK 3 L33: 3.0820 L12: -4.7686
REMARK 3 L13: -0.6443 L23: -1.5025
REMARK 3 S TENSOR
REMARK 3 S11: 0.2959 S12: 0.6941 S13: 0.9308
REMARK 3 S21: -0.1221 S22: 0.0136 S23: 0.2639
REMARK 3 S31: -0.5635 S32: -0.1170 S33: -0.3095
REMARK 3
REMARK 3 TLS GROUP : 18
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : F 191 F 374
REMARK 3 ORIGIN FOR THE GROUP (A): 107.8710 -5.3750 -48.9960
REMARK 3 T TENSOR
REMARK 3 T11: 2.4442 T22: 2.3553
REMARK 3 T33: 2.1005 T12: 0.1436
REMARK 3 T13: -0.4565 T23: -0.1018
REMARK 3 L TENSOR
REMARK 3 L11: 3.1776 L22: 4.2686
REMARK 3 L33: 7.9165 L12: -0.8233
REMARK 3 L13: -0.5536 L23: 2.3465
REMARK 3 S TENSOR
REMARK 3 S11: -0.0492 S12: -0.7498 S13: 0.8852
REMARK 3 S21: 1.2256 S22: 0.2974 S23: -0.8655
REMARK 3 S31: -0.0276 S32: 0.0681 S33: -0.2481
REMARK 3
REMARK 3 TLS GROUP : 19
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : G 2 G 135
REMARK 3 RESIDUE RANGE : G 410 G 525
REMARK 3 RESIDUE RANGE : G 600 G 603
REMARK 3 ORIGIN FOR THE GROUP (A): 49.4820 -16.8680 -12.7860
REMARK 3 T TENSOR
REMARK 3 T11: 0.3427 T22: 0.3829
REMARK 3 T33: 0.4223 T12: 0.0185
REMARK 3 T13: -0.0833 T23: -0.0129
REMARK 3 L TENSOR
REMARK 3 L11: 2.7489 L22: 5.2105
REMARK 3 L33: 0.5696 L12: 0.3579
REMARK 3 L13: -0.1700 L23: -0.5039
REMARK 3 S TENSOR
REMARK 3 S11: 0.0578 S12: 0.0097 S13: 0.1475
REMARK 3 S21: 0.0881 S22: 0.0225 S23: -0.1617
REMARK 3 S31: -0.0567 S32: -0.0161 S33: -0.0803
REMARK 3
REMARK 3 TLS GROUP : 20
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : G 136 G 190
REMARK 3 RESIDUE RANGE : G 375 G 409
REMARK 3 ORIGIN FOR THE GROUP (A): 44.7550 0.0030 -28.5930
REMARK 3 T TENSOR
REMARK 3 T11: 0.6943 T22: 0.6113
REMARK 3 T33: 0.9079 T12: 0.0274
REMARK 3 T13: -0.1386 T23: 0.0649
REMARK 3 L TENSOR
REMARK 3 L11: 11.5048 L22: 5.2881
REMARK 3 L33: 4.5629 L12: -0.6952
REMARK 3 L13: -2.0299 L23: -0.6132
REMARK 3 S TENSOR
REMARK 3 S11: 0.1638 S12: 0.9874 S13: 0.2025
REMARK 3 S21: -0.4386 S22: 0.1306 S23: 0.9769
REMARK 3 S31: -0.2503 S32: -0.9126 S33: -0.2944
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 : G 191 G 374
REMARK 3 ORIGIN FOR THE GROUP (A): 60.7100 -1.3030 -49.1720
REMARK 3 T TENSOR
REMARK 3 T11: 1.9147 T22: 2.1653
REMARK 3 T33: 1.9767 T12: -0.1042
REMARK 3 T13: 0.1044 T23: -0.4730
REMARK 3 L TENSOR
REMARK 3 L11: 7.3818 L22: 4.0909
REMARK 3 L33: 14.9399 L12: -0.1647
REMARK 3 L13: -3.9249 L23: 3.0019
REMARK 3 S TENSOR
REMARK 3 S11: 0.4214 S12: -1.4346 S13: 1.7424
REMARK 3 S21: 0.6177 S22: 0.0243 S23: 0.3220
REMARK 3 S31: -0.6250 S32: 0.1514 S33: -0.4456
REMARK 3
REMARK 3 TLS GROUP : 22
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : H 2 H 135
REMARK 3 RESIDUE RANGE : H 410 H 525
REMARK 3 ORIGIN FOR THE GROUP (A): 40.5550 -76.5050 19.5230
REMARK 3 T TENSOR
REMARK 3 T11: 0.3510 T22: 0.4377
REMARK 3 T33: 0.3435 T12: -0.0074
REMARK 3 T13: 0.0694 T23: 0.0200
REMARK 3 L TENSOR
REMARK 3 L11: 4.1563 L22: 5.6801
REMARK 3 L33: 1.2542 L12: 0.3767
REMARK 3 L13: 0.2810 L23: 0.1293
REMARK 3 S TENSOR
REMARK 3 S11: -0.0611 S12: 0.0399 S13: -0.2789
REMARK 3 S21: -0.0510 S22: 0.0627 S23: 0.2540
REMARK 3 S31: 0.1402 S32: -0.1883 S33: -0.0017
REMARK 3
REMARK 3 TLS GROUP : 23
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : H 136 H 190
REMARK 3 RESIDUE RANGE : H 375 H 409
REMARK 3 ORIGIN FOR THE GROUP (A): 25.6410 -89.3820 32.5860
REMARK 3 T TENSOR
REMARK 3 T11: 0.8960 T22: 0.8875
REMARK 3 T33: 1.0969 T12: -0.0804
REMARK 3 T13: 0.0921 T23: -0.0411
REMARK 3 L TENSOR
REMARK 3 L11: 9.1096 L22: 3.5240
REMARK 3 L33: 10.1069 L12: -3.2770
REMARK 3 L13: 6.6476 L23: -3.0984
REMARK 3 S TENSOR
REMARK 3 S11: 0.6026 S12: 0.1085 S13: -0.1858
REMARK 3 S21: -0.1576 S22: -0.2875 S23: 0.7161
REMARK 3 S31: 0.6685 S32: -0.4138 S33: -0.3152
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 : H 191 H 374
REMARK 3 ORIGIN FOR THE GROUP (A): 33.6250 -83.1120 57.6910
REMARK 3 T TENSOR
REMARK 3 T11: 1.2607 T22: 1.1627
REMARK 3 T33: 1.4790 T12: -0.0361
REMARK 3 T13: 0.0388 T23: -0.0412
REMARK 3 L TENSOR
REMARK 3 L11: 9.5788 L22: 6.5026
REMARK 3 L33: 4.3451 L12: 1.5039
REMARK 3 L13: -0.7327 L23: 0.7618
REMARK 3 S TENSOR
REMARK 3 S11: -0.3370 S12: 0.0980 S13: -1.2670
REMARK 3 S21: 0.3206 S22: -0.0673 S23: 0.1983
REMARK 3 S31: 0.5343 S32: -0.4586 S33: 0.4043
REMARK 3
REMARK 3 TLS GROUP : 25
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : I 2 I 135
REMARK 3 RESIDUE RANGE : I 410 I 525
REMARK 3 ORIGIN FOR THE GROUP (A): 74.1570 -97.4700 19.5200
REMARK 3 T TENSOR
REMARK 3 T11: 0.3642 T22: 0.4101
REMARK 3 T33: 0.0097 T12: -0.0053
REMARK 3 T13: 0.0291 T23: 0.0544
REMARK 3 L TENSOR
REMARK 3 L11: 5.1536 L22: 7.0853
REMARK 3 L33: 0.4577 L12: -0.9262
REMARK 3 L13: -0.1295 L23: 0.8617
REMARK 3 S TENSOR
REMARK 3 S11: 0.0948 S12: 0.0952 S13: 0.0149
REMARK 3 S21: -0.0645 S22: -0.0062 S23: 0.0851
REMARK 3 S31: 0.0719 S32: -0.0142 S33: -0.0885
REMARK 3
REMARK 3 TLS GROUP : 26
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : I 136 I 190
REMARK 3 RESIDUE RANGE : I 375 I 409
REMARK 3 ORIGIN FOR THE GROUP (A): 75.1780-117.3640 32.3950
REMARK 3 T TENSOR
REMARK 3 T11: 0.6966 T22: 0.6872
REMARK 3 T33: 0.8212 T12: -0.0496
REMARK 3 T13: 0.1632 T23: -0.0049
REMARK 3 L TENSOR
REMARK 3 L11: 6.4882 L22: 0.1176
REMARK 3 L33: 9.5438 L12: 0.4319
REMARK 3 L13: 2.5638 L23: 3.1334
REMARK 3 S TENSOR
REMARK 3 S11: 0.0422 S12: 0.2916 S13: -0.6659
REMARK 3 S21: 0.9948 S22: -0.3243 S23: -0.1689
REMARK 3 S31: 0.7591 S32: -0.4453 S33: 0.2820
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 : I 191 I 374
REMARK 3 ORIGIN FOR THE GROUP (A): 74.9030-107.8130 57.6130
REMARK 3 T TENSOR
REMARK 3 T11: 1.1259 T22: 1.2390
REMARK 3 T33: 1.3424 T12: 0.1266
REMARK 3 T13: 0.0800 T23: 0.1339
REMARK 3 L TENSOR
REMARK 3 L11: 7.8072 L22: 10.8026
REMARK 3 L33: 5.2234 L12: 0.7689
REMARK 3 L13: -1.1765 L23: 0.0749
REMARK 3 S TENSOR
REMARK 3 S11: -0.5080 S12: -0.6901 S13: -1.4293
REMARK 3 S21: 0.1565 S22: 0.2738 S23: -1.0577
REMARK 3 S31: 0.9242 S32: 0.2007 S33: 0.2343
REMARK 3
REMARK 3 TLS GROUP : 28
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : J 2 J 135
REMARK 3 RESIDUE RANGE : J 410 J 525
REMARK 3 ORIGIN FOR THE GROUP (A): 111.7680 -84.5050 19.7300
REMARK 3 T TENSOR
REMARK 3 T11: 0.3327 T22: 0.4370
REMARK 3 T33: 0.3860 T12: -0.0008
REMARK 3 T13: 0.0067 T23: 0.0163
REMARK 3 L TENSOR
REMARK 3 L11: 6.6828 L22: 3.7126
REMARK 3 L33: 0.6673 L12: 0.3233
REMARK 3 L13: -0.2304 L23: 0.2540
REMARK 3 S TENSOR
REMARK 3 S11: -0.1588 S12: 0.1550 S13: -0.2476
REMARK 3 S21: 0.0693 S22: 0.1250 S23: -0.0373
REMARK 3 S31: 0.0875 S32: 0.0888 S33: 0.0337
REMARK 3
REMARK 3 TLS GROUP : 29
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : J 136 J 190
REMARK 3 RESIDUE RANGE : J 375 J 409
REMARK 3 ORIGIN FOR THE GROUP (A): 127.3570 -96.2940 33.0190
REMARK 3 T TENSOR
REMARK 3 T11: 0.7902 T22: 0.9531
REMARK 3 T33: 0.9193 T12: 0.1856
REMARK 3 T13: 0.0511 T23: 0.1146
REMARK 3 L TENSOR
REMARK 3 L11: 2.8787 L22: 10.2318
REMARK 3 L33: 8.7830 L12: -1.0010
REMARK 3 L13: 1.2370 L23: 4.6902
REMARK 3 S TENSOR
REMARK 3 S11: 0.3145 S12: -0.1459 S13: -0.7142
REMARK 3 S21: -0.9978 S22: -0.3798 S23: 0.1179
REMARK 3 S31: 0.2835 S32: 0.5283 S33: 0.0653
REMARK 3
REMARK 3 TLS GROUP : 30
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : J 191 J 374
REMARK 3 ORIGIN FOR THE GROUP (A): 119.5230 -90.0700 58.1040
REMARK 3 T TENSOR
REMARK 3 T11: 0.8809 T22: 1.6413
REMARK 3 T33: 1.0730 T12: -0.0242
REMARK 3 T13: 0.1543 T23: 0.0793
REMARK 3 L TENSOR
REMARK 3 L11: 8.6016 L22: 8.2545
REMARK 3 L33: 6.6924 L12: -1.0145
REMARK 3 L13: 0.7650 L23: -2.2363
REMARK 3 S TENSOR
REMARK 3 S11: 0.4718 S12: -0.5607 S13: 0.1754
REMARK 3 S21: -0.1136 S22: -1.0042 S23: -0.9359
REMARK 3 S31: 0.5127 S32: 1.2685 S33: 0.5323
REMARK 3
REMARK 3 TLS GROUP : 31
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : K 2 K 135
REMARK 3 RESIDUE RANGE : K 410 K 525
REMARK 3 ORIGIN FOR THE GROUP (A): 124.8830 -46.6070 19.6230
REMARK 3 T TENSOR
REMARK 3 T11: 0.3747 T22: 0.4770
REMARK 3 T33: 0.5952 T12: -0.0081
REMARK 3 T13: -0.1049 T23: 0.0184
REMARK 3 L TENSOR
REMARK 3 L11: 5.0331 L22: 4.9276
REMARK 3 L33: 1.1990 L12: 1.3647
REMARK 3 L13: -0.5406 L23: -0.4371
REMARK 3 S TENSOR
REMARK 3 S11: -0.0778 S12: -0.0474 S13: 0.0726
REMARK 3 S21: -0.0560 S22: -0.0670 S23: -0.3552
REMARK 3 S31: -0.0790 S32: 0.2194 S33: 0.1448
REMARK 3
REMARK 3 TLS GROUP : 32
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : K 136 K 190
REMARK 3 RESIDUE RANGE : K 375 K 409
REMARK 3 ORIGIN FOR THE GROUP (A): 143.7750 -41.4640 32.7640
REMARK 3 T TENSOR
REMARK 3 T11: 0.7257 T22: 1.2377
REMARK 3 T33: 1.5158 T12: -0.1971
REMARK 3 T13: -0.1879 T23: 0.0467
REMARK 3 L TENSOR
REMARK 3 L11: 8.9246 L22: 0.8107
REMARK 3 L33: 9.3686 L12: -1.8791
REMARK 3 L13: -3.8745 L23: 2.8659
REMARK 3 S TENSOR
REMARK 3 S11: 0.2556 S12: 0.6151 S13: -0.5096
REMARK 3 S21: 0.5885 S22: -0.1953 S23: -0.7062
REMARK 3 S31: -0.3741 S32: 0.7910 S33: -0.0603
REMARK 3
REMARK 3 TLS GROUP : 33
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : K 191 K 374
REMARK 3 ORIGIN FOR THE GROUP (A): 133.6070 -43.9560 57.8060
REMARK 3 T TENSOR
REMARK 3 T11: 1.2311 T22: 1.3524
REMARK 3 T33: 1.6811 T12: -0.2690
REMARK 3 T13: -0.0781 T23: 0.0558
REMARK 3 L TENSOR
REMARK 3 L11: 7.9147 L22: 6.7298
REMARK 3 L33: 5.8367 L12: -0.4500
REMARK 3 L13: 0.8440 L23: -0.7430
REMARK 3 S TENSOR
REMARK 3 S11: -0.0717 S12: 0.1523 S13: 1.0788
REMARK 3 S21: 0.5389 S22: -0.4266 S23: -0.7562
REMARK 3 S31: -0.6440 S32: 1.0447 S33: 0.4982
REMARK 3
REMARK 3 TLS GROUP : 34
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : L 2 L 135
REMARK 3 RESIDUE RANGE : L 410 L 525
REMARK 3 ORIGIN FOR THE GROUP (A): 103.6670 -12.8510 19.7300
REMARK 3 T TENSOR
REMARK 3 T11: 0.4455 T22: 0.4896
REMARK 3 T33: 0.6795 T12: -0.0041
REMARK 3 T13: -0.1303 T23: -0.0480
REMARK 3 L TENSOR
REMARK 3 L11: 4.3476 L22: 7.1433
REMARK 3 L33: 1.6133 L12: -1.1104
REMARK 3 L13: 0.1384 L23: -1.0258
REMARK 3 S TENSOR
REMARK 3 S11: 0.0788 S12: 0.1562 S13: 0.4455
REMARK 3 S21: -0.1237 S22: -0.1962 S23: -0.3998
REMARK 3 S31: -0.3853 S32: 0.1533 S33: 0.1174
REMARK 3
REMARK 3 TLS GROUP : 35
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : L 136 L 190
REMARK 3 RESIDUE RANGE : L 375 L 409
REMARK 3 ORIGIN FOR THE GROUP (A): 111.1500 5.1970 32.9040
REMARK 3 T TENSOR
REMARK 3 T11: 1.3097 T22: 1.0048
REMARK 3 T33: 1.5723 T12: -0.2959
REMARK 3 T13: -0.4321 T23: -0.0578
REMARK 3 L TENSOR
REMARK 3 L11: 2.1219 L22: 0.4185
REMARK 3 L33: 8.9734 L12: -0.5235
REMARK 3 L13: -2.9668 L23: 2.7698
REMARK 3 S TENSOR
REMARK 3 S11: 0.0744 S12: -0.4185 S13: 0.2863
REMARK 3 S21: 0.5995 S22: 0.3980 S23: 0.0581
REMARK 3 S31: -1.3721 S32: 0.9637 S33: -0.4724
REMARK 3
REMARK 3 TLS GROUP : 36
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : L 191 L 374
REMARK 3 ORIGIN FOR THE GROUP (A): 106.4620 -4.0720 57.7970
REMARK 3 T TENSOR
REMARK 3 T11: 1.9111 T22: 1.1316
REMARK 3 T33: 1.8647 T12: 0.0467
REMARK 3 T13: -0.2936 T23: -0.0840
REMARK 3 L TENSOR
REMARK 3 L11: 8.5378 L22: 6.0616
REMARK 3 L33: 5.3586 L12: 1.9213
REMARK 3 L13: 1.4807 L23: -0.2832
REMARK 3 S TENSOR
REMARK 3 S11: -0.7506 S12: -0.1122 S13: 1.6484
REMARK 3 S21: 0.2333 S22: 0.3477 S23: 0.5675
REMARK 3 S31: -1.2897 S32: 0.1311 S33: 0.4029
REMARK 3
REMARK 3 TLS GROUP : 37
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : M 2 M 135
REMARK 3 RESIDUE RANGE : M 410 M 525
REMARK 3 ORIGIN FOR THE GROUP (A): 64.0700 -8.7060 19.4250
REMARK 3 T TENSOR
REMARK 3 T11: 0.3679 T22: 0.4312
REMARK 3 T33: 0.2648 T12: -0.0079
REMARK 3 T13: -0.0287 T23: -0.0371
REMARK 3 L TENSOR
REMARK 3 L11: 5.5201 L22: 5.8969
REMARK 3 L33: 0.5638 L12: -1.4193
REMARK 3 L13: 0.6260 L23: -0.5252
REMARK 3 S TENSOR
REMARK 3 S11: 0.0524 S12: 0.2578 S13: 0.0409
REMARK 3 S21: 0.1352 S22: 0.0040 S23: -0.1717
REMARK 3 S31: -0.0856 S32: 0.0672 S33: -0.0564
REMARK 3
REMARK 3 TLS GROUP : 38
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : M 136 M 190
REMARK 3 RESIDUE RANGE : M 375 M 409
REMARK 3 ORIGIN FOR THE GROUP (A): 54.1780 8.5160 32.2010
REMARK 3 T TENSOR
REMARK 3 T11: 0.8809 T22: 0.6318
REMARK 3 T33: 0.9310 T12: -0.0743
REMARK 3 T13: -0.1324 T23: -0.1240
REMARK 3 L TENSOR
REMARK 3 L11: 3.3027 L22: 6.4038
REMARK 3 L33: 7.7422 L12: 4.0299
REMARK 3 L13: -1.2877 L23: -4.1309
REMARK 3 S TENSOR
REMARK 3 S11: -0.7427 S12: -0.2332 S13: 0.2554
REMARK 3 S21: 0.5116 S22: 0.4530 S23: -0.1347
REMARK 3 S31: -0.4638 S32: -0.0880 S33: 0.2897
REMARK 3
REMARK 3 TLS GROUP : 39
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : M 191 M 374
REMARK 3 ORIGIN FOR THE GROUP (A): 58.5000 0.1440 57.4610
REMARK 3 T TENSOR
REMARK 3 T11: 1.4431 T22: 1.4154
REMARK 3 T33: 1.2073 T12: -0.0123
REMARK 3 T13: -0.0489 T23: -0.0772
REMARK 3 L TENSOR
REMARK 3 L11: 8.1203 L22: 9.0288
REMARK 3 L33: 4.8410 L12: -1.2768
REMARK 3 L13: 0.7684 L23: 0.5937
REMARK 3 S TENSOR
REMARK 3 S11: -0.1171 S12: -0.6757 S13: 0.5572
REMARK 3 S21: -0.0995 S22: -0.1329 S23: 0.9308
REMARK 3 S31: -0.7157 S32: -0.5467 S33: 0.2500
REMARK 3
REMARK 3 TLS GROUP : 40
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : N 2 N 135
REMARK 3 RESIDUE RANGE : N 410 N 525
REMARK 3 ORIGIN FOR THE GROUP (A): 35.9240 -36.7870 19.6420
REMARK 3 T TENSOR
REMARK 3 T11: 0.3939 T22: 0.4197
REMARK 3 T33: 0.3597 T12: 0.0025
REMARK 3 T13: -0.0549 T23: -0.0028
REMARK 3 L TENSOR
REMARK 3 L11: 6.8271 L22: 4.1714
REMARK 3 L33: 0.5608 L12: 1.7098
REMARK 3 L13: 0.1136 L23: 0.1601
REMARK 3 S TENSOR
REMARK 3 S11: -0.2532 S12: 0.0842 S13: 0.3568
REMARK 3 S21: -0.1122 S22: 0.2145 S23: 0.2428
REMARK 3 S31: -0.0857 S32: -0.0790 S33: 0.0387
REMARK 3
REMARK 3 TLS GROUP : 41
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : N 136 N 190
REMARK 3 RESIDUE RANGE : N 375 N 409
REMARK 3 ORIGIN FOR THE GROUP (A): 16.7400 -33.0820 32.9480
REMARK 3 T TENSOR
REMARK 3 T11: 0.7711 T22: 1.2086
REMARK 3 T33: 0.8203 T12: 0.0621
REMARK 3 T13: 0.0341 T23: -0.1413
REMARK 3 L TENSOR
REMARK 3 L11: 5.0196 L22: 8.3885
REMARK 3 L33: 8.1619 L12: 0.9663
REMARK 3 L13: -0.5103 L23: -3.6769
REMARK 3 S TENSOR
REMARK 3 S11: 0.0697 S12: 0.3452 S13: 1.0255
REMARK 3 S21: -0.5019 S22: 0.2765 S23: 0.5369
REMARK 3 S31: -0.2258 S32: -0.8167 S33: -0.3462
REMARK 3
REMARK 3 TLS GROUP : 42
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : N 191 N 374
REMARK 3 ORIGIN FOR THE GROUP (A): 26.3770 -35.4300 58.0320
REMARK 3 T TENSOR
REMARK 3 T11: 1.2053 T22: 1.5280
REMARK 3 T33: 1.3762 T12: -0.2356
REMARK 3 T13: -0.1818 T23: -0.1647
REMARK 3 L TENSOR
REMARK 3 L11: 8.7949 L22: 9.0637
REMARK 3 L33: 6.2183 L12: -1.4497
REMARK 3 L13: -1.7456 L23: 1.3609
REMARK 3 S TENSOR
REMARK 3 S11: 0.6072 S12: -0.0621 S13: -1.1425
REMARK 3 S21: 0.4954 S22: -1.0433 S23: 1.3756
REMARK 3 S31: -0.1158 S32: -1.0989 S33: 0.4361
REMARK 3
REMARK 3 TLS GROUP : 43
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : O 1 O 97
REMARK 3 ORIGIN FOR THE GROUP (A): 65.7220 -29.5560 -98.1260
REMARK 3 T TENSOR
REMARK 3 T11: 1.8145 T22: 1.8394
REMARK 3 T33: 1.3709 T12: -0.0643
REMARK 3 T13: -0.0075 T23: -0.0921
REMARK 3 L TENSOR
REMARK 3 L11: 8.5122 L22: 4.7923
REMARK 3 L33: 9.8536 L12: 2.7327
REMARK 3 L13: -3.4755 L23: -2.8614
REMARK 3 S TENSOR
REMARK 3 S11: 0.3692 S12: -0.2787 S13: -0.4064
REMARK 3 S21: 0.5688 S22: -0.4076 S23: 0.4651
REMARK 3 S31: -0.8752 S32: -0.4615 S33: 0.0384
REMARK 3
REMARK 3 TLS GROUP : 44
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : P 1 P 97
REMARK 3 ORIGIN FOR THE GROUP (A): 52.9980 -48.7480 -98.0830
REMARK 3 T TENSOR
REMARK 3 T11: 1.8006 T22: 2.0247
REMARK 3 T33: 1.3726 T12: -0.0022
REMARK 3 T13: 0.0543 T23: -0.1902
REMARK 3 L TENSOR
REMARK 3 L11: 4.2702 L22: 10.1108
REMARK 3 L33: 7.6103 L12: 3.3695
REMARK 3 L13: -1.8114 L23: -6.6623
REMARK 3 S TENSOR
REMARK 3 S11: -0.0032 S12: -0.2953 S13: -0.7258
REMARK 3 S21: 0.7808 S22: 0.0407 S23: -0.1251
REMARK 3 S31: -0.4267 S32: -0.2531 S33: -0.0375
REMARK 3
REMARK 3 TLS GROUP : 45
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : Q 1 Q 97
REMARK 3 ORIGIN FOR THE GROUP (A): 60.2040 -70.7420 -98.1070
REMARK 3 T TENSOR
REMARK 3 T11: 1.7009 T22: 2.1422
REMARK 3 T33: 1.3907 T12: -0.1085
REMARK 3 T13: 0.2414 T23: -0.0113
REMARK 3 L TENSOR
REMARK 3 L11: 4.2734 L22: 9.7593
REMARK 3 L33: 9.8893 L12: -3.7833
REMARK 3 L13: 3.5340 L23: -4.4063
REMARK 3 S TENSOR
REMARK 3 S11: 0.0276 S12: -0.6422 S13: -0.8134
REMARK 3 S21: 0.4617 S22: 0.0558 S23: 0.0008
REMARK 3 S31: 0.1877 S32: -0.2073 S33: -0.0834
REMARK 3
REMARK 3 TLS GROUP : 46
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : R 1 R 97
REMARK 3 ORIGIN FOR THE GROUP (A): 81.8750 -78.3980 -98.0250
REMARK 3 T TENSOR
REMARK 3 T11: 1.9101 T22: 1.9995
REMARK 3 T33: 1.3998 T12: -0.0506
REMARK 3 T13: 0.1556 T23: 0.1818
REMARK 3 L TENSOR
REMARK 3 L11: 10.3647 L22: 1.5795
REMARK 3 L33: 9.6435 L12: -0.7000
REMARK 3 L13: 5.0271 L23: 0.5128
REMARK 3 S TENSOR
REMARK 3 S11: 0.3108 S12: -0.6682 S13: -0.1589
REMARK 3 S21: 0.3830 S22: -0.0555 S23: -0.7297
REMARK 3 S31: 0.2237 S32: -0.0180 S33: -0.2553
REMARK 3
REMARK 3 TLS GROUP : 47
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : S 1 S 97
REMARK 3 ORIGIN FOR THE GROUP (A): 101.5240 -66.5430 -97.9680
REMARK 3 T TENSOR
REMARK 3 T11: 1.8330 T22: 1.9518
REMARK 3 T33: 1.5239 T12: 0.1358
REMARK 3 T13: 0.1962 T23: 0.2965
REMARK 3 L TENSOR
REMARK 3 L11: 9.4646 L22: 8.0801
REMARK 3 L33: 10.0806 L12: 4.1593
REMARK 3 L13: 5.0036 L23: 5.4218
REMARK 3 S TENSOR
REMARK 3 S11: 0.3424 S12: -0.4158 S13: 0.3595
REMARK 3 S21: 0.7058 S22: 0.0743 S23: -0.6861
REMARK 3 S31: 0.8432 S32: 0.0683 S33: -0.4167
REMARK 3
REMARK 3 TLS GROUP : 48
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : T 1 T 97
REMARK 3 ORIGIN FOR THE GROUP (A): 104.4370 -43.7020 -98.1440
REMARK 3 T TENSOR
REMARK 3 T11: 1.5758 T22: 2.1504
REMARK 3 T33: 1.5697 T12: 0.0544
REMARK 3 T13: 0.0001 T23: 0.2423
REMARK 3 L TENSOR
REMARK 3 L11: 3.7537 L22: 14.7623
REMARK 3 L33: 9.8965 L12: -0.6239
REMARK 3 L13: -1.2112 L23: 5.6545
REMARK 3 S TENSOR
REMARK 3 S11: -0.1035 S12: -0.5262 S13: 0.5457
REMARK 3 S21: 1.1387 S22: 0.5111 S23: -0.5617
REMARK 3 S31: 0.2260 S32: 0.4211 S33: -0.4076
REMARK 3
REMARK 3 TLS GROUP : 49
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : U 1 U 97
REMARK 3 ORIGIN FOR THE GROUP (A): 88.5350 -27.0200 -98.3380
REMARK 3 T TENSOR
REMARK 3 T11: 1.6862 T22: 2.0937
REMARK 3 T33: 1.4848 T12: -0.1774
REMARK 3 T13: -0.0528 T23: -0.0079
REMARK 3 L TENSOR
REMARK 3 L11: 7.2215 L22: 3.1239
REMARK 3 L33: 10.1555 L12: -2.6750
REMARK 3 L13: -2.3202 L23: 2.5592
REMARK 3 S TENSOR
REMARK 3 S11: -0.1382 S12: -0.9569 S13: 0.4174
REMARK 3 S21: 0.6255 S22: 0.1529 S23: 0.6524
REMARK 3 S31: -0.0594 S32: 0.3336 S33: -0.0147
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK BULK SOLVENT
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1SVT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-APR-04.
REMARK 100 THE RCSB ID CODE IS RCSB022035.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : NULL
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 231127
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 67.37
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.77
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG3000, CACODYLIC ACID, POTASSIUM
REMARK 280 CHLORIDE, PH 5.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 127.77300
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 133.42750
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 127.77300
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 133.42750
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 AUTHOR DETERMINED BIOLOGICAL UNIT: 21-MERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: 21-MERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 78620 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 317280 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -466.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I,
REMARK 350 AND CHAINS: J, K, L, M, N, O, P, Q, R,
REMARK 350 AND CHAINS: S, T, U
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 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 NH1 ARG A 452 O HOH A 614 1.88
REMARK 500 OH TYR G 478 O HOH G 611 1.88
REMARK 500 NZ LYS I 425 O HOH I 540 1.90
REMARK 500 N GLU H 434 O HOH H 536 1.93
REMARK 500 OE1 GLU G 409 O HOH G 619 1.95
REMARK 500 NZ LYS M 425 O HOH M 532 2.06
REMARK 500 O3B ADP D 600 F2 AF3 D 602 2.08
REMARK 500 O2A ADP C 600 F1 AF3 C 602 2.10
REMARK 500 NH2 ARG L 421 O HOH L 537 2.10
REMARK 500 O2A ADP E 600 F1 AF3 E 602 2.11
REMARK 500 O THR C 125 O HOH C 609 2.12
REMARK 500 O2A ADP A 600 F1 AF3 A 602 2.12
REMARK 500 O3B ADP B 600 F2 AF3 B 602 2.15
REMARK 500 OD2 ASP N 87 O HOH N 530 2.17
REMARK 500 O ASP B 359 OE2 GLU B 363 2.18
REMARK 500 O ASP E 359 OE2 GLU E 363 2.18
REMARK 500 NH1 ARG D 452 O HOH D 609 2.18
REMARK 500 O1B ADP D 600 F2 AF3 D 602 2.19
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 PHE A 44 CE1 PHE A 44 CZ 0.114
REMARK 500 MET A 73 SD MET A 73 CE 0.493
REMARK 500 GLU A 76 CD GLU A 76 OE1 0.114
REMARK 500 GLU A 76 CD GLU A 76 OE2 0.114
REMARK 500 MET A 111 SD MET A 111 CE 0.355
REMARK 500 GLU A 129 CG GLU A 129 CD 0.114
REMARK 500 GLU A 129 CD GLU A 129 OE1 0.089
REMARK 500 GLU A 129 CD GLU A 129 OE2 0.093
REMARK 500 GLU A 130 CD GLU A 130 OE1 0.084
REMARK 500 GLU A 391 CD GLU A 391 OE1 0.074
REMARK 500 GLU A 434 CG GLU A 434 CD 0.104
REMARK 500 GLU A 434 CD GLU A 434 OE1 0.074
REMARK 500 GLU A 484 CD GLU A 484 OE2 0.086
REMARK 500 TYR A 506 CG TYR A 506 CD1 -0.092
REMARK 500 VAL A 510 CB VAL A 510 CG1 -0.137
REMARK 500 GLU B 76 CD GLU B 76 OE1 0.089
REMARK 500 GLU B 102 CG GLU B 102 CD 0.096
REMARK 500 MET B 111 SD MET B 111 CE 0.368
REMARK 500 GLU B 129 CG GLU B 129 CD 0.093
REMARK 500 GLU B 391 CD GLU B 391 OE1 0.073
REMARK 500 GLU B 483 CD GLU B 483 OE1 0.098
REMARK 500 GLU B 484 CD GLU B 484 OE2 0.071
REMARK 500 MET B 514 SD MET B 514 CE 0.433
REMARK 500 MET C 73 SD MET C 73 CE 0.547
REMARK 500 GLU C 76 CD GLU C 76 OE1 0.131
REMARK 500 ASP C 83 C ASP C 83 O 0.156
REMARK 500 VAL C 94 C VAL C 94 O 0.163
REMARK 500 GLN C 97 CB GLN C 97 CG -0.197
REMARK 500 GLU C 102 CG GLU C 102 CD 0.145
REMARK 500 GLU C 102 CD GLU C 102 OE1 0.082
REMARK 500 LYS C 105 CD LYS C 105 CE 0.164
REMARK 500 LYS C 105 C LYS C 105 O 0.114
REMARK 500 LYS C 117 CB LYS C 117 CG -0.203
REMARK 500 GLU C 129 CG GLU C 129 CD 0.111
REMARK 500 GLU C 129 CD GLU C 129 OE1 0.079
REMARK 500 GLU C 391 CD GLU C 391 OE1 0.071
REMARK 500 GLU C 397 CD GLU C 397 OE2 0.070
REMARK 500 ASP C 398 CB ASP C 398 CG 0.172
REMARK 500 ASP C 398 CG ASP C 398 OD1 0.138
REMARK 500 GLN C 432 CG GLN C 432 CD 0.141
REMARK 500 CYS C 458 CB CYS C 458 SG -0.112
REMARK 500 ALA C 511 CA ALA C 511 CB 0.140
REMARK 500 MET C 514 SD MET C 514 CE 0.356
REMARK 500 PHE D 44 CE1 PHE D 44 CZ 0.125
REMARK 500 MET D 73 SD MET D 73 CE 0.394
REMARK 500 VAL D 74 CB VAL D 74 CG1 -0.130
REMARK 500 GLU D 76 CD GLU D 76 OE1 0.090
REMARK 500 GLU D 102 CG GLU D 102 CD 0.107
REMARK 500 GLU D 102 CD GLU D 102 OE1 0.078
REMARK 500 GLU D 102 CD GLU D 102 OE2 0.068
REMARK 500
REMARK 500 THIS ENTRY HAS 147 BOND DEVIATIONS.
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 ASP A 11 CB - CG - OD2 ANGL. DEV. = 6.7 DEGREES
REMARK 500 ILE A 49 CG1 - CB - CG2 ANGL. DEV. = -15.2 DEGREES
REMARK 500 ASP A 64 CB - CG - OD2 ANGL. DEV. = 8.4 DEGREES
REMARK 500 LYS A 65 CD - CE - NZ ANGL. DEV. = -14.0 DEGREES
REMARK 500 ASP A 87 CB - CG - OD1 ANGL. DEV. = 6.5 DEGREES
REMARK 500 ASP A 115 CB - CG - OD2 ANGL. DEV. = 7.1 DEGREES
REMARK 500 LEU A 116 CB - CG - CD1 ANGL. DEV. = -11.0 DEGREES
REMARK 500 ASP A 121 CB - CG - OD1 ANGL. DEV. = 6.9 DEGREES
REMARK 500 CYS A 138 CA - CB - SG ANGL. DEV. = 9.2 DEGREES
REMARK 500 ASP A 188 CB - CG - OD2 ANGL. DEV. = 5.9 DEGREES
REMARK 500 ASP A 328 CB - CG - OD2 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ASP A 398 CB - CG - OD1 ANGL. DEV. = 7.1 DEGREES
REMARK 500 LEU A 419 CB - CG - CD2 ANGL. DEV. = -10.2 DEGREES
REMARK 500 ASP A 435 CB - CG - OD2 ANGL. DEV. = 6.0 DEGREES
REMARK 500 LEU A 444 CB - CG - CD1 ANGL. DEV. = -11.4 DEGREES
REMARK 500 ARG A 452 NE - CZ - NH1 ANGL. DEV. = -3.8 DEGREES
REMARK 500 ASP A 523 CB - CG - OD2 ANGL. DEV. = 8.2 DEGREES
REMARK 500 ASP B 11 CB - CG - OD1 ANGL. DEV. = -7.6 DEGREES
REMARK 500 ASP B 11 CB - CG - OD2 ANGL. DEV. = 6.3 DEGREES
REMARK 500 ASP B 25 CB - CG - OD1 ANGL. DEV. = -6.0 DEGREES
REMARK 500 ILE B 49 CG1 - CB - CG2 ANGL. DEV. = -13.2 DEGREES
REMARK 500 LEU B 62 CB - CG - CD2 ANGL. DEV. = -14.2 DEGREES
REMARK 500 ASP B 115 CB - CG - OD2 ANGL. DEV. = 7.8 DEGREES
REMARK 500 ARG B 118 NE - CZ - NH1 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ASP B 140 CB - CG - OD2 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ASP B 328 CB - CG - OD2 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ASP B 398 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 LEU B 419 CB - CG - CD2 ANGL. DEV. = -12.2 DEGREES
REMARK 500 ASP B 435 CB - CG - OD2 ANGL. DEV. = 6.1 DEGREES
REMARK 500 ASP C 41 CB - CG - OD2 ANGL. DEV. = 6.2 DEGREES
REMARK 500 ILE C 49 CG1 - CB - CG2 ANGL. DEV. = -14.5 DEGREES
REMARK 500 LEU C 62 CB - CG - CD2 ANGL. DEV. = -12.7 DEGREES
REMARK 500 ASP C 64 CB - CG - OD2 ANGL. DEV. = 6.0 DEGREES
REMARK 500 ASP C 87 CB - CG - OD1 ANGL. DEV. = 6.6 DEGREES
REMARK 500 ILE C 100 CG1 - CB - CG2 ANGL. DEV. = -14.8 DEGREES
REMARK 500 ASP C 121 CB - CG - OD1 ANGL. DEV. = 8.4 DEGREES
REMARK 500 LEU C 131 CB - CG - CD2 ANGL. DEV. = -13.2 DEGREES
REMARK 500 LEU C 134 CB - CG - CD2 ANGL. DEV. = -10.7 DEGREES
REMARK 500 ASP C 398 CB - CG - OD1 ANGL. DEV. = 8.8 DEGREES
REMARK 500 ASP C 490 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ARG C 501 NE - CZ - NH2 ANGL. DEV. = 3.2 DEGREES
REMARK 500 LEU C 513 CA - CB - CG ANGL. DEV. = -16.0 DEGREES
REMARK 500 MET C 514 CG - SD - CE ANGL. DEV. = -11.9 DEGREES
REMARK 500 ASP C 523 CB - CG - OD2 ANGL. DEV. = 6.7 DEGREES
REMARK 500 ASP D 11 CB - CG - OD1 ANGL. DEV. = -6.4 DEGREES
REMARK 500 ASP D 11 CB - CG - OD2 ANGL. DEV. = 6.7 DEGREES
REMARK 500 ASP D 64 CB - CG - OD2 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ASP D 121 CB - CG - OD1 ANGL. DEV. = 9.2 DEGREES
REMARK 500 ASP D 121 CB - CG - OD2 ANGL. DEV. = -7.0 DEGREES
REMARK 500 ASP D 188 CB - CG - OD2 ANGL. DEV. = 6.6 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 155 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 34 31.11 -96.06
REMARK 500 PHE A 44 -94.13 8.83
REMARK 500 ARG A 58 -15.61 -49.92
REMARK 500 ALA A 84 -61.29 -103.46
REMARK 500 ALA A 85 -72.81 -63.18
REMARK 500 SER A 139 -31.95 -132.62
REMARK 500 ALA A 152 39.19 -84.35
REMARK 500 PRO A 202 3.04 -52.91
REMARK 500 LYS A 225 159.41 160.34
REMARK 500 ARG A 268 21.10 -75.30
REMARK 500 LYS A 311 53.68 -93.09
REMARK 500 ASP A 328 26.14 -155.60
REMARK 500 ASP A 334 84.51 61.77
REMARK 500 ALA A 356 99.76 -66.18
REMARK 500 ALA A 373 -107.64 -77.45
REMARK 500 THR A 385 -150.48 -109.68
REMARK 500 PHE B 44 -95.04 8.26
REMARK 500 ALA B 85 -74.70 -72.57
REMARK 500 SER B 139 -35.61 -132.08
REMARK 500 ALA B 152 44.09 -88.06
REMARK 500 PRO B 202 4.67 -53.40
REMARK 500 PHE B 204 -35.86 -39.94
REMARK 500 LYS B 225 164.62 162.55
REMARK 500 GLU B 257 -70.25 -47.64
REMARK 500 ARG B 268 21.95 -74.92
REMARK 500 LYS B 311 54.97 -94.67
REMARK 500 ASP B 328 24.98 -151.40
REMARK 500 ASP B 334 83.42 61.51
REMARK 500 ALA B 356 99.22 -66.83
REMARK 500 ALA B 373 -105.18 -78.34
REMARK 500 THR B 385 -145.60 -103.68
REMARK 500 SER B 463 -53.94 -28.47
REMARK 500 LEU C 23 -74.05 -54.12
REMARK 500 LYS C 28 -40.87 -28.93
REMARK 500 PHE C 44 -96.48 4.53
REMARK 500 ARG C 58 -17.92 -42.81
REMARK 500 ALA C 84 -60.27 -101.51
REMARK 500 ALA C 85 -84.38 -69.73
REMARK 500 SER C 139 -32.58 -132.27
REMARK 500 ALA C 152 42.25 -87.93
REMARK 500 PRO C 202 3.20 -54.23
REMARK 500 LYS C 225 164.28 162.46
REMARK 500 ARG C 268 22.35 -75.22
REMARK 500 ILE C 270 -72.14 -69.02
REMARK 500 LYS C 311 51.35 -91.56
REMARK 500 ASP C 328 25.44 -151.54
REMARK 500 ASP C 334 86.03 61.93
REMARK 500 ALA C 356 99.57 -66.72
REMARK 500 ALA C 373 -103.54 -77.62
REMARK 500 THR C 385 -150.35 -112.28
REMARK 500
REMARK 500 THIS ENTRY HAS 377 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 SER A 43 PHE A 44 149.78
REMARK 500 GLY H 32 PRO H 33 143.83
REMARK 500 GLY I 32 PRO I 33 138.93
REMARK 500 GLY J 32 PRO J 33 148.19
REMARK 500 GLY K 32 PRO K 33 147.25
REMARK 500 GLY L 32 PRO L 33 146.83
REMARK 500 GLY M 32 PRO M 33 145.16
REMARK 500 GLY N 32 PRO N 33 148.58
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 VAL A 422 24.1 L L OUTSIDE RANGE
REMARK 500 ALA A 449 24.2 L L OUTSIDE RANGE
REMARK 500 VAL A 499 23.2 L L OUTSIDE RANGE
REMARK 500 THR B 468 24.2 L L OUTSIDE RANGE
REMARK 500 VAL B 499 20.4 L L OUTSIDE RANGE
REMARK 500 ALA C 449 24.3 L L OUTSIDE RANGE
REMARK 500 THR C 468 25.0 L L OUTSIDE RANGE
REMARK 500 VAL C 499 22.3 L L OUTSIDE RANGE
REMARK 500 VAL D 422 22.0 L L OUTSIDE RANGE
REMARK 500 ALA D 423 23.4 L L OUTSIDE RANGE
REMARK 500 VAL E 499 24.0 L L OUTSIDE RANGE
REMARK 500 VAL F 422 24.9 L L OUTSIDE RANGE
REMARK 500 THR F 468 23.4 L L OUTSIDE RANGE
REMARK 500 VAL F 499 21.6 L L OUTSIDE RANGE
REMARK 500 VAL G 499 20.8 L L OUTSIDE RANGE
REMARK 500 THR H 468 21.6 L L OUTSIDE RANGE
REMARK 500 ALA I 78 22.4 L L OUTSIDE RANGE
REMARK 500 LEU I 426 24.7 L L OUTSIDE RANGE
REMARK 500 THR I 468 24.0 L L OUTSIDE RANGE
REMARK 500 THR J 468 21.5 L L OUTSIDE RANGE
REMARK 500 THR K 468 23.8 L L OUTSIDE RANGE
REMARK 500 THR L 468 22.1 L L OUTSIDE RANGE
REMARK 500 THR M 468 23.6 L L OUTSIDE RANGE
REMARK 500 THR N 468 19.2 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 601 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ADP A 600 O1B
REMARK 620 2 ADP A 600 O2A 80.3
REMARK 620 3 AF3 A 602 F1 97.5 74.8
REMARK 620 4 ASP A 87 OD1 90.5 158.2 87.0
REMARK 620 5 AF3 A 602 AL 67.3 89.7 36.4 68.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 AF3 A 602 AL
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 87 OD1
REMARK 620 2 AF3 A 602 F1 66.8
REMARK 620 3 AF3 A 602 F2 55.7 113.5
REMARK 620 4 AF3 A 602 F3 143.6 135.1 111.2
REMARK 620 5 ADP A 600 O1B 58.5 62.1 61.0 150.9
REMARK 620 6 ADP A 600 O3B 106.9 114.5 61.0 89.8 61.5
REMARK 620 7 ADP A 600 O2A 76.9 33.2 99.5 138.6 38.6 81.3
REMARK 620 8 ADP A 600 O3A 103.9 73.4 89.8 110.2 45.7 43.6 41.2
REMARK 620 9 THR A 89 OG1 107.5 172.9 64.2 47.2 119.4 70.8 151.9 112.8
REMARK 620 N 1 2 3 4 5 6 7 8
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K A 603 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ADP A 600 O3A
REMARK 620 2 THR A 30 O 104.1
REMARK 620 3 ADP A 600 O1A 47.1 64.4
REMARK 620 4 LYS A 51 O 156.5 93.6 134.4
REMARK 620 5 AF3 A 602 F3 79.5 172.8 115.9 81.3
REMARK 620 6 THR A 30 OG1 134.2 67.1 127.2 67.0 114.9
REMARK 620 7 THR A 90 OG1 78.3 124.6 121.1 104.4 61.9 72.8
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 601 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ADP B 600 O1B
REMARK 620 2 ADP B 600 O2A 87.9
REMARK 620 3 ASP B 87 OD1 79.0 154.7
REMARK 620 4 AF3 B 602 F1 83.7 74.2 82.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 AF3 B 602 AL
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ADP B 600 O3B
REMARK 620 2 AF3 B 602 F1 113.7
REMARK 620 3 AF3 B 602 F2 68.4 122.2
REMARK 620 4 AF3 B 602 F3 82.3 136.4 101.3
REMARK 620 5 MG B 601 MG 96.3 26.7 97.7 158.8
REMARK 620 6 ADP B 600 O2A 88.0 26.0 118.3 132.1 27.0
REMARK 620 7 ASP B 87 OD1 106.7 64.6 60.6 152.5 48.0 74.9
REMARK 620 8 THR B 89 OG1 69.4 165.4 44.3 57.1 141.9 155.1 100.9
REMARK 620 9 ADP B 600 O1B 65.7 56.2 78.4 145.9 31.9 40.4 55.7 116.9
REMARK 620 10 ADP B 600 O3A 48.3 69.3 107.5 101.4 63.7 43.7 103.8 117.1
REMARK 620 48.5
REMARK 620 11 K B 603 K 84.8 80.8 149.6 59.7 99.1 72.8 145.3 113.8
REMARK 620 103.9 59.2
REMARK 620 N 1 2 3 4 5 6 7 8
REMARK 620 9 10
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K B 603 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ADP B 600 O1A
REMARK 620 2 ADP B 600 O3A 47.4
REMARK 620 3 LYS B 51 O 141.4 158.4
REMARK 620 4 AF3 B 602 F3 117.2 75.9 84.6
REMARK 620 5 THR B 30 O 65.4 103.9 96.4 173.7
REMARK 620 6 THR B 30 OG1 122.9 123.4 71.5 108.6 66.0
REMARK 620 7 THR B 90 OG1 113.9 70.3 104.6 51.4 122.5 71.1
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C 601 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ADP C 600 O1B
REMARK 620 2 ADP C 600 O2A 86.4
REMARK 620 3 ASP C 87 OD1 73.5 156.0
REMARK 620 4 AF3 C 602 F1 94.9 74.7 93.7
REMARK 620 5 AF3 C 602 AL 64.2 85.7 73.9 33.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 AF3 C 602 AL
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ADP C 600 O3B
REMARK 620 2 AF3 C 602 F1 120.4
REMARK 620 3 AF3 C 602 F2 55.8 114.8
REMARK 620 4 AF3 C 602 F3 84.2 139.2 105.9
REMARK 620 5 ADP C 600 O3A 50.1 76.3 94.1 103.8
REMARK 620 6 ADP C 600 O2A 89.5 33.2 108.8 132.5 43.2
REMARK 620 7 ASP C 87 OD1 96.4 62.4 55.0 153.2 96.8 74.2
REMARK 620 8 ADP C 600 O1B 63.3 62.4 63.3 146.5 49.6 45.5 47.6
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K C 603 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ADP C 600 O3A
REMARK 620 2 ADP C 600 O1A 46.0
REMARK 620 3 AF3 C 602 F3 74.6 113.6
REMARK 620 4 THR C 90 OG1 69.8 112.5 52.6
REMARK 620 5 THR C 30 OG1 129.2 132.3 105.5 71.4
REMARK 620 6 LYS C 51 NZ 95.4 52.3 128.6 164.8 118.3
REMARK 620 7 LYS C 51 O 150.0 143.6 77.7 101.8 69.6 92.9
REMARK 620 8 THR C 30 O 107.8 69.0 177.4 126.9 72.2 52.7 100.1
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D 601 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ADP D 600 O2A
REMARK 620 2 ADP D 600 O1B 102.3
REMARK 620 3 ASP D 87 OD1 165.0 77.2
REMARK 620 4 AF3 D 602 F1 73.7 100.6 91.6
REMARK 620 5 AF3 D 602 AL 94.2 66.1 71.8 37.0
REMARK 620 6 AF3 D 602 F2 119.6 41.6 50.6 71.4 35.1
REMARK 620 7 HOH D 611 O 124.8 127.3 51.1 74.7 86.4 90.6
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 AF3 D 602 AL
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ADP D 600 O3B
REMARK 620 2 AF3 D 602 F1 116.5
REMARK 620 3 AF3 D 602 F2 63.9 110.2
REMARK 620 4 AF3 D 602 F3 84.1 137.2 112.5
REMARK 620 5 ADP D 600 O3A 46.4 71.7 89.8 109.4
REMARK 620 6 THR D 89 OG1 70.0 172.4 68.3 44.7 115.5
REMARK 620 7 ADP D 600 O2A 88.6 27.9 98.1 141.0 45.0 158.0
REMARK 620 8 ADP D 600 O1B 65.4 64.6 53.4 149.5 50.3 117.3 45.1
REMARK 620 9 ASP D 87 OD1 106.5 68.8 49.8 144.5 101.7 106.2 74.2 52.1
REMARK 620 N 1 2 3 4 5 6 7 8
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K D 603 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ADP D 600 O3A
REMARK 620 2 THR D 90 OG1 69.7
REMARK 620 3 AF3 D 602 F3 76.2 57.6
REMARK 620 4 ADP D 600 O1A 45.9 111.7 113.9
REMARK 620 5 THR D 30 O 100.6 116.9 174.2 65.6
REMARK 620 6 THR D 30 OG1 120.9 68.7 112.3 122.7 65.0
REMARK 620 7 LYS D 51 O 160.4 104.2 84.8 144.0 98.7 70.9
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG E 601 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ADP E 600 O1B
REMARK 620 2 ADP E 600 O2A 95.0
REMARK 620 3 HOH E 608 O 143.0 121.7
REMARK 620 4 AF3 E 602 F1 101.9 75.8 84.6
REMARK 620 5 ASP E 87 OD1 83.2 166.9 60.0 91.8
REMARK 620 6 AF3 E 602 AL 69.3 95.2 100.4 36.7 71.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 AF3 E 602 AL
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP E 87 OD1
REMARK 620 2 AF3 E 602 F1 68.1
REMARK 620 3 AF3 E 602 F2 52.2 118.7
REMARK 620 4 AF3 E 602 F3 153.9 133.4 107.8
REMARK 620 5 ADP E 600 O2A 74.0 29.7 111.3 132.1
REMARK 620 6 ADP E 600 O1B 53.4 64.4 69.8 142.4 43.0
REMARK 620 7 ADP E 600 O3A 101.6 72.1 105.0 100.0 43.7 48.8
REMARK 620 8 THR E 89 OG1 103.6 169.9 54.9 53.2 155.8 115.8 116.1
REMARK 620 9 ADP E 600 O3B 105.1 116.1 72.5 79.9 86.4 63.4 46.1 70.8
REMARK 620 N 1 2 3 4 5 6 7 8
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K E 603 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ADP E 600 O1A
REMARK 620 2 ADP E 600 O3A 44.4
REMARK 620 3 THR E 90 OG1 108.3 68.1
REMARK 620 4 THR E 30 OG1 124.0 124.2 72.1
REMARK 620 5 THR E 30 O 63.4 100.4 122.0 70.0
REMARK 620 6 AF3 E 602 F3 109.9 70.9 52.4 111.7 170.7
REMARK 620 7 LYS E 51 O 139.3 155.5 111.8 76.2 99.8 89.5
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG F 601 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ADP F 600 O2A
REMARK 620 2 ADP F 600 O1B 84.3
REMARK 620 3 AF3 F 602 F1 74.5 97.5
REMARK 620 4 ASP F 87 OD1 155.3 78.1 90.7
REMARK 620 5 AF3 F 602 AL 88.6 65.4 36.4 68.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 AF3 F 602 AL
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP F 87 OD1
REMARK 620 2 AF3 F 602 F1 69.1
REMARK 620 3 AF3 F 602 F2 51.0 117.4
REMARK 620 4 AF3 F 602 F3 150.8 134.9 107.6
REMARK 620 5 ADP F 600 O1B 53.4 64.1 66.6 143.9
REMARK 620 6 ADP F 600 O3B 100.8 116.1 66.0 83.5 61.3
REMARK 620 7 ADP F 600 O2A 74.7 32.1 106.8 134.4 40.9 84.0
REMARK 620 8 ADP F 600 O3A 98.8 73.8 97.0 104.0 45.6 44.6 42.6
REMARK 620 9 THR F 89 OG1 106.2 172.9 60.0 47.9 117.9 69.5 153.3 112.7
REMARK 620 10 K F 603 K 145.1 78.4 147.9 63.9 101.3 82.1 71.0 59.0
REMARK 620 107.2
REMARK 620 N 1 2 3 4 5 6 7 8
REMARK 620 9
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K F 603 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ADP F 600 O1A
REMARK 620 2 ADP F 600 O3A 46.1
REMARK 620 3 THR F 90 OG1 112.1 71.5
REMARK 620 4 THR F 30 OG1 118.8 119.2 66.1
REMARK 620 5 THR F 30 O 64.5 99.2 111.8 61.7
REMARK 620 6 AF3 F 602 F3 117.1 78.3 59.9 112.4 171.7
REMARK 620 7 LYS F 51 O 144.6 166.8 101.7 65.6 93.8 88.5
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG G 601 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ADP G 600 O2A
REMARK 620 2 ADP G 600 O1B 87.7
REMARK 620 3 AF3 G 602 F1 73.5 98.6
REMARK 620 4 ASP G 87 OD1 162.4 85.8 91.4
REMARK 620 5 AF3 G 602 AL 89.7 66.3 36.7 72.7
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 AF3 G 602 AL
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR G 89 OG1
REMARK 620 2 AF3 G 602 F1 169.3
REMARK 620 3 AF3 G 602 F2 53.5 118.5
REMARK 620 4 AF3 G 602 F3 55.8 132.7 108.8
REMARK 620 5 ADP G 600 O3B 70.9 114.5 69.2 81.4
REMARK 620 6 ADP G 600 O3A 115.2 72.0 101.5 99.7 45.0
REMARK 620 7 ASP G 87 OD1 106.4 63.4 58.2 157.1 107.7 101.4
REMARK 620 8 ADP G 600 O1B 115.4 62.8 69.3 142.1 62.1 47.2 55.4
REMARK 620 9 HOH G 618 O 51.7 120.0 65.6 78.8 120.6 165.1 78.6 127.7
REMARK 620 10 ADP G 600 O2A 154.4 30.5 112.4 127.6 84.3 41.8 74.9 43.7
REMARK 620 148.3
REMARK 620 N 1 2 3 4 5 6 7 8
REMARK 620 9
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K G 603 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR G 30 OG1
REMARK 620 2 THR G 30 O 64.3
REMARK 620 3 LYS G 51 O 72.8 95.0
REMARK 620 4 ADP G 600 O1A 120.3 62.7 136.1
REMARK 620 5 AF3 G 602 F3 118.3 176.8 87.7 114.1
REMARK 620 6 ADP G 600 O3A 125.1 100.0 160.5 45.7 77.0
REMARK 620 7 THR G 90 OG1 77.0 123.7 111.2 112.6 56.5 70.2
REMARK 620 N 1 2 3 4 5 6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K B 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K C 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K D 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG E 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K E 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG F 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K F 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG G 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K G 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AF3 A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP B 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AF3 B 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP C 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AF3 C 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP D 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AF3 D 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP E 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AF3 E 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP F 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AF3 F 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP G 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AF3 G 602
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1PCQ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF GROEL-GROES-ADP-ALFX
DBREF 1SVT A 2 525 UNP P0A6F5 CH60_ECOLI 1 524
DBREF 1SVT B 2 525 UNP P0A6F5 CH60_ECOLI 1 524
DBREF 1SVT C 2 525 UNP P0A6F5 CH60_ECOLI 1 524
DBREF 1SVT D 2 525 UNP P0A6F5 CH60_ECOLI 1 524
DBREF 1SVT E 2 525 UNP P0A6F5 CH60_ECOLI 1 524
DBREF 1SVT F 2 525 UNP P0A6F5 CH60_ECOLI 1 524
DBREF 1SVT G 2 525 UNP P0A6F5 CH60_ECOLI 1 524
DBREF 1SVT H 2 525 UNP P0A6F5 CH60_ECOLI 1 524
DBREF 1SVT I 2 525 UNP P0A6F5 CH60_ECOLI 1 524
DBREF 1SVT J 2 525 UNP P0A6F5 CH60_ECOLI 1 524
DBREF 1SVT K 2 525 UNP P0A6F5 CH60_ECOLI 1 524
DBREF 1SVT L 2 525 UNP P0A6F5 CH60_ECOLI 1 524
DBREF 1SVT M 2 525 UNP P0A6F5 CH60_ECOLI 1 524
DBREF 1SVT N 2 525 UNP P0A6F5 CH60_ECOLI 1 524
DBREF 1SVT O 1 97 UNP P0A6F9 CH10_ECOLI 1 97
DBREF 1SVT P 1 97 UNP P0A6F9 CH10_ECOLI 1 97
DBREF 1SVT Q 1 97 UNP P0A6F9 CH10_ECOLI 1 97
DBREF 1SVT R 1 97 UNP P0A6F9 CH10_ECOLI 1 97
DBREF 1SVT S 1 97 UNP P0A6F9 CH10_ECOLI 1 97
DBREF 1SVT T 1 97 UNP P0A6F9 CH10_ECOLI 1 97
DBREF 1SVT U 1 97 UNP P0A6F9 CH10_ECOLI 1 97
SEQRES 1 A 524 ALA ALA LYS ASP VAL LYS PHE GLY ASN ASP ALA ARG VAL
SEQRES 2 A 524 LYS MET LEU ARG GLY VAL ASN VAL LEU ALA ASP ALA VAL
SEQRES 3 A 524 LYS VAL THR LEU GLY PRO LYS GLY ARG ASN VAL VAL LEU
SEQRES 4 A 524 ASP LYS SER PHE GLY ALA PRO THR ILE THR LYS ASP GLY
SEQRES 5 A 524 VAL SER VAL ALA ARG GLU ILE GLU LEU GLU ASP LYS PHE
SEQRES 6 A 524 GLU ASN MET GLY ALA GLN MET VAL LYS GLU VAL ALA SER
SEQRES 7 A 524 LYS ALA ASN ASP ALA ALA GLY ASP GLY THR THR THR ALA
SEQRES 8 A 524 THR VAL LEU ALA GLN ALA ILE ILE THR GLU GLY LEU LYS
SEQRES 9 A 524 ALA VAL ALA ALA GLY MET ASN PRO MET ASP LEU LYS ARG
SEQRES 10 A 524 GLY ILE ASP LYS ALA VAL THR ALA ALA VAL GLU GLU LEU
SEQRES 11 A 524 LYS ALA LEU SER VAL PRO CYS SER ASP SER LYS ALA ILE
SEQRES 12 A 524 ALA GLN VAL GLY THR ILE SER ALA ASN SER ASP GLU THR
SEQRES 13 A 524 VAL GLY LYS LEU ILE ALA GLU ALA MET ASP LYS VAL GLY
SEQRES 14 A 524 LYS GLU GLY VAL ILE THR VAL GLU ASP GLY THR GLY LEU
SEQRES 15 A 524 GLN ASP GLU LEU ASP VAL VAL GLU GLY MET GLN PHE ASP
SEQRES 16 A 524 ARG GLY TYR LEU SER PRO TYR PHE ILE ASN LYS PRO GLU
SEQRES 17 A 524 THR GLY ALA VAL GLU LEU GLU SER PRO PHE ILE LEU LEU
SEQRES 18 A 524 ALA ASP LYS LYS ILE SER ASN ILE ARG GLU MET LEU PRO
SEQRES 19 A 524 VAL LEU GLU ALA VAL ALA LYS ALA GLY LYS PRO LEU LEU
SEQRES 20 A 524 ILE ILE ALA GLU ASP VAL GLU GLY GLU ALA LEU ALA THR
SEQRES 21 A 524 LEU VAL VAL ASN THR MET ARG GLY ILE VAL LYS VAL ALA
SEQRES 22 A 524 ALA VAL LYS ALA PRO GLY PHE GLY ASP ARG ARG LYS ALA
SEQRES 23 A 524 MET LEU GLN ASP ILE ALA THR LEU THR GLY GLY THR VAL
SEQRES 24 A 524 ILE SER GLU GLU ILE GLY MET GLU LEU GLU LYS ALA THR
SEQRES 25 A 524 LEU GLU ASP LEU GLY GLN ALA LYS ARG VAL VAL ILE ASN
SEQRES 26 A 524 LYS ASP THR THR THR ILE ILE ASP GLY VAL GLY GLU GLU
SEQRES 27 A 524 ALA ALA ILE GLN GLY ARG VAL ALA GLN ILE ARG GLN GLN
SEQRES 28 A 524 ILE GLU GLU ALA THR SER ASP TYR ASP ARG GLU LYS LEU
SEQRES 29 A 524 GLN GLU ARG VAL ALA LYS LEU ALA GLY GLY VAL ALA VAL
SEQRES 30 A 524 ILE LYS VAL GLY ALA ALA THR GLU VAL GLU MET LYS GLU
SEQRES 31 A 524 LYS LYS ALA ARG VAL GLU ASP ALA LEU HIS ALA THR ARG
SEQRES 32 A 524 ALA ALA VAL GLU GLU GLY VAL VAL ALA GLY GLY GLY VAL
SEQRES 33 A 524 ALA LEU ILE ARG VAL ALA SER LYS LEU ALA ASP LEU ARG
SEQRES 34 A 524 GLY GLN ASN GLU ASP GLN ASN VAL GLY ILE LYS VAL ALA
SEQRES 35 A 524 LEU ARG ALA MET GLU ALA PRO LEU ARG GLN ILE VAL LEU
SEQRES 36 A 524 ASN CYS GLY GLU GLU PRO SER VAL VAL ALA ASN THR VAL
SEQRES 37 A 524 LYS GLY GLY ASP GLY ASN TYR GLY TYR ASN ALA ALA THR
SEQRES 38 A 524 GLU GLU TYR GLY ASN MET ILE ASP MET GLY ILE LEU ASP
SEQRES 39 A 524 PRO THR LYS VAL THR ARG SER ALA LEU GLN TYR ALA ALA
SEQRES 40 A 524 SER VAL ALA GLY LEU MET ILE THR THR GLU CYS MET VAL
SEQRES 41 A 524 THR ASP LEU PRO
SEQRES 1 B 524 ALA ALA LYS ASP VAL LYS PHE GLY ASN ASP ALA ARG VAL
SEQRES 2 B 524 LYS MET LEU ARG GLY VAL ASN VAL LEU ALA ASP ALA VAL
SEQRES 3 B 524 LYS VAL THR LEU GLY PRO LYS GLY ARG ASN VAL VAL LEU
SEQRES 4 B 524 ASP LYS SER PHE GLY ALA PRO THR ILE THR LYS ASP GLY
SEQRES 5 B 524 VAL SER VAL ALA ARG GLU ILE GLU LEU GLU ASP LYS PHE
SEQRES 6 B 524 GLU ASN MET GLY ALA GLN MET VAL LYS GLU VAL ALA SER
SEQRES 7 B 524 LYS ALA ASN ASP ALA ALA GLY ASP GLY THR THR THR ALA
SEQRES 8 B 524 THR VAL LEU ALA GLN ALA ILE ILE THR GLU GLY LEU LYS
SEQRES 9 B 524 ALA VAL ALA ALA GLY MET ASN PRO MET ASP LEU LYS ARG
SEQRES 10 B 524 GLY ILE ASP LYS ALA VAL THR ALA ALA VAL GLU GLU LEU
SEQRES 11 B 524 LYS ALA LEU SER VAL PRO CYS SER ASP SER LYS ALA ILE
SEQRES 12 B 524 ALA GLN VAL GLY THR ILE SER ALA ASN SER ASP GLU THR
SEQRES 13 B 524 VAL GLY LYS LEU ILE ALA GLU ALA MET ASP LYS VAL GLY
SEQRES 14 B 524 LYS GLU GLY VAL ILE THR VAL GLU ASP GLY THR GLY LEU
SEQRES 15 B 524 GLN ASP GLU LEU ASP VAL VAL GLU GLY MET GLN PHE ASP
SEQRES 16 B 524 ARG GLY TYR LEU SER PRO TYR PHE ILE ASN LYS PRO GLU
SEQRES 17 B 524 THR GLY ALA VAL GLU LEU GLU SER PRO PHE ILE LEU LEU
SEQRES 18 B 524 ALA ASP LYS LYS ILE SER ASN ILE ARG GLU MET LEU PRO
SEQRES 19 B 524 VAL LEU GLU ALA VAL ALA LYS ALA GLY LYS PRO LEU LEU
SEQRES 20 B 524 ILE ILE ALA GLU ASP VAL GLU GLY GLU ALA LEU ALA THR
SEQRES 21 B 524 LEU VAL VAL ASN THR MET ARG GLY ILE VAL LYS VAL ALA
SEQRES 22 B 524 ALA VAL LYS ALA PRO GLY PHE GLY ASP ARG ARG LYS ALA
SEQRES 23 B 524 MET LEU GLN ASP ILE ALA THR LEU THR GLY GLY THR VAL
SEQRES 24 B 524 ILE SER GLU GLU ILE GLY MET GLU LEU GLU LYS ALA THR
SEQRES 25 B 524 LEU GLU ASP LEU GLY GLN ALA LYS ARG VAL VAL ILE ASN
SEQRES 26 B 524 LYS ASP THR THR THR ILE ILE ASP GLY VAL GLY GLU GLU
SEQRES 27 B 524 ALA ALA ILE GLN GLY ARG VAL ALA GLN ILE ARG GLN GLN
SEQRES 28 B 524 ILE GLU GLU ALA THR SER ASP TYR ASP ARG GLU LYS LEU
SEQRES 29 B 524 GLN GLU ARG VAL ALA LYS LEU ALA GLY GLY VAL ALA VAL
SEQRES 30 B 524 ILE LYS VAL GLY ALA ALA THR GLU VAL GLU MET LYS GLU
SEQRES 31 B 524 LYS LYS ALA ARG VAL GLU ASP ALA LEU HIS ALA THR ARG
SEQRES 32 B 524 ALA ALA VAL GLU GLU GLY VAL VAL ALA GLY GLY GLY VAL
SEQRES 33 B 524 ALA LEU ILE ARG VAL ALA SER LYS LEU ALA ASP LEU ARG
SEQRES 34 B 524 GLY GLN ASN GLU ASP GLN ASN VAL GLY ILE LYS VAL ALA
SEQRES 35 B 524 LEU ARG ALA MET GLU ALA PRO LEU ARG GLN ILE VAL LEU
SEQRES 36 B 524 ASN CYS GLY GLU GLU PRO SER VAL VAL ALA ASN THR VAL
SEQRES 37 B 524 LYS GLY GLY ASP GLY ASN TYR GLY TYR ASN ALA ALA THR
SEQRES 38 B 524 GLU GLU TYR GLY ASN MET ILE ASP MET GLY ILE LEU ASP
SEQRES 39 B 524 PRO THR LYS VAL THR ARG SER ALA LEU GLN TYR ALA ALA
SEQRES 40 B 524 SER VAL ALA GLY LEU MET ILE THR THR GLU CYS MET VAL
SEQRES 41 B 524 THR ASP LEU PRO
SEQRES 1 C 524 ALA ALA LYS ASP VAL LYS PHE GLY ASN ASP ALA ARG VAL
SEQRES 2 C 524 LYS MET LEU ARG GLY VAL ASN VAL LEU ALA ASP ALA VAL
SEQRES 3 C 524 LYS VAL THR LEU GLY PRO LYS GLY ARG ASN VAL VAL LEU
SEQRES 4 C 524 ASP LYS SER PHE GLY ALA PRO THR ILE THR LYS ASP GLY
SEQRES 5 C 524 VAL SER VAL ALA ARG GLU ILE GLU LEU GLU ASP LYS PHE
SEQRES 6 C 524 GLU ASN MET GLY ALA GLN MET VAL LYS GLU VAL ALA SER
SEQRES 7 C 524 LYS ALA ASN ASP ALA ALA GLY ASP GLY THR THR THR ALA
SEQRES 8 C 524 THR VAL LEU ALA GLN ALA ILE ILE THR GLU GLY LEU LYS
SEQRES 9 C 524 ALA VAL ALA ALA GLY MET ASN PRO MET ASP LEU LYS ARG
SEQRES 10 C 524 GLY ILE ASP LYS ALA VAL THR ALA ALA VAL GLU GLU LEU
SEQRES 11 C 524 LYS ALA LEU SER VAL PRO CYS SER ASP SER LYS ALA ILE
SEQRES 12 C 524 ALA GLN VAL GLY THR ILE SER ALA ASN SER ASP GLU THR
SEQRES 13 C 524 VAL GLY LYS LEU ILE ALA GLU ALA MET ASP LYS VAL GLY
SEQRES 14 C 524 LYS GLU GLY VAL ILE THR VAL GLU ASP GLY THR GLY LEU
SEQRES 15 C 524 GLN ASP GLU LEU ASP VAL VAL GLU GLY MET GLN PHE ASP
SEQRES 16 C 524 ARG GLY TYR LEU SER PRO TYR PHE ILE ASN LYS PRO GLU
SEQRES 17 C 524 THR GLY ALA VAL GLU LEU GLU SER PRO PHE ILE LEU LEU
SEQRES 18 C 524 ALA ASP LYS LYS ILE SER ASN ILE ARG GLU MET LEU PRO
SEQRES 19 C 524 VAL LEU GLU ALA VAL ALA LYS ALA GLY LYS PRO LEU LEU
SEQRES 20 C 524 ILE ILE ALA GLU ASP VAL GLU GLY GLU ALA LEU ALA THR
SEQRES 21 C 524 LEU VAL VAL ASN THR MET ARG GLY ILE VAL LYS VAL ALA
SEQRES 22 C 524 ALA VAL LYS ALA PRO GLY PHE GLY ASP ARG ARG LYS ALA
SEQRES 23 C 524 MET LEU GLN ASP ILE ALA THR LEU THR GLY GLY THR VAL
SEQRES 24 C 524 ILE SER GLU GLU ILE GLY MET GLU LEU GLU LYS ALA THR
SEQRES 25 C 524 LEU GLU ASP LEU GLY GLN ALA LYS ARG VAL VAL ILE ASN
SEQRES 26 C 524 LYS ASP THR THR THR ILE ILE ASP GLY VAL GLY GLU GLU
SEQRES 27 C 524 ALA ALA ILE GLN GLY ARG VAL ALA GLN ILE ARG GLN GLN
SEQRES 28 C 524 ILE GLU GLU ALA THR SER ASP TYR ASP ARG GLU LYS LEU
SEQRES 29 C 524 GLN GLU ARG VAL ALA LYS LEU ALA GLY GLY VAL ALA VAL
SEQRES 30 C 524 ILE LYS VAL GLY ALA ALA THR GLU VAL GLU MET LYS GLU
SEQRES 31 C 524 LYS LYS ALA ARG VAL GLU ASP ALA LEU HIS ALA THR ARG
SEQRES 32 C 524 ALA ALA VAL GLU GLU GLY VAL VAL ALA GLY GLY GLY VAL
SEQRES 33 C 524 ALA LEU ILE ARG VAL ALA SER LYS LEU ALA ASP LEU ARG
SEQRES 34 C 524 GLY GLN ASN GLU ASP GLN ASN VAL GLY ILE LYS VAL ALA
SEQRES 35 C 524 LEU ARG ALA MET GLU ALA PRO LEU ARG GLN ILE VAL LEU
SEQRES 36 C 524 ASN CYS GLY GLU GLU PRO SER VAL VAL ALA ASN THR VAL
SEQRES 37 C 524 LYS GLY GLY ASP GLY ASN TYR GLY TYR ASN ALA ALA THR
SEQRES 38 C 524 GLU GLU TYR GLY ASN MET ILE ASP MET GLY ILE LEU ASP
SEQRES 39 C 524 PRO THR LYS VAL THR ARG SER ALA LEU GLN TYR ALA ALA
SEQRES 40 C 524 SER VAL ALA GLY LEU MET ILE THR THR GLU CYS MET VAL
SEQRES 41 C 524 THR ASP LEU PRO
SEQRES 1 D 524 ALA ALA LYS ASP VAL LYS PHE GLY ASN ASP ALA ARG VAL
SEQRES 2 D 524 LYS MET LEU ARG GLY VAL ASN VAL LEU ALA ASP ALA VAL
SEQRES 3 D 524 LYS VAL THR LEU GLY PRO LYS GLY ARG ASN VAL VAL LEU
SEQRES 4 D 524 ASP LYS SER PHE GLY ALA PRO THR ILE THR LYS ASP GLY
SEQRES 5 D 524 VAL SER VAL ALA ARG GLU ILE GLU LEU GLU ASP LYS PHE
SEQRES 6 D 524 GLU ASN MET GLY ALA GLN MET VAL LYS GLU VAL ALA SER
SEQRES 7 D 524 LYS ALA ASN ASP ALA ALA GLY ASP GLY THR THR THR ALA
SEQRES 8 D 524 THR VAL LEU ALA GLN ALA ILE ILE THR GLU GLY LEU LYS
SEQRES 9 D 524 ALA VAL ALA ALA GLY MET ASN PRO MET ASP LEU LYS ARG
SEQRES 10 D 524 GLY ILE ASP LYS ALA VAL THR ALA ALA VAL GLU GLU LEU
SEQRES 11 D 524 LYS ALA LEU SER VAL PRO CYS SER ASP SER LYS ALA ILE
SEQRES 12 D 524 ALA GLN VAL GLY THR ILE SER ALA ASN SER ASP GLU THR
SEQRES 13 D 524 VAL GLY LYS LEU ILE ALA GLU ALA MET ASP LYS VAL GLY
SEQRES 14 D 524 LYS GLU GLY VAL ILE THR VAL GLU ASP GLY THR GLY LEU
SEQRES 15 D 524 GLN ASP GLU LEU ASP VAL VAL GLU GLY MET GLN PHE ASP
SEQRES 16 D 524 ARG GLY TYR LEU SER PRO TYR PHE ILE ASN LYS PRO GLU
SEQRES 17 D 524 THR GLY ALA VAL GLU LEU GLU SER PRO PHE ILE LEU LEU
SEQRES 18 D 524 ALA ASP LYS LYS ILE SER ASN ILE ARG GLU MET LEU PRO
SEQRES 19 D 524 VAL LEU GLU ALA VAL ALA LYS ALA GLY LYS PRO LEU LEU
SEQRES 20 D 524 ILE ILE ALA GLU ASP VAL GLU GLY GLU ALA LEU ALA THR
SEQRES 21 D 524 LEU VAL VAL ASN THR MET ARG GLY ILE VAL LYS VAL ALA
SEQRES 22 D 524 ALA VAL LYS ALA PRO GLY PHE GLY ASP ARG ARG LYS ALA
SEQRES 23 D 524 MET LEU GLN ASP ILE ALA THR LEU THR GLY GLY THR VAL
SEQRES 24 D 524 ILE SER GLU GLU ILE GLY MET GLU LEU GLU LYS ALA THR
SEQRES 25 D 524 LEU GLU ASP LEU GLY GLN ALA LYS ARG VAL VAL ILE ASN
SEQRES 26 D 524 LYS ASP THR THR THR ILE ILE ASP GLY VAL GLY GLU GLU
SEQRES 27 D 524 ALA ALA ILE GLN GLY ARG VAL ALA GLN ILE ARG GLN GLN
SEQRES 28 D 524 ILE GLU GLU ALA THR SER ASP TYR ASP ARG GLU LYS LEU
SEQRES 29 D 524 GLN GLU ARG VAL ALA LYS LEU ALA GLY GLY VAL ALA VAL
SEQRES 30 D 524 ILE LYS VAL GLY ALA ALA THR GLU VAL GLU MET LYS GLU
SEQRES 31 D 524 LYS LYS ALA ARG VAL GLU ASP ALA LEU HIS ALA THR ARG
SEQRES 32 D 524 ALA ALA VAL GLU GLU GLY VAL VAL ALA GLY GLY GLY VAL
SEQRES 33 D 524 ALA LEU ILE ARG VAL ALA SER LYS LEU ALA ASP LEU ARG
SEQRES 34 D 524 GLY GLN ASN GLU ASP GLN ASN VAL GLY ILE LYS VAL ALA
SEQRES 35 D 524 LEU ARG ALA MET GLU ALA PRO LEU ARG GLN ILE VAL LEU
SEQRES 36 D 524 ASN CYS GLY GLU GLU PRO SER VAL VAL ALA ASN THR VAL
SEQRES 37 D 524 LYS GLY GLY ASP GLY ASN TYR GLY TYR ASN ALA ALA THR
SEQRES 38 D 524 GLU GLU TYR GLY ASN MET ILE ASP MET GLY ILE LEU ASP
SEQRES 39 D 524 PRO THR LYS VAL THR ARG SER ALA LEU GLN TYR ALA ALA
SEQRES 40 D 524 SER VAL ALA GLY LEU MET ILE THR THR GLU CYS MET VAL
SEQRES 41 D 524 THR ASP LEU PRO
SEQRES 1 E 524 ALA ALA LYS ASP VAL LYS PHE GLY ASN ASP ALA ARG VAL
SEQRES 2 E 524 LYS MET LEU ARG GLY VAL ASN VAL LEU ALA ASP ALA VAL
SEQRES 3 E 524 LYS VAL THR LEU GLY PRO LYS GLY ARG ASN VAL VAL LEU
SEQRES 4 E 524 ASP LYS SER PHE GLY ALA PRO THR ILE THR LYS ASP GLY
SEQRES 5 E 524 VAL SER VAL ALA ARG GLU ILE GLU LEU GLU ASP LYS PHE
SEQRES 6 E 524 GLU ASN MET GLY ALA GLN MET VAL LYS GLU VAL ALA SER
SEQRES 7 E 524 LYS ALA ASN ASP ALA ALA GLY ASP GLY THR THR THR ALA
SEQRES 8 E 524 THR VAL LEU ALA GLN ALA ILE ILE THR GLU GLY LEU LYS
SEQRES 9 E 524 ALA VAL ALA ALA GLY MET ASN PRO MET ASP LEU LYS ARG
SEQRES 10 E 524 GLY ILE ASP LYS ALA VAL THR ALA ALA VAL GLU GLU LEU
SEQRES 11 E 524 LYS ALA LEU SER VAL PRO CYS SER ASP SER LYS ALA ILE
SEQRES 12 E 524 ALA GLN VAL GLY THR ILE SER ALA ASN SER ASP GLU THR
SEQRES 13 E 524 VAL GLY LYS LEU ILE ALA GLU ALA MET ASP LYS VAL GLY
SEQRES 14 E 524 LYS GLU GLY VAL ILE THR VAL GLU ASP GLY THR GLY LEU
SEQRES 15 E 524 GLN ASP GLU LEU ASP VAL VAL GLU GLY MET GLN PHE ASP
SEQRES 16 E 524 ARG GLY TYR LEU SER PRO TYR PHE ILE ASN LYS PRO GLU
SEQRES 17 E 524 THR GLY ALA VAL GLU LEU GLU SER PRO PHE ILE LEU LEU
SEQRES 18 E 524 ALA ASP LYS LYS ILE SER ASN ILE ARG GLU MET LEU PRO
SEQRES 19 E 524 VAL LEU GLU ALA VAL ALA LYS ALA GLY LYS PRO LEU LEU
SEQRES 20 E 524 ILE ILE ALA GLU ASP VAL GLU GLY GLU ALA LEU ALA THR
SEQRES 21 E 524 LEU VAL VAL ASN THR MET ARG GLY ILE VAL LYS VAL ALA
SEQRES 22 E 524 ALA VAL LYS ALA PRO GLY PHE GLY ASP ARG ARG LYS ALA
SEQRES 23 E 524 MET LEU GLN ASP ILE ALA THR LEU THR GLY GLY THR VAL
SEQRES 24 E 524 ILE SER GLU GLU ILE GLY MET GLU LEU GLU LYS ALA THR
SEQRES 25 E 524 LEU GLU ASP LEU GLY GLN ALA LYS ARG VAL VAL ILE ASN
SEQRES 26 E 524 LYS ASP THR THR THR ILE ILE ASP GLY VAL GLY GLU GLU
SEQRES 27 E 524 ALA ALA ILE GLN GLY ARG VAL ALA GLN ILE ARG GLN GLN
SEQRES 28 E 524 ILE GLU GLU ALA THR SER ASP TYR ASP ARG GLU LYS LEU
SEQRES 29 E 524 GLN GLU ARG VAL ALA LYS LEU ALA GLY GLY VAL ALA VAL
SEQRES 30 E 524 ILE LYS VAL GLY ALA ALA THR GLU VAL GLU MET LYS GLU
SEQRES 31 E 524 LYS LYS ALA ARG VAL GLU ASP ALA LEU HIS ALA THR ARG
SEQRES 32 E 524 ALA ALA VAL GLU GLU GLY VAL VAL ALA GLY GLY GLY VAL
SEQRES 33 E 524 ALA LEU ILE ARG VAL ALA SER LYS LEU ALA ASP LEU ARG
SEQRES 34 E 524 GLY GLN ASN GLU ASP GLN ASN VAL GLY ILE LYS VAL ALA
SEQRES 35 E 524 LEU ARG ALA MET GLU ALA PRO LEU ARG GLN ILE VAL LEU
SEQRES 36 E 524 ASN CYS GLY GLU GLU PRO SER VAL VAL ALA ASN THR VAL
SEQRES 37 E 524 LYS GLY GLY ASP GLY ASN TYR GLY TYR ASN ALA ALA THR
SEQRES 38 E 524 GLU GLU TYR GLY ASN MET ILE ASP MET GLY ILE LEU ASP
SEQRES 39 E 524 PRO THR LYS VAL THR ARG SER ALA LEU GLN TYR ALA ALA
SEQRES 40 E 524 SER VAL ALA GLY LEU MET ILE THR THR GLU CYS MET VAL
SEQRES 41 E 524 THR ASP LEU PRO
SEQRES 1 F 524 ALA ALA LYS ASP VAL LYS PHE GLY ASN ASP ALA ARG VAL
SEQRES 2 F 524 LYS MET LEU ARG GLY VAL ASN VAL LEU ALA ASP ALA VAL
SEQRES 3 F 524 LYS VAL THR LEU GLY PRO LYS GLY ARG ASN VAL VAL LEU
SEQRES 4 F 524 ASP LYS SER PHE GLY ALA PRO THR ILE THR LYS ASP GLY
SEQRES 5 F 524 VAL SER VAL ALA ARG GLU ILE GLU LEU GLU ASP LYS PHE
SEQRES 6 F 524 GLU ASN MET GLY ALA GLN MET VAL LYS GLU VAL ALA SER
SEQRES 7 F 524 LYS ALA ASN ASP ALA ALA GLY ASP GLY THR THR THR ALA
SEQRES 8 F 524 THR VAL LEU ALA GLN ALA ILE ILE THR GLU GLY LEU LYS
SEQRES 9 F 524 ALA VAL ALA ALA GLY MET ASN PRO MET ASP LEU LYS ARG
SEQRES 10 F 524 GLY ILE ASP LYS ALA VAL THR ALA ALA VAL GLU GLU LEU
SEQRES 11 F 524 LYS ALA LEU SER VAL PRO CYS SER ASP SER LYS ALA ILE
SEQRES 12 F 524 ALA GLN VAL GLY THR ILE SER ALA ASN SER ASP GLU THR
SEQRES 13 F 524 VAL GLY LYS LEU ILE ALA GLU ALA MET ASP LYS VAL GLY
SEQRES 14 F 524 LYS GLU GLY VAL ILE THR VAL GLU ASP GLY THR GLY LEU
SEQRES 15 F 524 GLN ASP GLU LEU ASP VAL VAL GLU GLY MET GLN PHE ASP
SEQRES 16 F 524 ARG GLY TYR LEU SER PRO TYR PHE ILE ASN LYS PRO GLU
SEQRES 17 F 524 THR GLY ALA VAL GLU LEU GLU SER PRO PHE ILE LEU LEU
SEQRES 18 F 524 ALA ASP LYS LYS ILE SER ASN ILE ARG GLU MET LEU PRO
SEQRES 19 F 524 VAL LEU GLU ALA VAL ALA LYS ALA GLY LYS PRO LEU LEU
SEQRES 20 F 524 ILE ILE ALA GLU ASP VAL GLU GLY GLU ALA LEU ALA THR
SEQRES 21 F 524 LEU VAL VAL ASN THR MET ARG GLY ILE VAL LYS VAL ALA
SEQRES 22 F 524 ALA VAL LYS ALA PRO GLY PHE GLY ASP ARG ARG LYS ALA
SEQRES 23 F 524 MET LEU GLN ASP ILE ALA THR LEU THR GLY GLY THR VAL
SEQRES 24 F 524 ILE SER GLU GLU ILE GLY MET GLU LEU GLU LYS ALA THR
SEQRES 25 F 524 LEU GLU ASP LEU GLY GLN ALA LYS ARG VAL VAL ILE ASN
SEQRES 26 F 524 LYS ASP THR THR THR ILE ILE ASP GLY VAL GLY GLU GLU
SEQRES 27 F 524 ALA ALA ILE GLN GLY ARG VAL ALA GLN ILE ARG GLN GLN
SEQRES 28 F 524 ILE GLU GLU ALA THR SER ASP TYR ASP ARG GLU LYS LEU
SEQRES 29 F 524 GLN GLU ARG VAL ALA LYS LEU ALA GLY GLY VAL ALA VAL
SEQRES 30 F 524 ILE LYS VAL GLY ALA ALA THR GLU VAL GLU MET LYS GLU
SEQRES 31 F 524 LYS LYS ALA ARG VAL GLU ASP ALA LEU HIS ALA THR ARG
SEQRES 32 F 524 ALA ALA VAL GLU GLU GLY VAL VAL ALA GLY GLY GLY VAL
SEQRES 33 F 524 ALA LEU ILE ARG VAL ALA SER LYS LEU ALA ASP LEU ARG
SEQRES 34 F 524 GLY GLN ASN GLU ASP GLN ASN VAL GLY ILE LYS VAL ALA
SEQRES 35 F 524 LEU ARG ALA MET GLU ALA PRO LEU ARG GLN ILE VAL LEU
SEQRES 36 F 524 ASN CYS GLY GLU GLU PRO SER VAL VAL ALA ASN THR VAL
SEQRES 37 F 524 LYS GLY GLY ASP GLY ASN TYR GLY TYR ASN ALA ALA THR
SEQRES 38 F 524 GLU GLU TYR GLY ASN MET ILE ASP MET GLY ILE LEU ASP
SEQRES 39 F 524 PRO THR LYS VAL THR ARG SER ALA LEU GLN TYR ALA ALA
SEQRES 40 F 524 SER VAL ALA GLY LEU MET ILE THR THR GLU CYS MET VAL
SEQRES 41 F 524 THR ASP LEU PRO
SEQRES 1 G 524 ALA ALA LYS ASP VAL LYS PHE GLY ASN ASP ALA ARG VAL
SEQRES 2 G 524 LYS MET LEU ARG GLY VAL ASN VAL LEU ALA ASP ALA VAL
SEQRES 3 G 524 LYS VAL THR LEU GLY PRO LYS GLY ARG ASN VAL VAL LEU
SEQRES 4 G 524 ASP LYS SER PHE GLY ALA PRO THR ILE THR LYS ASP GLY
SEQRES 5 G 524 VAL SER VAL ALA ARG GLU ILE GLU LEU GLU ASP LYS PHE
SEQRES 6 G 524 GLU ASN MET GLY ALA GLN MET VAL LYS GLU VAL ALA SER
SEQRES 7 G 524 LYS ALA ASN ASP ALA ALA GLY ASP GLY THR THR THR ALA
SEQRES 8 G 524 THR VAL LEU ALA GLN ALA ILE ILE THR GLU GLY LEU LYS
SEQRES 9 G 524 ALA VAL ALA ALA GLY MET ASN PRO MET ASP LEU LYS ARG
SEQRES 10 G 524 GLY ILE ASP LYS ALA VAL THR ALA ALA VAL GLU GLU LEU
SEQRES 11 G 524 LYS ALA LEU SER VAL PRO CYS SER ASP SER LYS ALA ILE
SEQRES 12 G 524 ALA GLN VAL GLY THR ILE SER ALA ASN SER ASP GLU THR
SEQRES 13 G 524 VAL GLY LYS LEU ILE ALA GLU ALA MET ASP LYS VAL GLY
SEQRES 14 G 524 LYS GLU GLY VAL ILE THR VAL GLU ASP GLY THR GLY LEU
SEQRES 15 G 524 GLN ASP GLU LEU ASP VAL VAL GLU GLY MET GLN PHE ASP
SEQRES 16 G 524 ARG GLY TYR LEU SER PRO TYR PHE ILE ASN LYS PRO GLU
SEQRES 17 G 524 THR GLY ALA VAL GLU LEU GLU SER PRO PHE ILE LEU LEU
SEQRES 18 G 524 ALA ASP LYS LYS ILE SER ASN ILE ARG GLU MET LEU PRO
SEQRES 19 G 524 VAL LEU GLU ALA VAL ALA LYS ALA GLY LYS PRO LEU LEU
SEQRES 20 G 524 ILE ILE ALA GLU ASP VAL GLU GLY GLU ALA LEU ALA THR
SEQRES 21 G 524 LEU VAL VAL ASN THR MET ARG GLY ILE VAL LYS VAL ALA
SEQRES 22 G 524 ALA VAL LYS ALA PRO GLY PHE GLY ASP ARG ARG LYS ALA
SEQRES 23 G 524 MET LEU GLN ASP ILE ALA THR LEU THR GLY GLY THR VAL
SEQRES 24 G 524 ILE SER GLU GLU ILE GLY MET GLU LEU GLU LYS ALA THR
SEQRES 25 G 524 LEU GLU ASP LEU GLY GLN ALA LYS ARG VAL VAL ILE ASN
SEQRES 26 G 524 LYS ASP THR THR THR ILE ILE ASP GLY VAL GLY GLU GLU
SEQRES 27 G 524 ALA ALA ILE GLN GLY ARG VAL ALA GLN ILE ARG GLN GLN
SEQRES 28 G 524 ILE GLU GLU ALA THR SER ASP TYR ASP ARG GLU LYS LEU
SEQRES 29 G 524 GLN GLU ARG VAL ALA LYS LEU ALA GLY GLY VAL ALA VAL
SEQRES 30 G 524 ILE LYS VAL GLY ALA ALA THR GLU VAL GLU MET LYS GLU
SEQRES 31 G 524 LYS LYS ALA ARG VAL GLU ASP ALA LEU HIS ALA THR ARG
SEQRES 32 G 524 ALA ALA VAL GLU GLU GLY VAL VAL ALA GLY GLY GLY VAL
SEQRES 33 G 524 ALA LEU ILE ARG VAL ALA SER LYS LEU ALA ASP LEU ARG
SEQRES 34 G 524 GLY GLN ASN GLU ASP GLN ASN VAL GLY ILE LYS VAL ALA
SEQRES 35 G 524 LEU ARG ALA MET GLU ALA PRO LEU ARG GLN ILE VAL LEU
SEQRES 36 G 524 ASN CYS GLY GLU GLU PRO SER VAL VAL ALA ASN THR VAL
SEQRES 37 G 524 LYS GLY GLY ASP GLY ASN TYR GLY TYR ASN ALA ALA THR
SEQRES 38 G 524 GLU GLU TYR GLY ASN MET ILE ASP MET GLY ILE LEU ASP
SEQRES 39 G 524 PRO THR LYS VAL THR ARG SER ALA LEU GLN TYR ALA ALA
SEQRES 40 G 524 SER VAL ALA GLY LEU MET ILE THR THR GLU CYS MET VAL
SEQRES 41 G 524 THR ASP LEU PRO
SEQRES 1 H 524 ALA ALA LYS ASP VAL LYS PHE GLY ASN ASP ALA ARG VAL
SEQRES 2 H 524 LYS MET LEU ARG GLY VAL ASN VAL LEU ALA ASP ALA VAL
SEQRES 3 H 524 LYS VAL THR LEU GLY PRO LYS GLY ARG ASN VAL VAL LEU
SEQRES 4 H 524 ASP LYS SER PHE GLY ALA PRO THR ILE THR LYS ASP GLY
SEQRES 5 H 524 VAL SER VAL ALA ARG GLU ILE GLU LEU GLU ASP LYS PHE
SEQRES 6 H 524 GLU ASN MET GLY ALA GLN MET VAL LYS GLU VAL ALA SER
SEQRES 7 H 524 LYS ALA ASN ASP ALA ALA GLY ASP GLY THR THR THR ALA
SEQRES 8 H 524 THR VAL LEU ALA GLN ALA ILE ILE THR GLU GLY LEU LYS
SEQRES 9 H 524 ALA VAL ALA ALA GLY MET ASN PRO MET ASP LEU LYS ARG
SEQRES 10 H 524 GLY ILE ASP LYS ALA VAL THR ALA ALA VAL GLU GLU LEU
SEQRES 11 H 524 LYS ALA LEU SER VAL PRO CYS SER ASP SER LYS ALA ILE
SEQRES 12 H 524 ALA GLN VAL GLY THR ILE SER ALA ASN SER ASP GLU THR
SEQRES 13 H 524 VAL GLY LYS LEU ILE ALA GLU ALA MET ASP LYS VAL GLY
SEQRES 14 H 524 LYS GLU GLY VAL ILE THR VAL GLU ASP GLY THR GLY LEU
SEQRES 15 H 524 GLN ASP GLU LEU ASP VAL VAL GLU GLY MET GLN PHE ASP
SEQRES 16 H 524 ARG GLY TYR LEU SER PRO TYR PHE ILE ASN LYS PRO GLU
SEQRES 17 H 524 THR GLY ALA VAL GLU LEU GLU SER PRO PHE ILE LEU LEU
SEQRES 18 H 524 ALA ASP LYS LYS ILE SER ASN ILE ARG GLU MET LEU PRO
SEQRES 19 H 524 VAL LEU GLU ALA VAL ALA LYS ALA GLY LYS PRO LEU LEU
SEQRES 20 H 524 ILE ILE ALA GLU ASP VAL GLU GLY GLU ALA LEU ALA THR
SEQRES 21 H 524 LEU VAL VAL ASN THR MET ARG GLY ILE VAL LYS VAL ALA
SEQRES 22 H 524 ALA VAL LYS ALA PRO GLY PHE GLY ASP ARG ARG LYS ALA
SEQRES 23 H 524 MET LEU GLN ASP ILE ALA THR LEU THR GLY GLY THR VAL
SEQRES 24 H 524 ILE SER GLU GLU ILE GLY MET GLU LEU GLU LYS ALA THR
SEQRES 25 H 524 LEU GLU ASP LEU GLY GLN ALA LYS ARG VAL VAL ILE ASN
SEQRES 26 H 524 LYS ASP THR THR THR ILE ILE ASP GLY VAL GLY GLU GLU
SEQRES 27 H 524 ALA ALA ILE GLN GLY ARG VAL ALA GLN ILE ARG GLN GLN
SEQRES 28 H 524 ILE GLU GLU ALA THR SER ASP TYR ASP ARG GLU LYS LEU
SEQRES 29 H 524 GLN GLU ARG VAL ALA LYS LEU ALA GLY GLY VAL ALA VAL
SEQRES 30 H 524 ILE LYS VAL GLY ALA ALA THR GLU VAL GLU MET LYS GLU
SEQRES 31 H 524 LYS LYS ALA ARG VAL GLU ASP ALA LEU HIS ALA THR ARG
SEQRES 32 H 524 ALA ALA VAL GLU GLU GLY VAL VAL ALA GLY GLY GLY VAL
SEQRES 33 H 524 ALA LEU ILE ARG VAL ALA SER LYS LEU ALA ASP LEU ARG
SEQRES 34 H 524 GLY GLN ASN GLU ASP GLN ASN VAL GLY ILE LYS VAL ALA
SEQRES 35 H 524 LEU ARG ALA MET GLU ALA PRO LEU ARG GLN ILE VAL LEU
SEQRES 36 H 524 ASN CYS GLY GLU GLU PRO SER VAL VAL ALA ASN THR VAL
SEQRES 37 H 524 LYS GLY GLY ASP GLY ASN TYR GLY TYR ASN ALA ALA THR
SEQRES 38 H 524 GLU GLU TYR GLY ASN MET ILE ASP MET GLY ILE LEU ASP
SEQRES 39 H 524 PRO THR LYS VAL THR ARG SER ALA LEU GLN TYR ALA ALA
SEQRES 40 H 524 SER VAL ALA GLY LEU MET ILE THR THR GLU CYS MET VAL
SEQRES 41 H 524 THR ASP LEU PRO
SEQRES 1 I 524 ALA ALA LYS ASP VAL LYS PHE GLY ASN ASP ALA ARG VAL
SEQRES 2 I 524 LYS MET LEU ARG GLY VAL ASN VAL LEU ALA ASP ALA VAL
SEQRES 3 I 524 LYS VAL THR LEU GLY PRO LYS GLY ARG ASN VAL VAL LEU
SEQRES 4 I 524 ASP LYS SER PHE GLY ALA PRO THR ILE THR LYS ASP GLY
SEQRES 5 I 524 VAL SER VAL ALA ARG GLU ILE GLU LEU GLU ASP LYS PHE
SEQRES 6 I 524 GLU ASN MET GLY ALA GLN MET VAL LYS GLU VAL ALA SER
SEQRES 7 I 524 LYS ALA ASN ASP ALA ALA GLY ASP GLY THR THR THR ALA
SEQRES 8 I 524 THR VAL LEU ALA GLN ALA ILE ILE THR GLU GLY LEU LYS
SEQRES 9 I 524 ALA VAL ALA ALA GLY MET ASN PRO MET ASP LEU LYS ARG
SEQRES 10 I 524 GLY ILE ASP LYS ALA VAL THR ALA ALA VAL GLU GLU LEU
SEQRES 11 I 524 LYS ALA LEU SER VAL PRO CYS SER ASP SER LYS ALA ILE
SEQRES 12 I 524 ALA GLN VAL GLY THR ILE SER ALA ASN SER ASP GLU THR
SEQRES 13 I 524 VAL GLY LYS LEU ILE ALA GLU ALA MET ASP LYS VAL GLY
SEQRES 14 I 524 LYS GLU GLY VAL ILE THR VAL GLU ASP GLY THR GLY LEU
SEQRES 15 I 524 GLN ASP GLU LEU ASP VAL VAL GLU GLY MET GLN PHE ASP
SEQRES 16 I 524 ARG GLY TYR LEU SER PRO TYR PHE ILE ASN LYS PRO GLU
SEQRES 17 I 524 THR GLY ALA VAL GLU LEU GLU SER PRO PHE ILE LEU LEU
SEQRES 18 I 524 ALA ASP LYS LYS ILE SER ASN ILE ARG GLU MET LEU PRO
SEQRES 19 I 524 VAL LEU GLU ALA VAL ALA LYS ALA GLY LYS PRO LEU LEU
SEQRES 20 I 524 ILE ILE ALA GLU ASP VAL GLU GLY GLU ALA LEU ALA THR
SEQRES 21 I 524 LEU VAL VAL ASN THR MET ARG GLY ILE VAL LYS VAL ALA
SEQRES 22 I 524 ALA VAL LYS ALA PRO GLY PHE GLY ASP ARG ARG LYS ALA
SEQRES 23 I 524 MET LEU GLN ASP ILE ALA THR LEU THR GLY GLY THR VAL
SEQRES 24 I 524 ILE SER GLU GLU ILE GLY MET GLU LEU GLU LYS ALA THR
SEQRES 25 I 524 LEU GLU ASP LEU GLY GLN ALA LYS ARG VAL VAL ILE ASN
SEQRES 26 I 524 LYS ASP THR THR THR ILE ILE ASP GLY VAL GLY GLU GLU
SEQRES 27 I 524 ALA ALA ILE GLN GLY ARG VAL ALA GLN ILE ARG GLN GLN
SEQRES 28 I 524 ILE GLU GLU ALA THR SER ASP TYR ASP ARG GLU LYS LEU
SEQRES 29 I 524 GLN GLU ARG VAL ALA LYS LEU ALA GLY GLY VAL ALA VAL
SEQRES 30 I 524 ILE LYS VAL GLY ALA ALA THR GLU VAL GLU MET LYS GLU
SEQRES 31 I 524 LYS LYS ALA ARG VAL GLU ASP ALA LEU HIS ALA THR ARG
SEQRES 32 I 524 ALA ALA VAL GLU GLU GLY VAL VAL ALA GLY GLY GLY VAL
SEQRES 33 I 524 ALA LEU ILE ARG VAL ALA SER LYS LEU ALA ASP LEU ARG
SEQRES 34 I 524 GLY GLN ASN GLU ASP GLN ASN VAL GLY ILE LYS VAL ALA
SEQRES 35 I 524 LEU ARG ALA MET GLU ALA PRO LEU ARG GLN ILE VAL LEU
SEQRES 36 I 524 ASN CYS GLY GLU GLU PRO SER VAL VAL ALA ASN THR VAL
SEQRES 37 I 524 LYS GLY GLY ASP GLY ASN TYR GLY TYR ASN ALA ALA THR
SEQRES 38 I 524 GLU GLU TYR GLY ASN MET ILE ASP MET GLY ILE LEU ASP
SEQRES 39 I 524 PRO THR LYS VAL THR ARG SER ALA LEU GLN TYR ALA ALA
SEQRES 40 I 524 SER VAL ALA GLY LEU MET ILE THR THR GLU CYS MET VAL
SEQRES 41 I 524 THR ASP LEU PRO
SEQRES 1 J 524 ALA ALA LYS ASP VAL LYS PHE GLY ASN ASP ALA ARG VAL
SEQRES 2 J 524 LYS MET LEU ARG GLY VAL ASN VAL LEU ALA ASP ALA VAL
SEQRES 3 J 524 LYS VAL THR LEU GLY PRO LYS GLY ARG ASN VAL VAL LEU
SEQRES 4 J 524 ASP LYS SER PHE GLY ALA PRO THR ILE THR LYS ASP GLY
SEQRES 5 J 524 VAL SER VAL ALA ARG GLU ILE GLU LEU GLU ASP LYS PHE
SEQRES 6 J 524 GLU ASN MET GLY ALA GLN MET VAL LYS GLU VAL ALA SER
SEQRES 7 J 524 LYS ALA ASN ASP ALA ALA GLY ASP GLY THR THR THR ALA
SEQRES 8 J 524 THR VAL LEU ALA GLN ALA ILE ILE THR GLU GLY LEU LYS
SEQRES 9 J 524 ALA VAL ALA ALA GLY MET ASN PRO MET ASP LEU LYS ARG
SEQRES 10 J 524 GLY ILE ASP LYS ALA VAL THR ALA ALA VAL GLU GLU LEU
SEQRES 11 J 524 LYS ALA LEU SER VAL PRO CYS SER ASP SER LYS ALA ILE
SEQRES 12 J 524 ALA GLN VAL GLY THR ILE SER ALA ASN SER ASP GLU THR
SEQRES 13 J 524 VAL GLY LYS LEU ILE ALA GLU ALA MET ASP LYS VAL GLY
SEQRES 14 J 524 LYS GLU GLY VAL ILE THR VAL GLU ASP GLY THR GLY LEU
SEQRES 15 J 524 GLN ASP GLU LEU ASP VAL VAL GLU GLY MET GLN PHE ASP
SEQRES 16 J 524 ARG GLY TYR LEU SER PRO TYR PHE ILE ASN LYS PRO GLU
SEQRES 17 J 524 THR GLY ALA VAL GLU LEU GLU SER PRO PHE ILE LEU LEU
SEQRES 18 J 524 ALA ASP LYS LYS ILE SER ASN ILE ARG GLU MET LEU PRO
SEQRES 19 J 524 VAL LEU GLU ALA VAL ALA LYS ALA GLY LYS PRO LEU LEU
SEQRES 20 J 524 ILE ILE ALA GLU ASP VAL GLU GLY GLU ALA LEU ALA THR
SEQRES 21 J 524 LEU VAL VAL ASN THR MET ARG GLY ILE VAL LYS VAL ALA
SEQRES 22 J 524 ALA VAL LYS ALA PRO GLY PHE GLY ASP ARG ARG LYS ALA
SEQRES 23 J 524 MET LEU GLN ASP ILE ALA THR LEU THR GLY GLY THR VAL
SEQRES 24 J 524 ILE SER GLU GLU ILE GLY MET GLU LEU GLU LYS ALA THR
SEQRES 25 J 524 LEU GLU ASP LEU GLY GLN ALA LYS ARG VAL VAL ILE ASN
SEQRES 26 J 524 LYS ASP THR THR THR ILE ILE ASP GLY VAL GLY GLU GLU
SEQRES 27 J 524 ALA ALA ILE GLN GLY ARG VAL ALA GLN ILE ARG GLN GLN
SEQRES 28 J 524 ILE GLU GLU ALA THR SER ASP TYR ASP ARG GLU LYS LEU
SEQRES 29 J 524 GLN GLU ARG VAL ALA LYS LEU ALA GLY GLY VAL ALA VAL
SEQRES 30 J 524 ILE LYS VAL GLY ALA ALA THR GLU VAL GLU MET LYS GLU
SEQRES 31 J 524 LYS LYS ALA ARG VAL GLU ASP ALA LEU HIS ALA THR ARG
SEQRES 32 J 524 ALA ALA VAL GLU GLU GLY VAL VAL ALA GLY GLY GLY VAL
SEQRES 33 J 524 ALA LEU ILE ARG VAL ALA SER LYS LEU ALA ASP LEU ARG
SEQRES 34 J 524 GLY GLN ASN GLU ASP GLN ASN VAL GLY ILE LYS VAL ALA
SEQRES 35 J 524 LEU ARG ALA MET GLU ALA PRO LEU ARG GLN ILE VAL LEU
SEQRES 36 J 524 ASN CYS GLY GLU GLU PRO SER VAL VAL ALA ASN THR VAL
SEQRES 37 J 524 LYS GLY GLY ASP GLY ASN TYR GLY TYR ASN ALA ALA THR
SEQRES 38 J 524 GLU GLU TYR GLY ASN MET ILE ASP MET GLY ILE LEU ASP
SEQRES 39 J 524 PRO THR LYS VAL THR ARG SER ALA LEU GLN TYR ALA ALA
SEQRES 40 J 524 SER VAL ALA GLY LEU MET ILE THR THR GLU CYS MET VAL
SEQRES 41 J 524 THR ASP LEU PRO
SEQRES 1 K 524 ALA ALA LYS ASP VAL LYS PHE GLY ASN ASP ALA ARG VAL
SEQRES 2 K 524 LYS MET LEU ARG GLY VAL ASN VAL LEU ALA ASP ALA VAL
SEQRES 3 K 524 LYS VAL THR LEU GLY PRO LYS GLY ARG ASN VAL VAL LEU
SEQRES 4 K 524 ASP LYS SER PHE GLY ALA PRO THR ILE THR LYS ASP GLY
SEQRES 5 K 524 VAL SER VAL ALA ARG GLU ILE GLU LEU GLU ASP LYS PHE
SEQRES 6 K 524 GLU ASN MET GLY ALA GLN MET VAL LYS GLU VAL ALA SER
SEQRES 7 K 524 LYS ALA ASN ASP ALA ALA GLY ASP GLY THR THR THR ALA
SEQRES 8 K 524 THR VAL LEU ALA GLN ALA ILE ILE THR GLU GLY LEU LYS
SEQRES 9 K 524 ALA VAL ALA ALA GLY MET ASN PRO MET ASP LEU LYS ARG
SEQRES 10 K 524 GLY ILE ASP LYS ALA VAL THR ALA ALA VAL GLU GLU LEU
SEQRES 11 K 524 LYS ALA LEU SER VAL PRO CYS SER ASP SER LYS ALA ILE
SEQRES 12 K 524 ALA GLN VAL GLY THR ILE SER ALA ASN SER ASP GLU THR
SEQRES 13 K 524 VAL GLY LYS LEU ILE ALA GLU ALA MET ASP LYS VAL GLY
SEQRES 14 K 524 LYS GLU GLY VAL ILE THR VAL GLU ASP GLY THR GLY LEU
SEQRES 15 K 524 GLN ASP GLU LEU ASP VAL VAL GLU GLY MET GLN PHE ASP
SEQRES 16 K 524 ARG GLY TYR LEU SER PRO TYR PHE ILE ASN LYS PRO GLU
SEQRES 17 K 524 THR GLY ALA VAL GLU LEU GLU SER PRO PHE ILE LEU LEU
SEQRES 18 K 524 ALA ASP LYS LYS ILE SER ASN ILE ARG GLU MET LEU PRO
SEQRES 19 K 524 VAL LEU GLU ALA VAL ALA LYS ALA GLY LYS PRO LEU LEU
SEQRES 20 K 524 ILE ILE ALA GLU ASP VAL GLU GLY GLU ALA LEU ALA THR
SEQRES 21 K 524 LEU VAL VAL ASN THR MET ARG GLY ILE VAL LYS VAL ALA
SEQRES 22 K 524 ALA VAL LYS ALA PRO GLY PHE GLY ASP ARG ARG LYS ALA
SEQRES 23 K 524 MET LEU GLN ASP ILE ALA THR LEU THR GLY GLY THR VAL
SEQRES 24 K 524 ILE SER GLU GLU ILE GLY MET GLU LEU GLU LYS ALA THR
SEQRES 25 K 524 LEU GLU ASP LEU GLY GLN ALA LYS ARG VAL VAL ILE ASN
SEQRES 26 K 524 LYS ASP THR THR THR ILE ILE ASP GLY VAL GLY GLU GLU
SEQRES 27 K 524 ALA ALA ILE GLN GLY ARG VAL ALA GLN ILE ARG GLN GLN
SEQRES 28 K 524 ILE GLU GLU ALA THR SER ASP TYR ASP ARG GLU LYS LEU
SEQRES 29 K 524 GLN GLU ARG VAL ALA LYS LEU ALA GLY GLY VAL ALA VAL
SEQRES 30 K 524 ILE LYS VAL GLY ALA ALA THR GLU VAL GLU MET LYS GLU
SEQRES 31 K 524 LYS LYS ALA ARG VAL GLU ASP ALA LEU HIS ALA THR ARG
SEQRES 32 K 524 ALA ALA VAL GLU GLU GLY VAL VAL ALA GLY GLY GLY VAL
SEQRES 33 K 524 ALA LEU ILE ARG VAL ALA SER LYS LEU ALA ASP LEU ARG
SEQRES 34 K 524 GLY GLN ASN GLU ASP GLN ASN VAL GLY ILE LYS VAL ALA
SEQRES 35 K 524 LEU ARG ALA MET GLU ALA PRO LEU ARG GLN ILE VAL LEU
SEQRES 36 K 524 ASN CYS GLY GLU GLU PRO SER VAL VAL ALA ASN THR VAL
SEQRES 37 K 524 LYS GLY GLY ASP GLY ASN TYR GLY TYR ASN ALA ALA THR
SEQRES 38 K 524 GLU GLU TYR GLY ASN MET ILE ASP MET GLY ILE LEU ASP
SEQRES 39 K 524 PRO THR LYS VAL THR ARG SER ALA LEU GLN TYR ALA ALA
SEQRES 40 K 524 SER VAL ALA GLY LEU MET ILE THR THR GLU CYS MET VAL
SEQRES 41 K 524 THR ASP LEU PRO
SEQRES 1 L 524 ALA ALA LYS ASP VAL LYS PHE GLY ASN ASP ALA ARG VAL
SEQRES 2 L 524 LYS MET LEU ARG GLY VAL ASN VAL LEU ALA ASP ALA VAL
SEQRES 3 L 524 LYS VAL THR LEU GLY PRO LYS GLY ARG ASN VAL VAL LEU
SEQRES 4 L 524 ASP LYS SER PHE GLY ALA PRO THR ILE THR LYS ASP GLY
SEQRES 5 L 524 VAL SER VAL ALA ARG GLU ILE GLU LEU GLU ASP LYS PHE
SEQRES 6 L 524 GLU ASN MET GLY ALA GLN MET VAL LYS GLU VAL ALA SER
SEQRES 7 L 524 LYS ALA ASN ASP ALA ALA GLY ASP GLY THR THR THR ALA
SEQRES 8 L 524 THR VAL LEU ALA GLN ALA ILE ILE THR GLU GLY LEU LYS
SEQRES 9 L 524 ALA VAL ALA ALA GLY MET ASN PRO MET ASP LEU LYS ARG
SEQRES 10 L 524 GLY ILE ASP LYS ALA VAL THR ALA ALA VAL GLU GLU LEU
SEQRES 11 L 524 LYS ALA LEU SER VAL PRO CYS SER ASP SER LYS ALA ILE
SEQRES 12 L 524 ALA GLN VAL GLY THR ILE SER ALA ASN SER ASP GLU THR
SEQRES 13 L 524 VAL GLY LYS LEU ILE ALA GLU ALA MET ASP LYS VAL GLY
SEQRES 14 L 524 LYS GLU GLY VAL ILE THR VAL GLU ASP GLY THR GLY LEU
SEQRES 15 L 524 GLN ASP GLU LEU ASP VAL VAL GLU GLY MET GLN PHE ASP
SEQRES 16 L 524 ARG GLY TYR LEU SER PRO TYR PHE ILE ASN LYS PRO GLU
SEQRES 17 L 524 THR GLY ALA VAL GLU LEU GLU SER PRO PHE ILE LEU LEU
SEQRES 18 L 524 ALA ASP LYS LYS ILE SER ASN ILE ARG GLU MET LEU PRO
SEQRES 19 L 524 VAL LEU GLU ALA VAL ALA LYS ALA GLY LYS PRO LEU LEU
SEQRES 20 L 524 ILE ILE ALA GLU ASP VAL GLU GLY GLU ALA LEU ALA THR
SEQRES 21 L 524 LEU VAL VAL ASN THR MET ARG GLY ILE VAL LYS VAL ALA
SEQRES 22 L 524 ALA VAL LYS ALA PRO GLY PHE GLY ASP ARG ARG LYS ALA
SEQRES 23 L 524 MET LEU GLN ASP ILE ALA THR LEU THR GLY GLY THR VAL
SEQRES 24 L 524 ILE SER GLU GLU ILE GLY MET GLU LEU GLU LYS ALA THR
SEQRES 25 L 524 LEU GLU ASP LEU GLY GLN ALA LYS ARG VAL VAL ILE ASN
SEQRES 26 L 524 LYS ASP THR THR THR ILE ILE ASP GLY VAL GLY GLU GLU
SEQRES 27 L 524 ALA ALA ILE GLN GLY ARG VAL ALA GLN ILE ARG GLN GLN
SEQRES 28 L 524 ILE GLU GLU ALA THR SER ASP TYR ASP ARG GLU LYS LEU
SEQRES 29 L 524 GLN GLU ARG VAL ALA LYS LEU ALA GLY GLY VAL ALA VAL
SEQRES 30 L 524 ILE LYS VAL GLY ALA ALA THR GLU VAL GLU MET LYS GLU
SEQRES 31 L 524 LYS LYS ALA ARG VAL GLU ASP ALA LEU HIS ALA THR ARG
SEQRES 32 L 524 ALA ALA VAL GLU GLU GLY VAL VAL ALA GLY GLY GLY VAL
SEQRES 33 L 524 ALA LEU ILE ARG VAL ALA SER LYS LEU ALA ASP LEU ARG
SEQRES 34 L 524 GLY GLN ASN GLU ASP GLN ASN VAL GLY ILE LYS VAL ALA
SEQRES 35 L 524 LEU ARG ALA MET GLU ALA PRO LEU ARG GLN ILE VAL LEU
SEQRES 36 L 524 ASN CYS GLY GLU GLU PRO SER VAL VAL ALA ASN THR VAL
SEQRES 37 L 524 LYS GLY GLY ASP GLY ASN TYR GLY TYR ASN ALA ALA THR
SEQRES 38 L 524 GLU GLU TYR GLY ASN MET ILE ASP MET GLY ILE LEU ASP
SEQRES 39 L 524 PRO THR LYS VAL THR ARG SER ALA LEU GLN TYR ALA ALA
SEQRES 40 L 524 SER VAL ALA GLY LEU MET ILE THR THR GLU CYS MET VAL
SEQRES 41 L 524 THR ASP LEU PRO
SEQRES 1 M 524 ALA ALA LYS ASP VAL LYS PHE GLY ASN ASP ALA ARG VAL
SEQRES 2 M 524 LYS MET LEU ARG GLY VAL ASN VAL LEU ALA ASP ALA VAL
SEQRES 3 M 524 LYS VAL THR LEU GLY PRO LYS GLY ARG ASN VAL VAL LEU
SEQRES 4 M 524 ASP LYS SER PHE GLY ALA PRO THR ILE THR LYS ASP GLY
SEQRES 5 M 524 VAL SER VAL ALA ARG GLU ILE GLU LEU GLU ASP LYS PHE
SEQRES 6 M 524 GLU ASN MET GLY ALA GLN MET VAL LYS GLU VAL ALA SER
SEQRES 7 M 524 LYS ALA ASN ASP ALA ALA GLY ASP GLY THR THR THR ALA
SEQRES 8 M 524 THR VAL LEU ALA GLN ALA ILE ILE THR GLU GLY LEU LYS
SEQRES 9 M 524 ALA VAL ALA ALA GLY MET ASN PRO MET ASP LEU LYS ARG
SEQRES 10 M 524 GLY ILE ASP LYS ALA VAL THR ALA ALA VAL GLU GLU LEU
SEQRES 11 M 524 LYS ALA LEU SER VAL PRO CYS SER ASP SER LYS ALA ILE
SEQRES 12 M 524 ALA GLN VAL GLY THR ILE SER ALA ASN SER ASP GLU THR
SEQRES 13 M 524 VAL GLY LYS LEU ILE ALA GLU ALA MET ASP LYS VAL GLY
SEQRES 14 M 524 LYS GLU GLY VAL ILE THR VAL GLU ASP GLY THR GLY LEU
SEQRES 15 M 524 GLN ASP GLU LEU ASP VAL VAL GLU GLY MET GLN PHE ASP
SEQRES 16 M 524 ARG GLY TYR LEU SER PRO TYR PHE ILE ASN LYS PRO GLU
SEQRES 17 M 524 THR GLY ALA VAL GLU LEU GLU SER PRO PHE ILE LEU LEU
SEQRES 18 M 524 ALA ASP LYS LYS ILE SER ASN ILE ARG GLU MET LEU PRO
SEQRES 19 M 524 VAL LEU GLU ALA VAL ALA LYS ALA GLY LYS PRO LEU LEU
SEQRES 20 M 524 ILE ILE ALA GLU ASP VAL GLU GLY GLU ALA LEU ALA THR
SEQRES 21 M 524 LEU VAL VAL ASN THR MET ARG GLY ILE VAL LYS VAL ALA
SEQRES 22 M 524 ALA VAL LYS ALA PRO GLY PHE GLY ASP ARG ARG LYS ALA
SEQRES 23 M 524 MET LEU GLN ASP ILE ALA THR LEU THR GLY GLY THR VAL
SEQRES 24 M 524 ILE SER GLU GLU ILE GLY MET GLU LEU GLU LYS ALA THR
SEQRES 25 M 524 LEU GLU ASP LEU GLY GLN ALA LYS ARG VAL VAL ILE ASN
SEQRES 26 M 524 LYS ASP THR THR THR ILE ILE ASP GLY VAL GLY GLU GLU
SEQRES 27 M 524 ALA ALA ILE GLN GLY ARG VAL ALA GLN ILE ARG GLN GLN
SEQRES 28 M 524 ILE GLU GLU ALA THR SER ASP TYR ASP ARG GLU LYS LEU
SEQRES 29 M 524 GLN GLU ARG VAL ALA LYS LEU ALA GLY GLY VAL ALA VAL
SEQRES 30 M 524 ILE LYS VAL GLY ALA ALA THR GLU VAL GLU MET LYS GLU
SEQRES 31 M 524 LYS LYS ALA ARG VAL GLU ASP ALA LEU HIS ALA THR ARG
SEQRES 32 M 524 ALA ALA VAL GLU GLU GLY VAL VAL ALA GLY GLY GLY VAL
SEQRES 33 M 524 ALA LEU ILE ARG VAL ALA SER LYS LEU ALA ASP LEU ARG
SEQRES 34 M 524 GLY GLN ASN GLU ASP GLN ASN VAL GLY ILE LYS VAL ALA
SEQRES 35 M 524 LEU ARG ALA MET GLU ALA PRO LEU ARG GLN ILE VAL LEU
SEQRES 36 M 524 ASN CYS GLY GLU GLU PRO SER VAL VAL ALA ASN THR VAL
SEQRES 37 M 524 LYS GLY GLY ASP GLY ASN TYR GLY TYR ASN ALA ALA THR
SEQRES 38 M 524 GLU GLU TYR GLY ASN MET ILE ASP MET GLY ILE LEU ASP
SEQRES 39 M 524 PRO THR LYS VAL THR ARG SER ALA LEU GLN TYR ALA ALA
SEQRES 40 M 524 SER VAL ALA GLY LEU MET ILE THR THR GLU CYS MET VAL
SEQRES 41 M 524 THR ASP LEU PRO
SEQRES 1 N 524 ALA ALA LYS ASP VAL LYS PHE GLY ASN ASP ALA ARG VAL
SEQRES 2 N 524 LYS MET LEU ARG GLY VAL ASN VAL LEU ALA ASP ALA VAL
SEQRES 3 N 524 LYS VAL THR LEU GLY PRO LYS GLY ARG ASN VAL VAL LEU
SEQRES 4 N 524 ASP LYS SER PHE GLY ALA PRO THR ILE THR LYS ASP GLY
SEQRES 5 N 524 VAL SER VAL ALA ARG GLU ILE GLU LEU GLU ASP LYS PHE
SEQRES 6 N 524 GLU ASN MET GLY ALA GLN MET VAL LYS GLU VAL ALA SER
SEQRES 7 N 524 LYS ALA ASN ASP ALA ALA GLY ASP GLY THR THR THR ALA
SEQRES 8 N 524 THR VAL LEU ALA GLN ALA ILE ILE THR GLU GLY LEU LYS
SEQRES 9 N 524 ALA VAL ALA ALA GLY MET ASN PRO MET ASP LEU LYS ARG
SEQRES 10 N 524 GLY ILE ASP LYS ALA VAL THR ALA ALA VAL GLU GLU LEU
SEQRES 11 N 524 LYS ALA LEU SER VAL PRO CYS SER ASP SER LYS ALA ILE
SEQRES 12 N 524 ALA GLN VAL GLY THR ILE SER ALA ASN SER ASP GLU THR
SEQRES 13 N 524 VAL GLY LYS LEU ILE ALA GLU ALA MET ASP LYS VAL GLY
SEQRES 14 N 524 LYS GLU GLY VAL ILE THR VAL GLU ASP GLY THR GLY LEU
SEQRES 15 N 524 GLN ASP GLU LEU ASP VAL VAL GLU GLY MET GLN PHE ASP
SEQRES 16 N 524 ARG GLY TYR LEU SER PRO TYR PHE ILE ASN LYS PRO GLU
SEQRES 17 N 524 THR GLY ALA VAL GLU LEU GLU SER PRO PHE ILE LEU LEU
SEQRES 18 N 524 ALA ASP LYS LYS ILE SER ASN ILE ARG GLU MET LEU PRO
SEQRES 19 N 524 VAL LEU GLU ALA VAL ALA LYS ALA GLY LYS PRO LEU LEU
SEQRES 20 N 524 ILE ILE ALA GLU ASP VAL GLU GLY GLU ALA LEU ALA THR
SEQRES 21 N 524 LEU VAL VAL ASN THR MET ARG GLY ILE VAL LYS VAL ALA
SEQRES 22 N 524 ALA VAL LYS ALA PRO GLY PHE GLY ASP ARG ARG LYS ALA
SEQRES 23 N 524 MET LEU GLN ASP ILE ALA THR LEU THR GLY GLY THR VAL
SEQRES 24 N 524 ILE SER GLU GLU ILE GLY MET GLU LEU GLU LYS ALA THR
SEQRES 25 N 524 LEU GLU ASP LEU GLY GLN ALA LYS ARG VAL VAL ILE ASN
SEQRES 26 N 524 LYS ASP THR THR THR ILE ILE ASP GLY VAL GLY GLU GLU
SEQRES 27 N 524 ALA ALA ILE GLN GLY ARG VAL ALA GLN ILE ARG GLN GLN
SEQRES 28 N 524 ILE GLU GLU ALA THR SER ASP TYR ASP ARG GLU LYS LEU
SEQRES 29 N 524 GLN GLU ARG VAL ALA LYS LEU ALA GLY GLY VAL ALA VAL
SEQRES 30 N 524 ILE LYS VAL GLY ALA ALA THR GLU VAL GLU MET LYS GLU
SEQRES 31 N 524 LYS LYS ALA ARG VAL GLU ASP ALA LEU HIS ALA THR ARG
SEQRES 32 N 524 ALA ALA VAL GLU GLU GLY VAL VAL ALA GLY GLY GLY VAL
SEQRES 33 N 524 ALA LEU ILE ARG VAL ALA SER LYS LEU ALA ASP LEU ARG
SEQRES 34 N 524 GLY GLN ASN GLU ASP GLN ASN VAL GLY ILE LYS VAL ALA
SEQRES 35 N 524 LEU ARG ALA MET GLU ALA PRO LEU ARG GLN ILE VAL LEU
SEQRES 36 N 524 ASN CYS GLY GLU GLU PRO SER VAL VAL ALA ASN THR VAL
SEQRES 37 N 524 LYS GLY GLY ASP GLY ASN TYR GLY TYR ASN ALA ALA THR
SEQRES 38 N 524 GLU GLU TYR GLY ASN MET ILE ASP MET GLY ILE LEU ASP
SEQRES 39 N 524 PRO THR LYS VAL THR ARG SER ALA LEU GLN TYR ALA ALA
SEQRES 40 N 524 SER VAL ALA GLY LEU MET ILE THR THR GLU CYS MET VAL
SEQRES 41 N 524 THR ASP LEU PRO
SEQRES 1 O 97 MET ASN ILE ARG PRO LEU HIS ASP ARG VAL ILE VAL LYS
SEQRES 2 O 97 ARG LYS GLU VAL GLU THR LYS SER ALA GLY GLY ILE VAL
SEQRES 3 O 97 LEU THR GLY SER ALA ALA ALA LYS SER THR ARG GLY GLU
SEQRES 4 O 97 VAL LEU ALA VAL GLY ASN GLY ARG ILE LEU GLU ASN GLY
SEQRES 5 O 97 GLU VAL LYS PRO LEU ASP VAL LYS VAL GLY ASP ILE VAL
SEQRES 6 O 97 ILE PHE ASN ASP GLY TYR GLY VAL LYS SER GLU LYS ILE
SEQRES 7 O 97 ASP ASN GLU GLU VAL LEU ILE MET SER GLU SER ASP ILE
SEQRES 8 O 97 LEU ALA ILE VAL GLU ALA
SEQRES 1 P 97 MET ASN ILE ARG PRO LEU HIS ASP ARG VAL ILE VAL LYS
SEQRES 2 P 97 ARG LYS GLU VAL GLU THR LYS SER ALA GLY GLY ILE VAL
SEQRES 3 P 97 LEU THR GLY SER ALA ALA ALA LYS SER THR ARG GLY GLU
SEQRES 4 P 97 VAL LEU ALA VAL GLY ASN GLY ARG ILE LEU GLU ASN GLY
SEQRES 5 P 97 GLU VAL LYS PRO LEU ASP VAL LYS VAL GLY ASP ILE VAL
SEQRES 6 P 97 ILE PHE ASN ASP GLY TYR GLY VAL LYS SER GLU LYS ILE
SEQRES 7 P 97 ASP ASN GLU GLU VAL LEU ILE MET SER GLU SER ASP ILE
SEQRES 8 P 97 LEU ALA ILE VAL GLU ALA
SEQRES 1 Q 97 MET ASN ILE ARG PRO LEU HIS ASP ARG VAL ILE VAL LYS
SEQRES 2 Q 97 ARG LYS GLU VAL GLU THR LYS SER ALA GLY GLY ILE VAL
SEQRES 3 Q 97 LEU THR GLY SER ALA ALA ALA LYS SER THR ARG GLY GLU
SEQRES 4 Q 97 VAL LEU ALA VAL GLY ASN GLY ARG ILE LEU GLU ASN GLY
SEQRES 5 Q 97 GLU VAL LYS PRO LEU ASP VAL LYS VAL GLY ASP ILE VAL
SEQRES 6 Q 97 ILE PHE ASN ASP GLY TYR GLY VAL LYS SER GLU LYS ILE
SEQRES 7 Q 97 ASP ASN GLU GLU VAL LEU ILE MET SER GLU SER ASP ILE
SEQRES 8 Q 97 LEU ALA ILE VAL GLU ALA
SEQRES 1 R 97 MET ASN ILE ARG PRO LEU HIS ASP ARG VAL ILE VAL LYS
SEQRES 2 R 97 ARG LYS GLU VAL GLU THR LYS SER ALA GLY GLY ILE VAL
SEQRES 3 R 97 LEU THR GLY SER ALA ALA ALA LYS SER THR ARG GLY GLU
SEQRES 4 R 97 VAL LEU ALA VAL GLY ASN GLY ARG ILE LEU GLU ASN GLY
SEQRES 5 R 97 GLU VAL LYS PRO LEU ASP VAL LYS VAL GLY ASP ILE VAL
SEQRES 6 R 97 ILE PHE ASN ASP GLY TYR GLY VAL LYS SER GLU LYS ILE
SEQRES 7 R 97 ASP ASN GLU GLU VAL LEU ILE MET SER GLU SER ASP ILE
SEQRES 8 R 97 LEU ALA ILE VAL GLU ALA
SEQRES 1 S 97 MET ASN ILE ARG PRO LEU HIS ASP ARG VAL ILE VAL LYS
SEQRES 2 S 97 ARG LYS GLU VAL GLU THR LYS SER ALA GLY GLY ILE VAL
SEQRES 3 S 97 LEU THR GLY SER ALA ALA ALA LYS SER THR ARG GLY GLU
SEQRES 4 S 97 VAL LEU ALA VAL GLY ASN GLY ARG ILE LEU GLU ASN GLY
SEQRES 5 S 97 GLU VAL LYS PRO LEU ASP VAL LYS VAL GLY ASP ILE VAL
SEQRES 6 S 97 ILE PHE ASN ASP GLY TYR GLY VAL LYS SER GLU LYS ILE
SEQRES 7 S 97 ASP ASN GLU GLU VAL LEU ILE MET SER GLU SER ASP ILE
SEQRES 8 S 97 LEU ALA ILE VAL GLU ALA
SEQRES 1 T 97 MET ASN ILE ARG PRO LEU HIS ASP ARG VAL ILE VAL LYS
SEQRES 2 T 97 ARG LYS GLU VAL GLU THR LYS SER ALA GLY GLY ILE VAL
SEQRES 3 T 97 LEU THR GLY SER ALA ALA ALA LYS SER THR ARG GLY GLU
SEQRES 4 T 97 VAL LEU ALA VAL GLY ASN GLY ARG ILE LEU GLU ASN GLY
SEQRES 5 T 97 GLU VAL LYS PRO LEU ASP VAL LYS VAL GLY ASP ILE VAL
SEQRES 6 T 97 ILE PHE ASN ASP GLY TYR GLY VAL LYS SER GLU LYS ILE
SEQRES 7 T 97 ASP ASN GLU GLU VAL LEU ILE MET SER GLU SER ASP ILE
SEQRES 8 T 97 LEU ALA ILE VAL GLU ALA
SEQRES 1 U 97 MET ASN ILE ARG PRO LEU HIS ASP ARG VAL ILE VAL LYS
SEQRES 2 U 97 ARG LYS GLU VAL GLU THR LYS SER ALA GLY GLY ILE VAL
SEQRES 3 U 97 LEU THR GLY SER ALA ALA ALA LYS SER THR ARG GLY GLU
SEQRES 4 U 97 VAL LEU ALA VAL GLY ASN GLY ARG ILE LEU GLU ASN GLY
SEQRES 5 U 97 GLU VAL LYS PRO LEU ASP VAL LYS VAL GLY ASP ILE VAL
SEQRES 6 U 97 ILE PHE ASN ASP GLY TYR GLY VAL LYS SER GLU LYS ILE
SEQRES 7 U 97 ASP ASN GLU GLU VAL LEU ILE MET SER GLU SER ASP ILE
SEQRES 8 U 97 LEU ALA ILE VAL GLU ALA
HET MG A 601 1
HET K A 603 1
HET MG B 601 1
HET K B 603 1
HET MG C 601 1
HET K C 603 1
HET MG D 601 1
HET K D 603 1
HET MG E 601 1
HET K E 603 1
HET MG F 601 1
HET K F 603 1
HET MG G 601 1
HET K G 603 1
HET ADP A 600 27
HET AF3 A 602 4
HET ADP B 600 27
HET AF3 B 602 4
HET ADP C 600 27
HET AF3 C 602 4
HET ADP D 600 27
HET AF3 D 602 4
HET ADP E 600 27
HET AF3 E 602 4
HET ADP F 600 27
HET AF3 F 602 4
HET ADP G 600 27
HET AF3 G 602 4
HETNAM MG MAGNESIUM ION
HETNAM K POTASSIUM ION
HETNAM ADP ADENOSINE-5'-DIPHOSPHATE
HETNAM AF3 ALUMINUM FLUORIDE
FORMUL 22 MG 7(MG 2+)
FORMUL 23 K 7(K 1+)
FORMUL 36 ADP 7(C10 H15 N5 O10 P2)
FORMUL 37 AF3 7(AL F3)
FORMUL 50 HOH *194(H2 O)
HELIX 1 1 GLY A 9 VAL A 29 1 21
HELIX 2 2 ASP A 52 ARG A 58 1 7
HELIX 3 3 ASP A 64 ALA A 85 1 22
HELIX 4 4 GLY A 88 ALA A 108 1 21
HELIX 5 5 ASN A 112 SER A 135 1 24
HELIX 6 6 ASP A 140 ALA A 152 1 13
HELIX 7 7 ASP A 155 GLY A 170 1 16
HELIX 8 8 ASN A 229 GLU A 232 5 4
HELIX 9 9 MET A 233 GLY A 244 1 12
HELIX 10 10 GLU A 255 ARG A 268 1 14
HELIX 11 11 PHE A 281 GLY A 297 1 17
HELIX 12 12 GLU A 304 GLY A 306 5 3
HELIX 13 13 GLU A 308 ALA A 312 5 5
HELIX 14 14 THR A 313 LEU A 317 5 5
HELIX 15 15 GLU A 338 GLU A 355 1 18
HELIX 16 16 ASP A 359 ALA A 373 1 15
HELIX 17 17 GLU A 386 GLY A 410 1 25
HELIX 18 18 GLY A 416 LEU A 426 1 11
HELIX 19 19 ALA A 427 LEU A 429 5 3
HELIX 20 20 ASN A 433 MET A 447 1 15
HELIX 21 21 GLU A 448 ASN A 457 1 10
HELIX 22 22 GLU A 461 GLY A 472 1 12
HELIX 23 23 THR A 497 ILE A 515 1 19
HELIX 24 24 GLY B 9 VAL B 29 1 21
HELIX 25 25 ASP B 52 ILE B 60 1 9
HELIX 26 26 ASP B 64 ALA B 85 1 22
HELIX 27 27 GLY B 88 ALA B 108 1 21
HELIX 28 28 ASN B 112 SER B 135 1 24
HELIX 29 29 ASP B 140 ALA B 152 1 13
HELIX 30 30 ASP B 155 GLY B 170 1 16
HELIX 31 31 ASN B 229 GLU B 232 5 4
HELIX 32 32 MET B 233 GLY B 244 1 12
HELIX 33 33 GLU B 255 ARG B 268 1 14
HELIX 34 34 PHE B 281 GLY B 297 1 17
HELIX 35 35 GLU B 304 GLY B 306 5 3
HELIX 36 36 GLU B 308 ALA B 312 5 5
HELIX 37 37 THR B 313 LEU B 317 5 5
HELIX 38 38 GLU B 338 GLU B 355 1 18
HELIX 39 39 ASP B 359 ALA B 373 1 15
HELIX 40 40 GLU B 386 GLY B 410 1 25
HELIX 41 41 GLY B 416 LEU B 426 1 11
HELIX 42 42 ALA B 427 LEU B 429 5 3
HELIX 43 43 ASN B 433 MET B 447 1 15
HELIX 44 44 GLU B 448 ASN B 457 1 10
HELIX 45 45 GLU B 461 GLY B 472 1 12
HELIX 46 46 THR B 497 ILE B 515 1 19
HELIX 47 47 GLY C 9 VAL C 29 1 21
HELIX 48 48 ASP C 52 ARG C 58 1 7
HELIX 49 49 ASP C 64 ALA C 85 1 22
HELIX 50 50 GLY C 88 ALA C 108 1 21
HELIX 51 51 ASN C 112 SER C 135 1 24
HELIX 52 52 ASP C 140 ALA C 152 1 13
HELIX 53 53 ASP C 155 GLY C 170 1 16
HELIX 54 54 ASN C 229 GLU C 232 5 4
HELIX 55 55 MET C 233 GLY C 244 1 12
HELIX 56 56 GLU C 255 ARG C 268 1 14
HELIX 57 57 PHE C 281 GLY C 297 1 17
HELIX 58 58 GLU C 304 GLY C 306 5 3
HELIX 59 59 GLU C 308 ALA C 312 5 5
HELIX 60 60 THR C 313 LEU C 317 5 5
HELIX 61 61 GLU C 338 ALA C 356 1 19
HELIX 62 62 ASP C 359 ALA C 373 1 15
HELIX 63 63 GLU C 386 GLY C 410 1 25
HELIX 64 64 GLY C 416 LEU C 426 1 11
HELIX 65 65 ALA C 427 LEU C 429 5 3
HELIX 66 66 ASN C 433 MET C 447 1 15
HELIX 67 67 GLU C 448 CYS C 458 1 11
HELIX 68 68 GLU C 461 GLY C 472 1 12
HELIX 69 69 THR C 497 ILE C 515 1 19
HELIX 70 70 GLY D 9 LYS D 28 1 20
HELIX 71 71 VAL D 29 LEU D 31 5 3
HELIX 72 72 ASP D 52 ARG D 58 1 7
HELIX 73 73 ASP D 64 ALA D 85 1 22
HELIX 74 74 GLY D 88 ALA D 108 1 21
HELIX 75 75 ASN D 112 SER D 135 1 24
HELIX 76 76 ASP D 140 ALA D 152 1 13
HELIX 77 77 ASP D 155 GLY D 170 1 16
HELIX 78 78 ASN D 229 GLU D 232 5 4
HELIX 79 79 MET D 233 GLY D 244 1 12
HELIX 80 80 GLU D 255 ARG D 268 1 14
HELIX 81 81 PHE D 281 GLY D 297 1 17
HELIX 82 82 GLU D 304 GLY D 306 5 3
HELIX 83 83 GLU D 308 ALA D 312 5 5
HELIX 84 84 THR D 313 LEU D 317 5 5
HELIX 85 85 GLU D 338 GLU D 355 1 18
HELIX 86 86 ASP D 359 ALA D 373 1 15
HELIX 87 87 GLU D 386 GLY D 410 1 25
HELIX 88 88 GLY D 416 LEU D 426 1 11
HELIX 89 89 ALA D 427 LEU D 429 5 3
HELIX 90 90 ASN D 433 MET D 447 1 15
HELIX 91 91 GLU D 448 ASN D 457 1 10
HELIX 92 92 GLU D 461 GLY D 471 1 11
HELIX 93 93 THR D 497 ILE D 515 1 19
HELIX 94 94 GLY E 9 VAL E 29 1 21
HELIX 95 95 ASP E 52 ARG E 58 1 7
HELIX 96 96 ASP E 64 ALA E 85 1 22
HELIX 97 97 GLY E 88 ALA E 108 1 21
HELIX 98 98 ASN E 112 SER E 135 1 24
HELIX 99 99 ASP E 140 ALA E 152 1 13
HELIX 100 100 ASP E 155 GLY E 170 1 16
HELIX 101 101 ASN E 229 GLU E 232 5 4
HELIX 102 102 MET E 233 GLY E 244 1 12
HELIX 103 103 GLU E 255 ARG E 268 1 14
HELIX 104 104 PHE E 281 GLY E 297 1 17
HELIX 105 105 GLU E 304 GLY E 306 5 3
HELIX 106 106 GLU E 308 ALA E 312 5 5
HELIX 107 107 THR E 313 LEU E 317 5 5
HELIX 108 108 GLU E 338 GLU E 355 1 18
HELIX 109 109 ASP E 359 ALA E 373 1 15
HELIX 110 110 GLU E 386 GLY E 410 1 25
HELIX 111 111 GLY E 416 LEU E 426 1 11
HELIX 112 112 ALA E 427 LEU E 429 5 3
HELIX 113 113 ASN E 433 GLU E 448 1 16
HELIX 114 114 GLU E 448 ASN E 457 1 10
HELIX 115 115 GLU E 461 GLY E 472 1 12
HELIX 116 116 THR E 497 ILE E 515 1 19
HELIX 117 117 GLY F 9 VAL F 29 1 21
HELIX 118 118 ASP F 52 ARG F 58 1 7
HELIX 119 119 ASP F 64 ALA F 85 1 22
HELIX 120 120 GLY F 88 ALA F 108 1 21
HELIX 121 121 ASN F 112 SER F 135 1 24
HELIX 122 122 ASP F 140 ALA F 152 1 13
HELIX 123 123 ASP F 155 GLY F 170 1 16
HELIX 124 124 ASN F 229 GLU F 232 5 4
HELIX 125 125 MET F 233 GLY F 244 1 12
HELIX 126 126 GLU F 255 ARG F 268 1 14
HELIX 127 127 PHE F 281 GLY F 297 1 17
HELIX 128 128 GLU F 304 GLY F 306 5 3
HELIX 129 129 GLU F 308 ALA F 312 5 5
HELIX 130 130 THR F 313 LEU F 317 5 5
HELIX 131 131 GLU F 338 GLU F 355 1 18
HELIX 132 132 ASP F 359 ALA F 373 1 15
HELIX 133 133 GLU F 386 GLY F 410 1 25
HELIX 134 134 GLY F 416 LEU F 426 1 11
HELIX 135 135 ALA F 427 LEU F 429 5 3
HELIX 136 136 ASN F 433 MET F 447 1 15
HELIX 137 137 GLU F 448 ASN F 457 1 10
HELIX 138 138 GLU F 461 GLY F 471 1 11
HELIX 139 139 THR F 497 ILE F 515 1 19
HELIX 140 140 GLY G 9 VAL G 29 1 21
HELIX 141 141 ASP G 52 ARG G 58 1 7
HELIX 142 142 ASP G 64 ALA G 85 1 22
HELIX 143 143 GLY G 88 ALA G 108 1 21
HELIX 144 144 ASN G 112 SER G 135 1 24
HELIX 145 145 ASP G 140 ALA G 152 1 13
HELIX 146 146 ASP G 155 GLY G 170 1 16
HELIX 147 147 ASN G 229 GLU G 232 5 4
HELIX 148 148 MET G 233 GLY G 244 1 12
HELIX 149 149 GLU G 255 ARG G 268 1 14
HELIX 150 150 PHE G 281 GLY G 297 1 17
HELIX 151 151 GLU G 304 GLY G 306 5 3
HELIX 152 152 GLU G 308 ALA G 312 5 5
HELIX 153 153 THR G 313 LEU G 317 5 5
HELIX 154 154 GLU G 338 GLU G 355 1 18
HELIX 155 155 ASP G 359 ALA G 373 1 15
HELIX 156 156 GLU G 386 GLY G 410 1 25
HELIX 157 157 GLY G 416 LEU G 426 1 11
HELIX 158 158 ALA G 427 LEU G 429 5 3
HELIX 159 159 ASN G 433 MET G 447 1 15
HELIX 160 160 GLU G 448 ASN G 457 1 10
HELIX 161 161 GLU G 461 GLY G 471 1 11
HELIX 162 162 THR G 497 ILE G 515 1 19
HELIX 163 163 GLY H 9 LYS H 28 1 20
HELIX 164 164 VAL H 29 LEU H 31 5 3
HELIX 165 165 ASP H 52 ILE H 60 1 9
HELIX 166 166 PHE H 66 ALA H 84 1 19
HELIX 167 167 GLY H 88 ALA H 108 1 21
HELIX 168 168 ASN H 112 SER H 135 1 24
HELIX 169 169 ASP H 140 ALA H 152 1 13
HELIX 170 170 ASP H 155 GLY H 170 1 16
HELIX 171 171 MET H 233 ALA H 243 1 11
HELIX 172 172 GLU H 255 ARG H 268 1 14
HELIX 173 173 PHE H 281 GLY H 297 1 17
HELIX 174 174 THR H 313 LEU H 317 5 5
HELIX 175 175 GLU H 338 ILE H 353 1 16
HELIX 176 176 SER H 358 GLY H 375 1 18
HELIX 177 177 THR H 385 GLY H 410 1 26
HELIX 178 178 GLY H 416 LEU H 426 1 11
HELIX 179 179 ASN H 433 MET H 447 1 15
HELIX 180 180 GLU H 448 CYS H 458 1 11
HELIX 181 181 GLU H 461 GLY H 471 1 11
HELIX 182 182 THR H 497 THR H 516 1 20
HELIX 183 183 GLY I 9 LYS I 28 1 20
HELIX 184 184 VAL I 29 LEU I 31 5 3
HELIX 185 185 ASP I 52 ILE I 60 1 9
HELIX 186 186 PHE I 66 ALA I 84 1 19
HELIX 187 187 GLY I 88 ALA I 108 1 21
HELIX 188 188 ASN I 112 SER I 135 1 24
HELIX 189 189 ASP I 140 ALA I 152 1 13
HELIX 190 190 ASP I 155 GLY I 170 1 16
HELIX 191 191 MET I 233 ALA I 241 1 9
HELIX 192 192 GLU I 255 ARG I 268 1 14
HELIX 193 193 PHE I 281 GLY I 297 1 17
HELIX 194 194 THR I 313 LEU I 317 5 5
HELIX 195 195 GLU I 338 ILE I 353 1 16
HELIX 196 196 SER I 358 GLY I 375 1 18
HELIX 197 197 THR I 385 GLY I 410 1 26
HELIX 198 198 GLY I 416 LEU I 426 1 11
HELIX 199 199 ASN I 433 MET I 447 1 15
HELIX 200 200 GLU I 448 CYS I 458 1 11
HELIX 201 201 GLU I 461 GLY I 472 1 12
HELIX 202 202 THR I 497 THR I 516 1 20
HELIX 203 203 GLY J 9 LYS J 28 1 20
HELIX 204 204 VAL J 29 LEU J 31 5 3
HELIX 205 205 ASP J 52 ILE J 60 1 9
HELIX 206 206 PHE J 66 ALA J 84 1 19
HELIX 207 207 GLY J 88 ALA J 108 1 21
HELIX 208 208 ASN J 112 SER J 135 1 24
HELIX 209 209 ASP J 140 ALA J 152 1 13
HELIX 210 210 ASP J 155 GLY J 170 1 16
HELIX 211 211 MET J 233 ALA J 241 1 9
HELIX 212 212 GLU J 255 ARG J 268 1 14
HELIX 213 213 PHE J 281 GLY J 297 1 17
HELIX 214 214 THR J 313 LEU J 317 5 5
HELIX 215 215 GLU J 338 ILE J 353 1 16
HELIX 216 216 SER J 358 GLY J 375 1 18
HELIX 217 217 THR J 385 GLY J 410 1 26
HELIX 218 218 GLY J 416 LEU J 426 1 11
HELIX 219 219 ASN J 433 MET J 447 1 15
HELIX 220 220 GLU J 448 ASN J 457 1 10
HELIX 221 221 GLU J 461 GLY J 471 1 11
HELIX 222 222 THR J 497 THR J 516 1 20
HELIX 223 223 GLY K 9 LYS K 28 1 20
HELIX 224 224 VAL K 29 LEU K 31 5 3
HELIX 225 225 ASP K 52 ILE K 60 1 9
HELIX 226 226 PHE K 66 ALA K 84 1 19
HELIX 227 227 GLY K 88 ALA K 108 1 21
HELIX 228 228 ASN K 112 SER K 135 1 24
HELIX 229 229 ASP K 140 ALA K 152 1 13
HELIX 230 230 ASP K 155 GLY K 170 1 16
HELIX 231 231 MET K 233 ALA K 243 1 11
HELIX 232 232 GLU K 255 ARG K 268 1 14
HELIX 233 233 PHE K 281 GLY K 297 1 17
HELIX 234 234 THR K 313 LEU K 317 5 5
HELIX 235 235 GLU K 338 ILE K 353 1 16
HELIX 236 236 SER K 358 GLY K 375 1 18
HELIX 237 237 THR K 385 GLY K 410 1 26
HELIX 238 238 GLY K 416 LEU K 426 1 11
HELIX 239 239 ASN K 433 ALA K 446 1 14
HELIX 240 240 GLU K 448 CYS K 458 1 11
HELIX 241 241 GLU K 461 GLY K 471 1 11
HELIX 242 242 THR K 497 THR K 516 1 20
HELIX 243 243 GLY L 9 LYS L 28 1 20
HELIX 244 244 VAL L 29 LEU L 31 5 3
HELIX 245 245 ASP L 52 ILE L 60 1 9
HELIX 246 246 PHE L 66 ALA L 84 1 19
HELIX 247 247 GLY L 88 ALA L 108 1 21
HELIX 248 248 ASN L 112 SER L 135 1 24
HELIX 249 249 ASP L 140 ALA L 152 1 13
HELIX 250 250 ASP L 155 GLY L 170 1 16
HELIX 251 251 MET L 233 ALA L 241 1 9
HELIX 252 252 GLU L 255 ARG L 268 1 14
HELIX 253 253 PHE L 281 GLY L 297 1 17
HELIX 254 254 THR L 313 LEU L 317 5 5
HELIX 255 255 GLU L 338 ILE L 353 1 16
HELIX 256 256 SER L 358 GLY L 375 1 18
HELIX 257 257 THR L 385 GLY L 410 1 26
HELIX 258 258 GLY L 416 LEU L 426 1 11
HELIX 259 259 ASN L 433 MET L 447 1 15
HELIX 260 260 GLU L 448 CYS L 458 1 11
HELIX 261 261 GLU L 461 GLY L 472 1 12
HELIX 262 262 THR L 497 THR L 516 1 20
HELIX 263 263 GLY M 9 LYS M 28 1 20
HELIX 264 264 VAL M 29 LEU M 31 5 3
HELIX 265 265 ASP M 52 ILE M 60 1 9
HELIX 266 266 PHE M 66 ALA M 84 1 19
HELIX 267 267 GLY M 88 ALA M 108 1 21
HELIX 268 268 ASN M 112 SER M 135 1 24
HELIX 269 269 ASP M 140 ALA M 152 1 13
HELIX 270 270 ASP M 155 GLY M 170 1 16
HELIX 271 271 MET M 233 ALA M 241 1 9
HELIX 272 272 GLU M 255 ARG M 268 1 14
HELIX 273 273 PHE M 281 GLY M 297 1 17
HELIX 274 274 THR M 313 LEU M 317 5 5
HELIX 275 275 GLU M 338 ILE M 353 1 16
HELIX 276 276 SER M 358 GLY M 375 1 18
HELIX 277 277 THR M 385 GLY M 410 1 26
HELIX 278 278 GLY M 416 LEU M 426 1 11
HELIX 279 279 ASN M 433 MET M 447 1 15
HELIX 280 280 GLU M 448 ASN M 457 1 10
HELIX 281 281 GLU M 461 GLY M 471 1 11
HELIX 282 282 THR M 497 THR M 516 1 20
HELIX 283 283 GLY N 9 LYS N 28 1 20
HELIX 284 284 VAL N 29 LEU N 31 5 3
HELIX 285 285 ASP N 52 ILE N 60 1 9
HELIX 286 286 PHE N 66 ALA N 84 1 19
HELIX 287 287 GLY N 88 ALA N 108 1 21
HELIX 288 288 ASN N 112 SER N 135 1 24
HELIX 289 289 ASP N 140 ALA N 152 1 13
HELIX 290 290 ASP N 155 GLY N 170 1 16
HELIX 291 291 MET N 233 ALA N 243 1 11
HELIX 292 292 GLU N 255 ARG N 268 1 14
HELIX 293 293 PHE N 281 GLY N 297 1 17
HELIX 294 294 THR N 313 LEU N 317 5 5
HELIX 295 295 GLU N 338 ILE N 353 1 16
HELIX 296 296 SER N 358 GLY N 375 1 18
HELIX 297 297 THR N 385 GLY N 410 1 26
HELIX 298 298 GLY N 416 LEU N 426 1 11
HELIX 299 299 ASN N 433 MET N 447 1 15
HELIX 300 300 GLU N 448 CYS N 458 1 11
HELIX 301 301 GLU N 461 GLY N 471 1 11
HELIX 302 302 THR N 497 THR N 516 1 20
SHEET 1 A 4 LYS A 4 PHE A 8 0
SHEET 2 A 4 THR A 517 ASP A 523 -1 O THR A 522 N ASP A 5
SHEET 3 A 4 ASN B 37 LEU B 40 1 O ASN B 37 N GLU A 518
SHEET 4 A 4 THR B 48 THR B 50 -1 O THR B 48 N LEU B 40
SHEET 1 B 4 THR A 48 THR A 50 0
SHEET 2 B 4 ASN A 37 LEU A 40 -1 N VAL A 38 O THR A 50
SHEET 3 B 4 THR G 517 ASP G 523 1 O CYS G 519 N VAL A 39
SHEET 4 B 4 LYS G 4 PHE G 8 -1 N ASP G 5 O THR G 522
SHEET 1 C 3 ILE A 175 ASP A 179 0
SHEET 2 C 3 VAL A 376 VAL A 381 1 O ILE A 379 N THR A 176
SHEET 3 C 3 GLU A 186 VAL A 190 -1 N GLU A 186 O LYS A 380
SHEET 1 D 6 MET A 193 PHE A 195 0
SHEET 2 D 6 THR A 330 GLY A 335 -1 O THR A 330 N PHE A 195
SHEET 3 D 6 GLY A 318 ILE A 325 -1 N VAL A 324 O THR A 331
SHEET 4 D 6 PHE A 219 ILE A 227 -1 N ILE A 220 O GLY A 318
SHEET 5 D 6 LEU A 247 VAL A 254 1 O LEU A 248 N LEU A 221
SHEET 6 D 6 VAL A 273 LYS A 277 1 O ALA A 274 N ILE A 249
SHEET 1 E 4 VAL A 213 GLU A 216 0
SHEET 2 E 4 GLY A 318 ILE A 325 -1 O VAL A 323 N LEU A 215
SHEET 3 E 4 PHE A 219 ILE A 227 -1 N ILE A 220 O GLY A 318
SHEET 4 E 4 ILE A 301 SER A 302 1 O ILE A 301 N LEU A 222
SHEET 1 F 2 VAL A 411 ALA A 413 0
SHEET 2 F 2 LEU A 494 PRO A 496 -1 O ASP A 495 N VAL A 412
SHEET 1 G 2 TYR A 476 ASN A 479 0
SHEET 2 G 2 GLU A 484 ASN A 487 -1 O GLY A 486 N GLY A 477
SHEET 1 H 4 LYS B 4 PHE B 8 0
SHEET 2 H 4 THR B 517 ASP B 523 -1 O THR B 522 N ASP B 5
SHEET 3 H 4 ASN C 37 LEU C 40 1 O ASN C 37 N GLU B 518
SHEET 4 H 4 THR C 48 THR C 50 -1 O THR C 48 N LEU C 40
SHEET 1 I 3 ILE B 175 ASP B 179 0
SHEET 2 I 3 VAL B 376 VAL B 381 1 O ILE B 379 N THR B 176
SHEET 3 I 3 GLU B 186 VAL B 190 -1 N GLU B 186 O LYS B 380
SHEET 1 J 6 MET B 193 PHE B 195 0
SHEET 2 J 6 THR B 330 GLY B 335 -1 O THR B 330 N PHE B 195
SHEET 3 J 6 GLY B 318 ILE B 325 -1 N VAL B 324 O THR B 331
SHEET 4 J 6 PHE B 219 ILE B 227 -1 N ILE B 220 O GLY B 318
SHEET 5 J 6 LEU B 247 VAL B 254 1 O LEU B 248 N LEU B 221
SHEET 6 J 6 VAL B 273 LYS B 277 1 O ALA B 274 N ILE B 249
SHEET 1 K 4 VAL B 213 GLU B 216 0
SHEET 2 K 4 GLY B 318 ILE B 325 -1 O ILE B 325 N VAL B 213
SHEET 3 K 4 PHE B 219 ILE B 227 -1 N ILE B 220 O GLY B 318
SHEET 4 K 4 ILE B 301 SER B 302 1 O ILE B 301 N LEU B 222
SHEET 1 L 2 VAL B 411 ALA B 413 0
SHEET 2 L 2 LEU B 494 PRO B 496 -1 O ASP B 495 N VAL B 412
SHEET 1 M 2 TYR B 476 ASN B 479 0
SHEET 2 M 2 GLU B 484 ASN B 487 -1 O GLY B 486 N GLY B 477
SHEET 1 N 4 LYS C 4 PHE C 8 0
SHEET 2 N 4 THR C 517 ASP C 523 -1 O THR C 522 N ASP C 5
SHEET 3 N 4 ASN D 37 LEU D 40 1 O ASN D 37 N GLU C 518
SHEET 4 N 4 THR D 48 THR D 50 -1 O THR D 50 N VAL D 38
SHEET 1 O 3 ILE C 175 ASP C 179 0
SHEET 2 O 3 VAL C 376 VAL C 381 1 O ILE C 379 N THR C 176
SHEET 3 O 3 GLU C 186 VAL C 190 -1 N GLU C 186 O LYS C 380
SHEET 1 P 6 MET C 193 PHE C 195 0
SHEET 2 P 6 THR C 330 GLY C 335 -1 O THR C 330 N PHE C 195
SHEET 3 P 6 GLY C 318 ILE C 325 -1 N VAL C 324 O THR C 331
SHEET 4 P 6 PHE C 219 ILE C 227 -1 N ILE C 220 O GLY C 318
SHEET 5 P 6 LEU C 247 VAL C 254 1 O ILE C 250 N LEU C 221
SHEET 6 P 6 VAL C 273 LYS C 277 1 O ALA C 274 N ILE C 249
SHEET 1 Q 4 VAL C 213 GLU C 216 0
SHEET 2 Q 4 GLY C 318 ILE C 325 -1 O ILE C 325 N VAL C 213
SHEET 3 Q 4 PHE C 219 ILE C 227 -1 N ILE C 220 O GLY C 318
SHEET 4 Q 4 ILE C 301 SER C 302 1 O ILE C 301 N LEU C 222
SHEET 1 R 2 VAL C 411 ALA C 413 0
SHEET 2 R 2 LEU C 494 PRO C 496 -1 O ASP C 495 N VAL C 412
SHEET 1 S 2 TYR C 476 ASN C 479 0
SHEET 2 S 2 GLU C 484 ASN C 487 -1 O GLY C 486 N GLY C 477
SHEET 1 T 4 LYS D 4 PHE D 8 0
SHEET 2 T 4 THR D 517 ASP D 523 -1 O THR D 522 N ASP D 5
SHEET 3 T 4 ASN E 37 LEU E 40 1 O ASN E 37 N GLU D 518
SHEET 4 T 4 THR E 48 THR E 50 -1 O THR E 50 N VAL E 38
SHEET 1 U 3 ILE D 175 ASP D 179 0
SHEET 2 U 3 VAL D 376 VAL D 381 1 O ILE D 379 N THR D 176
SHEET 3 U 3 GLU D 186 VAL D 190 -1 N GLU D 186 O LYS D 380
SHEET 1 V 6 MET D 193 PHE D 195 0
SHEET 2 V 6 THR D 330 GLY D 335 -1 O THR D 330 N PHE D 195
SHEET 3 V 6 GLY D 318 ILE D 325 -1 N VAL D 324 O THR D 331
SHEET 4 V 6 PHE D 219 ILE D 227 -1 N ILE D 220 O GLY D 318
SHEET 5 V 6 LEU D 247 VAL D 254 1 O ILE D 250 N LEU D 221
SHEET 6 V 6 VAL D 273 LYS D 277 1 O ALA D 274 N ILE D 249
SHEET 1 W 4 VAL D 213 GLU D 216 0
SHEET 2 W 4 GLY D 318 ILE D 325 -1 O ILE D 325 N VAL D 213
SHEET 3 W 4 PHE D 219 ILE D 227 -1 N ILE D 220 O GLY D 318
SHEET 4 W 4 ILE D 301 SER D 302 1 O ILE D 301 N LEU D 222
SHEET 1 X 2 VAL D 411 ALA D 413 0
SHEET 2 X 2 LEU D 494 PRO D 496 -1 O ASP D 495 N VAL D 412
SHEET 1 Y 2 TYR D 476 ASN D 479 0
SHEET 2 Y 2 GLU D 484 ASN D 487 -1 O GLY D 486 N GLY D 477
SHEET 1 Z 4 LYS E 4 PHE E 8 0
SHEET 2 Z 4 THR E 517 ASP E 523 -1 O THR E 522 N ASP E 5
SHEET 3 Z 4 ASN F 37 LEU F 40 1 O ASN F 37 N GLU E 518
SHEET 4 Z 4 THR F 48 THR F 50 -1 O THR F 48 N LEU F 40
SHEET 1 AA 3 VAL E 174 ASP E 179 0
SHEET 2 AA 3 VAL E 376 VAL E 381 1 O ILE E 379 N THR E 176
SHEET 3 AA 3 GLU E 186 VAL E 190 -1 N GLU E 186 O LYS E 380
SHEET 1 AB 6 MET E 193 PHE E 195 0
SHEET 2 AB 6 THR E 330 GLY E 335 -1 O THR E 330 N PHE E 195
SHEET 3 AB 6 GLY E 318 ILE E 325 -1 N VAL E 324 O THR E 331
SHEET 4 AB 6 PHE E 219 ILE E 227 -1 N ILE E 220 O GLY E 318
SHEET 5 AB 6 LEU E 247 VAL E 254 1 O LEU E 248 N LEU E 221
SHEET 6 AB 6 VAL E 273 LYS E 277 1 O ALA E 274 N ILE E 249
SHEET 1 AC 4 VAL E 213 GLU E 216 0
SHEET 2 AC 4 GLY E 318 ILE E 325 -1 O ILE E 325 N VAL E 213
SHEET 3 AC 4 PHE E 219 ILE E 227 -1 N ILE E 220 O GLY E 318
SHEET 4 AC 4 ILE E 301 SER E 302 1 O ILE E 301 N LEU E 222
SHEET 1 AD 2 VAL E 411 ALA E 413 0
SHEET 2 AD 2 LEU E 494 PRO E 496 -1 O ASP E 495 N VAL E 412
SHEET 1 AE 2 TYR E 476 ASN E 479 0
SHEET 2 AE 2 GLU E 484 ASN E 487 -1 O GLY E 486 N GLY E 477
SHEET 1 AF 4 LYS F 4 PHE F 8 0
SHEET 2 AF 4 THR F 517 ASP F 523 -1 O THR F 522 N ASP F 5
SHEET 3 AF 4 ASN G 37 LEU G 40 1 O ASN G 37 N GLU F 518
SHEET 4 AF 4 THR G 48 THR G 50 -1 O THR G 48 N LEU G 40
SHEET 1 AG 3 ILE F 175 ASP F 179 0
SHEET 2 AG 3 VAL F 376 VAL F 381 1 O ILE F 379 N THR F 176
SHEET 3 AG 3 GLU F 186 VAL F 190 -1 N GLU F 186 O LYS F 380
SHEET 1 AH 6 MET F 193 PHE F 195 0
SHEET 2 AH 6 THR F 330 GLY F 335 -1 O THR F 330 N PHE F 195
SHEET 3 AH 6 GLY F 318 ILE F 325 -1 N VAL F 324 O THR F 331
SHEET 4 AH 6 PHE F 219 ILE F 227 -1 N ILE F 220 O GLY F 318
SHEET 5 AH 6 LEU F 247 VAL F 254 1 O LEU F 248 N LEU F 221
SHEET 6 AH 6 VAL F 273 LYS F 277 1 O ALA F 274 N ILE F 249
SHEET 1 AI 4 VAL F 213 GLU F 216 0
SHEET 2 AI 4 GLY F 318 ILE F 325 -1 O ILE F 325 N VAL F 213
SHEET 3 AI 4 PHE F 219 ILE F 227 -1 N ILE F 220 O GLY F 318
SHEET 4 AI 4 ILE F 301 SER F 302 1 O ILE F 301 N LEU F 222
SHEET 1 AJ 2 VAL F 411 ALA F 413 0
SHEET 2 AJ 2 LEU F 494 PRO F 496 -1 O ASP F 495 N VAL F 412
SHEET 1 AK 2 TYR F 476 ASN F 479 0
SHEET 2 AK 2 GLU F 484 ASN F 487 -1 O GLY F 486 N GLY F 477
SHEET 1 AL 3 VAL G 174 ASP G 179 0
SHEET 2 AL 3 VAL G 376 VAL G 381 1 O ILE G 379 N THR G 176
SHEET 3 AL 3 GLU G 186 VAL G 190 -1 N GLU G 186 O LYS G 380
SHEET 1 AM 6 MET G 193 PHE G 195 0
SHEET 2 AM 6 THR G 330 GLY G 335 -1 O THR G 330 N PHE G 195
SHEET 3 AM 6 GLY G 318 ILE G 325 -1 N VAL G 324 O THR G 331
SHEET 4 AM 6 PHE G 219 ILE G 227 -1 N ILE G 220 O GLY G 318
SHEET 5 AM 6 LEU G 247 VAL G 254 1 O LEU G 248 N LEU G 221
SHEET 6 AM 6 VAL G 273 LYS G 277 1 O ALA G 274 N ILE G 249
SHEET 1 AN 4 VAL G 213 GLU G 216 0
SHEET 2 AN 4 GLY G 318 ILE G 325 -1 O ILE G 325 N VAL G 213
SHEET 3 AN 4 PHE G 219 ILE G 227 -1 N ILE G 220 O GLY G 318
SHEET 4 AN 4 ILE G 301 SER G 302 1 O ILE G 301 N LEU G 222
SHEET 1 AO 2 VAL G 411 ALA G 413 0
SHEET 2 AO 2 LEU G 494 PRO G 496 -1 O ASP G 495 N VAL G 412
SHEET 1 AP 2 TYR G 476 ASN G 479 0
SHEET 2 AP 2 GLU G 484 ASN G 487 -1 O GLY G 486 N GLY G 477
SHEET 1 AQ 4 LYS H 4 PHE H 8 0
SHEET 2 AQ 4 THR H 517 ASP H 523 -1 O THR H 522 N ASP H 5
SHEET 3 AQ 4 ASN N 37 LEU N 40 1 O VAL N 39 N VAL H 521
SHEET 4 AQ 4 THR N 48 THR N 50 -1 O THR N 48 N LEU N 40
SHEET 1 AR 4 THR H 48 THR H 50 0
SHEET 2 AR 4 ASN H 37 LEU H 40 -1 N LEU H 40 O THR H 48
SHEET 3 AR 4 THR I 517 ASP I 523 1 O CYS I 519 N VAL H 39
SHEET 4 AR 4 LYS I 4 PHE I 8 -1 N ASP I 5 O THR I 522
SHEET 1 AS 3 VAL H 174 ASP H 179 0
SHEET 2 AS 3 VAL H 376 VAL H 381 1 O ALA H 377 N VAL H 174
SHEET 3 AS 3 ASP H 188 VAL H 190 -1 N VAL H 190 O VAL H 376
SHEET 1 AT 6 MET H 193 PHE H 195 0
SHEET 2 AT 6 THR H 330 GLY H 335 -1 O ILE H 332 N MET H 193
SHEET 3 AT 6 GLY H 318 ILE H 325 -1 N ARG H 322 O ILE H 333
SHEET 4 AT 6 PHE H 219 ILE H 227 -1 N ILE H 220 O GLY H 318
SHEET 5 AT 6 LEU H 247 VAL H 254 1 O LEU H 248 N LEU H 221
SHEET 6 AT 6 VAL H 273 LYS H 277 1 O VAL H 276 N ILE H 249
SHEET 1 AU 4 VAL H 213 GLU H 216 0
SHEET 2 AU 4 GLY H 318 ILE H 325 -1 O ILE H 325 N VAL H 213
SHEET 3 AU 4 PHE H 219 ILE H 227 -1 N ILE H 220 O GLY H 318
SHEET 4 AU 4 VAL H 300 SER H 302 1 O ILE H 301 N LEU H 222
SHEET 1 AV 2 VAL H 411 ALA H 413 0
SHEET 2 AV 2 LEU H 494 PRO H 496 -1 O ASP H 495 N VAL H 412
SHEET 1 AW 2 TYR H 476 ASN H 479 0
SHEET 2 AW 2 GLU H 484 ASN H 487 -1 O GLY H 486 N GLY H 477
SHEET 1 AX 4 THR I 48 THR I 50 0
SHEET 2 AX 4 ASN I 37 LEU I 40 -1 N LEU I 40 O THR I 48
SHEET 3 AX 4 THR J 517 ASP J 523 1 O GLU J 518 N ASN I 37
SHEET 4 AX 4 LYS J 4 PHE J 8 -1 N ASP J 5 O THR J 522
SHEET 1 AY 3 VAL I 174 ASP I 179 0
SHEET 2 AY 3 VAL I 376 VAL I 381 1 O ALA I 377 N THR I 176
SHEET 3 AY 3 GLU I 186 VAL I 190 -1 N VAL I 190 O VAL I 376
SHEET 1 AZ 6 MET I 193 PHE I 195 0
SHEET 2 AZ 6 THR I 330 GLY I 335 -1 O ILE I 332 N MET I 193
SHEET 3 AZ 6 GLY I 318 ILE I 325 -1 N ARG I 322 O ILE I 333
SHEET 4 AZ 6 PHE I 219 ILE I 227 -1 N ILE I 220 O GLY I 318
SHEET 5 AZ 6 LEU I 247 VAL I 254 1 O LEU I 248 N LEU I 221
SHEET 6 AZ 6 VAL I 273 LYS I 277 1 O VAL I 276 N ILE I 249
SHEET 1 BA 4 VAL I 213 GLU I 216 0
SHEET 2 BA 4 GLY I 318 ILE I 325 -1 O ILE I 325 N VAL I 213
SHEET 3 BA 4 PHE I 219 ILE I 227 -1 N ILE I 220 O GLY I 318
SHEET 4 BA 4 VAL I 300 SER I 302 1 O ILE I 301 N LEU I 222
SHEET 1 BB 2 VAL I 411 ALA I 413 0
SHEET 2 BB 2 LEU I 494 PRO I 496 -1 O ASP I 495 N VAL I 412
SHEET 1 BC 2 TYR I 476 ASN I 479 0
SHEET 2 BC 2 GLU I 484 ASN I 487 -1 O GLU I 484 N ASN I 479
SHEET 1 BD 4 THR J 48 THR J 50 0
SHEET 2 BD 4 ASN J 37 LEU J 40 -1 N LEU J 40 O THR J 48
SHEET 3 BD 4 THR K 517 ASP K 523 1 O CYS K 519 N VAL J 39
SHEET 4 BD 4 LYS K 4 PHE K 8 -1 N ASP K 5 O THR K 522
SHEET 1 BE 3 VAL J 174 ASP J 179 0
SHEET 2 BE 3 VAL J 376 VAL J 381 1 O ALA J 377 N VAL J 174
SHEET 3 BE 3 GLU J 186 VAL J 190 -1 N VAL J 190 O VAL J 376
SHEET 1 BF 6 MET J 193 PHE J 195 0
SHEET 2 BF 6 THR J 330 GLY J 335 -1 O THR J 330 N PHE J 195
SHEET 3 BF 6 GLY J 318 ILE J 325 -1 N ARG J 322 O ILE J 333
SHEET 4 BF 6 PHE J 219 ILE J 227 -1 N ILE J 220 O GLY J 318
SHEET 5 BF 6 LEU J 247 VAL J 254 1 O LEU J 248 N LEU J 221
SHEET 6 BF 6 VAL J 273 LYS J 277 1 O VAL J 276 N ILE J 249
SHEET 1 BG 4 VAL J 213 GLU J 216 0
SHEET 2 BG 4 GLY J 318 ILE J 325 -1 O ILE J 325 N VAL J 213
SHEET 3 BG 4 PHE J 219 ILE J 227 -1 N ILE J 220 O GLY J 318
SHEET 4 BG 4 VAL J 300 SER J 302 1 O ILE J 301 N ASP J 224
SHEET 1 BH 2 VAL J 411 ALA J 413 0
SHEET 2 BH 2 LEU J 494 PRO J 496 -1 O ASP J 495 N VAL J 412
SHEET 1 BI 2 TYR J 476 ASN J 479 0
SHEET 2 BI 2 GLU J 484 ASN J 487 -1 O GLY J 486 N GLY J 477
SHEET 1 BJ 4 THR K 48 THR K 50 0
SHEET 2 BJ 4 ASN K 37 LEU K 40 -1 N LEU K 40 O THR K 48
SHEET 3 BJ 4 THR L 517 ASP L 523 1 O VAL L 521 N VAL K 39
SHEET 4 BJ 4 LYS L 4 PHE L 8 -1 N ASP L 5 O THR L 522
SHEET 1 BK 3 VAL K 174 ASP K 179 0
SHEET 2 BK 3 VAL K 376 VAL K 381 1 O ALA K 377 N VAL K 174
SHEET 3 BK 3 GLU K 186 VAL K 190 -1 N VAL K 190 O VAL K 376
SHEET 1 BL 6 MET K 193 PHE K 195 0
SHEET 2 BL 6 THR K 330 GLY K 335 -1 O ILE K 332 N MET K 193
SHEET 3 BL 6 GLY K 318 ILE K 325 -1 N ARG K 322 O ILE K 333
SHEET 4 BL 6 PHE K 219 ILE K 227 -1 N ILE K 220 O GLY K 318
SHEET 5 BL 6 LEU K 247 VAL K 254 1 O LEU K 248 N LEU K 221
SHEET 6 BL 6 VAL K 273 LYS K 277 1 O VAL K 276 N ILE K 249
SHEET 1 BM 4 VAL K 213 GLU K 216 0
SHEET 2 BM 4 GLY K 318 ILE K 325 -1 O ILE K 325 N VAL K 213
SHEET 3 BM 4 PHE K 219 ILE K 227 -1 N ILE K 220 O GLY K 318
SHEET 4 BM 4 VAL K 300 SER K 302 1 O ILE K 301 N ASP K 224
SHEET 1 BN 2 VAL K 411 ALA K 413 0
SHEET 2 BN 2 LEU K 494 PRO K 496 -1 O ASP K 495 N VAL K 412
SHEET 1 BO 2 TYR K 476 ASN K 479 0
SHEET 2 BO 2 GLU K 484 ASN K 487 -1 O GLY K 486 N GLY K 477
SHEET 1 BP 4 THR L 48 THR L 50 0
SHEET 2 BP 4 ASN L 37 LEU L 40 -1 N LEU L 40 O THR L 48
SHEET 3 BP 4 THR M 517 ASP M 523 1 O GLU M 518 N ASN L 37
SHEET 4 BP 4 LYS M 4 PHE M 8 -1 N ASP M 5 O THR M 522
SHEET 1 BQ 3 VAL L 174 ASP L 179 0
SHEET 2 BQ 3 VAL L 376 VAL L 381 1 O ALA L 377 N VAL L 174
SHEET 3 BQ 3 GLU L 186 VAL L 190 -1 N VAL L 190 O VAL L 376
SHEET 1 BR 6 MET L 193 PHE L 195 0
SHEET 2 BR 6 THR L 330 GLY L 335 -1 O ILE L 332 N MET L 193
SHEET 3 BR 6 GLY L 318 ILE L 325 -1 N ARG L 322 O ILE L 333
SHEET 4 BR 6 PHE L 219 ILE L 227 -1 N ILE L 220 O GLY L 318
SHEET 5 BR 6 LEU L 247 VAL L 254 1 O LEU L 248 N LEU L 221
SHEET 6 BR 6 VAL L 273 LYS L 277 1 O VAL L 276 N ILE L 249
SHEET 1 BS 4 VAL L 213 GLU L 216 0
SHEET 2 BS 4 GLY L 318 ILE L 325 -1 O ILE L 325 N VAL L 213
SHEET 3 BS 4 PHE L 219 ILE L 227 -1 N ILE L 220 O GLY L 318
SHEET 4 BS 4 VAL L 300 SER L 302 1 O ILE L 301 N LEU L 222
SHEET 1 BT 2 VAL L 411 ALA L 413 0
SHEET 2 BT 2 LEU L 494 PRO L 496 -1 O ASP L 495 N VAL L 412
SHEET 1 BU 2 TYR L 476 ASN L 479 0
SHEET 2 BU 2 GLU L 484 ASN L 487 -1 O GLY L 486 N GLY L 477
SHEET 1 BV 4 THR M 48 THR M 50 0
SHEET 2 BV 4 ASN M 37 LEU M 40 -1 N LEU M 40 O THR M 48
SHEET 3 BV 4 THR N 517 ASP N 523 1 O GLU N 518 N ASN M 37
SHEET 4 BV 4 LYS N 4 PHE N 8 -1 N ASP N 5 O THR N 522
SHEET 1 BW 3 VAL M 174 ASP M 179 0
SHEET 2 BW 3 VAL M 376 VAL M 381 1 O ALA M 377 N VAL M 174
SHEET 3 BW 3 ASP M 188 VAL M 190 -1 N VAL M 190 O VAL M 376
SHEET 1 BX 6 MET M 193 PHE M 195 0
SHEET 2 BX 6 THR M 330 GLY M 335 -1 O ILE M 332 N MET M 193
SHEET 3 BX 6 GLY M 318 ILE M 325 -1 N ARG M 322 O ILE M 333
SHEET 4 BX 6 PHE M 219 ILE M 227 -1 N ILE M 220 O GLY M 318
SHEET 5 BX 6 LEU M 247 VAL M 254 1 O LEU M 248 N LEU M 221
SHEET 6 BX 6 VAL M 273 LYS M 277 1 O VAL M 276 N ILE M 249
SHEET 1 BY 4 VAL M 213 GLU M 216 0
SHEET 2 BY 4 GLY M 318 ILE M 325 -1 O VAL M 323 N LEU M 215
SHEET 3 BY 4 PHE M 219 ILE M 227 -1 N ILE M 220 O GLY M 318
SHEET 4 BY 4 VAL M 300 SER M 302 1 O ILE M 301 N LEU M 222
SHEET 1 BZ 2 VAL M 411 ALA M 413 0
SHEET 2 BZ 2 LEU M 494 PRO M 496 -1 O ASP M 495 N VAL M 412
SHEET 1 CA 2 TYR M 476 ASN M 479 0
SHEET 2 CA 2 GLU M 484 ASN M 487 -1 O GLU M 484 N ASN M 479
SHEET 1 CB 3 VAL N 174 ASP N 179 0
SHEET 2 CB 3 VAL N 376 VAL N 381 1 O ALA N 377 N VAL N 174
SHEET 3 CB 3 ASP N 188 VAL N 190 -1 N VAL N 190 O VAL N 376
SHEET 1 CC 6 MET N 193 PHE N 195 0
SHEET 2 CC 6 THR N 330 GLY N 335 -1 O ILE N 332 N MET N 193
SHEET 3 CC 6 GLY N 318 ILE N 325 -1 N ARG N 322 O ILE N 333
SHEET 4 CC 6 PHE N 219 ILE N 227 -1 N ILE N 220 O GLY N 318
SHEET 5 CC 6 LEU N 247 VAL N 254 1 O LEU N 248 N LEU N 221
SHEET 6 CC 6 VAL N 273 LYS N 277 1 O VAL N 276 N ILE N 249
SHEET 1 CD 4 VAL N 213 GLU N 216 0
SHEET 2 CD 4 GLY N 318 ILE N 325 -1 O ILE N 325 N VAL N 213
SHEET 3 CD 4 PHE N 219 ILE N 227 -1 N ILE N 220 O GLY N 318
SHEET 4 CD 4 VAL N 300 SER N 302 1 O ILE N 301 N LEU N 222
SHEET 1 CE 2 VAL N 411 ALA N 413 0
SHEET 2 CE 2 LEU N 494 PRO N 496 -1 O ASP N 495 N VAL N 412
SHEET 1 CF 2 TYR N 476 ASN N 479 0
SHEET 2 CF 2 GLU N 484 ASN N 487 -1 O GLY N 486 N GLY N 477
SHEET 1 CG 7 ILE O 3 PRO O 5 0
SHEET 2 CG 7 ILE U 91 VAL U 95 -1 O ILE U 94 N ARG O 4
SHEET 3 CG 7 ILE U 64 PHE U 67 -1 N ILE U 64 O VAL U 95
SHEET 4 CG 7 ARG U 37 VAL U 43 -1 N GLY U 38 O VAL U 65
SHEET 5 CG 7 ARG U 9 ARG U 14 -1 N ILE U 11 O LEU U 41
SHEET 6 CG 7 GLU U 81 SER U 87 -1 O MET U 86 N VAL U 10
SHEET 7 CG 7 LYS U 74 ILE U 78 -1 N GLU U 76 O VAL U 83
SHEET 1 CH 7 LYS O 74 ILE O 78 0
SHEET 2 CH 7 GLU O 81 SER O 87 -1 O VAL O 83 N GLU O 76
SHEET 3 CH 7 ARG O 9 ARG O 14 -1 N VAL O 10 O MET O 86
SHEET 4 CH 7 ARG O 37 VAL O 43 -1 O LEU O 41 N ILE O 11
SHEET 5 CH 7 ILE O 64 PHE O 67 -1 O VAL O 65 N GLY O 38
SHEET 6 CH 7 ILE O 91 VAL O 95 -1 O VAL O 95 N ILE O 64
SHEET 7 CH 7 ILE P 3 PRO P 5 -1 O ARG P 4 N ILE O 94
SHEET 1 CI 2 GLY O 46 ARG O 47 0
SHEET 2 CI 2 LYS O 55 PRO O 56 -1 O LYS O 55 N ARG O 47
SHEET 1 CJ 7 LYS P 74 ILE P 78 0
SHEET 2 CJ 7 GLU P 81 SER P 87 -1 O VAL P 83 N GLU P 76
SHEET 3 CJ 7 ARG P 9 ARG P 14 -1 N VAL P 10 O MET P 86
SHEET 4 CJ 7 ARG P 37 VAL P 43 -1 O LEU P 41 N ILE P 11
SHEET 5 CJ 7 ILE P 64 PHE P 67 -1 O VAL P 65 N GLY P 38
SHEET 6 CJ 7 ILE P 91 VAL P 95 -1 O VAL P 95 N ILE P 64
SHEET 7 CJ 7 ILE Q 3 PRO Q 5 -1 O ARG Q 4 N ILE P 94
SHEET 1 CK 2 GLY P 46 ARG P 47 0
SHEET 2 CK 2 LYS P 55 PRO P 56 -1 O LYS P 55 N ARG P 47
SHEET 1 CL 7 LYS Q 74 ILE Q 78 0
SHEET 2 CL 7 GLU Q 81 SER Q 87 -1 O VAL Q 83 N GLU Q 76
SHEET 3 CL 7 ARG Q 9 ARG Q 14 -1 N VAL Q 10 O MET Q 86
SHEET 4 CL 7 ARG Q 37 VAL Q 43 -1 O LEU Q 41 N ILE Q 11
SHEET 5 CL 7 ILE Q 64 PHE Q 67 -1 O VAL Q 65 N GLY Q 38
SHEET 6 CL 7 ILE Q 91 VAL Q 95 -1 O VAL Q 95 N ILE Q 64
SHEET 7 CL 7 ILE R 3 PRO R 5 -1 O ARG R 4 N ILE Q 94
SHEET 1 CM 2 GLY Q 46 ARG Q 47 0
SHEET 2 CM 2 LYS Q 55 PRO Q 56 -1 O LYS Q 55 N ARG Q 47
SHEET 1 CN 7 LYS R 74 ILE R 78 0
SHEET 2 CN 7 GLU R 81 SER R 87 -1 O VAL R 83 N GLU R 76
SHEET 3 CN 7 ARG R 9 ARG R 14 -1 N VAL R 10 O MET R 86
SHEET 4 CN 7 ARG R 37 VAL R 43 -1 O LEU R 41 N ILE R 11
SHEET 5 CN 7 ILE R 64 PHE R 67 -1 O VAL R 65 N GLY R 38
SHEET 6 CN 7 ILE R 91 VAL R 95 -1 O VAL R 95 N ILE R 64
SHEET 7 CN 7 ILE S 3 PRO S 5 -1 O ARG S 4 N ILE R 94
SHEET 1 CO 2 GLY R 46 ARG R 47 0
SHEET 2 CO 2 LYS R 55 PRO R 56 -1 O LYS R 55 N ARG R 47
SHEET 1 CP 7 LYS S 74 ILE S 78 0
SHEET 2 CP 7 GLU S 81 SER S 87 -1 O VAL S 83 N GLU S 76
SHEET 3 CP 7 ARG S 9 ARG S 14 -1 N VAL S 10 O MET S 86
SHEET 4 CP 7 ARG S 37 VAL S 43 -1 O LEU S 41 N ILE S 11
SHEET 5 CP 7 ILE S 64 PHE S 67 -1 O VAL S 65 N GLY S 38
SHEET 6 CP 7 ILE S 91 VAL S 95 -1 O VAL S 95 N ILE S 64
SHEET 7 CP 7 ILE T 3 PRO T 5 -1 O ARG T 4 N ILE S 94
SHEET 1 CQ 2 GLY S 46 ARG S 47 0
SHEET 2 CQ 2 LYS S 55 PRO S 56 -1 O LYS S 55 N ARG S 47
SHEET 1 CR 7 LYS T 74 ILE T 78 0
SHEET 2 CR 7 GLU T 81 SER T 87 -1 O VAL T 83 N GLU T 76
SHEET 3 CR 7 ARG T 9 ARG T 14 -1 N VAL T 10 O MET T 86
SHEET 4 CR 7 ARG T 37 VAL T 43 -1 O LEU T 41 N ILE T 11
SHEET 5 CR 7 ILE T 64 PHE T 67 -1 O VAL T 65 N GLY T 38
SHEET 6 CR 7 ILE T 91 VAL T 95 -1 O VAL T 95 N ILE T 64
SHEET 7 CR 7 ILE U 3 PRO U 5 -1 O ARG U 4 N ILE T 94
SHEET 1 CS 2 GLY T 46 ARG T 47 0
SHEET 2 CS 2 LYS T 55 PRO T 56 -1 O LYS T 55 N ARG T 47
SHEET 1 CT 2 GLY U 46 ARG U 47 0
SHEET 2 CT 2 LYS U 55 PRO U 56 -1 O LYS U 55 N ARG U 47
LINK O1B ADP A 600 MG MG A 601 1555 1555 1.56
LINK O3B ADP A 600 F2 AF3 A 602 1555 1555 2.01
LINK O2A ADP A 600 MG MG A 601 1555 1555 1.74
LINK MG MG A 601 F1 AF3 A 602 1555 1555 1.76
LINK MG MG A 601 OD1 ASP A 87 1555 1555 2.35
LINK MG MG A 601 AL AF3 A 602 1555 1555 2.95
LINK AL AF3 A 602 OD1 ASP A 87 1555 1555 3.02
LINK AL AF3 A 602 O1B ADP A 600 1555 1555 2.75
LINK AL AF3 A 602 O3B ADP A 600 1555 1555 2.13
LINK AL AF3 A 602 O2A ADP A 600 1555 1555 3.42
LINK AL AF3 A 602 O3A ADP A 600 1555 1555 3.49
LINK AL AF3 A 602 OG1 THR A 89 1555 1555 3.59
LINK K K A 603 O3A ADP A 600 1555 1555 3.30
LINK K K A 603 O THR A 30 1555 1555 3.16
LINK K K A 603 O1A ADP A 600 1555 1555 2.90
LINK K K A 603 O LYS A 51 1555 1555 2.79
LINK K K A 603 F3 AF3 A 602 1555 1555 3.61
LINK K K A 603 OG1 THR A 30 1555 1555 2.90
LINK K K A 603 OG1 THR A 90 1555 1555 2.81
LINK O1B ADP B 600 MG MG B 601 1555 1555 1.71
LINK O3B ADP B 600 AL AF3 B 602 1555 1555 2.01
LINK O2A ADP B 600 MG MG B 601 1555 1555 1.61
LINK O2A ADP B 600 F1 AF3 B 602 1555 1555 2.05
LINK MG MG B 601 OD1 ASP B 87 1555 1555 2.64
LINK MG MG B 601 F1 AF3 B 602 1555 1555 1.77
LINK AL AF3 B 602 MG MG B 601 1555 1555 3.23
LINK AL AF3 B 602 O2A ADP B 600 1555 1555 3.55
LINK AL AF3 B 602 OD1 ASP B 87 1555 1555 3.28
LINK AL AF3 B 602 OG1 THR B 89 1555 1555 3.57
LINK AL AF3 B 602 O1B ADP B 600 1555 1555 2.77
LINK AL AF3 B 602 O3A ADP B 600 1555 1555 3.40
LINK AL AF3 B 602 K K B 603 1555 1555 3.69
LINK K K B 603 O1A ADP B 600 1555 1555 2.97
LINK K K B 603 O3A ADP B 600 1555 1555 3.51
LINK K K B 603 O LYS B 51 1555 1555 2.75
LINK K K B 603 F3 AF3 B 602 1555 1555 3.19
LINK K K B 603 O THR B 30 1555 1555 3.20
LINK K K B 603 OG1 THR B 30 1555 1555 3.04
LINK K K B 603 OG1 THR B 90 1555 1555 3.00
LINK O3B ADP C 600 F2 AF3 C 602 1555 1555 1.90
LINK O1B ADP C 600 MG MG C 601 1555 1555 1.76
LINK O2A ADP C 600 MG MG C 601 1555 1555 1.81
LINK MG MG C 601 OD1 ASP C 87 1555 1555 2.27
LINK MG MG C 601 F1 AF3 C 602 1555 1555 1.63
LINK MG MG C 601 AL AF3 C 602 1555 1555 3.00
LINK AL AF3 C 602 O3B ADP C 600 1555 1555 2.18
LINK AL AF3 C 602 O3A ADP C 600 1555 1555 3.46
LINK AL AF3 C 602 O2A ADP C 600 1555 1555 3.39
LINK AL AF3 C 602 OD1 ASP C 87 1555 1555 3.22
LINK AL AF3 C 602 O1B ADP C 600 1555 1555 2.74
LINK K K C 603 O3A ADP C 600 1555 1555 3.62
LINK K K C 603 O1A ADP C 600 1555 1555 2.83
LINK K K C 603 F3 AF3 C 602 1555 1555 3.41
LINK K K C 603 OG1 THR C 90 1555 1555 3.01
LINK K K C 603 OG1 THR C 30 1555 1555 2.89
LINK K K C 603 NZ LYS C 51 1555 1555 3.68
LINK K K C 603 O LYS C 51 1555 1555 2.78
LINK K K C 603 O THR C 30 1555 1555 2.92
LINK O2A ADP D 600 MG MG D 601 1555 1555 1.54
LINK O2A ADP D 600 F1 AF3 D 602 1555 1555 1.96
LINK O1B ADP D 600 MG MG D 601 1555 1555 1.59
LINK MG MG D 601 OD1 ASP D 87 1555 1555 2.48
LINK MG MG D 601 F1 AF3 D 602 1555 1555 1.73
LINK MG MG D 601 AL AF3 D 602 1555 1555 2.93
LINK MG MG D 601 F2 AF3 D 602 1555 1555 3.10
LINK MG MG D 601 O HOH D 611 1555 1555 3.11
LINK AL AF3 D 602 O3B ADP D 600 1555 1555 2.08
LINK AL AF3 D 602 O3A ADP D 600 1555 1555 3.47
LINK AL AF3 D 602 OG1 THR D 89 1555 1555 3.63
LINK AL AF3 D 602 O2A ADP D 600 1555 1555 3.41
LINK AL AF3 D 602 O1B ADP D 600 1555 1555 2.71
LINK AL AF3 D 602 OD1 ASP D 87 1555 1555 3.19
LINK K K D 603 O3A ADP D 600 1555 1555 3.53
LINK K K D 603 OG1 THR D 90 1555 1555 2.99
LINK K K D 603 F3 AF3 D 602 1555 1555 3.63
LINK K K D 603 O1A ADP D 600 1555 1555 2.83
LINK K K D 603 O THR D 30 1555 1555 3.19
LINK K K D 603 OG1 THR D 30 1555 1555 3.12
LINK K K D 603 O LYS D 51 1555 1555 2.67
LINK O1B ADP E 600 MG MG E 601 1555 1555 1.59
LINK O2A ADP E 600 MG MG E 601 1555 1555 1.67
LINK MG MG E 601 O HOH E 608 1555 1555 2.20
LINK MG MG E 601 F1 AF3 E 602 1555 1555 1.76
LINK MG MG E 601 OD1 ASP E 87 1555 1555 2.36
LINK MG MG E 601 AL AF3 E 602 1555 1555 2.93
LINK AL AF3 E 602 OD1 ASP E 87 1555 1555 3.14
LINK AL AF3 E 602 O2A ADP E 600 1555 1555 3.50
LINK AL AF3 E 602 O1B ADP E 600 1555 1555 2.80
LINK AL AF3 E 602 O3A ADP E 600 1555 1555 3.36
LINK AL AF3 E 602 OG1 THR E 89 1555 1555 3.56
LINK AL AF3 E 602 O3B ADP E 600 1555 1555 2.07
LINK K K E 603 O1A ADP E 600 1555 1555 3.17
LINK K K E 603 O3A ADP E 600 1555 1555 3.69
LINK K K E 603 OG1 THR E 90 1555 1555 3.01
LINK K K E 603 OG1 THR E 30 1555 1555 2.76
LINK K K E 603 O THR E 30 1555 1555 3.18
LINK K K E 603 F3 AF3 E 602 1555 1555 3.32
LINK K K E 603 O LYS E 51 1555 1555 2.48
LINK O2A ADP F 600 F1 AF3 F 602 1555 1555 2.00
LINK O2A ADP F 600 MG MG F 601 1555 1555 1.58
LINK O1B ADP F 600 MG MG F 601 1555 1555 1.67
LINK MG MG F 601 F1 AF3 F 602 1555 1555 1.71
LINK MG MG F 601 OD1 ASP F 87 1555 1555 2.36
LINK MG MG F 601 AL AF3 F 602 1555 1555 2.95
LINK AL AF3 F 602 OD1 ASP F 87 1555 1555 3.03
LINK AL AF3 F 602 O1B ADP F 600 1555 1555 2.72
LINK AL AF3 F 602 O3B ADP F 600 1555 1555 2.32
LINK AL AF3 F 602 O2A ADP F 600 1555 1555 3.32
LINK AL AF3 F 602 O3A ADP F 600 1555 1555 3.56
LINK AL AF3 F 602 OG1 THR F 89 1555 1555 3.57
LINK AL AF3 F 602 K K F 603 1555 1555 3.71
LINK K K F 603 O1A ADP F 600 1555 1555 3.06
LINK K K F 603 O3A ADP F 600 1555 1555 3.58
LINK K K F 603 OG1 THR F 90 1555 1555 3.04
LINK K K F 603 OG1 THR F 30 1555 1555 3.38
LINK K K F 603 O THR F 30 1555 1555 3.29
LINK K K F 603 F3 AF3 F 602 1555 1555 3.34
LINK K K F 603 O LYS F 51 1555 1555 2.77
LINK O2A ADP G 600 F1 AF3 G 602 1555 1555 2.00
LINK O2A ADP G 600 MG MG G 601 1555 1555 1.72
LINK O1B ADP G 600 MG MG G 601 1555 1555 1.68
LINK MG MG G 601 F1 AF3 G 602 1555 1555 1.63
LINK MG MG G 601 OD1 ASP G 87 1555 1555 2.30
LINK MG MG G 601 AL AF3 G 602 1555 1555 2.93
LINK AL AF3 G 602 OG1 THR G 89 1555 1555 3.61
LINK AL AF3 G 602 O3B ADP G 600 1555 1555 2.31
LINK AL AF3 G 602 O3A ADP G 600 1555 1555 3.49
LINK AL AF3 G 602 OD1 ASP G 87 1555 1555 3.14
LINK AL AF3 G 602 O1B ADP G 600 1555 1555 2.73
LINK AL AF3 G 602 O HOH G 618 1555 1555 3.69
LINK AL AF3 G 602 O2A ADP G 600 1555 1555 3.39
LINK K K G 603 OG1 THR G 30 1555 1555 2.90
LINK K K G 603 O THR G 30 1555 1555 3.21
LINK K K G 603 O LYS G 51 1555 1555 2.69
LINK K K G 603 O1A ADP G 600 1555 1555 3.06
LINK K K G 603 F3 AF3 G 602 1555 1555 3.20
LINK K K G 603 O3A ADP G 600 1555 1555 3.52
LINK K K G 603 OG1 THR G 90 1555 1555 2.79
SITE 1 AC1 3 ASP A 87 ADP A 600 AF3 A 602
SITE 1 AC2 5 THR A 30 LYS A 51 THR A 90 ADP A 600
SITE 2 AC2 5 AF3 A 602
SITE 1 AC3 3 ASP B 87 ADP B 600 AF3 B 602
SITE 1 AC4 5 THR B 30 LYS B 51 THR B 90 ADP B 600
SITE 2 AC4 5 AF3 B 602
SITE 1 AC5 3 ASP C 87 ADP C 600 AF3 C 602
SITE 1 AC6 5 THR C 30 LYS C 51 THR C 90 ADP C 600
SITE 2 AC6 5 AF3 C 602
SITE 1 AC7 3 ASP D 87 ADP D 600 AF3 D 602
SITE 1 AC8 5 THR D 30 LYS D 51 THR D 90 ADP D 600
SITE 2 AC8 5 AF3 D 602
SITE 1 AC9 4 ASP E 87 ADP E 600 AF3 E 602 HOH E 608
SITE 1 BC1 5 THR E 30 LYS E 51 THR E 90 ADP E 600
SITE 2 BC1 5 AF3 E 602
SITE 1 BC2 3 ASP F 87 ADP F 600 AF3 F 602
SITE 1 BC3 5 THR F 30 LYS F 51 THR F 90 ADP F 600
SITE 2 BC3 5 AF3 F 602
SITE 1 BC4 3 ASP G 87 ADP G 600 AF3 G 602
SITE 1 BC5 5 THR G 30 LYS G 51 THR G 90 ADP G 600
SITE 2 BC5 5 AF3 G 602
SITE 1 BC6 23 THR A 30 LEU A 31 GLY A 32 PRO A 33
SITE 2 BC6 23 LYS A 51 ASP A 87 GLY A 88 THR A 89
SITE 3 BC6 23 THR A 90 THR A 91 ILE A 150 GLY A 414
SITE 4 BC6 23 GLY A 415 ILE A 454 TYR A 478 ASN A 479
SITE 5 BC6 23 ALA A 480 ALA A 481 ILE A 493 ASP A 495
SITE 6 BC6 23 MG A 601 AF3 A 602 K A 603
SITE 1 BC7 9 ASP A 52 GLY A 53 ASP A 87 GLY A 88
SITE 2 BC7 9 THR A 89 THR A 90 ADP A 600 MG A 601
SITE 3 BC7 9 K A 603
SITE 1 BC8 23 THR B 30 LEU B 31 GLY B 32 PRO B 33
SITE 2 BC8 23 LYS B 51 ASP B 87 GLY B 88 THR B 89
SITE 3 BC8 23 THR B 90 THR B 91 ILE B 150 GLY B 414
SITE 4 BC8 23 GLY B 415 ILE B 454 TYR B 478 ASN B 479
SITE 5 BC8 23 ALA B 480 ALA B 481 ILE B 493 ASP B 495
SITE 6 BC8 23 MG B 601 AF3 B 602 K B 603
SITE 1 BC9 8 GLY B 53 ASP B 87 GLY B 88 THR B 89
SITE 2 BC9 8 THR B 90 ADP B 600 MG B 601 K B 603
SITE 1 CC1 22 THR C 30 LEU C 31 GLY C 32 PRO C 33
SITE 2 CC1 22 LYS C 51 ASP C 87 GLY C 88 THR C 89
SITE 3 CC1 22 THR C 90 THR C 91 ILE C 150 GLY C 414
SITE 4 CC1 22 GLY C 415 ILE C 454 TYR C 478 ASN C 479
SITE 5 CC1 22 ALA C 480 ALA C 481 ASP C 495 MG C 601
SITE 6 CC1 22 AF3 C 602 K C 603
SITE 1 CC2 9 ASP C 52 GLY C 53 ASP C 87 GLY C 88
SITE 2 CC2 9 THR C 89 THR C 90 ADP C 600 MG C 601
SITE 3 CC2 9 K C 603
SITE 1 CC3 23 THR D 30 LEU D 31 GLY D 32 PRO D 33
SITE 2 CC3 23 LYS D 51 ASP D 87 GLY D 88 THR D 89
SITE 3 CC3 23 THR D 90 THR D 91 ILE D 150 GLY D 414
SITE 4 CC3 23 GLY D 415 ILE D 454 TYR D 478 ASN D 479
SITE 5 CC3 23 ALA D 480 ALA D 481 ILE D 493 ASP D 495
SITE 6 CC3 23 MG D 601 AF3 D 602 K D 603
SITE 1 CC4 9 ASP D 52 GLY D 53 ASP D 87 GLY D 88
SITE 2 CC4 9 THR D 89 THR D 90 ADP D 600 MG D 601
SITE 3 CC4 9 K D 603
SITE 1 CC5 23 THR E 30 LEU E 31 GLY E 32 PRO E 33
SITE 2 CC5 23 LYS E 51 ASP E 87 GLY E 88 THR E 89
SITE 3 CC5 23 THR E 90 THR E 91 ILE E 150 GLY E 414
SITE 4 CC5 23 GLY E 415 ILE E 454 TYR E 478 ASN E 479
SITE 5 CC5 23 ALA E 480 ALA E 481 ILE E 493 ASP E 495
SITE 6 CC5 23 MG E 601 AF3 E 602 K E 603
SITE 1 CC6 9 GLY E 53 ASP E 87 GLY E 88 THR E 89
SITE 2 CC6 9 THR E 90 ADP E 600 MG E 601 K E 603
SITE 3 CC6 9 HOH E 608
SITE 1 CC7 23 THR F 30 LEU F 31 GLY F 32 PRO F 33
SITE 2 CC7 23 LYS F 51 ASP F 87 GLY F 88 THR F 89
SITE 3 CC7 23 THR F 90 THR F 91 ILE F 150 GLY F 414
SITE 4 CC7 23 GLY F 415 ILE F 454 TYR F 478 ASN F 479
SITE 5 CC7 23 ALA F 480 ALA F 481 ILE F 493 ASP F 495
SITE 6 CC7 23 MG F 601 AF3 F 602 K F 603
SITE 1 CC8 8 GLY F 53 ASP F 87 GLY F 88 THR F 89
SITE 2 CC8 8 THR F 90 ADP F 600 MG F 601 K F 603
SITE 1 CC9 22 THR G 30 LEU G 31 GLY G 32 PRO G 33
SITE 2 CC9 22 LYS G 51 ASP G 87 GLY G 88 THR G 89
SITE 3 CC9 22 THR G 90 THR G 91 ILE G 150 GLY G 414
SITE 4 CC9 22 GLY G 415 ILE G 454 TYR G 478 ASN G 479
SITE 5 CC9 22 ALA G 480 ALA G 481 ASP G 495 MG G 601
SITE 6 CC9 22 AF3 G 602 K G 603
SITE 1 DC1 8 GLY G 53 ASP G 87 GLY G 88 THR G 89
SITE 2 DC1 8 THR G 90 ADP G 600 MG G 601 K G 603
CRYST1 255.546 266.855 187.049 90.00 90.00 90.00 P 21 21 2 56
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 0.003913 0.000000 0.000000 0.00000
SCALE2 0.000000 0.003747 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005346 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
