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HEADER TRANSFERASE 04-SEP-07 2VAT
TITLE CRYSTAL STRUCTURE OF DEACETYLCEPHALOSPORIN C
TITLE 2 ACETYLTRANSFERASE IN COMPLEX WITH COENZYME A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYL-COA--DEACETYLCEPHALOSPORIN C
COMPND 3 ACETYLTRANSFERASE;
COMPND 4 CHAIN: A, B, C, D, E, F, G, H, I, J, K, L;
COMPND 5 SYNONYM: DCPC-ATF, DAC ACETYLTRANSFERASE, DAC-AT,
COMPND 6 DEACETYLCEPHALOSPORIN C ACETYLTRANSFERASE;
COMPND 7 EC: 2.3.1.175;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ACREMONIUM CHRYSOGENUM;
SOURCE 3 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 4 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 5 EXPRESSION_SYSTEM_PLASMID: PTWIN
KEYWDS ACETYL TRANSFERASE, A/B- HYDROLASE FOLD, TRANSFERASE,
KEYWDS 2 ACYLTRANSFERASE, ACETYL COENZYME A, ANTIBIOTIC
KEYWDS 3 BIOSYNTHESIS, CEPHALOSPORIN BIOSYNTHESIS
EXPDTA X-RAY DIFFRACTION
AUTHOR S.LEJON,J.ELLIS,K.VALEGARD
REVDAT 1 23-SEP-08 2VAT 0
JRNL AUTH S.LEJON,J.ELLIS,K.VALEGARD
JRNL TITL THE LAST STEP IN CEPHALOSPORIN C FORMATION
JRNL TITL 2 REVEALED: CRYSTAL STRUCTURES OF
JRNL TITL 3 DEACETYLCEPHALOSPORIN C ACETYLTRANSFERASE FROM
JRNL TITL 4 ACREMONIUM CHRYSOGENUM IN COMPLEXES WITH REACTION
JRNL TITL 5 INTERMEDIATES.
JRNL REF J.MOL.BIOL. V. 377 935 2008
JRNL REFN ASTM JMOBAK UK ISSN 0022-2836
REMARK 2
REMARK 2 RESOLUTION. 2.2 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 122.17
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.53
REMARK 3 NUMBER OF REFLECTIONS : 253887
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.20063
REMARK 3 R VALUE (WORKING SET) : 0.20006
REMARK 3 FREE R VALUE : 0.23034
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.7
REMARK 3 FREE R VALUE TEST SET COUNT : 4405
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) : 2.200
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.257
REMARK 3 REFLECTION IN BIN (WORKING SET) : 18133
REMARK 3 BIN R VALUE (WORKING SET) : 0.243
REMARK 3 BIN FREE R VALUE SET COUNT : 321
REMARK 3 BIN FREE R VALUE : 0.308
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 32804
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 636
REMARK 3 SOLVENT ATOMS : 1573
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.458
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.86
REMARK 3 B22 (A**2) : 2.10
REMARK 3 B33 (A**2) : -1.24
REMARK 3 B12 (A**2) : 0.00
REMARK 3 B13 (A**2) : -0.09
REMARK 3 B23 (A**2) : 0.00
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.247
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.190
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.144
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.616
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.937
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.913
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED (A): 34275 ; 0.019 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED (DEGREES): 46567 ; 1.435 ; 1.960
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 4170 ; 6.223 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 1650 ;30.782 ;22.582
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 5393 ;15.607 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 342 ;18.729 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 4929 ; 0.126 ; 0.200
REMARK 3 GENERAL PLANES REFINED (A): 26450 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED (A): 15329 ; 0.207 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED (A): 23387 ; 0.310 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED (A): 1832 ; 0.173 ; 0.200
REMARK 3 SYMMETRY VDW REFINED (A): 274 ; 0.233 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED (A): 47 ; 0.281 ; 0.200
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED (A**2): 21221 ; 1.087 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED (A**2): 33347 ; 1.731 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED (A**2): 14840 ; 2.749 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED (A**2): 13186 ; 4.321 ; 4.500
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF NCS GROUPS : 10
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B C D E F G H I J K L
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 7 A 32 1
REMARK 3 1 B 7 B 32 1
REMARK 3 1 C 7 C 32 1
REMARK 3 1 D 7 D 32 1
REMARK 3 1 E 7 E 32 1
REMARK 3 1 F 7 F 32 1
REMARK 3 1 G 7 G 32 1
REMARK 3 1 H 7 H 32 1
REMARK 3 1 I 7 I 32 1
REMARK 3 1 J 7 J 32 1
REMARK 3 1 K 7 K 32 1
REMARK 3 1 L 7 L 32 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 194 ; .08 ; .05
REMARK 3 TIGHT POSITIONAL 1 B (A): 194 ; .22 ; .05
REMARK 3 TIGHT POSITIONAL 1 C (A): 194 ; .09 ; .05
REMARK 3 TIGHT POSITIONAL 1 D (A): 194 ; .18 ; .05
REMARK 3 TIGHT POSITIONAL 1 E (A): 194 ; .09 ; .05
REMARK 3 TIGHT POSITIONAL 1 F (A): 194 ; .08 ; .05
REMARK 3 TIGHT POSITIONAL 1 G (A): 194 ; .09 ; .05
REMARK 3 TIGHT POSITIONAL 1 H (A): 194 ; .10 ; .05
REMARK 3 TIGHT POSITIONAL 1 I (A): 194 ; .09 ; .05
REMARK 3 TIGHT POSITIONAL 1 J (A): 194 ; .17 ; .05
REMARK 3 TIGHT POSITIONAL 1 K (A): 194 ; .09 ; .05
REMARK 3 TIGHT POSITIONAL 1 L (A): 194 ; .08 ; .05
REMARK 3 TIGHT THERMAL 1 A (A**2): 194 ; .46 ; .50
REMARK 3 TIGHT THERMAL 1 B (A**2): 194 ; .48 ; .50
REMARK 3 TIGHT THERMAL 1 C (A**2): 194 ; .25 ; .50
REMARK 3 TIGHT THERMAL 1 D (A**2): 194 ; .26 ; .50
REMARK 3 TIGHT THERMAL 1 E (A**2): 194 ; .47 ; .50
REMARK 3 TIGHT THERMAL 1 F (A**2): 194 ; .40 ; .50
REMARK 3 TIGHT THERMAL 1 G (A**2): 194 ; .23 ; .50
REMARK 3 TIGHT THERMAL 1 H (A**2): 194 ; .24 ; .50
REMARK 3 TIGHT THERMAL 1 I (A**2): 194 ; .49 ; .50
REMARK 3 TIGHT THERMAL 1 J (A**2): 194 ; .67 ; .50
REMARK 3 TIGHT THERMAL 1 K (A**2): 194 ; .63 ; .50
REMARK 3 TIGHT THERMAL 1 L (A**2): 194 ; .40 ; .50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : A B C D E F G H I J K L
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 35 A 46 1
REMARK 3 1 B 35 B 46 1
REMARK 3 1 C 35 C 46 1
REMARK 3 1 D 35 D 46 1
REMARK 3 1 E 35 E 46 1
REMARK 3 1 F 35 F 46 1
REMARK 3 1 G 35 G 46 1
REMARK 3 1 H 35 H 46 1
REMARK 3 1 I 35 I 46 1
REMARK 3 1 J 35 J 46 1
REMARK 3 1 K 35 K 46 1
REMARK 3 1 L 35 L 46 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 2 A (A): 98 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 2 B (A): 98 ; .07 ; .05
REMARK 3 TIGHT POSITIONAL 2 C (A): 98 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 2 D (A): 98 ; .07 ; .05
REMARK 3 TIGHT POSITIONAL 2 E (A): 98 ; .07 ; .05
REMARK 3 TIGHT POSITIONAL 2 F (A): 98 ; .08 ; .05
REMARK 3 TIGHT POSITIONAL 2 G (A): 98 ; .08 ; .05
REMARK 3 TIGHT POSITIONAL 2 H (A): 98 ; .09 ; .05
REMARK 3 TIGHT POSITIONAL 2 I (A): 98 ; .07 ; .05
REMARK 3 TIGHT POSITIONAL 2 J (A): 98 ; .08 ; .05
REMARK 3 TIGHT POSITIONAL 2 K (A): 98 ; .07 ; .05
REMARK 3 TIGHT POSITIONAL 2 L (A): 98 ; .08 ; .05
REMARK 3 TIGHT THERMAL 2 A (A**2): 98 ; .34 ; .50
REMARK 3 TIGHT THERMAL 2 B (A**2): 98 ; .35 ; .50
REMARK 3 TIGHT THERMAL 2 C (A**2): 98 ; .38 ; .50
REMARK 3 TIGHT THERMAL 2 D (A**2): 98 ; .38 ; .50
REMARK 3 TIGHT THERMAL 2 E (A**2): 98 ; .31 ; .50
REMARK 3 TIGHT THERMAL 2 F (A**2): 98 ; .32 ; .50
REMARK 3 TIGHT THERMAL 2 G (A**2): 98 ; .36 ; .50
REMARK 3 TIGHT THERMAL 2 H (A**2): 98 ; .33 ; .50
REMARK 3 TIGHT THERMAL 2 I (A**2): 98 ; .37 ; .50
REMARK 3 TIGHT THERMAL 2 J (A**2): 98 ; .72 ; .50
REMARK 3 TIGHT THERMAL 2 K (A**2): 98 ; .66 ; .50
REMARK 3 TIGHT THERMAL 2 L (A**2): 98 ; .31 ; .50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 3
REMARK 3 CHAIN NAMES : A B C D E F G H I J K L
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 48 A 127 1
REMARK 3 1 B 48 B 127 1
REMARK 3 1 C 48 C 127 1
REMARK 3 1 D 48 D 127 1
REMARK 3 1 E 48 E 127 1
REMARK 3 1 F 48 F 127 1
REMARK 3 1 G 48 G 127 1
REMARK 3 1 H 48 H 127 1
REMARK 3 1 I 48 I 127 1
REMARK 3 1 J 48 J 127 1
REMARK 3 1 K 48 K 127 1
REMARK 3 1 L 48 L 127 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 3 A (A): 557 ; .07 ; .05
REMARK 3 TIGHT POSITIONAL 3 B (A): 557 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 3 C (A): 557 ; .09 ; .05
REMARK 3 TIGHT POSITIONAL 3 D (A): 557 ; .09 ; .05
REMARK 3 TIGHT POSITIONAL 3 E (A): 557 ; .07 ; .05
REMARK 3 TIGHT POSITIONAL 3 F (A): 557 ; .08 ; .05
REMARK 3 TIGHT POSITIONAL 3 G (A): 557 ; .09 ; .05
REMARK 3 TIGHT POSITIONAL 3 H (A): 557 ; .09 ; .05
REMARK 3 TIGHT POSITIONAL 3 I (A): 557 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 3 J (A): 557 ; .07 ; .05
REMARK 3 TIGHT POSITIONAL 3 K (A): 557 ; .07 ; .05
REMARK 3 TIGHT POSITIONAL 3 L (A): 557 ; .08 ; .05
REMARK 3 TIGHT THERMAL 3 A (A**2): 557 ; .34 ; .50
REMARK 3 TIGHT THERMAL 3 B (A**2): 557 ; .41 ; .50
REMARK 3 TIGHT THERMAL 3 C (A**2): 557 ; .36 ; .50
REMARK 3 TIGHT THERMAL 3 D (A**2): 557 ; .33 ; .50
REMARK 3 TIGHT THERMAL 3 E (A**2): 557 ; .35 ; .50
REMARK 3 TIGHT THERMAL 3 F (A**2): 557 ; .33 ; .50
REMARK 3 TIGHT THERMAL 3 G (A**2): 557 ; .29 ; .50
REMARK 3 TIGHT THERMAL 3 H (A**2): 557 ; .31 ; .50
REMARK 3 TIGHT THERMAL 3 I (A**2): 557 ; .40 ; .50
REMARK 3 TIGHT THERMAL 3 J (A**2): 557 ; .70 ; .50
REMARK 3 TIGHT THERMAL 3 K (A**2): 557 ; .65 ; .50
REMARK 3 TIGHT THERMAL 3 L (A**2): 557 ; .33 ; .50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 4
REMARK 3 CHAIN NAMES : A B C D E F G H I J K L
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 129 A 139 1
REMARK 3 1 B 129 B 139 1
REMARK 3 1 C 129 C 139 1
REMARK 3 1 D 129 D 139 1
REMARK 3 1 E 129 E 139 1
REMARK 3 1 F 129 F 139 1
REMARK 3 1 G 129 G 139 1
REMARK 3 1 H 129 H 139 1
REMARK 3 1 I 129 I 139 1
REMARK 3 1 J 129 J 139 1
REMARK 3 1 K 129 K 139 1
REMARK 3 1 L 129 L 139 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 4 A (A): 75 ; .07 ; .05
REMARK 3 TIGHT POSITIONAL 4 B (A): 75 ; .07 ; .05
REMARK 3 TIGHT POSITIONAL 4 C (A): 75 ; .07 ; .05
REMARK 3 TIGHT POSITIONAL 4 D (A): 75 ; .08 ; .05
REMARK 3 TIGHT POSITIONAL 4 E (A): 75 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 4 F (A): 75 ; .09 ; .05
REMARK 3 TIGHT POSITIONAL 4 G (A): 75 ; .09 ; .05
REMARK 3 TIGHT POSITIONAL 4 H (A): 75 ; .07 ; .05
REMARK 3 TIGHT POSITIONAL 4 I (A): 75 ; .07 ; .05
REMARK 3 TIGHT POSITIONAL 4 J (A): 75 ; .10 ; .05
REMARK 3 TIGHT POSITIONAL 4 K (A): 75 ; .10 ; .05
REMARK 3 TIGHT POSITIONAL 4 L (A): 75 ; .09 ; .05
REMARK 3 TIGHT THERMAL 4 A (A**2): 75 ; .38 ; .50
REMARK 3 TIGHT THERMAL 4 B (A**2): 75 ; .55 ; .50
REMARK 3 TIGHT THERMAL 4 C (A**2): 75 ; .35 ; .50
REMARK 3 TIGHT THERMAL 4 D (A**2): 75 ; .34 ; .50
REMARK 3 TIGHT THERMAL 4 E (A**2): 75 ; .36 ; .50
REMARK 3 TIGHT THERMAL 4 F (A**2): 75 ; .29 ; .50
REMARK 3 TIGHT THERMAL 4 G (A**2): 75 ; .30 ; .50
REMARK 3 TIGHT THERMAL 4 H (A**2): 75 ; .29 ; .50
REMARK 3 TIGHT THERMAL 4 I (A**2): 75 ; .51 ; .50
REMARK 3 TIGHT THERMAL 4 J (A**2): 75 ; .75 ; .50
REMARK 3 TIGHT THERMAL 4 K (A**2): 75 ; .71 ; .50
REMARK 3 TIGHT THERMAL 4 L (A**2): 75 ; .32 ; .50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 5
REMARK 3 CHAIN NAMES : A B C D E F G H I J K L
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 141 A 268 1
REMARK 3 1 B 141 B 268 1
REMARK 3 1 C 141 C 268 1
REMARK 3 1 D 141 D 268 1
REMARK 3 1 E 141 E 268 1
REMARK 3 1 F 141 F 268 1
REMARK 3 1 G 141 G 268 1
REMARK 3 1 H 141 H 268 1
REMARK 3 1 I 141 I 268 1
REMARK 3 1 J 141 J 268 1
REMARK 3 1 K 141 K 268 1
REMARK 3 1 L 141 L 268 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 5 A (A): 757 ; .12 ; .05
REMARK 3 TIGHT POSITIONAL 5 B (A): 757 ; .18 ; .05
REMARK 3 TIGHT POSITIONAL 5 C (A): 757 ; .17 ; .05
REMARK 3 TIGHT POSITIONAL 5 D (A): 757 ; .11 ; .05
REMARK 3 TIGHT POSITIONAL 5 E (A): 757 ; .10 ; .05
REMARK 3 TIGHT POSITIONAL 5 F (A): 757 ; .16 ; .05
REMARK 3 TIGHT POSITIONAL 5 G (A): 757 ; .11 ; .05
REMARK 3 TIGHT POSITIONAL 5 H (A): 757 ; .11 ; .05
REMARK 3 TIGHT POSITIONAL 5 I (A): 757 ; .10 ; .05
REMARK 3 TIGHT POSITIONAL 5 J (A): 757 ; .11 ; .05
REMARK 3 TIGHT POSITIONAL 5 K (A): 757 ; .10 ; .05
REMARK 3 TIGHT POSITIONAL 5 L (A): 757 ; .09 ; .05
REMARK 3 TIGHT THERMAL 5 A (A**2): 757 ; .37 ; .50
REMARK 3 TIGHT THERMAL 5 B (A**2): 757 ; .36 ; .50
REMARK 3 TIGHT THERMAL 5 C (A**2): 757 ; .28 ; .50
REMARK 3 TIGHT THERMAL 5 D (A**2): 757 ; .28 ; .50
REMARK 3 TIGHT THERMAL 5 E (A**2): 757 ; .35 ; .50
REMARK 3 TIGHT THERMAL 5 F (A**2): 757 ; .28 ; .50
REMARK 3 TIGHT THERMAL 5 G (A**2): 757 ; .27 ; .50
REMARK 3 TIGHT THERMAL 5 H (A**2): 757 ; .27 ; .50
REMARK 3 TIGHT THERMAL 5 I (A**2): 757 ; .37 ; .50
REMARK 3 TIGHT THERMAL 5 J (A**2): 757 ; .49 ; .50
REMARK 3 TIGHT THERMAL 5 K (A**2): 757 ; .47 ; .50
REMARK 3 TIGHT THERMAL 5 L (A**2): 757 ; .29 ; .50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 6
REMARK 3 CHAIN NAMES : A B C D E F G H I J K L
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 272 A 309 1
REMARK 3 1 B 272 B 309 1
REMARK 3 1 C 272 C 309 1
REMARK 3 1 D 272 D 309 1
REMARK 3 1 E 272 E 309 1
REMARK 3 1 F 272 F 309 1
REMARK 3 1 G 272 G 309 1
REMARK 3 1 H 272 H 309 1
REMARK 3 1 I 272 I 309 1
REMARK 3 1 J 272 J 309 1
REMARK 3 1 K 272 K 309 1
REMARK 3 1 L 272 L 309 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 6 A (A): 295 ; .09 ; .05
REMARK 3 TIGHT POSITIONAL 6 B (A): 295 ; .09 ; .05
REMARK 3 TIGHT POSITIONAL 6 C (A): 295 ; .10 ; .05
REMARK 3 TIGHT POSITIONAL 6 D (A): 295 ; .10 ; .05
REMARK 3 TIGHT POSITIONAL 6 E (A): 295 ; .09 ; .05
REMARK 3 TIGHT POSITIONAL 6 F (A): 295 ; .09 ; .05
REMARK 3 TIGHT POSITIONAL 6 G (A): 295 ; .15 ; .05
REMARK 3 TIGHT POSITIONAL 6 H (A): 295 ; .14 ; .05
REMARK 3 TIGHT POSITIONAL 6 I (A): 295 ; .08 ; .05
REMARK 3 TIGHT POSITIONAL 6 J (A): 295 ; .08 ; .05
REMARK 3 TIGHT POSITIONAL 6 K (A): 295 ; .08 ; .05
REMARK 3 TIGHT POSITIONAL 6 L (A): 295 ; .09 ; .05
REMARK 3 TIGHT THERMAL 6 A (A**2): 295 ; .39 ; .50
REMARK 3 TIGHT THERMAL 6 B (A**2): 295 ; .38 ; .50
REMARK 3 TIGHT THERMAL 6 C (A**2): 295 ; .30 ; .50
REMARK 3 TIGHT THERMAL 6 D (A**2): 295 ; .30 ; .50
REMARK 3 TIGHT THERMAL 6 E (A**2): 295 ; .39 ; .50
REMARK 3 TIGHT THERMAL 6 F (A**2): 295 ; .32 ; .50
REMARK 3 TIGHT THERMAL 6 G (A**2): 295 ; .26 ; .50
REMARK 3 TIGHT THERMAL 6 H (A**2): 295 ; .27 ; .50
REMARK 3 TIGHT THERMAL 6 I (A**2): 295 ; .43 ; .50
REMARK 3 TIGHT THERMAL 6 J (A**2): 295 ; .51 ; .50
REMARK 3 TIGHT THERMAL 6 K (A**2): 295 ; .51 ; .50
REMARK 3 TIGHT THERMAL 6 L (A**2): 295 ; .36 ; .50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 7
REMARK 3 CHAIN NAMES : A B C D E F G H I J K L
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 311 A 330 1
REMARK 3 1 B 311 B 330 1
REMARK 3 1 C 311 C 330 1
REMARK 3 1 D 311 D 330 1
REMARK 3 1 E 311 E 330 1
REMARK 3 1 F 311 F 330 1
REMARK 3 1 G 311 G 330 1
REMARK 3 1 H 311 H 330 1
REMARK 3 1 I 311 I 330 1
REMARK 3 1 J 311 J 330 1
REMARK 3 1 K 311 K 330 1
REMARK 3 1 L 311 L 330 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 7 A (A): 136 ; .23 ; .05
REMARK 3 TIGHT POSITIONAL 7 B (A): 136 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 7 C (A): 136 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 7 D (A): 136 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 7 E (A): 136 ; .07 ; .05
REMARK 3 TIGHT POSITIONAL 7 F (A): 136 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 7 G (A): 136 ; .08 ; .05
REMARK 3 TIGHT POSITIONAL 7 H (A): 136 ; .09 ; .05
REMARK 3 TIGHT POSITIONAL 7 I (A): 136 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 7 J (A): 136 ; .07 ; .05
REMARK 3 TIGHT POSITIONAL 7 K (A): 136 ; .07 ; .05
REMARK 3 TIGHT POSITIONAL 7 L (A): 136 ; .06 ; .05
REMARK 3 TIGHT THERMAL 7 A (A**2): 136 ; .26 ; .50
REMARK 3 TIGHT THERMAL 7 B (A**2): 136 ; .31 ; .50
REMARK 3 TIGHT THERMAL 7 C (A**2): 136 ; .26 ; .50
REMARK 3 TIGHT THERMAL 7 D (A**2): 136 ; .21 ; .50
REMARK 3 TIGHT THERMAL 7 E (A**2): 136 ; .27 ; .50
REMARK 3 TIGHT THERMAL 7 F (A**2): 136 ; .20 ; .50
REMARK 3 TIGHT THERMAL 7 G (A**2): 136 ; .22 ; .50
REMARK 3 TIGHT THERMAL 7 H (A**2): 136 ; .26 ; .50
REMARK 3 TIGHT THERMAL 7 I (A**2): 136 ; .31 ; .50
REMARK 3 TIGHT THERMAL 7 J (A**2): 136 ; .44 ; .50
REMARK 3 TIGHT THERMAL 7 K (A**2): 136 ; .42 ; .50
REMARK 3 TIGHT THERMAL 7 L (A**2): 136 ; .24 ; .50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 8
REMARK 3 CHAIN NAMES : A B C D E F G H I J K L
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 332 A 345 1
REMARK 3 1 B 332 B 345 1
REMARK 3 1 C 332 C 345 1
REMARK 3 1 D 332 D 345 1
REMARK 3 1 E 332 E 345 1
REMARK 3 1 F 332 F 345 1
REMARK 3 1 G 332 G 345 1
REMARK 3 1 H 332 H 345 1
REMARK 3 1 I 332 I 345 1
REMARK 3 1 J 332 J 345 1
REMARK 3 1 K 332 K 345 1
REMARK 3 1 L 332 L 345 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 8 A (A): 110 ; .07 ; .05
REMARK 3 TIGHT POSITIONAL 8 B (A): 110 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 8 C (A): 110 ; .07 ; .05
REMARK 3 TIGHT POSITIONAL 8 D (A): 110 ; .26 ; .05
REMARK 3 TIGHT POSITIONAL 8 E (A): 110 ; .08 ; .05
REMARK 3 TIGHT POSITIONAL 8 F (A): 110 ; .08 ; .05
REMARK 3 TIGHT POSITIONAL 8 G (A): 110 ; .07 ; .05
REMARK 3 TIGHT POSITIONAL 8 H (A): 110 ; .07 ; .05
REMARK 3 TIGHT POSITIONAL 8 I (A): 110 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 8 J (A): 110 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 8 K (A): 110 ; .07 ; .05
REMARK 3 TIGHT POSITIONAL 8 L (A): 110 ; .07 ; .05
REMARK 3 TIGHT THERMAL 8 A (A**2): 110 ; .29 ; .50
REMARK 3 TIGHT THERMAL 8 B (A**2): 110 ; .27 ; .50
REMARK 3 TIGHT THERMAL 8 C (A**2): 110 ; .27 ; .50
REMARK 3 TIGHT THERMAL 8 D (A**2): 110 ; .27 ; .50
REMARK 3 TIGHT THERMAL 8 E (A**2): 110 ; .33 ; .50
REMARK 3 TIGHT THERMAL 8 F (A**2): 110 ; .25 ; .50
REMARK 3 TIGHT THERMAL 8 G (A**2): 110 ; .26 ; .50
REMARK 3 TIGHT THERMAL 8 H (A**2): 110 ; .26 ; .50
REMARK 3 TIGHT THERMAL 8 I (A**2): 110 ; .29 ; .50
REMARK 3 TIGHT THERMAL 8 J (A**2): 110 ; .41 ; .50
REMARK 3 TIGHT THERMAL 8 K (A**2): 110 ; .40 ; .50
REMARK 3 TIGHT THERMAL 8 L (A**2): 110 ; .26 ; .50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 9
REMARK 3 CHAIN NAMES : A B C D E F G H I J K L
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 347 A 359 1
REMARK 3 1 B 347 B 359 1
REMARK 3 1 C 347 C 359 1
REMARK 3 1 D 347 D 359 1
REMARK 3 1 E 347 E 359 1
REMARK 3 1 F 347 F 359 1
REMARK 3 1 G 347 G 359 1
REMARK 3 1 H 347 H 359 1
REMARK 3 1 I 347 I 359 1
REMARK 3 1 J 347 J 359 1
REMARK 3 1 K 347 K 359 1
REMARK 3 1 L 347 L 359 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 9 A (A): 97 ; .09 ; .05
REMARK 3 TIGHT POSITIONAL 9 B (A): 97 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 9 C (A): 97 ; .08 ; .05
REMARK 3 TIGHT POSITIONAL 9 D (A): 97 ; .07 ; .05
REMARK 3 TIGHT POSITIONAL 9 E (A): 97 ; .09 ; .05
REMARK 3 TIGHT POSITIONAL 9 F (A): 97 ; .08 ; .05
REMARK 3 TIGHT POSITIONAL 9 G (A): 97 ; .08 ; .05
REMARK 3 TIGHT POSITIONAL 9 H (A): 97 ; .07 ; .05
REMARK 3 TIGHT POSITIONAL 9 I (A): 97 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 9 J (A): 97 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 9 K (A): 97 ; .07 ; .05
REMARK 3 TIGHT POSITIONAL 9 L (A): 97 ; .08 ; .05
REMARK 3 TIGHT THERMAL 9 A (A**2): 97 ; .25 ; .50
REMARK 3 TIGHT THERMAL 9 B (A**2): 97 ; .29 ; .50
REMARK 3 TIGHT THERMAL 9 C (A**2): 97 ; .25 ; .50
REMARK 3 TIGHT THERMAL 9 D (A**2): 97 ; .23 ; .50
REMARK 3 TIGHT THERMAL 9 E (A**2): 97 ; .26 ; .50
REMARK 3 TIGHT THERMAL 9 F (A**2): 97 ; .20 ; .50
REMARK 3 TIGHT THERMAL 9 G (A**2): 97 ; .21 ; .50
REMARK 3 TIGHT THERMAL 9 H (A**2): 97 ; .22 ; .50
REMARK 3 TIGHT THERMAL 9 I (A**2): 97 ; .24 ; .50
REMARK 3 TIGHT THERMAL 9 J (A**2): 97 ; .33 ; .50
REMARK 3 TIGHT THERMAL 9 K (A**2): 97 ; .34 ; .50
REMARK 3 TIGHT THERMAL 9 L (A**2): 97 ; .22 ; .50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 10
REMARK 3 CHAIN NAMES : A B C D E F G H I J K L
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 361 A 382 1
REMARK 3 1 B 361 B 382 1
REMARK 3 1 C 361 C 382 1
REMARK 3 1 D 361 D 382 1
REMARK 3 1 E 361 E 382 1
REMARK 3 1 F 361 F 382 1
REMARK 3 1 G 361 G 382 1
REMARK 3 1 H 361 H 382 1
REMARK 3 1 I 361 I 382 1
REMARK 3 1 J 361 J 382 1
REMARK 3 1 K 361 K 382 1
REMARK 3 1 L 361 L 382 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 10 A (A): 163 ; .07 ; .05
REMARK 3 TIGHT POSITIONAL 10 B (A): 163 ; .23 ; .05
REMARK 3 TIGHT POSITIONAL 10 C (A): 163 ; .21 ; .05
REMARK 3 TIGHT POSITIONAL 10 D (A): 163 ; .07 ; .05
REMARK 3 TIGHT POSITIONAL 10 E (A): 163 ; .07 ; .05
REMARK 3 TIGHT POSITIONAL 10 F (A): 163 ; .07 ; .05
REMARK 3 TIGHT POSITIONAL 10 G (A): 163 ; .07 ; .05
REMARK 3 TIGHT POSITIONAL 10 H (A): 163 ; .07 ; .05
REMARK 3 TIGHT POSITIONAL 10 I (A): 163 ; .08 ; .05
REMARK 3 TIGHT POSITIONAL 10 J (A): 163 ; .08 ; .05
REMARK 3 TIGHT POSITIONAL 10 K (A): 163 ; .09 ; .05
REMARK 3 TIGHT POSITIONAL 10 L (A): 163 ; .07 ; .05
REMARK 3 TIGHT THERMAL 10 A (A**2): 163 ; .22 ; .50
REMARK 3 TIGHT THERMAL 10 B (A**2): 163 ; .37 ; .50
REMARK 3 TIGHT THERMAL 10 C (A**2): 163 ; .27 ; .50
REMARK 3 TIGHT THERMAL 10 D (A**2): 163 ; .24 ; .50
REMARK 3 TIGHT THERMAL 10 E (A**2): 163 ; .22 ; .50
REMARK 3 TIGHT THERMAL 10 F (A**2): 163 ; .24 ; .50
REMARK 3 TIGHT THERMAL 10 G (A**2): 163 ; .23 ; .50
REMARK 3 TIGHT THERMAL 10 H (A**2): 163 ; .24 ; .50
REMARK 3 TIGHT THERMAL 10 I (A**2): 163 ; .35 ; .50
REMARK 3 TIGHT THERMAL 10 J (A**2): 163 ; .45 ; .50
REMARK 3 TIGHT THERMAL 10 K (A**2): 163 ; .49 ; .50
REMARK 3 TIGHT THERMAL 10 L (A**2): 163 ; .21 ; .50
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS. RESIDUES 242-267 ARE DISORDERED.
REMARK 3 ACETYL MOIETY WAS LEFT UNMODELLED.
REMARK 3 RESIDUAL DENSITY NEAR SER149, POSSIBLY INDICATING MULTIPLE
REMARK 3 REACTION STATES WITH PARTIAL OCCUPANCIES, WAS LEFT
REMARK 3 UNMODELLED.
REMARK 4
REMARK 4 2VAT COMPLIES WITH FORMAT V. 3.1, 01-AUG-2007
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY EBI ON 4-SEP-2007.
REMARK 100 THE EBI ID CODE IS EBI-33680.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-APR-2004
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y ; Y
REMARK 200 RADIATION SOURCE : ESRF ; MAX II
REMARK 200 BEAMLINE : ID14-1 ; I911-3
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M ; M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.934 ; 0.978
REMARK 200 MONOCHROMATOR : DIAMOND (111), GE(220)
REMARK 200 OPTICS : TOROIDAL MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 258318
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.20
REMARK 200 RESOLUTION RANGE LOW (A) : 60.97
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 6.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 200 DATA REDUNDANCY : 3.1
REMARK 200 R MERGE (I) : 0.09
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 10.60
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.32
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.8
REMARK 200 DATA REDUNDANCY IN SHELL : 2.9
REMARK 200 R MERGE FOR SHELL (I) : 0.25
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.70
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHELX, AUTOSHARP
REMARK 200 STARTING MODEL: NONE
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.56
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 18-19% PEG 4000, 0.1M IMIDAZOLE,
REMARK 280 0.5M NACL, 0.2M SODIUM ACETATE
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 54.63900
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 295
REMARK 295 NON-CRYSTALLOGRAPHIC SYMMETRY
REMARK 295 THE TRANSFORMATIONS PRESENTED ON THE MTRIX RECORDS BELOW
REMARK 295 DESCRIBE NON-CRYSTALLOGRAPHIC RELATIONSHIPS AMONG ATOMS
REMARK 295 IN THIS ENTRY. APPLYING THE APPROPRIATE MTRIX
REMARK 295 TRANSFORMATION TO THE RESIDUES LISTED FIRST WILL YIELD
REMARK 295 APPROXIMATE COORDINATES FOR THE RESIDUES LISTED SECOND.
REMARK 295 CHAIN IDENTIFIERS GIVEN AS "?" REFER TO CHAINS FOR WHICH
REMARK 295 ATOMS ARE NOT FOUND IN THIS ENTRY.
REMARK 295
REMARK 295 APPLIED TO TRANSFORMED TO
REMARK 295 TRANSFORM CHAIN RESIDUES CHAIN RESIDUES RMSD
REMARK 295 M 1 B 7 .. 382 A 7 .. 382 0.362
REMARK 295 M 2 C 7 .. 382 A 7 .. 382 0.517
REMARK 295 M 3 D 7 .. 382 A 7 .. 382 0.520
REMARK 295 M 4 E 7 .. 382 A 7 .. 382 0.195
REMARK 295 M 5 F 7 .. 382 A 7 .. 382 0.515
REMARK 295 M 6 G 7 .. 382 A 7 .. 382 0.584
REMARK 295 M 7 H 7 .. 382 A 7 .. 382 0.520
REMARK 295 M 8 I 7 .. 382 A 7 .. 382 0.351
REMARK 295 M 9 J 7 .. 382 A 7 .. 382 0.408
REMARK 295 M 10 K 7 .. 382 A 7 .. 382 0.392
REMARK 295 M 11 L 7 .. 382 A 7 .. 382 0.500
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6
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 GENERATING THE BIOMOLECULE
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4900 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 31460 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -38.9 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, I
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4950 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 31280 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -30.1 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, E
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4260 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 31170 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.4 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, K
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3460 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 30580 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -30.2 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F, H
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMOLECULE: 5
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4300 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 30380 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, L
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMOLECULE: 6
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4220 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 31320 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.5 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, J
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A -58
REMARK 465 LEU A -57
REMARK 465 PRO A -56
REMARK 465 SER A -55
REMARK 465 ALA A -54
REMARK 465 GLN A -53
REMARK 465 VAL A -52
REMARK 465 ALA A -51
REMARK 465 ARG A -50
REMARK 465 LEU A -49
REMARK 465 LYS A -48
REMARK 465 PRO A -47
REMARK 465 ASP A -46
REMARK 465 PRO A -45
REMARK 465 PHE A -44
REMARK 465 PRO A -43
REMARK 465 PRO A -42
REMARK 465 SER A -41
REMARK 465 LEU A -40
REMARK 465 SER A -39
REMARK 465 PRO A -38
REMARK 465 ILE A -37
REMARK 465 PRO A -36
REMARK 465 HIS A -35
REMARK 465 GLY A -34
REMARK 465 ALA A -33
REMARK 465 VAL A -32
REMARK 465 THR A -31
REMARK 465 PHE A -30
REMARK 465 ALA A -29
REMARK 465 ALA A -28
REMARK 465 LEU A -27
REMARK 465 ALA A -26
REMARK 465 PRO A -25
REMARK 465 CYS A -24
REMARK 465 HIS A -23
REMARK 465 ASN A -22
REMARK 465 LEU A -21
REMARK 465 PRO A -20
REMARK 465 ILE A -19
REMARK 465 PHE A -18
REMARK 465 SER A -17
REMARK 465 SER A -16
REMARK 465 ARG A -15
REMARK 465 GLN A -14
REMARK 465 MET A -13
REMARK 465 LEU A -12
REMARK 465 ARG A -11
REMARK 465 ASP A -10
REMARK 465 SER A -9
REMARK 465 LEU A -8
REMARK 465 THR A -7
REMARK 465 TYR A -6
REMARK 465 SER A -5
REMARK 465 HIS A -4
REMARK 465 THR A -3
REMARK 465 SER A -2
REMARK 465 PRO A -1
REMARK 465 THR A 0
REMARK 465 MET A 1
REMARK 465 SER A 2
REMARK 465 PRO A 3
REMARK 465 GLN A 4
REMARK 465 ILE A 5
REMARK 465 ALA A 6
REMARK 465 GLY A 110
REMARK 465 GLN A 111
REMARK 465 GLN A 242
REMARK 465 ALA A 243
REMARK 465 GLY A 244
REMARK 465 ARG A 245
REMARK 465 ASN A 246
REMARK 465 ILE A 247
REMARK 465 SER A 248
REMARK 465 SER A 249
REMARK 465 GLN A 250
REMARK 465 ASP A 251
REMARK 465 ALA A 252
REMARK 465 LYS A 253
REMARK 465 LYS A 254
REMARK 465 GLU A 255
REMARK 465 ILE A 256
REMARK 465 ASN A 257
REMARK 465 GLY A 258
REMARK 465 THR A 259
REMARK 465 ASP A 260
REMARK 465 SER A 261
REMARK 465 GLY A 262
REMARK 465 ASN A 263
REMARK 465 SER A 264
REMARK 465 HIS A 265
REMARK 465 ARG A 266
REMARK 465 ALA A 267
REMARK 465 GLY A 268
REMARK 465 SER A 383
REMARK 465 LEU A 384
REMARK 465 MET A 385
REMARK 465 MET B -58
REMARK 465 LEU B -57
REMARK 465 PRO B -56
REMARK 465 SER B -55
REMARK 465 ALA B -54
REMARK 465 GLN B -53
REMARK 465 VAL B -52
REMARK 465 ALA B -51
REMARK 465 ARG B -50
REMARK 465 LEU B -49
REMARK 465 LYS B -48
REMARK 465 PRO B -47
REMARK 465 ASP B -46
REMARK 465 PRO B -45
REMARK 465 PHE B -44
REMARK 465 PRO B -43
REMARK 465 PRO B -42
REMARK 465 SER B -41
REMARK 465 LEU B -40
REMARK 465 SER B -39
REMARK 465 PRO B -38
REMARK 465 ILE B -37
REMARK 465 PRO B -36
REMARK 465 HIS B -35
REMARK 465 GLY B -34
REMARK 465 ALA B -33
REMARK 465 VAL B -32
REMARK 465 THR B -31
REMARK 465 PHE B -30
REMARK 465 ALA B -29
REMARK 465 ALA B -28
REMARK 465 LEU B -27
REMARK 465 ALA B -26
REMARK 465 PRO B -25
REMARK 465 CYS B -24
REMARK 465 HIS B -23
REMARK 465 ASN B -22
REMARK 465 LEU B -21
REMARK 465 PRO B -20
REMARK 465 ILE B -19
REMARK 465 PHE B -18
REMARK 465 SER B -17
REMARK 465 SER B -16
REMARK 465 ARG B -15
REMARK 465 GLN B -14
REMARK 465 MET B -13
REMARK 465 LEU B -12
REMARK 465 ARG B -11
REMARK 465 ASP B -10
REMARK 465 SER B -9
REMARK 465 LEU B -8
REMARK 465 THR B -7
REMARK 465 TYR B -6
REMARK 465 SER B -5
REMARK 465 HIS B -4
REMARK 465 THR B -3
REMARK 465 SER B -2
REMARK 465 PRO B -1
REMARK 465 THR B 0
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 PRO B 3
REMARK 465 GLN B 4
REMARK 465 ILE B 5
REMARK 465 ALA B 6
REMARK 465 GLU B 109
REMARK 465 GLY B 110
REMARK 465 GLN B 111
REMARK 465 GLN B 242
REMARK 465 ALA B 243
REMARK 465 GLY B 244
REMARK 465 ARG B 245
REMARK 465 ASN B 246
REMARK 465 ILE B 247
REMARK 465 SER B 248
REMARK 465 SER B 249
REMARK 465 GLN B 250
REMARK 465 ASP B 251
REMARK 465 ALA B 252
REMARK 465 LYS B 253
REMARK 465 LYS B 254
REMARK 465 GLU B 255
REMARK 465 ILE B 256
REMARK 465 ASN B 257
REMARK 465 GLY B 258
REMARK 465 THR B 259
REMARK 465 ASP B 260
REMARK 465 SER B 261
REMARK 465 GLY B 262
REMARK 465 ASN B 263
REMARK 465 SER B 264
REMARK 465 HIS B 265
REMARK 465 ARG B 266
REMARK 465 ALA B 267
REMARK 465 SER B 383
REMARK 465 LEU B 384
REMARK 465 MET B 385
REMARK 465 MET C -58
REMARK 465 LEU C -57
REMARK 465 PRO C -56
REMARK 465 SER C -55
REMARK 465 ALA C -54
REMARK 465 GLN C -53
REMARK 465 VAL C -52
REMARK 465 ALA C -51
REMARK 465 ARG C -50
REMARK 465 LEU C -49
REMARK 465 LYS C -48
REMARK 465 PRO C -47
REMARK 465 ASP C -46
REMARK 465 PRO C -45
REMARK 465 PHE C -44
REMARK 465 PRO C -43
REMARK 465 PRO C -42
REMARK 465 SER C -41
REMARK 465 LEU C -40
REMARK 465 SER C -39
REMARK 465 PRO C -38
REMARK 465 ILE C -37
REMARK 465 PRO C -36
REMARK 465 HIS C -35
REMARK 465 GLY C -34
REMARK 465 ALA C -33
REMARK 465 VAL C -32
REMARK 465 THR C -31
REMARK 465 PHE C -30
REMARK 465 ALA C -29
REMARK 465 ALA C -28
REMARK 465 LEU C -27
REMARK 465 ALA C -26
REMARK 465 PRO C -25
REMARK 465 CYS C -24
REMARK 465 HIS C -23
REMARK 465 ASN C -22
REMARK 465 LEU C -21
REMARK 465 PRO C -20
REMARK 465 ILE C -19
REMARK 465 PHE C -18
REMARK 465 SER C -17
REMARK 465 SER C -16
REMARK 465 ARG C -15
REMARK 465 GLN C -14
REMARK 465 MET C -13
REMARK 465 LEU C -12
REMARK 465 ARG C -11
REMARK 465 ASP C -10
REMARK 465 SER C -9
REMARK 465 LEU C -8
REMARK 465 THR C -7
REMARK 465 TYR C -6
REMARK 465 SER C -5
REMARK 465 HIS C -4
REMARK 465 THR C -3
REMARK 465 SER C -2
REMARK 465 PRO C -1
REMARK 465 THR C 0
REMARK 465 MET C 1
REMARK 465 SER C 2
REMARK 465 PRO C 3
REMARK 465 GLN C 4
REMARK 465 ILE C 5
REMARK 465 ALA C 6
REMARK 465 ALA C 238
REMARK 465 PRO C 239
REMARK 465 GLY C 240
REMARK 465 VAL C 241
REMARK 465 GLN C 242
REMARK 465 ALA C 243
REMARK 465 GLY C 244
REMARK 465 ARG C 245
REMARK 465 ASN C 246
REMARK 465 ILE C 247
REMARK 465 SER C 248
REMARK 465 SER C 249
REMARK 465 GLN C 250
REMARK 465 ASP C 251
REMARK 465 ALA C 252
REMARK 465 LYS C 253
REMARK 465 LYS C 254
REMARK 465 GLU C 255
REMARK 465 ILE C 256
REMARK 465 ASN C 257
REMARK 465 GLY C 258
REMARK 465 THR C 259
REMARK 465 ASP C 260
REMARK 465 SER C 261
REMARK 465 GLY C 262
REMARK 465 ASN C 263
REMARK 465 SER C 264
REMARK 465 HIS C 265
REMARK 465 ARG C 266
REMARK 465 ALA C 267
REMARK 465 GLY C 268
REMARK 465 SER C 383
REMARK 465 LEU C 384
REMARK 465 MET C 385
REMARK 465 MET D -58
REMARK 465 LEU D -57
REMARK 465 PRO D -56
REMARK 465 SER D -55
REMARK 465 ALA D -54
REMARK 465 GLN D -53
REMARK 465 VAL D -52
REMARK 465 ALA D -51
REMARK 465 ARG D -50
REMARK 465 LEU D -49
REMARK 465 LYS D -48
REMARK 465 PRO D -47
REMARK 465 ASP D -46
REMARK 465 PRO D -45
REMARK 465 PHE D -44
REMARK 465 PRO D -43
REMARK 465 PRO D -42
REMARK 465 SER D -41
REMARK 465 LEU D -40
REMARK 465 SER D -39
REMARK 465 PRO D -38
REMARK 465 ILE D -37
REMARK 465 PRO D -36
REMARK 465 HIS D -35
REMARK 465 GLY D -34
REMARK 465 ALA D -33
REMARK 465 VAL D -32
REMARK 465 THR D -31
REMARK 465 PHE D -30
REMARK 465 ALA D -29
REMARK 465 ALA D -28
REMARK 465 LEU D -27
REMARK 465 ALA D -26
REMARK 465 PRO D -25
REMARK 465 CYS D -24
REMARK 465 HIS D -23
REMARK 465 ASN D -22
REMARK 465 LEU D -21
REMARK 465 PRO D -20
REMARK 465 ILE D -19
REMARK 465 PHE D -18
REMARK 465 SER D -17
REMARK 465 SER D -16
REMARK 465 ARG D -15
REMARK 465 GLN D -14
REMARK 465 MET D -13
REMARK 465 LEU D -12
REMARK 465 ARG D -11
REMARK 465 ASP D -10
REMARK 465 SER D -9
REMARK 465 LEU D -8
REMARK 465 THR D -7
REMARK 465 TYR D -6
REMARK 465 SER D -5
REMARK 465 HIS D -4
REMARK 465 THR D -3
REMARK 465 SER D -2
REMARK 465 PRO D -1
REMARK 465 THR D 0
REMARK 465 MET D 1
REMARK 465 SER D 2
REMARK 465 PRO D 3
REMARK 465 GLN D 4
REMARK 465 ILE D 5
REMARK 465 ALA D 6
REMARK 465 ALA D 238
REMARK 465 PRO D 239
REMARK 465 GLY D 240
REMARK 465 VAL D 241
REMARK 465 GLN D 242
REMARK 465 ALA D 243
REMARK 465 GLY D 244
REMARK 465 ARG D 245
REMARK 465 ASN D 246
REMARK 465 ILE D 247
REMARK 465 SER D 248
REMARK 465 SER D 249
REMARK 465 GLN D 250
REMARK 465 ASP D 251
REMARK 465 ALA D 252
REMARK 465 LYS D 253
REMARK 465 LYS D 254
REMARK 465 GLU D 255
REMARK 465 ILE D 256
REMARK 465 ASN D 257
REMARK 465 GLY D 258
REMARK 465 THR D 259
REMARK 465 ASP D 260
REMARK 465 SER D 261
REMARK 465 GLY D 262
REMARK 465 ASN D 263
REMARK 465 SER D 264
REMARK 465 HIS D 265
REMARK 465 ARG D 266
REMARK 465 ALA D 267
REMARK 465 GLY D 268
REMARK 465 SER D 383
REMARK 465 LEU D 384
REMARK 465 MET D 385
REMARK 465 MET E -58
REMARK 465 LEU E -57
REMARK 465 PRO E -56
REMARK 465 SER E -55
REMARK 465 ALA E -54
REMARK 465 GLN E -53
REMARK 465 VAL E -52
REMARK 465 ALA E -51
REMARK 465 ARG E -50
REMARK 465 LEU E -49
REMARK 465 LYS E -48
REMARK 465 PRO E -47
REMARK 465 ASP E -46
REMARK 465 PRO E -45
REMARK 465 PHE E -44
REMARK 465 PRO E -43
REMARK 465 PRO E -42
REMARK 465 SER E -41
REMARK 465 LEU E -40
REMARK 465 SER E -39
REMARK 465 PRO E -38
REMARK 465 ILE E -37
REMARK 465 PRO E -36
REMARK 465 HIS E -35
REMARK 465 GLY E -34
REMARK 465 ALA E -33
REMARK 465 VAL E -32
REMARK 465 THR E -31
REMARK 465 PHE E -30
REMARK 465 ALA E -29
REMARK 465 ALA E -28
REMARK 465 LEU E -27
REMARK 465 ALA E -26
REMARK 465 PRO E -25
REMARK 465 CYS E -24
REMARK 465 HIS E -23
REMARK 465 ASN E -22
REMARK 465 LEU E -21
REMARK 465 PRO E -20
REMARK 465 ILE E -19
REMARK 465 PHE E -18
REMARK 465 SER E -17
REMARK 465 SER E -16
REMARK 465 ARG E -15
REMARK 465 GLN E -14
REMARK 465 MET E -13
REMARK 465 LEU E -12
REMARK 465 ARG E -11
REMARK 465 ASP E -10
REMARK 465 SER E -9
REMARK 465 LEU E -8
REMARK 465 THR E -7
REMARK 465 TYR E -6
REMARK 465 SER E -5
REMARK 465 HIS E -4
REMARK 465 THR E -3
REMARK 465 SER E -2
REMARK 465 PRO E -1
REMARK 465 THR E 0
REMARK 465 MET E 1
REMARK 465 SER E 2
REMARK 465 PRO E 3
REMARK 465 GLN E 4
REMARK 465 ILE E 5
REMARK 465 ALA E 6
REMARK 465 GLU E 109
REMARK 465 GLY E 110
REMARK 465 GLN E 111
REMARK 465 ARG E 112
REMARK 465 GLN E 242
REMARK 465 ALA E 243
REMARK 465 GLY E 244
REMARK 465 ARG E 245
REMARK 465 ASN E 246
REMARK 465 ILE E 247
REMARK 465 SER E 248
REMARK 465 SER E 249
REMARK 465 GLN E 250
REMARK 465 ASP E 251
REMARK 465 ALA E 252
REMARK 465 LYS E 253
REMARK 465 LYS E 254
REMARK 465 GLU E 255
REMARK 465 ILE E 256
REMARK 465 ASN E 257
REMARK 465 GLY E 258
REMARK 465 THR E 259
REMARK 465 ASP E 260
REMARK 465 SER E 261
REMARK 465 GLY E 262
REMARK 465 ASN E 263
REMARK 465 SER E 264
REMARK 465 HIS E 265
REMARK 465 ARG E 266
REMARK 465 ALA E 267
REMARK 465 SER E 383
REMARK 465 LEU E 384
REMARK 465 MET E 385
REMARK 465 MET F -58
REMARK 465 LEU F -57
REMARK 465 PRO F -56
REMARK 465 SER F -55
REMARK 465 ALA F -54
REMARK 465 GLN F -53
REMARK 465 VAL F -52
REMARK 465 ALA F -51
REMARK 465 ARG F -50
REMARK 465 LEU F -49
REMARK 465 LYS F -48
REMARK 465 PRO F -47
REMARK 465 ASP F -46
REMARK 465 PRO F -45
REMARK 465 PHE F -44
REMARK 465 PRO F -43
REMARK 465 PRO F -42
REMARK 465 SER F -41
REMARK 465 LEU F -40
REMARK 465 SER F -39
REMARK 465 PRO F -38
REMARK 465 ILE F -37
REMARK 465 PRO F -36
REMARK 465 HIS F -35
REMARK 465 GLY F -34
REMARK 465 ALA F -33
REMARK 465 VAL F -32
REMARK 465 THR F -31
REMARK 465 PHE F -30
REMARK 465 ALA F -29
REMARK 465 ALA F -28
REMARK 465 LEU F -27
REMARK 465 ALA F -26
REMARK 465 PRO F -25
REMARK 465 CYS F -24
REMARK 465 HIS F -23
REMARK 465 ASN F -22
REMARK 465 LEU F -21
REMARK 465 PRO F -20
REMARK 465 ILE F -19
REMARK 465 PHE F -18
REMARK 465 SER F -17
REMARK 465 SER F -16
REMARK 465 ARG F -15
REMARK 465 GLN F -14
REMARK 465 MET F -13
REMARK 465 LEU F -12
REMARK 465 ARG F -11
REMARK 465 ASP F -10
REMARK 465 SER F -9
REMARK 465 LEU F -8
REMARK 465 THR F -7
REMARK 465 TYR F -6
REMARK 465 SER F -5
REMARK 465 HIS F -4
REMARK 465 THR F -3
REMARK 465 SER F -2
REMARK 465 PRO F -1
REMARK 465 THR F 0
REMARK 465 MET F 1
REMARK 465 SER F 2
REMARK 465 PRO F 3
REMARK 465 GLN F 4
REMARK 465 ILE F 5
REMARK 465 ALA F 6
REMARK 465 GLU F 109
REMARK 465 GLY F 110
REMARK 465 GLN F 111
REMARK 465 ARG F 112
REMARK 465 ALA F 238
REMARK 465 PRO F 239
REMARK 465 GLY F 240
REMARK 465 VAL F 241
REMARK 465 GLN F 242
REMARK 465 ALA F 243
REMARK 465 GLY F 244
REMARK 465 ARG F 245
REMARK 465 ASN F 246
REMARK 465 ILE F 247
REMARK 465 SER F 248
REMARK 465 SER F 249
REMARK 465 GLN F 250
REMARK 465 ASP F 251
REMARK 465 ALA F 252
REMARK 465 LYS F 253
REMARK 465 LYS F 254
REMARK 465 GLU F 255
REMARK 465 ILE F 256
REMARK 465 ASN F 257
REMARK 465 GLY F 258
REMARK 465 THR F 259
REMARK 465 ASP F 260
REMARK 465 SER F 261
REMARK 465 GLY F 262
REMARK 465 ASN F 263
REMARK 465 SER F 264
REMARK 465 HIS F 265
REMARK 465 ARG F 266
REMARK 465 ALA F 267
REMARK 465 SER F 383
REMARK 465 LEU F 384
REMARK 465 MET F 385
REMARK 465 MET G -58
REMARK 465 LEU G -57
REMARK 465 PRO G -56
REMARK 465 SER G -55
REMARK 465 ALA G -54
REMARK 465 GLN G -53
REMARK 465 VAL G -52
REMARK 465 ALA G -51
REMARK 465 ARG G -50
REMARK 465 LEU G -49
REMARK 465 LYS G -48
REMARK 465 PRO G -47
REMARK 465 ASP G -46
REMARK 465 PRO G -45
REMARK 465 PHE G -44
REMARK 465 PRO G -43
REMARK 465 PRO G -42
REMARK 465 SER G -41
REMARK 465 LEU G -40
REMARK 465 SER G -39
REMARK 465 PRO G -38
REMARK 465 ILE G -37
REMARK 465 PRO G -36
REMARK 465 HIS G -35
REMARK 465 GLY G -34
REMARK 465 ALA G -33
REMARK 465 VAL G -32
REMARK 465 THR G -31
REMARK 465 PHE G -30
REMARK 465 ALA G -29
REMARK 465 ALA G -28
REMARK 465 LEU G -27
REMARK 465 ALA G -26
REMARK 465 PRO G -25
REMARK 465 CYS G -24
REMARK 465 HIS G -23
REMARK 465 ASN G -22
REMARK 465 LEU G -21
REMARK 465 PRO G -20
REMARK 465 ILE G -19
REMARK 465 PHE G -18
REMARK 465 SER G -17
REMARK 465 SER G -16
REMARK 465 ARG G -15
REMARK 465 GLN G -14
REMARK 465 MET G -13
REMARK 465 LEU G -12
REMARK 465 ARG G -11
REMARK 465 ASP G -10
REMARK 465 SER G -9
REMARK 465 LEU G -8
REMARK 465 THR G -7
REMARK 465 TYR G -6
REMARK 465 SER G -5
REMARK 465 HIS G -4
REMARK 465 THR G -3
REMARK 465 SER G -2
REMARK 465 PRO G -1
REMARK 465 THR G 0
REMARK 465 MET G 1
REMARK 465 SER G 2
REMARK 465 PRO G 3
REMARK 465 GLN G 4
REMARK 465 ILE G 5
REMARK 465 ALA G 6
REMARK 465 GLU G 109
REMARK 465 GLY G 110
REMARK 465 GLN G 111
REMARK 465 ALA G 238
REMARK 465 PRO G 239
REMARK 465 GLY G 240
REMARK 465 VAL G 241
REMARK 465 GLN G 242
REMARK 465 ALA G 243
REMARK 465 GLY G 244
REMARK 465 ARG G 245
REMARK 465 ASN G 246
REMARK 465 ILE G 247
REMARK 465 SER G 248
REMARK 465 SER G 249
REMARK 465 GLN G 250
REMARK 465 ASP G 251
REMARK 465 ALA G 252
REMARK 465 LYS G 253
REMARK 465 LYS G 254
REMARK 465 GLU G 255
REMARK 465 ILE G 256
REMARK 465 ASN G 257
REMARK 465 GLY G 258
REMARK 465 THR G 259
REMARK 465 ASP G 260
REMARK 465 SER G 261
REMARK 465 GLY G 262
REMARK 465 ASN G 263
REMARK 465 SER G 264
REMARK 465 HIS G 265
REMARK 465 ARG G 266
REMARK 465 ALA G 267
REMARK 465 GLY G 268
REMARK 465 SER G 383
REMARK 465 LEU G 384
REMARK 465 MET G 385
REMARK 465 MET H -58
REMARK 465 LEU H -57
REMARK 465 PRO H -56
REMARK 465 SER H -55
REMARK 465 ALA H -54
REMARK 465 GLN H -53
REMARK 465 VAL H -52
REMARK 465 ALA H -51
REMARK 465 ARG H -50
REMARK 465 LEU H -49
REMARK 465 LYS H -48
REMARK 465 PRO H -47
REMARK 465 ASP H -46
REMARK 465 PRO H -45
REMARK 465 PHE H -44
REMARK 465 PRO H -43
REMARK 465 PRO H -42
REMARK 465 SER H -41
REMARK 465 LEU H -40
REMARK 465 SER H -39
REMARK 465 PRO H -38
REMARK 465 ILE H -37
REMARK 465 PRO H -36
REMARK 465 HIS H -35
REMARK 465 GLY H -34
REMARK 465 ALA H -33
REMARK 465 VAL H -32
REMARK 465 THR H -31
REMARK 465 PHE H -30
REMARK 465 ALA H -29
REMARK 465 ALA H -28
REMARK 465 LEU H -27
REMARK 465 ALA H -26
REMARK 465 PRO H -25
REMARK 465 CYS H -24
REMARK 465 HIS H -23
REMARK 465 ASN H -22
REMARK 465 LEU H -21
REMARK 465 PRO H -20
REMARK 465 ILE H -19
REMARK 465 PHE H -18
REMARK 465 SER H -17
REMARK 465 SER H -16
REMARK 465 ARG H -15
REMARK 465 GLN H -14
REMARK 465 MET H -13
REMARK 465 LEU H -12
REMARK 465 ARG H -11
REMARK 465 ASP H -10
REMARK 465 SER H -9
REMARK 465 LEU H -8
REMARK 465 THR H -7
REMARK 465 TYR H -6
REMARK 465 SER H -5
REMARK 465 HIS H -4
REMARK 465 THR H -3
REMARK 465 SER H -2
REMARK 465 PRO H -1
REMARK 465 THR H 0
REMARK 465 MET H 1
REMARK 465 SER H 2
REMARK 465 PRO H 3
REMARK 465 GLN H 4
REMARK 465 ILE H 5
REMARK 465 ALA H 6
REMARK 465 GLU H 109
REMARK 465 GLY H 110
REMARK 465 GLN H 111
REMARK 465 VAL H 241
REMARK 465 GLN H 242
REMARK 465 ALA H 243
REMARK 465 GLY H 244
REMARK 465 ARG H 245
REMARK 465 ASN H 246
REMARK 465 ILE H 247
REMARK 465 SER H 248
REMARK 465 SER H 249
REMARK 465 GLN H 250
REMARK 465 ASP H 251
REMARK 465 ALA H 252
REMARK 465 LYS H 253
REMARK 465 LYS H 254
REMARK 465 GLU H 255
REMARK 465 ILE H 256
REMARK 465 ASN H 257
REMARK 465 GLY H 258
REMARK 465 THR H 259
REMARK 465 ASP H 260
REMARK 465 SER H 261
REMARK 465 GLY H 262
REMARK 465 ASN H 263
REMARK 465 SER H 264
REMARK 465 HIS H 265
REMARK 465 ARG H 266
REMARK 465 ALA H 267
REMARK 465 GLY H 268
REMARK 465 SER H 383
REMARK 465 LEU H 384
REMARK 465 MET H 385
REMARK 465 MET I -58
REMARK 465 LEU I -57
REMARK 465 PRO I -56
REMARK 465 SER I -55
REMARK 465 ALA I -54
REMARK 465 GLN I -53
REMARK 465 VAL I -52
REMARK 465 ALA I -51
REMARK 465 ARG I -50
REMARK 465 LEU I -49
REMARK 465 LYS I -48
REMARK 465 PRO I -47
REMARK 465 ASP I -46
REMARK 465 PRO I -45
REMARK 465 PHE I -44
REMARK 465 PRO I -43
REMARK 465 PRO I -42
REMARK 465 SER I -41
REMARK 465 LEU I -40
REMARK 465 SER I -39
REMARK 465 PRO I -38
REMARK 465 ILE I -37
REMARK 465 PRO I -36
REMARK 465 HIS I -35
REMARK 465 GLY I -34
REMARK 465 ALA I -33
REMARK 465 VAL I -32
REMARK 465 THR I -31
REMARK 465 PHE I -30
REMARK 465 ALA I -29
REMARK 465 ALA I -28
REMARK 465 LEU I -27
REMARK 465 ALA I -26
REMARK 465 PRO I -25
REMARK 465 CYS I -24
REMARK 465 HIS I -23
REMARK 465 ASN I -22
REMARK 465 LEU I -21
REMARK 465 PRO I -20
REMARK 465 ILE I -19
REMARK 465 PHE I -18
REMARK 465 SER I -17
REMARK 465 SER I -16
REMARK 465 ARG I -15
REMARK 465 GLN I -14
REMARK 465 MET I -13
REMARK 465 LEU I -12
REMARK 465 ARG I -11
REMARK 465 ASP I -10
REMARK 465 SER I -9
REMARK 465 LEU I -8
REMARK 465 THR I -7
REMARK 465 TYR I -6
REMARK 465 SER I -5
REMARK 465 HIS I -4
REMARK 465 THR I -3
REMARK 465 SER I -2
REMARK 465 PRO I -1
REMARK 465 THR I 0
REMARK 465 MET I 1
REMARK 465 SER I 2
REMARK 465 PRO I 3
REMARK 465 GLN I 4
REMARK 465 ILE I 5
REMARK 465 ALA I 6
REMARK 465 GLU I 109
REMARK 465 GLY I 110
REMARK 465 GLN I 111
REMARK 465 GLN I 242
REMARK 465 ALA I 243
REMARK 465 GLY I 244
REMARK 465 ARG I 245
REMARK 465 ASN I 246
REMARK 465 ILE I 247
REMARK 465 SER I 248
REMARK 465 SER I 249
REMARK 465 GLN I 250
REMARK 465 ASP I 251
REMARK 465 ALA I 252
REMARK 465 LYS I 253
REMARK 465 LYS I 254
REMARK 465 GLU I 255
REMARK 465 ILE I 256
REMARK 465 ASN I 257
REMARK 465 GLY I 258
REMARK 465 THR I 259
REMARK 465 ASP I 260
REMARK 465 SER I 261
REMARK 465 GLY I 262
REMARK 465 ASN I 263
REMARK 465 SER I 264
REMARK 465 HIS I 265
REMARK 465 ARG I 266
REMARK 465 ALA I 267
REMARK 465 SER I 383
REMARK 465 LEU I 384
REMARK 465 MET I 385
REMARK 465 MET J -58
REMARK 465 LEU J -57
REMARK 465 PRO J -56
REMARK 465 SER J -55
REMARK 465 ALA J -54
REMARK 465 GLN J -53
REMARK 465 VAL J -52
REMARK 465 ALA J -51
REMARK 465 ARG J -50
REMARK 465 LEU J -49
REMARK 465 LYS J -48
REMARK 465 PRO J -47
REMARK 465 ASP J -46
REMARK 465 PRO J -45
REMARK 465 PHE J -44
REMARK 465 PRO J -43
REMARK 465 PRO J -42
REMARK 465 SER J -41
REMARK 465 LEU J -40
REMARK 465 SER J -39
REMARK 465 PRO J -38
REMARK 465 ILE J -37
REMARK 465 PRO J -36
REMARK 465 HIS J -35
REMARK 465 GLY J -34
REMARK 465 ALA J -33
REMARK 465 VAL J -32
REMARK 465 THR J -31
REMARK 465 PHE J -30
REMARK 465 ALA J -29
REMARK 465 ALA J -28
REMARK 465 LEU J -27
REMARK 465 ALA J -26
REMARK 465 PRO J -25
REMARK 465 CYS J -24
REMARK 465 HIS J -23
REMARK 465 ASN J -22
REMARK 465 LEU J -21
REMARK 465 PRO J -20
REMARK 465 ILE J -19
REMARK 465 PHE J -18
REMARK 465 SER J -17
REMARK 465 SER J -16
REMARK 465 ARG J -15
REMARK 465 GLN J -14
REMARK 465 MET J -13
REMARK 465 LEU J -12
REMARK 465 ARG J -11
REMARK 465 ASP J -10
REMARK 465 SER J -9
REMARK 465 LEU J -8
REMARK 465 THR J -7
REMARK 465 TYR J -6
REMARK 465 SER J -5
REMARK 465 HIS J -4
REMARK 465 THR J -3
REMARK 465 SER J -2
REMARK 465 PRO J -1
REMARK 465 THR J 0
REMARK 465 MET J 1
REMARK 465 SER J 2
REMARK 465 PRO J 3
REMARK 465 GLN J 4
REMARK 465 ILE J 5
REMARK 465 ALA J 6
REMARK 465 GLU J 109
REMARK 465 GLY J 110
REMARK 465 GLN J 111
REMARK 465 ARG J 112
REMARK 465 ALA J 238
REMARK 465 PRO J 239
REMARK 465 GLY J 240
REMARK 465 VAL J 241
REMARK 465 GLN J 242
REMARK 465 ALA J 243
REMARK 465 GLY J 244
REMARK 465 ARG J 245
REMARK 465 ASN J 246
REMARK 465 ILE J 247
REMARK 465 SER J 248
REMARK 465 SER J 249
REMARK 465 GLN J 250
REMARK 465 ASP J 251
REMARK 465 ALA J 252
REMARK 465 LYS J 253
REMARK 465 LYS J 254
REMARK 465 GLU J 255
REMARK 465 ILE J 256
REMARK 465 ASN J 257
REMARK 465 GLY J 258
REMARK 465 THR J 259
REMARK 465 ASP J 260
REMARK 465 SER J 261
REMARK 465 GLY J 262
REMARK 465 ASN J 263
REMARK 465 SER J 264
REMARK 465 HIS J 265
REMARK 465 ARG J 266
REMARK 465 ALA J 267
REMARK 465 MET J 385
REMARK 465 MET K -58
REMARK 465 LEU K -57
REMARK 465 PRO K -56
REMARK 465 SER K -55
REMARK 465 ALA K -54
REMARK 465 GLN K -53
REMARK 465 VAL K -52
REMARK 465 ALA K -51
REMARK 465 ARG K -50
REMARK 465 LEU K -49
REMARK 465 LYS K -48
REMARK 465 PRO K -47
REMARK 465 ASP K -46
REMARK 465 PRO K -45
REMARK 465 PHE K -44
REMARK 465 PRO K -43
REMARK 465 PRO K -42
REMARK 465 SER K -41
REMARK 465 LEU K -40
REMARK 465 SER K -39
REMARK 465 PRO K -38
REMARK 465 ILE K -37
REMARK 465 PRO K -36
REMARK 465 HIS K -35
REMARK 465 GLY K -34
REMARK 465 ALA K -33
REMARK 465 VAL K -32
REMARK 465 THR K -31
REMARK 465 PHE K -30
REMARK 465 ALA K -29
REMARK 465 ALA K -28
REMARK 465 LEU K -27
REMARK 465 ALA K -26
REMARK 465 PRO K -25
REMARK 465 CYS K -24
REMARK 465 HIS K -23
REMARK 465 ASN K -22
REMARK 465 LEU K -21
REMARK 465 PRO K -20
REMARK 465 ILE K -19
REMARK 465 PHE K -18
REMARK 465 SER K -17
REMARK 465 SER K -16
REMARK 465 ARG K -15
REMARK 465 GLN K -14
REMARK 465 MET K -13
REMARK 465 LEU K -12
REMARK 465 ARG K -11
REMARK 465 ASP K -10
REMARK 465 SER K -9
REMARK 465 LEU K -8
REMARK 465 THR K -7
REMARK 465 TYR K -6
REMARK 465 SER K -5
REMARK 465 HIS K -4
REMARK 465 THR K -3
REMARK 465 SER K -2
REMARK 465 PRO K -1
REMARK 465 THR K 0
REMARK 465 MET K 1
REMARK 465 SER K 2
REMARK 465 PRO K 3
REMARK 465 GLN K 4
REMARK 465 ILE K 5
REMARK 465 ALA K 6
REMARK 465 GLU K 109
REMARK 465 GLY K 110
REMARK 465 GLN K 111
REMARK 465 ARG K 112
REMARK 465 ALA K 238
REMARK 465 PRO K 239
REMARK 465 GLY K 240
REMARK 465 VAL K 241
REMARK 465 GLN K 242
REMARK 465 ALA K 243
REMARK 465 GLY K 244
REMARK 465 ARG K 245
REMARK 465 ASN K 246
REMARK 465 ILE K 247
REMARK 465 SER K 248
REMARK 465 SER K 249
REMARK 465 GLN K 250
REMARK 465 ASP K 251
REMARK 465 ALA K 252
REMARK 465 LYS K 253
REMARK 465 LYS K 254
REMARK 465 GLU K 255
REMARK 465 ILE K 256
REMARK 465 ASN K 257
REMARK 465 GLY K 258
REMARK 465 THR K 259
REMARK 465 ASP K 260
REMARK 465 SER K 261
REMARK 465 GLY K 262
REMARK 465 ASN K 263
REMARK 465 SER K 264
REMARK 465 HIS K 265
REMARK 465 ARG K 266
REMARK 465 ALA K 267
REMARK 465 MET K 385
REMARK 465 MET L -58
REMARK 465 LEU L -57
REMARK 465 PRO L -56
REMARK 465 SER L -55
REMARK 465 ALA L -54
REMARK 465 GLN L -53
REMARK 465 VAL L -52
REMARK 465 ALA L -51
REMARK 465 ARG L -50
REMARK 465 LEU L -49
REMARK 465 LYS L -48
REMARK 465 PRO L -47
REMARK 465 ASP L -46
REMARK 465 PRO L -45
REMARK 465 PHE L -44
REMARK 465 PRO L -43
REMARK 465 PRO L -42
REMARK 465 SER L -41
REMARK 465 LEU L -40
REMARK 465 SER L -39
REMARK 465 PRO L -38
REMARK 465 ILE L -37
REMARK 465 PRO L -36
REMARK 465 HIS L -35
REMARK 465 GLY L -34
REMARK 465 ALA L -33
REMARK 465 VAL L -32
REMARK 465 THR L -31
REMARK 465 PHE L -30
REMARK 465 ALA L -29
REMARK 465 ALA L -28
REMARK 465 LEU L -27
REMARK 465 ALA L -26
REMARK 465 PRO L -25
REMARK 465 CYS L -24
REMARK 465 HIS L -23
REMARK 465 ASN L -22
REMARK 465 LEU L -21
REMARK 465 PRO L -20
REMARK 465 ILE L -19
REMARK 465 PHE L -18
REMARK 465 SER L -17
REMARK 465 SER L -16
REMARK 465 ARG L -15
REMARK 465 GLN L -14
REMARK 465 MET L -13
REMARK 465 LEU L -12
REMARK 465 ARG L -11
REMARK 465 ASP L -10
REMARK 465 SER L -9
REMARK 465 LEU L -8
REMARK 465 THR L -7
REMARK 465 TYR L -6
REMARK 465 SER L -5
REMARK 465 HIS L -4
REMARK 465 THR L -3
REMARK 465 SER L -2
REMARK 465 PRO L -1
REMARK 465 THR L 0
REMARK 465 MET L 1
REMARK 465 SER L 2
REMARK 465 PRO L 3
REMARK 465 GLN L 4
REMARK 465 ILE L 5
REMARK 465 ALA L 6
REMARK 465 ALA L 108
REMARK 465 GLU L 109
REMARK 465 GLY L 110
REMARK 465 GLN L 111
REMARK 465 ARG L 112
REMARK 465 ALA L 238
REMARK 465 PRO L 239
REMARK 465 GLY L 240
REMARK 465 VAL L 241
REMARK 465 GLN L 242
REMARK 465 ALA L 243
REMARK 465 GLY L 244
REMARK 465 ARG L 245
REMARK 465 ASN L 246
REMARK 465 ILE L 247
REMARK 465 SER L 248
REMARK 465 SER L 249
REMARK 465 GLN L 250
REMARK 465 ASP L 251
REMARK 465 ALA L 252
REMARK 465 LYS L 253
REMARK 465 LYS L 254
REMARK 465 GLU L 255
REMARK 465 ILE L 256
REMARK 465 ASN L 257
REMARK 465 GLY L 258
REMARK 465 THR L 259
REMARK 465 ASP L 260
REMARK 465 SER L 261
REMARK 465 GLY L 262
REMARK 465 ASN L 263
REMARK 465 SER L 264
REMARK 465 HIS L 265
REMARK 465 ARG L 266
REMARK 465 ALA L 267
REMARK 465 SER L 383
REMARK 465 LEU L 384
REMARK 465 MET L 385
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 OG1 THR B 303 - O HOH B 2124 2.16
REMARK 500 O ARG C 20 - NH1 ARG C 136 2.08
REMARK 500 NE1 TRP D 68 - O HOH D 2029 2.18
REMARK 500 OD1 ASP E 14 - O HOH E 2005 1.72
REMARK 500 N GLY E 268 - N6A COA E 1383 2.03
REMARK 500 OG SER F 332 - O GLU F 360 2.05
REMARK 500 OG SER G 332 - O GLU G 360 2.13
REMARK 500 OG1 THR H 303 - O HOH H 2117 1.67
REMARK 500 OG SER H 332 - O GLU H 360 2.01
REMARK 500 OH TYR J 280 - O7A COA J 1385 2.17
REMARK 500 O GLU J 360 - O HOH J 2076 1.89
REMARK 500 OG SER L 332 - O GLU L 360 2.06
REMARK 500 O9A COA B 1383 - O HOH B 2170 2.01
REMARK 500 O2B COA H 1383 - O HOH H 2144 2.04
REMARK 500 O HOH I 2042 - O HOH I 2160 2.07
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,A3,1X,A1,I4,A1,1X,2(A4,A1,3X),12X,F5.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCELIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 LEU A 326 CG LEU A 326 CD2 -0.313
REMARK 500 ARG B 8 CZ ARG B 8 NH1 -0.121
REMARK 500 ARG B 8 CZ ARG B 8 NH2 -0.110
REMARK 500 PHE B 186 CE1 PHE B 186 CZ -0.223
REMARK 500 PHE B 186 CE2 PHE B 186 CZ -0.188
REMARK 500 PHE B 186 CG PHE B 186 CD1 -0.140
REMARK 500 PHE B 186 CG PHE B 186 CD2 -0.168
REMARK 500 ASN B 373 CG ASN B 373 OD1 -0.133
REMARK 500 GLN C 189 CD GLN C 189 NE2 -0.158
REMARK 500 GLN C 191 CD GLN C 191 NE2 -0.154
REMARK 500 GLU D 27 CD GLU D 27 OE1 -0.108
REMARK 500 GLU D 27 CD GLU D 27 OE2 -0.081
REMARK 500 LEU D 200 CG LEU D 200 CD2 -0.235
REMARK 500 GLU D 340 CD GLU D 340 OE1 -0.117
REMARK 500 GLU D 340 CD GLU D 340 OE2 -0.116
REMARK 500 ARG F 190 CZ ARG F 190 NH1 -0.120
REMARK 500 ARG F 190 CZ ARG F 190 NH2 -0.092
REMARK 500 GLU J 27 CD GLU J 27 OE1 -0.096
REMARK 500 GLU J 27 CD GLU J 27 OE2 -0.081
REMARK 500 CYS F 176 CB CYS F 176 SG -0.103
REMARK 500 CYS G 102 CB CYS G 102 SG -0.098
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: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCELIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 177 NE - CZ - NH1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ARG A 177 NE - CZ - NH2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 LEU A 326 CD1 - CG - CD2 ANGL. DEV. = -23.6 DEGREES
REMARK 500 ARG B 8 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ARG B 8 NE - CZ - NH2 ANGL. DEV. = 5.2 DEGREES
REMARK 500 ARG B 8 NH1 - CZ - NH2 ANGL. DEV. = -8.9 DEGREES
REMARK 500 ARG C 310 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 GLU D 27 OE1 - CD - OE2 ANGL. DEV. = -11.9 DEGREES
REMARK 500 GLU D 340 OE1 - CD - OE2 ANGL. DEV. = -12.0 DEGREES
REMARK 500 ARG F 190 NE - CZ - NH1 ANGL. DEV. = 4.6 DEGREES
REMARK 500 ARG F 190 NE - CZ - NH2 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ARG F 190 NH1 - CZ - NH2 ANGL. DEV. = -8.2 DEGREES
REMARK 500 MET G 297 CG - SD - CE ANGL. DEV. = 10.5 DEGREES
REMARK 500 MET H 297 CG - SD - CE ANGL. DEV. = 10.4 DEGREES
REMARK 500 ARG H 310 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 ARG H 310 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 GLU J 27 OE1 - CD - OE2 ANGL. DEV. = -11.7 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500 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 ALA A 108 -5.92 -158.66
REMARK 500 SER A 149 -122.56 67.66
REMARK 500 LYS A 226 -158.01 -104.90
REMARK 500 ASP A 305 102.71 -172.02
REMARK 500 ASN A 350 73.41 -115.92
REMARK 500 GLU A 368 41.00 -106.24
REMARK 500 SER B 149 -119.59 65.60
REMARK 500 LYS B 226 -165.32 -104.73
REMARK 500 GLN B 269 -29.60 -153.48
REMARK 500 ASP B 305 109.94 -169.11
REMARK 500 ASN B 350 70.44 -115.91
REMARK 500 GLU B 368 40.64 -102.91
REMARK 500 ASP C 107 30.72 -82.98
REMARK 500 ALA C 108 16.27 -154.62
REMARK 500 SER C 149 -122.63 67.35
REMARK 500 LYS C 226 -169.00 -107.41
REMARK 500 ASP C 305 106.01 -173.99
REMARK 500 ASN C 350 71.58 -119.15
REMARK 500 SER D 149 -120.12 65.22
REMARK 500 LYS D 226 -167.17 -101.06
REMARK 500 ASP D 305 109.74 -170.94
REMARK 500 ASN D 350 72.73 -118.11
REMARK 500 ASP D 363 -9.32 -56.78
REMARK 500 SER E 149 -123.70 65.35
REMARK 500 LYS E 226 -159.87 -107.69
REMARK 500 GLN E 269 -26.56 -149.81
REMARK 500 ASP E 305 102.09 -171.18
REMARK 500 ASN E 350 72.28 -116.44
REMARK 500 ASP E 363 -6.84 -58.91
REMARK 500 THR F 81 0.02 -69.18
REMARK 500 SER F 149 -124.07 65.00
REMARK 500 LYS F 226 -169.54 -108.24
REMARK 500 ASP F 305 108.31 -167.87
REMARK 500 ASN F 350 74.00 -111.50
REMARK 500 ASP F 363 -13.65 -48.81
REMARK 500 ASP G 14 171.41 -59.39
REMARK 500 SER G 149 -121.57 67.32
REMARK 500 ASP G 305 110.71 -167.33
REMARK 500 ASN G 350 70.86 -114.18
REMARK 500 GLU G 368 43.79 -106.42
REMARK 500 SER H 149 -121.48 67.04
REMARK 500 ASP H 305 108.59 -167.02
REMARK 500 ASN H 350 69.97 -113.82
REMARK 500 GLU H 368 45.72 -106.79
REMARK 500 SER I 149 -118.95 67.04
REMARK 500 LYS I 226 -164.81 -104.03
REMARK 500 GLN I 269 -21.38 -150.56
REMARK 500 ASP I 305 107.95 -169.29
REMARK 500 ASN I 350 74.55 -113.10
REMARK 500 GLU I 368 43.70 -102.78
REMARK 500 ASN J 46 -168.35 -77.42
REMARK 500 SER J 149 -117.89 72.62
REMARK 500 ASP J 305 105.91 -172.02
REMARK 500 ASN J 350 64.64 -112.39
REMARK 500 SER K 149 -121.90 70.00
REMARK 500 LYS K 226 -169.32 -100.40
REMARK 500 ASP K 305 107.43 -169.50
REMARK 500 ASN K 350 63.28 -110.86
REMARK 500 ASP K 363 -7.44 -58.57
REMARK 500 GLU K 368 41.34 -105.70
REMARK 500 THR L 81 2.04 -69.69
REMARK 500 SER L 149 -122.58 63.61
REMARK 500 LYS L 226 -165.90 -103.81
REMARK 500 GLN L 269 -35.20 -141.48
REMARK 500 ASP L 305 107.81 -168.08
REMARK 500 ASN L 350 76.07 -110.65
REMARK 500 GLU L 368 43.41 -107.28
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLY L 268 GLN L 269 0 147.64
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COA A 1383
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COA B 1383
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COA C 1383
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COA D 1383
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COA E 1383
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COA F 1383
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COA G 1383
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COA H 1383
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COA I 1383
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COA J 1385
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COA K 1385
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COA L 1383
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 1384
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL I 1384
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 1384
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 1385
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT E 1384
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT I 1385
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT H 1384
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT G 1384
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT D 1384
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT C 1384
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT F 1384
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT J 1386
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT K 1386
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT L 1384
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2VAV RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF DEACETYLCEPHALOSPORIN C
REMARK 900 ACETYLTRANSFERASE (COMPLEX I)
REMARK 900 RELATED ID: 2VAX RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF DEACETYLCEPHALOSPORIN C
REMARK 900 ACETYLTRANSFERASE (COMPLEX II)
DBREF 2VAT A -58 385 UNP P39058 CEFG_CEPAC 1 444
DBREF 2VAT B -58 385 UNP P39058 CEFG_CEPAC 1 444
DBREF 2VAT C -58 385 UNP P39058 CEFG_CEPAC 1 444
DBREF 2VAT D -58 385 UNP P39058 CEFG_CEPAC 1 444
DBREF 2VAT E -58 385 UNP P39058 CEFG_CEPAC 1 444
DBREF 2VAT F -58 385 UNP P39058 CEFG_CEPAC 1 444
DBREF 2VAT G -58 385 UNP P39058 CEFG_CEPAC 1 444
DBREF 2VAT H -58 385 UNP P39058 CEFG_CEPAC 1 444
DBREF 2VAT I -58 385 UNP P39058 CEFG_CEPAC 1 444
DBREF 2VAT J -58 385 UNP P39058 CEFG_CEPAC 1 444
DBREF 2VAT K -58 385 UNP P39058 CEFG_CEPAC 1 444
DBREF 2VAT L -58 385 UNP P39058 CEFG_CEPAC 1 444
SEQRES 1 A 444 MET LEU PRO SER ALA GLN VAL ALA ARG LEU LYS PRO ASP
SEQRES 2 A 444 PRO PHE PRO PRO SER LEU SER PRO ILE PRO HIS GLY ALA
SEQRES 3 A 444 VAL THR PHE ALA ALA LEU ALA PRO CYS HIS ASN LEU PRO
SEQRES 4 A 444 ILE PHE SER SER ARG GLN MET LEU ARG ASP SER LEU THR
SEQRES 5 A 444 TYR SER HIS THR SER PRO THR MET SER PRO GLN ILE ALA
SEQRES 6 A 444 ASN ARG PHE GLU ALA SER LEU ASP ALA GLN ASP ILE ALA
SEQRES 7 A 444 ARG ILE SER LEU PHE THR LEU GLU SER GLY VAL ILE LEU
SEQRES 8 A 444 ARG ASP VAL PRO VAL ALA TYR LYS SER TRP GLY ARG MET
SEQRES 9 A 444 ASN VAL SER ARG ASP ASN CYS VAL ILE VAL CYS HIS THR
SEQRES 10 A 444 LEU THR SER SER ALA HIS VAL THR SER TRP TRP PRO THR
SEQRES 11 A 444 LEU PHE GLY GLN GLY ARG ALA PHE ASP THR SER ARG TYR
SEQRES 12 A 444 PHE ILE ILE CYS LEU ASN TYR LEU GLY SER PRO PHE GLY
SEQRES 13 A 444 SER ALA GLY PRO CYS SER PRO ASP PRO ASP ALA GLU GLY
SEQRES 14 A 444 GLN ARG PRO TYR GLY ALA LYS PHE PRO ARG THR THR ILE
SEQRES 15 A 444 ARG ASP ASP VAL ARG ILE HIS ARG GLN VAL LEU ASP ARG
SEQRES 16 A 444 LEU GLY VAL ARG GLN ILE ALA ALA VAL VAL GLY ALA SER
SEQRES 17 A 444 MET GLY GLY MET HIS THR LEU GLU TRP ALA PHE PHE GLY
SEQRES 18 A 444 PRO GLU TYR VAL ARG LYS ILE VAL PRO ILE ALA THR SER
SEQRES 19 A 444 CYS ARG GLN SER GLY TRP CYS ALA ALA TRP PHE GLU THR
SEQRES 20 A 444 GLN ARG GLN CYS ILE TYR ASP ASP PRO LYS TYR LEU ASP
SEQRES 21 A 444 GLY GLU TYR ASP VAL ASP ASP GLN PRO VAL ARG GLY LEU
SEQRES 22 A 444 GLU THR ALA ARG LYS ILE ALA ASN LEU THR TYR LYS SER
SEQRES 23 A 444 LYS PRO ALA MET ASP GLU ARG PHE HIS MET ALA PRO GLY
SEQRES 24 A 444 VAL GLN ALA GLY ARG ASN ILE SER SER GLN ASP ALA LYS
SEQRES 25 A 444 LYS GLU ILE ASN GLY THR ASP SER GLY ASN SER HIS ARG
SEQRES 26 A 444 ALA GLY GLN PRO ILE GLU ALA VAL SER SER TYR LEU ARG
SEQRES 27 A 444 TYR GLN ALA GLN LYS PHE ALA ALA SER PHE ASP ALA ASN
SEQRES 28 A 444 CYS TYR ILE ALA MET THR LEU LYS PHE ASP THR HIS ASP
SEQRES 29 A 444 ILE SER ARG GLY ARG ALA GLY SER ILE PRO GLU ALA LEU
SEQRES 30 A 444 ALA MET ILE THR GLN PRO ALA LEU ILE ILE CYS ALA ARG
SEQRES 31 A 444 SER ASP GLY LEU TYR SER PHE ASP GLU HIS VAL GLU MET
SEQRES 32 A 444 GLY ARG SER ILE PRO ASN SER ARG LEU CYS VAL VAL ASP
SEQRES 33 A 444 THR ASN GLU GLY HIS ASP PHE PHE VAL MET GLU ALA ASP
SEQRES 34 A 444 LYS VAL ASN ASP ALA VAL ARG GLY PHE LEU ASP GLN SER
SEQRES 35 A 444 LEU MET
SEQRES 1 B 444 MET LEU PRO SER ALA GLN VAL ALA ARG LEU LYS PRO ASP
SEQRES 2 B 444 PRO PHE PRO PRO SER LEU SER PRO ILE PRO HIS GLY ALA
SEQRES 3 B 444 VAL THR PHE ALA ALA LEU ALA PRO CYS HIS ASN LEU PRO
SEQRES 4 B 444 ILE PHE SER SER ARG GLN MET LEU ARG ASP SER LEU THR
SEQRES 5 B 444 TYR SER HIS THR SER PRO THR MET SER PRO GLN ILE ALA
SEQRES 6 B 444 ASN ARG PHE GLU ALA SER LEU ASP ALA GLN ASP ILE ALA
SEQRES 7 B 444 ARG ILE SER LEU PHE THR LEU GLU SER GLY VAL ILE LEU
SEQRES 8 B 444 ARG ASP VAL PRO VAL ALA TYR LYS SER TRP GLY ARG MET
SEQRES 9 B 444 ASN VAL SER ARG ASP ASN CYS VAL ILE VAL CYS HIS THR
SEQRES 10 B 444 LEU THR SER SER ALA HIS VAL THR SER TRP TRP PRO THR
SEQRES 11 B 444 LEU PHE GLY GLN GLY ARG ALA PHE ASP THR SER ARG TYR
SEQRES 12 B 444 PHE ILE ILE CYS LEU ASN TYR LEU GLY SER PRO PHE GLY
SEQRES 13 B 444 SER ALA GLY PRO CYS SER PRO ASP PRO ASP ALA GLU GLY
SEQRES 14 B 444 GLN ARG PRO TYR GLY ALA LYS PHE PRO ARG THR THR ILE
SEQRES 15 B 444 ARG ASP ASP VAL ARG ILE HIS ARG GLN VAL LEU ASP ARG
SEQRES 16 B 444 LEU GLY VAL ARG GLN ILE ALA ALA VAL VAL GLY ALA SER
SEQRES 17 B 444 MET GLY GLY MET HIS THR LEU GLU TRP ALA PHE PHE GLY
SEQRES 18 B 444 PRO GLU TYR VAL ARG LYS ILE VAL PRO ILE ALA THR SER
SEQRES 19 B 444 CYS ARG GLN SER GLY TRP CYS ALA ALA TRP PHE GLU THR
SEQRES 20 B 444 GLN ARG GLN CYS ILE TYR ASP ASP PRO LYS TYR LEU ASP
SEQRES 21 B 444 GLY GLU TYR ASP VAL ASP ASP GLN PRO VAL ARG GLY LEU
SEQRES 22 B 444 GLU THR ALA ARG LYS ILE ALA ASN LEU THR TYR LYS SER
SEQRES 23 B 444 LYS PRO ALA MET ASP GLU ARG PHE HIS MET ALA PRO GLY
SEQRES 24 B 444 VAL GLN ALA GLY ARG ASN ILE SER SER GLN ASP ALA LYS
SEQRES 25 B 444 LYS GLU ILE ASN GLY THR ASP SER GLY ASN SER HIS ARG
SEQRES 26 B 444 ALA GLY GLN PRO ILE GLU ALA VAL SER SER TYR LEU ARG
SEQRES 27 B 444 TYR GLN ALA GLN LYS PHE ALA ALA SER PHE ASP ALA ASN
SEQRES 28 B 444 CYS TYR ILE ALA MET THR LEU LYS PHE ASP THR HIS ASP
SEQRES 29 B 444 ILE SER ARG GLY ARG ALA GLY SER ILE PRO GLU ALA LEU
SEQRES 30 B 444 ALA MET ILE THR GLN PRO ALA LEU ILE ILE CYS ALA ARG
SEQRES 31 B 444 SER ASP GLY LEU TYR SER PHE ASP GLU HIS VAL GLU MET
SEQRES 32 B 444 GLY ARG SER ILE PRO ASN SER ARG LEU CYS VAL VAL ASP
SEQRES 33 B 444 THR ASN GLU GLY HIS ASP PHE PHE VAL MET GLU ALA ASP
SEQRES 34 B 444 LYS VAL ASN ASP ALA VAL ARG GLY PHE LEU ASP GLN SER
SEQRES 35 B 444 LEU MET
SEQRES 1 C 444 MET LEU PRO SER ALA GLN VAL ALA ARG LEU LYS PRO ASP
SEQRES 2 C 444 PRO PHE PRO PRO SER LEU SER PRO ILE PRO HIS GLY ALA
SEQRES 3 C 444 VAL THR PHE ALA ALA LEU ALA PRO CYS HIS ASN LEU PRO
SEQRES 4 C 444 ILE PHE SER SER ARG GLN MET LEU ARG ASP SER LEU THR
SEQRES 5 C 444 TYR SER HIS THR SER PRO THR MET SER PRO GLN ILE ALA
SEQRES 6 C 444 ASN ARG PHE GLU ALA SER LEU ASP ALA GLN ASP ILE ALA
SEQRES 7 C 444 ARG ILE SER LEU PHE THR LEU GLU SER GLY VAL ILE LEU
SEQRES 8 C 444 ARG ASP VAL PRO VAL ALA TYR LYS SER TRP GLY ARG MET
SEQRES 9 C 444 ASN VAL SER ARG ASP ASN CYS VAL ILE VAL CYS HIS THR
SEQRES 10 C 444 LEU THR SER SER ALA HIS VAL THR SER TRP TRP PRO THR
SEQRES 11 C 444 LEU PHE GLY GLN GLY ARG ALA PHE ASP THR SER ARG TYR
SEQRES 12 C 444 PHE ILE ILE CYS LEU ASN TYR LEU GLY SER PRO PHE GLY
SEQRES 13 C 444 SER ALA GLY PRO CYS SER PRO ASP PRO ASP ALA GLU GLY
SEQRES 14 C 444 GLN ARG PRO TYR GLY ALA LYS PHE PRO ARG THR THR ILE
SEQRES 15 C 444 ARG ASP ASP VAL ARG ILE HIS ARG GLN VAL LEU ASP ARG
SEQRES 16 C 444 LEU GLY VAL ARG GLN ILE ALA ALA VAL VAL GLY ALA SER
SEQRES 17 C 444 MET GLY GLY MET HIS THR LEU GLU TRP ALA PHE PHE GLY
SEQRES 18 C 444 PRO GLU TYR VAL ARG LYS ILE VAL PRO ILE ALA THR SER
SEQRES 19 C 444 CYS ARG GLN SER GLY TRP CYS ALA ALA TRP PHE GLU THR
SEQRES 20 C 444 GLN ARG GLN CYS ILE TYR ASP ASP PRO LYS TYR LEU ASP
SEQRES 21 C 444 GLY GLU TYR ASP VAL ASP ASP GLN PRO VAL ARG GLY LEU
SEQRES 22 C 444 GLU THR ALA ARG LYS ILE ALA ASN LEU THR TYR LYS SER
SEQRES 23 C 444 LYS PRO ALA MET ASP GLU ARG PHE HIS MET ALA PRO GLY
SEQRES 24 C 444 VAL GLN ALA GLY ARG ASN ILE SER SER GLN ASP ALA LYS
SEQRES 25 C 444 LYS GLU ILE ASN GLY THR ASP SER GLY ASN SER HIS ARG
SEQRES 26 C 444 ALA GLY GLN PRO ILE GLU ALA VAL SER SER TYR LEU ARG
SEQRES 27 C 444 TYR GLN ALA GLN LYS PHE ALA ALA SER PHE ASP ALA ASN
SEQRES 28 C 444 CYS TYR ILE ALA MET THR LEU LYS PHE ASP THR HIS ASP
SEQRES 29 C 444 ILE SER ARG GLY ARG ALA GLY SER ILE PRO GLU ALA LEU
SEQRES 30 C 444 ALA MET ILE THR GLN PRO ALA LEU ILE ILE CYS ALA ARG
SEQRES 31 C 444 SER ASP GLY LEU TYR SER PHE ASP GLU HIS VAL GLU MET
SEQRES 32 C 444 GLY ARG SER ILE PRO ASN SER ARG LEU CYS VAL VAL ASP
SEQRES 33 C 444 THR ASN GLU GLY HIS ASP PHE PHE VAL MET GLU ALA ASP
SEQRES 34 C 444 LYS VAL ASN ASP ALA VAL ARG GLY PHE LEU ASP GLN SER
SEQRES 35 C 444 LEU MET
SEQRES 1 D 444 MET LEU PRO SER ALA GLN VAL ALA ARG LEU LYS PRO ASP
SEQRES 2 D 444 PRO PHE PRO PRO SER LEU SER PRO ILE PRO HIS GLY ALA
SEQRES 3 D 444 VAL THR PHE ALA ALA LEU ALA PRO CYS HIS ASN LEU PRO
SEQRES 4 D 444 ILE PHE SER SER ARG GLN MET LEU ARG ASP SER LEU THR
SEQRES 5 D 444 TYR SER HIS THR SER PRO THR MET SER PRO GLN ILE ALA
SEQRES 6 D 444 ASN ARG PHE GLU ALA SER LEU ASP ALA GLN ASP ILE ALA
SEQRES 7 D 444 ARG ILE SER LEU PHE THR LEU GLU SER GLY VAL ILE LEU
SEQRES 8 D 444 ARG ASP VAL PRO VAL ALA TYR LYS SER TRP GLY ARG MET
SEQRES 9 D 444 ASN VAL SER ARG ASP ASN CYS VAL ILE VAL CYS HIS THR
SEQRES 10 D 444 LEU THR SER SER ALA HIS VAL THR SER TRP TRP PRO THR
SEQRES 11 D 444 LEU PHE GLY GLN GLY ARG ALA PHE ASP THR SER ARG TYR
SEQRES 12 D 444 PHE ILE ILE CYS LEU ASN TYR LEU GLY SER PRO PHE GLY
SEQRES 13 D 444 SER ALA GLY PRO CYS SER PRO ASP PRO ASP ALA GLU GLY
SEQRES 14 D 444 GLN ARG PRO TYR GLY ALA LYS PHE PRO ARG THR THR ILE
SEQRES 15 D 444 ARG ASP ASP VAL ARG ILE HIS ARG GLN VAL LEU ASP ARG
SEQRES 16 D 444 LEU GLY VAL ARG GLN ILE ALA ALA VAL VAL GLY ALA SER
SEQRES 17 D 444 MET GLY GLY MET HIS THR LEU GLU TRP ALA PHE PHE GLY
SEQRES 18 D 444 PRO GLU TYR VAL ARG LYS ILE VAL PRO ILE ALA THR SER
SEQRES 19 D 444 CYS ARG GLN SER GLY TRP CYS ALA ALA TRP PHE GLU THR
SEQRES 20 D 444 GLN ARG GLN CYS ILE TYR ASP ASP PRO LYS TYR LEU ASP
SEQRES 21 D 444 GLY GLU TYR ASP VAL ASP ASP GLN PRO VAL ARG GLY LEU
SEQRES 22 D 444 GLU THR ALA ARG LYS ILE ALA ASN LEU THR TYR LYS SER
SEQRES 23 D 444 LYS PRO ALA MET ASP GLU ARG PHE HIS MET ALA PRO GLY
SEQRES 24 D 444 VAL GLN ALA GLY ARG ASN ILE SER SER GLN ASP ALA LYS
SEQRES 25 D 444 LYS GLU ILE ASN GLY THR ASP SER GLY ASN SER HIS ARG
SEQRES 26 D 444 ALA GLY GLN PRO ILE GLU ALA VAL SER SER TYR LEU ARG
SEQRES 27 D 444 TYR GLN ALA GLN LYS PHE ALA ALA SER PHE ASP ALA ASN
SEQRES 28 D 444 CYS TYR ILE ALA MET THR LEU LYS PHE ASP THR HIS ASP
SEQRES 29 D 444 ILE SER ARG GLY ARG ALA GLY SER ILE PRO GLU ALA LEU
SEQRES 30 D 444 ALA MET ILE THR GLN PRO ALA LEU ILE ILE CYS ALA ARG
SEQRES 31 D 444 SER ASP GLY LEU TYR SER PHE ASP GLU HIS VAL GLU MET
SEQRES 32 D 444 GLY ARG SER ILE PRO ASN SER ARG LEU CYS VAL VAL ASP
SEQRES 33 D 444 THR ASN GLU GLY HIS ASP PHE PHE VAL MET GLU ALA ASP
SEQRES 34 D 444 LYS VAL ASN ASP ALA VAL ARG GLY PHE LEU ASP GLN SER
SEQRES 35 D 444 LEU MET
SEQRES 1 E 444 MET LEU PRO SER ALA GLN VAL ALA ARG LEU LYS PRO ASP
SEQRES 2 E 444 PRO PHE PRO PRO SER LEU SER PRO ILE PRO HIS GLY ALA
SEQRES 3 E 444 VAL THR PHE ALA ALA LEU ALA PRO CYS HIS ASN LEU PRO
SEQRES 4 E 444 ILE PHE SER SER ARG GLN MET LEU ARG ASP SER LEU THR
SEQRES 5 E 444 TYR SER HIS THR SER PRO THR MET SER PRO GLN ILE ALA
SEQRES 6 E 444 ASN ARG PHE GLU ALA SER LEU ASP ALA GLN ASP ILE ALA
SEQRES 7 E 444 ARG ILE SER LEU PHE THR LEU GLU SER GLY VAL ILE LEU
SEQRES 8 E 444 ARG ASP VAL PRO VAL ALA TYR LYS SER TRP GLY ARG MET
SEQRES 9 E 444 ASN VAL SER ARG ASP ASN CYS VAL ILE VAL CYS HIS THR
SEQRES 10 E 444 LEU THR SER SER ALA HIS VAL THR SER TRP TRP PRO THR
SEQRES 11 E 444 LEU PHE GLY GLN GLY ARG ALA PHE ASP THR SER ARG TYR
SEQRES 12 E 444 PHE ILE ILE CYS LEU ASN TYR LEU GLY SER PRO PHE GLY
SEQRES 13 E 444 SER ALA GLY PRO CYS SER PRO ASP PRO ASP ALA GLU GLY
SEQRES 14 E 444 GLN ARG PRO TYR GLY ALA LYS PHE PRO ARG THR THR ILE
SEQRES 15 E 444 ARG ASP ASP VAL ARG ILE HIS ARG GLN VAL LEU ASP ARG
SEQRES 16 E 444 LEU GLY VAL ARG GLN ILE ALA ALA VAL VAL GLY ALA SER
SEQRES 17 E 444 MET GLY GLY MET HIS THR LEU GLU TRP ALA PHE PHE GLY
SEQRES 18 E 444 PRO GLU TYR VAL ARG LYS ILE VAL PRO ILE ALA THR SER
SEQRES 19 E 444 CYS ARG GLN SER GLY TRP CYS ALA ALA TRP PHE GLU THR
SEQRES 20 E 444 GLN ARG GLN CYS ILE TYR ASP ASP PRO LYS TYR LEU ASP
SEQRES 21 E 444 GLY GLU TYR ASP VAL ASP ASP GLN PRO VAL ARG GLY LEU
SEQRES 22 E 444 GLU THR ALA ARG LYS ILE ALA ASN LEU THR TYR LYS SER
SEQRES 23 E 444 LYS PRO ALA MET ASP GLU ARG PHE HIS MET ALA PRO GLY
SEQRES 24 E 444 VAL GLN ALA GLY ARG ASN ILE SER SER GLN ASP ALA LYS
SEQRES 25 E 444 LYS GLU ILE ASN GLY THR ASP SER GLY ASN SER HIS ARG
SEQRES 26 E 444 ALA GLY GLN PRO ILE GLU ALA VAL SER SER TYR LEU ARG
SEQRES 27 E 444 TYR GLN ALA GLN LYS PHE ALA ALA SER PHE ASP ALA ASN
SEQRES 28 E 444 CYS TYR ILE ALA MET THR LEU LYS PHE ASP THR HIS ASP
SEQRES 29 E 444 ILE SER ARG GLY ARG ALA GLY SER ILE PRO GLU ALA LEU
SEQRES 30 E 444 ALA MET ILE THR GLN PRO ALA LEU ILE ILE CYS ALA ARG
SEQRES 31 E 444 SER ASP GLY LEU TYR SER PHE ASP GLU HIS VAL GLU MET
SEQRES 32 E 444 GLY ARG SER ILE PRO ASN SER ARG LEU CYS VAL VAL ASP
SEQRES 33 E 444 THR ASN GLU GLY HIS ASP PHE PHE VAL MET GLU ALA ASP
SEQRES 34 E 444 LYS VAL ASN ASP ALA VAL ARG GLY PHE LEU ASP GLN SER
SEQRES 35 E 444 LEU MET
SEQRES 1 F 444 MET LEU PRO SER ALA GLN VAL ALA ARG LEU LYS PRO ASP
SEQRES 2 F 444 PRO PHE PRO PRO SER LEU SER PRO ILE PRO HIS GLY ALA
SEQRES 3 F 444 VAL THR PHE ALA ALA LEU ALA PRO CYS HIS ASN LEU PRO
SEQRES 4 F 444 ILE PHE SER SER ARG GLN MET LEU ARG ASP SER LEU THR
SEQRES 5 F 444 TYR SER HIS THR SER PRO THR MET SER PRO GLN ILE ALA
SEQRES 6 F 444 ASN ARG PHE GLU ALA SER LEU ASP ALA GLN ASP ILE ALA
SEQRES 7 F 444 ARG ILE SER LEU PHE THR LEU GLU SER GLY VAL ILE LEU
SEQRES 8 F 444 ARG ASP VAL PRO VAL ALA TYR LYS SER TRP GLY ARG MET
SEQRES 9 F 444 ASN VAL SER ARG ASP ASN CYS VAL ILE VAL CYS HIS THR
SEQRES 10 F 444 LEU THR SER SER ALA HIS VAL THR SER TRP TRP PRO THR
SEQRES 11 F 444 LEU PHE GLY GLN GLY ARG ALA PHE ASP THR SER ARG TYR
SEQRES 12 F 444 PHE ILE ILE CYS LEU ASN TYR LEU GLY SER PRO PHE GLY
SEQRES 13 F 444 SER ALA GLY PRO CYS SER PRO ASP PRO ASP ALA GLU GLY
SEQRES 14 F 444 GLN ARG PRO TYR GLY ALA LYS PHE PRO ARG THR THR ILE
SEQRES 15 F 444 ARG ASP ASP VAL ARG ILE HIS ARG GLN VAL LEU ASP ARG
SEQRES 16 F 444 LEU GLY VAL ARG GLN ILE ALA ALA VAL VAL GLY ALA SER
SEQRES 17 F 444 MET GLY GLY MET HIS THR LEU GLU TRP ALA PHE PHE GLY
SEQRES 18 F 444 PRO GLU TYR VAL ARG LYS ILE VAL PRO ILE ALA THR SER
SEQRES 19 F 444 CYS ARG GLN SER GLY TRP CYS ALA ALA TRP PHE GLU THR
SEQRES 20 F 444 GLN ARG GLN CYS ILE TYR ASP ASP PRO LYS TYR LEU ASP
SEQRES 21 F 444 GLY GLU TYR ASP VAL ASP ASP GLN PRO VAL ARG GLY LEU
SEQRES 22 F 444 GLU THR ALA ARG LYS ILE ALA ASN LEU THR TYR LYS SER
SEQRES 23 F 444 LYS PRO ALA MET ASP GLU ARG PHE HIS MET ALA PRO GLY
SEQRES 24 F 444 VAL GLN ALA GLY ARG ASN ILE SER SER GLN ASP ALA LYS
SEQRES 25 F 444 LYS GLU ILE ASN GLY THR ASP SER GLY ASN SER HIS ARG
SEQRES 26 F 444 ALA GLY GLN PRO ILE GLU ALA VAL SER SER TYR LEU ARG
SEQRES 27 F 444 TYR GLN ALA GLN LYS PHE ALA ALA SER PHE ASP ALA ASN
SEQRES 28 F 444 CYS TYR ILE ALA MET THR LEU LYS PHE ASP THR HIS ASP
SEQRES 29 F 444 ILE SER ARG GLY ARG ALA GLY SER ILE PRO GLU ALA LEU
SEQRES 30 F 444 ALA MET ILE THR GLN PRO ALA LEU ILE ILE CYS ALA ARG
SEQRES 31 F 444 SER ASP GLY LEU TYR SER PHE ASP GLU HIS VAL GLU MET
SEQRES 32 F 444 GLY ARG SER ILE PRO ASN SER ARG LEU CYS VAL VAL ASP
SEQRES 33 F 444 THR ASN GLU GLY HIS ASP PHE PHE VAL MET GLU ALA ASP
SEQRES 34 F 444 LYS VAL ASN ASP ALA VAL ARG GLY PHE LEU ASP GLN SER
SEQRES 35 F 444 LEU MET
SEQRES 1 G 444 MET LEU PRO SER ALA GLN VAL ALA ARG LEU LYS PRO ASP
SEQRES 2 G 444 PRO PHE PRO PRO SER LEU SER PRO ILE PRO HIS GLY ALA
SEQRES 3 G 444 VAL THR PHE ALA ALA LEU ALA PRO CYS HIS ASN LEU PRO
SEQRES 4 G 444 ILE PHE SER SER ARG GLN MET LEU ARG ASP SER LEU THR
SEQRES 5 G 444 TYR SER HIS THR SER PRO THR MET SER PRO GLN ILE ALA
SEQRES 6 G 444 ASN ARG PHE GLU ALA SER LEU ASP ALA GLN ASP ILE ALA
SEQRES 7 G 444 ARG ILE SER LEU PHE THR LEU GLU SER GLY VAL ILE LEU
SEQRES 8 G 444 ARG ASP VAL PRO VAL ALA TYR LYS SER TRP GLY ARG MET
SEQRES 9 G 444 ASN VAL SER ARG ASP ASN CYS VAL ILE VAL CYS HIS THR
SEQRES 10 G 444 LEU THR SER SER ALA HIS VAL THR SER TRP TRP PRO THR
SEQRES 11 G 444 LEU PHE GLY GLN GLY ARG ALA PHE ASP THR SER ARG TYR
SEQRES 12 G 444 PHE ILE ILE CYS LEU ASN TYR LEU GLY SER PRO PHE GLY
SEQRES 13 G 444 SER ALA GLY PRO CYS SER PRO ASP PRO ASP ALA GLU GLY
SEQRES 14 G 444 GLN ARG PRO TYR GLY ALA LYS PHE PRO ARG THR THR ILE
SEQRES 15 G 444 ARG ASP ASP VAL ARG ILE HIS ARG GLN VAL LEU ASP ARG
SEQRES 16 G 444 LEU GLY VAL ARG GLN ILE ALA ALA VAL VAL GLY ALA SER
SEQRES 17 G 444 MET GLY GLY MET HIS THR LEU GLU TRP ALA PHE PHE GLY
SEQRES 18 G 444 PRO GLU TYR VAL ARG LYS ILE VAL PRO ILE ALA THR SER
SEQRES 19 G 444 CYS ARG GLN SER GLY TRP CYS ALA ALA TRP PHE GLU THR
SEQRES 20 G 444 GLN ARG GLN CYS ILE TYR ASP ASP PRO LYS TYR LEU ASP
SEQRES 21 G 444 GLY GLU TYR ASP VAL ASP ASP GLN PRO VAL ARG GLY LEU
SEQRES 22 G 444 GLU THR ALA ARG LYS ILE ALA ASN LEU THR TYR LYS SER
SEQRES 23 G 444 LYS PRO ALA MET ASP GLU ARG PHE HIS MET ALA PRO GLY
SEQRES 24 G 444 VAL GLN ALA GLY ARG ASN ILE SER SER GLN ASP ALA LYS
SEQRES 25 G 444 LYS GLU ILE ASN GLY THR ASP SER GLY ASN SER HIS ARG
SEQRES 26 G 444 ALA GLY GLN PRO ILE GLU ALA VAL SER SER TYR LEU ARG
SEQRES 27 G 444 TYR GLN ALA GLN LYS PHE ALA ALA SER PHE ASP ALA ASN
SEQRES 28 G 444 CYS TYR ILE ALA MET THR LEU LYS PHE ASP THR HIS ASP
SEQRES 29 G 444 ILE SER ARG GLY ARG ALA GLY SER ILE PRO GLU ALA LEU
SEQRES 30 G 444 ALA MET ILE THR GLN PRO ALA LEU ILE ILE CYS ALA ARG
SEQRES 31 G 444 SER ASP GLY LEU TYR SER PHE ASP GLU HIS VAL GLU MET
SEQRES 32 G 444 GLY ARG SER ILE PRO ASN SER ARG LEU CYS VAL VAL ASP
SEQRES 33 G 444 THR ASN GLU GLY HIS ASP PHE PHE VAL MET GLU ALA ASP
SEQRES 34 G 444 LYS VAL ASN ASP ALA VAL ARG GLY PHE LEU ASP GLN SER
SEQRES 35 G 444 LEU MET
SEQRES 1 H 444 MET LEU PRO SER ALA GLN VAL ALA ARG LEU LYS PRO ASP
SEQRES 2 H 444 PRO PHE PRO PRO SER LEU SER PRO ILE PRO HIS GLY ALA
SEQRES 3 H 444 VAL THR PHE ALA ALA LEU ALA PRO CYS HIS ASN LEU PRO
SEQRES 4 H 444 ILE PHE SER SER ARG GLN MET LEU ARG ASP SER LEU THR
SEQRES 5 H 444 TYR SER HIS THR SER PRO THR MET SER PRO GLN ILE ALA
SEQRES 6 H 444 ASN ARG PHE GLU ALA SER LEU ASP ALA GLN ASP ILE ALA
SEQRES 7 H 444 ARG ILE SER LEU PHE THR LEU GLU SER GLY VAL ILE LEU
SEQRES 8 H 444 ARG ASP VAL PRO VAL ALA TYR LYS SER TRP GLY ARG MET
SEQRES 9 H 444 ASN VAL SER ARG ASP ASN CYS VAL ILE VAL CYS HIS THR
SEQRES 10 H 444 LEU THR SER SER ALA HIS VAL THR SER TRP TRP PRO THR
SEQRES 11 H 444 LEU PHE GLY GLN GLY ARG ALA PHE ASP THR SER ARG TYR
SEQRES 12 H 444 PHE ILE ILE CYS LEU ASN TYR LEU GLY SER PRO PHE GLY
SEQRES 13 H 444 SER ALA GLY PRO CYS SER PRO ASP PRO ASP ALA GLU GLY
SEQRES 14 H 444 GLN ARG PRO TYR GLY ALA LYS PHE PRO ARG THR THR ILE
SEQRES 15 H 444 ARG ASP ASP VAL ARG ILE HIS ARG GLN VAL LEU ASP ARG
SEQRES 16 H 444 LEU GLY VAL ARG GLN ILE ALA ALA VAL VAL GLY ALA SER
SEQRES 17 H 444 MET GLY GLY MET HIS THR LEU GLU TRP ALA PHE PHE GLY
SEQRES 18 H 444 PRO GLU TYR VAL ARG LYS ILE VAL PRO ILE ALA THR SER
SEQRES 19 H 444 CYS ARG GLN SER GLY TRP CYS ALA ALA TRP PHE GLU THR
SEQRES 20 H 444 GLN ARG GLN CYS ILE TYR ASP ASP PRO LYS TYR LEU ASP
SEQRES 21 H 444 GLY GLU TYR ASP VAL ASP ASP GLN PRO VAL ARG GLY LEU
SEQRES 22 H 444 GLU THR ALA ARG LYS ILE ALA ASN LEU THR TYR LYS SER
SEQRES 23 H 444 LYS PRO ALA MET ASP GLU ARG PHE HIS MET ALA PRO GLY
SEQRES 24 H 444 VAL GLN ALA GLY ARG ASN ILE SER SER GLN ASP ALA LYS
SEQRES 25 H 444 LYS GLU ILE ASN GLY THR ASP SER GLY ASN SER HIS ARG
SEQRES 26 H 444 ALA GLY GLN PRO ILE GLU ALA VAL SER SER TYR LEU ARG
SEQRES 27 H 444 TYR GLN ALA GLN LYS PHE ALA ALA SER PHE ASP ALA ASN
SEQRES 28 H 444 CYS TYR ILE ALA MET THR LEU LYS PHE ASP THR HIS ASP
SEQRES 29 H 444 ILE SER ARG GLY ARG ALA GLY SER ILE PRO GLU ALA LEU
SEQRES 30 H 444 ALA MET ILE THR GLN PRO ALA LEU ILE ILE CYS ALA ARG
SEQRES 31 H 444 SER ASP GLY LEU TYR SER PHE ASP GLU HIS VAL GLU MET
SEQRES 32 H 444 GLY ARG SER ILE PRO ASN SER ARG LEU CYS VAL VAL ASP
SEQRES 33 H 444 THR ASN GLU GLY HIS ASP PHE PHE VAL MET GLU ALA ASP
SEQRES 34 H 444 LYS VAL ASN ASP ALA VAL ARG GLY PHE LEU ASP GLN SER
SEQRES 35 H 444 LEU MET
SEQRES 1 I 444 MET LEU PRO SER ALA GLN VAL ALA ARG LEU LYS PRO ASP
SEQRES 2 I 444 PRO PHE PRO PRO SER LEU SER PRO ILE PRO HIS GLY ALA
SEQRES 3 I 444 VAL THR PHE ALA ALA LEU ALA PRO CYS HIS ASN LEU PRO
SEQRES 4 I 444 ILE PHE SER SER ARG GLN MET LEU ARG ASP SER LEU THR
SEQRES 5 I 444 TYR SER HIS THR SER PRO THR MET SER PRO GLN ILE ALA
SEQRES 6 I 444 ASN ARG PHE GLU ALA SER LEU ASP ALA GLN ASP ILE ALA
SEQRES 7 I 444 ARG ILE SER LEU PHE THR LEU GLU SER GLY VAL ILE LEU
SEQRES 8 I 444 ARG ASP VAL PRO VAL ALA TYR LYS SER TRP GLY ARG MET
SEQRES 9 I 444 ASN VAL SER ARG ASP ASN CYS VAL ILE VAL CYS HIS THR
SEQRES 10 I 444 LEU THR SER SER ALA HIS VAL THR SER TRP TRP PRO THR
SEQRES 11 I 444 LEU PHE GLY GLN GLY ARG ALA PHE ASP THR SER ARG TYR
SEQRES 12 I 444 PHE ILE ILE CYS LEU ASN TYR LEU GLY SER PRO PHE GLY
SEQRES 13 I 444 SER ALA GLY PRO CYS SER PRO ASP PRO ASP ALA GLU GLY
SEQRES 14 I 444 GLN ARG PRO TYR GLY ALA LYS PHE PRO ARG THR THR ILE
SEQRES 15 I 444 ARG ASP ASP VAL ARG ILE HIS ARG GLN VAL LEU ASP ARG
SEQRES 16 I 444 LEU GLY VAL ARG GLN ILE ALA ALA VAL VAL GLY ALA SER
SEQRES 17 I 444 MET GLY GLY MET HIS THR LEU GLU TRP ALA PHE PHE GLY
SEQRES 18 I 444 PRO GLU TYR VAL ARG LYS ILE VAL PRO ILE ALA THR SER
SEQRES 19 I 444 CYS ARG GLN SER GLY TRP CYS ALA ALA TRP PHE GLU THR
SEQRES 20 I 444 GLN ARG GLN CYS ILE TYR ASP ASP PRO LYS TYR LEU ASP
SEQRES 21 I 444 GLY GLU TYR ASP VAL ASP ASP GLN PRO VAL ARG GLY LEU
SEQRES 22 I 444 GLU THR ALA ARG LYS ILE ALA ASN LEU THR TYR LYS SER
SEQRES 23 I 444 LYS PRO ALA MET ASP GLU ARG PHE HIS MET ALA PRO GLY
SEQRES 24 I 444 VAL GLN ALA GLY ARG ASN ILE SER SER GLN ASP ALA LYS
SEQRES 25 I 444 LYS GLU ILE ASN GLY THR ASP SER GLY ASN SER HIS ARG
SEQRES 26 I 444 ALA GLY GLN PRO ILE GLU ALA VAL SER SER TYR LEU ARG
SEQRES 27 I 444 TYR GLN ALA GLN LYS PHE ALA ALA SER PHE ASP ALA ASN
SEQRES 28 I 444 CYS TYR ILE ALA MET THR LEU LYS PHE ASP THR HIS ASP
SEQRES 29 I 444 ILE SER ARG GLY ARG ALA GLY SER ILE PRO GLU ALA LEU
SEQRES 30 I 444 ALA MET ILE THR GLN PRO ALA LEU ILE ILE CYS ALA ARG
SEQRES 31 I 444 SER ASP GLY LEU TYR SER PHE ASP GLU HIS VAL GLU MET
SEQRES 32 I 444 GLY ARG SER ILE PRO ASN SER ARG LEU CYS VAL VAL ASP
SEQRES 33 I 444 THR ASN GLU GLY HIS ASP PHE PHE VAL MET GLU ALA ASP
SEQRES 34 I 444 LYS VAL ASN ASP ALA VAL ARG GLY PHE LEU ASP GLN SER
SEQRES 35 I 444 LEU MET
SEQRES 1 J 444 MET LEU PRO SER ALA GLN VAL ALA ARG LEU LYS PRO ASP
SEQRES 2 J 444 PRO PHE PRO PRO SER LEU SER PRO ILE PRO HIS GLY ALA
SEQRES 3 J 444 VAL THR PHE ALA ALA LEU ALA PRO CYS HIS ASN LEU PRO
SEQRES 4 J 444 ILE PHE SER SER ARG GLN MET LEU ARG ASP SER LEU THR
SEQRES 5 J 444 TYR SER HIS THR SER PRO THR MET SER PRO GLN ILE ALA
SEQRES 6 J 444 ASN ARG PHE GLU ALA SER LEU ASP ALA GLN ASP ILE ALA
SEQRES 7 J 444 ARG ILE SER LEU PHE THR LEU GLU SER GLY VAL ILE LEU
SEQRES 8 J 444 ARG ASP VAL PRO VAL ALA TYR LYS SER TRP GLY ARG MET
SEQRES 9 J 444 ASN VAL SER ARG ASP ASN CYS VAL ILE VAL CYS HIS THR
SEQRES 10 J 444 LEU THR SER SER ALA HIS VAL THR SER TRP TRP PRO THR
SEQRES 11 J 444 LEU PHE GLY GLN GLY ARG ALA PHE ASP THR SER ARG TYR
SEQRES 12 J 444 PHE ILE ILE CYS LEU ASN TYR LEU GLY SER PRO PHE GLY
SEQRES 13 J 444 SER ALA GLY PRO CYS SER PRO ASP PRO ASP ALA GLU GLY
SEQRES 14 J 444 GLN ARG PRO TYR GLY ALA LYS PHE PRO ARG THR THR ILE
SEQRES 15 J 444 ARG ASP ASP VAL ARG ILE HIS ARG GLN VAL LEU ASP ARG
SEQRES 16 J 444 LEU GLY VAL ARG GLN ILE ALA ALA VAL VAL GLY ALA SER
SEQRES 17 J 444 MET GLY GLY MET HIS THR LEU GLU TRP ALA PHE PHE GLY
SEQRES 18 J 444 PRO GLU TYR VAL ARG LYS ILE VAL PRO ILE ALA THR SER
SEQRES 19 J 444 CYS ARG GLN SER GLY TRP CYS ALA ALA TRP PHE GLU THR
SEQRES 20 J 444 GLN ARG GLN CYS ILE TYR ASP ASP PRO LYS TYR LEU ASP
SEQRES 21 J 444 GLY GLU TYR ASP VAL ASP ASP GLN PRO VAL ARG GLY LEU
SEQRES 22 J 444 GLU THR ALA ARG LYS ILE ALA ASN LEU THR TYR LYS SER
SEQRES 23 J 444 LYS PRO ALA MET ASP GLU ARG PHE HIS MET ALA PRO GLY
SEQRES 24 J 444 VAL GLN ALA GLY ARG ASN ILE SER SER GLN ASP ALA LYS
SEQRES 25 J 444 LYS GLU ILE ASN GLY THR ASP SER GLY ASN SER HIS ARG
SEQRES 26 J 444 ALA GLY GLN PRO ILE GLU ALA VAL SER SER TYR LEU ARG
SEQRES 27 J 444 TYR GLN ALA GLN LYS PHE ALA ALA SER PHE ASP ALA ASN
SEQRES 28 J 444 CYS TYR ILE ALA MET THR LEU LYS PHE ASP THR HIS ASP
SEQRES 29 J 444 ILE SER ARG GLY ARG ALA GLY SER ILE PRO GLU ALA LEU
SEQRES 30 J 444 ALA MET ILE THR GLN PRO ALA LEU ILE ILE CYS ALA ARG
SEQRES 31 J 444 SER ASP GLY LEU TYR SER PHE ASP GLU HIS VAL GLU MET
SEQRES 32 J 444 GLY ARG SER ILE PRO ASN SER ARG LEU CYS VAL VAL ASP
SEQRES 33 J 444 THR ASN GLU GLY HIS ASP PHE PHE VAL MET GLU ALA ASP
SEQRES 34 J 444 LYS VAL ASN ASP ALA VAL ARG GLY PHE LEU ASP GLN SER
SEQRES 35 J 444 LEU MET
SEQRES 1 K 444 MET LEU PRO SER ALA GLN VAL ALA ARG LEU LYS PRO ASP
SEQRES 2 K 444 PRO PHE PRO PRO SER LEU SER PRO ILE PRO HIS GLY ALA
SEQRES 3 K 444 VAL THR PHE ALA ALA LEU ALA PRO CYS HIS ASN LEU PRO
SEQRES 4 K 444 ILE PHE SER SER ARG GLN MET LEU ARG ASP SER LEU THR
SEQRES 5 K 444 TYR SER HIS THR SER PRO THR MET SER PRO GLN ILE ALA
SEQRES 6 K 444 ASN ARG PHE GLU ALA SER LEU ASP ALA GLN ASP ILE ALA
SEQRES 7 K 444 ARG ILE SER LEU PHE THR LEU GLU SER GLY VAL ILE LEU
SEQRES 8 K 444 ARG ASP VAL PRO VAL ALA TYR LYS SER TRP GLY ARG MET
SEQRES 9 K 444 ASN VAL SER ARG ASP ASN CYS VAL ILE VAL CYS HIS THR
SEQRES 10 K 444 LEU THR SER SER ALA HIS VAL THR SER TRP TRP PRO THR
SEQRES 11 K 444 LEU PHE GLY GLN GLY ARG ALA PHE ASP THR SER ARG TYR
SEQRES 12 K 444 PHE ILE ILE CYS LEU ASN TYR LEU GLY SER PRO PHE GLY
SEQRES 13 K 444 SER ALA GLY PRO CYS SER PRO ASP PRO ASP ALA GLU GLY
SEQRES 14 K 444 GLN ARG PRO TYR GLY ALA LYS PHE PRO ARG THR THR ILE
SEQRES 15 K 444 ARG ASP ASP VAL ARG ILE HIS ARG GLN VAL LEU ASP ARG
SEQRES 16 K 444 LEU GLY VAL ARG GLN ILE ALA ALA VAL VAL GLY ALA SER
SEQRES 17 K 444 MET GLY GLY MET HIS THR LEU GLU TRP ALA PHE PHE GLY
SEQRES 18 K 444 PRO GLU TYR VAL ARG LYS ILE VAL PRO ILE ALA THR SER
SEQRES 19 K 444 CYS ARG GLN SER GLY TRP CYS ALA ALA TRP PHE GLU THR
SEQRES 20 K 444 GLN ARG GLN CYS ILE TYR ASP ASP PRO LYS TYR LEU ASP
SEQRES 21 K 444 GLY GLU TYR ASP VAL ASP ASP GLN PRO VAL ARG GLY LEU
SEQRES 22 K 444 GLU THR ALA ARG LYS ILE ALA ASN LEU THR TYR LYS SER
SEQRES 23 K 444 LYS PRO ALA MET ASP GLU ARG PHE HIS MET ALA PRO GLY
SEQRES 24 K 444 VAL GLN ALA GLY ARG ASN ILE SER SER GLN ASP ALA LYS
SEQRES 25 K 444 LYS GLU ILE ASN GLY THR ASP SER GLY ASN SER HIS ARG
SEQRES 26 K 444 ALA GLY GLN PRO ILE GLU ALA VAL SER SER TYR LEU ARG
SEQRES 27 K 444 TYR GLN ALA GLN LYS PHE ALA ALA SER PHE ASP ALA ASN
SEQRES 28 K 444 CYS TYR ILE ALA MET THR LEU LYS PHE ASP THR HIS ASP
SEQRES 29 K 444 ILE SER ARG GLY ARG ALA GLY SER ILE PRO GLU ALA LEU
SEQRES 30 K 444 ALA MET ILE THR GLN PRO ALA LEU ILE ILE CYS ALA ARG
SEQRES 31 K 444 SER ASP GLY LEU TYR SER PHE ASP GLU HIS VAL GLU MET
SEQRES 32 K 444 GLY ARG SER ILE PRO ASN SER ARG LEU CYS VAL VAL ASP
SEQRES 33 K 444 THR ASN GLU GLY HIS ASP PHE PHE VAL MET GLU ALA ASP
SEQRES 34 K 444 LYS VAL ASN ASP ALA VAL ARG GLY PHE LEU ASP GLN SER
SEQRES 35 K 444 LEU MET
SEQRES 1 L 444 MET LEU PRO SER ALA GLN VAL ALA ARG LEU LYS PRO ASP
SEQRES 2 L 444 PRO PHE PRO PRO SER LEU SER PRO ILE PRO HIS GLY ALA
SEQRES 3 L 444 VAL THR PHE ALA ALA LEU ALA PRO CYS HIS ASN LEU PRO
SEQRES 4 L 444 ILE PHE SER SER ARG GLN MET LEU ARG ASP SER LEU THR
SEQRES 5 L 444 TYR SER HIS THR SER PRO THR MET SER PRO GLN ILE ALA
SEQRES 6 L 444 ASN ARG PHE GLU ALA SER LEU ASP ALA GLN ASP ILE ALA
SEQRES 7 L 444 ARG ILE SER LEU PHE THR LEU GLU SER GLY VAL ILE LEU
SEQRES 8 L 444 ARG ASP VAL PRO VAL ALA TYR LYS SER TRP GLY ARG MET
SEQRES 9 L 444 ASN VAL SER ARG ASP ASN CYS VAL ILE VAL CYS HIS THR
SEQRES 10 L 444 LEU THR SER SER ALA HIS VAL THR SER TRP TRP PRO THR
SEQRES 11 L 444 LEU PHE GLY GLN GLY ARG ALA PHE ASP THR SER ARG TYR
SEQRES 12 L 444 PHE ILE ILE CYS LEU ASN TYR LEU GLY SER PRO PHE GLY
SEQRES 13 L 444 SER ALA GLY PRO CYS SER PRO ASP PRO ASP ALA GLU GLY
SEQRES 14 L 444 GLN ARG PRO TYR GLY ALA LYS PHE PRO ARG THR THR ILE
SEQRES 15 L 444 ARG ASP ASP VAL ARG ILE HIS ARG GLN VAL LEU ASP ARG
SEQRES 16 L 444 LEU GLY VAL ARG GLN ILE ALA ALA VAL VAL GLY ALA SER
SEQRES 17 L 444 MET GLY GLY MET HIS THR LEU GLU TRP ALA PHE PHE GLY
SEQRES 18 L 444 PRO GLU TYR VAL ARG LYS ILE VAL PRO ILE ALA THR SER
SEQRES 19 L 444 CYS ARG GLN SER GLY TRP CYS ALA ALA TRP PHE GLU THR
SEQRES 20 L 444 GLN ARG GLN CYS ILE TYR ASP ASP PRO LYS TYR LEU ASP
SEQRES 21 L 444 GLY GLU TYR ASP VAL ASP ASP GLN PRO VAL ARG GLY LEU
SEQRES 22 L 444 GLU THR ALA ARG LYS ILE ALA ASN LEU THR TYR LYS SER
SEQRES 23 L 444 LYS PRO ALA MET ASP GLU ARG PHE HIS MET ALA PRO GLY
SEQRES 24 L 444 VAL GLN ALA GLY ARG ASN ILE SER SER GLN ASP ALA LYS
SEQRES 25 L 444 LYS GLU ILE ASN GLY THR ASP SER GLY ASN SER HIS ARG
SEQRES 26 L 444 ALA GLY GLN PRO ILE GLU ALA VAL SER SER TYR LEU ARG
SEQRES 27 L 444 TYR GLN ALA GLN LYS PHE ALA ALA SER PHE ASP ALA ASN
SEQRES 28 L 444 CYS TYR ILE ALA MET THR LEU LYS PHE ASP THR HIS ASP
SEQRES 29 L 444 ILE SER ARG GLY ARG ALA GLY SER ILE PRO GLU ALA LEU
SEQRES 30 L 444 ALA MET ILE THR GLN PRO ALA LEU ILE ILE CYS ALA ARG
SEQRES 31 L 444 SER ASP GLY LEU TYR SER PHE ASP GLU HIS VAL GLU MET
SEQRES 32 L 444 GLY ARG SER ILE PRO ASN SER ARG LEU CYS VAL VAL ASP
SEQRES 33 L 444 THR ASN GLU GLY HIS ASP PHE PHE VAL MET GLU ALA ASP
SEQRES 34 L 444 LYS VAL ASN ASP ALA VAL ARG GLY PHE LEU ASP GLN SER
SEQRES 35 L 444 LEU MET
HET COA A1383 48
HET COA B1383 48
HET COA C1383 48
HET COA D1383 48
HET COA E1383 48
HET COA F1383 48
HET COA G1383 48
HET COA H1383 48
HET COA I1383 48
HET COA J1385 48
HET COA K1385 48
HET COA L1383 48
HET GOL B1384 6
HET GOL I1384 6
HET ACT A1384 4
HET ACT B1385 4
HET ACT E1384 4
HET ACT I1385 4
HET ACT H1384 4
HET ACT G1384 4
HET ACT D1384 4
HET ACT C1384 4
HET ACT F1384 4
HET ACT J1386 4
HET ACT K1386 4
HET ACT L1384 4
HETNAM COA COENZYME A
HETNAM ACT ACETATE ION
HETNAM GOL GLYCEROL
FORMUL 13 COA 12(C21 H36 N7 O16 P3 S)
FORMUL 14 ACT 12(C2 H3 O2 1-)
FORMUL 15 GOL 2(C3 H8 O3)
FORMUL 16 HOH *1573(H2 O1)
HELIX 1 1 ASN A 7 SER A 12 1 6
HELIX 2 2 HIS A 64 TRP A 68 5 5
HELIX 3 3 TRP A 69 LEU A 72 5 4
HELIX 4 4 TYR A 114 PHE A 118 5 5
HELIX 5 5 THR A 122 GLY A 138 1 17
HELIX 6 6 SER A 149 ALA A 159 1 11
HELIX 7 7 PHE A 160 GLY A 162 5 3
HELIX 8 8 SER A 179 ASP A 196 1 18
HELIX 9 9 TYR A 199 GLU A 203 5 5
HELIX 10 10 PRO A 210 TYR A 225 1 16
HELIX 11 11 SER A 227 PHE A 235 1 9
HELIX 12 12 PRO A 270 GLU A 272 5 3
HELIX 13 13 ALA A 273 SER A 288 1 16
HELIX 14 14 ASP A 290 THR A 303 1 14
HELIX 15 15 SER A 313 ALA A 319 1 7
HELIX 16 16 SER A 337 ILE A 348 1 12
HELIX 17 17 GLU A 360 HIS A 362 5 3
HELIX 18 18 ASP A 363 GLU A 368 1 6
HELIX 19 19 GLU A 368 ASP A 381 1 14
HELIX 20 20 ASN B 7 SER B 12 1 6
HELIX 21 21 HIS B 64 TRP B 68 5 5
HELIX 22 22 TRP B 69 LEU B 72 5 4
HELIX 23 23 TYR B 114 PHE B 118 5 5
HELIX 24 24 THR B 122 GLY B 138 1 17
HELIX 25 25 SER B 149 ALA B 159 1 11
HELIX 26 26 PHE B 160 GLY B 162 5 3
HELIX 27 27 SER B 179 ASP B 195 1 17
HELIX 28 28 TYR B 199 GLU B 203 5 5
HELIX 29 29 PRO B 210 TYR B 225 1 16
HELIX 30 30 SER B 227 PHE B 235 1 9
HELIX 31 31 PRO B 270 GLU B 272 5 3
HELIX 32 32 ALA B 273 SER B 288 1 16
HELIX 33 33 ASP B 290 LYS B 300 1 11
HELIX 34 34 PHE B 301 HIS B 304 5 4
HELIX 35 35 SER B 313 MET B 320 1 8
HELIX 36 36 SER B 337 ILE B 348 1 12
HELIX 37 37 GLU B 360 HIS B 362 5 3
HELIX 38 38 ASP B 363 GLU B 368 1 6
HELIX 39 39 GLU B 368 ASP B 381 1 14
HELIX 40 40 ASN C 7 SER C 12 1 6
HELIX 41 41 HIS C 64 TRP C 68 5 5
HELIX 42 42 TRP C 69 LEU C 72 5 4
HELIX 43 43 ASP C 105 GLU C 109 5 5
HELIX 44 44 TYR C 114 PHE C 118 5 5
HELIX 45 45 THR C 122 GLY C 138 1 17
HELIX 46 46 SER C 149 ALA C 159 1 11
HELIX 47 47 PHE C 160 GLY C 162 5 3
HELIX 48 48 SER C 179 ASP C 196 1 18
HELIX 49 49 TYR C 199 GLU C 203 5 5
HELIX 50 50 PRO C 210 TYR C 225 1 16
HELIX 51 51 SER C 227 PHE C 235 1 9
HELIX 52 52 PRO C 270 GLU C 272 5 3
HELIX 53 53 ALA C 273 SER C 288 1 16
HELIX 54 54 ASP C 290 THR C 303 1 14
HELIX 55 55 SER C 313 MET C 320 1 8
HELIX 56 56 SER C 337 ILE C 348 1 12
HELIX 57 57 ASP C 363 GLU C 368 1 6
HELIX 58 58 GLU C 368 GLN C 382 1 15
HELIX 59 59 ASN D 7 SER D 12 1 6
HELIX 60 60 HIS D 64 TRP D 68 5 5
HELIX 61 61 TRP D 69 LEU D 72 5 4
HELIX 62 62 ASP D 105 GLU D 109 5 5
HELIX 63 63 TYR D 114 PHE D 118 5 5
HELIX 64 64 THR D 122 GLY D 138 1 17
HELIX 65 65 SER D 149 ALA D 159 1 11
HELIX 66 66 PHE D 160 GLY D 162 5 3
HELIX 67 67 SER D 179 ASP D 196 1 18
HELIX 68 68 TYR D 199 GLU D 203 5 5
HELIX 69 69 PRO D 210 TYR D 225 1 16
HELIX 70 70 SER D 227 PHE D 235 1 9
HELIX 71 71 PRO D 270 GLU D 272 5 3
HELIX 72 72 ALA D 273 ALA D 287 1 15
HELIX 73 73 ASP D 290 THR D 303 1 14
HELIX 74 74 SER D 313 MET D 320 1 8
HELIX 75 75 SER D 337 ILE D 348 1 12
HELIX 76 76 GLU D 360 HIS D 362 5 3
HELIX 77 77 ASP D 363 GLU D 368 1 6
HELIX 78 78 GLU D 368 ASP D 381 1 14
HELIX 79 79 ASN E 7 SER E 12 1 6
HELIX 80 80 HIS E 64 TRP E 68 5 5
HELIX 81 81 TRP E 69 LEU E 72 5 4
HELIX 82 82 TYR E 114 PHE E 118 5 5
HELIX 83 83 THR E 122 GLY E 138 1 17
HELIX 84 84 SER E 149 ALA E 159 1 11
HELIX 85 85 PHE E 160 GLY E 162 5 3
HELIX 86 86 SER E 179 ASP E 195 1 17
HELIX 87 87 TYR E 199 GLU E 203 5 5
HELIX 88 88 PRO E 210 TYR E 225 1 16
HELIX 89 89 SER E 227 PHE E 235 1 9
HELIX 90 90 PRO E 270 GLU E 272 5 3
HELIX 91 91 ALA E 273 SER E 288 1 16
HELIX 92 92 ASP E 290 THR E 303 1 14
HELIX 93 93 SER E 313 ALA E 319 1 7
HELIX 94 94 SER E 337 ILE E 348 1 12
HELIX 95 95 GLU E 360 HIS E 362 5 3
HELIX 96 96 ASP E 363 GLU E 368 1 6
HELIX 97 97 GLU E 368 ASP E 381 1 14
HELIX 98 98 ASN F 7 SER F 12 1 6
HELIX 99 99 HIS F 64 TRP F 68 5 5
HELIX 100 100 TRP F 69 LEU F 72 5 4
HELIX 101 101 TYR F 114 PHE F 118 5 5
HELIX 102 102 THR F 122 GLY F 138 1 17
HELIX 103 103 SER F 149 ALA F 159 1 11
HELIX 104 104 PHE F 160 GLY F 162 5 3
HELIX 105 105 SER F 179 ASP F 195 1 17
HELIX 106 106 TYR F 199 GLU F 203 5 5
HELIX 107 107 PRO F 210 TYR F 225 1 16
HELIX 108 108 SER F 227 PHE F 235 1 9
HELIX 109 109 PRO F 270 GLU F 272 5 3
HELIX 110 110 ALA F 273 SER F 288 1 16
HELIX 111 111 ASP F 290 ASP F 302 1 13
HELIX 112 112 SER F 313 MET F 320 1 8
HELIX 113 113 SER F 337 ILE F 348 1 12
HELIX 114 114 ASP F 363 GLU F 368 1 6
HELIX 115 115 GLU F 368 GLN F 382 1 15
HELIX 116 116 ASN G 7 SER G 12 1 6
HELIX 117 117 HIS G 64 TRP G 68 5 5
HELIX 118 118 TRP G 69 LEU G 72 5 4
HELIX 119 119 TYR G 114 PHE G 118 5 5
HELIX 120 120 THR G 122 LEU G 137 1 16
HELIX 121 121 SER G 149 ALA G 159 1 11
HELIX 122 122 PHE G 160 GLY G 162 5 3
HELIX 123 123 SER G 179 ASP G 196 1 18
HELIX 124 124 TYR G 199 GLU G 203 5 5
HELIX 125 125 PRO G 210 TYR G 225 1 16
HELIX 126 126 SER G 227 PHE G 235 1 9
HELIX 127 127 PRO G 270 GLU G 272 5 3
HELIX 128 128 ALA G 273 ALA G 287 1 15
HELIX 129 129 ASP G 290 LYS G 300 1 11
HELIX 130 130 PHE G 301 HIS G 304 5 4
HELIX 131 131 SER G 313 MET G 320 1 8
HELIX 132 132 SER G 337 ILE G 348 1 12
HELIX 133 133 ASP G 363 GLU G 368 1 6
HELIX 134 134 GLU G 368 GLN G 382 1 15
HELIX 135 135 ASN H 7 SER H 12 1 6
HELIX 136 136 HIS H 64 TRP H 68 5 5
HELIX 137 137 TRP H 69 LEU H 72 5 4
HELIX 138 138 TYR H 114 PHE H 118 5 5
HELIX 139 139 THR H 122 LEU H 137 1 16
HELIX 140 140 SER H 149 ALA H 159 1 11
HELIX 141 141 PHE H 160 GLY H 162 5 3
HELIX 142 142 SER H 179 ASP H 195 1 17
HELIX 143 143 TYR H 199 GLU H 203 5 5
HELIX 144 144 PRO H 210 TYR H 225 1 16
HELIX 145 145 SER H 227 PHE H 235 1 9
HELIX 146 146 PRO H 270 GLU H 272 5 3
HELIX 147 147 ALA H 273 SER H 288 1 16
HELIX 148 148 ASP H 290 LYS H 300 1 11
HELIX 149 149 PHE H 301 HIS H 304 5 4
HELIX 150 150 SER H 313 MET H 320 1 8
HELIX 151 151 SER H 337 ILE H 348 1 12
HELIX 152 152 ASP H 363 GLU H 368 1 6
HELIX 153 153 GLU H 368 GLN H 382 1 15
HELIX 154 154 ASN I 7 SER I 12 1 6
HELIX 155 155 HIS I 64 TRP I 68 5 5
HELIX 156 156 TRP I 69 LEU I 72 5 4
HELIX 157 157 TYR I 114 PHE I 118 5 5
HELIX 158 158 THR I 122 GLY I 138 1 17
HELIX 159 159 SER I 149 ALA I 159 1 11
HELIX 160 160 PHE I 160 GLY I 162 5 3
HELIX 161 161 SER I 179 ASP I 195 1 17
HELIX 162 162 TYR I 199 GLU I 203 5 5
HELIX 163 163 PRO I 210 TYR I 225 1 16
HELIX 164 164 SER I 227 PHE I 235 1 9
HELIX 165 165 PRO I 270 GLU I 272 5 3
HELIX 166 166 ALA I 273 SER I 288 1 16
HELIX 167 167 ASP I 290 LYS I 300 1 11
HELIX 168 168 PHE I 301 HIS I 304 5 4
HELIX 169 169 SER I 313 ALA I 319 1 7
HELIX 170 170 SER I 337 ILE I 348 1 12
HELIX 171 171 GLU I 360 HIS I 362 5 3
HELIX 172 172 ASP I 363 GLU I 368 1 6
HELIX 173 173 GLU I 368 ASP I 381 1 14
HELIX 174 174 ASN J 7 SER J 12 1 6
HELIX 175 175 HIS J 64 TRP J 68 5 5
HELIX 176 176 TRP J 69 LEU J 72 5 4
HELIX 177 177 TYR J 114 PHE J 118 5 5
HELIX 178 178 THR J 122 LEU J 137 1 16
HELIX 179 179 SER J 149 ALA J 159 1 11
HELIX 180 180 PHE J 160 GLY J 162 5 3
HELIX 181 181 SER J 179 ASP J 196 1 18
HELIX 182 182 PRO J 197 GLU J 203 5 7
HELIX 183 183 PRO J 210 TYR J 225 1 16
HELIX 184 184 SER J 227 PHE J 235 1 9
HELIX 185 185 ALA J 273 ALA J 287 1 15
HELIX 186 186 ASP J 290 ASP J 302 1 13
HELIX 187 187 SER J 313 MET J 320 1 8
HELIX 188 188 SER J 337 ILE J 348 1 12
HELIX 189 189 ASP J 363 GLU J 368 1 6
HELIX 190 190 GLU J 368 GLN J 382 1 15
HELIX 191 191 ASN K 7 SER K 12 1 6
HELIX 192 192 HIS K 64 TRP K 68 5 5
HELIX 193 193 TRP K 69 LEU K 72 5 4
HELIX 194 194 TYR K 114 PHE K 118 5 5
HELIX 195 195 THR K 122 LEU K 137 1 16
HELIX 196 196 SER K 149 ALA K 159 1 11
HELIX 197 197 PHE K 160 GLY K 162 5 3
HELIX 198 198 SER K 179 ASP K 196 1 18
HELIX 199 199 PRO K 197 GLU K 203 5 7
HELIX 200 200 PRO K 210 TYR K 225 1 16
HELIX 201 201 SER K 227 PHE K 235 1 9
HELIX 202 202 ALA K 273 ALA K 287 1 15
HELIX 203 203 ASP K 290 ASP K 302 1 13
HELIX 204 204 SER K 313 MET K 320 1 8
HELIX 205 205 SER K 337 ILE K 348 1 12
HELIX 206 206 ASP K 363 GLU K 368 1 6
HELIX 207 207 GLU K 368 ASP K 381 1 14
HELIX 208 208 ASN L 7 SER L 12 1 6
HELIX 209 209 HIS L 64 TRP L 68 5 5
HELIX 210 210 TRP L 69 LEU L 72 5 4
HELIX 211 211 TYR L 114 PHE L 118 5 5
HELIX 212 212 THR L 122 GLY L 138 1 17
HELIX 213 213 SER L 149 ALA L 159 1 11
HELIX 214 214 PHE L 160 GLY L 162 5 3
HELIX 215 215 SER L 179 ASP L 195 1 17
HELIX 216 216 ASP L 196 GLU L 203 5 8
HELIX 217 217 PRO L 210 TYR L 225 1 16
HELIX 218 218 SER L 227 PHE L 235 1 9
HELIX 219 219 PRO L 270 GLU L 272 5 3
HELIX 220 220 ALA L 273 SER L 288 1 16
HELIX 221 221 ASP L 290 ASP L 302 1 13
HELIX 222 222 SER L 313 ALA L 319 1 7
HELIX 223 223 SER L 337 ILE L 348 1 12
HELIX 224 224 ASP L 363 GLU L 368 1 6
HELIX 225 225 GLU L 368 GLN L 382 1 15
SHEET 1 AA 6 ASP A 17 THR A 25 0
SHEET 2 AA 6 ILE A 31 TRP A 42 -1 O LEU A 32 N PHE A 24
SHEET 3 AA 6 PHE A 85 LEU A 89 -1 O ILE A 86 N TRP A 42
SHEET 4 AA 6 CYS A 52 CYS A 56 1 O VAL A 53 N ILE A 87
SHEET 5 AA 6 ILE A 142 ALA A 148 1 N ALA A 143 O CYS A 52
SHEET 6 AA 6 ILE A 169 ILE A 172 1 O VAL A 170 N GLY A 147
SHEET 1 AB 3 ALA A 325 CYS A 329 0
SHEET 2 AB 3 SER A 351 VAL A 355 1 O ARG A 352 N ILE A 327
SHEET 3 AB 3 GLN K 382 SER K 383 1 O SER K 383 N VAL A 355
SHEET 1 BA 6 ASP B 17 THR B 25 0
SHEET 2 BA 6 ILE B 31 TRP B 42 -1 O LEU B 32 N PHE B 24
SHEET 3 BA 6 PHE B 85 LEU B 89 -1 O ILE B 86 N TRP B 42
SHEET 4 BA 6 CYS B 52 CYS B 56 1 O VAL B 53 N ILE B 87
SHEET 5 BA 6 ILE B 142 ALA B 148 1 N ALA B 143 O CYS B 52
SHEET 6 BA 6 ILE B 169 ILE B 172 1 O VAL B 170 N GLY B 147
SHEET 1 BB 2 ALA B 325 CYS B 329 0
SHEET 2 BB 2 SER B 351 VAL B 355 1 O ARG B 352 N ILE B 327
SHEET 1 CA 6 ASP C 17 THR C 25 0
SHEET 2 CA 6 ILE C 31 TRP C 42 -1 O LEU C 32 N PHE C 24
SHEET 3 CA 6 PHE C 85 LEU C 89 -1 O ILE C 86 N TRP C 42
SHEET 4 CA 6 CYS C 52 CYS C 56 1 O VAL C 53 N ILE C 87
SHEET 5 CA 6 ILE C 142 ALA C 148 1 N ALA C 143 O CYS C 52
SHEET 6 CA 6 ILE C 169 ILE C 172 1 O VAL C 170 N GLY C 147
SHEET 1 CB 2 ALA C 325 ALA C 330 0
SHEET 2 CB 2 SER C 351 VAL C 356 1 O ARG C 352 N ILE C 327
SHEET 1 DA 6 ASP D 17 THR D 25 0
SHEET 2 DA 6 ILE D 31 TRP D 42 -1 O LEU D 32 N PHE D 24
SHEET 3 DA 6 PHE D 85 LEU D 89 -1 O ILE D 86 N TRP D 42
SHEET 4 DA 6 CYS D 52 CYS D 56 1 O VAL D 53 N ILE D 87
SHEET 5 DA 6 ILE D 142 ALA D 148 1 N ALA D 143 O CYS D 52
SHEET 6 DA 6 ILE D 169 ILE D 172 1 O VAL D 170 N GLY D 147
SHEET 1 DB 2 ALA D 325 CYS D 329 0
SHEET 2 DB 2 SER D 351 VAL D 355 1 O ARG D 352 N ILE D 327
SHEET 1 EA 6 ASP E 17 THR E 25 0
SHEET 2 EA 6 ILE E 31 TRP E 42 -1 O LEU E 32 N PHE E 24
SHEET 3 EA 6 PHE E 85 LEU E 89 -1 O ILE E 86 N TRP E 42
SHEET 4 EA 6 CYS E 52 CYS E 56 1 O VAL E 53 N ILE E 87
SHEET 5 EA 6 ILE E 142 ALA E 148 1 N ALA E 143 O CYS E 52
SHEET 6 EA 6 ILE E 169 ILE E 172 1 O VAL E 170 N GLY E 147
SHEET 1 EB 2 ALA E 325 CYS E 329 0
SHEET 2 EB 2 SER E 351 VAL E 355 1 O ARG E 352 N ILE E 327
SHEET 1 FA 6 ASP F 17 THR F 25 0
SHEET 2 FA 6 ILE F 31 TRP F 42 -1 O LEU F 32 N PHE F 24
SHEET 3 FA 6 PHE F 85 LEU F 89 -1 O ILE F 86 N TRP F 42
SHEET 4 FA 6 CYS F 52 CYS F 56 1 O VAL F 53 N ILE F 87
SHEET 5 FA 6 ILE F 142 ALA F 148 1 N ALA F 143 O CYS F 52
SHEET 6 FA 6 ILE F 169 ILE F 172 1 O VAL F 170 N GLY F 147
SHEET 1 FB 2 ALA F 325 CYS F 329 0
SHEET 2 FB 2 SER F 351 VAL F 355 1 O ARG F 352 N ILE F 327
SHEET 1 GA 6 ASP G 17 THR G 25 0
SHEET 2 GA 6 ILE G 31 TRP G 42 -1 O LEU G 32 N PHE G 24
SHEET 3 GA 6 PHE G 85 LEU G 89 -1 O ILE G 86 N TRP G 42
SHEET 4 GA 6 CYS G 52 CYS G 56 1 O VAL G 53 N ILE G 87
SHEET 5 GA 6 ILE G 142 ALA G 148 1 N ALA G 143 O CYS G 52
SHEET 6 GA 6 ILE G 169 ILE G 172 1 O VAL G 170 N GLY G 147
SHEET 1 GB 2 ALA G 325 CYS G 329 0
SHEET 2 GB 2 SER G 351 VAL G 355 1 O ARG G 352 N ILE G 327
SHEET 1 HA 6 ASP H 17 THR H 25 0
SHEET 2 HA 6 ILE H 31 TRP H 42 -1 O LEU H 32 N PHE H 24
SHEET 3 HA 6 PHE H 85 LEU H 89 -1 O ILE H 86 N TRP H 42
SHEET 4 HA 6 CYS H 52 CYS H 56 1 O VAL H 53 N ILE H 87
SHEET 5 HA 6 ILE H 142 ALA H 148 1 N ALA H 143 O CYS H 52
SHEET 6 HA 6 ILE H 169 ILE H 172 1 O VAL H 170 N GLY H 147
SHEET 1 HB 2 ALA H 325 CYS H 329 0
SHEET 2 HB 2 SER H 351 VAL H 355 1 O ARG H 352 N ILE H 327
SHEET 1 IA 6 ASP I 17 THR I 25 0
SHEET 2 IA 6 ILE I 31 TRP I 42 -1 O LEU I 32 N PHE I 24
SHEET 3 IA 6 PHE I 85 LEU I 89 -1 O ILE I 86 N TRP I 42
SHEET 4 IA 6 CYS I 52 CYS I 56 1 O VAL I 53 N ILE I 87
SHEET 5 IA 6 ILE I 142 ALA I 148 1 N ALA I 143 O CYS I 52
SHEET 6 IA 6 ILE I 169 ILE I 172 1 O VAL I 170 N GLY I 147
SHEET 1 IB 2 ALA I 325 CYS I 329 0
SHEET 2 IB 2 SER I 351 VAL I 355 1 O ARG I 352 N ILE I 327
SHEET 1 JA 6 ASP J 17 THR J 25 0
SHEET 2 JA 6 ILE J 31 TRP J 42 -1 O LEU J 32 N PHE J 24
SHEET 3 JA 6 PHE J 85 LEU J 89 -1 O ILE J 86 N TRP J 42
SHEET 4 JA 6 CYS J 52 CYS J 56 1 O VAL J 53 N ILE J 87
SHEET 5 JA 6 ILE J 142 ALA J 148 1 N ALA J 143 O CYS J 52
SHEET 6 JA 6 ILE J 169 ILE J 172 1 O VAL J 170 N GLY J 147
SHEET 1 JB 2 ALA J 325 CYS J 329 0
SHEET 2 JB 2 SER J 351 VAL J 355 1 O ARG J 352 N ILE J 327
SHEET 1 KA 6 ASP K 17 THR K 25 0
SHEET 2 KA 6 ILE K 31 TRP K 42 -1 O LEU K 32 N PHE K 24
SHEET 3 KA 6 PHE K 85 LEU K 89 -1 O ILE K 86 N TRP K 42
SHEET 4 KA 6 CYS K 52 CYS K 56 1 O VAL K 53 N ILE K 87
SHEET 5 KA 6 ILE K 142 ALA K 148 1 N ALA K 143 O CYS K 52
SHEET 6 KA 6 ILE K 169 ILE K 172 1 O VAL K 170 N GLY K 147
SHEET 1 KB 2 ALA K 325 CYS K 329 0
SHEET 2 KB 2 SER K 351 VAL K 355 1 O ARG K 352 N ILE K 327
SHEET 1 LA 6 ASP L 17 THR L 25 0
SHEET 2 LA 6 ILE L 31 TRP L 42 -1 O LEU L 32 N PHE L 24
SHEET 3 LA 6 PHE L 85 LEU L 89 -1 O ILE L 86 N TRP L 42
SHEET 4 LA 6 CYS L 52 CYS L 56 1 O VAL L 53 N ILE L 87
SHEET 5 LA 6 ILE L 142 ALA L 148 1 N ALA L 143 O CYS L 52
SHEET 6 LA 6 ILE L 169 ILE L 172 1 O VAL L 170 N GLY L 147
SHEET 1 LB 2 ALA L 325 ALA L 330 0
SHEET 2 LB 2 SER L 351 VAL L 356 1 O ARG L 352 N ILE L 327
SITE 1 AC1 17 SER A 149 ARG A 218 TYR A 225 LYS A 226
SITE 2 AC1 17 ARG A 234 ALA A 273 SER A 276 TYR A 277
SITE 3 AC1 17 TYR A 280 GLN A 281 LYS A 284 ASP A 363
SITE 4 AC1 17 MET A 367 HOH A2096 HOH A2163 HOH A2164
SITE 5 AC1 17 HOH A2165
SITE 1 AC2 18 ARG B 218 TYR B 225 LYS B 226 ARG B 234
SITE 2 AC2 18 GLY B 268 ALA B 273 SER B 276 TYR B 277
SITE 3 AC2 18 TYR B 280 GLN B 281 LYS B 284 HIS B 362
SITE 4 AC2 18 ASP B 363 MET B 367 HOH B2168 HOH B2169
SITE 5 AC2 18 HOH B2170 HOH B2171
SITE 1 AC3 14 THR C 60 TYR C 225 LYS C 226 ARG C 234
SITE 2 AC3 14 ALA C 273 SER C 276 TYR C 277 TYR C 280
SITE 3 AC3 14 GLN C 281 LYS C 284 ASP C 363 PHE C 365
SITE 4 AC3 14 MET C 367 HOH C2136
SITE 1 AC4 14 THR D 60 ARG D 218 TYR D 225 LYS D 226
SITE 2 AC4 14 ARG D 234 ALA D 273 SER D 276 TYR D 277
SITE 3 AC4 14 TYR D 280 GLN D 281 LYS D 284 ASP D 363
SITE 4 AC4 14 MET D 367 HOH D2123
SITE 1 AC5 19 SER E 149 ARG E 218 TYR E 225 LYS E 226
SITE 2 AC5 19 ARG E 234 GLY E 268 ALA E 273 SER E 276
SITE 3 AC5 19 TYR E 277 TYR E 280 GLN E 281 LYS E 284
SITE 4 AC5 19 HIS E 362 ASP E 363 MET E 367 HOH E2161
SITE 5 AC5 19 HOH E2162 HOH E2163 HOH E2164
SITE 1 AC6 17 THR F 58 THR F 60 ARG F 218 TYR F 225
SITE 2 AC6 17 LYS F 226 ARG F 234 GLY F 268 ALA F 273
SITE 3 AC6 17 SER F 276 TYR F 277 TYR F 280 GLN F 281
SITE 4 AC6 17 LYS F 284 ASP F 363 MET F 367 HOH F2054
SITE 5 AC6 17 HOH F2102
SITE 1 AC7 13 TYR G 225 ALA G 273 SER G 276 TYR G 277
SITE 2 AC7 13 TYR G 280 GLN G 281 LYS G 284 ASP G 363
SITE 3 AC7 13 PHE G 365 MET G 367 HOH G2140 ASP J 135
SITE 4 AC7 13 ARG J 136
SITE 1 AC8 13 SER H 149 TYR H 225 ALA H 273 SER H 276
SITE 2 AC8 13 TYR H 277 TYR H 280 GLN H 281 LYS H 284
SITE 3 AC8 13 HIS H 362 ASP H 363 PHE H 365 MET H 367
SITE 4 AC8 13 HOH H2144
SITE 1 AC9 17 THR I 58 ARG I 218 TYR I 225 LYS I 226
SITE 2 AC9 17 ARG I 234 GLY I 268 ALA I 273 SER I 276
SITE 3 AC9 17 TYR I 277 TYR I 280 GLN I 281 LYS I 284
SITE 4 AC9 17 HIS I 362 ASP I 363 MET I 367 HOH I2162
SITE 5 AC9 17 HOH I2163
SITE 1 BC1 16 THR J 58 LEU J 59 THR J 60 ARG J 218
SITE 2 BC1 16 LYS J 226 ARG J 234 GLY J 268 SER J 276
SITE 3 BC1 16 TYR J 277 TYR J 280 GLN J 281 LYS J 284
SITE 4 BC1 16 HIS J 362 ASP J 363 PHE J 365 MET J 367
SITE 1 BC2 17 THR K 58 SER K 149 ARG K 218 TYR K 225
SITE 2 BC2 17 LYS K 226 ARG K 234 GLY K 268 ALA K 273
SITE 3 BC2 17 SER K 276 TYR K 277 TYR K 280 GLN K 281
SITE 4 BC2 17 LYS K 284 HIS K 362 ASP K 363 PHE K 365
SITE 5 BC2 17 MET K 367
SITE 1 BC3 16 THR L 58 THR L 60 ARG L 218 TYR L 225
SITE 2 BC3 16 LYS L 226 ARG L 234 GLY L 268 ALA L 273
SITE 3 BC3 16 SER L 276 TYR L 277 TYR L 280 GLN L 281
SITE 4 BC3 16 LYS L 284 ASP L 363 MET L 367 HOH L2104
SITE 1 BC4 3 TRP B 185 THR B 224 GLY B 334
SITE 1 BC5 4 HOH A2101 TRP I 185 THR I 224 GLY I 334
SITE 1 BC6 6 ARG A 124 GLU A 157 PHE A 161 ARG A 310
SITE 2 BC6 6 THR B 25 ILE B 31
SITE 1 BC7 5 THR A 25 ILE A 31 GLU B 157 PHE B 161
SITE 2 BC7 5 ARG B 310
SITE 1 BC8 6 ARG E 124 ARG E 128 GLU E 157 PHE E 161
SITE 2 BC8 6 THR I 25 ILE I 31
SITE 1 BC9 6 THR E 25 ILE E 31 ARG I 124 GLU I 157
SITE 2 BC9 6 PHE I 160 PHE I 161
SITE 1 CC1 2 ARG H 128 GLU H 157
SITE 1 CC2 3 ARG G 124 ARG G 128 GLU G 157
SITE 1 CC3 3 ARG D 128 GLU D 157 PHE D 161
SITE 1 CC4 3 ARG C 128 GLU C 157 PHE C 161
SITE 1 CC5 2 ARG F 128 GLU F 157
SITE 1 CC6 2 GLU J 157 PHE J 161
SITE 1 CC7 2 ARG K 128 GLU K 157
SITE 1 CC8 2 ARG L 128 GLU L 157
CRYST1 121.959 109.278 197.001 90.00 90.23 90.00 P 1 21 1 24
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 0.008199 0.000000 0.000033 0.00000
SCALE2 0.000000 0.009151 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005076 0.00000
MTRIX1 1 -0.999800 -0.009359 -0.015010 152.40000 1
MTRIX2 1 0.009254 -0.999900 0.007044 21.19000 1
MTRIX3 1 -0.015070 0.006904 0.999900 1.12600 1
MTRIX1 2 -0.784400 0.113400 -0.609800 146.40000 1
MTRIX2 2 0.084500 0.993500 0.076100 0.03458 1
MTRIX3 2 0.614500 0.008163 -0.788900 -20.22000 1
MTRIX1 3 0.787400 -0.116000 -0.605400 58.80000 1
MTRIX2 3 -0.087180 -0.993200 0.076940 -24.09000 1
MTRIX3 3 -0.610200 -0.007808 -0.792200 169.20000 1
MTRIX1 4 1.000000 0.000224 0.001490 60.92000 1
MTRIX2 4 0.000226 -1.000000 -0.000907 22.17000 1
MTRIX3 4 0.001489 0.000907 -1.000000 98.46000 1
MTRIX1 5 -0.517400 0.487000 0.703700 109.60000 1
MTRIX2 5 0.343500 0.871300 -0.350400 -8.06400 1
MTRIX3 5 -0.783800 0.060450 -0.618100 56.55000 1
MTRIX1 6 0.537000 0.481000 0.693000 -9.02700 1
MTRIX2 6 0.364000 -0.873200 0.324100 -42.79000 1
MTRIX3 6 0.761000 0.078180 -0.644000 58.66000 1
MTRIX1 7 0.536300 -0.479600 -0.694500 37.05000 1
MTRIX2 7 0.363700 0.873900 -0.322600 -52.50000 1
MTRIX3 7 0.761600 -0.079620 0.643100 -49.85000 1
MTRIX1 8 -0.999900 0.010300 0.013020 211.70000 1
MTRIX2 8 0.010220 0.999900 -0.006346 -0.94620 1
MTRIX3 8 -0.013090 -0.006212 -0.999900 100.50000 1
MTRIX1 9 -0.769200 -0.126800 -0.626300 154.90000 1
MTRIX2 9 -0.093990 0.991900 -0.085340 65.11000 1
MTRIX3 9 0.632100 -0.006770 -0.774900 42.63000 1
MTRIX1 10 -0.776300 0.126900 0.617500 152.30000 1
MTRIX2 10 -0.094950 -0.991900 0.084410 -23.86000 1
MTRIX3 10 0.623200 0.006894 0.782100 -70.99000 1
MTRIX1 11 -0.518100 -0.488800 -0.701900 220.90000 1
MTRIX2 11 0.342000 -0.870600 0.353800 -44.32000 1
MTRIX3 11 -0.784000 -0.056770 0.618200 44.42000 1
TER 2745 GLN A 382
TER 5490 GLN B 382
TER 8236 GLN C 382
TER 10985 GLN D 382
TER 13730 GLN E 382
TER 16425 GLN F 382
TER 19159 GLN G 382
TER 21920 GLN H 382
TER 24660 GLN I 382
TER 27385 LEU J 384
TER 30118 LEU K 384
TER 32816 GLN L 382
MASTER 2205 0 26 225 97 0 72 3935013 12 636 420
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