| content |
HEADER TRANSFERASE 04-SEP-07 2VAX
TITLE CRYSTAL STRUCTURE OF DEACETYLCEPHALOSPORIN C
TITLE 2 ACETYLTRANSFERASE (CEPHALOSPORIN C-SOAK)
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 DEACETYLCEPHALOSPORIN C, CEPHALOSPORIN BIOSYNTHESIS, A/B-
KEYWDS 2 HYDROLASE FOLD, ANTIBIOTIC BIOSYNTHESIS, TRANSFERASE,
KEYWDS 3 ACYLTRANSFERASE, ACETYL TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.LEJON,J.ELLIS,K.VALEGARD
REVDAT 1 23-SEP-08 2VAX 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. 2.6 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) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 62.75
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.77
REMARK 3 NUMBER OF REFLECTIONS : 153301
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) : 0.21169
REMARK 3 R VALUE (WORKING SET) : 0.21106
REMARK 3 FREE R VALUE : 0.24047
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.2
REMARK 3 FREE R VALUE TEST SET COUNT : 3414
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) : 2.600
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.667
REMARK 3 REFLECTION IN BIN (WORKING SET) : 11466
REMARK 3 BIN R VALUE (WORKING SET) : 0.239
REMARK 3 BIN FREE R VALUE SET COUNT : 0
REMARK 3 BIN FREE R VALUE : 0
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 32675
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 448
REMARK 3 SOLVENT ATOMS : 207
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.993
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.33
REMARK 3 B22 (A**2) : 2.10
REMARK 3 B33 (A**2) : -1.77
REMARK 3 B12 (A**2) : 0.00
REMARK 3 B13 (A**2) : -0.07
REMARK 3 B23 (A**2) : 0.00
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.715
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.294
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.236
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.879
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.923
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.901
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED (A): 33955 ; 0.017 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED (DEGREES): 46024 ; 1.909 ; 1.952
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 4145 ; 5.994 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 1640 ;31.354 ;22.610
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 5358 ;17.107 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 336 ;20.932 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 4911 ; 0.128 ; 0.200
REMARK 3 GENERAL PLANES REFINED (A): 26528 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED (A): 15295 ; 0.215 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED (A): 23563 ; 0.317 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED (A): 1125 ; 0.136 ; 0.200
REMARK 3 SYMMETRY VDW REFINED (A): 253 ; 0.291 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED (A): 19 ; 0.233 ; 0.200
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED (A**2): 21088 ; 0.868 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED (A**2): 33285 ; 1.414 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED (A**2): 14489 ; 2.169 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED (A**2): 12694 ; 3.642 ; 4.500
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF NCS GROUPS : 12
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 33 1
REMARK 3 1 B 7 B 33 1
REMARK 3 1 C 7 C 33 1
REMARK 3 1 D 7 D 33 1
REMARK 3 1 E 7 E 33 1
REMARK 3 1 F 7 F 33 1
REMARK 3 1 G 7 G 33 1
REMARK 3 1 H 7 H 33 1
REMARK 3 1 I 7 I 33 1
REMARK 3 1 J 7 J 33 1
REMARK 3 1 K 7 K 33 1
REMARK 3 1 L 7 L 33 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 197 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 1 B (A): 197 ; .11 ; .05
REMARK 3 TIGHT POSITIONAL 1 C (A): 197 ; .07 ; .05
REMARK 3 TIGHT POSITIONAL 1 D (A): 197 ; .07 ; .05
REMARK 3 TIGHT POSITIONAL 1 E (A): 197 ; .07 ; .05
REMARK 3 TIGHT POSITIONAL 1 F (A): 197 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 1 G (A): 197 ; .13 ; .05
REMARK 3 TIGHT POSITIONAL 1 H (A): 197 ; .10 ; .05
REMARK 3 TIGHT POSITIONAL 1 I (A): 197 ; .07 ; .05
REMARK 3 TIGHT POSITIONAL 1 J (A): 197 ; .08 ; .05
REMARK 3 TIGHT POSITIONAL 1 K (A): 197 ; .07 ; .05
REMARK 3 TIGHT POSITIONAL 1 L (A): 197 ; .06 ; .05
REMARK 3 TIGHT THERMAL 1 A (A**2): 197 ; .15 ; .50
REMARK 3 TIGHT THERMAL 1 B (A**2): 197 ; .19 ; .50
REMARK 3 TIGHT THERMAL 1 C (A**2): 197 ; .22 ; .50
REMARK 3 TIGHT THERMAL 1 D (A**2): 197 ; .21 ; .50
REMARK 3 TIGHT THERMAL 1 E (A**2): 197 ; .15 ; .50
REMARK 3 TIGHT THERMAL 1 F (A**2): 197 ; .16 ; .50
REMARK 3 TIGHT THERMAL 1 G (A**2): 197 ; .13 ; .50
REMARK 3 TIGHT THERMAL 1 H (A**2): 197 ; .13 ; .50
REMARK 3 TIGHT THERMAL 1 I (A**2): 197 ; .19 ; .50
REMARK 3 TIGHT THERMAL 1 J (A**2): 197 ; .32 ; .50
REMARK 3 TIGHT THERMAL 1 K (A**2): 197 ; .33 ; .50
REMARK 3 TIGHT THERMAL 1 L (A**2): 197 ; .16 ; .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 59 1
REMARK 3 1 B 35 B 59 1
REMARK 3 1 C 35 C 59 1
REMARK 3 1 D 35 D 59 1
REMARK 3 1 E 35 E 59 1
REMARK 3 1 F 35 F 59 1
REMARK 3 1 G 35 G 59 1
REMARK 3 1 H 35 H 59 1
REMARK 3 1 I 35 I 59 1
REMARK 3 1 J 35 J 59 1
REMARK 3 1 K 35 K 59 1
REMARK 3 1 L 35 L 59 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 2 A (A): 189 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 2 B (A): 189 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 2 C (A): 189 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 2 D (A): 189 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 2 E (A): 189 ; .05 ; .05
REMARK 3 TIGHT POSITIONAL 2 F (A): 189 ; .07 ; .05
REMARK 3 TIGHT POSITIONAL 2 G (A): 189 ; .07 ; .05
REMARK 3 TIGHT POSITIONAL 2 H (A): 189 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 2 I (A): 189 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 2 J (A): 189 ; .05 ; .05
REMARK 3 TIGHT POSITIONAL 2 K (A): 189 ; .05 ; .05
REMARK 3 TIGHT POSITIONAL 2 L (A): 189 ; .06 ; .05
REMARK 3 TIGHT THERMAL 2 A (A**2): 189 ; .19 ; .50
REMARK 3 TIGHT THERMAL 2 B (A**2): 189 ; .13 ; .50
REMARK 3 TIGHT THERMAL 2 C (A**2): 189 ; .24 ; .50
REMARK 3 TIGHT THERMAL 2 D (A**2): 189 ; .23 ; .50
REMARK 3 TIGHT THERMAL 2 E (A**2): 189 ; .18 ; .50
REMARK 3 TIGHT THERMAL 2 F (A**2): 189 ; .18 ; .50
REMARK 3 TIGHT THERMAL 2 G (A**2): 189 ; .20 ; .50
REMARK 3 TIGHT THERMAL 2 H (A**2): 189 ; .20 ; .50
REMARK 3 TIGHT THERMAL 2 I (A**2): 189 ; .12 ; .50
REMARK 3 TIGHT THERMAL 2 J (A**2): 189 ; .29 ; .50
REMARK 3 TIGHT THERMAL 2 K (A**2): 189 ; .31 ; .50
REMARK 3 TIGHT THERMAL 2 L (A**2): 189 ; .18 ; .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 61 A 127 1
REMARK 3 1 B 61 B 127 1
REMARK 3 1 C 61 C 127 1
REMARK 3 1 D 61 D 127 1
REMARK 3 1 E 61 E 127 1
REMARK 3 1 F 61 F 127 1
REMARK 3 1 G 61 G 127 1
REMARK 3 1 H 61 H 127 1
REMARK 3 1 I 61 I 127 1
REMARK 3 1 J 61 J 127 1
REMARK 3 1 K 61 K 127 1
REMARK 3 1 L 61 L 127 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 3 A (A): 469 ; .05 ; .05
REMARK 3 TIGHT POSITIONAL 3 B (A): 469 ; .05 ; .05
REMARK 3 TIGHT POSITIONAL 3 C (A): 469 ; .07 ; .05
REMARK 3 TIGHT POSITIONAL 3 D (A): 469 ; .07 ; .05
REMARK 3 TIGHT POSITIONAL 3 E (A): 469 ; .05 ; .05
REMARK 3 TIGHT POSITIONAL 3 F (A): 469 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 3 G (A): 469 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 3 H (A): 469 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 3 I (A): 469 ; .05 ; .05
REMARK 3 TIGHT POSITIONAL 3 J (A): 469 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 3 K (A): 469 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 3 L (A): 469 ; .06 ; .05
REMARK 3 TIGHT THERMAL 3 A (A**2): 469 ; .15 ; .50
REMARK 3 TIGHT THERMAL 3 B (A**2): 469 ; .15 ; .50
REMARK 3 TIGHT THERMAL 3 C (A**2): 469 ; .23 ; .50
REMARK 3 TIGHT THERMAL 3 D (A**2): 469 ; .23 ; .50
REMARK 3 TIGHT THERMAL 3 E (A**2): 469 ; .15 ; .50
REMARK 3 TIGHT THERMAL 3 F (A**2): 469 ; .15 ; .50
REMARK 3 TIGHT THERMAL 3 G (A**2): 469 ; .16 ; .50
REMARK 3 TIGHT THERMAL 3 H (A**2): 469 ; .16 ; .50
REMARK 3 TIGHT THERMAL 3 I (A**2): 469 ; .15 ; .50
REMARK 3 TIGHT THERMAL 3 J (A**2): 469 ; .29 ; .50
REMARK 3 TIGHT THERMAL 3 K (A**2): 469 ; .30 ; .50
REMARK 3 TIGHT THERMAL 3 L (A**2): 469 ; .15 ; .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): 83 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 4 B (A): 83 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 4 C (A): 83 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 4 D (A): 83 ; .07 ; .05
REMARK 3 TIGHT POSITIONAL 4 E (A): 83 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 4 F (A): 83 ; .07 ; .05
REMARK 3 TIGHT POSITIONAL 4 G (A): 83 ; .08 ; .05
REMARK 3 TIGHT POSITIONAL 4 H (A): 83 ; .05 ; .05
REMARK 3 TIGHT POSITIONAL 4 I (A): 83 ; .05 ; .05
REMARK 3 TIGHT POSITIONAL 4 J (A): 83 ; .08 ; .05
REMARK 3 TIGHT POSITIONAL 4 K (A): 83 ; .07 ; .05
REMARK 3 TIGHT POSITIONAL 4 L (A): 83 ; .06 ; .05
REMARK 3 TIGHT THERMAL 4 A (A**2): 83 ; .14 ; .50
REMARK 3 TIGHT THERMAL 4 B (A**2): 83 ; .20 ; .50
REMARK 3 TIGHT THERMAL 4 C (A**2): 83 ; .24 ; .50
REMARK 3 TIGHT THERMAL 4 D (A**2): 83 ; .25 ; .50
REMARK 3 TIGHT THERMAL 4 E (A**2): 83 ; .15 ; .50
REMARK 3 TIGHT THERMAL 4 F (A**2): 83 ; .17 ; .50
REMARK 3 TIGHT THERMAL 4 G (A**2): 83 ; .15 ; .50
REMARK 3 TIGHT THERMAL 4 H (A**2): 83 ; .16 ; .50
REMARK 3 TIGHT THERMAL 4 I (A**2): 83 ; .18 ; .50
REMARK 3 TIGHT THERMAL 4 J (A**2): 83 ; .35 ; .50
REMARK 3 TIGHT THERMAL 4 K (A**2): 83 ; .33 ; .50
REMARK 3 TIGHT THERMAL 4 L (A**2): 83 ; .18 ; .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 159 1
REMARK 3 1 B 141 B 159 1
REMARK 3 1 C 141 C 159 1
REMARK 3 1 D 141 D 159 1
REMARK 3 1 E 141 E 159 1
REMARK 3 1 F 141 F 159 1
REMARK 3 1 G 141 G 159 1
REMARK 3 1 H 141 H 159 1
REMARK 3 1 I 141 I 159 1
REMARK 3 1 J 141 J 159 1
REMARK 3 1 K 141 K 159 1
REMARK 3 1 L 141 L 159 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 5 A (A): 136 ; .08 ; .05
REMARK 3 TIGHT POSITIONAL 5 B (A): 136 ; .05 ; .05
REMARK 3 TIGHT POSITIONAL 5 C (A): 136 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 5 D (A): 136 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 5 E (A): 136 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 5 F (A): 136 ; .05 ; .05
REMARK 3 TIGHT POSITIONAL 5 G (A): 136 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 5 H (A): 136 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 5 I (A): 136 ; .05 ; .05
REMARK 3 TIGHT POSITIONAL 5 J (A): 136 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 5 K (A): 136 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 5 L (A): 136 ; .05 ; .05
REMARK 3 TIGHT THERMAL 5 A (A**2): 136 ; .16 ; .50
REMARK 3 TIGHT THERMAL 5 B (A**2): 136 ; .16 ; .50
REMARK 3 TIGHT THERMAL 5 C (A**2): 136 ; .18 ; .50
REMARK 3 TIGHT THERMAL 5 D (A**2): 136 ; .19 ; .50
REMARK 3 TIGHT THERMAL 5 E (A**2): 136 ; .16 ; .50
REMARK 3 TIGHT THERMAL 5 F (A**2): 136 ; .17 ; .50
REMARK 3 TIGHT THERMAL 5 G (A**2): 136 ; .20 ; .50
REMARK 3 TIGHT THERMAL 5 H (A**2): 136 ; .20 ; .50
REMARK 3 TIGHT THERMAL 5 I (A**2): 136 ; .17 ; .50
REMARK 3 TIGHT THERMAL 5 J (A**2): 136 ; .32 ; .50
REMARK 3 TIGHT THERMAL 5 K (A**2): 136 ; .31 ; .50
REMARK 3 TIGHT THERMAL 5 L (A**2): 136 ; .14 ; .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 161 A 217 1
REMARK 3 1 B 161 B 217 1
REMARK 3 1 C 161 C 217 1
REMARK 3 1 D 161 D 217 1
REMARK 3 1 E 161 E 217 1
REMARK 3 1 F 161 F 217 1
REMARK 3 1 G 161 G 217 1
REMARK 3 1 H 161 H 217 1
REMARK 3 1 I 161 I 217 1
REMARK 3 1 J 161 J 217 1
REMARK 3 1 K 161 K 217 1
REMARK 3 1 L 161 L 217 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 6 A (A): 457 ; .08 ; .05
REMARK 3 TIGHT POSITIONAL 6 B (A): 457 ; .05 ; .05
REMARK 3 TIGHT POSITIONAL 6 C (A): 457 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 6 D (A): 457 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 6 E (A): 457 ; .05 ; .05
REMARK 3 TIGHT POSITIONAL 6 F (A): 457 ; .08 ; .05
REMARK 3 TIGHT POSITIONAL 6 G (A): 457 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 6 H (A): 457 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 6 I (A): 457 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 6 J (A): 457 ; .05 ; .05
REMARK 3 TIGHT POSITIONAL 6 K (A): 457 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 6 L (A): 457 ; .05 ; .05
REMARK 3 TIGHT THERMAL 6 A (A**2): 457 ; .14 ; .50
REMARK 3 TIGHT THERMAL 6 B (A**2): 457 ; .13 ; .50
REMARK 3 TIGHT THERMAL 6 C (A**2): 457 ; .13 ; .50
REMARK 3 TIGHT THERMAL 6 D (A**2): 457 ; .13 ; .50
REMARK 3 TIGHT THERMAL 6 E (A**2): 457 ; .14 ; .50
REMARK 3 TIGHT THERMAL 6 F (A**2): 457 ; .15 ; .50
REMARK 3 TIGHT THERMAL 6 G (A**2): 457 ; .17 ; .50
REMARK 3 TIGHT THERMAL 6 H (A**2): 457 ; .17 ; .50
REMARK 3 TIGHT THERMAL 6 I (A**2): 457 ; .14 ; .50
REMARK 3 TIGHT THERMAL 6 J (A**2): 457 ; .20 ; .50
REMARK 3 TIGHT THERMAL 6 K (A**2): 457 ; .20 ; .50
REMARK 3 TIGHT THERMAL 6 L (A**2): 457 ; .15 ; .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 219 A 235 1
REMARK 3 1 B 219 B 235 1
REMARK 3 1 C 219 C 235 1
REMARK 3 1 D 219 D 235 1
REMARK 3 1 E 219 E 235 1
REMARK 3 1 F 219 F 235 1
REMARK 3 1 G 219 G 235 1
REMARK 3 1 H 219 H 235 1
REMARK 3 1 I 219 I 235 1
REMARK 3 1 J 219 J 235 1
REMARK 3 1 K 219 K 235 1
REMARK 3 1 L 219 L 235 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 7 A (A): 140 ; .07 ; .05
REMARK 3 TIGHT POSITIONAL 7 B (A): 140 ; .05 ; .05
REMARK 3 TIGHT POSITIONAL 7 C (A): 140 ; .05 ; .05
REMARK 3 TIGHT POSITIONAL 7 D (A): 140 ; .05 ; .05
REMARK 3 TIGHT POSITIONAL 7 E (A): 140 ; .07 ; .05
REMARK 3 TIGHT POSITIONAL 7 F (A): 140 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 7 G (A): 140 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 7 H (A): 140 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 7 I (A): 140 ; .05 ; .05
REMARK 3 TIGHT POSITIONAL 7 J (A): 140 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 7 K (A): 140 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 7 L (A): 140 ; .06 ; .05
REMARK 3 TIGHT THERMAL 7 A (A**2): 140 ; .15 ; .50
REMARK 3 TIGHT THERMAL 7 B (A**2): 140 ; .16 ; .50
REMARK 3 TIGHT THERMAL 7 C (A**2): 140 ; .15 ; .50
REMARK 3 TIGHT THERMAL 7 D (A**2): 140 ; .16 ; .50
REMARK 3 TIGHT THERMAL 7 E (A**2): 140 ; .15 ; .50
REMARK 3 TIGHT THERMAL 7 F (A**2): 140 ; .19 ; .50
REMARK 3 TIGHT THERMAL 7 G (A**2): 140 ; .13 ; .50
REMARK 3 TIGHT THERMAL 7 H (A**2): 140 ; .12 ; .50
REMARK 3 TIGHT THERMAL 7 I (A**2): 140 ; .16 ; .50
REMARK 3 TIGHT THERMAL 7 J (A**2): 140 ; .13 ; .50
REMARK 3 TIGHT THERMAL 7 K (A**2): 140 ; .13 ; .50
REMARK 3 TIGHT THERMAL 7 L (A**2): 140 ; .19 ; .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 237 A 279 1
REMARK 3 1 B 237 B 279 1
REMARK 3 1 C 237 C 279 1
REMARK 3 1 D 237 D 279 1
REMARK 3 1 E 237 E 279 1
REMARK 3 1 F 237 F 279 1
REMARK 3 1 G 237 G 279 1
REMARK 3 1 H 237 H 279 1
REMARK 3 1 I 237 I 279 1
REMARK 3 1 J 237 J 279 1
REMARK 3 1 K 237 K 279 1
REMARK 3 1 L 237 L 279 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 8 A (A): 96 ; .05 ; .05
REMARK 3 TIGHT POSITIONAL 8 B (A): 96 ; .05 ; .05
REMARK 3 TIGHT POSITIONAL 8 C (A): 96 ; .04 ; .05
REMARK 3 TIGHT POSITIONAL 8 D (A): 96 ; .05 ; .05
REMARK 3 TIGHT POSITIONAL 8 E (A): 96 ; .05 ; .05
REMARK 3 TIGHT POSITIONAL 8 F (A): 96 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 8 G (A): 96 ; .05 ; .05
REMARK 3 TIGHT POSITIONAL 8 H (A): 96 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 8 I (A): 96 ; .05 ; .05
REMARK 3 TIGHT POSITIONAL 8 J (A): 96 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 8 K (A): 96 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 8 L (A): 96 ; .05 ; .05
REMARK 3 TIGHT THERMAL 8 A (A**2): 96 ; .09 ; .50
REMARK 3 TIGHT THERMAL 8 B (A**2): 96 ; .14 ; .50
REMARK 3 TIGHT THERMAL 8 C (A**2): 96 ; .13 ; .50
REMARK 3 TIGHT THERMAL 8 D (A**2): 96 ; .13 ; .50
REMARK 3 TIGHT THERMAL 8 E (A**2): 96 ; .09 ; .50
REMARK 3 TIGHT THERMAL 8 F (A**2): 96 ; .11 ; .50
REMARK 3 TIGHT THERMAL 8 G (A**2): 96 ; .12 ; .50
REMARK 3 TIGHT THERMAL 8 H (A**2): 96 ; .12 ; .50
REMARK 3 TIGHT THERMAL 8 I (A**2): 96 ; .13 ; .50
REMARK 3 TIGHT THERMAL 8 J (A**2): 96 ; .19 ; .50
REMARK 3 TIGHT THERMAL 8 K (A**2): 96 ; .19 ; .50
REMARK 3 TIGHT THERMAL 8 L (A**2): 96 ; .11 ; .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 282 A 307 1
REMARK 3 1 B 282 B 307 1
REMARK 3 1 C 282 C 307 1
REMARK 3 1 D 282 D 307 1
REMARK 3 1 E 282 E 307 1
REMARK 3 1 F 282 F 307 1
REMARK 3 1 G 282 G 307 1
REMARK 3 1 H 282 H 307 1
REMARK 3 1 I 282 I 307 1
REMARK 3 1 J 282 J 307 1
REMARK 3 1 K 282 K 307 1
REMARK 3 1 L 282 L 307 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 9 A (A): 203 ; .05 ; .05
REMARK 3 TIGHT POSITIONAL 9 B (A): 203 ; .05 ; .05
REMARK 3 TIGHT POSITIONAL 9 C (A): 203 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 9 D (A): 203 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 9 E (A): 203 ; .05 ; .05
REMARK 3 TIGHT POSITIONAL 9 F (A): 203 ; .05 ; .05
REMARK 3 TIGHT POSITIONAL 9 G (A): 203 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 9 H (A): 203 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 9 I (A): 203 ; .05 ; .05
REMARK 3 TIGHT POSITIONAL 9 J (A): 203 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 9 K (A): 203 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 9 L (A): 203 ; .05 ; .05
REMARK 3 TIGHT THERMAL 9 A (A**2): 203 ; .11 ; .50
REMARK 3 TIGHT THERMAL 9 B (A**2): 203 ; .16 ; .50
REMARK 3 TIGHT THERMAL 9 C (A**2): 203 ; .18 ; .50
REMARK 3 TIGHT THERMAL 9 D (A**2): 203 ; .17 ; .50
REMARK 3 TIGHT THERMAL 9 E (A**2): 203 ; .11 ; .50
REMARK 3 TIGHT THERMAL 9 F (A**2): 203 ; .16 ; .50
REMARK 3 TIGHT THERMAL 9 G (A**2): 203 ; .13 ; .50
REMARK 3 TIGHT THERMAL 9 H (A**2): 203 ; .13 ; .50
REMARK 3 TIGHT THERMAL 9 I (A**2): 203 ; .16 ; .50
REMARK 3 TIGHT THERMAL 9 J (A**2): 203 ; .27 ; .50
REMARK 3 TIGHT THERMAL 9 K (A**2): 203 ; .28 ; .50
REMARK 3 TIGHT THERMAL 9 L (A**2): 203 ; .15 ; .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 309 A 330 1
REMARK 3 1 B 309 B 330 1
REMARK 3 1 C 309 C 330 1
REMARK 3 1 D 309 D 330 1
REMARK 3 1 E 309 E 330 1
REMARK 3 1 F 309 F 330 1
REMARK 3 1 G 309 G 330 1
REMARK 3 1 H 309 H 330 1
REMARK 3 1 I 309 I 330 1
REMARK 3 1 J 309 J 330 1
REMARK 3 1 K 309 K 330 1
REMARK 3 1 L 309 L 330 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 10 A (A): 151 ; .08 ; .05
REMARK 3 TIGHT POSITIONAL 10 B (A): 151 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 10 C (A): 151 ; .05 ; .05
REMARK 3 TIGHT POSITIONAL 10 D (A): 151 ; .11 ; .05
REMARK 3 TIGHT POSITIONAL 10 E (A): 151 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 10 F (A): 151 ; .05 ; .05
REMARK 3 TIGHT POSITIONAL 10 G (A): 151 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 10 H (A): 151 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 10 I (A): 151 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 10 J (A): 151 ; .05 ; .05
REMARK 3 TIGHT POSITIONAL 10 K (A): 151 ; .05 ; .05
REMARK 3 TIGHT POSITIONAL 10 L (A): 151 ; .05 ; .05
REMARK 3 TIGHT THERMAL 10 A (A**2): 151 ; .15 ; .50
REMARK 3 TIGHT THERMAL 10 B (A**2): 151 ; .15 ; .50
REMARK 3 TIGHT THERMAL 10 C (A**2): 151 ; .13 ; .50
REMARK 3 TIGHT THERMAL 10 D (A**2): 151 ; .12 ; .50
REMARK 3 TIGHT THERMAL 10 E (A**2): 151 ; .15 ; .50
REMARK 3 TIGHT THERMAL 10 F (A**2): 151 ; .12 ; .50
REMARK 3 TIGHT THERMAL 10 G (A**2): 151 ; .15 ; .50
REMARK 3 TIGHT THERMAL 10 H (A**2): 151 ; .16 ; .50
REMARK 3 TIGHT THERMAL 10 I (A**2): 151 ; .16 ; .50
REMARK 3 TIGHT THERMAL 10 J (A**2): 151 ; .21 ; .50
REMARK 3 TIGHT THERMAL 10 K (A**2): 151 ; .22 ; .50
REMARK 3 TIGHT THERMAL 10 L (A**2): 151 ; .12 ; .50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 11
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 11 A (A): 110 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 11 B (A): 110 ; .05 ; .05
REMARK 3 TIGHT POSITIONAL 11 C (A): 110 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 11 D (A): 110 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 11 E (A): 110 ; .06 ; .05
REMARK 3 TIGHT POSITIONAL 11 F (A): 110 ; .05 ; .05
REMARK 3 TIGHT POSITIONAL 11 G (A): 110 ; .04 ; .05
REMARK 3 TIGHT POSITIONAL 11 H (A): 110 ; .04 ; .05
REMARK 3 TIGHT POSITIONAL 11 I (A): 110 ; .05 ; .05
REMARK 3 TIGHT POSITIONAL 11 J (A): 110 ; .05 ; .05
REMARK 3 TIGHT POSITIONAL 11 K (A): 110 ; .05 ; .05
REMARK 3 TIGHT POSITIONAL 11 L (A): 110 ; .05 ; .05
REMARK 3 TIGHT THERMAL 11 A (A**2): 110 ; .16 ; .50
REMARK 3 TIGHT THERMAL 11 B (A**2): 110 ; .13 ; .50
REMARK 3 TIGHT THERMAL 11 C (A**2): 110 ; .13 ; .50
REMARK 3 TIGHT THERMAL 11 D (A**2): 110 ; .13 ; .50
REMARK 3 TIGHT THERMAL 11 E (A**2): 110 ; .15 ; .50
REMARK 3 TIGHT THERMAL 11 F (A**2): 110 ; .14 ; .50
REMARK 3 TIGHT THERMAL 11 G (A**2): 110 ; .15 ; .50
REMARK 3 TIGHT THERMAL 11 H (A**2): 110 ; .13 ; .50
REMARK 3 TIGHT THERMAL 11 I (A**2): 110 ; .11 ; .50
REMARK 3 TIGHT THERMAL 11 J (A**2): 110 ; .12 ; .50
REMARK 3 TIGHT THERMAL 11 K (A**2): 110 ; .13 ; .50
REMARK 3 TIGHT THERMAL 11 L (A**2): 110 ; .14 ; .50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 12
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 381 1
REMARK 3 1 B 347 B 381 1
REMARK 3 1 C 347 C 381 1
REMARK 3 1 D 347 D 381 1
REMARK 3 1 E 347 E 381 1
REMARK 3 1 F 347 F 381 1
REMARK 3 1 G 347 G 381 1
REMARK 3 1 H 347 H 381 1
REMARK 3 1 I 347 I 381 1
REMARK 3 1 J 347 J 381 1
REMARK 3 1 K 347 K 381 1
REMARK 3 1 L 347 L 381 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 12 A (A): 273 ; .08 ; .05
REMARK 3 TIGHT POSITIONAL 12 B (A): 273 ; .13 ; .05
REMARK 3 TIGHT POSITIONAL 12 C (A): 273 ; .08 ; .05
REMARK 3 TIGHT POSITIONAL 12 D (A): 273 ; .08 ; .05
REMARK 3 TIGHT POSITIONAL 12 E (A): 273 ; .08 ; .05
REMARK 3 TIGHT POSITIONAL 12 F (A): 273 ; .13 ; .05
REMARK 3 TIGHT POSITIONAL 12 G (A): 273 ; .08 ; .05
REMARK 3 TIGHT POSITIONAL 12 H (A): 273 ; .13 ; .05
REMARK 3 TIGHT POSITIONAL 12 I (A): 273 ; .13 ; .05
REMARK 3 TIGHT POSITIONAL 12 J (A): 273 ; .08 ; .05
REMARK 3 TIGHT POSITIONAL 12 K (A): 273 ; .08 ; .05
REMARK 3 TIGHT POSITIONAL 12 L (A): 273 ; .08 ; .05
REMARK 3 TIGHT THERMAL 12 A (A**2): 273 ; .15 ; .50
REMARK 3 TIGHT THERMAL 12 B (A**2): 273 ; .13 ; .50
REMARK 3 TIGHT THERMAL 12 C (A**2): 273 ; .12 ; .50
REMARK 3 TIGHT THERMAL 12 D (A**2): 273 ; .12 ; .50
REMARK 3 TIGHT THERMAL 12 E (A**2): 273 ; .15 ; .50
REMARK 3 TIGHT THERMAL 12 F (A**2): 273 ; .15 ; .50
REMARK 3 TIGHT THERMAL 12 G (A**2): 273 ; .14 ; .50
REMARK 3 TIGHT THERMAL 12 H (A**2): 273 ; .14 ; .50
REMARK 3 TIGHT THERMAL 12 I (A**2): 273 ; .14 ; .50
REMARK 3 TIGHT THERMAL 12 J (A**2): 273 ; .16 ; .50
REMARK 3 TIGHT THERMAL 12 K (A**2): 273 ; .16 ; .50
REMARK 3 TIGHT THERMAL 12 L (A**2): 273 ; .15 ; .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 241-267 ARE DISORDERED.
REMARK 4
REMARK 4 2VAX COMPLIES WITH FORMAT V. 3.1, 01-AUG-2007
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY EBI ON 6-SEP-2007.
REMARK 100 THE EBI ID CODE IS EBI-33688.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-MAR-2007
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-3
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.931
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 : 156738
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.60
REMARK 200 RESOLUTION RANGE LOW (A) : 65.09
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 6.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 3.8
REMARK 200 R MERGE (I) : 0.07
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 14.70
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.74
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7
REMARK 200 DATA REDUNDANCY IN SHELL : 3.8
REMARK 200 R MERGE FOR SHELL (I) : 0.22
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 5.80
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER
REMARK 200 SOFTWARE USED: REFMAC
REMARK 200 STARTING MODEL: NONE
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.52
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 54.64400
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 A 7 .. 382 B 7 .. 382 0.328
REMARK 295 M 2 A 7 .. 382 C 7 .. 382 0.451
REMARK 295 M 3 A 7 .. 382 D 7 .. 382 0.407
REMARK 295 M 4 A 7 .. 382 E 7 .. 382 0.236
REMARK 295 M 5 A 7 .. 382 F 7 .. 382 0.460
REMARK 295 M 6 A 7 .. 382 G 7 .. 382 0.541
REMARK 295 M 7 A 7 .. 382 H 7 .. 382 0.473
REMARK 295 M 8 A 7 .. 382 I 7 .. 382 0.356
REMARK 295 M 9 A 7 .. 382 J 7 .. 382 0.531
REMARK 295 M 10 A 7 .. 382 K 7 .. 382 0.437
REMARK 295 M 11 A 7 .. 382 L 7 .. 382 0.478
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: 4470 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 31570 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -36.8 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: 4880 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 31350 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.1 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: 4330 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 30910 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.7 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: 3670 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 30250 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.4 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: 4260 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 30410 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.2 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: 4410 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 31140 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.4 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 GLU A 109
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 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 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 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 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 GLU D 109
REMARK 465 GLY D 110
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 GLY F 268
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 ALA H 238
REMARK 465 PRO H 239
REMARK 465 GLY H 240
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 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 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 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 SER F 383 CA C O CB OG
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 60 - O42 CSC B 1384 2.16
REMARK 500 O GLU G 360 - O HOH G 2021 2.19
REMARK 500 OG1 THR H 60 - O42 CSC H 1383 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500
REMARK 500 NE2 GLN G 283 NH2 ARG J 49 1556 2.09
REMARK 500 NE2 GLN H 283 NH2 ARG K 49 1655 2.10
REMARK 500 NH2 ARG J 49 NE2 GLN G 283 1554 2.09
REMARK 500 NH2 ARG K 49 NE2 GLN H 283 1645 2.10
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 GLU B 360 C GLU B 360 O -0.180
REMARK 500 GLU F 360 C GLU F 360 O -0.186
REMARK 500 GLU G 27 CD GLU G 27 OE1 -0.085
REMARK 500 GLU G 27 CD GLU G 27 OE2 -0.088
REMARK 500 GLU H 360 C GLU H 360 O -0.177
REMARK 500 GLU I 360 C GLU I 360 O -0.180
REMARK 500 CYS F 176 CB CYS F 176 SG -0.129
REMARK 500 CYS I 176 CB CYS I 176 SG -0.098
REMARK 500 CYS J 176 CB CYS J 176 SG -0.107
REMARK 500 CYS K 176 CB CYS K 176 SG -0.102
REMARK 500 CYS L 176 CB CYS L 176 SG -0.130
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 PRO A 113 C - N - CA ANGL. DEV. = 9.0 DEGREES
REMARK 500 ARG A 177 NE - CZ - NH1 ANGL. DEV. = 7.5 DEGREES
REMARK 500 ARG A 177 NE - CZ - NH2 ANGL. DEV. = -8.6 DEGREES
REMARK 500 ARG B 8 CD - NE - CZ ANGL. DEV. = 14.3 DEGREES
REMARK 500 ARG B 8 NE - CZ - NH1 ANGL. DEV. = 10.8 DEGREES
REMARK 500 ARG B 8 NE - CZ - NH2 ANGL. DEV. = -10.9 DEGREES
REMARK 500 PRO B 113 C - N - CA ANGL. DEV. = 10.1 DEGREES
REMARK 500 ARG B 310 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 GLU B 360 CA - C - N ANGL. DEV. = 13.5 DEGREES
REMARK 500 GLU B 360 O - C - N ANGL. DEV. = -10.7 DEGREES
REMARK 500 ARG C 167 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG C 310 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 ARG C 310 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ARG C 331 NE - CZ - NH1 ANGL. DEV. = -3.7 DEGREES
REMARK 500 GLU D 27 OE1 - CD - OE2 ANGL. DEV. = -9.1 DEGREES
REMARK 500 ARG D 167 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG D 310 CD - NE - CZ ANGL. DEV. = 12.8 DEGREES
REMARK 500 ARG D 310 NE - CZ - NH1 ANGL. DEV. = -8.6 DEGREES
REMARK 500 ARG D 310 NE - CZ - NH2 ANGL. DEV. = 8.8 DEGREES
REMARK 500 ARG D 331 NE - CZ - NH1 ANGL. DEV. = -3.0 DEGREES
REMARK 500 ARG E 310 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ARG F 167 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ARG F 190 CD - NE - CZ ANGL. DEV. = 14.6 DEGREES
REMARK 500 ARG F 190 NE - CZ - NH1 ANGL. DEV. = 8.6 DEGREES
REMARK 500 ARG F 190 NE - CZ - NH2 ANGL. DEV. = -9.9 DEGREES
REMARK 500 GLU F 360 CA - C - N ANGL. DEV. = 14.0 DEGREES
REMARK 500 GLU F 360 O - C - N ANGL. DEV. = -12.1 DEGREES
REMARK 500 GLU G 27 OE1 - CD - OE2 ANGL. DEV. = -15.1 DEGREES
REMARK 500 GLU H 27 OE1 - CD - OE2 ANGL. DEV. = -10.8 DEGREES
REMARK 500 ARG H 308 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ARG H 310 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 GLU H 360 CA - C - N ANGL. DEV. = 13.4 DEGREES
REMARK 500 GLU H 360 O - C - N ANGL. DEV. = -11.2 DEGREES
REMARK 500 PRO I 113 C - N - CA ANGL. DEV. = 10.2 DEGREES
REMARK 500 ARG I 167 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG I 310 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 GLU I 360 CA - C - N ANGL. DEV. = 13.9 DEGREES
REMARK 500 GLU I 360 O - C - N ANGL. DEV. = -10.8 DEGREES
REMARK 500 ARG L 167 NE - CZ - NH1 ANGL. DEV. = 3.2 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 PRO A 106 -2.79 -57.79
REMARK 500 ASP A 107 55.13 -104.37
REMARK 500 ASP A 208 58.43 -143.36
REMARK 500 PRO A 239 161.10 -42.89
REMARK 500 GLN A 269 -31.37 -151.34
REMARK 500 ASP A 305 111.06 -167.47
REMARK 500 ASN A 350 73.26 -108.05
REMARK 500 PRO B 106 -5.47 -58.97
REMARK 500 ASP B 107 65.16 -103.62
REMARK 500 PRO B 239 170.17 -52.74
REMARK 500 GLN B 269 -27.68 -152.00
REMARK 500 ASP B 305 107.51 -165.38
REMARK 500 ASN B 350 75.58 -110.11
REMARK 500 ALA C 108 16.71 171.06
REMARK 500 ASP C 305 109.02 -166.48
REMARK 500 ASN C 350 72.75 -107.20
REMARK 500 ASP D 107 58.64 -95.69
REMARK 500 ASP D 305 108.44 -165.51
REMARK 500 ASN D 350 75.51 -106.22
REMARK 500 PRO E 106 -2.84 -57.88
REMARK 500 ASP E 107 55.11 -103.77
REMARK 500 ALA E 144 146.95 -171.08
REMARK 500 ASP E 208 58.51 -143.76
REMARK 500 PRO E 210 73.69 -69.34
REMARK 500 PRO E 239 164.53 -47.98
REMARK 500 GLN E 269 -32.12 -155.34
REMARK 500 ASP E 305 110.48 -167.11
REMARK 500 ASN E 350 72.39 -104.66
REMARK 500 ASP F 107 56.27 -98.65
REMARK 500 ASP F 208 57.99 -142.65
REMARK 500 ASP F 305 110.94 -169.97
REMARK 500 ASN F 350 73.07 -106.98
REMARK 500 PRO G 106 -8.66 -55.34
REMARK 500 ASP G 107 75.70 -100.21
REMARK 500 TYR G 280 -81.67 -57.69
REMARK 500 ASP G 305 107.86 -170.48
REMARK 500 ASN G 350 72.94 -108.42
REMARK 500 PRO H 106 -7.42 -56.76
REMARK 500 ASP H 107 71.97 -100.15
REMARK 500 TYR H 280 -78.14 -62.60
REMARK 500 ASP H 305 108.39 -168.43
REMARK 500 ASN H 350 71.81 -107.60
REMARK 500 PRO I 106 -6.02 -58.92
REMARK 500 ASP I 107 68.84 -102.46
REMARK 500 GLN I 269 -26.75 -153.96
REMARK 500 ASP I 305 107.99 -165.93
REMARK 500 ASN I 350 77.20 -110.81
REMARK 500 ASP J 14 -178.83 -66.75
REMARK 500 PRO J 106 -5.69 -57.52
REMARK 500 ASP J 107 58.88 -103.74
REMARK 500 ASP J 208 59.57 -142.42
REMARK 500 GLN J 269 -32.70 -154.51
REMARK 500 ASP J 305 112.22 -168.55
REMARK 500 ARG J 310 -36.86 -133.68
REMARK 500 ASN J 350 70.92 -107.95
REMARK 500 ASP K 34 78.26 38.21
REMARK 500 GLN K 75 122.85 -37.09
REMARK 500 PRO K 106 -6.48 -57.35
REMARK 500 ASP K 107 57.47 -104.55
REMARK 500 ASP K 208 59.97 -142.35
REMARK 500 GLN K 269 -31.93 -157.81
REMARK 500 ASP K 305 111.74 -170.44
REMARK 500 ARG K 310 -36.33 -131.44
REMARK 500 ASN K 350 68.71 -109.52
REMARK 500 ASP L 14 -179.99 -68.28
REMARK 500 PRO L 106 -6.38 -59.52
REMARK 500 ASP L 208 58.92 -143.43
REMARK 500 GLN L 269 -32.76 -158.48
REMARK 500 ASP L 305 110.93 -168.98
REMARK 500 ASN L 350 72.52 -107.26
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 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 CSC A 1383
REMARK 610 CSC B 1384
REMARK 610 CSC C 1383
REMARK 610 CSC D 1383
REMARK 610 CSC E 1383
REMARK 610 CSC F 1384
REMARK 610 CSC G 1383
REMARK 610 CSC H 1383
REMARK 610 CSC I 1384
REMARK 610 CSC J 1385
REMARK 610 CSC K 1385
REMARK 610 CSC L 1383
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CSC A 1383
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 1384
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CSC B 1384
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 1385
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CSC C 1383
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT C 1384
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CSC D 1383
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT D 1384
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CSC E 1383
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT E 1384
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CSC F 1384
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT F 1385
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CSC G 1383
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT G 1384
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CSC H 1383
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT H 1384
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CSC I 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 CSC J 1385
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CSC K 1385
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CSC L 1383
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT L 1384
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2VAT RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF DEACETYLCEPHALOSPORIN C
REMARK 900 ACETYLTRANSFERASE IN COMPLEX WITH COENZYME A
REMARK 900 RELATED ID: 2VAV RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF DEACETYLCEPHALOSPORIN C
REMARK 900 ACETYLTRANSFERASE (COMPLEX I)
DBREF 2VAX A -58 385 UNP P39058 CEFG_CEPAC 1 444
DBREF 2VAX B -58 385 UNP P39058 CEFG_CEPAC 1 444
DBREF 2VAX C -58 385 UNP P39058 CEFG_CEPAC 1 444
DBREF 2VAX D -58 385 UNP P39058 CEFG_CEPAC 1 444
DBREF 2VAX E -58 385 UNP P39058 CEFG_CEPAC 1 444
DBREF 2VAX F -58 385 UNP P39058 CEFG_CEPAC 1 444
DBREF 2VAX G -58 385 UNP P39058 CEFG_CEPAC 1 444
DBREF 2VAX H -58 385 UNP P39058 CEFG_CEPAC 1 444
DBREF 2VAX I -58 385 UNP P39058 CEFG_CEPAC 1 444
DBREF 2VAX J -58 385 UNP P39058 CEFG_CEPAC 1 444
DBREF 2VAX K -58 385 UNP P39058 CEFG_CEPAC 1 444
DBREF 2VAX 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 OAS
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 OAS
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 OAS
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 OAS
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 OAS
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 OAS
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 OAS
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 OAS
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 OAS
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 OAS
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 OAS
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 OAS
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
MODRES 2VAX OAS A 149 SER O-ACETYLSERINE
MODRES 2VAX OAS B 149 SER O-ACETYLSERINE
MODRES 2VAX OAS C 149 SER O-ACETYLSERINE
MODRES 2VAX OAS D 149 SER O-ACETYLSERINE
MODRES 2VAX OAS E 149 SER O-ACETYLSERINE
MODRES 2VAX OAS F 149 SER O-ACETYLSERINE
MODRES 2VAX OAS G 149 SER O-ACETYLSERINE
MODRES 2VAX OAS H 149 SER O-ACETYLSERINE
MODRES 2VAX OAS I 149 SER O-ACETYLSERINE
MODRES 2VAX OAS J 149 SER O-ACETYLSERINE
MODRES 2VAX OAS K 149 SER O-ACETYLSERINE
MODRES 2VAX OAS L 149 SER O-ACETYLSERINE
HET OAS A 149 9
HET CSC A1383 25
HET ACT A1384 4
HET OAS B 149 9
HET CSC B1384 25
HET ACT B1385 4
HET OAS C 149 9
HET CSC C1383 25
HET ACT C1384 4
HET OAS D 149 9
HET CSC D1383 25
HET ACT D1384 4
HET OAS E 149 9
HET CSC E1383 25
HET ACT E1384 4
HET OAS F 149 9
HET CSC F1384 25
HET ACT F1385 4
HET OAS G 149 9
HET CSC G1383 25
HET ACT G1384 4
HET OAS H 149 9
HET CSC H1383 25
HET ACT H1384 4
HET OAS I 149 9
HET CSC I1384 25
HET ACT I1385 4
HET OAS J 149 9
HET CSC J1385 25
HET OAS K 149 9
HET CSC K1385 25
HET OAS L 149 9
HET CSC L1383 25
HET ACT L1384 4
HETNAM CSC 4-(3-ACETOXYMETHYL-2-CARBOXY-8-OXO-5-THIA-1-
HETNAM 2 CSC AZA-BICYCLO[4.2.0]OCT-2-EN-7-YLCARBAMOYL)-1-
HETNAM 3 CSC CARBOXY-BUTYL-AMMONIUM
HETNAM ACT ACETATE ION
HETNAM OAS O-ACETYLSERINE
FORMUL 13 CSC 12(C16 H22 N3 O8 S)
FORMUL 14 ACT 10(C2 H3 O2 1-)
FORMUL 15 OAS 12(C5 H9 N O4)
FORMUL 16 HOH *207(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 OAS 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 195 1 17
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 ALA A 273 SER A 288 1 16
HELIX 13 13 ASP A 290 THR A 303 1 14
HELIX 14 14 SER A 313 MET A 320 1 8
HELIX 15 15 SER A 337 ILE A 348 1 12
HELIX 16 16 ASP A 363 GLU A 368 1 6
HELIX 17 17 GLU A 368 GLN A 382 1 15
HELIX 18 18 ASN B 7 SER B 12 1 6
HELIX 19 19 HIS B 64 TRP B 68 5 5
HELIX 20 20 TRP B 69 LEU B 72 5 4
HELIX 21 21 TYR B 114 PHE B 118 5 5
HELIX 22 22 THR B 122 LEU B 137 1 16
HELIX 23 23 OAS B 149 ALA B 159 1 11
HELIX 24 24 PHE B 160 GLY B 162 5 3
HELIX 25 25 SER B 179 ASP B 195 1 17
HELIX 26 26 TYR B 199 GLU B 203 5 5
HELIX 27 27 PRO B 210 TYR B 225 1 16
HELIX 28 28 SER B 227 PHE B 235 1 9
HELIX 29 29 ALA B 273 SER B 288 1 16
HELIX 30 30 ASP B 290 HIS B 304 1 15
HELIX 31 31 SER B 313 ALA B 319 1 7
HELIX 32 32 SER B 337 ILE B 348 1 12
HELIX 33 33 ASP B 363 GLU B 368 1 6
HELIX 34 34 GLU B 368 GLN B 382 1 15
HELIX 35 35 ASN C 7 SER C 12 1 6
HELIX 36 36 HIS C 64 TRP C 68 5 5
HELIX 37 37 TRP C 69 LEU C 72 5 4
HELIX 38 38 TYR C 114 PHE C 118 5 5
HELIX 39 39 THR C 122 LEU C 137 1 16
HELIX 40 40 OAS C 149 ALA C 159 1 11
HELIX 41 41 PHE C 160 GLY C 162 5 3
HELIX 42 42 SER C 179 ASP C 195 1 17
HELIX 43 43 TYR C 199 GLU C 203 5 5
HELIX 44 44 PRO C 210 TYR C 225 1 16
HELIX 45 45 SER C 227 PHE C 235 1 9
HELIX 46 46 ALA C 273 SER C 288 1 16
HELIX 47 47 ASP C 290 HIS C 304 1 15
HELIX 48 48 SER C 313 MET C 320 1 8
HELIX 49 49 SER C 337 ILE C 348 1 12
HELIX 50 50 ASP C 363 GLU C 368 1 6
HELIX 51 51 GLU C 368 GLN C 382 1 15
HELIX 52 52 ASN D 7 SER D 12 1 6
HELIX 53 53 HIS D 64 TRP D 68 5 5
HELIX 54 54 TRP D 69 LEU D 72 5 4
HELIX 55 55 TYR D 114 PHE D 118 5 5
HELIX 56 56 THR D 122 LEU D 137 1 16
HELIX 57 57 OAS D 149 ALA D 159 1 11
HELIX 58 58 PHE D 160 GLY D 162 5 3
HELIX 59 59 SER D 179 ASP D 195 1 17
HELIX 60 60 TYR D 199 GLU D 203 5 5
HELIX 61 61 PRO D 210 TYR D 225 1 16
HELIX 62 62 SER D 227 PHE D 235 1 9
HELIX 63 63 ALA D 273 SER D 288 1 16
HELIX 64 64 ASP D 290 HIS D 304 1 15
HELIX 65 65 SER D 313 MET D 320 1 8
HELIX 66 66 SER D 337 ILE D 348 1 12
HELIX 67 67 ASP D 363 GLU D 368 1 6
HELIX 68 68 GLU D 368 GLN D 382 1 15
HELIX 69 69 ASN E 7 SER E 12 1 6
HELIX 70 70 HIS E 64 TRP E 68 5 5
HELIX 71 71 TRP E 69 LEU E 72 5 4
HELIX 72 72 TYR E 114 PHE E 118 5 5
HELIX 73 73 THR E 122 LEU E 137 1 16
HELIX 74 74 OAS E 149 ALA E 159 1 11
HELIX 75 75 PHE E 160 GLY E 162 5 3
HELIX 76 76 SER E 179 ASP E 195 1 17
HELIX 77 77 TYR E 199 GLU E 203 5 5
HELIX 78 78 PRO E 210 TYR E 225 1 16
HELIX 79 79 SER E 227 PHE E 235 1 9
HELIX 80 80 ALA E 273 SER E 288 1 16
HELIX 81 81 ASP E 290 THR E 303 1 14
HELIX 82 82 SER E 313 MET E 320 1 8
HELIX 83 83 SER E 337 ILE E 348 1 12
HELIX 84 84 ASP E 363 GLU E 368 1 6
HELIX 85 85 GLU E 368 GLN E 382 1 15
HELIX 86 86 ASN F 7 SER F 12 1 6
HELIX 87 87 HIS F 64 TRP F 68 5 5
HELIX 88 88 TRP F 69 LEU F 72 5 4
HELIX 89 89 TYR F 114 PHE F 118 5 5
HELIX 90 90 THR F 122 GLY F 138 1 17
HELIX 91 91 OAS F 149 ALA F 159 1 11
HELIX 92 92 PHE F 160 GLY F 162 5 3
HELIX 93 93 SER F 179 ASP F 195 1 17
HELIX 94 94 TYR F 199 GLU F 203 5 5
HELIX 95 95 PRO F 210 TYR F 225 1 16
HELIX 96 96 SER F 227 PHE F 235 1 9
HELIX 97 97 ALA F 273 ALA F 287 1 15
HELIX 98 98 ASP F 290 THR F 303 1 14
HELIX 99 99 SER F 313 MET F 320 1 8
HELIX 100 100 SER F 337 ILE F 348 1 12
HELIX 101 101 ASP F 363 GLU F 368 1 6
HELIX 102 102 GLU F 368 GLN F 382 1 15
HELIX 103 103 ASN G 7 SER G 12 1 6
HELIX 104 104 HIS G 64 TRP G 68 5 5
HELIX 105 105 TRP G 69 LEU G 72 5 4
HELIX 106 106 TYR G 114 PHE G 118 5 5
HELIX 107 107 THR G 122 LEU G 137 1 16
HELIX 108 108 OAS G 149 ALA G 159 1 11
HELIX 109 109 PHE G 160 GLY G 162 5 3
HELIX 110 110 SER G 179 ASP G 195 1 17
HELIX 111 111 TYR G 199 GLU G 203 5 5
HELIX 112 112 PRO G 210 TYR G 225 1 16
HELIX 113 113 SER G 227 PHE G 235 1 9
HELIX 114 114 ALA G 273 SER G 288 1 16
HELIX 115 115 ASP G 290 HIS G 304 1 15
HELIX 116 116 SER G 313 MET G 320 1 8
HELIX 117 117 SER G 337 ILE G 348 1 12
HELIX 118 118 ASP G 363 GLU G 368 1 6
HELIX 119 119 GLU G 368 GLN G 382 1 15
HELIX 120 120 ASN H 7 SER H 12 1 6
HELIX 121 121 HIS H 64 TRP H 68 5 5
HELIX 122 122 TRP H 69 LEU H 72 5 4
HELIX 123 123 TYR H 114 PHE H 118 5 5
HELIX 124 124 THR H 122 LEU H 137 1 16
HELIX 125 125 OAS H 149 ALA H 159 1 11
HELIX 126 126 PHE H 160 GLY H 162 5 3
HELIX 127 127 SER H 179 ASP H 195 1 17
HELIX 128 128 TYR H 199 GLU H 203 5 5
HELIX 129 129 PRO H 210 TYR H 225 1 16
HELIX 130 130 SER H 227 PHE H 235 1 9
HELIX 131 131 ALA H 273 SER H 288 1 16
HELIX 132 132 ASP H 290 HIS H 304 1 15
HELIX 133 133 SER H 313 MET H 320 1 8
HELIX 134 134 SER H 337 ILE H 348 1 12
HELIX 135 135 ASP H 363 GLU H 368 1 6
HELIX 136 136 GLU H 368 GLN H 382 1 15
HELIX 137 137 ASN I 7 SER I 12 1 6
HELIX 138 138 HIS I 64 TRP I 68 5 5
HELIX 139 139 TRP I 69 LEU I 72 5 4
HELIX 140 140 TYR I 114 PHE I 118 5 5
HELIX 141 141 THR I 122 LEU I 137 1 16
HELIX 142 142 OAS I 149 ALA I 159 1 11
HELIX 143 143 PHE I 160 GLY I 162 5 3
HELIX 144 144 SER I 179 ASP I 195 1 17
HELIX 145 145 TYR I 199 GLU I 203 5 5
HELIX 146 146 PRO I 210 TYR I 225 1 16
HELIX 147 147 SER I 227 PHE I 235 1 9
HELIX 148 148 ALA I 273 SER I 288 1 16
HELIX 149 149 ASP I 290 PHE I 301 1 12
HELIX 150 150 ASP I 302 HIS I 304 5 3
HELIX 151 151 SER I 313 MET I 320 1 8
HELIX 152 152 SER I 337 ILE I 348 1 12
HELIX 153 153 ASP I 363 GLU I 368 1 6
HELIX 154 154 GLU I 368 GLN I 382 1 15
HELIX 155 155 ASN J 7 SER J 12 1 6
HELIX 156 156 HIS J 64 TRP J 68 5 5
HELIX 157 157 TRP J 69 LEU J 72 5 4
HELIX 158 158 TYR J 114 PHE J 118 5 5
HELIX 159 159 THR J 122 LEU J 137 1 16
HELIX 160 160 OAS J 149 ALA J 159 1 11
HELIX 161 161 PHE J 160 GLY J 162 5 3
HELIX 162 162 SER J 179 ASP J 195 1 17
HELIX 163 163 TYR J 199 GLU J 203 5 5
HELIX 164 164 PRO J 210 TYR J 225 1 16
HELIX 165 165 SER J 227 PHE J 235 1 9
HELIX 166 166 ALA J 273 SER J 288 1 16
HELIX 167 167 ASP J 290 THR J 303 1 14
HELIX 168 168 SER J 313 MET J 320 1 8
HELIX 169 169 SER J 337 ILE J 348 1 12
HELIX 170 170 ASP J 363 GLU J 368 1 6
HELIX 171 171 GLU J 368 GLN J 382 1 15
HELIX 172 172 ASN K 7 SER K 12 1 6
HELIX 173 173 HIS K 64 TRP K 68 5 5
HELIX 174 174 TRP K 69 LEU K 72 5 4
HELIX 175 175 TYR K 114 PHE K 118 5 5
HELIX 176 176 THR K 122 LEU K 137 1 16
HELIX 177 177 OAS K 149 ALA K 159 1 11
HELIX 178 178 PHE K 160 GLY K 162 5 3
HELIX 179 179 SER K 179 ASP K 195 1 17
HELIX 180 180 TYR K 199 GLU K 203 5 5
HELIX 181 181 PRO K 210 TYR K 225 1 16
HELIX 182 182 SER K 227 PHE K 235 1 9
HELIX 183 183 ALA K 273 SER K 288 1 16
HELIX 184 184 ASP K 290 PHE K 301 1 12
HELIX 185 185 ASP K 302 HIS K 304 5 3
HELIX 186 186 SER K 313 MET K 320 1 8
HELIX 187 187 SER K 337 ILE K 348 1 12
HELIX 188 188 ASP K 363 GLU K 368 1 6
HELIX 189 189 GLU K 368 GLN K 382 1 15
HELIX 190 190 ASN L 7 SER L 12 1 6
HELIX 191 191 HIS L 64 TRP L 68 5 5
HELIX 192 192 TRP L 69 LEU L 72 5 4
HELIX 193 193 TYR L 114 PHE L 118 5 5
HELIX 194 194 THR L 122 GLY L 138 1 17
HELIX 195 195 OAS L 149 ALA L 159 1 11
HELIX 196 196 PHE L 160 GLY L 162 5 3
HELIX 197 197 SER L 179 ASP L 195 1 17
HELIX 198 198 TYR L 199 GLU L 203 5 5
HELIX 199 199 PRO L 210 TYR L 225 1 16
HELIX 200 200 SER L 227 PHE L 235 1 9
HELIX 201 201 ALA L 273 ALA L 287 1 15
HELIX 202 202 ASP L 290 THR L 303 1 14
HELIX 203 203 SER L 313 MET L 320 1 8
HELIX 204 204 SER L 337 ILE L 348 1 12
HELIX 205 205 ASP L 363 GLU L 368 1 6
HELIX 206 206 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 2 ALA A 325 CYS A 329 0
SHEET 2 AB 2 SER A 351 VAL A 355 1 O ARG A 352 N ILE A 327
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 CYS C 329 0
SHEET 2 CB 2 SER C 351 VAL C 355 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 CYS L 329 0
SHEET 2 LB 2 SER L 351 VAL L 355 1 O ARG L 352 N ILE L 327
LINK C ALA A 148 N OAS A 149 1555 1555 1.33
LINK C OAS A 149 N MET A 150 1555 1555 1.33
LINK C ALA B 148 N OAS B 149 1555 1555 1.33
LINK C OAS B 149 N MET B 150 1555 1555 1.33
LINK C ALA C 148 N OAS C 149 1555 1555 1.33
LINK C OAS C 149 N MET C 150 1555 1555 1.32
LINK C ALA D 148 N OAS D 149 1555 1555 1.33
LINK C OAS D 149 N MET D 150 1555 1555 1.32
LINK C ALA E 148 N OAS E 149 1555 1555 1.33
LINK C OAS E 149 N MET E 150 1555 1555 1.33
LINK C ALA F 148 N OAS F 149 1555 1555 1.33
LINK C OAS F 149 N MET F 150 1555 1555 1.33
LINK C ALA G 148 N OAS G 149 1555 1555 1.33
LINK C OAS G 149 N MET G 150 1555 1555 1.33
LINK C ALA H 148 N OAS H 149 1555 1555 1.32
LINK C OAS H 149 N MET H 150 1555 1555 1.33
LINK C ALA I 148 N OAS I 149 1555 1555 1.33
LINK C OAS I 149 N MET I 150 1555 1555 1.33
LINK C ALA J 148 N OAS J 149 1555 1555 1.33
LINK C OAS J 149 N MET J 150 1555 1555 1.33
LINK C ALA K 148 N OAS K 149 1555 1555 1.34
LINK C OAS K 149 N MET K 150 1555 1555 1.33
LINK C ALA L 148 N OAS L 149 1555 1555 1.33
LINK C OAS L 149 N MET L 150 1555 1555 1.33
SITE 1 AC1 10 THR A 58 LEU A 59 THR A 60 ARG A 218
SITE 2 AC1 10 TYR A 225 ARG A 234 GLN A 281 HIS A 362
SITE 3 AC1 10 ASP A 363 MET A 367
SITE 1 AC2 5 ARG A 124 GLU A 157 PHE A 161 THR B 25
SITE 2 AC2 5 ILE B 31
SITE 1 AC3 10 THR B 58 LEU B 59 THR B 60 ARG B 218
SITE 2 AC3 10 ASN B 222 LYS B 226 TYR B 277 GLN B 281
SITE 3 AC3 10 HIS B 362 ASP B 363
SITE 1 AC4 4 THR A 25 ILE A 31 ARG B 124 GLU B 157
SITE 1 AC5 11 THR C 58 LEU C 59 THR C 60 ARG C 218
SITE 2 AC5 11 TYR C 225 LYS C 226 TYR C 277 GLN C 281
SITE 3 AC5 11 HIS C 362 ASP C 363 MET C 367
SITE 1 AC6 3 ARG C 124 ARG C 128 GLU C 157
SITE 1 AC7 8 THR D 58 LEU D 59 THR D 60 ARG D 218
SITE 2 AC7 8 TYR D 225 GLN D 281 HIS D 362 ASP D 363
SITE 1 AC8 4 ARG D 124 ARG D 128 GLU D 157 ARG D 310
SITE 1 AC9 11 THR E 58 LEU E 59 THR E 60 ARG E 218
SITE 2 AC9 11 TYR E 225 LYS E 226 ARG E 234 GLN E 281
SITE 3 AC9 11 HIS E 362 ASP E 363 MET E 367
SITE 1 BC1 3 GLU E 157 THR I 25 ILE I 31
SITE 1 BC2 11 THR F 58 LEU F 59 THR F 60 ARG F 218
SITE 2 BC2 11 LYS F 226 ARG F 234 TYR F 277 GLN F 281
SITE 3 BC2 11 HIS F 362 PHE F 365 MET F 367
SITE 1 BC3 4 ARG F 124 ARG F 128 GLU F 157 PHE F 161
SITE 1 BC4 12 THR G 58 LEU G 59 THR G 60 ARG G 218
SITE 2 BC4 12 TYR G 225 LYS G 226 ARG G 234 GLN G 281
SITE 3 BC4 12 HIS G 362 ASP G 363 MET G 367 HOH G2003
SITE 1 BC5 2 ARG G 128 GLU G 157
SITE 1 BC6 12 THR H 58 LEU H 59 THR H 60 TRP H 68
SITE 2 BC6 12 ARG H 218 LYS H 226 ARG H 234 TYR H 277
SITE 3 BC6 12 HIS H 362 ASP H 363 PHE H 365 HOH H2005
SITE 1 BC7 3 ARG H 124 ARG H 128 GLU H 157
SITE 1 BC8 10 THR I 58 LEU I 59 THR I 60 ARG I 218
SITE 2 BC8 10 ASN I 222 LYS I 226 TYR I 277 GLN I 281
SITE 3 BC8 10 HIS I 362 ASP I 363
SITE 1 BC9 3 THR E 25 ARG I 124 GLU I 157
SITE 1 CC1 13 THR J 58 LEU J 59 THR J 60 ARG J 218
SITE 2 CC1 13 TYR J 225 LYS J 226 ARG J 234 TYR J 277
SITE 3 CC1 13 GLN J 281 HIS J 362 ASP J 363 PHE J 365
SITE 4 CC1 13 MET J 367
SITE 1 CC2 10 THR K 58 LEU K 59 THR K 60 ARG K 218
SITE 2 CC2 10 TYR K 225 LYS K 226 TYR K 277 HIS K 362
SITE 3 CC2 10 ASP K 363 PHE K 365
SITE 1 CC3 11 THR L 58 LEU L 59 THR L 60 ARG L 218
SITE 2 CC3 11 LYS L 226 ARG L 234 TYR L 277 GLN L 281
SITE 3 CC3 11 HIS L 362 ASP L 363 PHE L 365
SITE 1 CC4 4 ARG L 124 ARG L 128 GLU L 157 PHE L 161
CRYST1 121.357 109.288 195.388 90.00 90.03 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 0.008240 0.000000 0.000004 0.00000
SCALE2 0.000000 0.009150 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005118 0.00000
MTRIX1 1 -0.999900 -0.010800 0.010950 152.70000 1
MTRIX2 1 0.010460 -0.999500 0.030440 19.97000 1
MTRIX3 1 -0.011270 0.030330 0.999500 0.62750 1
MTRIX1 2 -0.797300 0.100600 -0.595100 147.60000 1
MTRIX2 2 0.077060 0.994900 0.064920 0.99310 1
MTRIX3 2 0.598600 0.005905 -0.801000 -18.94000 1
MTRIX1 3 0.798100 -0.100000 -0.594200 57.25000 1
MTRIX2 3 -0.076330 -0.995000 0.064930 -23.75000 1
MTRIX3 3 -0.597700 -0.006466 -0.801700 168.00000 1
MTRIX1 4 1.000000 0.000720 0.000016 60.68000 1
MTRIX2 4 0.000720 -1.000000 0.000534 22.07000 1
MTRIX3 4 0.000016 -0.000534 -1.000000 97.70000 1
MTRIX1 5 -0.518500 0.500700 0.693100 110.20000 1
MTRIX2 5 0.340300 0.864500 -0.369900 -7.28100 1
MTRIX3 5 -0.784400 0.044060 -0.618700 56.21000 1
MTRIX1 6 0.528000 0.487600 0.695300 -8.55800 1
MTRIX2 6 0.384800 -0.867200 0.316000 -42.44000 1
MTRIX3 6 0.757100 0.100700 -0.645500 58.06000 1
MTRIX1 7 0.527500 -0.487300 -0.695900 38.16000 1
MTRIX2 7 0.385100 0.867300 -0.315500 -54.17000 1
MTRIX3 7 0.757200 -0.101600 0.645200 -48.77000 1
MTRIX1 8 -0.999900 0.011860 0.010860 212.00000 1
MTRIX2 8 0.011520 0.999500 -0.030400 0.06128 1
MTRIX3 8 -0.011210 -0.030270 -0.999500 99.62000 1
MTRIX1 9 -0.800500 -0.096540 -0.591500 157.40000 1
MTRIX2 9 -0.047780 0.994100 -0.097570 63.95000 1
MTRIX3 9 0.597500 -0.049840 -0.800400 41.78000 1
MTRIX1 10 -0.802700 0.100400 0.587800 156.50000 1
MTRIX2 10 -0.050100 -0.993600 0.101300 -29.16000 1
MTRIX3 10 0.594200 0.051900 0.802600 -67.97000 1
MTRIX1 11 -0.518400 -0.500700 -0.693300 220.40000 1
MTRIX2 11 0.340100 -0.864500 0.370000 -44.90000 1
MTRIX3 11 -0.784600 -0.043990 0.618400 44.34000 1
TER 2740 GLN A 382
TER 5491 SER B 383
TER 8262 GLN C 382
TER 11005 GLN D 382
TER 13734 GLN E 382
TER 16434 SER F 383
TER 19161 GLN G 382
TER 21890 GLN H 382
TER 24657 SER I 383
TER 27377 LEU J 384
TER 30097 LEU K 384
TER 32795 GLN L 382
MASTER 2308 0 34 206 96 0 47 3933330 12 472 420
END |